1	1	complex	Cdc4	Skp1	A 2.7 A X-ray crystal structure of a Skp1-Cdc4 complex bound to a high-affinity CPD phosphopeptide from human cyclin E reveals a core CPD motif, Leu-Leu-pThr-Pro, bound to an eight-bladed WD40 propeller domain in Cdc4.
1	2	complex	Skp1	Cdc4	A 2.7 A X-ray crystal structure of a Skp1-Cdc4 complex bound to a high-affinity CPD phosphopeptide from human cyclin E reveals a core CPD motif, Leu-Leu-pThr-Pro, bound to an eight-bladed WD40 propeller domain in Cdc4.
2	3	interaction	NEDD8	S5a	A GST pull-down assay revealed that the overexpression of NUB1 leads to a greater precipitation of NEDD8 conjugates with GST-S5a, suggesting that NUB1 might have an adaptor function between S5a and NEDD8.
2	4	interaction	S5a	NEDD8	A GST pull-down assay revealed that the overexpression of NUB1 leads to a greater precipitation of NEDD8 conjugates with GST-S5a, suggesting that NUB1 might have an adaptor function between S5a and NEDD8.
3	5	interaction	Fwd2	Skp1	A coimmunoprecipitation assay has revealed the in vivo interaction between Skp1 and Fwd2 through the F-box domain.
3	6	interaction	Skp1	Fwd2	A coimmunoprecipitation assay has revealed the in vivo interaction between Skp1 and Fwd2 through the F-box domain.
4	7	interact	Agp5p	Apg3p	A cross-linking experiment revealed that Apg3p interacts with the endogenous Apg12p/Apg5p conjugate.
4	8	interact	Apg12p	Apg3p	A cross-linking experiment revealed that Apg3p interacts with the endogenous Apg12p/Apg5p conjugate.
4	9	interact	Apg3p	Agp5p	A cross-linking experiment revealed that Apg3p interacts with the endogenous Apg12p/Apg5p conjugate.
4	10	interact	Apg3p	Apg12p	A cross-linking experiment revealed that Apg3p interacts with the endogenous Apg12p/Apg5p conjugate.
5	11	interact	SCON2	SCON3	A crucial set of experiments, by using a yeast two-hybrid approach with confirming coimmunoprecipitation assays, demonstrated that SCON3 interacts with SCON2 in a manner dependent upon the F-box motif of SCON2.
5	12	interact	SCON3	SCON2	A crucial set of experiments, by using a yeast two-hybrid approach with confirming coimmunoprecipitation assays, demonstrated that SCON3 interacts with SCON2 in a manner dependent upon the F-box motif of SCON2.
6	13	ubiquitinate	Rpb1	Rpf1	A human WW domain-containing hect (WW-hect) E3 protein closely related to Rsp5, Rpf1/hNedd4, also binds and ubiquitinates both yeast and human Rpb1 in vitro, suggesting that Rpf1 and/or another WW-hect E3 protein mediates UV-induced degradation of the large subunit of polymerase II in human cells.
6	14	ubiquitinate	Rpb1	hNedd4	A human WW domain-containing hect (WW-hect) E3 protein closely related to Rsp5, Rpf1/hNedd4, also binds and ubiquitinates both yeast and human Rpb1 in vitro, suggesting that Rpf1 and/or another WW-hect E3 protein mediates UV-induced degradation of the large subunit of polymerase II in human cells.
6	15	ubiquitinate	Rpf1	Rpb1	A human WW domain-containing hect (WW-hect) E3 protein closely related to Rsp5, Rpf1/hNedd4, also binds and ubiquitinates both yeast and human Rpb1 in vitro, suggesting that Rpf1 and/or another WW-hect E3 protein mediates UV-induced degradation of the large subunit of polymerase II in human cells.
6	16	ubiquitinate	hNedd4	Rpb1	A human WW domain-containing hect (WW-hect) E3 protein closely related to Rsp5, Rpf1/hNedd4, also binds and ubiquitinates both yeast and human Rpb1 in vitro, suggesting that Rpf1 and/or another WW-hect E3 protein mediates UV-induced degradation of the large subunit of polymerase II in human cells.
7	17	binding	YUH1	ubiquitin	A model for ubiquitin binding to YUH1 is proposed, in which a good correlation was observed for the lateral binding of ubiquitin to UCH-L3 (YUH1), stabilized by the electrostatic and hydrophobic interactions.
7	18	binding	ubiquitin	YUH1	A model for ubiquitin binding to YUH1 is proposed, in which a good correlation was observed for the lateral binding of ubiquitin to UCH-L3 (YUH1), stabilized by the electrostatic and hydrophobic interactions.
8	19	binding	Cdc28	Cks1	A mutation in Cdc28 (cdc28-1N) that interferes with Cks1 binding, or inactivation of Cks1 itself, confers stabilization of Clb2, the principal mitotic B-type cyclin in budding yeast.
8	20	binding	Cks1	Cdc28	A mutation in Cdc28 (cdc28-1N) that interferes with Cks1 binding, or inactivation of Cks1 itself, confers stabilization of Clb2, the principal mitotic B-type cyclin in budding yeast.
9	21	regulate	COP9	selenocystine133-to-Cy	A recent report by Lyapina et al. shows that the COP9/signalosome (CSN), a multifunctional eight subunit complex, regulates Ned8p modification of Pcu1p.
9	22	modification	Ned8p	Pcu1p	A recent report by Lyapina et al. shows that the COP9/signalosome (CSN), a multifunctional eight subunit complex, regulates Ned8p modification of Pcu1p.
9	23	modification	Pcu1p	Ned8p	A recent report by Lyapina et al. shows that the COP9/signalosome (CSN), a multifunctional eight subunit complex, regulates Ned8p modification of Pcu1p.
9	24	regulate	selenocystine133-to-Cy	COP9	A recent report by Lyapina et al. shows that the COP9/signalosome (CSN), a multifunctional eight subunit complex, regulates Ned8p modification of Pcu1p.
10	25	bind	CMG-2	collagen type IV	A recombinant portion of CMG-2 was found to bind collagen type IV and laminin, suggesting a potential role in basement membrane matrix synthesis and assembly.
10	26	bind	CMG-2	laminin	A recombinant portion of CMG-2 was found to bind collagen type IV and laminin, suggesting a potential role in basement membrane matrix synthesis and assembly.
10	27	bind	collagen type IV	CMG-2	A recombinant portion of CMG-2 was found to bind collagen type IV and laminin, suggesting a potential role in basement membrane matrix synthesis and assembly.
10	28	bind	laminin	CMG-2	A recombinant portion of CMG-2 was found to bind collagen type IV and laminin, suggesting a potential role in basement membrane matrix synthesis and assembly.
11	29	binding	Cdc4pF-beta-gal	SCF	A stable truncated Cdc4pF-beta-gal hybrid protein capable of binding Skp1p and entering into an SCF complex interfered with proteolysis of SCF targets and inhibited cell proliferation.
11	30	binding	SCF	Cdc4pF-beta-gal	A stable truncated Cdc4pF-beta-gal hybrid protein capable of binding Skp1p and entering into an SCF complex interfered with proteolysis of SCF targets and inhibited cell proliferation.
12	31	associate	CBP	GRIP1	A subpopulation of GRIP1 foci associate with ND10s, small nuclear bodies that contain several proteins including PML, SP100, DAXX, and CREB-binding protein (CBP).
12	32	associate	DAXX	GRIP1	A subpopulation of GRIP1 foci associate with ND10s, small nuclear bodies that contain several proteins including PML, SP100, DAXX, and CREB-binding protein (CBP).
12	33	associate	GRIP1	CBP	A subpopulation of GRIP1 foci associate with ND10s, small nuclear bodies that contain several proteins including PML, SP100, DAXX, and CREB-binding protein (CBP).
12	34	associate	GRIP1	DAXX	A subpopulation of GRIP1 foci associate with ND10s, small nuclear bodies that contain several proteins including PML, SP100, DAXX, and CREB-binding protein (CBP).
12	35	associate	GRIP1	ND10s	A subpopulation of GRIP1 foci associate with ND10s, small nuclear bodies that contain several proteins including PML, SP100, DAXX, and CREB-binding protein (CBP).
12	36	associate	GRIP1	PML	A subpopulation of GRIP1 foci associate with ND10s, small nuclear bodies that contain several proteins including PML, SP100, DAXX, and CREB-binding protein (CBP).
12	37	associate	GRIP1	SP100	A subpopulation of GRIP1 foci associate with ND10s, small nuclear bodies that contain several proteins including PML, SP100, DAXX, and CREB-binding protein (CBP).
12	38	associate	ND10s	GRIP1	A subpopulation of GRIP1 foci associate with ND10s, small nuclear bodies that contain several proteins including PML, SP100, DAXX, and CREB-binding protein (CBP).
12	39	associate	PML	GRIP1	A subpopulation of GRIP1 foci associate with ND10s, small nuclear bodies that contain several proteins including PML, SP100, DAXX, and CREB-binding protein (CBP).
12	40	associate	SP100	GRIP1	A subpopulation of GRIP1 foci associate with ND10s, small nuclear bodies that contain several proteins including PML, SP100, DAXX, and CREB-binding protein (CBP).
13	41	interact	hApg12p	hApg7p	A two-hybrid experiment indicated that hApg12p interacts with hApg7p.
13	42	interact	hApg7p	hApg12p	A two-hybrid experiment indicated that hApg12p interacts with hApg7p.
14	43	bound	MDM2	ubiquitin	A ubiquitin molecule bound MDM2 through sulfhydroxy bond which is characteristic of ubiquitin ligase (E3)-ubiquitin binding.
14	44	bound	ubiquitin	MDM2	A ubiquitin molecule bound MDM2 through sulfhydroxy bond which is characteristic of ubiquitin ligase (E3)-ubiquitin binding.
15	45	interact	TopBP1	hHYD	A yeast two-hybrid screen showed that DNA topoisomerase IIbeta-binding protein 1 (TopBP1) interacted with hHYD.
15	46	interact	hHYD	TopBP1	A yeast two-hybrid screen showed that DNA topoisomerase IIbeta-binding protein 1 (TopBP1) interacted with hHYD.
16	47	ubiquitinate	Cdc20	securin	APC(Cdc20) promotes sister-chromatid separation by ubiquitinating securin, whereas APC(Cdh1) ubiquitinates mitotic cyclins, allowing the exit from mitosis.
16	48	ubiquitinate	Cdh1	cyclins	APC(Cdc20) promotes sister-chromatid separation by ubiquitinating securin, whereas APC(Cdh1) ubiquitinates mitotic cyclins, allowing the exit from mitosis.
16	49	ubiquitinate	cyclins	Cdh1	APC(Cdc20) promotes sister-chromatid separation by ubiquitinating securin, whereas APC(Cdh1) ubiquitinates mitotic cyclins, allowing the exit from mitosis.
16	50	ubiquitinate	securin	Cdc20	APC(Cdc20) promotes sister-chromatid separation by ubiquitinating securin, whereas APC(Cdh1) ubiquitinates mitotic cyclins, allowing the exit from mitosis.
17	51	ubiquitinate	APC11	cyclin B	APC11 and UBC4 are also able to ubiquitinate securin and cyclin B, but these reactions show a decreased dependency on the destruction box.
17	52	ubiquitinate	APC11	securin	APC11 and UBC4 are also able to ubiquitinate securin and cyclin B, but these reactions show a decreased dependency on the destruction box.
17	53	ubiquitinate	UBC4	cyclin B	APC11 and UBC4 are also able to ubiquitinate securin and cyclin B, but these reactions show a decreased dependency on the destruction box.
17	54	ubiquitinate	UBC4	securin	APC11 and UBC4 are also able to ubiquitinate securin and cyclin B, but these reactions show a decreased dependency on the destruction box.
17	55	ubiquitinate	cyclin B	APC11	APC11 and UBC4 are also able to ubiquitinate securin and cyclin B, but these reactions show a decreased dependency on the destruction box.
17	56	ubiquitinate	cyclin B	UBC4	APC11 and UBC4 are also able to ubiquitinate securin and cyclin B, but these reactions show a decreased dependency on the destruction box.
17	57	ubiquitinate	securin	APC11	APC11 and UBC4 are also able to ubiquitinate securin and cyclin B, but these reactions show a decreased dependency on the destruction box.
17	58	ubiquitinate	securin	UBC4	APC11 and UBC4 are also able to ubiquitinate securin and cyclin B, but these reactions show a decreased dependency on the destruction box.
18	59	bind	APP	APP-BP1	APP-BP1 binds to the amyloid precursor protein (APP) carboxyl-terminal domain.
18	60	bind	APP-BP1	APP	APP-BP1 binds to the amyloid precursor protein (APP) carboxyl-terminal domain.
19	61	bind	ARF	MDM2	ARF binds directly to MDM2, and prevents MDM2 from targeting p53 for degradation by inhibiting the E3 ligase activity of MDM2 and preventing nuclear export of MDM2 and p53.
19	62	bind	MDM2	ARF	ARF binds directly to MDM2, and prevents MDM2 from targeting p53 for degradation by inhibiting the E3 ligase activity of MDM2 and preventing nuclear export of MDM2 and p53.
20	63	phosphorylate	ATM	FANCD2	ATM phosphorylates FANCD2 on serine 222 in vitro.
20	64	phosphorylate	FANCD2	ATM	ATM phosphorylates FANCD2 on serine 222 in vitro.
21	65	interact	HsUbc9	Rad51	According to the Ga14 two-hybrid system analysis, HsUbc9 protein interacts with human recombination protein Rad51.
21	66	interact	Rad51	HsUbc9	According to the Ga14 two-hybrid system analysis, HsUbc9 protein interacts with human recombination protein Rad51.
22	67	conjugation	SUMO-1	p53	Accordingly, we provide evidence that conjugation of SUMO-1 to wild-type p53 results in an increased transactivation ability of p53.
22	68	conjugation	p53	SUMO-1	Accordingly, we provide evidence that conjugation of SUMO-1 to wild-type p53 results in an increased transactivation ability of p53.
23	69	binding	APC	CDC20	Activation of the anaphase-promoting complex (APC) by binding of CDC20 and CDH1 is required for exit from mitosis, and APC has been implicated as a target for the checkpoint intervention.
23	70	binding	APC	CDH1	Activation of the anaphase-promoting complex (APC) by binding of CDC20 and CDH1 is required for exit from mitosis, and APC has been implicated as a target for the checkpoint intervention.
23	71	binding	CDC20	APC	Activation of the anaphase-promoting complex (APC) by binding of CDC20 and CDH1 is required for exit from mitosis, and APC has been implicated as a target for the checkpoint intervention.
23	72	binding	CDH1	APC	Activation of the anaphase-promoting complex (APC) by binding of CDC20 and CDH1 is required for exit from mitosis, and APC has been implicated as a target for the checkpoint intervention.
24	73	phosphorylation	APC	Cdk1	Activation requires phosphorylation of the cyclosome/APC by protein kinase Cdk1/cyclin B. The lag kinetics of cyclosome activation may be explained by Suc1-assisted multiple phosphorylations of partly phosphorylated complex.
24	74	phosphorylation	APC	Suc1	Activation requires phosphorylation of the cyclosome/APC by protein kinase Cdk1/cyclin B. The lag kinetics of cyclosome activation may be explained by Suc1-assisted multiple phosphorylations of partly phosphorylated complex.
24	75	phosphorylation	APC	cyclin B	Activation requires phosphorylation of the cyclosome/APC by protein kinase Cdk1/cyclin B. The lag kinetics of cyclosome activation may be explained by Suc1-assisted multiple phosphorylations of partly phosphorylated complex.
24	76	phosphorylation	Cdk1	APC	Activation requires phosphorylation of the cyclosome/APC by protein kinase Cdk1/cyclin B. The lag kinetics of cyclosome activation may be explained by Suc1-assisted multiple phosphorylations of partly phosphorylated complex.
24	77	phosphorylation	Suc1	APC	Activation requires phosphorylation of the cyclosome/APC by protein kinase Cdk1/cyclin B. The lag kinetics of cyclosome activation may be explained by Suc1-assisted multiple phosphorylations of partly phosphorylated complex.
24	78	phosphorylation	cyclin B	APC	Activation requires phosphorylation of the cyclosome/APC by protein kinase Cdk1/cyclin B. The lag kinetics of cyclosome activation may be explained by Suc1-assisted multiple phosphorylations of partly phosphorylated complex.
25	79	interact	NFB42	Skp1p	Additional experiments demonstrate that NFB42 interacts with Skp1p, a component of the proteasome pathway, and deletion of the F box also inhibits this interaction.
25	80	interact	Skp1p	NFB42	Additional experiments demonstrate that NFB42 interacts with Skp1p, a component of the proteasome pathway, and deletion of the F box also inhibits this interaction.
26	81	bind	IL-6	IL-6R alpha	After secretion, IL-6 binds to its receptor IL-6R alpha (gp 80), the IL-6R alpha complex then recruits the signal-transducing beta-subunit (gp 130), which is the functional complex for signal transduction.
26	82	bind	IL-6R alpha	IL-6	After secretion, IL-6 binds to its receptor IL-6R alpha (gp 80), the IL-6R alpha complex then recruits the signal-transducing beta-subunit (gp 130), which is the functional complex for signal transduction.
26	83	recruits	IL-6R alpha	gp 130	After secretion, IL-6 binds to its receptor IL-6R alpha (gp 80), the IL-6R alpha complex then recruits the signal-transducing beta-subunit (gp 130), which is the functional complex for signal transduction.
26	84	recruits	gp 130	IL-6R alpha	After secretion, IL-6 binds to its receptor IL-6R alpha (gp 80), the IL-6R alpha complex then recruits the signal-transducing beta-subunit (gp 130), which is the functional complex for signal transduction.
27	85	bind	Cks1	Skp2	All proteins of this family have Cdk-binding and anion-binding sites, but only mammalian Cks1 binds to Skp2 and promotes the association of Skp2 with p27 phosphorylated on Thr-187.
27	86	bind	Skp2	Cks1	All proteins of this family have Cdk-binding and anion-binding sites, but only mammalian Cks1 binds to Skp2 and promotes the association of Skp2 with p27 phosphorylated on Thr-187.
27	87	associate	Skp2	p27	All proteins of this family have Cdk-binding and anion-binding sites, but only mammalian Cks1 binds to Skp2 and promotes the association of Skp2 with p27 phosphorylated on Thr-187.
27	88	associate	p27	Skp2	All proteins of this family have Cdk-binding and anion-binding sites, but only mammalian Cks1 binds to Skp2 and promotes the association of Skp2 with p27 phosphorylated on Thr-187.
28	89	interaction	B-crystallin R120G	Fbx4	Also B-crystallin R120G, a mutant found to co-segregate with a desmin related myopathy (DRM), displays increased interaction with Fbx4.
28	90	interaction	Fbx4	B-crystallin R120G	Also B-crystallin R120G, a mutant found to co-segregate with a desmin related myopathy (DRM), displays increased interaction with Fbx4.
29	91	bind	ICP0	cdc34	Also in infected cells, cdc34, a polyubiquitinated E2 ubiquitin-conjugating enzyme, exhibits increased ICP0-dependent dynamic interaction with proteasomes. (ii) In an in vitro substrate-independent ubiquitination system, the RING finger domain encoded by exon 2 of ICP0 binds cdc34, whereas the carboxyl-terminal domain of ICP0 functions as an E3 ligase independent of the RING finger domain.
29	92	bind	cdc34	ICP0	Also in infected cells, cdc34, a polyubiquitinated E2 ubiquitin-conjugating enzyme, exhibits increased ICP0-dependent dynamic interaction with proteasomes. (ii) In an in vitro substrate-independent ubiquitination system, the RING finger domain encoded by exon 2 of ICP0 binds cdc34, whereas the carboxyl-terminal domain of ICP0 functions as an E3 ligase independent of the RING finger domain.
30	93	interact	Daxx	Ubc9	Also, Daxx interacted with Ubc9, an essential protein as a key conjugating enzyme.
30	94	interact	Ubc9	Daxx	Also, Daxx interacted with Ubc9, an essential protein as a key conjugating enzyme.
31	95	bind	AR	Bag1	Although Bag1L, Bag1M, and Bag1 can bind the androgen receptor (AR) in vitro, only Bag1L enhanced AR transcriptional activity.
31	96	bind	AR	Bag1L	Although Bag1L, Bag1M, and Bag1 can bind the androgen receptor (AR) in vitro, only Bag1L enhanced AR transcriptional activity.
31	97	bind	AR	Bag1M	Although Bag1L, Bag1M, and Bag1 can bind the androgen receptor (AR) in vitro, only Bag1L enhanced AR transcriptional activity.
31	98	bind	Bag1	AR	Although Bag1L, Bag1M, and Bag1 can bind the androgen receptor (AR) in vitro, only Bag1L enhanced AR transcriptional activity.
31	99	bind	Bag1L	AR	Although Bag1L, Bag1M, and Bag1 can bind the androgen receptor (AR) in vitro, only Bag1L enhanced AR transcriptional activity.
31	100	bind	Bag1M	AR	Although Bag1L, Bag1M, and Bag1 can bind the androgen receptor (AR) in vitro, only Bag1L enhanced AR transcriptional activity.
32	101	binding	Mdm2	p53	Although Mdm2 binding to p53 triggers ubiquitin-mediated proteosome degradation, p63 protein levels were unaltered by association with either Mdm2 or MdmX.
32	102	association	Mdm2	p63	Although Mdm2 binding to p53 triggers ubiquitin-mediated proteosome degradation, p63 protein levels were unaltered by association with either Mdm2 or MdmX.
32	103	association	MdmX	p63	Although Mdm2 binding to p53 triggers ubiquitin-mediated proteosome degradation, p63 protein levels were unaltered by association with either Mdm2 or MdmX.
32	104	binding	p53	Mdm2	Although Mdm2 binding to p53 triggers ubiquitin-mediated proteosome degradation, p63 protein levels were unaltered by association with either Mdm2 or MdmX.
32	105	association	p63	Mdm2	Although Mdm2 binding to p53 triggers ubiquitin-mediated proteosome degradation, p63 protein levels were unaltered by association with either Mdm2 or MdmX.
32	106	association	p63	MdmX	Although Mdm2 binding to p53 triggers ubiquitin-mediated proteosome degradation, p63 protein levels were unaltered by association with either Mdm2 or MdmX.
33	107	binding	ARF	Mdm2	Although a nucleolar localization signal (NrLS) maps within a different segment (residues 82 to 101) of the human p14(ARF) protein, binding to Mdm2 and nucleolar import of ARF-Mdm2 complexes are both required for cell cycle arrest induced by either the mouse or human ARF proteins.
33	108	binding	Mdm2	ARF	Although a nucleolar localization signal (NrLS) maps within a different segment (residues 82 to 101) of the human p14(ARF) protein, binding to Mdm2 and nucleolar import of ARF-Mdm2 complexes are both required for cell cycle arrest induced by either the mouse or human ARF proteins.
33	109	binding	Mdm2	p14	Although a nucleolar localization signal (NrLS) maps within a different segment (residues 82 to 101) of the human p14(ARF) protein, binding to Mdm2 and nucleolar import of ARF-Mdm2 complexes are both required for cell cycle arrest induced by either the mouse or human ARF proteins.
33	110	binding	p14	Mdm2	Although a nucleolar localization signal (NrLS) maps within a different segment (residues 82 to 101) of the human p14(ARF) protein, binding to Mdm2 and nucleolar import of ARF-Mdm2 complexes are both required for cell cycle arrest induced by either the mouse or human ARF proteins.
34	111	complexed	XPC	hHR23B	Although a small proportion of hHR23B is tightly complexed with the XP-C responsible gene product, XPC protein, a vast majority exists as an XPC-free form, indicating that hHR23B has additional functions other than NER in vivo.
34	112	complexed	hHR23B	XPC	Although a small proportion of hHR23B is tightly complexed with the XP-C responsible gene product, XPC protein, a vast majority exists as an XPC-free form, indicating that hHR23B has additional functions other than NER in vivo.
35	113	bound	TRAF1	c-IAP1	Although c-IAP1 bound TRAF2 and TRAF1 in vitro, it ubiquitinated only TRAF2.
35	114	bound	TRAF2	c-IAP1	Although c-IAP1 bound TRAF2 and TRAF1 in vitro, it ubiquitinated only TRAF2.
35	115	bound	c-IAP1	TRAF1	Although c-IAP1 bound TRAF2 and TRAF1 in vitro, it ubiquitinated only TRAF2.
35	116	bound	c-IAP1	TRAF2	Although c-IAP1 bound TRAF2 and TRAF1 in vitro, it ubiquitinated only TRAF2.
36	117	association	MITF	ubiquitin	Although hUBC9 is known to interact preferentially with SENTRIN/SUMO1, in vitro transcription/translation analysis demonstrated greater association of MITF with ubiquitin than with SENTRIN.
36	118	interact	SENTRIN	hUBC9	Although hUBC9 is known to interact preferentially with SENTRIN/SUMO1, in vitro transcription/translation analysis demonstrated greater association of MITF with ubiquitin than with SENTRIN.
36	119	interact	SUMO1	hUBC9	Although hUBC9 is known to interact preferentially with SENTRIN/SUMO1, in vitro transcription/translation analysis demonstrated greater association of MITF with ubiquitin than with SENTRIN.
36	120	interact	hUBC9	SENTRIN	Although hUBC9 is known to interact preferentially with SENTRIN/SUMO1, in vitro transcription/translation analysis demonstrated greater association of MITF with ubiquitin than with SENTRIN.
36	121	interact	hUBC9	SUMO1	Although hUBC9 is known to interact preferentially with SENTRIN/SUMO1, in vitro transcription/translation analysis demonstrated greater association of MITF with ubiquitin than with SENTRIN.
36	122	association	ubiquitin	MITF	Although hUBC9 is known to interact preferentially with SENTRIN/SUMO1, in vitro transcription/translation analysis demonstrated greater association of MITF with ubiquitin than with SENTRIN.
37	123	modified	Cul-1	Nedd8	Although only a minute fraction of total cellular Cul-1 is modified by Nedd8, the Cul-1 associated with ectopically expressed betaTrCP was highly enriched for the Nedd8-conjugated form.
37	124	modified	Nedd8	Cul-1	Although only a minute fraction of total cellular Cul-1 is modified by Nedd8, the Cul-1 associated with ectopically expressed betaTrCP was highly enriched for the Nedd8-conjugated form.
38	125	modification	PML	SUMO-1	Although recruitment of proteins through interferon-induced upregulation and SUMO-1 modification level of PML had been defined, it is not known whether release of proteins is regulated and has physiological consequences.
38	126	modification	SUMO-1	PML	Although recruitment of proteins through interferon-induced upregulation and SUMO-1 modification level of PML had been defined, it is not known whether release of proteins is regulated and has physiological consequences.
39	127	binding	E2-25K	polyUb	Among Ub-conjugating enzymes, E2-25K is unique in its ability to synthesize in vitro unanchored Lys(48)-linked poly-Ub chains from mono- or poly-Ub, E1, and ATP; thus, E2-25K has distinct binding sites for donor and acceptor (poly)Ub.
39	128	binding	polyUb	E2-25K	Among Ub-conjugating enzymes, E2-25K is unique in its ability to synthesize in vitro unanchored Lys(48)-linked poly-Ub chains from mono- or poly-Ub, E1, and ATP; thus, E2-25K has distinct binding sites for donor and acceptor (poly)Ub.
40	129	ubiquitinate	E3-alpha	alpha-lactalbumin	Among other effects, p-aminophenylarsenoxide decreased the steady-state level of ubiquitinated human alpha-lactalbumin; this is a substrate which is acted upon directly by ubiquitin-protein ligase-alpha (E3-alpha).
40	130	ubiquitinate	alpha-lactalbumin	E3-alpha	Among other effects, p-aminophenylarsenoxide decreased the steady-state level of ubiquitinated human alpha-lactalbumin; this is a substrate which is acted upon directly by ubiquitin-protein ligase-alpha (E3-alpha).
41	131	bind	Smad2	SnoN	Among receptor-regulated Smads, c-Ski and SnoN bind more strongly to Smad2 and Smad3 than to Smad1.
41	132	bind	Smad2	c-Ski	Among receptor-regulated Smads, c-Ski and SnoN bind more strongly to Smad2 and Smad3 than to Smad1.
41	133	bind	Smad3	SnoN	Among receptor-regulated Smads, c-Ski and SnoN bind more strongly to Smad2 and Smad3 than to Smad1.
41	134	bind	Smad3	c-Ski	Among receptor-regulated Smads, c-Ski and SnoN bind more strongly to Smad2 and Smad3 than to Smad1.
41	135	bind	SnoN	Smad2	Among receptor-regulated Smads, c-Ski and SnoN bind more strongly to Smad2 and Smad3 than to Smad1.
41	136	bind	SnoN	Smad3	Among receptor-regulated Smads, c-Ski and SnoN bind more strongly to Smad2 and Smad3 than to Smad1.
41	137	bind	c-Ski	Smad2	Among receptor-regulated Smads, c-Ski and SnoN bind more strongly to Smad2 and Smad3 than to Smad1.
41	138	bind	c-Ski	Smad3	Among receptor-regulated Smads, c-Ski and SnoN bind more strongly to Smad2 and Smad3 than to Smad1.
42	139	link	Cdc4p	Cdc53p	Among the domains of Cdc4p that are crucial for function are the F-box, which links Cdc4p to Cdc53p through Skp1p, and the WD-40 repeats, which are required for binding the substrate for Cdc34p.
42	140	link	Cdc53p	Cdc4p	Among the domains of Cdc4p that are crucial for function are the F-box, which links Cdc4p to Cdc53p through Skp1p, and the WD-40 repeats, which are required for binding the substrate for Cdc34p.
43	141	binding	Pof10	Skp1	Among them, Pof10 is a novel F-box protein consisting of 662 amino acids, harboring the F-box domain required for the binding to Skp1 and followed by four WD40 repeats.
43	142	binding	Skp1	Pof10	Among them, Pof10 is a novel F-box protein consisting of 662 amino acids, harboring the F-box domain required for the binding to Skp1 and followed by four WD40 repeats.
44	143	bound	APC/C	Cdh1p	An essential step for initiating mitosis is the inactivation of proteolysis mediated by the anaphase-promoting complex/cyclosome (APC/C) bound to its regulator Cdh1p/Hct1p.
44	144	bound	APC/C	Hct1p	An essential step for initiating mitosis is the inactivation of proteolysis mediated by the anaphase-promoting complex/cyclosome (APC/C) bound to its regulator Cdh1p/Hct1p.
44	145	bound	Cdh1p	APC/C	An essential step for initiating mitosis is the inactivation of proteolysis mediated by the anaphase-promoting complex/cyclosome (APC/C) bound to its regulator Cdh1p/Hct1p.
44	146	bound	Hct1p	APC/C	An essential step for initiating mitosis is the inactivation of proteolysis mediated by the anaphase-promoting complex/cyclosome (APC/C) bound to its regulator Cdh1p/Hct1p.
45	147	association	APC	Hct1	Analysis of Hct1 derivatives identified the C-box, a motif required for APC association of Hct1 and conserved among Cdc20-related proteins.
45	148	association	Hct1	APC	Analysis of Hct1 derivatives identified the C-box, a motif required for APC association of Hct1 and conserved among Cdc20-related proteins.
46	149	interaction	HIF-alpha	pVHL	Analysis of pVHL/HIF-alpha interactions defined short sequences of conserved residues within the internal transactivation domains of HIF-alpha molecules sufficient for recognition by pVHL.
46	150	interaction	pVHL	HIF-alpha	Analysis of pVHL/HIF-alpha interactions defined short sequences of conserved residues within the internal transactivation domains of HIF-alpha molecules sufficient for recognition by pVHL.
47	151	interaction	SIP	Siah1	Analysis of the electrostatic surface potential of the Siah1 dimer reveals that the beta-sheet concavity is predominately electronegative, suggesting that the protein-protein interactions between Siah1 and SIP are mediated by ionic contacts.
47	152	interaction	Siah1	SIP	Analysis of the electrostatic surface potential of the Siah1 dimer reveals that the beta-sheet concavity is predominately electronegative, suggesting that the protein-protein interactions between Siah1 and SIP are mediated by ionic contacts.
48	153	target	APC	Cut2	Anaphase-promoting complex or cyclosome (APC) is a ubiquitin ligase which specifically targets mitotic regulatory factors such as Pds1/Cut2 and cyclin B. Identification of the subunits of multiprotein complex APC in several species revealed the highly conserved composition of APC from yeast to human.
48	154	target	APC	Pds1	Anaphase-promoting complex or cyclosome (APC) is a ubiquitin ligase which specifically targets mitotic regulatory factors such as Pds1/Cut2 and cyclin B. Identification of the subunits of multiprotein complex APC in several species revealed the highly conserved composition of APC from yeast to human.
48	155	target	APC	cyclin B	Anaphase-promoting complex or cyclosome (APC) is a ubiquitin ligase which specifically targets mitotic regulatory factors such as Pds1/Cut2 and cyclin B. Identification of the subunits of multiprotein complex APC in several species revealed the highly conserved composition of APC from yeast to human.
48	156	target	Cut2	APC	Anaphase-promoting complex or cyclosome (APC) is a ubiquitin ligase which specifically targets mitotic regulatory factors such as Pds1/Cut2 and cyclin B. Identification of the subunits of multiprotein complex APC in several species revealed the highly conserved composition of APC from yeast to human.
48	157	target	Pds1	APC	Anaphase-promoting complex or cyclosome (APC) is a ubiquitin ligase which specifically targets mitotic regulatory factors such as Pds1/Cut2 and cyclin B. Identification of the subunits of multiprotein complex APC in several species revealed the highly conserved composition of APC from yeast to human.
48	158	target	cyclin B	APC	Anaphase-promoting complex or cyclosome (APC) is a ubiquitin ligase which specifically targets mitotic regulatory factors such as Pds1/Cut2 and cyclin B. Identification of the subunits of multiprotein complex APC in several species revealed the highly conserved composition of APC from yeast to human.
49	159	target	APC	cyclin B	Anaphase-promoting complex/cyclosome (APC) is a ubiquitin ligase that targets cyclin B and factors regulating sister chromatid separation for proteolysis by the proteasome and, consequently, regulates metaphase-anaphase transition and exit from mitosis.
49	160	target	cyclin B	APC	Anaphase-promoting complex/cyclosome (APC) is a ubiquitin ligase that targets cyclin B and factors regulating sister chromatid separation for proteolysis by the proteasome and, consequently, regulates metaphase-anaphase transition and exit from mitosis.
50	161	ubiquitinate	APC	Cut2	Anaphase-promoting complex/cyclosome (APC) specifically ubiquitinates Cut2/Pds1 at metaphase-anaphase transition, and ubiquitinates Cyclin B in late mitosis and G1 phase.
50	162	ubiquitinate	APC	Cyclin B	Anaphase-promoting complex/cyclosome (APC) specifically ubiquitinates Cut2/Pds1 at metaphase-anaphase transition, and ubiquitinates Cyclin B in late mitosis and G1 phase.
50	163	ubiquitinate	APC	Pds1	Anaphase-promoting complex/cyclosome (APC) specifically ubiquitinates Cut2/Pds1 at metaphase-anaphase transition, and ubiquitinates Cyclin B in late mitosis and G1 phase.
50	164	ubiquitinate	Cut2	APC	Anaphase-promoting complex/cyclosome (APC) specifically ubiquitinates Cut2/Pds1 at metaphase-anaphase transition, and ubiquitinates Cyclin B in late mitosis and G1 phase.
50	165	ubiquitinate	Cyclin B	APC	Anaphase-promoting complex/cyclosome (APC) specifically ubiquitinates Cut2/Pds1 at metaphase-anaphase transition, and ubiquitinates Cyclin B in late mitosis and G1 phase.
50	166	ubiquitinate	Pds1	APC	Anaphase-promoting complex/cyclosome (APC) specifically ubiquitinates Cut2/Pds1 at metaphase-anaphase transition, and ubiquitinates Cyclin B in late mitosis and G1 phase.
51	167	phosphorylation	IKK alpha	p100	Another activation pathway, with no known physiological inducers, involves ubiquitin-mediated processing of the NF-kappa B2 inhibitory protein p100 and is dependent on phosphorylation of p100 by IKK alpha.
51	168	inhibitory	NF-kappa B2	p100	Another activation pathway, with no known physiological inducers, involves ubiquitin-mediated processing of the NF-kappa B2 inhibitory protein p100 and is dependent on phosphorylation of p100 by IKK alpha.
51	169	phosphorylation	p100	IKK alpha	Another activation pathway, with no known physiological inducers, involves ubiquitin-mediated processing of the NF-kappa B2 inhibitory protein p100 and is dependent on phosphorylation of p100 by IKK alpha.
51	170	inhibitory	p100	NF-kappa B2	Another activation pathway, with no known physiological inducers, involves ubiquitin-mediated processing of the NF-kappa B2 inhibitory protein p100 and is dependent on phosphorylation of p100 by IKK alpha.
52	171	conjugated	Apg12	Apg5	Apg12 is finally conjugated to Apg5 via an isopeptide bond.
52	172	conjugated	Apg5	Apg12	Apg12 is finally conjugated to Apg5 via an isopeptide bond.
53	173	transferred	Apg10p	Apg12p	Apg12p is then transferred to Apg10p, an E2-like enzyme, and conjugated with Apg5p, whereas Apg8p is transferred to Apg3p, another E2-like enzyme, followed by conjugation with phosphatidylethanolamine.
53	174	transferred	Apg12p	Apg10p	Apg12p is then transferred to Apg10p, an E2-like enzyme, and conjugated with Apg5p, whereas Apg8p is transferred to Apg3p, another E2-like enzyme, followed by conjugation with phosphatidylethanolamine.
53	175	conjugate	Apg12p	Apg5p	Apg12p is then transferred to Apg10p, an E2-like enzyme, and conjugated with Apg5p, whereas Apg8p is transferred to Apg3p, another E2-like enzyme, followed by conjugation with phosphatidylethanolamine.
53	176	transferred	Apg3p	Apg8p	Apg12p is then transferred to Apg10p, an E2-like enzyme, and conjugated with Apg5p, whereas Apg8p is transferred to Apg3p, another E2-like enzyme, followed by conjugation with phosphatidylethanolamine.
53	177	conjugate	Apg5p	Apg12p	Apg12p is then transferred to Apg10p, an E2-like enzyme, and conjugated with Apg5p, whereas Apg8p is transferred to Apg3p, another E2-like enzyme, followed by conjugation with phosphatidylethanolamine.
53	178	transferred	Apg8p	Apg3p	Apg12p is then transferred to Apg10p, an E2-like enzyme, and conjugated with Apg5p, whereas Apg8p is transferred to Apg3p, another E2-like enzyme, followed by conjugation with phosphatidylethanolamine.
54	179	interact	Apg16p	Apg5p	Apg16p interacts with Apg12p-conjugated Apg5p and less preferentially with unconjugated Apg5p.
54	180	interact	Apg5p	Apg16p	Apg16p interacts with Apg12p-conjugated Apg5p and less preferentially with unconjugated Apg5p.
55	181	activate	Apg12	Apg7	Apg7 activates two different ubiquitin-like proteins, Apg12 and Apg8, and assigns them to specific E2 enzymes, Apg10 and Apg3, respectively.
55	182	activate	Apg7	Apg12	Apg7 activates two different ubiquitin-like proteins, Apg12 and Apg8, and assigns them to specific E2 enzymes, Apg10 and Apg3, respectively.
55	183	activate	Apg7	Apg8	Apg7 activates two different ubiquitin-like proteins, Apg12 and Apg8, and assigns them to specific E2 enzymes, Apg10 and Apg3, respectively.
55	184	activate	Apg8	Apg7	Apg7 activates two different ubiquitin-like proteins, Apg12 and Apg8, and assigns them to specific E2 enzymes, Apg10 and Apg3, respectively.
56	185	conjugation	Apg12p	Apg5p	Apg7p and Apg10p catalyze the conjugation of Apg12p to Apg5p.
56	186	conjugation	Apg5p	Apg12p	Apg7p and Apg10p catalyze the conjugation of Apg12p to Apg5p.
57	187	transfer	Apg3	Apg8	Apg8 is a ubiquitin-like protein that is activated by an E1 protein, Apg7, and is transferred subsequently to the E2 enzymes Apg3/Aut1.
57	188	activate	Apg7	Apg8	Apg8 is a ubiquitin-like protein that is activated by an E1 protein, Apg7, and is transferred subsequently to the E2 enzymes Apg3/Aut1.
57	189	transfer	Apg8	Apg3	Apg8 is a ubiquitin-like protein that is activated by an E1 protein, Apg7, and is transferred subsequently to the E2 enzymes Apg3/Aut1.
57	190	activate	Apg8	Apg7	Apg8 is a ubiquitin-like protein that is activated by an E1 protein, Apg7, and is transferred subsequently to the E2 enzymes Apg3/Aut1.
57	191	transfer	Apg8	Aut1	Apg8 is a ubiquitin-like protein that is activated by an E1 protein, Apg7, and is transferred subsequently to the E2 enzymes Apg3/Aut1.
57	192	transfer	Aut1	Apg8	Apg8 is a ubiquitin-like protein that is activated by an E1 protein, Apg7, and is transferred subsequently to the E2 enzymes Apg3/Aut1.
58	193	interact	Ark1p	Bir1p	Ark1p interacts physically and/or genetically with the survivin and INCENP orthologs Bir1p and Pic1p.
58	194	interact	Ark1p	Pic1p	Ark1p interacts physically and/or genetically with the survivin and INCENP orthologs Bir1p and Pic1p.
58	195	interact	Ark1p	survivin	Ark1p interacts physically and/or genetically with the survivin and INCENP orthologs Bir1p and Pic1p.
58	196	interact	Bir1p	Ark1p	Ark1p interacts physically and/or genetically with the survivin and INCENP orthologs Bir1p and Pic1p.
58	197	interact	Pic1p	Ark1p	Ark1p interacts physically and/or genetically with the survivin and INCENP orthologs Bir1p and Pic1p.
58	198	interact	survivin	Ark1p	Ark1p interacts physically and/or genetically with the survivin and INCENP orthologs Bir1p and Pic1p.
59	199	bind	N4WBP5A	Nedd4	As N4WBP5A binds Nedd4/Nedd4-2 via PPXY motif/WW domain interactions and appears to be associated with specific intracellular vesicles, we propose that N4WBP5A functions by regulating Nedd4/Nedd4-2 availability and trafficking.
59	200	bind	N4WBP5A	Nedd4-2	As N4WBP5A binds Nedd4/Nedd4-2 via PPXY motif/WW domain interactions and appears to be associated with specific intracellular vesicles, we propose that N4WBP5A functions by regulating Nedd4/Nedd4-2 availability and trafficking.
59	201	bind	Nedd4	N4WBP5A	As N4WBP5A binds Nedd4/Nedd4-2 via PPXY motif/WW domain interactions and appears to be associated with specific intracellular vesicles, we propose that N4WBP5A functions by regulating Nedd4/Nedd4-2 availability and trafficking.
59	202	bind	Nedd4-2	N4WBP5A	As N4WBP5A binds Nedd4/Nedd4-2 via PPXY motif/WW domain interactions and appears to be associated with specific intracellular vesicles, we propose that N4WBP5A functions by regulating Nedd4/Nedd4-2 availability and trafficking.
60	203	conjugate	IkappaBalpha	SUMO-1	As SAE1/SAE2, Ubch9, SUMO-1, and IkappaBalpha are all homogeneous, recombinant proteins, it appears that SUMO-1 conjugation of IkappaBalpha in vitro does not require the equivalent of an E3 ubiquitin protein ligase activity.
60	204	conjugate	SUMO-1	IkappaBalpha	As SAE1/SAE2, Ubch9, SUMO-1, and IkappaBalpha are all homogeneous, recombinant proteins, it appears that SUMO-1 conjugation of IkappaBalpha in vitro does not require the equivalent of an E3 ubiquitin protein ligase activity.
61	205	interaction	E6	E6AP	As an attempt to employ interaction between HPV viral oncogene E6 and a cellular protein E6AP for in vitro screening system of drugs against HPV infection, we primarily investigated the E6AP-E6 binding through pull down assay and enzyme-linked immunosorbent assay (ELISA).
61	206	interaction	E6AP	E6	As an attempt to employ interaction between HPV viral oncogene E6 and a cellular protein E6AP for in vitro screening system of drugs against HPV infection, we primarily investigated the E6AP-E6 binding through pull down assay and enzyme-linked immunosorbent assay (ELISA).
62	207	activate	APC	MPF	As these phosphorylations are thought to be essential for APC/cyclosome activation in eggs and early embryos, we conclude that at least two events are required for MPF to activate the APC/cyclosome, allowing both chromatid segregation and full degradation of mitotic cyclins.
62	208	activate	MPF	APC	As these phosphorylations are thought to be essential for APC/cyclosome activation in eggs and early embryos, we conclude that at least two events are required for MPF to activate the APC/cyclosome, allowing both chromatid segregation and full degradation of mitotic cyclins.
63	209	bind	CSN	p53	As visualized by electron microscopy, p53 binds with high affinity to the native CSN complex.
63	210	bind	p53	CSN	As visualized by electron microscopy, p53 binds with high affinity to the native CSN complex.
64	211	modification	SUMO-1	c-Jun	As with c-Jun, SUMO-1 modification of p53 is abrogated by phosphorylation but remains unaltered upon chemical damage to DNA or Mdm2-mediated ubiquitination.
64	212	modification	SUMO-1	p53	As with c-Jun, SUMO-1 modification of p53 is abrogated by phosphorylation but remains unaltered upon chemical damage to DNA or Mdm2-mediated ubiquitination.
64	213	modification	c-Jun	SUMO-1	As with c-Jun, SUMO-1 modification of p53 is abrogated by phosphorylation but remains unaltered upon chemical damage to DNA or Mdm2-mediated ubiquitination.
64	214	modification	p53	SUMO-1	As with c-Jun, SUMO-1 modification of p53 is abrogated by phosphorylation but remains unaltered upon chemical damage to DNA or Mdm2-mediated ubiquitination.
65	215	interaction	a1	alpha2	Association depends on N-terminal coiled-coil interactions between a1 and alpha2.
65	216	interaction	alpha2	a1	Association depends on N-terminal coiled-coil interactions between a1 and alpha2.
66	217	bind	IPaseT	Ub	At high Ub concentrations, where both the activation and inhibition sites are occupied, IPaseT cannot bind Ub-H.
66	218	bind	Ub	IPaseT	At high Ub concentrations, where both the activation and inhibition sites are occupied, IPaseT cannot bind Ub-H.
67	219	ubiquitinate	APC	Cut2	At the metaphase-anaphase transition the APC ubiquitinates proteins such as Pds1 in budding yeast and Cut2 in fission yeast whose subsequent degradation by the 26S proteasome is essential for the initiation of sister chromatid separation.
67	220	ubiquitinate	APC	Pds1	At the metaphase-anaphase transition the APC ubiquitinates proteins such as Pds1 in budding yeast and Cut2 in fission yeast whose subsequent degradation by the 26S proteasome is essential for the initiation of sister chromatid separation.
67	221	ubiquitinate	Cut2	APC	At the metaphase-anaphase transition the APC ubiquitinates proteins such as Pds1 in budding yeast and Cut2 in fission yeast whose subsequent degradation by the 26S proteasome is essential for the initiation of sister chromatid separation.
67	222	ubiquitinate	Pds1	APC	At the metaphase-anaphase transition the APC ubiquitinates proteins such as Pds1 in budding yeast and Cut2 in fission yeast whose subsequent degradation by the 26S proteasome is essential for the initiation of sister chromatid separation.
68	223	associate	AtCul1	AtRbx1	AtRbx1 also associates with AtCul1 and the Arabidopsis SKP1-related proteins in planta, indicating that it is part of plant SCF complexes.
68	224	associate	AtRbx1	AtCul1	AtRbx1 also associates with AtCul1 and the Arabidopsis SKP1-related proteins in planta, indicating that it is part of plant SCF complexes.
69	225	ubiquitinate	Cdc20	Cdh1	Aur-A contains both of the two known APC/C recognition signals, (1) a C-terminal D box similar to those required for ubiquitin-dependent destruction of cyclin B and several other mitotic proteins, and (2) an N-terminal KEN box similar to that found on cdc20, which is ubiquitinated in response to APC/C(Cdh1).
69	226	ubiquitinate	Cdh1	Cdc20	Aur-A contains both of the two known APC/C recognition signals, (1) a C-terminal D box similar to those required for ubiquitin-dependent destruction of cyclin B and several other mitotic proteins, and (2) an N-terminal KEN box similar to that found on cdc20, which is ubiquitinated in response to APC/C(Cdh1).
70	227	interaction	AxinDeltaC6	MEKK1	AxinDeltaC6 also failed to activate JNK, although it was intact in both its interaction with MEKK1 and homodimerization.
70	228	interaction	MEKK1	AxinDeltaC6	AxinDeltaC6 also failed to activate JNK, although it was intact in both its interaction with MEKK1 and homodimerization.
71	229	interact	BAG-1	CHIP	BAG-1 directly interacts with CHIP; it accepts substrates from Hsc/Hsp70 and presents associated proteins to the CHIP ubiquitin conjugation machinery.
71	230	interact	CHIP	BAG-1	BAG-1 directly interacts with CHIP; it accepts substrates from Hsc/Hsp70 and presents associated proteins to the CHIP ubiquitin conjugation machinery.
72	231	bind	E6	E6-AP	BPV-1 E6 also binds E6-AP, a ubiquitin ligase necessary for HPV E6-induced p53 degradation.
72	232	bind	E6-AP	E6	BPV-1 E6 also binds E6-AP, a ubiquitin ligase necessary for HPV E6-induced p53 degradation.
73	233	interact	TEL	UBC9	Based on our data, we conclude that UBC9 physically interacts with TEL through the HLH domain and that the interaction leads to modulation of the transcription activity of TEL.
73	234	interact	UBC9	TEL	Based on our data, we conclude that UBC9 physically interacts with TEL through the HLH domain and that the interaction leads to modulation of the transcription activity of TEL.
74	235	associate	Cdc34	Cul-1	Based on the requirement for CREM/ICER and Rad6B proteins in spermatogenesis, we determined expression of Cdc34, Rad6B, CREM/ICER isoforms, and the Skp1-Cullin-F-box ubiquitin protein ligase subunits Cul-1 and Cul-2, which are associated with Cdc34 activity during murine testicular development.
74	236	associate	Cdc34	Cul-2	Based on the requirement for CREM/ICER and Rad6B proteins in spermatogenesis, we determined expression of Cdc34, Rad6B, CREM/ICER isoforms, and the Skp1-Cullin-F-box ubiquitin protein ligase subunits Cul-1 and Cul-2, which are associated with Cdc34 activity during murine testicular development.
74	237	associate	Cul-1	Cdc34	Based on the requirement for CREM/ICER and Rad6B proteins in spermatogenesis, we determined expression of Cdc34, Rad6B, CREM/ICER isoforms, and the Skp1-Cullin-F-box ubiquitin protein ligase subunits Cul-1 and Cul-2, which are associated with Cdc34 activity during murine testicular development.
74	238	associate	Cul-2	Cdc34	Based on the requirement for CREM/ICER and Rad6B proteins in spermatogenesis, we determined expression of Cdc34, Rad6B, CREM/ICER isoforms, and the Skp1-Cullin-F-box ubiquitin protein ligase subunits Cul-1 and Cul-2, which are associated with Cdc34 activity during murine testicular development.
75	239	association	Cln2	grr1	Based on these results, we constructed grr1 mutants that are defective in association with either Skp1 or Cln2.
75	240	association	Skp1	grr1	Based on these results, we constructed grr1 mutants that are defective in association with either Skp1 or Cln2.
75	241	association	grr1	Cln2	Based on these results, we constructed grr1 mutants that are defective in association with either Skp1 or Cln2.
75	242	association	grr1	Skp1	Based on these results, we constructed grr1 mutants that are defective in association with either Skp1 or Cln2.
76	243	modification	AtCUL1	RUB	Because AtCUL1 is a component of the ubiquitin protein ligase SCF(TIR1), a complex that also functions in auxin response, we propose that RUB modification of AtCUL1 is important for auxin response.
76	244	modification	RUB	AtCUL1	Because AtCUL1 is a component of the ubiquitin protein ligase SCF(TIR1), a complex that also functions in auxin response, we propose that RUB modification of AtCUL1 is important for auxin response.
77	245	inhibit	APC	BubR1	Because BubR1 also interacts with the mitotic motor CENP-E, the ability of BubR1 to inhibit APC may be regulated by kinetochore tension or occupancy.
77	246	inhibit	BubR1	APC	Because BubR1 also interacts with the mitotic motor CENP-E, the ability of BubR1 to inhibit APC may be regulated by kinetochore tension or occupancy.
77	247	interact	BubR1	CENP-E	Because BubR1 also interacts with the mitotic motor CENP-E, the ability of BubR1 to inhibit APC may be regulated by kinetochore tension or occupancy.
77	248	interact	CENP-E	BubR1	Because BubR1 also interacts with the mitotic motor CENP-E, the ability of BubR1 to inhibit APC may be regulated by kinetochore tension or occupancy.
78	249	bound	H2A	ubiquitin	Because a 10% increase in the H2A/DNA ratio observed in interphase-mitosis transition explained the stoichiometric conversion of A24 to H2A, it appears that ubiquitin bound to H2A of nucleosomal surfaces in interphase is released at mitosis whereas the total H2A remains as a structural component of nucleosomes.
78	250	bound	ubiquitin	H2A	Because a 10% increase in the H2A/DNA ratio observed in interphase-mitosis transition explained the stoichiometric conversion of A24 to H2A, it appears that ubiquitin bound to H2A of nucleosomal surfaces in interphase is released at mitosis whereas the total H2A remains as a structural component of nucleosomes.
79	251	interact	HDACs	TFII-I	Because nuclear dots are believed often to harbor components of histone deacetylase enzymes (HDACs), we investigated whether TFII-I family proteins colocalize and interact with HDACs.
79	252	interact	TFII-I	HDACs	Because nuclear dots are believed often to harbor components of histone deacetylase enzymes (HDACs), we investigated whether TFII-I family proteins colocalize and interact with HDACs.
80	253	interact	IFN-alpha receptor	IFN-tau	Because type 1 IFNs induce UCRP, IFN-tau probably interacts with the janus kinase (Jak)-associated IFN-alpha receptor to phosphorylate signal transducers and activators of transcription (STAT) and/or interferon regulatory factor-1 (IRF-1).
80	254	interact	IFN-tau	IFN-alpha receptor	Because type 1 IFNs induce UCRP, IFN-tau probably interacts with the janus kinase (Jak)-associated IFN-alpha receptor to phosphorylate signal transducers and activators of transcription (STAT) and/or interferon regulatory factor-1 (IRF-1).
80	255	phosphorylate	IFN-tau	IRF-1	Because type 1 IFNs induce UCRP, IFN-tau probably interacts with the janus kinase (Jak)-associated IFN-alpha receptor to phosphorylate signal transducers and activators of transcription (STAT) and/or interferon regulatory factor-1 (IRF-1).
80	256	phosphorylate	IFN-tau	STATs	Because type 1 IFNs induce UCRP, IFN-tau probably interacts with the janus kinase (Jak)-associated IFN-alpha receptor to phosphorylate signal transducers and activators of transcription (STAT) and/or interferon regulatory factor-1 (IRF-1).
80	257	phosphorylate	IRF-1	IFN-tau	Because type 1 IFNs induce UCRP, IFN-tau probably interacts with the janus kinase (Jak)-associated IFN-alpha receptor to phosphorylate signal transducers and activators of transcription (STAT) and/or interferon regulatory factor-1 (IRF-1).
80	258	phosphorylate	STATs	IFN-tau	Because type 1 IFNs induce UCRP, IFN-tau probably interacts with the janus kinase (Jak)-associated IFN-alpha receptor to phosphorylate signal transducers and activators of transcription (STAT) and/or interferon regulatory factor-1 (IRF-1).
81	259	complex	Cullin1	HOS	Being a part of SCF complex with Skp1 and Cullin1, HOS specifically interacted with the phosphorylated IkappaB and beta-catenin, targeting these proteins for proteasome-dependent degradation in vivo.
81	260	complex	Cullin1	Skp1	Being a part of SCF complex with Skp1 and Cullin1, HOS specifically interacted with the phosphorylated IkappaB and beta-catenin, targeting these proteins for proteasome-dependent degradation in vivo.
81	261	complex	HOS	Cullin1	Being a part of SCF complex with Skp1 and Cullin1, HOS specifically interacted with the phosphorylated IkappaB and beta-catenin, targeting these proteins for proteasome-dependent degradation in vivo.
81	262	interact	HOS	IkappaB	Being a part of SCF complex with Skp1 and Cullin1, HOS specifically interacted with the phosphorylated IkappaB and beta-catenin, targeting these proteins for proteasome-dependent degradation in vivo.
81	263	complex	HOS	Skp1	Being a part of SCF complex with Skp1 and Cullin1, HOS specifically interacted with the phosphorylated IkappaB and beta-catenin, targeting these proteins for proteasome-dependent degradation in vivo.
81	264	interact	HOS	beta-catenin	Being a part of SCF complex with Skp1 and Cullin1, HOS specifically interacted with the phosphorylated IkappaB and beta-catenin, targeting these proteins for proteasome-dependent degradation in vivo.
81	265	interact	IkappaB	HOS	Being a part of SCF complex with Skp1 and Cullin1, HOS specifically interacted with the phosphorylated IkappaB and beta-catenin, targeting these proteins for proteasome-dependent degradation in vivo.
81	266	complex	Skp1	Cullin1	Being a part of SCF complex with Skp1 and Cullin1, HOS specifically interacted with the phosphorylated IkappaB and beta-catenin, targeting these proteins for proteasome-dependent degradation in vivo.
81	267	complex	Skp1	HOS	Being a part of SCF complex with Skp1 and Cullin1, HOS specifically interacted with the phosphorylated IkappaB and beta-catenin, targeting these proteins for proteasome-dependent degradation in vivo.
81	268	interact	beta-catenin	HOS	Being a part of SCF complex with Skp1 and Cullin1, HOS specifically interacted with the phosphorylated IkappaB and beta-catenin, targeting these proteins for proteasome-dependent degradation in vivo.
82	269	associating	BetaTrCP	IkappaB	BetaTrCP and HOS are closely related F-box proteins, which play key roles in ubiquitination and degradation of beta-catenin and IkappaB through associating with those phosphorylated substrates and recruiting SCF E3 ubiquitin ligase.
82	270	associating	BetaTrCP	beta-catenin	BetaTrCP and HOS are closely related F-box proteins, which play key roles in ubiquitination and degradation of beta-catenin and IkappaB through associating with those phosphorylated substrates and recruiting SCF E3 ubiquitin ligase.
82	271	associating	HOS	IkappaB	BetaTrCP and HOS are closely related F-box proteins, which play key roles in ubiquitination and degradation of beta-catenin and IkappaB through associating with those phosphorylated substrates and recruiting SCF E3 ubiquitin ligase.
82	272	associating	HOS	beta-catenin	BetaTrCP and HOS are closely related F-box proteins, which play key roles in ubiquitination and degradation of beta-catenin and IkappaB through associating with those phosphorylated substrates and recruiting SCF E3 ubiquitin ligase.
82	273	associating	IkappaB	BetaTrCP	BetaTrCP and HOS are closely related F-box proteins, which play key roles in ubiquitination and degradation of beta-catenin and IkappaB through associating with those phosphorylated substrates and recruiting SCF E3 ubiquitin ligase.
82	274	associating	IkappaB	HOS	BetaTrCP and HOS are closely related F-box proteins, which play key roles in ubiquitination and degradation of beta-catenin and IkappaB through associating with those phosphorylated substrates and recruiting SCF E3 ubiquitin ligase.
82	275	associating	beta-catenin	BetaTrCP	BetaTrCP and HOS are closely related F-box proteins, which play key roles in ubiquitination and degradation of beta-catenin and IkappaB through associating with those phosphorylated substrates and recruiting SCF E3 ubiquitin ligase.
82	276	associating	beta-catenin	HOS	BetaTrCP and HOS are closely related F-box proteins, which play key roles in ubiquitination and degradation of beta-catenin and IkappaB through associating with those phosphorylated substrates and recruiting SCF E3 ubiquitin ligase.
83	277	recognize	HOS	IkBa	Binding of Skp1 augments the ability of HOS to recognize the phosphorylated IkBa.
83	278	recognize	IkBa	HOS	Binding of Skp1 augments the ability of HOS to recognize the phosphorylated IkBa.
84	279	bind	APC11	APC2	Both APC11 and UbcH10 bind to the C-terminal cullin homology domain of APC2, whereas Ubc4 interacts with APC11 directly.
84	280	interact	APC11	Ubc4	Both APC11 and UbcH10 bind to the C-terminal cullin homology domain of APC2, whereas Ubc4 interacts with APC11 directly.
84	281	bind	APC2	APC11	Both APC11 and UbcH10 bind to the C-terminal cullin homology domain of APC2, whereas Ubc4 interacts with APC11 directly.
84	282	bind	APC2	UbcH10	Both APC11 and UbcH10 bind to the C-terminal cullin homology domain of APC2, whereas Ubc4 interacts with APC11 directly.
84	283	interact	Ubc4	APC11	Both APC11 and UbcH10 bind to the C-terminal cullin homology domain of APC2, whereas Ubc4 interacts with APC11 directly.
84	284	bind	UbcH10	APC2	Both APC11 and UbcH10 bind to the C-terminal cullin homology domain of APC2, whereas Ubc4 interacts with APC11 directly.
85	285	associate	COP9	NbRar1	Both NbRar1 and NbSGT1 associate with the COP9 signalosome, another multiprotein complex involved in protein degradation via the ubiquitin-proteasome pathway.
85	286	associate	COP9	NbSGT1	Both NbRar1 and NbSGT1 associate with the COP9 signalosome, another multiprotein complex involved in protein degradation via the ubiquitin-proteasome pathway.
85	287	associate	NbRar1	COP9	Both NbRar1 and NbSGT1 associate with the COP9 signalosome, another multiprotein complex involved in protein degradation via the ubiquitin-proteasome pathway.
85	288	associate	NbSGT1	COP9	Both NbRar1 and NbSGT1 associate with the COP9 signalosome, another multiprotein complex involved in protein degradation via the ubiquitin-proteasome pathway.
86	289	interaction	Pap1	Uba2	Both Uba2 and Ufd1 can be co-immunoprecipitated from extracts with Pap1, confirming in vitro the interaction identified by two-hybrid analysis.
86	290	interaction	Pap1	Ufd1	Both Uba2 and Ufd1 can be co-immunoprecipitated from extracts with Pap1, confirming in vitro the interaction identified by two-hybrid analysis.
86	291	interaction	Uba2	Pap1	Both Uba2 and Ufd1 can be co-immunoprecipitated from extracts with Pap1, confirming in vitro the interaction identified by two-hybrid analysis.
86	292	interaction	Ufd1	Pap1	Both Uba2 and Ufd1 can be co-immunoprecipitated from extracts with Pap1, confirming in vitro the interaction identified by two-hybrid analysis.
87	293	bind	NXF2	nxt	Both human p15 homologues (nxt and nxt2) bind TAP, NXF2, and NXF3.
87	294	bind	NXF2	nxt2	Both human p15 homologues (nxt and nxt2) bind TAP, NXF2, and NXF3.
87	295	bind	NXF3	nxt	Both human p15 homologues (nxt and nxt2) bind TAP, NXF2, and NXF3.
87	296	bind	NXF3	nxt2	Both human p15 homologues (nxt and nxt2) bind TAP, NXF2, and NXF3.
87	297	bind	TAP	nxt	Both human p15 homologues (nxt and nxt2) bind TAP, NXF2, and NXF3.
87	298	bind	TAP	nxt2	Both human p15 homologues (nxt and nxt2) bind TAP, NXF2, and NXF3.
87	299	bind	nxt	NXF2	Both human p15 homologues (nxt and nxt2) bind TAP, NXF2, and NXF3.
87	300	bind	nxt	NXF3	Both human p15 homologues (nxt and nxt2) bind TAP, NXF2, and NXF3.
87	301	bind	nxt	TAP	Both human p15 homologues (nxt and nxt2) bind TAP, NXF2, and NXF3.
87	302	bind	nxt2	NXF2	Both human p15 homologues (nxt and nxt2) bind TAP, NXF2, and NXF3.
87	303	bind	nxt2	NXF3	Both human p15 homologues (nxt and nxt2) bind TAP, NXF2, and NXF3.
87	304	bind	nxt2	TAP	Both human p15 homologues (nxt and nxt2) bind TAP, NXF2, and NXF3.
88	305	bind	CAND1	CUL1	Both in vivo and in vitro, CAND1 prevents the binding of SKP1 and SKP2 to CUL1 while dissociation of CAND1 from CUL1 promotes the reverse reaction.
88	306	bind	CUL1	CAND1	Both in vivo and in vitro, CAND1 prevents the binding of SKP1 and SKP2 to CUL1 while dissociation of CAND1 from CUL1 promotes the reverse reaction.
88	307	binding	CUL1	SKP1	Both in vivo and in vitro, CAND1 prevents the binding of SKP1 and SKP2 to CUL1 while dissociation of CAND1 from CUL1 promotes the reverse reaction.
88	308	binding	CUL1	SKP2	Both in vivo and in vitro, CAND1 prevents the binding of SKP1 and SKP2 to CUL1 while dissociation of CAND1 from CUL1 promotes the reverse reaction.
88	309	binding	SKP1	CUL1	Both in vivo and in vitro, CAND1 prevents the binding of SKP1 and SKP2 to CUL1 while dissociation of CAND1 from CUL1 promotes the reverse reaction.
88	310	binding	SKP2	CUL1	Both in vivo and in vitro, CAND1 prevents the binding of SKP1 and SKP2 to CUL1 while dissociation of CAND1 from CUL1 promotes the reverse reaction.
89	311	bind	Mdm2	p53	Both p53 function and stability are tightly controlled by Mdm2, which binds to the p53 N-terminus and targets p53 for ubiquitin-mediated proteolysis.
89	312	bind	p53	Mdm2	Both p53 function and stability are tightly controlled by Mdm2, which binds to the p53 N-terminus and targets p53 for ubiquitin-mediated proteolysis.
90	313	activation	Cdc14	Cdh1	Both processes require the Cdc14 phosphatase, whose release from the nucleolus during anaphase causes dephosphorylation and thereby activation of Cdh1 and accumulation of another protein, Sic1.
90	314	activation	Cdh1	Cdc14	Both processes require the Cdc14 phosphatase, whose release from the nucleolus during anaphase causes dephosphorylation and thereby activation of Cdh1 and accumulation of another protein, Sic1.
91	315	bound	Smad7	Smurf1	Both wild-type Smurf1 (Smurf1(WT)) and Smurf1 lacking the C2 domain (Smurf1(deltaC2)) bound to Smad7 and translocated nuclear Smad7 to the cytoplasm.
91	316	bound	Smurf1	Smad7	Both wild-type Smurf1 (Smurf1(WT)) and Smurf1 lacking the C2 domain (Smurf1(deltaC2)) bound to Smad7 and translocated nuclear Smad7 to the cytoplasm.
92	317	bind	Bul1	Rsp5	Bul1 and Bul2 have been reported to bind to Rsp5, a hect (for homologous to E6-associated-protein carboxyl terminus)-type ubiquitin ligase, but involvement of Bul1 and Bul2 in protein degradation has not been demonstrated.
92	318	bind	Bul2	Rsp5	Bul1 and Bul2 have been reported to bind to Rsp5, a hect (for homologous to E6-associated-protein carboxyl terminus)-type ubiquitin ligase, but involvement of Bul1 and Bul2 in protein degradation has not been demonstrated.
92	319	bind	Rsp5	Bul1	Bul1 and Bul2 have been reported to bind to Rsp5, a hect (for homologous to E6-associated-protein carboxyl terminus)-type ubiquitin ligase, but involvement of Bul1 and Bul2 in protein degradation has not been demonstrated.
92	320	bind	Rsp5	Bul2	Bul1 and Bul2 have been reported to bind to Rsp5, a hect (for homologous to E6-associated-protein carboxyl terminus)-type ubiquitin ligase, but involvement of Bul1 and Bul2 in protein degradation has not been demonstrated.
93	321	interact	SCONB	SCONC	By analogy with other systems, it seems likely that the SCONC protein interacts with SCONB. sconC mRNA is present in the sconC3 and sconB2 mutants and the level of the sconC transcript seems not to be significantly regulated by supplementation of the medium with sulphur.
93	322	interact	SCONC	SCONB	By analogy with other systems, it seems likely that the SCONC protein interacts with SCONB. sconC mRNA is present in the sconC3 and sconB2 mutants and the level of the sconC transcript seems not to be significantly regulated by supplementation of the medium with sulphur.
94	323	interact	Cdc20	Pds1	By co-immunoprecipitation, we found that Hct1 interacted with the mitotic cyclins Clb2 and Clb3 and the polo-related kinase Cdc5, whereas Cdc20 interacted with the securin Pds1.
94	324	interact	Cdc5	Hct1	By co-immunoprecipitation, we found that Hct1 interacted with the mitotic cyclins Clb2 and Clb3 and the polo-related kinase Cdc5, whereas Cdc20 interacted with the securin Pds1.
94	325	interact	Clb2	Hct1	By co-immunoprecipitation, we found that Hct1 interacted with the mitotic cyclins Clb2 and Clb3 and the polo-related kinase Cdc5, whereas Cdc20 interacted with the securin Pds1.
94	326	interact	Clb3	Hct1	By co-immunoprecipitation, we found that Hct1 interacted with the mitotic cyclins Clb2 and Clb3 and the polo-related kinase Cdc5, whereas Cdc20 interacted with the securin Pds1.
94	327	interact	Hct1	Cdc5	By co-immunoprecipitation, we found that Hct1 interacted with the mitotic cyclins Clb2 and Clb3 and the polo-related kinase Cdc5, whereas Cdc20 interacted with the securin Pds1.
94	328	interact	Hct1	Clb2	By co-immunoprecipitation, we found that Hct1 interacted with the mitotic cyclins Clb2 and Clb3 and the polo-related kinase Cdc5, whereas Cdc20 interacted with the securin Pds1.
94	329	interact	Hct1	Clb3	By co-immunoprecipitation, we found that Hct1 interacted with the mitotic cyclins Clb2 and Clb3 and the polo-related kinase Cdc5, whereas Cdc20 interacted with the securin Pds1.
94	330	interact	Pds1	Cdc20	By co-immunoprecipitation, we found that Hct1 interacted with the mitotic cyclins Clb2 and Clb3 and the polo-related kinase Cdc5, whereas Cdc20 interacted with the securin Pds1.
95	331	activation	Akt	IRS-1	By contrast, IRS-1 activation of Akt and ERK1/2 was not inhibited by chronic insulin/IGF-1 stimulation in IRS-2-deficient mouse embryo fibroblasts.
95	332	activation	ERK1	IRS-1	By contrast, IRS-1 activation of Akt and ERK1/2 was not inhibited by chronic insulin/IGF-1 stimulation in IRS-2-deficient mouse embryo fibroblasts.
95	333	activation	ERK2	IRS-1	By contrast, IRS-1 activation of Akt and ERK1/2 was not inhibited by chronic insulin/IGF-1 stimulation in IRS-2-deficient mouse embryo fibroblasts.
95	334	activation	IRS-1	Akt	By contrast, IRS-1 activation of Akt and ERK1/2 was not inhibited by chronic insulin/IGF-1 stimulation in IRS-2-deficient mouse embryo fibroblasts.
95	335	activation	IRS-1	ERK1	By contrast, IRS-1 activation of Akt and ERK1/2 was not inhibited by chronic insulin/IGF-1 stimulation in IRS-2-deficient mouse embryo fibroblasts.
95	336	activation	IRS-1	ERK2	By contrast, IRS-1 activation of Akt and ERK1/2 was not inhibited by chronic insulin/IGF-1 stimulation in IRS-2-deficient mouse embryo fibroblasts.
96	337	reduce	208-kDa	PRL1	By contrast, PRL1 reduces the interaction of SKP1/ASK1 with SnRKs.
96	338	interact	ASK1	SnRK	By contrast, PRL1 reduces the interaction of SKP1/ASK1 with SnRKs.
96	339	reduce	Gsa11	PRL1	By contrast, PRL1 reduces the interaction of SKP1/ASK1 with SnRKs.
96	340	reduce	PRL1	208-kDa	By contrast, PRL1 reduces the interaction of SKP1/ASK1 with SnRKs.
96	341	reduce	PRL1	Gsa11	By contrast, PRL1 reduces the interaction of SKP1/ASK1 with SnRKs.
96	342	interact	SKP1	SnRK	By contrast, PRL1 reduces the interaction of SKP1/ASK1 with SnRKs.
96	343	interact	SnRK	ASK1	By contrast, PRL1 reduces the interaction of SKP1/ASK1 with SnRKs.
96	344	interact	SnRK	SKP1	By contrast, PRL1 reduces the interaction of SKP1/ASK1 with SnRKs.
97	345	interaction	Hsa-AIP4	Hsa-CBLC	By screening in parallel a human and a Caenorhabditis elegans library using the two-hybrid procedure in yeast, we found a novel interaction between Hsa-CBLC and Hsa-AIP4 or its C. elegans counterpart Cel-WWP1.
97	346	interaction	Hsa-CBLC	Hsa-AIP4	By screening in parallel a human and a Caenorhabditis elegans library using the two-hybrid procedure in yeast, we found a novel interaction between Hsa-CBLC and Hsa-AIP4 or its C. elegans counterpart Cel-WWP1.
98	347	interact	Dot4p	Sir4p	By two-hybrid analysis, the amino-terminal third of Dot4p interacts with the silencing protein Sir4p.
98	348	interact	Sir4p	Dot4p	By two-hybrid analysis, the amino-terminal third of Dot4p interacts with the silencing protein Sir4p.
99	349	inhibitor	Z-DEVDfmk	caspase 3	C(2)-ceramide, sphingosine, and sphingomyelinase induced apoptosis in BMCMC in the presence of rIL-3 and/or rSCF, and Z-VAD-fmk (a broad caspase inhibitor), Z-DEVD-fmk (a caspase 3 inhibitor), and Z-IETD-fmk (a caspase 8 inhibitor) partially prevented apoptosis of BMCMC induced by C(2)-ceramide but not sphingosine.
99	350	inhibitor	Z-IETDfmk	caspase 8	C(2)-ceramide, sphingosine, and sphingomyelinase induced apoptosis in BMCMC in the presence of rIL-3 and/or rSCF, and Z-VAD-fmk (a broad caspase inhibitor), Z-DEVD-fmk (a caspase 3 inhibitor), and Z-IETD-fmk (a caspase 8 inhibitor) partially prevented apoptosis of BMCMC induced by C(2)-ceramide but not sphingosine.
99	351	inhibitor	Z-VADfmk	caspase	C(2)-ceramide, sphingosine, and sphingomyelinase induced apoptosis in BMCMC in the presence of rIL-3 and/or rSCF, and Z-VAD-fmk (a broad caspase inhibitor), Z-DEVD-fmk (a caspase 3 inhibitor), and Z-IETD-fmk (a caspase 8 inhibitor) partially prevented apoptosis of BMCMC induced by C(2)-ceramide but not sphingosine.
99	352	inhibitor	caspase 3	Z-DEVDfmk	C(2)-ceramide, sphingosine, and sphingomyelinase induced apoptosis in BMCMC in the presence of rIL-3 and/or rSCF, and Z-VAD-fmk (a broad caspase inhibitor), Z-DEVD-fmk (a caspase 3 inhibitor), and Z-IETD-fmk (a caspase 8 inhibitor) partially prevented apoptosis of BMCMC induced by C(2)-ceramide but not sphingosine.
99	353	inhibitor	caspase 8	Z-IETDfmk	C(2)-ceramide, sphingosine, and sphingomyelinase induced apoptosis in BMCMC in the presence of rIL-3 and/or rSCF, and Z-VAD-fmk (a broad caspase inhibitor), Z-DEVD-fmk (a caspase 3 inhibitor), and Z-IETD-fmk (a caspase 8 inhibitor) partially prevented apoptosis of BMCMC induced by C(2)-ceramide but not sphingosine.
99	354	inhibitor	caspase	Z-VADfmk	C(2)-ceramide, sphingosine, and sphingomyelinase induced apoptosis in BMCMC in the presence of rIL-3 and/or rSCF, and Z-VAD-fmk (a broad caspase inhibitor), Z-DEVD-fmk (a caspase 3 inhibitor), and Z-IETD-fmk (a caspase 8 inhibitor) partially prevented apoptosis of BMCMC induced by C(2)-ceramide but not sphingosine.
100	355	interact	C/EBPalpha	Ubc9	C/EBPalpha interacts directly with the E2 SUMO-conjugating enzyme Ubc9 and can be SUMOylated in vitro using purified recombinant components.
100	356	interact	Ubc9	C/EBPalpha	C/EBPalpha interacts directly with the E2 SUMO-conjugating enzyme Ubc9 and can be SUMOylated in vitro using purified recombinant components.
101	357	activate	APC	CDC20	CDC20 activates APC at the onset of anaphase in a destruction box (DB)-dependent manner, while CDH1 activates APC from late anaphase through G1 with apparently a much relaxed specificity for the DB.
101	358	activate	APC	CDH1	CDC20 activates APC at the onset of anaphase in a destruction box (DB)-dependent manner, while CDH1 activates APC from late anaphase through G1 with apparently a much relaxed specificity for the DB.
101	359	activate	CDC20	APC	CDC20 activates APC at the onset of anaphase in a destruction box (DB)-dependent manner, while CDH1 activates APC from late anaphase through G1 with apparently a much relaxed specificity for the DB.
101	360	activate	CDH1	APC	CDC20 activates APC at the onset of anaphase in a destruction box (DB)-dependent manner, while CDH1 activates APC from late anaphase through G1 with apparently a much relaxed specificity for the DB.
102	361	activate	APC	CDC20	CDC20/CDH1 activates the anaphase-promoting complex (APC) and targets various substrates for degradation, thereby allowing the ordered progression through mitosis and G(1).
102	362	activate	APC	CDH1	CDC20/CDH1 activates the anaphase-promoting complex (APC) and targets various substrates for degradation, thereby allowing the ordered progression through mitosis and G(1).
102	363	activate	CDC20	APC	CDC20/CDH1 activates the anaphase-promoting complex (APC) and targets various substrates for degradation, thereby allowing the ordered progression through mitosis and G(1).
102	364	activate	CDH1	APC	CDC20/CDH1 activates the anaphase-promoting complex (APC) and targets various substrates for degradation, thereby allowing the ordered progression through mitosis and G(1).
103	365	interact	CHIP	UBCH5	CHIP interacts functionally and physically with the stress-responsive ubiquitin-conjugating enzyme family UBCH5.
103	366	interact	UBCH5	CHIP	CHIP interacts functionally and physically with the stress-responsive ubiquitin-conjugating enzyme family UBCH5.
104	367	attachment	BAG-1	CHIP	CHIP mediates attachment of ubiquitin moieties to BAG-1 in conjunction with ubiquitin-conjugating enzymes of the Ubc4/5 family.
104	368	attachment	BAG-1	ubiquitin	CHIP mediates attachment of ubiquitin moieties to BAG-1 in conjunction with ubiquitin-conjugating enzymes of the Ubc4/5 family.
104	369	attachment	CHIP	BAG-1	CHIP mediates attachment of ubiquitin moieties to BAG-1 in conjunction with ubiquitin-conjugating enzymes of the Ubc4/5 family.
104	370	attachment	ubiquitin	BAG-1	CHIP mediates attachment of ubiquitin moieties to BAG-1 in conjunction with ubiquitin-conjugating enzymes of the Ubc4/5 family.
105	371	associate	CHUK	IkappaB-alpha	CHUK associates with the NF-kappaB inhibitory protein, IkappaB-alpha, in mammalian cells.
105	372	associate	IkappaB-alpha	CHUK	CHUK associates with the NF-kappaB inhibitory protein, IkappaB-alpha, in mammalian cells.
106	373	phosphorylate	CHUK	IkappaB-alpha	CHUK specifically phosphorylates IkappaB-alpha on both serine 32 and serine 36, modifications that are required for targeted degradation of IkappaB-alpha via the ubiquitin-proteasome pathway.
106	374	phosphorylate	IkappaB-alpha	CHUK	CHUK specifically phosphorylates IkappaB-alpha on both serine 32 and serine 36, modifications that are required for targeted degradation of IkappaB-alpha via the ubiquitin-proteasome pathway.
107	375	phosphorylate	CK2	MDM2	CK2 phosphorylates a single major site, Ser(267), which lies within the central acidic domain of MDM2.
107	376	phosphorylate	MDM2	CK2	CK2 phosphorylates a single major site, Ser(267), which lies within the central acidic domain of MDM2.
108	377	bind	CNrasGEF	Nedd4	CNrasGEF is ubiquitinated in cells, and this ubiquitination is augmented upon overexpression of wt-Nedd4 but is inhibited in cells overexpressing a catalytically inactive Nedd4 (Nedd4(CS)) or in cells expressing CNrasGEFDelta2PY, which cannot bind Nedd4.
108	378	bind	Nedd4	CNrasGEF	CNrasGEF is ubiquitinated in cells, and this ubiquitination is augmented upon overexpression of wt-Nedd4 but is inhibited in cells overexpressing a catalytically inactive Nedd4 (Nedd4(CS)) or in cells expressing CNrasGEFDelta2PY, which cannot bind Nedd4.
109	379	interaction	CSN	Cul1	CSN2 integrates into the CSN complex via its C-terminal region and its N-terminal half region is necessary for direct interaction with Cul1.
109	380	interaction	Cul1	CSN	CSN2 integrates into the CSN complex via its C-terminal region and its N-terminal half region is necessary for direct interaction with Cul1.
110	381	associate	CUL-1	SKP1	CUL-1 also associates with cyclin A and p19(SKP1) in vivo and, with p45(SKP2), they assemble into a large multiprotein complex.
110	382	complex	CUL-1	SKP2	CUL-1 also associates with cyclin A and p19(SKP1) in vivo and, with p45(SKP2), they assemble into a large multiprotein complex.
110	383	associate	CUL-1	cyclin A	CUL-1 also associates with cyclin A and p19(SKP1) in vivo and, with p45(SKP2), they assemble into a large multiprotein complex.
110	384	associate	CUL-1	p19	CUL-1 also associates with cyclin A and p19(SKP1) in vivo and, with p45(SKP2), they assemble into a large multiprotein complex.
110	385	complex	CUL-1	p45	CUL-1 also associates with cyclin A and p19(SKP1) in vivo and, with p45(SKP2), they assemble into a large multiprotein complex.
110	386	associate	SKP1	CUL-1	CUL-1 also associates with cyclin A and p19(SKP1) in vivo and, with p45(SKP2), they assemble into a large multiprotein complex.
110	387	complex	SKP1	SKP2	CUL-1 also associates with cyclin A and p19(SKP1) in vivo and, with p45(SKP2), they assemble into a large multiprotein complex.
110	388	complex	SKP1	cyclin A	CUL-1 also associates with cyclin A and p19(SKP1) in vivo and, with p45(SKP2), they assemble into a large multiprotein complex.
110	389	complex	SKP1	p45	CUL-1 also associates with cyclin A and p19(SKP1) in vivo and, with p45(SKP2), they assemble into a large multiprotein complex.
110	390	complex	SKP2	CUL-1	CUL-1 also associates with cyclin A and p19(SKP1) in vivo and, with p45(SKP2), they assemble into a large multiprotein complex.
110	391	complex	SKP2	SKP1	CUL-1 also associates with cyclin A and p19(SKP1) in vivo and, with p45(SKP2), they assemble into a large multiprotein complex.
110	392	complex	SKP2	cyclin A	CUL-1 also associates with cyclin A and p19(SKP1) in vivo and, with p45(SKP2), they assemble into a large multiprotein complex.
110	393	complex	SKP2	p19	CUL-1 also associates with cyclin A and p19(SKP1) in vivo and, with p45(SKP2), they assemble into a large multiprotein complex.
110	394	associate	cyclin A	CUL-1	CUL-1 also associates with cyclin A and p19(SKP1) in vivo and, with p45(SKP2), they assemble into a large multiprotein complex.
110	395	complex	cyclin A	SKP1	CUL-1 also associates with cyclin A and p19(SKP1) in vivo and, with p45(SKP2), they assemble into a large multiprotein complex.
110	396	complex	cyclin A	SKP2	CUL-1 also associates with cyclin A and p19(SKP1) in vivo and, with p45(SKP2), they assemble into a large multiprotein complex.
110	397	complex	cyclin A	p19	CUL-1 also associates with cyclin A and p19(SKP1) in vivo and, with p45(SKP2), they assemble into a large multiprotein complex.
110	398	complex	cyclin A	p45	CUL-1 also associates with cyclin A and p19(SKP1) in vivo and, with p45(SKP2), they assemble into a large multiprotein complex.
110	399	associate	p19	CUL-1	CUL-1 also associates with cyclin A and p19(SKP1) in vivo and, with p45(SKP2), they assemble into a large multiprotein complex.
110	400	complex	p19	SKP2	CUL-1 also associates with cyclin A and p19(SKP1) in vivo and, with p45(SKP2), they assemble into a large multiprotein complex.
110	401	complex	p19	cyclin A	CUL-1 also associates with cyclin A and p19(SKP1) in vivo and, with p45(SKP2), they assemble into a large multiprotein complex.
110	402	complex	p19	p45	CUL-1 also associates with cyclin A and p19(SKP1) in vivo and, with p45(SKP2), they assemble into a large multiprotein complex.
110	403	complex	p45	CUL-1	CUL-1 also associates with cyclin A and p19(SKP1) in vivo and, with p45(SKP2), they assemble into a large multiprotein complex.
110	404	complex	p45	SKP1	CUL-1 also associates with cyclin A and p19(SKP1) in vivo and, with p45(SKP2), they assemble into a large multiprotein complex.
110	405	complex	p45	cyclin A	CUL-1 also associates with cyclin A and p19(SKP1) in vivo and, with p45(SKP2), they assemble into a large multiprotein complex.
110	406	complex	p45	p19	CUL-1 also associates with cyclin A and p19(SKP1) in vivo and, with p45(SKP2), they assemble into a large multiprotein complex.
111	407	interact	CUL-1	SKR-1	CUL-1 was found to interact with SKR-1, -2, -3, -7, -8, and -10 in the yeast two-hybrid system.
111	408	interact	CUL-1	SKR-10	CUL-1 was found to interact with SKR-1, -2, -3, -7, -8, and -10 in the yeast two-hybrid system.
111	409	interact	CUL-1	SKR-2	CUL-1 was found to interact with SKR-1, -2, -3, -7, -8, and -10 in the yeast two-hybrid system.
111	410	interact	CUL-1	SKR-3	CUL-1 was found to interact with SKR-1, -2, -3, -7, -8, and -10 in the yeast two-hybrid system.
111	411	interact	CUL-1	SKR-7	CUL-1 was found to interact with SKR-1, -2, -3, -7, -8, and -10 in the yeast two-hybrid system.
111	412	interact	CUL-1	SKR-8	CUL-1 was found to interact with SKR-1, -2, -3, -7, -8, and -10 in the yeast two-hybrid system.
111	413	interact	SKR-1	CUL-1	CUL-1 was found to interact with SKR-1, -2, -3, -7, -8, and -10 in the yeast two-hybrid system.
111	414	interact	SKR-10	CUL-1	CUL-1 was found to interact with SKR-1, -2, -3, -7, -8, and -10 in the yeast two-hybrid system.
111	415	interact	SKR-2	CUL-1	CUL-1 was found to interact with SKR-1, -2, -3, -7, -8, and -10 in the yeast two-hybrid system.
111	416	interact	SKR-3	CUL-1	CUL-1 was found to interact with SKR-1, -2, -3, -7, -8, and -10 in the yeast two-hybrid system.
111	417	interact	SKR-7	CUL-1	CUL-1 was found to interact with SKR-1, -2, -3, -7, -8, and -10 in the yeast two-hybrid system.
111	418	interact	SKR-8	CUL-1	CUL-1 was found to interact with SKR-1, -2, -3, -7, -8, and -10 in the yeast two-hybrid system.
112	419	modification	HDAC4	SUMO-1	Calcium/calmodulin-dependent protein kinase (CaMK) signalling, which induces nuclear export, abrogates SUMO-1 modification of HDAC4.
112	420	modification	SUMO-1	HDAC4	Calcium/calmodulin-dependent protein kinase (CaMK) signalling, which induces nuclear export, abrogates SUMO-1 modification of HDAC4.
113	421	bind	E6	p53	Cancer-related HPVs E6 proteins bind the tumor suppressor p53 and promotes its degradation through an ubiquitin-dependent pathway.
113	422	bind	p53	E6	Cancer-related HPVs E6 proteins bind the tumor suppressor p53 and promotes its degradation through an ubiquitin-dependent pathway.
114	423	recruitment	CD28	p85	Cbl-b is involved in the recruitment of p85 to CD28 and T cell antigen receptor zeta through its E3 ubiquitin ligase activity.
114	424	recruitment	T cell antigen receptor zeta	p85	Cbl-b is involved in the recruitment of p85 to CD28 and T cell antigen receptor zeta through its E3 ubiquitin ligase activity.
114	425	recruitment	p85	CD28	Cbl-b is involved in the recruitment of p85 to CD28 and T cell antigen receptor zeta through its E3 ubiquitin ligase activity.
114	426	recruitment	p85	T cell antigen receptor zeta	Cbl-b is involved in the recruitment of p85 to CD28 and T cell antigen receptor zeta through its E3 ubiquitin ligase activity.
115	427	bind	Cdc25A	Cdk1	Cdc25A binds and activates cyclin B-Cdk1, accelerates cell division when overexpressed, and its downregulation by RNA interference (RNAi) delays mitotic entry.
115	428	bind	Cdc25A	cyclin B	Cdc25A binds and activates cyclin B-Cdk1, accelerates cell division when overexpressed, and its downregulation by RNA interference (RNAi) delays mitotic entry.
115	429	bind	Cdk1	Cdc25A	Cdc25A binds and activates cyclin B-Cdk1, accelerates cell division when overexpressed, and its downregulation by RNA interference (RNAi) delays mitotic entry.
115	430	bind	cyclin B	Cdc25A	Cdc25A binds and activates cyclin B-Cdk1, accelerates cell division when overexpressed, and its downregulation by RNA interference (RNAi) delays mitotic entry.
116	431	associate	Cdc16	Cdc26	Cdc26 associates in vivo with Doc1, Cdc16, Cdc23, and Cdc27.
116	432	associate	Cdc23	Cdc26	Cdc26 associates in vivo with Doc1, Cdc16, Cdc23, and Cdc27.
116	433	associate	Cdc26	Cdc16	Cdc26 associates in vivo with Doc1, Cdc16, Cdc23, and Cdc27.
116	434	associate	Cdc26	Cdc23	Cdc26 associates in vivo with Doc1, Cdc16, Cdc23, and Cdc27.
116	435	associate	Cdc26	Cdc27	Cdc26 associates in vivo with Doc1, Cdc16, Cdc23, and Cdc27.
116	436	associate	Cdc26	Doc1	Cdc26 associates in vivo with Doc1, Cdc16, Cdc23, and Cdc27.
116	437	associate	Cdc27	Cdc26	Cdc26 associates in vivo with Doc1, Cdc16, Cdc23, and Cdc27.
116	438	associate	Doc1	Cdc26	Cdc26 associates in vivo with Doc1, Cdc16, Cdc23, and Cdc27.
117	439	inhibitor	Cdc2p	Rum1p	Cdc6p cannot functionally replace Cdc18p, but instead interferes with the proteolysis of both Cdc18p and Rum1p, the inhibitor of the protein kinase Cdc2p.
117	440	inhibitor	Rum1p	Cdc2p	Cdc6p cannot functionally replace Cdc18p, but instead interferes with the proteolysis of both Cdc18p and Rum1p, the inhibitor of the protein kinase Cdc2p.
118	441	bind	Cdh1p	Msn5p	Cdh1p binds to the importin Pse1p and the exportin Msn5p, which is necessary and sufficient to promote efficient export of Cdh1p in vivo.
118	442	bind	Cdh1p	Pse1p	Cdh1p binds to the importin Pse1p and the exportin Msn5p, which is necessary and sufficient to promote efficient export of Cdh1p in vivo.
118	443	bind	Msn5p	Cdh1p	Cdh1p binds to the importin Pse1p and the exportin Msn5p, which is necessary and sufficient to promote efficient export of Cdh1p in vivo.
118	444	bind	Pse1p	Cdh1p	Cdh1p binds to the importin Pse1p and the exportin Msn5p, which is necessary and sufficient to promote efficient export of Cdh1p in vivo.
119	445	complex	E6	E6AP	Characterization of the E6AP-E6-hScrib complex indicated that hScrib binds directly to E6 and that the binding is mediated by the PDZ domains of hScrib and a carboxyl-terminal epitope conserved among the high-risk HPV E6 proteins.
119	446	complex	E6	hScrib	Characterization of the E6AP-E6-hScrib complex indicated that hScrib binds directly to E6 and that the binding is mediated by the PDZ domains of hScrib and a carboxyl-terminal epitope conserved among the high-risk HPV E6 proteins.
119	447	complex	E6AP	E6	Characterization of the E6AP-E6-hScrib complex indicated that hScrib binds directly to E6 and that the binding is mediated by the PDZ domains of hScrib and a carboxyl-terminal epitope conserved among the high-risk HPV E6 proteins.
119	448	complex	E6AP	hScrib	Characterization of the E6AP-E6-hScrib complex indicated that hScrib binds directly to E6 and that the binding is mediated by the PDZ domains of hScrib and a carboxyl-terminal epitope conserved among the high-risk HPV E6 proteins.
119	449	complex	hScrib	E6	Characterization of the E6AP-E6-hScrib complex indicated that hScrib binds directly to E6 and that the binding is mediated by the PDZ domains of hScrib and a carboxyl-terminal epitope conserved among the high-risk HPV E6 proteins.
119	450	complex	hScrib	E6AP	Characterization of the E6AP-E6-hScrib complex indicated that hScrib binds directly to E6 and that the binding is mediated by the PDZ domains of hScrib and a carboxyl-terminal epitope conserved among the high-risk HPV E6 proteins.
120	451	binding	YUH1	ubiquitin	Chemical shift perturbation of backbone (1)H(N), (15)N, and (13)C(alpha) resonances of YUH1, in a YUH1-ubiquitin mixture and in a 35 kDa covalent complex with ubiquitin (a stable analogue of the tetrahedral reaction intermediate), was employed to identify the ubiquitin binding interface of YUH1.
120	452	binding	ubiquitin	YUH1	Chemical shift perturbation of backbone (1)H(N), (15)N, and (13)C(alpha) resonances of YUH1, in a YUH1-ubiquitin mixture and in a 35 kDa covalent complex with ubiquitin (a stable analogue of the tetrahedral reaction intermediate), was employed to identify the ubiquitin binding interface of YUH1.
121	453	interact	Cdc4	Cic1	Cic1 interacts in vitro and in vivo with Cdc4, suggesting a function as a new kind of substrate recruiting factor or adaptor associated with the proteasome.
121	454	interact	Cic1	Cdc4	Cic1 interacts in vitro and in vivo with Cdc4, suggesting a function as a new kind of substrate recruiting factor or adaptor associated with the proteasome.
122	455	associate	Cks1	Skp2	Cks1 associates with the F box protein Skp2 and is essential for recognition of the p27Kip1 substrate for ubiquitination in vivo and in vitro.
122	456	associate	Skp2	Cks1	Cks1 associates with the F box protein Skp2 and is essential for recognition of the p27Kip1 substrate for ubiquitination in vivo and in vitro.
123	457	associate	Cdc28	Cln3	Cln3 associates with Cdc28 to form an active kinase complex that phosphorylates Cln3 itself and a co-precipitated substrate of 45 kDa.
123	458	associate	Cln3	Cdc28	Cln3 associates with Cdc28 to form an active kinase complex that phosphorylates Cln3 itself and a co-precipitated substrate of 45 kDa.
124	459	modification	IRF-1	SUMO-1	Co-expression of PIAS3 induced SUMO-1 modification of IRF-1 in a RING finger domain-dependent manner and also repressed transcriptional activity of IRF-1.
124	460	modification	SUMO-1	IRF-1	Co-expression of PIAS3 induced SUMO-1 modification of IRF-1 in a RING finger domain-dependent manner and also repressed transcriptional activity of IRF-1.
125	461	interact	CUL1	FBW6	Co-immunoprecipitation analysis showed that FBW6 interacts with SKP1 and CUL1, indicating that these three proteins form an SCF complex.
125	462	interact	FBW6	CUL1	Co-immunoprecipitation analysis showed that FBW6 interacts with SKP1 and CUL1, indicating that these three proteins form an SCF complex.
125	463	interact	FBW6	SKP1	Co-immunoprecipitation analysis showed that FBW6 interacts with SKP1 and CUL1, indicating that these three proteins form an SCF complex.
125	464	interact	SKP1	FBW6	Co-immunoprecipitation analysis showed that FBW6 interacts with SKP1 and CUL1, indicating that these three proteins form an SCF complex.
126	465	interact	COI1	cullin	Co-immunoprecipitation experiments confirmed the interaction in planta of COI1 with SKP1-like proteins and histone deacetylase, and also indicated that COI1 interacted with cullin.
126	466	interaction	COI1	histone deacetylase	Co-immunoprecipitation experiments confirmed the interaction in planta of COI1 with SKP1-like proteins and histone deacetylase, and also indicated that COI1 interacted with cullin.
126	467	interact	cullin	COI1	Co-immunoprecipitation experiments confirmed the interaction in planta of COI1 with SKP1-like proteins and histone deacetylase, and also indicated that COI1 interacted with cullin.
126	468	interaction	histone deacetylase	COI1	Co-immunoprecipitation experiments confirmed the interaction in planta of COI1 with SKP1-like proteins and histone deacetylase, and also indicated that COI1 interacted with cullin.
127	469	binding	ARF	Mdm2	Collectively, the results suggest that ARF binding to Mdm2 induces a conformational change that facilitates nucleolar import of the ARF-Mdm2 complex and p53-dependent cell cycle arrest.
127	470	binding	Mdm2	ARF	Collectively, the results suggest that ARF binding to Mdm2 induces a conformational change that facilitates nucleolar import of the ARF-Mdm2 complex and p53-dependent cell cycle arrest.
128	471	activate	APC	Cdh1	Collectively, these data provide a mechanistic explanation for the mutual functional interplay between cyclin A-Cdk2 and APC-Cdh1 and the first evidence that Cdh1 may activate the APC by binding specific substrates.
128	472	activate	Cdh1	APC	Collectively, these data provide a mechanistic explanation for the mutual functional interplay between cyclin A-Cdk2 and APC-Cdh1 and the first evidence that Cdh1 may activate the APC by binding specific substrates.
128	473	interplay	Cdk2	cyclin A	Collectively, these data provide a mechanistic explanation for the mutual functional interplay between cyclin A-Cdk2 and APC-Cdh1 and the first evidence that Cdh1 may activate the APC by binding specific substrates.
128	474	interplay	cyclin A	Cdk2	Collectively, these data provide a mechanistic explanation for the mutual functional interplay between cyclin A-Cdk2 and APC-Cdh1 and the first evidence that Cdh1 may activate the APC by binding specific substrates.
129	475	activate	Ref-1	p53	Colocalization of Ref-1 and p53 suggests that Ref-1 might activate p53 function in LPSE-induced neurodegeneration.
129	476	activate	p53	Ref-1	Colocalization of Ref-1 and p53 suggests that Ref-1 might activate p53 function in LPSE-induced neurodegeneration.
130	477	complex	Cul1	Skp1	Components of the SCF ubiquitin-ligase complex, including Skp1 and Cul1, are also recruited to chromatin through cyclin E-Cdk2 and the preinitiation complex.
130	478	complex	Skp1	Cul1	Components of the SCF ubiquitin-ligase complex, including Skp1 and Cul1, are also recruited to chromatin through cyclin E-Cdk2 and the preinitiation complex.
131	479	bind	CacyBP	S100	Consequently we carried out experiments to determine if CacyBP/SIP binds to other S100 proteins in this tissue.
131	480	bind	S100	CacyBP	Consequently we carried out experiments to determine if CacyBP/SIP binds to other S100 proteins in this tissue.
131	481	bind	S100	SIP	Consequently we carried out experiments to determine if CacyBP/SIP binds to other S100 proteins in this tissue.
131	482	bind	SIP	S100	Consequently we carried out experiments to determine if CacyBP/SIP binds to other S100 proteins in this tissue.
132	483	bind	Rhp23	ubiquitin	Consistent with a role in protein ubiquitination, Rhp23 binds ubiquitin, as determined by two-hybrid analysis.
132	484	bind	ubiquitin	Rhp23	Consistent with a role in protein ubiquitination, Rhp23 binds ubiquitin, as determined by two-hybrid analysis.
133	485	interact	HDAC3	PIASxbeta	Consistent with our earlier observation that TFII-I family proteins also interact with PIASxbeta, a member of the E3 ligase family involved in the small ubiquitin-like modifier (SUMO) pathway, we show further that PIASxbeta physically and functionally interacts with HDAC3 and relieves the transcriptional repression exerted by HDAC3 upon TFII-I-mediated gene activation.
133	486	interact	PIASxbeta	HDAC3	Consistent with our earlier observation that TFII-I family proteins also interact with PIASxbeta, a member of the E3 ligase family involved in the small ubiquitin-like modifier (SUMO) pathway, we show further that PIASxbeta physically and functionally interacts with HDAC3 and relieves the transcriptional repression exerted by HDAC3 upon TFII-I-mediated gene activation.
133	487	interact	PIASxbeta	TFII-I	Consistent with our earlier observation that TFII-I family proteins also interact with PIASxbeta, a member of the E3 ligase family involved in the small ubiquitin-like modifier (SUMO) pathway, we show further that PIASxbeta physically and functionally interacts with HDAC3 and relieves the transcriptional repression exerted by HDAC3 upon TFII-I-mediated gene activation.
133	488	interact	TFII-I	PIASxbeta	Consistent with our earlier observation that TFII-I family proteins also interact with PIASxbeta, a member of the E3 ligase family involved in the small ubiquitin-like modifier (SUMO) pathway, we show further that PIASxbeta physically and functionally interacts with HDAC3 and relieves the transcriptional repression exerted by HDAC3 upon TFII-I-mediated gene activation.
134	489	association	DIAP1	Morgue	Consistent with potential substrate binding functions in an SCF ubiquitin E3 ligase complex, Morgue exhibited F box-dependent association with SkpA and F box-independent association with DIAP1.
134	490	association	Morgue	DIAP1	Consistent with potential substrate binding functions in an SCF ubiquitin E3 ligase complex, Morgue exhibited F box-dependent association with SkpA and F box-independent association with DIAP1.
134	491	association	Morgue	SkpA	Consistent with potential substrate binding functions in an SCF ubiquitin E3 ligase complex, Morgue exhibited F box-dependent association with SkpA and F box-independent association with DIAP1.
134	492	association	SkpA	Morgue	Consistent with potential substrate binding functions in an SCF ubiquitin E3 ligase complex, Morgue exhibited F box-dependent association with SkpA and F box-independent association with DIAP1.
135	493	interaction	55K	Orf3	Consistent with the observed increase in the biochemical interaction between 55K and Orf3 in the absence of Orf6, the 55K association with Orf3 in ND10 was also found to increase in the absence of Orf6.
135	494	interaction	Orf3	55K	Consistent with the observed increase in the biochemical interaction between 55K and Orf3 in the absence of Orf6, the 55K association with Orf3 in ND10 was also found to increase in the absence of Orf6.
136	495	binding	Cdc18p	Pop2p	Consistent with this hypothesis, Pop1p and Pop2p formed heterooligomeric complexes when overexpressed, and binding of Cdc18p to Pop2p was dependent on Pop1p.
136	496	binding	Pop2p	Cdc18p	Consistent with this hypothesis, Pop1p and Pop2p formed heterooligomeric complexes when overexpressed, and binding of Cdc18p to Pop2p was dependent on Pop1p.
137	497	attachment	Mdm2	SUMO-1	Covalent attachment of SUMO-1 to Mdm2 requires the activation of a heterodimeric Aos1-Uba2 enzyme (ubiquitin-activating enzyme (E1)) followed by the conjugation of Sumo-1 to Mdm2 by Ubc9, a protein with a strong sequence similarity to ubiquitin carrier proteins (E2s).
137	498	conjugation	Mdm2	Sumo-1	Covalent attachment of SUMO-1 to Mdm2 requires the activation of a heterodimeric Aos1-Uba2 enzyme (ubiquitin-activating enzyme (E1)) followed by the conjugation of Sumo-1 to Mdm2 by Ubc9, a protein with a strong sequence similarity to ubiquitin carrier proteins (E2s).
137	499	attachment	SUMO-1	Mdm2	Covalent attachment of SUMO-1 to Mdm2 requires the activation of a heterodimeric Aos1-Uba2 enzyme (ubiquitin-activating enzyme (E1)) followed by the conjugation of Sumo-1 to Mdm2 by Ubc9, a protein with a strong sequence similarity to ubiquitin carrier proteins (E2s).
137	500	conjugation	Sumo-1	Mdm2	Covalent attachment of SUMO-1 to Mdm2 requires the activation of a heterodimeric Aos1-Uba2 enzyme (ubiquitin-activating enzyme (E1)) followed by the conjugation of Sumo-1 to Mdm2 by Ubc9, a protein with a strong sequence similarity to ubiquitin carrier proteins (E2s).
138	501	interacting	CDC53	ROC1	Cullin 1/CDC53 functions as an E3 ligase by interacting with RING finger protein ROC1 and recruiting phosphorylated substrate.
138	502	interacting	Cullin 1	ROC1	Cullin 1/CDC53 functions as an E3 ligase by interacting with RING finger protein ROC1 and recruiting phosphorylated substrate.
138	503	interacting	ROC1	CDC53	Cullin 1/CDC53 functions as an E3 ligase by interacting with RING finger protein ROC1 and recruiting phosphorylated substrate.
138	504	interacting	ROC1	Cullin 1	Cullin 1/CDC53 functions as an E3 ligase by interacting with RING finger protein ROC1 and recruiting phosphorylated substrate.
139	505	modified	Cullin-1	Nedd8	Cullin-1, a component of SCF, is modified by ubiquitin-like protein Nedd8.
139	506	modified	Nedd8	Cullin-1	Cullin-1, a component of SCF, is modified by ubiquitin-like protein Nedd8.
140	507	activate	Cullin	NEDD8	Cullins are activated by NEDD8 modification; therefore, to determine whether Cullin complexes are required for adenovirus-induced p53 degradation, studies were conducted in ts41 Chinese hamster ovary cells that are temperature sensitive for the NEDD8 pathway.
140	508	activate	NEDD8	Cullin	Cullins are activated by NEDD8 modification; therefore, to determine whether Cullin complexes are required for adenovirus-induced p53 degradation, studies were conducted in ts41 Chinese hamster ovary cells that are temperature sensitive for the NEDD8 pathway.
141	509	interact	Cut20	Cut4	Cut20 interacts closely with Cut4 in the assembly process of cyclosome.
141	510	interact	Cut4	Cut20	Cut20 interacts closely with Cut4 in the assembly process of cyclosome.
142	511	complex	Cdk2	Cyclin A	Cyclin A-Cdk2 complexes bind to Skp1 and Skp2 during S phase, but the function of Skp1 and Skp2 is unclear.
142	512	complex	Cdk2	Skp1	Cyclin A-Cdk2 complexes bind to Skp1 and Skp2 during S phase, but the function of Skp1 and Skp2 is unclear.
142	513	complex	Cdk2	Skp2	Cyclin A-Cdk2 complexes bind to Skp1 and Skp2 during S phase, but the function of Skp1 and Skp2 is unclear.
142	514	complex	Cyclin A	Cdk2	Cyclin A-Cdk2 complexes bind to Skp1 and Skp2 during S phase, but the function of Skp1 and Skp2 is unclear.
142	515	complex	Cyclin A	Skp1	Cyclin A-Cdk2 complexes bind to Skp1 and Skp2 during S phase, but the function of Skp1 and Skp2 is unclear.
142	516	complex	Cyclin A	Skp2	Cyclin A-Cdk2 complexes bind to Skp1 and Skp2 during S phase, but the function of Skp1 and Skp2 is unclear.
142	517	complex	Skp1	Cdk2	Cyclin A-Cdk2 complexes bind to Skp1 and Skp2 during S phase, but the function of Skp1 and Skp2 is unclear.
142	518	complex	Skp1	Cyclin A	Cyclin A-Cdk2 complexes bind to Skp1 and Skp2 during S phase, but the function of Skp1 and Skp2 is unclear.
142	519	complex	Skp1	Skp2	Cyclin A-Cdk2 complexes bind to Skp1 and Skp2 during S phase, but the function of Skp1 and Skp2 is unclear.
142	520	complex	Skp2	Cdk2	Cyclin A-Cdk2 complexes bind to Skp1 and Skp2 during S phase, but the function of Skp1 and Skp2 is unclear.
142	521	complex	Skp2	Cyclin A	Cyclin A-Cdk2 complexes bind to Skp1 and Skp2 during S phase, but the function of Skp1 and Skp2 is unclear.
142	522	complex	Skp2	Skp1	Cyclin A-Cdk2 complexes bind to Skp1 and Skp2 during S phase, but the function of Skp1 and Skp2 is unclear.
143	523	bind	Cyclin F	cyclin B	Cyclin F, a cyclin that can form SCF complexes and bind to cyclin B, oscillates in the cell cycle with a pattern similar to cyclin A and cyclin B. Ectopic expression of cyclin F arrests the cell cycle in G(2)/M.
143	524	bind	cyclin B	Cyclin F	Cyclin F, a cyclin that can form SCF complexes and bind to cyclin B, oscillates in the cell cycle with a pattern similar to cyclin A and cyclin B. Ectopic expression of cyclin F arrests the cell cycle in G(2)/M.
144	525	interaction	RARs	Stat5	Cytokine-mediated physical and functional interactions between Stat5 and RARs may play critical roles in regulating different stages of hematopoiesis.
144	526	interaction	Stat5	RARs	Cytokine-mediated physical and functional interactions between Stat5 and RARs may play critical roles in regulating different stages of hematopoiesis.
145	527	bind	DIAPs	Grim-Rpr	DIAPs also bind to Grim-Rpr proteins, an interaction that promotes caspase activity and the initiation of apoptosis.
145	528	bind	Grim-Rpr	DIAPs	DIAPs also bind to Grim-Rpr proteins, an interaction that promotes caspase activity and the initiation of apoptosis.
146	529	phosphorylate	DNA-dependent protein kinase	p53	DNA-dependent protein kinase is known to phosphorylate p53 on Mdm2-binding sites, where DNA damage induces phosphorylation, and p53 phosphorylated by this kinase is not a good substrate for Mdm2.
146	530	phosphorylate	p53	DNA-dependent protein kinase	DNA-dependent protein kinase is known to phosphorylate p53 on Mdm2-binding sites, where DNA damage induces phosphorylation, and p53 phosphorylated by this kinase is not a good substrate for Mdm2.
147	531	activation	Cdc14	Cdh1	Degradation of Pds1 is necessary for release of Cdc14 from the nucleolus, whereas degradation of Clb5 is crucial if Cdc14 is to overwhelm Cdk1 and activate its foes (Cdh1 and Sic1).
147	532	activation	Cdc14	Sic1	Degradation of Pds1 is necessary for release of Cdc14 from the nucleolus, whereas degradation of Clb5 is crucial if Cdc14 is to overwhelm Cdk1 and activate its foes (Cdh1 and Sic1).
147	533	activation	Cdh1	Cdc14	Degradation of Pds1 is necessary for release of Cdc14 from the nucleolus, whereas degradation of Clb5 is crucial if Cdc14 is to overwhelm Cdk1 and activate its foes (Cdh1 and Sic1).
147	534	activation	Sic1	Cdc14	Degradation of Pds1 is necessary for release of Cdc14 from the nucleolus, whereas degradation of Clb5 is crucial if Cdc14 is to overwhelm Cdk1 and activate its foes (Cdh1 and Sic1).
148	535	interact	Dnmt3b	SUMO-1	Deletion analysis and colocalization experiment demonstrated that Dnmt3b interacts with SUMO-1 and Ubc9 at its N-terminal region.
148	536	interact	Dnmt3b	Ubc9	Deletion analysis and colocalization experiment demonstrated that Dnmt3b interacts with SUMO-1 and Ubc9 at its N-terminal region.
148	537	interact	SUMO-1	Dnmt3b	Deletion analysis and colocalization experiment demonstrated that Dnmt3b interacts with SUMO-1 and Ubc9 at its N-terminal region.
148	538	interact	Ubc9	Dnmt3b	Deletion analysis and colocalization experiment demonstrated that Dnmt3b interacts with SUMO-1 and Ubc9 at its N-terminal region.
149	539	binding	FWD1	Skp1	Deletion analysis of Skp1 revealed that residues 61-143 of this protein are required for binding to FWD1.
149	540	binding	Skp1	FWD1	Deletion analysis of Skp1 revealed that residues 61-143 of this protein are required for binding to FWD1.
150	541	binding	CUL1	Skp1	Deletion analysis reveals that the N terminus of CUL1 is both necessary and sufficient for binding Skp1 but is devoid of ROC1-binding activity and, hence, is inactive in catalyzing ubiquitin ligation.
150	542	binding	Skp1	CUL1	Deletion analysis reveals that the N terminus of CUL1 is both necessary and sufficient for binding Skp1 but is devoid of ROC1-binding activity and, hence, is inactive in catalyzing ubiquitin ligation.
151	543	phosphorylation	Axin	beta-catenin	Deregulation of beta-catenin accumulation as a result of mutations in adenomatous polyposis coli (APC) tumor suppressor protein is believed to initiate colorectal neoplasia. beta-catenin levels are regulated by the ubiquitin-dependent proteolysis system and beta-catenin ubiquitination is preceded by phosphorylation of its N-terminal region by the glycogen synthase kinase-3beta (GSK-3beta)/Axin kinase complex.
151	544	phosphorylation	GSK-3beta	beta-catenin	Deregulation of beta-catenin accumulation as a result of mutations in adenomatous polyposis coli (APC) tumor suppressor protein is believed to initiate colorectal neoplasia. beta-catenin levels are regulated by the ubiquitin-dependent proteolysis system and beta-catenin ubiquitination is preceded by phosphorylation of its N-terminal region by the glycogen synthase kinase-3beta (GSK-3beta)/Axin kinase complex.
151	545	phosphorylation	beta-catenin	Axin	Deregulation of beta-catenin accumulation as a result of mutations in adenomatous polyposis coli (APC) tumor suppressor protein is believed to initiate colorectal neoplasia. beta-catenin levels are regulated by the ubiquitin-dependent proteolysis system and beta-catenin ubiquitination is preceded by phosphorylation of its N-terminal region by the glycogen synthase kinase-3beta (GSK-3beta)/Axin kinase complex.
151	546	phosphorylation	beta-catenin	GSK-3beta	Deregulation of beta-catenin accumulation as a result of mutations in adenomatous polyposis coli (APC) tumor suppressor protein is believed to initiate colorectal neoplasia. beta-catenin levels are regulated by the ubiquitin-dependent proteolysis system and beta-catenin ubiquitination is preceded by phosphorylation of its N-terminal region by the glycogen synthase kinase-3beta (GSK-3beta)/Axin kinase complex.
152	547	activate	APC	Cdc20	Despite evidence showing that Cdc20 and Cdh1 bind and activate the anaphase-promoting complex (APC) in a substrate-specific manner, there is no evidence that the activating protein and substrate interact directly; hence, no clear model exists for the mechanism of APC activation or recruitment of substrates.
152	548	activate	APC	Cdh1	Despite evidence showing that Cdc20 and Cdh1 bind and activate the anaphase-promoting complex (APC) in a substrate-specific manner, there is no evidence that the activating protein and substrate interact directly; hence, no clear model exists for the mechanism of APC activation or recruitment of substrates.
152	549	activate	Cdc20	APC	Despite evidence showing that Cdc20 and Cdh1 bind and activate the anaphase-promoting complex (APC) in a substrate-specific manner, there is no evidence that the activating protein and substrate interact directly; hence, no clear model exists for the mechanism of APC activation or recruitment of substrates.
152	550	activate	Cdh1	APC	Despite evidence showing that Cdc20 and Cdh1 bind and activate the anaphase-promoting complex (APC) in a substrate-specific manner, there is no evidence that the activating protein and substrate interact directly; hence, no clear model exists for the mechanism of APC activation or recruitment of substrates.
153	551	interaction	G-CSF	SCF	Despite the clinical importance of the interaction between SCF and G-CSF, the absence of a model system in which it could be studied at the cellular level had impaired the ability to understand the basis of their co-operation.
153	552	interaction	SCF	G-CSF	Despite the clinical importance of the interaction between SCF and G-CSF, the absence of a model system in which it could be studied at the cellular level had impaired the ability to understand the basis of their co-operation.
154	553	interaction	ASK1	PAD1	Detection of SnRK in purified 26S proteasomes and co-purification of epitope- tagged SKP1/ASK1 with SnRK, cullin and proteasomal alpha-subunits indicate that the observed protein interactions between SnRK, SKP1/ASK1 and alpha4/PAD1 are involved in proteasomal binding of an SCF ubiquitin ligase in Arabidopsis.
154	554	interaction	ASK1	SnRK	Detection of SnRK in purified 26S proteasomes and co-purification of epitope- tagged SKP1/ASK1 with SnRK, cullin and proteasomal alpha-subunits indicate that the observed protein interactions between SnRK, SKP1/ASK1 and alpha4/PAD1 are involved in proteasomal binding of an SCF ubiquitin ligase in Arabidopsis.
154	555	interaction	ASK1	alpha4	Detection of SnRK in purified 26S proteasomes and co-purification of epitope- tagged SKP1/ASK1 with SnRK, cullin and proteasomal alpha-subunits indicate that the observed protein interactions between SnRK, SKP1/ASK1 and alpha4/PAD1 are involved in proteasomal binding of an SCF ubiquitin ligase in Arabidopsis.
154	556	interaction	PAD1	ASK1	Detection of SnRK in purified 26S proteasomes and co-purification of epitope- tagged SKP1/ASK1 with SnRK, cullin and proteasomal alpha-subunits indicate that the observed protein interactions between SnRK, SKP1/ASK1 and alpha4/PAD1 are involved in proteasomal binding of an SCF ubiquitin ligase in Arabidopsis.
154	557	interaction	PAD1	SKP1	Detection of SnRK in purified 26S proteasomes and co-purification of epitope- tagged SKP1/ASK1 with SnRK, cullin and proteasomal alpha-subunits indicate that the observed protein interactions between SnRK, SKP1/ASK1 and alpha4/PAD1 are involved in proteasomal binding of an SCF ubiquitin ligase in Arabidopsis.
154	558	interaction	PAD1	SnRK	Detection of SnRK in purified 26S proteasomes and co-purification of epitope- tagged SKP1/ASK1 with SnRK, cullin and proteasomal alpha-subunits indicate that the observed protein interactions between SnRK, SKP1/ASK1 and alpha4/PAD1 are involved in proteasomal binding of an SCF ubiquitin ligase in Arabidopsis.
154	559	interaction	SKP1	PAD1	Detection of SnRK in purified 26S proteasomes and co-purification of epitope- tagged SKP1/ASK1 with SnRK, cullin and proteasomal alpha-subunits indicate that the observed protein interactions between SnRK, SKP1/ASK1 and alpha4/PAD1 are involved in proteasomal binding of an SCF ubiquitin ligase in Arabidopsis.
154	560	interaction	SKP1	SnRK	Detection of SnRK in purified 26S proteasomes and co-purification of epitope- tagged SKP1/ASK1 with SnRK, cullin and proteasomal alpha-subunits indicate that the observed protein interactions between SnRK, SKP1/ASK1 and alpha4/PAD1 are involved in proteasomal binding of an SCF ubiquitin ligase in Arabidopsis.
154	561	interaction	SKP1	alpha4	Detection of SnRK in purified 26S proteasomes and co-purification of epitope- tagged SKP1/ASK1 with SnRK, cullin and proteasomal alpha-subunits indicate that the observed protein interactions between SnRK, SKP1/ASK1 and alpha4/PAD1 are involved in proteasomal binding of an SCF ubiquitin ligase in Arabidopsis.
154	562	interaction	SnRK	ASK1	Detection of SnRK in purified 26S proteasomes and co-purification of epitope- tagged SKP1/ASK1 with SnRK, cullin and proteasomal alpha-subunits indicate that the observed protein interactions between SnRK, SKP1/ASK1 and alpha4/PAD1 are involved in proteasomal binding of an SCF ubiquitin ligase in Arabidopsis.
154	563	interaction	SnRK	PAD1	Detection of SnRK in purified 26S proteasomes and co-purification of epitope- tagged SKP1/ASK1 with SnRK, cullin and proteasomal alpha-subunits indicate that the observed protein interactions between SnRK, SKP1/ASK1 and alpha4/PAD1 are involved in proteasomal binding of an SCF ubiquitin ligase in Arabidopsis.
154	564	interaction	SnRK	SKP1	Detection of SnRK in purified 26S proteasomes and co-purification of epitope- tagged SKP1/ASK1 with SnRK, cullin and proteasomal alpha-subunits indicate that the observed protein interactions between SnRK, SKP1/ASK1 and alpha4/PAD1 are involved in proteasomal binding of an SCF ubiquitin ligase in Arabidopsis.
154	565	interaction	SnRK	alpha4	Detection of SnRK in purified 26S proteasomes and co-purification of epitope- tagged SKP1/ASK1 with SnRK, cullin and proteasomal alpha-subunits indicate that the observed protein interactions between SnRK, SKP1/ASK1 and alpha4/PAD1 are involved in proteasomal binding of an SCF ubiquitin ligase in Arabidopsis.
154	566	interaction	alpha4	ASK1	Detection of SnRK in purified 26S proteasomes and co-purification of epitope- tagged SKP1/ASK1 with SnRK, cullin and proteasomal alpha-subunits indicate that the observed protein interactions between SnRK, SKP1/ASK1 and alpha4/PAD1 are involved in proteasomal binding of an SCF ubiquitin ligase in Arabidopsis.
154	567	interaction	alpha4	SKP1	Detection of SnRK in purified 26S proteasomes and co-purification of epitope- tagged SKP1/ASK1 with SnRK, cullin and proteasomal alpha-subunits indicate that the observed protein interactions between SnRK, SKP1/ASK1 and alpha4/PAD1 are involved in proteasomal binding of an SCF ubiquitin ligase in Arabidopsis.
154	568	interaction	alpha4	SnRK	Detection of SnRK in purified 26S proteasomes and co-purification of epitope- tagged SKP1/ASK1 with SnRK, cullin and proteasomal alpha-subunits indicate that the observed protein interactions between SnRK, SKP1/ASK1 and alpha4/PAD1 are involved in proteasomal binding of an SCF ubiquitin ligase in Arabidopsis.
155	569	modification	CUL1	NEDD8	Disruption of ROC1 binding impaired nuclear accumulation of CUL1 and decreased NEDD8 modification in vivo but had no effect on NEDD8 modification of CUL1 in vitro, suggesting that ROC1 promotes CUL1 nuclear accumulation to facilitate its NEDD8 modification.
155	570	modification	NEDD8	CUL1	Disruption of ROC1 binding impaired nuclear accumulation of CUL1 and decreased NEDD8 modification in vivo but had no effect on NEDD8 modification of CUL1 in vitro, suggesting that ROC1 promotes CUL1 nuclear accumulation to facilitate its NEDD8 modification.
156	571	interaction	E2F-1	p45SKP2	Disruption of the interaction between E2F-1 and p45SKP2 results in a reduction in ubiquitination of E2F-1 and the stabilization and accumulation of transcriptionally active E2F-1 protein.
156	572	interaction	p45SKP2	E2F-1	Disruption of the interaction between E2F-1 and p45SKP2 results in a reduction in ubiquitination of E2F-1 and the stabilization and accumulation of transcriptionally active E2F-1 protein.
157	573	binding	CDK2	p27(Kip1)	Downregulation of the kinase activities is mediated by induction of cyclin dependent kinase (CDK) inhibitor p15(Ink4b) which blocks CDK4 and CDK6 kinases and leads to binding of p27(Kip1) to CDK2-cyclin E complex.
157	574	binding	cyclin E	p27(Kip1)	Downregulation of the kinase activities is mediated by induction of cyclin dependent kinase (CDK) inhibitor p15(Ink4b) which blocks CDK4 and CDK6 kinases and leads to binding of p27(Kip1) to CDK2-cyclin E complex.
157	575	binding	p27(Kip1)	CDK2	Downregulation of the kinase activities is mediated by induction of cyclin dependent kinase (CDK) inhibitor p15(Ink4b) which blocks CDK4 and CDK6 kinases and leads to binding of p27(Kip1) to CDK2-cyclin E complex.
157	576	binding	p27(Kip1)	cyclin E	Downregulation of the kinase activities is mediated by induction of cyclin dependent kinase (CDK) inhibitor p15(Ink4b) which blocks CDK4 and CDK6 kinases and leads to binding of p27(Kip1) to CDK2-cyclin E complex.
158	577	interacting	CaMKII	DmUba2	Drosophila Uba2 and Ubc9 SUMO-1 conjugation enzyme homologs (DmUba2 and DmUbc9) were isolated as calcium/calmodulin-dependent kinase II (CaMKII) interacting proteins by yeast two-hybrid screening of an adult head cDNA library.
158	578	interacting	CaMKII	DmUbc9	Drosophila Uba2 and Ubc9 SUMO-1 conjugation enzyme homologs (DmUba2 and DmUbc9) were isolated as calcium/calmodulin-dependent kinase II (CaMKII) interacting proteins by yeast two-hybrid screening of an adult head cDNA library.
158	579	interacting	DmUba2	CaMKII	Drosophila Uba2 and Ubc9 SUMO-1 conjugation enzyme homologs (DmUba2 and DmUbc9) were isolated as calcium/calmodulin-dependent kinase II (CaMKII) interacting proteins by yeast two-hybrid screening of an adult head cDNA library.
158	580	interacting	DmUbc9	CaMKII	Drosophila Uba2 and Ubc9 SUMO-1 conjugation enzyme homologs (DmUba2 and DmUbc9) were isolated as calcium/calmodulin-dependent kinase II (CaMKII) interacting proteins by yeast two-hybrid screening of an adult head cDNA library.
159	581	interact	E2	PKR	E2 interacts with PKR and inhibits its kinase activity.
159	582	interact	PKR	E2	E2 interacts with PKR and inhibits its kinase activity.
160	583	transfer	E2-C	ubiquitin	E3-C is present but inactive during interphase; it can be activated in vitro by the addition of cdc2, enabling the transfer of ubiquitin from E2-C to cyclin.
160	584	activate	E3-C	cdc2	E3-C is present but inactive during interphase; it can be activated in vitro by the addition of cdc2, enabling the transfer of ubiquitin from E2-C to cyclin.
160	585	activate	cdc2	E3-C	E3-C is present but inactive during interphase; it can be activated in vitro by the addition of cdc2, enabling the transfer of ubiquitin from E2-C to cyclin.
160	586	transfer	ubiquitin	E2-C	E3-C is present but inactive during interphase; it can be activated in vitro by the addition of cdc2, enabling the transfer of ubiquitin from E2-C to cyclin.
161	587	transfers	E6-AP	ubiquitin	E6-AP is an E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.
161	588	transfers	ubiquitin	E6-AP	E6-AP is an E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.
162	589	binding	E6	E6AP	E6-mediated degradation of E6AP requires (i) the binding of E6 to E6AP, (ii) the catalytic activity of E6AP, and (iii) activity of the 26S proteasome, suggesting that E6-E6AP interaction results in E6AP self-ubiquitination and degradation.
162	590	binding	E6AP	E6	E6-mediated degradation of E6AP requires (i) the binding of E6 to E6AP, (ii) the catalytic activity of E6AP, and (iii) activity of the 26S proteasome, suggesting that E6-E6AP interaction results in E6AP self-ubiquitination and degradation.
163	591	transfer	p53	ubiquitin	E6AP and E6 together provide the E3-ubiquitin protein ligase activity in the transfer of ubiquitin to p53.
163	592	transfer	ubiquitin	p53	E6AP and E6 together provide the E3-ubiquitin protein ligase activity in the transfer of ubiquitin to p53.
164	593	associate	EBNA-3C	PU1	EBNA-3C associates with the cellular DNA sequence-specific transcription factors RBP-Jkappa and PU1 and coactivates the EBV LMP1 promoter with EBNA-2 in BL2 and Raji cells under conditions of restrictive growth.
164	594	associate	EBNA-3C	RBP-Jkappa	EBNA-3C associates with the cellular DNA sequence-specific transcription factors RBP-Jkappa and PU1 and coactivates the EBV LMP1 promoter with EBNA-2 in BL2 and Raji cells under conditions of restrictive growth.
164	595	associate	PU1	EBNA-3C	EBNA-3C associates with the cellular DNA sequence-specific transcription factors RBP-Jkappa and PU1 and coactivates the EBV LMP1 promoter with EBNA-2 in BL2 and Raji cells under conditions of restrictive growth.
164	596	associate	RBP-Jkappa	EBNA-3C	EBNA-3C associates with the cellular DNA sequence-specific transcription factors RBP-Jkappa and PU1 and coactivates the EBV LMP1 promoter with EBNA-2 in BL2 and Raji cells under conditions of restrictive growth.
165	597	function	AXR1	ECR1	ECR1 functions together with AXR1 to activate members of the RUB/NEDD8 family of ubiquitin-related proteins.
165	598	activate	AXR1	NEDD8	ECR1 functions together with AXR1 to activate members of the RUB/NEDD8 family of ubiquitin-related proteins.
165	599	activate	AXR1	RUB	ECR1 functions together with AXR1 to activate members of the RUB/NEDD8 family of ubiquitin-related proteins.
165	600	function	ECR1	AXR1	ECR1 functions together with AXR1 to activate members of the RUB/NEDD8 family of ubiquitin-related proteins.
165	601	activate	ECR1	NEDD8	ECR1 functions together with AXR1 to activate members of the RUB/NEDD8 family of ubiquitin-related proteins.
165	602	activate	ECR1	RUB	ECR1 functions together with AXR1 to activate members of the RUB/NEDD8 family of ubiquitin-related proteins.
165	603	activate	NEDD8	AXR1	ECR1 functions together with AXR1 to activate members of the RUB/NEDD8 family of ubiquitin-related proteins.
165	604	activate	NEDD8	ECR1	ECR1 functions together with AXR1 to activate members of the RUB/NEDD8 family of ubiquitin-related proteins.
165	605	activate	RUB	AXR1	ECR1 functions together with AXR1 to activate members of the RUB/NEDD8 family of ubiquitin-related proteins.
165	606	activate	RUB	ECR1	ECR1 functions together with AXR1 to activate members of the RUB/NEDD8 family of ubiquitin-related proteins.
166	607	bind	EDD	PR	EDD also binds progesterone receptor (PR) and potentiates progestin-mediated gene transactivation.
166	608	bind	PR	EDD	EDD also binds progesterone receptor (PR) and potentiates progestin-mediated gene transactivation.
167	609	bound	EGF	EGFR	EGF remains bound to the EGFR upon endocytosis, whereas TGF alpha dissociates from the EGFR.
167	610	bound	EGFR	EGF	EGF remains bound to the EGFR upon endocytosis, whereas TGF alpha dissociates from the EGFR.
168	611	transfer	MBP	ubiquitin	EL5 possesses the activity to catalyse the transfer of ubiquitin to the MBP moiety, and the RING-H2 finger motif of EL5 is necessary for this activity.
168	612	transfer	ubiquitin	MBP	EL5 possesses the activity to catalyse the transfer of ubiquitin to the MBP moiety, and the RING-H2 finger motif of EL5 is necessary for this activity.
169	613	interact	Bul	Rsp5	Each Bul protein has a putative PY-motif that has been predicted to interact with one of three WW-domains of Rsp5.
169	614	interact	Rsp5	Bul	Each Bul protein has a putative PY-motif that has been predicted to interact with one of three WW-domains of Rsp5.
170	615	interaction	ENaC	Nedd4	Effects of the above phosphorylations on interactions between ENaC and Nedd4 have been studied using surface plasmon resonance.
170	616	interaction	Nedd4	ENaC	Effects of the above phosphorylations on interactions between ENaC and Nedd4 have been studied using surface plasmon resonance.
171	617	bound	TopBP1	hHYD	Endogenous hHYD bound the BRCA1 C-terminus domains of TopBP1 that are highlighted in DNA damage checkpoint proteins and cell cycle regulators.
171	618	bound	hHYD	TopBP1	Endogenous hHYD bound the BRCA1 C-terminus domains of TopBP1 that are highlighted in DNA damage checkpoint proteins and cell cycle regulators.
172	619	complex	Cdc16p	Cdc23p	Entry into anaphase and proteolysis of B-type cyclins depend on a complex containing the tetratricopeptide repeat proteins Cdc16p, Cdc23p, and Cdc27p.
172	620	complex	Cdc16p	Cdc27p	Entry into anaphase and proteolysis of B-type cyclins depend on a complex containing the tetratricopeptide repeat proteins Cdc16p, Cdc23p, and Cdc27p.
172	621	complex	Cdc23p	Cdc16p	Entry into anaphase and proteolysis of B-type cyclins depend on a complex containing the tetratricopeptide repeat proteins Cdc16p, Cdc23p, and Cdc27p.
172	622	complex	Cdc23p	Cdc27p	Entry into anaphase and proteolysis of B-type cyclins depend on a complex containing the tetratricopeptide repeat proteins Cdc16p, Cdc23p, and Cdc27p.
172	623	complex	Cdc27p	Cdc16p	Entry into anaphase and proteolysis of B-type cyclins depend on a complex containing the tetratricopeptide repeat proteins Cdc16p, Cdc23p, and Cdc27p.
172	624	complex	Cdc27p	Cdc23p	Entry into anaphase and proteolysis of B-type cyclins depend on a complex containing the tetratricopeptide repeat proteins Cdc16p, Cdc23p, and Cdc27p.
173	625	interaction	HIF-1alpha	pVHL	Equally regulation of the HIF-1alpha/pVHL interaction in normal cells should provide insights into the physiological mechanisms operating in cellular oxygen sensing.
173	626	interaction	pVHL	HIF-1alpha	Equally regulation of the HIF-1alpha/pVHL interaction in normal cells should provide insights into the physiological mechanisms operating in cellular oxygen sensing.
174	627	bind	Ess1	RpbI	Ess1, a prolyl-isomerase, binds the CTD and is thought to play a positive role in pol II transcription by generating conformational isomers of the CTD.
174	628	bind	RpbI	Ess1	Ess1, a prolyl-isomerase, binds the CTD and is thought to play a positive role in pol II transcription by generating conformational isomers of the CTD.
175	629	associate	BAP1	BRCA1	Even though BRCA1 has been reported to associate with a C-terminal ubiquitin hydrolase, BAP1, this enzyme does not appear to function in the deubiquitylation of the BRCA1/BARD1 complex.
175	630	complex	BARD1	BRCA1	Even though BRCA1 has been reported to associate with a C-terminal ubiquitin hydrolase, BAP1, this enzyme does not appear to function in the deubiquitylation of the BRCA1/BARD1 complex.
175	631	associate	BRCA1	BAP1	Even though BRCA1 has been reported to associate with a C-terminal ubiquitin hydrolase, BAP1, this enzyme does not appear to function in the deubiquitylation of the BRCA1/BARD1 complex.
175	632	complex	BRCA1	BARD1	Even though BRCA1 has been reported to associate with a C-terminal ubiquitin hydrolase, BAP1, this enzyme does not appear to function in the deubiquitylation of the BRCA1/BARD1 complex.
176	633	interact	E6	p53	Evidence is also provided that, in vivo, E6 can interact with p53 in the absence of E6-AP and that E6-AP can interact with p53 in the absence of E6.
176	634	interact	E6-AP	p53	Evidence is also provided that, in vivo, E6 can interact with p53 in the absence of E6-AP and that E6-AP can interact with p53 in the absence of E6.
176	635	interact	p53	E6	Evidence is also provided that, in vivo, E6 can interact with p53 in the absence of E6-AP and that E6-AP can interact with p53 in the absence of E6.
176	636	interact	p53	E6-AP	Evidence is also provided that, in vivo, E6 can interact with p53 in the absence of E6-AP and that E6-AP can interact with p53 in the absence of E6.
177	637	bound	APC	Cdc20	Exit from mitosis requires the degradation of regulatory proteins including the mitotic cyclins and securin through ubiquitination by the anaphase promoting complex (APC) bound to Cdc20 or Cdh1.
177	638	bound	APC	Cdh1	Exit from mitosis requires the degradation of regulatory proteins including the mitotic cyclins and securin through ubiquitination by the anaphase promoting complex (APC) bound to Cdc20 or Cdh1.
177	639	bound	Cdc20	APC	Exit from mitosis requires the degradation of regulatory proteins including the mitotic cyclins and securin through ubiquitination by the anaphase promoting complex (APC) bound to Cdc20 or Cdh1.
177	640	bound	Cdh1	APC	Exit from mitosis requires the degradation of regulatory proteins including the mitotic cyclins and securin through ubiquitination by the anaphase promoting complex (APC) bound to Cdc20 or Cdh1.
178	641	binding	mdm2	p53	Expression of exon alpha disrupts in vitro translation of the p53 binding domain of mdm2.
178	642	binding	p53	mdm2	Expression of exon alpha disrupts in vitro translation of the p53 binding domain of mdm2.
179	643	interaction	Cdc53-Cullin1	F-box	F-box proteins, a critical component of the evolutionary conserved ubiquitin-protein ligase complex SCF (Skp1/Cdc53-Cullin1/F-box), recruit substrates for ubiquitination and consequent degradation through their specific protein-protein interaction domains.
179	644	interaction	Cdc53-Cullin1	Skp1	F-box proteins, a critical component of the evolutionary conserved ubiquitin-protein ligase complex SCF (Skp1/Cdc53-Cullin1/F-box), recruit substrates for ubiquitination and consequent degradation through their specific protein-protein interaction domains.
179	645	interaction	F-box	Cdc53-Cullin1	F-box proteins, a critical component of the evolutionary conserved ubiquitin-protein ligase complex SCF (Skp1/Cdc53-Cullin1/F-box), recruit substrates for ubiquitination and consequent degradation through their specific protein-protein interaction domains.
179	646	interaction	F-box	Skp1	F-box proteins, a critical component of the evolutionary conserved ubiquitin-protein ligase complex SCF (Skp1/Cdc53-Cullin1/F-box), recruit substrates for ubiquitination and consequent degradation through their specific protein-protein interaction domains.
179	647	interaction	Skp1	Cdc53-Cullin1	F-box proteins, a critical component of the evolutionary conserved ubiquitin-protein ligase complex SCF (Skp1/Cdc53-Cullin1/F-box), recruit substrates for ubiquitination and consequent degradation through their specific protein-protein interaction domains.
179	648	interaction	Skp1	F-box	F-box proteins, a critical component of the evolutionary conserved ubiquitin-protein ligase complex SCF (Skp1/Cdc53-Cullin1/F-box), recruit substrates for ubiquitination and consequent degradation through their specific protein-protein interaction domains.
180	649	interact	FWD1	IkappaBalpha	FWD1 (the mouse homolog of Drosophila Slimb and Xenopus betaTrCP, a member of the F-box- and WD40 repeat-containing family of proteins, and a component of the SCF ubiquitin ligase complex) was recently shown to interact with IkappaBalpha and thereby to promote its ubiquitination and degradation.
180	650	interact	IkappaBalpha	FWD1	FWD1 (the mouse homolog of Drosophila Slimb and Xenopus betaTrCP, a member of the F-box- and WD40 repeat-containing family of proteins, and a component of the SCF ubiquitin ligase complex) was recently shown to interact with IkappaBalpha and thereby to promote its ubiquitination and degradation.
181	651	interact	FWD1	IkappaBepsilon	FWD1 also interacts with other sites in the NH(2)-terminal region of IkappaBepsilon.
181	652	interact	IkappaBepsilon	FWD1	FWD1 also interacts with other sites in the NH(2)-terminal region of IkappaBepsilon.
182	653	recognize	FWD1	IkappaBalpha	FWD1 associates with Skp1 through the F-box domain and also recognizes the conserved DSGXXS motif of IkappaBalpha.
182	654	associate	FWD1	Skp1	FWD1 associates with Skp1 through the F-box domain and also recognizes the conserved DSGXXS motif of IkappaBalpha.
182	655	recognize	IkappaBalpha	FWD1	FWD1 associates with Skp1 through the F-box domain and also recognizes the conserved DSGXXS motif of IkappaBalpha.
182	656	associate	Skp1	FWD1	FWD1 associates with Skp1 through the F-box domain and also recognizes the conserved DSGXXS motif of IkappaBalpha.
183	657	associates	Fbw7	cyclin E	Fbw7 associates specifically with phosphorylated cyclin E, and SCFFbw7 catalyzes cyclin E ubiquitination in vitro.
183	658	associates	cyclin E	Fbw7	Fbw7 associates specifically with phosphorylated cyclin E, and SCFFbw7 catalyzes cyclin E ubiquitination in vitro.
184	659	bind	Cdc18	Pop1	Finally we show that Pop1 binds Cdc18 in vivo.
184	660	bind	Pop1	Cdc18	Finally we show that Pop1 binds Cdc18 in vivo.
185	661	bind	TBP	p53	Finally we show that the ability of p53 to bind to TBP is a function of its oligomeric state and correlates in part with its ability to transrepress but not with its ability to transactivate.
185	662	bind	p53	TBP	Finally we show that the ability of p53 to bind to TBP is a function of its oligomeric state and correlates in part with its ability to transrepress but not with its ability to transactivate.
186	663	interaction	A2	pVHL	Finally, an in vivo interaction between pVHL and hnRNP A2 was demonstrated in both the nucleus and the cytoplasm.
186	664	interaction	pVHL	A2	Finally, an in vivo interaction between pVHL and hnRNP A2 was demonstrated in both the nucleus and the cytoplasm.
187	665	complex	HP1	SP100	Finally, in vitro experiments indicate that SUMO modification of SP100 enhances the stability of SP100-HP1 complexes.
187	666	complex	SP100	HP1	Finally, in vitro experiments indicate that SUMO modification of SP100 enhances the stability of SP100-HP1 complexes.
187	667	modification	SP100	SUMO	Finally, in vitro experiments indicate that SUMO modification of SP100 enhances the stability of SP100-HP1 complexes.
187	668	modification	SUMO	SP100	Finally, in vitro experiments indicate that SUMO modification of SP100 enhances the stability of SP100-HP1 complexes.
188	669	associate	APC/C	Ama1p	First, coimmunoprecipitation assays indicate that Ama1p associates with the APC/C in vivo.
188	670	associate	Ama1p	APC/C	First, coimmunoprecipitation assays indicate that Ama1p associates with the APC/C in vivo.
189	671	complex	Cdc4p	Cdc6p	First, phosphorylation of N-terminal sites targets Cdc6p for polyubiquitination probably, as expected, through promoting interaction with Cdc4p, an F box protein involved in substrate recognition by the Skp1-Cdc53-F-box protein (SCF) ubiquitin ligase.
189	672	complex	Cdc6p	Cdc4p	First, phosphorylation of N-terminal sites targets Cdc6p for polyubiquitination probably, as expected, through promoting interaction with Cdc4p, an F box protein involved in substrate recognition by the Skp1-Cdc53-F-box protein (SCF) ubiquitin ligase.
190	673	interact	BEN	Miz1	First, the interactions are biochemically confirmed in mammalian cells where Miz1/mPIASxbeta interacts with both TFII-I and hMusTRD1/BEN when these proteins are ectopically co-expressed.
190	674	interact	BEN	mPIASxbeta	First, the interactions are biochemically confirmed in mammalian cells where Miz1/mPIASxbeta interacts with both TFII-I and hMusTRD1/BEN when these proteins are ectopically co-expressed.
190	675	interact	Miz1	BEN	First, the interactions are biochemically confirmed in mammalian cells where Miz1/mPIASxbeta interacts with both TFII-I and hMusTRD1/BEN when these proteins are ectopically co-expressed.
190	676	interact	Miz1	TFII-I	First, the interactions are biochemically confirmed in mammalian cells where Miz1/mPIASxbeta interacts with both TFII-I and hMusTRD1/BEN when these proteins are ectopically co-expressed.
190	677	interact	Miz1	hMusTRD1	First, the interactions are biochemically confirmed in mammalian cells where Miz1/mPIASxbeta interacts with both TFII-I and hMusTRD1/BEN when these proteins are ectopically co-expressed.
190	678	interact	TFII-I	Miz1	First, the interactions are biochemically confirmed in mammalian cells where Miz1/mPIASxbeta interacts with both TFII-I and hMusTRD1/BEN when these proteins are ectopically co-expressed.
190	679	interact	TFII-I	mPIASxbeta	First, the interactions are biochemically confirmed in mammalian cells where Miz1/mPIASxbeta interacts with both TFII-I and hMusTRD1/BEN when these proteins are ectopically co-expressed.
190	680	interact	hMusTRD1	Miz1	First, the interactions are biochemically confirmed in mammalian cells where Miz1/mPIASxbeta interacts with both TFII-I and hMusTRD1/BEN when these proteins are ectopically co-expressed.
190	681	interact	hMusTRD1	mPIASxbeta	First, the interactions are biochemically confirmed in mammalian cells where Miz1/mPIASxbeta interacts with both TFII-I and hMusTRD1/BEN when these proteins are ectopically co-expressed.
190	682	interact	mPIASxbeta	BEN	First, the interactions are biochemically confirmed in mammalian cells where Miz1/mPIASxbeta interacts with both TFII-I and hMusTRD1/BEN when these proteins are ectopically co-expressed.
190	683	interact	mPIASxbeta	TFII-I	First, the interactions are biochemically confirmed in mammalian cells where Miz1/mPIASxbeta interacts with both TFII-I and hMusTRD1/BEN when these proteins are ectopically co-expressed.
190	684	interact	mPIASxbeta	hMusTRD1	First, the interactions are biochemically confirmed in mammalian cells where Miz1/mPIASxbeta interacts with both TFII-I and hMusTRD1/BEN when these proteins are ectopically co-expressed.
191	685	bind	UBC3	beta-TrCP	Following CK2-dependent phosphorylation both UBC3B and UBC3 bind to the F-box protein beta-TrCP, the substrate recognition subunit of an SCF (Skp1, Cul1, F-box) ubiquitin ligase.
191	686	bind	UBC3B	beta-TrCP	Following CK2-dependent phosphorylation both UBC3B and UBC3 bind to the F-box protein beta-TrCP, the substrate recognition subunit of an SCF (Skp1, Cul1, F-box) ubiquitin ligase.
191	687	bind	beta-TrCP	UBC3	Following CK2-dependent phosphorylation both UBC3B and UBC3 bind to the F-box protein beta-TrCP, the substrate recognition subunit of an SCF (Skp1, Cul1, F-box) ubiquitin ligase.
191	688	bind	beta-TrCP	UBC3B	Following CK2-dependent phosphorylation both UBC3B and UBC3 bind to the F-box protein beta-TrCP, the substrate recognition subunit of an SCF (Skp1, Cul1, F-box) ubiquitin ligase.
192	689	phosphorylate	IKK	p105	Following the stimulation of cells with tumor necrosis factor alpha (TNF-alpha), the IkappaB kinase (IKK) complex rapidly phosphorylates NF-kappaB1 p105 on serine 927 in the PEST region.
192	690	phosphorylate	p105	IKK	Following the stimulation of cells with tumor necrosis factor alpha (TNF-alpha), the IkappaB kinase (IKK) complex rapidly phosphorylates NF-kappaB1 p105 on serine 927 in the PEST region.
193	691	interaction	55K	Orf3	From our data, we infer that the Orf3 and Orf6 interactions with 55K may be mutually exclusive.
193	692	interaction	55K	Orf6	From our data, we infer that the Orf3 and Orf6 interactions with 55K may be mutually exclusive.
193	693	interaction	Orf3	55K	From our data, we infer that the Orf3 and Orf6 interactions with 55K may be mutually exclusive.
193	694	interaction	Orf6	55K	From our data, we infer that the Orf3 and Orf6 interactions with 55K may be mutually exclusive.
194	695	associate	Hsp70	Sec72p	From this observation it is suggested that Sec72p associates with a heat-shock protein, Hsp70, in a manner analogous to that known for Hop (Hsp70/Hsp90 organizing protein).
194	696	associate	Sec72p	Hsp70	From this observation it is suggested that Sec72p associates with a heat-shock protein, Hsp70, in a manner analogous to that known for Hop (Hsp70/Hsp90 organizing protein).
195	697	interaction	DmUbc9	Hsp27	Further, two-hybrid system analysis reveals DmUbc9 interaction with Drosophila and mammalian Hsp27.
195	698	interaction	Hsp27	DmUbc9	Further, two-hybrid system analysis reveals DmUbc9 interaction with Drosophila and mammalian Hsp27.
196	699	ubiquitinate	CDC6	CDH1	Furthermore, APC, in association with CDH1, ubiquitinates CDC6 in vitro, and both APC and CDH1 are required and limiting for CDC6 proteolysis in vivo.
196	700	ubiquitinate	CDH1	CDC6	Furthermore, APC, in association with CDH1, ubiquitinates CDC6 in vitro, and both APC and CDH1 are required and limiting for CDC6 proteolysis in vivo.
197	701	ubiquitinate	APC	Aurora2	Furthermore, Aurora2 is polyubiquitinated in vivo and in vitro using anaphase-promoting complex (APC).
197	702	ubiquitinate	Aurora2	APC	Furthermore, Aurora2 is polyubiquitinated in vivo and in vitro using anaphase-promoting complex (APC).
198	703	phosphorylate	BUBR1	p55CDC	Furthermore, BUBR1 phosphorylates p55CDC in vitro, and the phosphorylation of p55CDC by BUBR1 appears to be correlated with spindle checkpoint activation.
198	704	phosphorylate	p55CDC	BUBR1	Furthermore, BUBR1 phosphorylates p55CDC in vitro, and the phosphorylation of p55CDC by BUBR1 appears to be correlated with spindle checkpoint activation.
199	705	complex	CUL1	Cdc34	Furthermore, C42S/C45S and H80A mutations reduce the ability of ROC1 to interact with CUL1 in transfected cells and diminish the capacity of ROC1-CUL1 to form a stable complex with Cdc34 in vitro.
199	706	interact	CUL1	ROC1	Furthermore, C42S/C45S and H80A mutations reduce the ability of ROC1 to interact with CUL1 in transfected cells and diminish the capacity of ROC1-CUL1 to form a stable complex with Cdc34 in vitro.
199	707	complex	Cdc34	CUL1	Furthermore, C42S/C45S and H80A mutations reduce the ability of ROC1 to interact with CUL1 in transfected cells and diminish the capacity of ROC1-CUL1 to form a stable complex with Cdc34 in vitro.
199	708	complex	Cdc34	ROC1	Furthermore, C42S/C45S and H80A mutations reduce the ability of ROC1 to interact with CUL1 in transfected cells and diminish the capacity of ROC1-CUL1 to form a stable complex with Cdc34 in vitro.
199	709	interact	ROC1	CUL1	Furthermore, C42S/C45S and H80A mutations reduce the ability of ROC1 to interact with CUL1 in transfected cells and diminish the capacity of ROC1-CUL1 to form a stable complex with Cdc34 in vitro.
199	710	complex	ROC1	Cdc34	Furthermore, C42S/C45S and H80A mutations reduce the ability of ROC1 to interact with CUL1 in transfected cells and diminish the capacity of ROC1-CUL1 to form a stable complex with Cdc34 in vitro.
200	711	association	CHIP	ErbB2	Furthermore, CHIP association with ErbB2 requires a chaperone intermediate and is increased by the chaperone-binding drug geldanamycin, a potent stimulator of ErbB2 ubiquitination and degradation.
200	712	association	ErbB2	CHIP	Furthermore, CHIP association with ErbB2 requires a chaperone intermediate and is increased by the chaperone-binding drug geldanamycin, a potent stimulator of ErbB2 ubiquitination and degradation.
201	713	ubiquitinate	CDCrel-1	Parkin	Furthermore, Parkin ubiquitinates and promotes the degradation of CDCrel-1.
201	714	ubiquitinate	Parkin	CDCrel-1	Furthermore, Parkin ubiquitinates and promotes the degradation of CDCrel-1.
202	715	bound	E2	Siz1	Furthermore, Siz1 was localized at the mother-bud neck in the M-phase and physically bound to both E2 and the target proteins.
202	716	bound	Siz1	E2	Furthermore, Siz1 was localized at the mother-bud neck in the M-phase and physically bound to both E2 and the target proteins.
203	717	associate	Cln2	Skp1	Furthermore, Skp1 associated in vivo with phosphorylated Cln2 in a Grr1-dependent manner.
203	718	associate	Skp1	Cln2	Furthermore, Skp1 associated in vivo with phosphorylated Cln2 in a Grr1-dependent manner.
204	719	bind	Cdk2	Cip1	Furthermore, Skp2 and the CDK inhibitor p21 (Cip1/WAF1) bind to cyclin A-Cdk2 in a mutually exclusive manner.
204	720	bind	Cdk2	Skp2	Furthermore, Skp2 and the CDK inhibitor p21 (Cip1/WAF1) bind to cyclin A-Cdk2 in a mutually exclusive manner.
204	721	bind	Cdk2	WAF1	Furthermore, Skp2 and the CDK inhibitor p21 (Cip1/WAF1) bind to cyclin A-Cdk2 in a mutually exclusive manner.
204	722	bind	Cdk2	p21	Furthermore, Skp2 and the CDK inhibitor p21 (Cip1/WAF1) bind to cyclin A-Cdk2 in a mutually exclusive manner.
204	723	bind	Cip1	Cdk2	Furthermore, Skp2 and the CDK inhibitor p21 (Cip1/WAF1) bind to cyclin A-Cdk2 in a mutually exclusive manner.
204	724	bind	Cip1	cyclin A	Furthermore, Skp2 and the CDK inhibitor p21 (Cip1/WAF1) bind to cyclin A-Cdk2 in a mutually exclusive manner.
204	725	bind	Skp2	Cdk2	Furthermore, Skp2 and the CDK inhibitor p21 (Cip1/WAF1) bind to cyclin A-Cdk2 in a mutually exclusive manner.
204	726	bind	Skp2	cyclin A	Furthermore, Skp2 and the CDK inhibitor p21 (Cip1/WAF1) bind to cyclin A-Cdk2 in a mutually exclusive manner.
204	727	bind	WAF1	Cdk2	Furthermore, Skp2 and the CDK inhibitor p21 (Cip1/WAF1) bind to cyclin A-Cdk2 in a mutually exclusive manner.
204	728	bind	WAF1	cyclin A	Furthermore, Skp2 and the CDK inhibitor p21 (Cip1/WAF1) bind to cyclin A-Cdk2 in a mutually exclusive manner.
204	729	bind	cyclin A	Cip1	Furthermore, Skp2 and the CDK inhibitor p21 (Cip1/WAF1) bind to cyclin A-Cdk2 in a mutually exclusive manner.
204	730	bind	cyclin A	Skp2	Furthermore, Skp2 and the CDK inhibitor p21 (Cip1/WAF1) bind to cyclin A-Cdk2 in a mutually exclusive manner.
204	731	bind	cyclin A	WAF1	Furthermore, Skp2 and the CDK inhibitor p21 (Cip1/WAF1) bind to cyclin A-Cdk2 in a mutually exclusive manner.
204	732	bind	cyclin A	p21	Furthermore, Skp2 and the CDK inhibitor p21 (Cip1/WAF1) bind to cyclin A-Cdk2 in a mutually exclusive manner.
204	733	bind	p21	Cdk2	Furthermore, Skp2 and the CDK inhibitor p21 (Cip1/WAF1) bind to cyclin A-Cdk2 in a mutually exclusive manner.
204	734	bind	p21	cyclin A	Furthermore, Skp2 and the CDK inhibitor p21 (Cip1/WAF1) bind to cyclin A-Cdk2 in a mutually exclusive manner.
205	735	binding	Smad2	Smurf2	Furthermore, Smurf2 exhibited higher binding affinity to activated Smad2 upon TGF-beta stimulation.
205	736	binding	Smurf2	Smad2	Furthermore, Smurf2 exhibited higher binding affinity to activated Smad2 upon TGF-beta stimulation.
206	737	blocked	IkappaBbeta	UIP1	Furthermore, UIP1 blocked the interaction between UCH37 and S14 in vitro.
206	738	interaction	S14	UCH37	Furthermore, UIP1 blocked the interaction between UCH37 and S14 in vitro.
206	739	interaction	UCH37	S14	Furthermore, UIP1 blocked the interaction between UCH37 and S14 in vitro.
206	740	blocked	UIP1	IkappaBbeta	Furthermore, UIP1 blocked the interaction between UCH37 and S14 in vitro.
207	741	ubiquitinate	SKP2	p27	Furthermore, both in vivo and in vitro, SKP2 is a rate-limiting component of the machinery that ubiquitinates and degrades phosphorylated p27.
207	742	ubiquitinate	p27	SKP2	Furthermore, both in vivo and in vitro, SKP2 is a rate-limiting component of the machinery that ubiquitinates and degrades phosphorylated p27.
208	743	bound	AR	HDAC1	Furthermore, histone deacetylase 1 (HDAC1) bound the AR both in vivo and in cultured cells and HDAC1 binding to the AR was disengaged in a DHT-dependent manner.
208	744	bound	HDAC1	AR	Furthermore, histone deacetylase 1 (HDAC1) bound the AR both in vivo and in cultured cells and HDAC1 binding to the AR was disengaged in a DHT-dependent manner.
209	745	modified	RanGAP1	SUMO-1	Furthermore, in an in vitro system, RanGAP1 was modified by SUMO-1 in the presence of Sua1p/Uba2p and hUbc9p, showing that the modification of SUMO-1 could be catalyzed by two enzyme steps, although ubiquitination usually requires three enzyme steps.
209	746	modified	SUMO-1	RanGAP1	Furthermore, in an in vitro system, RanGAP1 was modified by SUMO-1 in the presence of Sua1p/Uba2p and hUbc9p, showing that the modification of SUMO-1 could be catalyzed by two enzyme steps, although ubiquitination usually requires three enzyme steps.
210	747	interaction	RING-H2	UbcH7	Furthermore, mutation of the RING1 finger domain of HHARI from a RING-HC to a RING-H2 type abolishes interaction with UbcH7.
210	748	interaction	UbcH7	RING-H2	Furthermore, mutation of the RING1 finger domain of HHARI from a RING-HC to a RING-H2 type abolishes interaction with UbcH7.
211	749	interaction	Nedd4	Ubc4	Furthermore, nuclear localization of N-terminal deletion mutant Nedd4 enabled us to investigate the interaction between Nedd4 and E2 enzyme (Ubc4 or UbcH7) in the cell.
211	750	interaction	Nedd4	UbcH7	Furthermore, nuclear localization of N-terminal deletion mutant Nedd4 enabled us to investigate the interaction between Nedd4 and E2 enzyme (Ubc4 or UbcH7) in the cell.
211	751	interaction	Ubc4	Nedd4	Furthermore, nuclear localization of N-terminal deletion mutant Nedd4 enabled us to investigate the interaction between Nedd4 and E2 enzyme (Ubc4 or UbcH7) in the cell.
211	752	interaction	UbcH7	Nedd4	Furthermore, nuclear localization of N-terminal deletion mutant Nedd4 enabled us to investigate the interaction between Nedd4 and E2 enzyme (Ubc4 or UbcH7) in the cell.
212	753	interaction	Cdc34	Cdc53	Furthermore, physical interactions between Met30, Cdc53, Cdc34, and Skp1 in vivo provide evidence for an SCFMet30 complex.
212	754	interaction	Cdc34	Met30	Furthermore, physical interactions between Met30, Cdc53, Cdc34, and Skp1 in vivo provide evidence for an SCFMet30 complex.
212	755	interaction	Cdc53	Cdc34	Furthermore, physical interactions between Met30, Cdc53, Cdc34, and Skp1 in vivo provide evidence for an SCFMet30 complex.
212	756	interaction	Cdc53	Met30	Furthermore, physical interactions between Met30, Cdc53, Cdc34, and Skp1 in vivo provide evidence for an SCFMet30 complex.
212	757	interaction	Cdc53	Skp1	Furthermore, physical interactions between Met30, Cdc53, Cdc34, and Skp1 in vivo provide evidence for an SCFMet30 complex.
212	758	interaction	Met30	Cdc34	Furthermore, physical interactions between Met30, Cdc53, Cdc34, and Skp1 in vivo provide evidence for an SCFMet30 complex.
212	759	interaction	Met30	Cdc53	Furthermore, physical interactions between Met30, Cdc53, Cdc34, and Skp1 in vivo provide evidence for an SCFMet30 complex.
212	760	interaction	Met30	Skp1	Furthermore, physical interactions between Met30, Cdc53, Cdc34, and Skp1 in vivo provide evidence for an SCFMet30 complex.
212	761	interaction	Skp1	Cdc53	Furthermore, physical interactions between Met30, Cdc53, Cdc34, and Skp1 in vivo provide evidence for an SCFMet30 complex.
212	762	interaction	Skp1	Met30	Furthermore, physical interactions between Met30, Cdc53, Cdc34, and Skp1 in vivo provide evidence for an SCFMet30 complex.
213	763	interact	COP9	RAR1	Furthermore, the RAR1-SGT1 complex also interacts with two COP9 signalosome components.
213	764	interact	COP9	SGT1	Furthermore, the RAR1-SGT1 complex also interacts with two COP9 signalosome components.
213	765	interact	RAR1	COP9	Furthermore, the RAR1-SGT1 complex also interacts with two COP9 signalosome components.
213	766	complex	RAR1	SGT1	Furthermore, the RAR1-SGT1 complex also interacts with two COP9 signalosome components.
213	767	interact	SGT1	COP9	Furthermore, the RAR1-SGT1 complex also interacts with two COP9 signalosome components.
213	768	complex	SGT1	RAR1	Furthermore, the RAR1-SGT1 complex also interacts with two COP9 signalosome components.
214	769	conjugation	SUMO-1	p53	Furthermore, the SUMO-1 conjugation site of p53 does not form any defined secondary structure when either free or bound to Ubc9.
214	770	bound	Ubc9	p53	Furthermore, the SUMO-1 conjugation site of p53 does not form any defined secondary structure when either free or bound to Ubc9.
214	771	conjugation	p53	SUMO-1	Furthermore, the SUMO-1 conjugation site of p53 does not form any defined secondary structure when either free or bound to Ubc9.
214	772	bound	p53	Ubc9	Furthermore, the SUMO-1 conjugation site of p53 does not form any defined secondary structure when either free or bound to Ubc9.
215	773	binding	Cdc4p	Skp1p	Furthermore, we show that binding of Skp1p to the F-box of Cdc4p inhibits R-motif-dependent degradation of Cdc4p.
215	774	binding	Skp1p	Cdc4p	Furthermore, we show that binding of Skp1p to the F-box of Cdc4p inhibits R-motif-dependent degradation of Cdc4p.
216	775	modified	AtCUL1	RUB1	Furthermore, we showed that the Skp1-Cul1/Cdc53-F-box (SCF) subunit AtCUL1 is modified by RUB1 in vivo.
216	776	modified	RUB1	AtCUL1	Furthermore, we showed that the Skp1-Cul1/Cdc53-F-box (SCF) subunit AtCUL1 is modified by RUB1 in vivo.
217	777	interact	Cul1	Fwd2	Fwd2 also interacts with Cul1 through Skp1, suggesting that Skp1, Cul1, and the F-box protein Fwd2 form an SCF complex (SCF(Fwd2)).
217	778	complex	Cul1	Skp1	Fwd2 also interacts with Cul1 through Skp1, suggesting that Skp1, Cul1, and the F-box protein Fwd2 form an SCF complex (SCF(Fwd2)).
217	779	interact	Fwd2	Cul1	Fwd2 also interacts with Cul1 through Skp1, suggesting that Skp1, Cul1, and the F-box protein Fwd2 form an SCF complex (SCF(Fwd2)).
217	780	complex	Fwd2	Skp1	Fwd2 also interacts with Cul1 through Skp1, suggesting that Skp1, Cul1, and the F-box protein Fwd2 form an SCF complex (SCF(Fwd2)).
217	781	complex	Skp1	Cul1	Fwd2 also interacts with Cul1 through Skp1, suggesting that Skp1, Cul1, and the F-box protein Fwd2 form an SCF complex (SCF(Fwd2)).
217	782	complex	Skp1	Fwd2	Fwd2 also interacts with Cul1 through Skp1, suggesting that Skp1, Cul1, and the F-box protein Fwd2 form an SCF complex (SCF(Fwd2)).
218	783	activation	Cdk2	p27	G1 nuclear export of p27 and its Ser10 phosphorylation precede cyclin-dependent kinase 2 (Cdk2) activation and degradation of the bulk of p27.
218	784	activation	p27	Cdk2	G1 nuclear export of p27 and its Ser10 phosphorylation precede cyclin-dependent kinase 2 (Cdk2) activation and degradation of the bulk of p27.
219	785	interaction	apoB48	hsp90	GA increased the recovery of microsomal apoB48 approximately 3-fold and disrupted the interaction between hsp90 and apoB48.
219	786	interaction	hsp90	apoB48	GA increased the recovery of microsomal apoB48 approximately 3-fold and disrupted the interaction between hsp90 and apoB48.
220	787	bind	GABA(A)	GABARAP	GABARAP recognizes and binds the gamma2 subunit of the GABA(A) receptor, interacts with microtubules and the N-ethyl maleimide sensitive factor, and is proposed to function in GABA(A) receptor trafficking and postsynaptic localization.
220	788	bind	GABARAP	GABA(A)	GABARAP recognizes and binds the gamma2 subunit of the GABA(A) receptor, interacts with microtubules and the N-ethyl maleimide sensitive factor, and is proposed to function in GABA(A) receptor trafficking and postsynaptic localization.
221	789	binding	GH	GHR	GH binding to the GHR results in the formation of a GH-(GHR)(2) complex and the initiation of signal transduction cascades via the activation of the tyrosine kinase JAK2.
221	790	binding	GHR	GH	GH binding to the GHR results in the formation of a GH-(GHR)(2) complex and the initiation of signal transduction cascades via the activation of the tyrosine kinase JAK2.
221	791	activation	JAK2	SKP1	GH binding to the GHR results in the formation of a GH-(GHR)(2) complex and the initiation of signal transduction cascades via the activation of the tyrosine kinase JAK2.
221	792	activation	JAK2	p19	GH binding to the GHR results in the formation of a GH-(GHR)(2) complex and the initiation of signal transduction cascades via the activation of the tyrosine kinase JAK2.
221	793	activation	SKP1	JAK2	GH binding to the GHR results in the formation of a GH-(GHR)(2) complex and the initiation of signal transduction cascades via the activation of the tyrosine kinase JAK2.
221	794	activation	p19	JAK2	GH binding to the GHR results in the formation of a GH-(GHR)(2) complex and the initiation of signal transduction cascades via the activation of the tyrosine kinase JAK2.
222	795	binding	C3b	MCP	GM2 had the same structure as GMP1, except that it lacked the fourth SCR, which is presumed to be essential for C3b binding of human MCP.
222	796	binding	MCP	C3b	GM2 had the same structure as GMP1, except that it lacked the fourth SCR, which is presumed to be essential for C3b binding of human MCP.
223	797	interaction	AdAM19	ArgBP1	GST-Pulldown assay has confirmed the interaction between AdAM19 and ArgBP1.
223	798	interaction	ArgBP1	AdAM19	GST-Pulldown assay has confirmed the interaction between AdAM19 and ArgBP1.
224	799	interaction	mTOR	ubiquilin	GST-ubiquilin 1 binds specifically to FLAG-mTOR (residues 1-670) in mammalian cells; residues 570-670 of mTOR and 226-323 of ubiquilin 1 are required for this interaction.
224	800	interaction	ubiquilin	mTOR	GST-ubiquilin 1 binds specifically to FLAG-mTOR (residues 1-670) in mammalian cells; residues 570-670 of mTOR and 226-323 of ubiquilin 1 are required for this interaction.
225	801	bound	Gankyrin	RB1	Gankyrin bound to the product of the retinoblastoma gene (RB1), increasing its phosphorylation and releasing the activity of the transcription factor E2F-1.
225	802	bound	RB1	Gankyrin	Gankyrin bound to the product of the retinoblastoma gene (RB1), increasing its phosphorylation and releasing the activity of the transcription factor E2F-1.
226	803	ubiquitinate	APC	Geminin	Geminin has a destruction box sequence and is ubiquitinated anaphase-promoting complex (APC) in vitro.
226	804	ubiquitinate	Geminin	APC	Geminin has a destruction box sequence and is ubiquitinated anaphase-promoting complex (APC) in vitro.
227	805	interact	mal2	mis12	Genetic evidence indicates that mal2(+) interacts with mis12(+), encoding another component of the inner centromere core complex.
227	806	interact	mis12	mal2	Genetic evidence indicates that mal2(+) interacts with mis12(+), encoding another component of the inner centromere core complex.
228	807	interacted	Gle1	Ulp1	Gle1, another NPC-associating component, also interacted with Ulp1 in the two-hybrid system and co-immunoprecipitation experiment.
228	808	interacted	Ulp1	Gle1	Gle1, another NPC-associating component, also interacted with Ulp1 in the two-hybrid system and co-immunoprecipitation experiment.
229	809	interaction	Grb10	Nedd4	Grb10 interacting with Nedd4 was not ubiquitinated in vivo, raising the possibility that this interaction may be used to target other proteins, like tyrosine kinase receptors, for ubiquitination.
229	810	interaction	Nedd4	Grb10	Grb10 interacting with Nedd4 was not ubiquitinated in vivo, raising the possibility that this interaction may be used to target other proteins, like tyrosine kinase receptors, for ubiquitination.
230	811	interact	Cln1	Grr1	Grr1 also interacts in vitro with phosphorylated Cln1 and Cln2.
230	812	interact	Cln2	Grr1	Grr1 also interacts in vitro with phosphorylated Cln1 and Cln2.
230	813	interact	Grr1	Cln1	Grr1 also interacts in vitro with phosphorylated Cln1 and Cln2.
230	814	interact	Grr1	Cln2	Grr1 also interacts in vitro with phosphorylated Cln1 and Cln2.
231	815	interact	Grr1	Skp1	Grr1, which is required for degradation of G1 cyclins Cln1 and Cln2 as well as for regulation of glucose repression, is an F-box protein and interacts with Skp1 through the F-box motif.
231	816	interact	Skp1	Grr1	Grr1, which is required for degradation of G1 cyclins Cln1 and Cln2 as well as for regulation of glucose repression, is an F-box protein and interacts with Skp1 through the F-box motif.
232	817	bind	HAUSP	Vmw110	HAUSP binds strongly to Vmw110, a herpesvirus regulatory protein which has the ability to disrupt ND10, while PIC1 was identified as a protein which interacts with PML, the prototype ND10 protein.
232	818	interact	PIC1	PML	HAUSP binds strongly to Vmw110, a herpesvirus regulatory protein which has the ability to disrupt ND10, while PIC1 was identified as a protein which interacts with PML, the prototype ND10 protein.
232	819	interact	PML	PIC1	HAUSP binds strongly to Vmw110, a herpesvirus regulatory protein which has the ability to disrupt ND10, while PIC1 was identified as a protein which interacts with PML, the prototype ND10 protein.
232	820	bind	Vmw110	HAUSP	HAUSP binds strongly to Vmw110, a herpesvirus regulatory protein which has the ability to disrupt ND10, while PIC1 was identified as a protein which interacts with PML, the prototype ND10 protein.
233	821	bind	E6AP	HHR23A	HHR23A binds E6AP and is ubiquitinated in vitro in an E6AP-dependent manner.
233	822	bind	HHR23A	E6AP	HHR23A binds E6AP and is ubiquitinated in vitro in an E6AP-dependent manner.
234	823	associate	HIF-1 alpha	Hsp90	HIF-1 alpha also associates with the molecular chaperone Hsp90.
234	824	associate	Hsp90	HIF-1 alpha	HIF-1 alpha also associates with the molecular chaperone Hsp90.
235	825	modified	HIPK-2	SUMO-1	HIPK-2 has been found to interact with the SUMO-1-conjugating enzyme Ubc9 and can be covalently modified by SUMO-1.
235	826	interact	HIPK-2	Ubc9	HIPK-2 has been found to interact with the SUMO-1-conjugating enzyme Ubc9 and can be covalently modified by SUMO-1.
235	827	modified	SUMO-1	HIPK-2	HIPK-2 has been found to interact with the SUMO-1-conjugating enzyme Ubc9 and can be covalently modified by SUMO-1.
235	828	interact	Ubc9	HIPK-2	HIPK-2 has been found to interact with the SUMO-1-conjugating enzyme Ubc9 and can be covalently modified by SUMO-1.
236	829	associate	Cor1	Hsubc9	Hamster Cor1 and Syn1 proteins both associate with the human ubiquitin-conjugation enzyme Hsubc9 as well as with the hamster Ubc9 homologue.
236	830	associate	Hsubc9	Cor1	Hamster Cor1 and Syn1 proteins both associate with the human ubiquitin-conjugation enzyme Hsubc9 as well as with the hamster Ubc9 homologue.
236	831	associate	Hsubc9	Syn1	Hamster Cor1 and Syn1 proteins both associate with the human ubiquitin-conjugation enzyme Hsubc9 as well as with the hamster Ubc9 homologue.
236	832	associate	Syn1	Hsubc9	Hamster Cor1 and Syn1 proteins both associate with the human ubiquitin-conjugation enzyme Hsubc9 as well as with the hamster Ubc9 homologue.
237	833	interaction	Skp1	Skp2	Here we characterized the interaction between Skp1 and the F-box protein Skp2.
237	834	interaction	Skp2	Skp1	Here we characterized the interaction between Skp1 and the F-box protein Skp2.
238	835	interact	HBX	PSMC1	Here we demonstrate that PSMC1, an ATPase-like subunit of the 19 S proteasome component, also interacts with HBX and PSMA7.
238	836	interact	PSMA7	PSMC1	Here we demonstrate that PSMC1, an ATPase-like subunit of the 19 S proteasome component, also interacts with HBX and PSMA7.
238	837	interact	PSMC1	HBX	Here we demonstrate that PSMC1, an ATPase-like subunit of the 19 S proteasome component, also interacts with HBX and PSMA7.
238	838	interact	PSMC1	PSMA7	Here we demonstrate that PSMC1, an ATPase-like subunit of the 19 S proteasome component, also interacts with HBX and PSMA7.
239	839	associate	Mdm2	Ubc9	Here we demonstrate that Ubc9 can associate with Mdm2 only if amino acids 40-59 within the N terminus of Mdm2 are present.
239	840	associate	Ubc9	Mdm2	Here we demonstrate that Ubc9 can associate with Mdm2 only if amino acids 40-59 within the N terminus of Mdm2 are present.
240	841	conjugate	Mdm2	SUMO-1	Here we demonstrate that p14ARF promotes accumulation of (H)Mdm2 conjugated to the small ubiquitin-like protein SUMO-1.
240	842	conjugate	SUMO-1	Mdm2	Here we demonstrate that p14ARF promotes accumulation of (H)Mdm2 conjugated to the small ubiquitin-like protein SUMO-1.
241	843	conjugation	Cdc53	Rub1	Here we demonstrate that the Cdc53/Rbx1 and Cul2/Rbx1 modules also activate conjugation of the ubiquitin-like protein Rub1 to Cdc53 and Cul2 by the dedicated E2 Rub1 conjugating enzyme Ubc12.
241	844	conjugation	Cul2	Rub1	Here we demonstrate that the Cdc53/Rbx1 and Cul2/Rbx1 modules also activate conjugation of the ubiquitin-like protein Rub1 to Cdc53 and Cul2 by the dedicated E2 Rub1 conjugating enzyme Ubc12.
241	845	conjugation	Rub1	Cdc53	Here we demonstrate that the Cdc53/Rbx1 and Cul2/Rbx1 modules also activate conjugation of the ubiquitin-like protein Rub1 to Cdc53 and Cul2 by the dedicated E2 Rub1 conjugating enzyme Ubc12.
241	846	conjugation	Rub1	Cul2	Here we demonstrate that the Cdc53/Rbx1 and Cul2/Rbx1 modules also activate conjugation of the ubiquitin-like protein Rub1 to Cdc53 and Cul2 by the dedicated E2 Rub1 conjugating enzyme Ubc12.
242	847	modified	HDAC4	SUMO-1	Here we demonstrate that the class II histone deacetylase HDAC4 is covalently modified by the ubiquitin-related SUMO-1 modifier.
242	848	modified	SUMO-1	HDAC4	Here we demonstrate that the class II histone deacetylase HDAC4 is covalently modified by the ubiquitin-related SUMO-1 modifier.
243	849	ubiquitinate	H2A	RAD6	Here we demonstrate that the protein encoded by the RAD6 gene, previously shown to be a ubiquitin-conjugating (E2) enzyme, multiply ubiquitinates histones H2A and H2B efficiently to give products containing as many as seven or more molecules of ubiquitin.
243	850	ubiquitinate	H2B	RAD6	Here we demonstrate that the protein encoded by the RAD6 gene, previously shown to be a ubiquitin-conjugating (E2) enzyme, multiply ubiquitinates histones H2A and H2B efficiently to give products containing as many as seven or more molecules of ubiquitin.
243	851	ubiquitinate	RAD6	H2A	Here we demonstrate that the protein encoded by the RAD6 gene, previously shown to be a ubiquitin-conjugating (E2) enzyme, multiply ubiquitinates histones H2A and H2B efficiently to give products containing as many as seven or more molecules of ubiquitin.
243	852	ubiquitinate	RAD6	H2B	Here we demonstrate that the protein encoded by the RAD6 gene, previously shown to be a ubiquitin-conjugating (E2) enzyme, multiply ubiquitinates histones H2A and H2B efficiently to give products containing as many as seven or more molecules of ubiquitin.
244	853	interact	elongin B	pVHL	Here we demonstrate that the vector YIpDCE1 can be used to express elongins B and C in yeast, and that these proteins form a stable complex that interacts with the von Hippel-Lindau tumor-suppressor gene product (pVHL).
244	854	interact	elongin C	pVHL	Here we demonstrate that the vector YIpDCE1 can be used to express elongins B and C in yeast, and that these proteins form a stable complex that interacts with the von Hippel-Lindau tumor-suppressor gene product (pVHL).
244	855	interact	pVHL	elongin B	Here we demonstrate that the vector YIpDCE1 can be used to express elongins B and C in yeast, and that these proteins form a stable complex that interacts with the von Hippel-Lindau tumor-suppressor gene product (pVHL).
244	856	interact	pVHL	elongin C	Here we demonstrate that the vector YIpDCE1 can be used to express elongins B and C in yeast, and that these proteins form a stable complex that interacts with the von Hippel-Lindau tumor-suppressor gene product (pVHL).
245	857	recognize	IkappaBalpha	SCFbeta-TRCP	Here we describe a biochemical dissection of a novel mammalian SCF complex, SCFbeta-TRCP, that specifically recognizes a 19-amino-acid destruction motif in IkappaBalpha (residues 21-41) in a phosphorylation-dependent manner.
245	858	recognize	SCFbeta-TRCP	IkappaBalpha	Here we describe a biochemical dissection of a novel mammalian SCF complex, SCFbeta-TRCP, that specifically recognizes a 19-amino-acid destruction motif in IkappaBalpha (residues 21-41) in a phosphorylation-dependent manner.
246	859	interact	Cdc20	Pds1	Here we find that Pds1 interacts directly with Cdc20 and that this interaction requires Pds1's destruction box.
246	860	interact	Pds1	Cdc20	Here we find that Pds1 interacts directly with Cdc20 and that this interaction requires Pds1's destruction box.
247	861	binding	Cln2	Grr1	Here we identify the domain of Cln2 that confers instability and describe the signals in Cln2 that result in binding to Grr1 and rapid degradation.
247	862	binding	Grr1	Cln2	Here we identify the domain of Cln2 that confers instability and describe the signals in Cln2 that result in binding to Grr1 and rapid degradation.
248	863	bind	APC	APC10	Here we isolated and characterized human APC10/Doc1, and found that APC10/Doc1 binds to APC core subunits throughout the cell cycle.
248	864	bind	APC	Doc1	Here we isolated and characterized human APC10/Doc1, and found that APC10/Doc1 binds to APC core subunits throughout the cell cycle.
248	865	bind	APC10	APC	Here we isolated and characterized human APC10/Doc1, and found that APC10/Doc1 binds to APC core subunits throughout the cell cycle.
248	866	bind	Doc1	APC	Here we isolated and characterized human APC10/Doc1, and found that APC10/Doc1 binds to APC core subunits throughout the cell cycle.
249	867	interact	Smad7	p300	Here we present evidence that Smad7 interacts with the transcriptional coactivator p300, resulting in acetylation of Smad7 on two lysine residues in its N terminus.
249	868	interact	p300	Smad7	Here we present evidence that Smad7 interacts with the transcriptional coactivator p300, resulting in acetylation of Smad7 on two lysine residues in its N terminus.
250	869	inhibitor	IkappaBalpha	NF-kappaB	Here we present evidence that ts1 infection of astrocytes in vitro activates NF-kappaB by enhanced proteolysis of the NF-kappaB inhibitors, IkappaBalpha and IkappaBbeta.
250	870	inhibitor	IkappaBbeta	NF-kappaB	Here we present evidence that ts1 infection of astrocytes in vitro activates NF-kappaB by enhanced proteolysis of the NF-kappaB inhibitors, IkappaBalpha and IkappaBbeta.
250	871	inhibitor	NF-kappaB	IkappaBalpha	Here we present evidence that ts1 infection of astrocytes in vitro activates NF-kappaB by enhanced proteolysis of the NF-kappaB inhibitors, IkappaBalpha and IkappaBbeta.
250	872	inhibitor	NF-kappaB	IkappaBbeta	Here we present evidence that ts1 infection of astrocytes in vitro activates NF-kappaB by enhanced proteolysis of the NF-kappaB inhibitors, IkappaBalpha and IkappaBbeta.
251	873	activate	APC	Plk	Here we report that Cdc2-cyclin B-activated Polo-like kinase (Plk) specifically phosphorylates at least three components of APC and activates APC to ubiquitinate cyclin B in the in vitro-reconstituted system.
251	874	ubiquitinate	APC	cyclin B	Here we report that Cdc2-cyclin B-activated Polo-like kinase (Plk) specifically phosphorylates at least three components of APC and activates APC to ubiquitinate cyclin B in the in vitro-reconstituted system.
251	875	activate	Cdc2	Plk	Here we report that Cdc2-cyclin B-activated Polo-like kinase (Plk) specifically phosphorylates at least three components of APC and activates APC to ubiquitinate cyclin B in the in vitro-reconstituted system.
251	876	activate	Plk	APC	Here we report that Cdc2-cyclin B-activated Polo-like kinase (Plk) specifically phosphorylates at least three components of APC and activates APC to ubiquitinate cyclin B in the in vitro-reconstituted system.
251	877	activate	Plk	Cdc2	Here we report that Cdc2-cyclin B-activated Polo-like kinase (Plk) specifically phosphorylates at least three components of APC and activates APC to ubiquitinate cyclin B in the in vitro-reconstituted system.
251	878	activate	Plk	cyclin B	Here we report that Cdc2-cyclin B-activated Polo-like kinase (Plk) specifically phosphorylates at least three components of APC and activates APC to ubiquitinate cyclin B in the in vitro-reconstituted system.
251	879	ubiquitinate	cyclin B	APC	Here we report that Cdc2-cyclin B-activated Polo-like kinase (Plk) specifically phosphorylates at least three components of APC and activates APC to ubiquitinate cyclin B in the in vitro-reconstituted system.
251	880	activate	cyclin B	Plk	Here we report that Cdc2-cyclin B-activated Polo-like kinase (Plk) specifically phosphorylates at least three components of APC and activates APC to ubiquitinate cyclin B in the in vitro-reconstituted system.
252	881	conjugation	CUL1	Nedd8	Here we report that the conjugation of Nedd8 to ROC1-CUL1, a subcomplex of the SCF-ROC1 E3 ubiquitin ligase, selectively stimulates Cdc34-catalyzed lysine 48-linked multiubiquitin chain assembly.
252	882	conjugation	Nedd8	CUL1	Here we report that the conjugation of Nedd8 to ROC1-CUL1, a subcomplex of the SCF-ROC1 E3 ubiquitin ligase, selectively stimulates Cdc34-catalyzed lysine 48-linked multiubiquitin chain assembly.
252	883	conjugation	Nedd8	ROC1	Here we report that the conjugation of Nedd8 to ROC1-CUL1, a subcomplex of the SCF-ROC1 E3 ubiquitin ligase, selectively stimulates Cdc34-catalyzed lysine 48-linked multiubiquitin chain assembly.
252	884	conjugation	ROC1	Nedd8	Here we report that the conjugation of Nedd8 to ROC1-CUL1, a subcomplex of the SCF-ROC1 E3 ubiquitin ligase, selectively stimulates Cdc34-catalyzed lysine 48-linked multiubiquitin chain assembly.
253	885	interacting	CK2	UBC3B	Here we report the identification by yeast interaction trap of a CK2 interacting protein, UBC3B, which is highly homologous to the E2 ubiquitin conjugating enzyme UBC3/CDC34.
253	886	interacting	UBC3B	CK2	Here we report the identification by yeast interaction trap of a CK2 interacting protein, UBC3B, which is highly homologous to the E2 ubiquitin conjugating enzyme UBC3/CDC34.
254	887	conjugation	H2A	ubiquitin	Here we report the purification and characterization of a novel protein that is required along with the protease for the degradation of ubiquitin conjugates of histone H2A, an N-alpha-acetylated protein.
254	888	conjugation	ubiquitin	H2A	Here we report the purification and characterization of a novel protein that is required along with the protease for the degradation of ubiquitin conjugates of histone H2A, an N-alpha-acetylated protein.
255	889	interact	CDC16	PP5	Here we show by a combination of two-hybrid analysis and in vitro binding that PP5 interacts with CDC16 and CDC27, two subunits of the anaphase-promoting complex.
255	890	interact	CDC27	PP5	Here we show by a combination of two-hybrid analysis and in vitro binding that PP5 interacts with CDC16 and CDC27, two subunits of the anaphase-promoting complex.
255	891	interact	PP5	CDC16	Here we show by a combination of two-hybrid analysis and in vitro binding that PP5 interacts with CDC16 and CDC27, two subunits of the anaphase-promoting complex.
255	892	interact	PP5	CDC27	Here we show by a combination of two-hybrid analysis and in vitro binding that PP5 interacts with CDC16 and CDC27, two subunits of the anaphase-promoting complex.
256	893	interact	Nedd4-2	Sgk1 kinase	Here we show by expression studies in Xenopus laevis oocytes that the aldosterone-induced Sgk1 kinase interacts with the ubiquitin protein ligase Nedd4-2 in a PY motif-dependent manner and phosphorylates Nedd4-2 on Ser444 and, to a lesser extent, Ser338.
256	894	interact	Sgk1 kinase	Nedd4-2	Here we show by expression studies in Xenopus laevis oocytes that the aldosterone-induced Sgk1 kinase interacts with the ubiquitin protein ligase Nedd4-2 in a PY motif-dependent manner and phosphorylates Nedd4-2 on Ser444 and, to a lesser extent, Ser338.
257	895	associate	55K	Orf3	Here we show that 55K also associates with Orf3 and that this interaction is necessary for 55K to localize to the nuclear matrix fraction of the cell.
257	896	associate	Orf3	55K	Here we show that 55K also associates with Orf3 and that this interaction is necessary for 55K to localize to the nuclear matrix fraction of the cell.
258	897	modification	Cul-1	Nedd8	Here we show that Nedd8 modification of the Cul-1 component of SCF(beta(TrCP)) is important for function of SCF(beta(TrCP)) in ubiquitination of IkappaBalpha.
258	898	modification	Nedd8	Cul-1	Here we show that Nedd8 modification of the Cul-1 component of SCF(beta(TrCP)) is important for function of SCF(beta(TrCP)) in ubiquitination of IkappaBalpha.
259	899	interact	26S	Rad23	Here we show that Rad23 interacts with the 26S proteasome through an amino-terminal ubiquitin-like domain (UbL[R23]).
259	900	interact	Rad23	26S	Here we show that Rad23 interacts with the 26S proteasome through an amino-terminal ubiquitin-like domain (UbL[R23]).
260	901	ubiquitinate	NAC1	SINAT5	Here we show that SINAT5, an Arabidopsis homologue of the RING-finger Drosophila protein SINA, has ubiquitin protein ligase activity and can ubiquitinate NAC1.
260	902	ubiquitinate	SINAT5	NAC1	Here we show that SINAT5, an Arabidopsis homologue of the RING-finger Drosophila protein SINA, has ubiquitin protein ligase activity and can ubiquitinate NAC1.
261	903	interact	ASK1	SnRK	Here we show that SKP1/ASK1, a conserved SCF (Skp1-cullin-F-box) ubiquitin ligase subunit, which suppresses the skp1-4 mitotic defect in yeast, interacts with the PRL1-binding C-terminal domains of SnRKs.
261	904	interact	SKP1	SnRK	Here we show that SKP1/ASK1, a conserved SCF (Skp1-cullin-F-box) ubiquitin ligase subunit, which suppresses the skp1-4 mitotic defect in yeast, interacts with the PRL1-binding C-terminal domains of SnRKs.
261	905	interact	SnRK	ASK1	Here we show that SKP1/ASK1, a conserved SCF (Skp1-cullin-F-box) ubiquitin ligase subunit, which suppresses the skp1-4 mitotic defect in yeast, interacts with the PRL1-binding C-terminal domains of SnRKs.
261	906	interact	SnRK	SKP1	Here we show that SKP1/ASK1, a conserved SCF (Skp1-cullin-F-box) ubiquitin ligase subunit, which suppresses the skp1-4 mitotic defect in yeast, interacts with the PRL1-binding C-terminal domains of SnRKs.
262	907	associate	NM23-H1	STK15	Here we show that STK15 associates with a putative tumor and metastasis suppressor, NM23-H1.
262	908	associate	STK15	NM23-H1	Here we show that STK15 associates with a putative tumor and metastasis suppressor, NM23-H1.
263	909	modify	PML	SUMO-1	Here we show that SUMO-1 covalently modifies PML both in vivo and in vitro and that the modification is mediated either directly or indirectly by the interaction of UBC9 with PML through the RING finger domain.
263	910	interaction	PML	UBC9	Here we show that SUMO-1 covalently modifies PML both in vivo and in vitro and that the modification is mediated either directly or indirectly by the interaction of UBC9 with PML through the RING finger domain.
263	911	modify	SUMO-1	PML	Here we show that SUMO-1 covalently modifies PML both in vivo and in vitro and that the modification is mediated either directly or indirectly by the interaction of UBC9 with PML through the RING finger domain.
263	912	interaction	UBC9	PML	Here we show that SUMO-1 covalently modifies PML both in vivo and in vitro and that the modification is mediated either directly or indirectly by the interaction of UBC9 with PML through the RING finger domain.
264	913	interact	Smad7	Smurf1	Here we show that Smurf1, an E3 ubiquitin ligase for bone morphogenetic protein-specific Smads, also interacts with Smad7 and induces Smad7 ubiquitination and translocation into the cytoplasm.
264	914	interact	Smurf1	Smad7	Here we show that Smurf1, an E3 ubiquitin ligase for bone morphogenetic protein-specific Smads, also interacts with Smad7 and induces Smad7 ubiquitination and translocation into the cytoplasm.
265	915	interact	26S	Ubr1p	Here we show that Ubr1p and Ufd4p, the E3 components of two distinct Ub ligases, directly interact with the 26S proteasome.
265	916	interact	26S	Ufd4p	Here we show that Ubr1p and Ufd4p, the E3 components of two distinct Ub ligases, directly interact with the 26S proteasome.
265	917	interact	Ubr1p	26S	Here we show that Ubr1p and Ufd4p, the E3 components of two distinct Ub ligases, directly interact with the 26S proteasome.
265	918	interact	Ufd4p	26S	Here we show that Ubr1p and Ufd4p, the E3 components of two distinct Ub ligases, directly interact with the 26S proteasome.
266	919	binding	TNF-RII	TNF-alpha	Here we show that binding of TNF-alpha to TNF-RII induces ubiquitination and proteasomal degradation of TRAF2.
266	920	binding	TNF-alpha	TNF-RII	Here we show that binding of TNF-alpha to TNF-RII induces ubiquitination and proteasomal degradation of TRAF2.
267	921	modified	SUMO-1	p53	Here we show that p53 is modified by the small ubiquitin-like protein SUMO-1 at a single site, K386, in the C-terminus of the protein.
267	922	modified	p53	SUMO-1	Here we show that p53 is modified by the small ubiquitin-like protein SUMO-1 at a single site, K386, in the C-terminus of the protein.
268	923	bind	HIF	pVHL	Here we show that pVHL, through its beta-domain, binds directly to hypoxia-inducible factor (HIF), thereby targeting HIF for ubiquitination in an alpha-domain-dependent manner.
268	924	bind	pVHL	HIF	Here we show that pVHL, through its beta-domain, binds directly to hypoxia-inducible factor (HIF), thereby targeting HIF for ubiquitination in an alpha-domain-dependent manner.
269	925	complex	Apg16	Apg5	Here we show that the Apg12-Apg5 conjugate and Apg16 form a approximately 350-kDa complex in the cytosol.
269	926	complex	Apg5	Apg16	Here we show that the Apg12-Apg5 conjugate and Apg16 form a approximately 350-kDa complex in the cytosol.
270	927	recognize	SKP2	p27	Here we show that the F-box protein SKP2 specifically recognizes p27 in a phosphorylation-dependent manner that is characteristic of an F-box-protein-substrate interaction.
270	928	recognize	p27	SKP2	Here we show that the F-box protein SKP2 specifically recognizes p27 in a phosphorylation-dependent manner that is characteristic of an F-box-protein-substrate interaction.
271	929	modification	PML	SUMO-1	Here we show that the HSV ICP0 and CMV IE1 proteins specifically abrogate the SUMO-1 modification of PML and Sp100, whereas the adenovirus E4 ORF3 protein does not affect this process.
271	930	modification	SUMO-1	PML	Here we show that the HSV ICP0 and CMV IE1 proteins specifically abrogate the SUMO-1 modification of PML and Sp100, whereas the adenovirus E4 ORF3 protein does not affect this process.
271	931	modification	SUMO-1	Sp100	Here we show that the HSV ICP0 and CMV IE1 proteins specifically abrogate the SUMO-1 modification of PML and Sp100, whereas the adenovirus E4 ORF3 protein does not affect this process.
271	932	modification	Sp100	SUMO-1	Here we show that the HSV ICP0 and CMV IE1 proteins specifically abrogate the SUMO-1 modification of PML and Sp100, whereas the adenovirus E4 ORF3 protein does not affect this process.
272	933	bind	AIP4	LMP2A	Here we show that the PPPPY motifs of LMP2A bind multiple WW domains of E3 protein-ubiquitin ligases of the Nedd4 family, including AIP4 and KIAA0439, and demonstrate that AIP4 and KIAA0439 form physiological complexes with LMP2A in EBV-positive B cells.
272	934	bind	KIAA0439	LMP2A	Here we show that the PPPPY motifs of LMP2A bind multiple WW domains of E3 protein-ubiquitin ligases of the Nedd4 family, including AIP4 and KIAA0439, and demonstrate that AIP4 and KIAA0439 form physiological complexes with LMP2A in EBV-positive B cells.
272	935	bind	LMP2A	AIP4	Here we show that the PPPPY motifs of LMP2A bind multiple WW domains of E3 protein-ubiquitin ligases of the Nedd4 family, including AIP4 and KIAA0439, and demonstrate that AIP4 and KIAA0439 form physiological complexes with LMP2A in EBV-positive B cells.
272	936	bind	LMP2A	KIAA0439	Here we show that the PPPPY motifs of LMP2A bind multiple WW domains of E3 protein-ubiquitin ligases of the Nedd4 family, including AIP4 and KIAA0439, and demonstrate that AIP4 and KIAA0439 form physiological complexes with LMP2A in EBV-positive B cells.
273	937	bind	CDKs	Cks	Here we show that the missing factor is CDK subunit 1 (Cks1), which belongs to the highly conserved Suc1/Cks family of proteins that bind to some CDKs and phosphorylated proteins and are essential for cell-cycle progression.
273	938	bind	CDKs	Cks1	Here we show that the missing factor is CDK subunit 1 (Cks1), which belongs to the highly conserved Suc1/Cks family of proteins that bind to some CDKs and phosphorylated proteins and are essential for cell-cycle progression.
273	939	bind	CDKs	Suc1	Here we show that the missing factor is CDK subunit 1 (Cks1), which belongs to the highly conserved Suc1/Cks family of proteins that bind to some CDKs and phosphorylated proteins and are essential for cell-cycle progression.
273	940	bind	Cks	CDKs	Here we show that the missing factor is CDK subunit 1 (Cks1), which belongs to the highly conserved Suc1/Cks family of proteins that bind to some CDKs and phosphorylated proteins and are essential for cell-cycle progression.
273	941	bind	Cks1	CDKs	Here we show that the missing factor is CDK subunit 1 (Cks1), which belongs to the highly conserved Suc1/Cks family of proteins that bind to some CDKs and phosphorylated proteins and are essential for cell-cycle progression.
273	942	bind	Suc1	CDKs	Here we show that the missing factor is CDK subunit 1 (Cks1), which belongs to the highly conserved Suc1/Cks family of proteins that bind to some CDKs and phosphorylated proteins and are essential for cell-cycle progression.
274	943	complex	Cb1	FRS2	Here, we demonstrate that Grb2 bound to tyrosine-phosphorylated FRS2 alpha forms a ternary complex with Cbl by means of its Src homology 3 domains resulting in the ubiquitination of fibroblast growth factor (FGF) receptor and FRS2 alpha in response to FGF stimulation.
274	944	complex	Cb1	Grb2	Here, we demonstrate that Grb2 bound to tyrosine-phosphorylated FRS2 alpha forms a ternary complex with Cbl by means of its Src homology 3 domains resulting in the ubiquitination of fibroblast growth factor (FGF) receptor and FRS2 alpha in response to FGF stimulation.
274	945	complex	FRS2	Cb1	Here, we demonstrate that Grb2 bound to tyrosine-phosphorylated FRS2 alpha forms a ternary complex with Cbl by means of its Src homology 3 domains resulting in the ubiquitination of fibroblast growth factor (FGF) receptor and FRS2 alpha in response to FGF stimulation.
274	946	bound	FRS2	Grb2	Here, we demonstrate that Grb2 bound to tyrosine-phosphorylated FRS2 alpha forms a ternary complex with Cbl by means of its Src homology 3 domains resulting in the ubiquitination of fibroblast growth factor (FGF) receptor and FRS2 alpha in response to FGF stimulation.
274	947	complex	Grb2	Cb1	Here, we demonstrate that Grb2 bound to tyrosine-phosphorylated FRS2 alpha forms a ternary complex with Cbl by means of its Src homology 3 domains resulting in the ubiquitination of fibroblast growth factor (FGF) receptor and FRS2 alpha in response to FGF stimulation.
274	948	bound	Grb2	FRS2	Here, we demonstrate that Grb2 bound to tyrosine-phosphorylated FRS2 alpha forms a ternary complex with Cbl by means of its Src homology 3 domains resulting in the ubiquitination of fibroblast growth factor (FGF) receptor and FRS2 alpha in response to FGF stimulation.
275	949	associate	26S	PA28	Here, we demonstrate that, in vitro, PA28 can associate with 'singly capped' 26S (i.e. 19S-20S) proteasomes.
275	950	associate	PA28	26S	Here, we demonstrate that, in vitro, PA28 can associate with 'singly capped' 26S (i.e. 19S-20S) proteasomes.
276	951	associate	Smad7	Smurf2	Here, we identify Smurf2, a C2-WW-HECT domain ubiquitin ligase and show that Smurf2 associates constitutively with Smad7.
276	952	associate	Smurf2	Smad7	Here, we identify Smurf2, a C2-WW-HECT domain ubiquitin ligase and show that Smurf2 associates constitutively with Smad7.
277	953	modified	ARNT	SUMO-1	Here, we report that ARNT is modified by SUMO-1 chiefly at Lys(245) within the PAS domain of this protein, both in vivo and in vitro.
277	954	modified	SUMO-1	ARNT	Here, we report that ARNT is modified by SUMO-1 chiefly at Lys(245) within the PAS domain of this protein, both in vivo and in vitro.
278	955	interact	Nedd4	VP40	Here, we report that Ebola VP40 can interact with cellular factors human Nedd4 and Tsg101 in vitro.
278	956	interact	Tsg101	VP40	Here, we report that Ebola VP40 can interact with cellular factors human Nedd4 and Tsg101 in vitro.
278	957	interact	VP40	Nedd4	Here, we report that Ebola VP40 can interact with cellular factors human Nedd4 and Tsg101 in vitro.
278	958	interact	VP40	Tsg101	Here, we report that Ebola VP40 can interact with cellular factors human Nedd4 and Tsg101 in vitro.
279	959	activate	IFN-alpha	JAK-STAT1	Here, we report that IFN-alpha/beta and IFN-gamma rapidly activate the JAK-STAT1 (Janus kinase-signal transducer and activator transcription factor 1) and p42/44 mitogen-activated protein kinase (p42/44 MAPK) in freshly isolated rat hepatocytes.
279	960	activate	IFN-alpha	p42/44 MAPK	Here, we report that IFN-alpha/beta and IFN-gamma rapidly activate the JAK-STAT1 (Janus kinase-signal transducer and activator transcription factor 1) and p42/44 mitogen-activated protein kinase (p42/44 MAPK) in freshly isolated rat hepatocytes.
279	961	activate	IFN-beta	JAK-STAT1	Here, we report that IFN-alpha/beta and IFN-gamma rapidly activate the JAK-STAT1 (Janus kinase-signal transducer and activator transcription factor 1) and p42/44 mitogen-activated protein kinase (p42/44 MAPK) in freshly isolated rat hepatocytes.
279	962	activate	IFN-beta	p42/44 MAPK	Here, we report that IFN-alpha/beta and IFN-gamma rapidly activate the JAK-STAT1 (Janus kinase-signal transducer and activator transcription factor 1) and p42/44 mitogen-activated protein kinase (p42/44 MAPK) in freshly isolated rat hepatocytes.
279	963	activate	IFN-gamma	JAK-STAT1	Here, we report that IFN-alpha/beta and IFN-gamma rapidly activate the JAK-STAT1 (Janus kinase-signal transducer and activator transcription factor 1) and p42/44 mitogen-activated protein kinase (p42/44 MAPK) in freshly isolated rat hepatocytes.
279	964	activate	IFN-gamma	p42/44 MAPK	Here, we report that IFN-alpha/beta and IFN-gamma rapidly activate the JAK-STAT1 (Janus kinase-signal transducer and activator transcription factor 1) and p42/44 mitogen-activated protein kinase (p42/44 MAPK) in freshly isolated rat hepatocytes.
279	965	activate	JAK-STAT1	IFN-alpha	Here, we report that IFN-alpha/beta and IFN-gamma rapidly activate the JAK-STAT1 (Janus kinase-signal transducer and activator transcription factor 1) and p42/44 mitogen-activated protein kinase (p42/44 MAPK) in freshly isolated rat hepatocytes.
279	966	activate	JAK-STAT1	IFN-beta	Here, we report that IFN-alpha/beta and IFN-gamma rapidly activate the JAK-STAT1 (Janus kinase-signal transducer and activator transcription factor 1) and p42/44 mitogen-activated protein kinase (p42/44 MAPK) in freshly isolated rat hepatocytes.
279	967	activate	JAK-STAT1	IFN-gamma	Here, we report that IFN-alpha/beta and IFN-gamma rapidly activate the JAK-STAT1 (Janus kinase-signal transducer and activator transcription factor 1) and p42/44 mitogen-activated protein kinase (p42/44 MAPK) in freshly isolated rat hepatocytes.
279	968	activate	p42/44 MAPK	IFN-alpha	Here, we report that IFN-alpha/beta and IFN-gamma rapidly activate the JAK-STAT1 (Janus kinase-signal transducer and activator transcription factor 1) and p42/44 mitogen-activated protein kinase (p42/44 MAPK) in freshly isolated rat hepatocytes.
279	969	activate	p42/44 MAPK	IFN-beta	Here, we report that IFN-alpha/beta and IFN-gamma rapidly activate the JAK-STAT1 (Janus kinase-signal transducer and activator transcription factor 1) and p42/44 mitogen-activated protein kinase (p42/44 MAPK) in freshly isolated rat hepatocytes.
279	970	activate	p42/44 MAPK	IFN-gamma	Here, we report that IFN-alpha/beta and IFN-gamma rapidly activate the JAK-STAT1 (Janus kinase-signal transducer and activator transcription factor 1) and p42/44 mitogen-activated protein kinase (p42/44 MAPK) in freshly isolated rat hepatocytes.
280	971	interact	Skp1	VirF	Here, we report that the VirF protein is the first prokaryotic protein with an F box by which it can interact with plant homologs of the yeast Skp1 protein.
280	972	interact	VirF	Skp1	Here, we report that the VirF protein is the first prokaryotic protein with an F box by which it can interact with plant homologs of the yeast Skp1 protein.
281	973	complex	CHIP	Hsp70	Here, we show that CHIP, Hsp70, Parkin, and Pael-R formed a complex in vitro and in vivo.
281	974	complex	CHIP	Pael-R	Here, we show that CHIP, Hsp70, Parkin, and Pael-R formed a complex in vitro and in vivo.
281	975	complex	CHIP	Parkin	Here, we show that CHIP, Hsp70, Parkin, and Pael-R formed a complex in vitro and in vivo.
281	976	complex	Hsp70	CHIP	Here, we show that CHIP, Hsp70, Parkin, and Pael-R formed a complex in vitro and in vivo.
281	977	complex	Hsp70	Pael-R	Here, we show that CHIP, Hsp70, Parkin, and Pael-R formed a complex in vitro and in vivo.
281	978	complex	Hsp70	Parkin	Here, we show that CHIP, Hsp70, Parkin, and Pael-R formed a complex in vitro and in vivo.
281	979	complex	Pael-R	CHIP	Here, we show that CHIP, Hsp70, Parkin, and Pael-R formed a complex in vitro and in vivo.
281	980	complex	Pael-R	Hsp70	Here, we show that CHIP, Hsp70, Parkin, and Pael-R formed a complex in vitro and in vivo.
281	981	complex	Pael-R	Parkin	Here, we show that CHIP, Hsp70, Parkin, and Pael-R formed a complex in vitro and in vivo.
281	982	complex	Parkin	CHIP	Here, we show that CHIP, Hsp70, Parkin, and Pael-R formed a complex in vitro and in vivo.
281	983	complex	Parkin	Hsp70	Here, we show that CHIP, Hsp70, Parkin, and Pael-R formed a complex in vitro and in vivo.
281	984	complex	Parkin	Pael-R	Here, we show that CHIP, Hsp70, Parkin, and Pael-R formed a complex in vitro and in vivo.
282	985	interact	RAR1	SGT1	Here, we show that RAR1 interacts with plant orthologs of the yeast protein SGT1, an essential regulator in the cell cycle.
282	986	interact	SGT1	RAR1	Here, we show that RAR1 interacts with plant orthologs of the yeast protein SGT1, an essential regulator in the cell cycle.
283	987	interact	Ddi1	ubiquitin	Here, we show that Rad23 and Ddi1 interact directly with ubiquitin and that this interaction is dependent on their UBA domains, providing a possible mechanism for UBA-dependent cell cycle control.
283	988	interact	Rad23	ubiquitin	Here, we show that Rad23 and Ddi1 interact directly with ubiquitin and that this interaction is dependent on their UBA domains, providing a possible mechanism for UBA-dependent cell cycle control.
283	989	interact	ubiquitin	Ddi1	Here, we show that Rad23 and Ddi1 interact directly with ubiquitin and that this interaction is dependent on their UBA domains, providing a possible mechanism for UBA-dependent cell cycle control.
283	990	interact	ubiquitin	Rad23	Here, we show that Rad23 and Ddi1 interact directly with ubiquitin and that this interaction is dependent on their UBA domains, providing a possible mechanism for UBA-dependent cell cycle control.
284	991	interact	BEN	HDAC3	Here, we show that TFII-I and its related member hMusTRD1/BEN physically and functionally interact with HDAC3.
284	992	interact	HDAC3	BEN	Here, we show that TFII-I and its related member hMusTRD1/BEN physically and functionally interact with HDAC3.
284	993	interact	HDAC3	TFII-I	Here, we show that TFII-I and its related member hMusTRD1/BEN physically and functionally interact with HDAC3.
284	994	interact	HDAC3	hMusTRD1	Here, we show that TFII-I and its related member hMusTRD1/BEN physically and functionally interact with HDAC3.
284	995	interact	TFII-I	HDAC3	Here, we show that TFII-I and its related member hMusTRD1/BEN physically and functionally interact with HDAC3.
284	996	interact	hMusTRD1	HDAC3	Here, we show that TFII-I and its related member hMusTRD1/BEN physically and functionally interact with HDAC3.
285	997	transferred	Apg10p	Apg12p	Here, we show that after activation by Apg7p, Apg12p is transferred to the Cys-133 residue of Apg10p to form an Apg12p-Apg10p thioester.
285	998	transferred	Apg12p	Apg10p	Here, we show that after activation by Apg7p, Apg12p is transferred to the Cys-133 residue of Apg10p to form an Apg12p-Apg10p thioester.
285	999	activate	Apg12p	Apg7p	Here, we show that after activation by Apg7p, Apg12p is transferred to the Cys-133 residue of Apg10p to form an Apg12p-Apg10p thioester.
285	1000	activate	Apg7p	Apg12p	Here, we show that after activation by Apg7p, Apg12p is transferred to the Cys-133 residue of Apg10p to form an Apg12p-Apg10p thioester.
286	1001	modified	NEDD8	hCUL-2	Here, we show that hCUL-2 is modified by the conserved ubiquitin-like protein NEDD8 and that NEDD8-hCUL-2 conjugates are part of CBCVHL complexes in vivo.
286	1002	modified	hCUL-2	NEDD8	Here, we show that hCUL-2 is modified by the conserved ubiquitin-like protein NEDD8 and that NEDD8-hCUL-2 conjugates are part of CBCVHL complexes in vivo.
287	1003	interact	SKP2	hCUL1	Here, we show that hCUL1 associates with hSKP1 in vivo and directly interacts with both hSKP1 and the human F-box protein SKP2 in vitro, forming an SCF-like particle.
287	1004	interact	hCUL1	SKP2	Here, we show that hCUL1 associates with hSKP1 in vivo and directly interacts with both hSKP1 and the human F-box protein SKP2 in vitro, forming an SCF-like particle.
287	1005	interact	hCUL1	hSKP1	Here, we show that hCUL1 associates with hSKP1 in vivo and directly interacts with both hSKP1 and the human F-box protein SKP2 in vitro, forming an SCF-like particle.
287	1006	interact	hSKP1	hCUL1	Here, we show that hCUL1 associates with hSKP1 in vivo and directly interacts with both hSKP1 and the human F-box protein SKP2 in vitro, forming an SCF-like particle.
288	1007	bound	APC	hCDC20	Here, we show that the amount of hCDC20 and hCDH1 bound to APC correlates with a high ubiquitination activity of APC and that binding of recombinant hCDC20 and hCDH1 can activate APC in vitro.
288	1008	bound	APC	hCDH1	Here, we show that the amount of hCDC20 and hCDH1 bound to APC correlates with a high ubiquitination activity of APC and that binding of recombinant hCDC20 and hCDH1 can activate APC in vitro.
288	1009	bound	hCDC20	APC	Here, we show that the amount of hCDC20 and hCDH1 bound to APC correlates with a high ubiquitination activity of APC and that binding of recombinant hCDC20 and hCDH1 can activate APC in vitro.
288	1010	binding	hCDC20	hCDH1	Here, we show that the amount of hCDC20 and hCDH1 bound to APC correlates with a high ubiquitination activity of APC and that binding of recombinant hCDC20 and hCDH1 can activate APC in vitro.
288	1011	bound	hCDH1	APC	Here, we show that the amount of hCDC20 and hCDH1 bound to APC correlates with a high ubiquitination activity of APC and that binding of recombinant hCDC20 and hCDH1 can activate APC in vitro.
288	1012	binding	hCDH1	hCDC20	Here, we show that the amount of hCDC20 and hCDH1 bound to APC correlates with a high ubiquitination activity of APC and that binding of recombinant hCDC20 and hCDH1 can activate APC in vitro.
289	1013	interact	SALL1	SUMO-1	Here, we show that the ubiquitin-conjugating enzyme 2I (UBE2I), the human homolog of S. cerevisiae UBC9, and the small ubiquitin-like modifier-1 (SUMO-1) interact with SALL1 in the yeast two-hybrid system.
289	1014	interact	SALL1	UBE2I	Here, we show that the ubiquitin-conjugating enzyme 2I (UBE2I), the human homolog of S. cerevisiae UBC9, and the small ubiquitin-like modifier-1 (SUMO-1) interact with SALL1 in the yeast two-hybrid system.
289	1015	interact	SUMO-1	SALL1	Here, we show that the ubiquitin-conjugating enzyme 2I (UBE2I), the human homolog of S. cerevisiae UBC9, and the small ubiquitin-like modifier-1 (SUMO-1) interact with SALL1 in the yeast two-hybrid system.
289	1016	interact	UBE2I	SALL1	Here, we show that the ubiquitin-conjugating enzyme 2I (UBE2I), the human homolog of S. cerevisiae UBC9, and the small ubiquitin-like modifier-1 (SUMO-1) interact with SALL1 in the yeast two-hybrid system.
290	1017	interact	S4	ataxin-7	Herein, we show that ataxin-7 interacts with the ATPase subunit S4 of the proteasomal 19S regulatory complex.
290	1018	interact	ataxin-7	S4	Herein, we show that ataxin-7 interacts with the ATPase subunit S4 of the proteasomal 19S regulatory complex.
291	1019	binding	YUH1	ubiquitin	Heteronuclear NMR spectroscopy has been utilized to map the YUH1 binding surface on ubiquitin.
291	1020	binding	ubiquitin	YUH1	Heteronuclear NMR spectroscopy has been utilized to map the YUH1 binding surface on ubiquitin.
292	1021	bind	E6	p53	High-risk mucosal human papillomaviruses encode an E6 oncoprotein, which binds the cellular p53 tumor suppressor protein, thereby marking it for degradation through the ubiquitin-mediated pathway.
292	1022	bind	p53	E6	High-risk mucosal human papillomaviruses encode an E6 oncoprotein, which binds the cellular p53 tumor suppressor protein, thereby marking it for degradation through the ubiquitin-mediated pathway.
293	1023	interact	Apg12p	Apg3p	However, Apg3p itself interacts with free Apg12p more preferentially than the Apg12p.Apg5p conjugate, when free Apg12p exists.
293	1024	interact	Apg3p	Apg12p	However, Apg3p itself interacts with free Apg12p more preferentially than the Apg12p.Apg5p conjugate, when free Apg12p exists.
294	1025	binding	Imp13	eIF1A	However, Imp13 operates differently from typical exportins in that the binding of eIF1A to Imp13 is only regulated indirectly by RanGTP, and the cytoplasmic release of eIF1A from Imp13 is triggered by the loading of import substrates onto Imp13.
294	1026	binding	eIF1A	Imp13	However, Imp13 operates differently from typical exportins in that the binding of eIF1A to Imp13 is only regulated indirectly by RanGTP, and the cytoplasmic release of eIF1A from Imp13 is triggered by the loading of import substrates onto Imp13.
295	1027	interaction	Cullin-1	Rac	However, Rac-Cullin-1 interactions may serve to regulate other E3 ligase functions such as subcellular localization.
295	1028	interaction	Rac	Cullin-1	However, Rac-Cullin-1 interactions may serve to regulate other E3 ligase functions such as subcellular localization.
296	1029	interaction	Cbf3p	Ubc9	However, S. cerevisiae Ubc9p interacts only with the Cbf3p subunit (64 kDa) of the CBF3 complex, indicating the specificity of the interaction between S. cerevisiae Ubc9 and Cbf3p proteins.
296	1030	interact	Cbf3p	Ubc9p	However, S. cerevisiae Ubc9p interacts only with the Cbf3p subunit (64 kDa) of the CBF3 complex, indicating the specificity of the interaction between S. cerevisiae Ubc9 and Cbf3p proteins.
296	1031	interaction	Ubc9	Cbf3p	However, S. cerevisiae Ubc9p interacts only with the Cbf3p subunit (64 kDa) of the CBF3 complex, indicating the specificity of the interaction between S. cerevisiae Ubc9 and Cbf3p proteins.
296	1032	interact	Ubc9p	Cbf3p	However, S. cerevisiae Ubc9p interacts only with the Cbf3p subunit (64 kDa) of the CBF3 complex, indicating the specificity of the interaction between S. cerevisiae Ubc9 and Cbf3p proteins.
297	1033	interaction	Ubc2p	Ubr1p	However, mutations of the BRR domain that strongly decrease the interaction between Ubr1p and Ubc2p do not prevent the degradation of N-end rule substrates.
297	1034	interaction	Ubr1p	Ubc2p	However, mutations of the BRR domain that strongly decrease the interaction between Ubr1p and Ubc2p do not prevent the degradation of N-end rule substrates.
298	1035	modification	DmSmt3	septins	However, we did observe DmSmt3 localization to the midbody during cytokinesis both in tissue-culture cells and in embryonic mitotic domains, suggesting that DmSmt3 modification of septins and/or other midzone proteins occurs during cytokinesis in Drosophila.
298	1036	modification	septins	DmSmt3	However, we did observe DmSmt3 localization to the midbody during cytokinesis both in tissue-culture cells and in embryonic mitotic domains, suggesting that DmSmt3 modification of septins and/or other midzone proteins occurs during cytokinesis in Drosophila.
299	1037	modify	Pdx1	SUMO-1	However, we found that Pdx1 was modified by SUMO-1 (small ubiquitin-related modifier 1) in beta-TC-6 as well as COS-7 cells, which were transfected with Pdx1 cDNA.
299	1038	modify	SUMO-1	Pdx1	However, we found that Pdx1 was modified by SUMO-1 (small ubiquitin-related modifier 1) in beta-TC-6 as well as COS-7 cells, which were transfected with Pdx1 cDNA.
300	1039	associate	beta-TrCP	beta-catenin	However, when plakoglobin was overexpressed, it readily associated with beta-TrCP, efficiently competed with beta-catenin for binding to beta-TrCP and became polyubiquitinated.
300	1040	associate	beta-TrCP	plakoglobin	However, when plakoglobin was overexpressed, it readily associated with beta-TrCP, efficiently competed with beta-catenin for binding to beta-TrCP and became polyubiquitinated.
300	1041	associate	beta-catenin	beta-TrCP	However, when plakoglobin was overexpressed, it readily associated with beta-TrCP, efficiently competed with beta-catenin for binding to beta-TrCP and became polyubiquitinated.
300	1042	associate	plakoglobin	beta-TrCP	However, when plakoglobin was overexpressed, it readily associated with beta-TrCP, efficiently competed with beta-catenin for binding to beta-TrCP and became polyubiquitinated.
301	1043	binds	Cks1	Skp2	Human Cks1, but not other members of the family, reconstitutes ubiquitin ligation of p27 in a completely purified system, binds to Skp2 and greatly increases binding of T187-phosphorylated p27 to Skp2.
301	1044	binds	Skp2	Cks1	Human Cks1, but not other members of the family, reconstitutes ubiquitin ligation of p27 in a completely purified system, binds to Skp2 and greatly increases binding of T187-phosphorylated p27 to Skp2.
301	1045	binding	Skp2	p27	Human Cks1, but not other members of the family, reconstitutes ubiquitin ligation of p27 in a completely purified system, binds to Skp2 and greatly increases binding of T187-phosphorylated p27 to Skp2.
301	1046	binding	p27	Skp2	Human Cks1, but not other members of the family, reconstitutes ubiquitin ligation of p27 in a completely purified system, binds to Skp2 and greatly increases binding of T187-phosphorylated p27 to Skp2.
302	1047	associate	APC	hCDC20	Human orthologs of these proteins (hCDC20/p55CDC and hCDH1) have recently been found to associate with APC in a cell-cycle-dependent manner.
302	1048	associate	APC	hCDH1	Human orthologs of these proteins (hCDC20/p55CDC and hCDH1) have recently been found to associate with APC in a cell-cycle-dependent manner.
302	1049	associate	APC	p55CDC	Human orthologs of these proteins (hCDC20/p55CDC and hCDH1) have recently been found to associate with APC in a cell-cycle-dependent manner.
302	1050	associate	hCDC20	APC	Human orthologs of these proteins (hCDC20/p55CDC and hCDH1) have recently been found to associate with APC in a cell-cycle-dependent manner.
302	1051	associate	hCDH1	APC	Human orthologs of these proteins (hCDC20/p55CDC and hCDH1) have recently been found to associate with APC in a cell-cycle-dependent manner.
302	1052	associate	p55CDC	APC	Human orthologs of these proteins (hCDC20/p55CDC and hCDH1) have recently been found to associate with APC in a cell-cycle-dependent manner.
303	1053	interact	IDE	insulin	IDE is the primary enzyme involved in cellular degradation of insulin, and insulin has been shown to interact with cytosolic IDE.
303	1054	interact	insulin	IDE	IDE is the primary enzyme involved in cellular degradation of insulin, and insulin has been shown to interact with cytosolic IDE.
304	1055	modification	IE1B	SUMO-1	IE1B undergoes further post-translational modification with its conjugation to the small ubiquitin-like modifier (SUMO-1) peptide.
304	1056	modification	SUMO-1	IE1B	IE1B undergoes further post-translational modification with its conjugation to the small ubiquitin-like modifier (SUMO-1) peptide.
305	1057	activation	JNK	RANKL	IFN-gamma induces rapid degradation of the RANK adapter protein, TRAF6 (tumour necrosis factor receptor-associated factor 6), which results in strong inhibition of the RANKL-induced activation of the transcription factor NF-kappaB and JNK.
305	1058	activation	NF-kappaB	RANKL	IFN-gamma induces rapid degradation of the RANK adapter protein, TRAF6 (tumour necrosis factor receptor-associated factor 6), which results in strong inhibition of the RANKL-induced activation of the transcription factor NF-kappaB and JNK.
305	1059	activation	RANKL	JNK	IFN-gamma induces rapid degradation of the RANK adapter protein, TRAF6 (tumour necrosis factor receptor-associated factor 6), which results in strong inhibition of the RANKL-induced activation of the transcription factor NF-kappaB and JNK.
305	1060	activation	RANKL	NF-kappaB	IFN-gamma induces rapid degradation of the RANK adapter protein, TRAF6 (tumour necrosis factor receptor-associated factor 6), which results in strong inhibition of the RANKL-induced activation of the transcription factor NF-kappaB and JNK.
306	1061	activation	ARE	Nrf2	INrf2 tethering of the transcription factor Nrf2 in the cytosol prevents Nrf2 activation of antioxidant response element (ARE) mediated gene expression.
306	1062	activation	Nrf2	ARE	INrf2 tethering of the transcription factor Nrf2 in the cytosol prevents Nrf2 activation of antioxidant response element (ARE) mediated gene expression.
307	1063	phosphorylate	IKK	IkappaBs	IkappaB kinase (IKK) phosphorylates inhibitors of NF-kappaB (IkappaBs).
307	1064	phosphorylate	IkappaBs	IKK	IkappaB kinase (IKK) phosphorylates inhibitors of NF-kappaB (IkappaBs).
308	1065	phosphorylation	IkappaB kinase	p105	IkappaB kinase-mediated phosphorylation of the C-terminal domain of p105 recruits the SCF(beta-TrCP) ubiquitin ligase, resulting in rapid ubiquitination and subsequent processing/degradation of p105.
308	1066	phosphorylation	p105	IkappaB kinase	IkappaB kinase-mediated phosphorylation of the C-terminal domain of p105 recruits the SCF(beta-TrCP) ubiquitin ligase, resulting in rapid ubiquitination and subsequent processing/degradation of p105.
309	1067	binding	NF-kappaB	p65	IkappaB-alpha and the p65 binding subunit of NF-kappaB were detected by Western blots.
309	1068	binding	p65	NF-kappaB	IkappaB-alpha and the p65 binding subunit of NF-kappaB were detected by Western blots.
310	1069	bound	IkappaBalpha-E3	pIkappaBalpha	IkappaBalpha-E3 bound to pIkappaBalpha catalyzed in vitro ubiquitination of pIkappaBalpha in the presence of ATP, Ub, and E1-activating and E2-conjugating enzymes.
310	1070	bound	pIkappaBalpha	IkappaBalpha-E3	IkappaBalpha-E3 bound to pIkappaBalpha catalyzed in vitro ubiquitination of pIkappaBalpha in the presence of ATP, Ub, and E1-activating and E2-conjugating enzymes.
311	1071	bind	MDM2	p53	Immediately after the application of cellular stress, the ability of MDM2 to bind to p53 is blocked or altered in a fashion that prevents MDM2-mediated degradation.
311	1072	bind	p53	MDM2	Immediately after the application of cellular stress, the ability of MDM2 to bind to p53 is blocked or altered in a fashion that prevents MDM2-mediated degradation.
312	1073	conjugate	SUMO-1	topoisomerase IIalpha	Immunological characterization of these conjugates suggests that both topoisomerase IIalpha and IIbeta isozymes are conjugated to SUMO-1.
312	1074	conjugate	SUMO-1	topoisomerase IIbeta	Immunological characterization of these conjugates suggests that both topoisomerase IIalpha and IIbeta isozymes are conjugated to SUMO-1.
312	1075	conjugate	topoisomerase IIalpha	SUMO-1	Immunological characterization of these conjugates suggests that both topoisomerase IIalpha and IIbeta isozymes are conjugated to SUMO-1.
312	1076	conjugate	topoisomerase IIbeta	SUMO-1	Immunological characterization of these conjugates suggests that both topoisomerase IIalpha and IIbeta isozymes are conjugated to SUMO-1.
313	1077	interaction	HIF-alpha	pVHL	Importantly, the classical features of regulation by iron and oxygen availability are reflected in regulation of the HIF-alpha/pVHL interaction.
313	1078	interaction	pVHL	HIF-alpha	Importantly, the classical features of regulation by iron and oxygen availability are reflected in regulation of the HIF-alpha/pVHL interaction.
314	1079	interact	Importin-11	RanGTPase	Importin-11 interacts with the RanGTPase, and constitutively shuttles between the nuclear and cytoplasmic compartments.
314	1080	interact	RanGTPase	Importin-11	Importin-11 interacts with the RanGTPase, and constitutively shuttles between the nuclear and cytoplasmic compartments.
315	1081	interact	Mms2	ubiquitin	In (1)H (15)N HSQC ((1)H (15)N heteronuclear single quantum coherence) NMR experiments, we have mapped the surface determinants of tethered and untethered ubiquitin that interact with Mms2 and Ubc13 in both their monomeric and dimeric forms.
315	1082	interact	Ubc13	ubiquitin	In (1)H (15)N HSQC ((1)H (15)N heteronuclear single quantum coherence) NMR experiments, we have mapped the surface determinants of tethered and untethered ubiquitin that interact with Mms2 and Ubc13 in both their monomeric and dimeric forms.
315	1083	interact	ubiquitin	Mms2	In (1)H (15)N HSQC ((1)H (15)N heteronuclear single quantum coherence) NMR experiments, we have mapped the surface determinants of tethered and untethered ubiquitin that interact with Mms2 and Ubc13 in both their monomeric and dimeric forms.
315	1084	interact	ubiquitin	Ubc13	In (1)H (15)N HSQC ((1)H (15)N heteronuclear single quantum coherence) NMR experiments, we have mapped the surface determinants of tethered and untethered ubiquitin that interact with Mms2 and Ubc13 in both their monomeric and dimeric forms.
316	1085	interact	APC/C	srw1	In G(1), when cdc2-cyclin kinase activity is low, unphosphorylated ste9/srw1 interacts with APC/C.
316	1086	interact	APC/C	ste9	In G(1), when cdc2-cyclin kinase activity is low, unphosphorylated ste9/srw1 interacts with APC/C.
316	1087	interact	srw1	APC/C	In G(1), when cdc2-cyclin kinase activity is low, unphosphorylated ste9/srw1 interacts with APC/C.
316	1088	interact	ste9	APC/C	In G(1), when cdc2-cyclin kinase activity is low, unphosphorylated ste9/srw1 interacts with APC/C.
317	1089	bind	UIP5	UbcM4	In addition to UbcM4, several other ubiquitin-conjugating enzymes (E2s) that share the same sequence within the L1 loop bind to UIP5.
317	1090	bind	UbcM4	UIP5	In addition to UbcM4, several other ubiquitin-conjugating enzymes (E2s) that share the same sequence within the L1 loop bind to UIP5.
318	1091	modification	CUL1	RUB	In addition to its direct role in SCF E3 ligase activity, RBX1 promotes the RUB modification of CUL1 and probably functions as an E3 ligase in the RUB pathway.
318	1092	modification	RUB	CUL1	In addition to its direct role in SCF E3 ligase activity, RBX1 promotes the RUB modification of CUL1 and probably functions as an E3 ligase in the RUB pathway.
319	1093	associate	Cac3p	Npr1p	In addition, Cac3p associates with Npr1p, a cytoplasmic kinase that stablizes several nutrient transporters by antagonizing a ubiquitin-mediated protein degradation pathway.
319	1094	associate	Npr1p	Cac3p	In addition, Cac3p associates with Npr1p, a cytoplasmic kinase that stablizes several nutrient transporters by antagonizing a ubiquitin-mediated protein degradation pathway.
320	1095	bound	PIAS1	Ubc9	In addition, PIAS1 bound p53 and Ubc9, the E2 for SUMO.
320	1096	bound	PIAS1	p53	In addition, PIAS1 bound p53 and Ubc9, the E2 for SUMO.
320	1097	bound	Ubc9	PIAS1	In addition, PIAS1 bound p53 and Ubc9, the E2 for SUMO.
320	1098	bound	p53	PIAS1	In addition, PIAS1 bound p53 and Ubc9, the E2 for SUMO.
321	1099	ubiquitinate	APC	Pds1p	In addition, Pds1p is directly ubiquitinated by the Xenopus APC.
321	1100	ubiquitinate	Pds1p	APC	In addition, Pds1p is directly ubiquitinated by the Xenopus APC.
322	1101	modification	PML	SUMO-1	In addition, SUMO-1 modification of PML is required for sequestration of Daxx to the PODs and for efficient inhibition of Daxx-mediated transcriptional repression.
322	1102	modification	SUMO-1	PML	In addition, SUMO-1 modification of PML is required for sequestration of Daxx to the PODs and for efficient inhibition of Daxx-mediated transcriptional repression.
323	1103	associate	Smurf1	TbetaR-I	In addition, Smurf1 associates with TbetaR-I via Smad7, with subsequent enhancement of turnover of TbetaR-I and Smad7.
323	1104	associate	TbetaR-I	Smurf1	In addition, Smurf1 associates with TbetaR-I via Smad7, with subsequent enhancement of turnover of TbetaR-I and Smad7.
324	1105	binding	E6-AP	p53	In addition, highly ubiquitinated forms of E6-AP cannot bind to p53 in the presence of the E6 oncoprotein and, conversely, binding of E6-AP to p53 interferes with ubiquitination of E6-AP.
324	1106	binding	p53	E6-AP	In addition, highly ubiquitinated forms of E6-AP cannot bind to p53 in the presence of the E6 oncoprotein and, conversely, binding of E6-AP to p53 interferes with ubiquitination of E6-AP.
325	1107	interact	IRS-2	SOCS-6	In addition, these SH2 domains interacted with a protein complex consisting of insulin receptor substrate 4 (IRS-4), IRS-2, and the p85 regulatory subunit of phosphatidylinositol 3-kinase.
325	1108	interact	IRS-4	SOCS-6	In addition, these SH2 domains interacted with a protein complex consisting of insulin receptor substrate 4 (IRS-4), IRS-2, and the p85 regulatory subunit of phosphatidylinositol 3-kinase.
325	1109	interact	SOCS-6	IRS-2	In addition, these SH2 domains interacted with a protein complex consisting of insulin receptor substrate 4 (IRS-4), IRS-2, and the p85 regulatory subunit of phosphatidylinositol 3-kinase.
325	1110	interact	SOCS-6	IRS-4	In addition, these SH2 domains interacted with a protein complex consisting of insulin receptor substrate 4 (IRS-4), IRS-2, and the p85 regulatory subunit of phosphatidylinositol 3-kinase.
325	1111	interact	SOCS-6	p85	In addition, these SH2 domains interacted with a protein complex consisting of insulin receptor substrate 4 (IRS-4), IRS-2, and the p85 regulatory subunit of phosphatidylinositol 3-kinase.
325	1112	interact	p85	SOCS-6	In addition, these SH2 domains interacted with a protein complex consisting of insulin receptor substrate 4 (IRS-4), IRS-2, and the p85 regulatory subunit of phosphatidylinositol 3-kinase.
326	1113	interaction	S4	S7	In addition, we provide genetic evidence for a physical interaction between the S4 and the related S7 subunit in the 26S multiprotein protease.
326	1114	interaction	S7	S4	In addition, we provide genetic evidence for a physical interaction between the S4 and the related S7 subunit in the 26S multiprotein protease.
327	1115	interact	NbSGT1	NbSKP1	In addition, we show that NbSGT1 interacts with NbSKP1.
327	1116	interact	NbSKP1	NbSGT1	In addition, we show that NbSGT1 interacts with NbSKP1.
328	1117	modified	SALL1	SUMO-1	In an in vitro assay, it could be demonstrated that SALL1 is covalently modified by at least two SUMO-1 molecules in the presence of UBA2/AOS1 and UBE2I.
328	1118	modified	SUMO-1	SALL1	In an in vitro assay, it could be demonstrated that SALL1 is covalently modified by at least two SUMO-1 molecules in the presence of UBA2/AOS1 and UBE2I.
329	1119	polyubiquitinate	alphaSp22	parkin	In an in vitro ubiquitination assay, alphaSp22 was modified by normal but not mutant parkin into polyubiquitinated, high molecular weight species.
329	1120	polyubiquitinate	parkin	alphaSp22	In an in vitro ubiquitination assay, alphaSp22 was modified by normal but not mutant parkin into polyubiquitinated, high molecular weight species.
330	1121	activated	Cdc28	Cln1	In budding yeast, cell division is initiated in late G1 phase once the Cdc28 cyclin-dependent kinase is activated by the G1 cyclins Cln1, Cln2, and Cln3.
330	1122	activated	Cdc28	Cln2	In budding yeast, cell division is initiated in late G1 phase once the Cdc28 cyclin-dependent kinase is activated by the G1 cyclins Cln1, Cln2, and Cln3.
330	1123	activated	Cdc28	Cln3	In budding yeast, cell division is initiated in late G1 phase once the Cdc28 cyclin-dependent kinase is activated by the G1 cyclins Cln1, Cln2, and Cln3.
330	1124	activated	Cln1	Cdc28	In budding yeast, cell division is initiated in late G1 phase once the Cdc28 cyclin-dependent kinase is activated by the G1 cyclins Cln1, Cln2, and Cln3.
330	1125	activated	Cln2	Cdc28	In budding yeast, cell division is initiated in late G1 phase once the Cdc28 cyclin-dependent kinase is activated by the G1 cyclins Cln1, Cln2, and Cln3.
330	1126	activated	Cln3	Cdc28	In budding yeast, cell division is initiated in late G1 phase once the Cdc28 cyclin-dependent kinase is activated by the G1 cyclins Cln1, Cln2, and Cln3.
331	1127	complex	Cdc4	Cdc53	In budding yeast, ubiquitination of the cyclin-dependent kinase (Cdk) inhibitor Sic1 is catalyzed by the E2 ubiquitin conjugating enzyme Cdc34 in conjunction with an E3 ubiquitin ligase complex composed of Skp1, Cdc53 and the F-box protein, Cdc4 (the SCFCdc4 complex).
331	1128	complex	Cdc4	Skp1	In budding yeast, ubiquitination of the cyclin-dependent kinase (Cdk) inhibitor Sic1 is catalyzed by the E2 ubiquitin conjugating enzyme Cdc34 in conjunction with an E3 ubiquitin ligase complex composed of Skp1, Cdc53 and the F-box protein, Cdc4 (the SCFCdc4 complex).
331	1129	complex	Cdc53	Cdc4	In budding yeast, ubiquitination of the cyclin-dependent kinase (Cdk) inhibitor Sic1 is catalyzed by the E2 ubiquitin conjugating enzyme Cdc34 in conjunction with an E3 ubiquitin ligase complex composed of Skp1, Cdc53 and the F-box protein, Cdc4 (the SCFCdc4 complex).
331	1130	complex	Cdc53	Skp1	In budding yeast, ubiquitination of the cyclin-dependent kinase (Cdk) inhibitor Sic1 is catalyzed by the E2 ubiquitin conjugating enzyme Cdc34 in conjunction with an E3 ubiquitin ligase complex composed of Skp1, Cdc53 and the F-box protein, Cdc4 (the SCFCdc4 complex).
331	1131	complex	Skp1	Cdc4	In budding yeast, ubiquitination of the cyclin-dependent kinase (Cdk) inhibitor Sic1 is catalyzed by the E2 ubiquitin conjugating enzyme Cdc34 in conjunction with an E3 ubiquitin ligase complex composed of Skp1, Cdc53 and the F-box protein, Cdc4 (the SCFCdc4 complex).
331	1132	complex	Skp1	Cdc53	In budding yeast, ubiquitination of the cyclin-dependent kinase (Cdk) inhibitor Sic1 is catalyzed by the E2 ubiquitin conjugating enzyme Cdc34 in conjunction with an E3 ubiquitin ligase complex composed of Skp1, Cdc53 and the F-box protein, Cdc4 (the SCFCdc4 complex).
332	1133	ubiquitinate	ErbB3	Nrdp1	In cell-free systems, Nrdp1 has ubiquitin ligase (E3) activity and ubiquitinates ErbB3, as well as itself, in the presence of the ubiquitin-carrier protein (E2), UbcH5.
332	1134	ubiquitinate	Nrdp1	ErbB3	In cell-free systems, Nrdp1 has ubiquitin ligase (E3) activity and ubiquitinates ErbB3, as well as itself, in the presence of the ubiquitin-carrier protein (E2), UbcH5.
333	1135	binding	ND10	Sp100	In cells induced to overexpress Sp100, ND10 binding of Sp100 was saturable and excess Sp100 formed new aggregation sites devoid of other ND10-associated proteins, suggesting that homo-oligomerization is the basis for aggregation.
333	1136	binding	Sp100	ND10	In cells induced to overexpress Sp100, ND10 binding of Sp100 was saturable and excess Sp100 formed new aggregation sites devoid of other ND10-associated proteins, suggesting that homo-oligomerization is the basis for aggregation.
334	1137	interaction	52Ro	UnpEL	In conclusion, the interaction of full-length 52Ro and UnpEL implies that the former may also be involved in the ubiquitin pathway, an observation of particular interest since 52Ro contains a RING finger domain, a motif common to several recently reported proteins involved in modulating ubiquitination.
334	1138	interaction	UnpEL	52Ro	In conclusion, the interaction of full-length 52Ro and UnpEL implies that the former may also be involved in the ubiquitin pathway, an observation of particular interest since 52Ro contains a RING finger domain, a motif common to several recently reported proteins involved in modulating ubiquitination.
335	1139	interact	CED-3	ceBNIP3	In conclusion, we find that although ceBNIP3 interacts with CED-9 and CED-3 it kills by a BH3- and caspase-independent mechanism.
335	1140	interact	CED-9	ceBNIP3	In conclusion, we find that although ceBNIP3 interacts with CED-9 and CED-3 it kills by a BH3- and caspase-independent mechanism.
335	1141	interact	ceBNIP3	CED-3	In conclusion, we find that although ceBNIP3 interacts with CED-9 and CED-3 it kills by a BH3- and caspase-independent mechanism.
335	1142	interact	ceBNIP3	CED-9	In conclusion, we find that although ceBNIP3 interacts with CED-9 and CED-3 it kills by a BH3- and caspase-independent mechanism.
336	1143	transfer	histone	ubiquitin	In contrast to E2 preparations obtained from rabbit reticulocytes and erythrocytes or Saccharomyces cerevisiae, the placental E2 preparation lacks E2(Mr = 14,000) and E2(Mr = 20,000) which are both unique in catalysing the ligase-independent transfer of ubiquitin to histones.
336	1144	transfer	ubiquitin	histone	In contrast to E2 preparations obtained from rabbit reticulocytes and erythrocytes or Saccharomyces cerevisiae, the placental E2 preparation lacks E2(Mr = 14,000) and E2(Mr = 20,000) which are both unique in catalysing the ligase-independent transfer of ubiquitin to histones.
337	1145	interaction	dac	eya	In contrast to a direct interaction between Drosophila dachshund (dac) and eyes absent (eya)gene products, we cannot detect by the same methods that mDac binds to mEya2, a functional mouse homologue of the Drosophila Eya.
337	1146	interaction	eya	dac	In contrast to a direct interaction between Drosophila dachshund (dac) and eyes absent (eya)gene products, we cannot detect by the same methods that mDac binds to mEya2, a functional mouse homologue of the Drosophila Eya.
338	1147	activate	IFN-beta	p42/44 MAPK	In contrast with the JAK-STAT signalling pathway, acute ethanol exposure significantly potentiated IFN-beta or IFN-gamma-induced activation of p42/44 MAPK, and caused marked activation of protein kinase C (PKC).
338	1148	activate	IFN-gamma	p42/44 MAPK	In contrast with the JAK-STAT signalling pathway, acute ethanol exposure significantly potentiated IFN-beta or IFN-gamma-induced activation of p42/44 MAPK, and caused marked activation of protein kinase C (PKC).
338	1149	activate	p42/44 MAPK	IFN-beta	In contrast with the JAK-STAT signalling pathway, acute ethanol exposure significantly potentiated IFN-beta or IFN-gamma-induced activation of p42/44 MAPK, and caused marked activation of protein kinase C (PKC).
338	1150	activate	p42/44 MAPK	IFN-gamma	In contrast with the JAK-STAT signalling pathway, acute ethanol exposure significantly potentiated IFN-beta or IFN-gamma-induced activation of p42/44 MAPK, and caused marked activation of protein kinase C (PKC).
339	1151	bound	ENaC	Nedd4-2	In contrast, all four human Nedd4-2 WW domains bound to ENaC.
339	1152	bound	Nedd4-2	ENaC	In contrast, all four human Nedd4-2 WW domains bound to ENaC.
340	1153	bound	Mdm2	p53	In contrast, recombinant p53 bound strongly to the Mdm2 binding site in the absence of PAb421 antibody.
340	1154	bound	p53	Mdm2	In contrast, recombinant p53 bound strongly to the Mdm2 binding site in the absence of PAb421 antibody.
341	1155	interact	CUL1	ROC1	In contrast, the C terminus of CUL1 alone interacts with ROC1 through a region containing the cullin consensus domain, to form a complex fully active in supporting ubiquitin polymerization.
341	1156	interact	ROC1	CUL1	In contrast, the C terminus of CUL1 alone interacts with ROC1 through a region containing the cullin consensus domain, to form a complex fully active in supporting ubiquitin polymerization.
342	1157	interaction	Elongin B	VHL	In contrast, the VHL protein is stabilized by interaction with the Elongin B and C subunits of CBC(VHL) in cells.
342	1158	interaction	Elongin C	VHL	In contrast, the VHL protein is stabilized by interaction with the Elongin B and C subunits of CBC(VHL) in cells.
342	1159	interaction	VHL	Elongin B	In contrast, the VHL protein is stabilized by interaction with the Elongin B and C subunits of CBC(VHL) in cells.
342	1160	interaction	VHL	Elongin C	In contrast, the VHL protein is stabilized by interaction with the Elongin B and C subunits of CBC(VHL) in cells.
343	1161	binding	E6	p53	In contrast, we found E6AP-independent binding of HPV16 E6 and HPV6 E6 to p53, although both proteins were different in their transforming potential.
343	1162	binding	p53	E6	In contrast, we found E6AP-independent binding of HPV16 E6 and HPV6 E6 to p53, although both proteins were different in their transforming potential.
344	1163	interaction	HIF-alpha	pVHL	In contrast, while full-length pVHL and the p19 variant interact with HIF-alpha, the association was abrogated by further N-terminal and C-terminal truncations.
344	1164	interaction	pVHL	HIF-alpha	In contrast, while full-length pVHL and the p19 variant interact with HIF-alpha, the association was abrogated by further N-terminal and C-terminal truncations.
345	1165	modified	HIPK2	SUMO-1	In cultured cells, HIPK2 is covalently modified by SUMO-1, and the SUMO-1 modification of HIPK2 correlates with its localization to nuclear speckles (dots).
345	1166	modified	SUMO-1	HIPK2	In cultured cells, HIPK2 is covalently modified by SUMO-1, and the SUMO-1 modification of HIPK2 correlates with its localization to nuclear speckles (dots).
346	1167	phosphorylate	Cdk1	p27	In fact, cyclin B/Cdk1 which can phosphorylate p27 efficiently, but cannot form a stable complex with it, is unable to stimulate p27 ubiquitination by G1 extracts.
346	1168	phosphorylate	cyclin B	p27	In fact, cyclin B/Cdk1 which can phosphorylate p27 efficiently, but cannot form a stable complex with it, is unable to stimulate p27 ubiquitination by G1 extracts.
346	1169	phosphorylate	p27	Cdk1	In fact, cyclin B/Cdk1 which can phosphorylate p27 efficiently, but cannot form a stable complex with it, is unable to stimulate p27 ubiquitination by G1 extracts.
346	1170	phosphorylate	p27	cyclin B	In fact, cyclin B/Cdk1 which can phosphorylate p27 efficiently, but cannot form a stable complex with it, is unable to stimulate p27 ubiquitination by G1 extracts.
347	1171	bound	Cullin-1	V12Rac3	In mammalian cell lysates, Cullin-1 bound to V12Rac3, effector domain mutants V12L37Rac3 and V12H40Rac3, and insert domain deletion mutant V12Rac3DeltaIns(124-135).
347	1172	bound	V12Rac3	Cullin-1	In mammalian cell lysates, Cullin-1 bound to V12Rac3, effector domain mutants V12L37Rac3 and V12H40Rac3, and insert domain deletion mutant V12Rac3DeltaIns(124-135).
348	1173	complex	CDK2	SKP1	In normal and transformed cells, the F-box protein p45(SKP2) is required for S phase and forms stable complexes with p19(SKP1) and cyclin A-cyclin-dependent kinase (CDK)2.
348	1174	complex	CDK2	SKP2	In normal and transformed cells, the F-box protein p45(SKP2) is required for S phase and forms stable complexes with p19(SKP1) and cyclin A-cyclin-dependent kinase (CDK)2.
348	1175	complex	CDK2	p19	In normal and transformed cells, the F-box protein p45(SKP2) is required for S phase and forms stable complexes with p19(SKP1) and cyclin A-cyclin-dependent kinase (CDK)2.
348	1176	complex	CDK2	p45	In normal and transformed cells, the F-box protein p45(SKP2) is required for S phase and forms stable complexes with p19(SKP1) and cyclin A-cyclin-dependent kinase (CDK)2.
348	1177	complex	SKP1	CDK2	In normal and transformed cells, the F-box protein p45(SKP2) is required for S phase and forms stable complexes with p19(SKP1) and cyclin A-cyclin-dependent kinase (CDK)2.
348	1178	complex	SKP1	SKP2	In normal and transformed cells, the F-box protein p45(SKP2) is required for S phase and forms stable complexes with p19(SKP1) and cyclin A-cyclin-dependent kinase (CDK)2.
348	1179	complex	SKP1	p45	In normal and transformed cells, the F-box protein p45(SKP2) is required for S phase and forms stable complexes with p19(SKP1) and cyclin A-cyclin-dependent kinase (CDK)2.
348	1180	complex	SKP2	CDK2	In normal and transformed cells, the F-box protein p45(SKP2) is required for S phase and forms stable complexes with p19(SKP1) and cyclin A-cyclin-dependent kinase (CDK)2.
348	1181	complex	SKP2	SKP1	In normal and transformed cells, the F-box protein p45(SKP2) is required for S phase and forms stable complexes with p19(SKP1) and cyclin A-cyclin-dependent kinase (CDK)2.
348	1182	complex	SKP2	p19	In normal and transformed cells, the F-box protein p45(SKP2) is required for S phase and forms stable complexes with p19(SKP1) and cyclin A-cyclin-dependent kinase (CDK)2.
348	1183	complex	p19	CDK2	In normal and transformed cells, the F-box protein p45(SKP2) is required for S phase and forms stable complexes with p19(SKP1) and cyclin A-cyclin-dependent kinase (CDK)2.
348	1184	complex	p19	SKP2	In normal and transformed cells, the F-box protein p45(SKP2) is required for S phase and forms stable complexes with p19(SKP1) and cyclin A-cyclin-dependent kinase (CDK)2.
348	1185	complex	p19	p45	In normal and transformed cells, the F-box protein p45(SKP2) is required for S phase and forms stable complexes with p19(SKP1) and cyclin A-cyclin-dependent kinase (CDK)2.
348	1186	complex	p45	CDK2	In normal and transformed cells, the F-box protein p45(SKP2) is required for S phase and forms stable complexes with p19(SKP1) and cyclin A-cyclin-dependent kinase (CDK)2.
348	1187	complex	p45	SKP1	In normal and transformed cells, the F-box protein p45(SKP2) is required for S phase and forms stable complexes with p19(SKP1) and cyclin A-cyclin-dependent kinase (CDK)2.
348	1188	complex	p45	p19	In normal and transformed cells, the F-box protein p45(SKP2) is required for S phase and forms stable complexes with p19(SKP1) and cyclin A-cyclin-dependent kinase (CDK)2.
349	1189	bind	MDM2	p53	In normal cells the MDM2 protein binds to the p53 protein and maintains p53 at low levels by increasing its susceptibility to proteolysis by the 26S proteosome.
349	1190	bind	p53	MDM2	In normal cells the MDM2 protein binds to the p53 protein and maintains p53 at low levels by increasing its susceptibility to proteolysis by the 26S proteosome.
350	1191	associate	CRK	CYC3	In order to examine whether CYC3 associates in vivo with a trypanosome cdc2-related kinase (CRK), the CYC3 gene was fused with the TY-epitope tag, integrated into the trypanosome genome and expressed under inducible control.
350	1192	associate	CYC3	CRK	In order to examine whether CYC3 associates in vivo with a trypanosome cdc2-related kinase (CRK), the CYC3 gene was fused with the TY-epitope tag, integrated into the trypanosome genome and expressed under inducible control.
351	1193	modification	SUMO1	septin	In our previous report, we showed that Siz1/Ull1 (YDR409w) of budding yeast, a member of the human PIAS family containing a RING-like domain, is a strong candidate for SUMO1/Smt3 ligase because the SUMO1/Smt3 modification of septin components was abolished in the ull1 mutant and Ull1 associated with E2 (Ubc9) and the substrates (septin components) in immunoprecipitation experiments.
351	1194	modification	Smt3	septin	In our previous report, we showed that Siz1/Ull1 (YDR409w) of budding yeast, a member of the human PIAS family containing a RING-like domain, is a strong candidate for SUMO1/Smt3 ligase because the SUMO1/Smt3 modification of septin components was abolished in the ull1 mutant and Ull1 associated with E2 (Ubc9) and the substrates (septin components) in immunoprecipitation experiments.
351	1195	modification	septin	SUMO1	In our previous report, we showed that Siz1/Ull1 (YDR409w) of budding yeast, a member of the human PIAS family containing a RING-like domain, is a strong candidate for SUMO1/Smt3 ligase because the SUMO1/Smt3 modification of septin components was abolished in the ull1 mutant and Ull1 associated with E2 (Ubc9) and the substrates (septin components) in immunoprecipitation experiments.
351	1196	modification	septin	Smt3	In our previous report, we showed that Siz1/Ull1 (YDR409w) of budding yeast, a member of the human PIAS family containing a RING-like domain, is a strong candidate for SUMO1/Smt3 ligase because the SUMO1/Smt3 modification of septin components was abolished in the ull1 mutant and Ull1 associated with E2 (Ubc9) and the substrates (septin components) in immunoprecipitation experiments.
352	1197	bind	HIF-1alpha	VHL	In particular, the von Hippel-Lindau (VHL) protein complex, an E3 ubiquitin ligase, binds to the ODD upon hydroxylation of HIF-1alpha Pro-564.
352	1198	bind	VHL	HIF-1alpha	In particular, the von Hippel-Lindau (VHL) protein complex, an E3 ubiquitin ligase, binds to the ODD upon hydroxylation of HIF-1alpha Pro-564.
353	1199	modified	CREB	SUMO-1	In prolonged hypoxia, CREB is posttranslationally modified by SUMO-1.
353	1200	modified	SUMO-1	CREB	In prolonged hypoxia, CREB is posttranslationally modified by SUMO-1.
354	1201	inhibits	Cdc20-APC	Mad2	In response to activation of the checkpoint, Mad2 binds to and inhibits Cdc20-APC.
354	1202	inhibits	Mad2	Cdc20-APC	In response to activation of the checkpoint, Mad2 binds to and inhibits Cdc20-APC.
355	1203	interaction	Axin	beta-TRCP	In spite of the fact that CKIepsilon was found as a positive regulator of the Wnt pathway, mutational analysis suggests that mutation of Ser-45 regulates beta-catenin stability by inhibiting the ability of GSK3 to phosphorylate Ser-33 and -37, thereby disrupting the interaction between beta-catenin, beta-TRCP and Axin.
355	1204	interaction	Axin	beta-catenin	In spite of the fact that CKIepsilon was found as a positive regulator of the Wnt pathway, mutational analysis suggests that mutation of Ser-45 regulates beta-catenin stability by inhibiting the ability of GSK3 to phosphorylate Ser-33 and -37, thereby disrupting the interaction between beta-catenin, beta-TRCP and Axin.
355	1205	interaction	beta-TRCP	Axin	In spite of the fact that CKIepsilon was found as a positive regulator of the Wnt pathway, mutational analysis suggests that mutation of Ser-45 regulates beta-catenin stability by inhibiting the ability of GSK3 to phosphorylate Ser-33 and -37, thereby disrupting the interaction between beta-catenin, beta-TRCP and Axin.
355	1206	interaction	beta-TRCP	beta-catenin	In spite of the fact that CKIepsilon was found as a positive regulator of the Wnt pathway, mutational analysis suggests that mutation of Ser-45 regulates beta-catenin stability by inhibiting the ability of GSK3 to phosphorylate Ser-33 and -37, thereby disrupting the interaction between beta-catenin, beta-TRCP and Axin.
355	1207	interaction	beta-catenin	Axin	In spite of the fact that CKIepsilon was found as a positive regulator of the Wnt pathway, mutational analysis suggests that mutation of Ser-45 regulates beta-catenin stability by inhibiting the ability of GSK3 to phosphorylate Ser-33 and -37, thereby disrupting the interaction between beta-catenin, beta-TRCP and Axin.
355	1208	interaction	beta-catenin	beta-TRCP	In spite of the fact that CKIepsilon was found as a positive regulator of the Wnt pathway, mutational analysis suggests that mutation of Ser-45 regulates beta-catenin stability by inhibiting the ability of GSK3 to phosphorylate Ser-33 and -37, thereby disrupting the interaction between beta-catenin, beta-TRCP and Axin.
356	1209	conjugate	PTHrP	ubiquitin	In studying the post-translational regulation of PTHrP, we observed that PTHrP was conjugated to multiple ubiquitin moieties.
356	1210	conjugate	ubiquitin	PTHrP	In studying the post-translational regulation of PTHrP, we observed that PTHrP was conjugated to multiple ubiquitin moieties.
357	1211	phosphorylate	c-Abl	gamma-PAK	In summary, we describe a functional interaction between gamma-PAK and c-Abl in which gamma-PAK stimulates c-Abl tyrosine kinase activity and c-Abl phosphorylates and down-regulates gamma-PAK, suggesting the existence of a negative feedback loop between c-Abl and gamma-PAK.
357	1212	phosphorylate	gamma-PAK	c-Abl	In summary, we describe a functional interaction between gamma-PAK and c-Abl in which gamma-PAK stimulates c-Abl tyrosine kinase activity and c-Abl phosphorylates and down-regulates gamma-PAK, suggesting the existence of a negative feedback loop between c-Abl and gamma-PAK.
358	1213	binding	APC	Cdc20	In the absence of Mad2, BubR1 inhibits the activity of APC by blocking the binding of Cdc20 to APC.
358	1214	inhibit	BubR1	Cdc20	In the absence of Mad2, BubR1 inhibits the activity of APC by blocking the binding of Cdc20 to APC.
358	1215	binding	Cdc20	APC	In the absence of Mad2, BubR1 inhibits the activity of APC by blocking the binding of Cdc20 to APC.
358	1216	inhibit	Cdc20	BubR1	In the absence of Mad2, BubR1 inhibits the activity of APC by blocking the binding of Cdc20 to APC.
359	1217	interact	IkappaB-alpha	NF-kappaB	In the best characterized example, IkappaB-alpha interacts with a p50/RelA (NF-kappaB) heterodimer to retain the complex in the cytoplasm and inhibit its DNA-binding activity.
359	1218	interact	NF-kappaB	IkappaB-alpha	In the best characterized example, IkappaB-alpha interacts with a p50/RelA (NF-kappaB) heterodimer to retain the complex in the cytoplasm and inhibit its DNA-binding activity.
360	1219	binding	MDM2	p53	In the current study, we examined whether the MDM2 binding domain of p53 could be provided in trans through oligomerization between two p53 molecules.
360	1220	binding	p53	MDM2	In the current study, we examined whether the MDM2 binding domain of p53 could be provided in trans through oligomerization between two p53 molecules.
361	1221	conjugation	histone	ubiquitin	In the nucleus ubiquitin is conjugated to histone 2A to form the nuclear protein A24 which may play a role in regulation of chromatin structure, and in the cytoplasm is part of an ATP-dependent non-lysosomal proteolytic pathway.
361	1222	conjugation	ubiquitin	histone	In the nucleus ubiquitin is conjugated to histone 2A to form the nuclear protein A24 which may play a role in regulation of chromatin structure, and in the cytoplasm is part of an ATP-dependent non-lysosomal proteolytic pathway.
362	1223	interact	A1Up	ataxin-1	In the nucleus, A1Up co-localized with mutant ataxin-1, further demonstrating that A1Up interacts with ataxin-1.
362	1224	interact	ataxin-1	A1Up	In the nucleus, A1Up co-localized with mutant ataxin-1, further demonstrating that A1Up interacts with ataxin-1.
363	1225	conjugate	histone 2A	ubiquitin	In the nucleus, ubiquitin is conjugated to histone 2A and may play a role in regulation of chromatin structure and/or regulation of transcriptional activity.
363	1226	conjugate	ubiquitin	histone 2A	In the nucleus, ubiquitin is conjugated to histone 2A and may play a role in regulation of chromatin structure and/or regulation of transcriptional activity.
364	1227	interaction	MuV-V	STAT-1	In the presence of MG132, ubiquitination of STAT-1 and the interaction of MuV-V with STAT-1 were demonstrated in FLMT cells by immunoprecipitation with anti-STAT-1 antibody.
364	1228	interaction	STAT-1	MuV-V	In the presence of MG132, ubiquitination of STAT-1 and the interaction of MuV-V with STAT-1 were demonstrated in FLMT cells by immunoprecipitation with anti-STAT-1 antibody.
365	1229	conjugate	IkappaBalpha	SUMO-1	In the presence of SAE1/SAE2, Ubch9, and ATP, SUMO-1 was efficiently conjugated to the protein substrate IkappaBalpha.
365	1230	conjugate	SUMO-1	IkappaBalpha	In the presence of SAE1/SAE2, Ubch9, and ATP, SUMO-1 was efficiently conjugated to the protein substrate IkappaBalpha.
366	1231	conjugate	IkappaBalpha	SUMO-1	In the presence of an E1 SUMO-1-activating enzyme, Ubch9 conjugated SUMO-1 to IkappaBalpha primarily on K21, which is also utilized for ubiquitin modification.
366	1232	conjugated	IkappaBalpha	Ubch9	In the presence of an E1 SUMO-1-activating enzyme, Ubch9 conjugated SUMO-1 to IkappaBalpha primarily on K21, which is also utilized for ubiquitin modification.
366	1233	conjugate	SUMO-1	IkappaBalpha	In the presence of an E1 SUMO-1-activating enzyme, Ubch9 conjugated SUMO-1 to IkappaBalpha primarily on K21, which is also utilized for ubiquitin modification.
366	1234	conjugated	SUMO-1	Ubch9	In the presence of an E1 SUMO-1-activating enzyme, Ubch9 conjugated SUMO-1 to IkappaBalpha primarily on K21, which is also utilized for ubiquitin modification.
366	1235	conjugated	Ubch9	IkappaBalpha	In the presence of an E1 SUMO-1-activating enzyme, Ubch9 conjugated SUMO-1 to IkappaBalpha primarily on K21, which is also utilized for ubiquitin modification.
366	1236	conjugated	Ubch9	SUMO-1	In the presence of an E1 SUMO-1-activating enzyme, Ubch9 conjugated SUMO-1 to IkappaBalpha primarily on K21, which is also utilized for ubiquitin modification.
367	1237	interact	CFTR	ENaC	In the present study we examined whether CFTR interacts with ENaC by interfering with the Nedd4- and ubiquitin-mediated endocytosis of ENaC.
367	1238	interact	ENaC	CFTR	In the present study we examined whether CFTR interacts with ENaC by interfering with the Nedd4- and ubiquitin-mediated endocytosis of ENaC.
368	1239	modified	GR	SUMO-1	In the present study, we show that GR is post-translationally modified by SUMO-1 (sumoylated) in a ligand-enhanced fashion.
368	1240	modified	SUMO-1	GR	In the present study, we show that GR is post-translationally modified by SUMO-1 (sumoylated) in a ligand-enhanced fashion.
369	1241	interact	AR	Ubc9	In the present work, we find that Ubc9 interacts with the androgen receptor (AR), a member of the steroid receptor family of ligand-activated transcription factors.
369	1242	interact	Ubc9	AR	In the present work, we find that Ubc9 interacts with the androgen receptor (AR), a member of the steroid receptor family of ligand-activated transcription factors.
370	1243	interact	Apg12	Apg16	In the yeast Saccharomyces cerevisiae, the Apg12-Apg5 conjugate further interacts with a small coiled-coil protein, Apg16.
370	1244	interact	Apg16	Apg12	In the yeast Saccharomyces cerevisiae, the Apg12-Apg5 conjugate further interacts with a small coiled-coil protein, Apg16.
370	1245	interact	Apg16	Apg5	In the yeast Saccharomyces cerevisiae, the Apg12-Apg5 conjugate further interacts with a small coiled-coil protein, Apg16.
370	1246	interact	Apg5	Apg16	In the yeast Saccharomyces cerevisiae, the Apg12-Apg5 conjugate further interacts with a small coiled-coil protein, Apg16.
371	1247	interact	p62	ubiquitin	In the yeast two-hybrid system, p62 specifically interacted with ubiquitin in vivo.
371	1248	interact	ubiquitin	p62	In the yeast two-hybrid system, p62 specifically interacted with ubiquitin in vivo.
372	1249	bound	SUMO-1	hUba2	In this complex, hUba2 bound SUMO-1 and this complex had the activity of the SUMO-1 activating enzyme.
372	1250	bound	hUba2	SUMO-1	In this complex, hUba2 bound SUMO-1 and this complex had the activity of the SUMO-1 activating enzyme.
373	1251	interact	E6-AP	UbcH5	In this paper, we describe the isolation of two human E2s, designated as UbcH6 and UbcH7, that in addition to UbcH5 can interact with E6-AP.
373	1252	interact	E6-AP	UbcH6	In this paper, we describe the isolation of two human E2s, designated as UbcH6 and UbcH7, that in addition to UbcH5 can interact with E6-AP.
373	1253	interact	E6-AP	UbcH7	In this paper, we describe the isolation of two human E2s, designated as UbcH6 and UbcH7, that in addition to UbcH5 can interact with E6-AP.
373	1254	interact	UbcH5	E6-AP	In this paper, we describe the isolation of two human E2s, designated as UbcH6 and UbcH7, that in addition to UbcH5 can interact with E6-AP.
373	1255	interact	UbcH6	E6-AP	In this paper, we describe the isolation of two human E2s, designated as UbcH6 and UbcH7, that in addition to UbcH5 can interact with E6-AP.
373	1256	interact	UbcH7	E6-AP	In this paper, we describe the isolation of two human E2s, designated as UbcH6 and UbcH7, that in addition to UbcH5 can interact with E6-AP.
374	1257	bind	E6	p53	In this study we demonstrate that the E6 proteins of the oncogenic HPVs that bind p53 stimulate the degradation of p53.
374	1258	bind	p53	E6	In this study we demonstrate that the E6 proteins of the oncogenic HPVs that bind p53 stimulate the degradation of p53.
375	1259	interact	Egr-1	PRC8	In this study, the yeast two-hybrid screening revealed that Egr-1 interacts significantly with PRC8 (proteasome component C8) and the specific interaction was confirmed by GST pull-down assay and coimmunoprecipitation.
375	1260	interact	PRC8	Egr-1	In this study, the yeast two-hybrid screening revealed that Egr-1 interacts significantly with PRC8 (proteasome component C8) and the specific interaction was confirmed by GST pull-down assay and coimmunoprecipitation.
376	1261	conjugation	E2-F1	p53	In this study, we demonstrate reconstitution of a cell-free processing system and demonstrate directly that: (a) the ubiquitin-proteasome system is involved in processing of the intact p105 precursor, (b) conjugation of ubiquitin to the precursor is an essential intermediate step in the processing, (c) the recently discovered novel species of the ubiquitin-carrier protein, E2-F1, that is involved in the conjugation and degradation of p53, is also required for the limited processing of the p105 precursor, and (d) a novel, approximately 320-kDa species of ubiquitin-protein ligase, is involved in the process.
376	1262	conjugation	p53	E2-F1	In this study, we demonstrate reconstitution of a cell-free processing system and demonstrate directly that: (a) the ubiquitin-proteasome system is involved in processing of the intact p105 precursor, (b) conjugation of ubiquitin to the precursor is an essential intermediate step in the processing, (c) the recently discovered novel species of the ubiquitin-carrier protein, E2-F1, that is involved in the conjugation and degradation of p53, is also required for the limited processing of the p105 precursor, and (d) a novel, approximately 320-kDa species of ubiquitin-protein ligase, is involved in the process.
377	1263	associate	ASK1	COI1	In this study, we demonstrate that COI1 associates physically with AtCUL1, AtRbx1, and either of the Arabidopsis Skp1-like proteins ASK1 or ASK2 to assemble ubiquitin-ligase complexes, which we have designated SCF(COI1).
377	1264	associate	ASK2	COI1	In this study, we demonstrate that COI1 associates physically with AtCUL1, AtRbx1, and either of the Arabidopsis Skp1-like proteins ASK1 or ASK2 to assemble ubiquitin-ligase complexes, which we have designated SCF(COI1).
377	1265	associate	AtCUL1	COI1	In this study, we demonstrate that COI1 associates physically with AtCUL1, AtRbx1, and either of the Arabidopsis Skp1-like proteins ASK1 or ASK2 to assemble ubiquitin-ligase complexes, which we have designated SCF(COI1).
377	1266	associate	AtRbx1	COI1	In this study, we demonstrate that COI1 associates physically with AtCUL1, AtRbx1, and either of the Arabidopsis Skp1-like proteins ASK1 or ASK2 to assemble ubiquitin-ligase complexes, which we have designated SCF(COI1).
377	1267	associate	COI1	ASK1	In this study, we demonstrate that COI1 associates physically with AtCUL1, AtRbx1, and either of the Arabidopsis Skp1-like proteins ASK1 or ASK2 to assemble ubiquitin-ligase complexes, which we have designated SCF(COI1).
377	1268	associate	COI1	ASK2	In this study, we demonstrate that COI1 associates physically with AtCUL1, AtRbx1, and either of the Arabidopsis Skp1-like proteins ASK1 or ASK2 to assemble ubiquitin-ligase complexes, which we have designated SCF(COI1).
377	1269	associate	COI1	AtCUL1	In this study, we demonstrate that COI1 associates physically with AtCUL1, AtRbx1, and either of the Arabidopsis Skp1-like proteins ASK1 or ASK2 to assemble ubiquitin-ligase complexes, which we have designated SCF(COI1).
377	1270	associate	COI1	AtRbx1	In this study, we demonstrate that COI1 associates physically with AtCUL1, AtRbx1, and either of the Arabidopsis Skp1-like proteins ASK1 or ASK2 to assemble ubiquitin-ligase complexes, which we have designated SCF(COI1).
378	1271	interact	Mdm2	beta-arrestin1	In this study, we found that though both beta-arrestin1 and beta-arrestin2 are able to interact with E3 ubiquitin ligase Mdm2, only expression of beta-arrestin2 leads to the relocalization of Mdm2 from the nucleus to the cytoplasm.
378	1272	interact	Mdm2	beta-arrestin2	In this study, we found that though both beta-arrestin1 and beta-arrestin2 are able to interact with E3 ubiquitin ligase Mdm2, only expression of beta-arrestin2 leads to the relocalization of Mdm2 from the nucleus to the cytoplasm.
378	1273	interact	beta-arrestin1	Mdm2	In this study, we found that though both beta-arrestin1 and beta-arrestin2 are able to interact with E3 ubiquitin ligase Mdm2, only expression of beta-arrestin2 leads to the relocalization of Mdm2 from the nucleus to the cytoplasm.
378	1274	interact	beta-arrestin2	Mdm2	In this study, we found that though both beta-arrestin1 and beta-arrestin2 are able to interact with E3 ubiquitin ligase Mdm2, only expression of beta-arrestin2 leads to the relocalization of Mdm2 from the nucleus to the cytoplasm.
379	1275	binds	IkappaB(alpha)	mHOS	In this study, we identified a novel murine F-box/WD40 repeat-containing protein, mHOS (a homologue of HOS/betaTrCP2). mHOS efficiently binds Skp1 protein (a 'core' component of SCF ubiquitin ligase), and phosphorylated IkappaB(alpha).
379	1276	binds	Skp1	mHOS	In this study, we identified a novel murine F-box/WD40 repeat-containing protein, mHOS (a homologue of HOS/betaTrCP2). mHOS efficiently binds Skp1 protein (a 'core' component of SCF ubiquitin ligase), and phosphorylated IkappaB(alpha).
379	1277	binds	mHOS	IkappaB(alpha)	In this study, we identified a novel murine F-box/WD40 repeat-containing protein, mHOS (a homologue of HOS/betaTrCP2). mHOS efficiently binds Skp1 protein (a 'core' component of SCF ubiquitin ligase), and phosphorylated IkappaB(alpha).
379	1278	binds	mHOS	Skp1	In this study, we identified a novel murine F-box/WD40 repeat-containing protein, mHOS (a homologue of HOS/betaTrCP2). mHOS efficiently binds Skp1 protein (a 'core' component of SCF ubiquitin ligase), and phosphorylated IkappaB(alpha).
380	1279	modified	IE1	SUMO-1	In this study, we provide direct evidence that IE1 is also covalently modified by SUMO-1 in both infected and cotransfected cells, as well as in in vitro assays, with up to 30% of the protein representing the covalently conjugated 90-kDa form in stable U373/IE1 cell lines.
380	1280	modified	SUMO-1	IE1	In this study, we provide direct evidence that IE1 is also covalently modified by SUMO-1 in both infected and cotransfected cells, as well as in in vitro assays, with up to 30% of the protein representing the covalently conjugated 90-kDa form in stable U373/IE1 cell lines.
381	1281	conjugated	H2A	ubiquitin	In this study, we show that histone H2A, alpha-crystallin, and actin are conjugated to ubiquitin, resulting in higher molecular mass species, which are detected by anti-ubiquitin antibodies.
381	1282	conjugate	actin	ubiquitin	In this study, we show that histone H2A, alpha-crystallin, and actin are conjugated to ubiquitin, resulting in higher molecular mass species, which are detected by anti-ubiquitin antibodies.
381	1283	conjugate	alpha-crystallin	ubiquitin	In this study, we show that histone H2A, alpha-crystallin, and actin are conjugated to ubiquitin, resulting in higher molecular mass species, which are detected by anti-ubiquitin antibodies.
381	1284	conjugated	ubiquitin	H2A	In this study, we show that histone H2A, alpha-crystallin, and actin are conjugated to ubiquitin, resulting in higher molecular mass species, which are detected by anti-ubiquitin antibodies.
381	1285	conjugate	ubiquitin	actin	In this study, we show that histone H2A, alpha-crystallin, and actin are conjugated to ubiquitin, resulting in higher molecular mass species, which are detected by anti-ubiquitin antibodies.
381	1286	conjugate	ubiquitin	alpha-crystallin	In this study, we show that histone H2A, alpha-crystallin, and actin are conjugated to ubiquitin, resulting in higher molecular mass species, which are detected by anti-ubiquitin antibodies.
382	1287	interact	PS1	SEL-10	In this study, we show that human SEL-10 interacts with PS1 and enhances PS1 ubiquitination, thus altering cellular levels of unprocessed PS1 and its N- and C-terminal fragments.
382	1288	interact	SEL-10	PS1	In this study, we show that human SEL-10 interacts with PS1 and enhances PS1 ubiquitination, thus altering cellular levels of unprocessed PS1 and its N- and C-terminal fragments.
383	1289	interact	ETS-1	huUBC9	In two different yeast assays, ETS-1 interacted with huUBC9.
383	1290	interact	huUBC9	ETS-1	In two different yeast assays, ETS-1 interacted with huUBC9.
384	1291	inhibit	APC	Rsk	In vertebrate unfertilized eggs, a special form of meiotic metaphase arrest by cytostatic factor (CSF) is mediated by MAPK activation of the protein kinase p90(Rsk), which leads to inhibition of the APC.
384	1292	inhibit	APC	p90	In vertebrate unfertilized eggs, a special form of meiotic metaphase arrest by cytostatic factor (CSF) is mediated by MAPK activation of the protein kinase p90(Rsk), which leads to inhibition of the APC.
384	1293	activation	MAPK	Rsk	In vertebrate unfertilized eggs, a special form of meiotic metaphase arrest by cytostatic factor (CSF) is mediated by MAPK activation of the protein kinase p90(Rsk), which leads to inhibition of the APC.
384	1294	activation	MAPK	p90	In vertebrate unfertilized eggs, a special form of meiotic metaphase arrest by cytostatic factor (CSF) is mediated by MAPK activation of the protein kinase p90(Rsk), which leads to inhibition of the APC.
384	1295	inhibit	Rsk	APC	In vertebrate unfertilized eggs, a special form of meiotic metaphase arrest by cytostatic factor (CSF) is mediated by MAPK activation of the protein kinase p90(Rsk), which leads to inhibition of the APC.
384	1296	activation	Rsk	MAPK	In vertebrate unfertilized eggs, a special form of meiotic metaphase arrest by cytostatic factor (CSF) is mediated by MAPK activation of the protein kinase p90(Rsk), which leads to inhibition of the APC.
384	1297	inhibit	p90	APC	In vertebrate unfertilized eggs, a special form of meiotic metaphase arrest by cytostatic factor (CSF) is mediated by MAPK activation of the protein kinase p90(Rsk), which leads to inhibition of the APC.
384	1298	activation	p90	MAPK	In vertebrate unfertilized eggs, a special form of meiotic metaphase arrest by cytostatic factor (CSF) is mediated by MAPK activation of the protein kinase p90(Rsk), which leads to inhibition of the APC.
385	1299	bound	NEDD8	UCH-L3	In vitro GST pull-down assay demonstrated that UCH-L3 bound to both NEDD8 and ubiquitin.
385	1300	bound	UCH-L3	NEDD8	In vitro GST pull-down assay demonstrated that UCH-L3 bound to both NEDD8 and ubiquitin.
385	1301	bound	UCH-L3	ubiquitin	In vitro GST pull-down assay demonstrated that UCH-L3 bound to both NEDD8 and ubiquitin.
385	1302	bound	ubiquitin	UCH-L3	In vitro GST pull-down assay demonstrated that UCH-L3 bound to both NEDD8 and ubiquitin.
386	1303	interact	Nedd4	annexin XIIIa	In vitro binding and coprecipitation experiments showed that the Nedd4-C2 domain interacts with both annexin XIIIa and b in the presence of Ca(2+), and the interaction is direct and optimal at 1 microM Ca(2+).
386	1304	interact	Nedd4	annexin XIIIb	In vitro binding and coprecipitation experiments showed that the Nedd4-C2 domain interacts with both annexin XIIIa and b in the presence of Ca(2+), and the interaction is direct and optimal at 1 microM Ca(2+).
386	1305	interact	annexin XIIIa	Nedd4	In vitro binding and coprecipitation experiments showed that the Nedd4-C2 domain interacts with both annexin XIIIa and b in the presence of Ca(2+), and the interaction is direct and optimal at 1 microM Ca(2+).
386	1306	interact	annexin XIIIb	Nedd4	In vitro binding and coprecipitation experiments showed that the Nedd4-C2 domain interacts with both annexin XIIIa and b in the presence of Ca(2+), and the interaction is direct and optimal at 1 microM Ca(2+).
387	1307	interact	UL9	hTid-1	In vitro immunoprecipitation experiments confirmed that hTid-1 interacts with the UL9 protein.
387	1308	interact	hTid-1	UL9	In vitro immunoprecipitation experiments confirmed that hTid-1 interacts with the UL9 protein.
388	1309	phosphorylate	CK17	US3	In vitro kinase and co-immunoprecipitation assays provided evidence that US3 PK directly phosphorylates CK17.
388	1310	phosphorylate	US3	CK17	In vitro kinase and co-immunoprecipitation assays provided evidence that US3 PK directly phosphorylates CK17.
389	1311	transfer	E6AP	ubiquitin	In vitro studies have shown that E6AP can form a high energy thiolester bond with ubiquitin and, in the presence of E6, transfer ubiquitin to p53.
389	1312	transfer	p53	ubiquitin	In vitro studies have shown that E6AP can form a high energy thiolester bond with ubiquitin and, in the presence of E6, transfer ubiquitin to p53.
389	1313	transfer	ubiquitin	E6AP	In vitro studies have shown that E6AP can form a high energy thiolester bond with ubiquitin and, in the presence of E6, transfer ubiquitin to p53.
389	1314	transfer	ubiquitin	p53	In vitro studies have shown that E6AP can form a high energy thiolester bond with ubiquitin and, in the presence of E6, transfer ubiquitin to p53.
390	1315	interact	PCNA	p21	In vitro studies have suggested a role for PCNA-in the repair synthesis step of nucleotide excision repair, and PCNA interacts with the cyclin-dependent kinase inhibitor p21.
390	1316	interact	p21	PCNA	In vitro studies have suggested a role for PCNA-in the repair synthesis step of nucleotide excision repair, and PCNA interacts with the cyclin-dependent kinase inhibitor p21.
391	1317	bound	Daxx	GST-sentrin	In vitro translated Daxx bound to GST-sentrin fusion protein.
391	1318	bound	GST-sentrin	Daxx	In vitro translated Daxx bound to GST-sentrin fusion protein.
392	1319	ubiquitinate	E2F1	Ubc5	In vitro, E2F1 can be ubiquitinated by E2/Ubc5 but not by E2/CDC34, is dependent on catalytically active ROC1, and is protected by the Rb protein.
392	1320	inhibit	Rb	boxSkp2	In vitro, E2F1 can be ubiquitinated by E2/Ubc5 but not by E2/CDC34, is dependent on catalytically active ROC1, and is protected by the Rb protein.
392	1321	ubiquitinate	Ubc5	E2F1	In vitro, E2F1 can be ubiquitinated by E2/Ubc5 but not by E2/CDC34, is dependent on catalytically active ROC1, and is protected by the Rb protein.
392	1322	inhibit	boxSkp2	Rb	In vitro, E2F1 can be ubiquitinated by E2/Ubc5 but not by E2/CDC34, is dependent on catalytically active ROC1, and is protected by the Rb protein.
393	1323	conjugate	Vsx-1	ubiquitin	In vitro, Vsx-1 was conjugated with multiple ubiquitin moieties.
393	1324	conjugate	ubiquitin	Vsx-1	In vitro, Vsx-1 was conjugated with multiple ubiquitin moieties.
394	1325	interact	ARI-1	UbcD10	In yeast two-hybrid assays, the protein ARI-1 interacts with a novel ubiquitin-conjugating enzyme, UbcD10, whose sequence is also reported here.
394	1326	interact	UbcD10	ARI-1	In yeast two-hybrid assays, the protein ARI-1 interacts with a novel ubiquitin-conjugating enzyme, UbcD10, whose sequence is also reported here.
395	1327	conjugation	Cdc53	Rub1	In yeast, a similar E3 complex, SCFCDC4, is regulated by conjugation of the ubiquitin-related protein Rub1 to the Cdc53 protein.
395	1328	conjugation	Rub1	Cdc53	In yeast, a similar E3 complex, SCFCDC4, is regulated by conjugation of the ubiquitin-related protein Rub1 to the Cdc53 protein.
396	1329	multiubiquitinate	Rsp5	VSV M	Indeed, the VSV M protein was multiubiquitinated by Rsp5 in an in vitro ubiquitination assay.
396	1330	multiubiquitinate	VSV M	Rsp5	Indeed, the VSV M protein was multiubiquitinated by Rsp5 in an in vitro ubiquitination assay.
397	1331	bind	DCC	Siah-1	Independent studies have shown that Sina and its highly related mammalian homologues Siah-1 and Siah-2 bind to the DCC (deleted in colorectal cancer) protein and promote its proteolysis via the ubiquitin-proteasome pathway.
397	1332	bind	DCC	Siah-2	Independent studies have shown that Sina and its highly related mammalian homologues Siah-1 and Siah-2 bind to the DCC (deleted in colorectal cancer) protein and promote its proteolysis via the ubiquitin-proteasome pathway.
397	1333	bind	Siah-1	DCC	Independent studies have shown that Sina and its highly related mammalian homologues Siah-1 and Siah-2 bind to the DCC (deleted in colorectal cancer) protein and promote its proteolysis via the ubiquitin-proteasome pathway.
397	1334	bind	Siah-2	DCC	Independent studies have shown that Sina and its highly related mammalian homologues Siah-1 and Siah-2 bind to the DCC (deleted in colorectal cancer) protein and promote its proteolysis via the ubiquitin-proteasome pathway.
398	1335	interact	IDE	Insulin	Insulin interacts with IDE and alters the activity of MCP, suggesting a functional relationship between these two components and a mechanism for an intracellular action of insulin.
398	1336	interact	Insulin	IDE	Insulin interacts with IDE and alters the activity of MCP, suggesting a functional relationship between these two components and a mechanism for an intracellular action of insulin.
399	1337	Interaction	ARF	MDM2	Interaction between ARF and MDM2 results in the localization of both proteins to the nucleolus through nucleolar localization signals (NoLS) in ARF and MDM2.
399	1338	Interaction	MDM2	ARF	Interaction between ARF and MDM2 results in the localization of both proteins to the nucleolus through nucleolar localization signals (NoLS) in ARF and MDM2.
400	1339	Interaction	NIRF	PCNP	Interaction between PCNP and NIRF was clarified by mammalian two-hybrid system, GST pull-down assay, and nuclear co-localization.
400	1340	Interaction	PCNP	NIRF	Interaction between PCNP and NIRF was clarified by mammalian two-hybrid system, GST pull-down assay, and nuclear co-localization.
401	1341	Interaction	OBF-1	Siah-1	Interaction between Siah-1 and OBF-1 leads to downregulation of OBF-1 protein level but not mRNA, and to a corresponding reduction in octamer site-dependent transcription activation.
401	1342	Interaction	Siah-1	OBF-1	Interaction between Siah-1 and OBF-1 leads to downregulation of OBF-1 protein level but not mRNA, and to a corresponding reduction in octamer site-dependent transcription activation.
402	1343	Interaction	UIP5	UbcM4	Interaction between UbcM4 and UIP5 was observed in vivo and in vitro with bacterially expressed proteins.
402	1344	Interaction	UbcM4	UIP5	Interaction between UbcM4 and UIP5 was observed in vivo and in vitro with bacterially expressed proteins.
403	1345	ubiquitinate	IkappaBbeta	beta-TrCP	Interaction with beta-TrCP is also necessary for ubiquitination of IkappaBbeta upon stimulation of cells, and deletion of the F-box in beta-TrCP abolishes its ability to ubiquitinate IkappaBbeta.
403	1346	ubiquitinate	beta-TrCP	IkappaBbeta	Interaction with beta-TrCP is also necessary for ubiquitination of IkappaBbeta upon stimulation of cells, and deletion of the F-box in beta-TrCP abolishes its ability to ubiquitinate IkappaBbeta.
404	1347	interact	CUL-1	SKR-3	Interestingly, SKR-3 could interact with both CUL-1 and its close paralog CUL-6.
404	1348	interact	CUL-6	SKR-3	Interestingly, SKR-3 could interact with both CUL-1 and its close paralog CUL-6.
404	1349	interact	SKR-3	CUL-1	Interestingly, SKR-3 could interact with both CUL-1 and its close paralog CUL-6.
404	1350	interact	SKR-3	CUL-6	Interestingly, SKR-3 could interact with both CUL-1 and its close paralog CUL-6.
405	1351	modification	HSF2	SUMO-1	Interestingly, SUMO-1 modification of HSF2 results in conversion of this factor to the active DNA binding form.
405	1352	modification	SUMO-1	HSF2	Interestingly, SUMO-1 modification of HSF2 results in conversion of this factor to the active DNA binding form.
406	1353	interaction	S9	p100	Interestingly, the S9/p100 interaction could be induced by NIK but not by a catalytically inactive NIK mutant.
406	1354	interaction	p100	S9	Interestingly, the S9/p100 interaction could be induced by NIK but not by a catalytically inactive NIK mutant.
407	1355	modification	CUL1	RUB1	Interestingly, the auxin response mutant axr1-12, in which RUB1 modification of the SCF component CUL1 is impaired, shows increased AtE2Fc protein levels, suggesting a dysfunction in the control of AtE2Fc stability.
407	1356	modification	RUB1	CUL1	Interestingly, the auxin response mutant axr1-12, in which RUB1 modification of the SCF component CUL1 is impaired, shows increased AtE2Fc protein levels, suggesting a dysfunction in the control of AtE2Fc stability.
408	1357	binds	Cln2	Grr1	Interestingly, the phosphoacceptor domain of Cln2 binds to Grr1 but is not ubiquitinated and is stable.
408	1358	binds	Grr1	Cln2	Interestingly, the phosphoacceptor domain of Cln2 binds to Grr1 but is not ubiquitinated and is stable.
409	1359	modified	SUMO-1	Topo1	Intriguingly, Topo1 is modified rapidly and extensively with SUMO-1, a ubiquitin-like protein, in response to CPT.
409	1360	modified	Topo1	SUMO-1	Intriguingly, Topo1 is modified rapidly and extensively with SUMO-1, a ubiquitin-like protein, in response to CPT.
410	1361	associate	55K	Orf6	It has previously been shown that 55K associates with Orf6.
410	1362	associate	Orf6	55K	It has previously been shown that 55K associates with Orf6.
411	1363	interaction	RanBP2	RanGAP1	It has recently been shown that mammalian RanGAP1 can be conjugated with SUMO-1, a small ubiquitin-related modifier, and that SUMO-1 conjugation promotes RanGAP1's interaction with RanBP2.
411	1364	interaction	RanGAP1	RanBP2	It has recently been shown that mammalian RanGAP1 can be conjugated with SUMO-1, a small ubiquitin-related modifier, and that SUMO-1 conjugation promotes RanGAP1's interaction with RanBP2.
411	1365	conjugated	RanGAP1	SUMO-1	It has recently been shown that mammalian RanGAP1 can be conjugated with SUMO-1, a small ubiquitin-related modifier, and that SUMO-1 conjugation promotes RanGAP1's interaction with RanBP2.
411	1366	conjugated	SUMO-1	RanGAP1	It has recently been shown that mammalian RanGAP1 can be conjugated with SUMO-1, a small ubiquitin-related modifier, and that SUMO-1 conjugation promotes RanGAP1's interaction with RanBP2.
412	1367	associate	26S	Mif1	It is anticipated that Mif1 may associate through its ubiquitin-like domain with the 26S proteasome, in this way connecting the protein degradation machinery to the ER membrane and resulting in an efficient ERAD.
412	1368	associate	Mif1	26S	It is anticipated that Mif1 may associate through its ubiquitin-like domain with the 26S proteasome, in this way connecting the protein degradation machinery to the ER membrane and resulting in an efficient ERAD.
413	1369	interact	AtUBC8-CIP8	COP1	It is possible that the AtUBC8-CIP8 module might interact with COP1 in vivo, thereby participating in proteasome-mediated degradation of HY5.
413	1370	interact	COP1	AtUBC8-CIP8	It is possible that the AtUBC8-CIP8 module might interact with COP1 in vivo, thereby participating in proteasome-mediated degradation of HY5.
414	1371	conjugate	Nedd8	cullin	It promotes cleavage of the Nedd8 conjugate (deneddylation) from the cullin component of SCF ubiquitin ligases.
414	1372	conjugate	cullin	Nedd8	It promotes cleavage of the Nedd8 conjugate (deneddylation) from the cullin component of SCF ubiquitin ligases.
415	1373	associate	RAD51	UBL1	It was previously reported that a ubiquitin-like protein, UBL1, associates with RAD51 in the yeast two-hybrid system.
415	1374	associate	UBL1	RAD51	It was previously reported that a ubiquitin-like protein, UBL1, associates with RAD51 in the yeast two-hybrid system.
416	1375	interaction	Daxx	PML	Its recruitment to ND10 from condensed chromatin requires a small ubiquitin-related modifier (SUMO-1) modification of PML and reflects the interaction between the COOH-terminal domain of Daxx and PML.
416	1376	interaction	PML	Daxx	Its recruitment to ND10 from condensed chromatin requires a small ubiquitin-related modifier (SUMO-1) modification of PML and reflects the interaction between the COOH-terminal domain of Daxx and PML.
416	1377	modification	PML	SUMO-1	Its recruitment to ND10 from condensed chromatin requires a small ubiquitin-related modifier (SUMO-1) modification of PML and reflects the interaction between the COOH-terminal domain of Daxx and PML.
416	1378	modification	SUMO-1	PML	Its recruitment to ND10 from condensed chromatin requires a small ubiquitin-related modifier (SUMO-1) modification of PML and reflects the interaction between the COOH-terminal domain of Daxx and PML.
417	1379	bind	JAB1	p27KIP1	JAB1, which is thought to bind p27KIP1 and transport it from the nucleus to the cytoplasm for proteasome/ubiquitin-mediated degradation, was found to be localized both in the cytoplasm and the nucleus in undifferentiated and differentiating tumors whereas located predominantly in the nucleus of differentiated tumor cells.
417	1380	bind	p27KIP1	JAB1	JAB1, which is thought to bind p27KIP1 and transport it from the nucleus to the cytoplasm for proteasome/ubiquitin-mediated degradation, was found to be localized both in the cytoplasm and the nucleus in undifferentiated and differentiating tumors whereas located predominantly in the nucleus of differentiated tumor cells.
418	1381	modify	FT85	Skp1	Kinetic analysis of FT85 suggests that its two glycosyltransferase activities normally modify Skp1 processively but can have partial function individually.
418	1382	modify	Skp1	FT85	Kinetic analysis of FT85 suggests that its two glycosyltransferase activities normally modify Skp1 processively but can have partial function individually.
419	1383	interacting	E1B-55K	importin-alpha 1	Lastly, we describe the identification and characterization of two novel E1B-55K interacting factors, importin-alpha 1 and pp32, that may also participate in the functions previously ascribed to E1B-55K and E4-orf6.
419	1384	interacting	E1B-55K	pp32	Lastly, we describe the identification and characterization of two novel E1B-55K interacting factors, importin-alpha 1 and pp32, that may also participate in the functions previously ascribed to E1B-55K and E4-orf6.
419	1385	interacting	importin-alpha 1	E1B-55K	Lastly, we describe the identification and characterization of two novel E1B-55K interacting factors, importin-alpha 1 and pp32, that may also participate in the functions previously ascribed to E1B-55K and E4-orf6.
419	1386	interacting	pp32	E1B-55K	Lastly, we describe the identification and characterization of two novel E1B-55K interacting factors, importin-alpha 1 and pp32, that may also participate in the functions previously ascribed to E1B-55K and E4-orf6.
420	1387	ubiquitinate	Skp2	h0rc1p	Later, as cyclin A accumulates and cells enter S phase, hOrc1p is ubiquitinated on chromatin and then degraded. hOrc1p destruction occurs through the proteasome and is signaled in part by the SCF(Skp2) ubiquitin-ligase complex.
420	1388	ubiquitinate	h0rc1p	Skp2	Later, as cyclin A accumulates and cells enter S phase, hOrc1p is ubiquitinated on chromatin and then degraded. hOrc1p destruction occurs through the proteasome and is signaled in part by the SCF(Skp2) ubiquitin-ligase complex.
421	1389	interaction	ENaC	Nedd4	Liddle's syndrome mutations disrupt the interaction between ENaC and Nedd4, resulting in an increase in the number of ENaC channels at the cell surface.
421	1390	interaction	Nedd4	ENaC	Liddle's syndrome mutations disrupt the interaction between ENaC and Nedd4, resulting in an increase in the number of ENaC channels at the cell surface.
422	1391	interaction	ENaC	Nedd4	Liddle's syndrome-associated mutations that prevent the interaction between Nedd4 and ENaC abolished inhibition, suggesting that a direct interaction is required for inhibition by Nedd4.
422	1392	interaction	Nedd4	ENaC	Liddle's syndrome-associated mutations that prevent the interaction between Nedd4 and ENaC abolished inhibition, suggesting that a direct interaction is required for inhibition by Nedd4.
423	1393	interact	VDU1	pVHL	Like VDU1, VDU2 interacts with pVHL beta-domain and these two proteins can compete with each other to bind to pVHL.
423	1394	interact	VDU2	pVHL	Like VDU1, VDU2 interacts with pVHL beta-domain and these two proteins can compete with each other to bind to pVHL.
423	1395	interact	pVHL	VDU1	Like VDU1, VDU2 interacts with pVHL beta-domain and these two proteins can compete with each other to bind to pVHL.
423	1396	interact	pVHL	VDU2	Like VDU1, VDU2 interacts with pVHL beta-domain and these two proteins can compete with each other to bind to pVHL.
424	1397	activation	AR	PIASx	Likewise, Lys-731 and Lys-788 mutants of GRIP1 have attenuated ability to enhance AR-dependent transcription and fail to synergize with PIASx beta-mediated activation of AR function, indicating that sumoylation modifies the ability of GRIP1 to function as a steroid receptor coactivator.
424	1398	activation	PIASx	AR	Likewise, Lys-731 and Lys-788 mutants of GRIP1 have attenuated ability to enhance AR-dependent transcription and fail to synergize with PIASx beta-mediated activation of AR function, indicating that sumoylation modifies the ability of GRIP1 to function as a steroid receptor coactivator.
425	1399	interact	Cdc4p	Cdc6p	Likewise, mutations in the Cdc4/34/53 pathway involved in ubiquitin-mediated degradation block proteolysis and genetic evidence is presented indicating that the N-terminus of Cdc6p interacts with the Cdc4/34/53 pathway, probably through Cdc4p.
425	1400	interact	Cdc6p	Cdc4p	Likewise, mutations in the Cdc4/34/53 pathway involved in ubiquitin-mediated degradation block proteolysis and genetic evidence is presented indicating that the N-terminus of Cdc6p interacts with the Cdc4/34/53 pathway, probably through Cdc4p.
426	1401	complex	BARD1	BRCA1	Limited proteolysis of BRCA1/BARD1 complexes, monitored by matrix-assisted laser desorption ionization time-of-flight spectrometry, show that the mutations cause a local structural perturbation that is primarily confined to the second Zn(2+) binding loop of the BRCA1 subunit.
426	1402	complex	BRCA1	BARD1	Limited proteolysis of BRCA1/BARD1 complexes, monitored by matrix-assisted laser desorption ionization time-of-flight spectrometry, show that the mutations cause a local structural perturbation that is primarily confined to the second Zn(2+) binding loop of the BRCA1 subunit.
427	1403	interaction	USP7	ataxin-1	Liquid beta-galactosidase assay and coimmunoprecipitation experiments revealed that the strength of the interaction between USP7 and ataxin-1 is influenced by the length of the polyglutamine tract in the ataxin-1; weaker interaction was observed in mutant ataxin-1 with longer polyglutamine tract and USP7 was not recruited to the mutant ataxin-1 aggregates in the Purkinje cells of SCA1 transgenic mice.
427	1404	interaction	ataxin-1	USP7	Liquid beta-galactosidase assay and coimmunoprecipitation experiments revealed that the strength of the interaction between USP7 and ataxin-1 is influenced by the length of the polyglutamine tract in the ataxin-1; weaker interaction was observed in mutant ataxin-1 with longer polyglutamine tract and USP7 was not recruited to the mutant ataxin-1 aggregates in the Purkinje cells of SCA1 transgenic mice.
428	1405	modification	IE72	SUMO-1	Lysine 450 is within a sumoylation consensus site (I,V,L)KXE; changing lysine 450 to arginine by point mutation abolishes SUMO-1 modification of IE72.
428	1406	modification	SUMO-1	IE72	Lysine 450 is within a sumoylation consensus site (I,V,L)KXE; changing lysine 450 to arginine by point mutation abolishes SUMO-1 modification of IE72.
429	1407	bind	MDM2	p53	MDM2 binds p53 and promotes its rapid degradation.
429	1408	bind	p53	MDM2	MDM2 binds p53 and promotes its rapid degradation.
430	1409	bind	MDM4	p53	MDM4 binds and inhibits p53 transcriptional activity in vitro.
430	1410	bind	p53	MDM4	MDM4 binds and inhibits p53 transcriptional activity in vitro.
431	1411	activate	MMS	Mif1	MMS, on the other hand, activates Mif1 via an UPR-independent pathway.
431	1412	activate	Mif1	MMS	MMS, on the other hand, activates Mif1 via an UPR-independent pathway.
432	1413	binding	MUL	TRAF1	MUL and USP7 are capable of binding in vitro via their TDs to all of the previously identified TRAF family proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, and TRAF6), whereas the TD of SPOP interacts weakly with TRAF1 and TRAF6 only.
432	1414	binding	MUL	TRAF2	MUL and USP7 are capable of binding in vitro via their TDs to all of the previously identified TRAF family proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, and TRAF6), whereas the TD of SPOP interacts weakly with TRAF1 and TRAF6 only.
432	1415	binding	MUL	TRAF3	MUL and USP7 are capable of binding in vitro via their TDs to all of the previously identified TRAF family proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, and TRAF6), whereas the TD of SPOP interacts weakly with TRAF1 and TRAF6 only.
432	1416	binding	MUL	TRAF4	MUL and USP7 are capable of binding in vitro via their TDs to all of the previously identified TRAF family proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, and TRAF6), whereas the TD of SPOP interacts weakly with TRAF1 and TRAF6 only.
432	1417	binding	MUL	TRAF5	MUL and USP7 are capable of binding in vitro via their TDs to all of the previously identified TRAF family proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, and TRAF6), whereas the TD of SPOP interacts weakly with TRAF1 and TRAF6 only.
432	1418	binding	MUL	TRAF6	MUL and USP7 are capable of binding in vitro via their TDs to all of the previously identified TRAF family proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, and TRAF6), whereas the TD of SPOP interacts weakly with TRAF1 and TRAF6 only.
432	1419	interact	SPOP	TRAF1	MUL and USP7 are capable of binding in vitro via their TDs to all of the previously identified TRAF family proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, and TRAF6), whereas the TD of SPOP interacts weakly with TRAF1 and TRAF6 only.
432	1420	interact	SPOP	TRAF6	MUL and USP7 are capable of binding in vitro via their TDs to all of the previously identified TRAF family proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, and TRAF6), whereas the TD of SPOP interacts weakly with TRAF1 and TRAF6 only.
432	1421	binding	TRAF1	MUL	MUL and USP7 are capable of binding in vitro via their TDs to all of the previously identified TRAF family proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, and TRAF6), whereas the TD of SPOP interacts weakly with TRAF1 and TRAF6 only.
432	1422	interact	TRAF1	SPOP	MUL and USP7 are capable of binding in vitro via their TDs to all of the previously identified TRAF family proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, and TRAF6), whereas the TD of SPOP interacts weakly with TRAF1 and TRAF6 only.
432	1423	binding	TRAF1	USP7	MUL and USP7 are capable of binding in vitro via their TDs to all of the previously identified TRAF family proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, and TRAF6), whereas the TD of SPOP interacts weakly with TRAF1 and TRAF6 only.
432	1424	binding	TRAF2	MUL	MUL and USP7 are capable of binding in vitro via their TDs to all of the previously identified TRAF family proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, and TRAF6), whereas the TD of SPOP interacts weakly with TRAF1 and TRAF6 only.
432	1425	binding	TRAF2	USP7	MUL and USP7 are capable of binding in vitro via their TDs to all of the previously identified TRAF family proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, and TRAF6), whereas the TD of SPOP interacts weakly with TRAF1 and TRAF6 only.
432	1426	binding	TRAF3	MUL	MUL and USP7 are capable of binding in vitro via their TDs to all of the previously identified TRAF family proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, and TRAF6), whereas the TD of SPOP interacts weakly with TRAF1 and TRAF6 only.
432	1427	binding	TRAF3	USP7	MUL and USP7 are capable of binding in vitro via their TDs to all of the previously identified TRAF family proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, and TRAF6), whereas the TD of SPOP interacts weakly with TRAF1 and TRAF6 only.
432	1428	binding	TRAF4	MUL	MUL and USP7 are capable of binding in vitro via their TDs to all of the previously identified TRAF family proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, and TRAF6), whereas the TD of SPOP interacts weakly with TRAF1 and TRAF6 only.
432	1429	binding	TRAF4	USP7	MUL and USP7 are capable of binding in vitro via their TDs to all of the previously identified TRAF family proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, and TRAF6), whereas the TD of SPOP interacts weakly with TRAF1 and TRAF6 only.
432	1430	binding	TRAF5	MUL	MUL and USP7 are capable of binding in vitro via their TDs to all of the previously identified TRAF family proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, and TRAF6), whereas the TD of SPOP interacts weakly with TRAF1 and TRAF6 only.
432	1431	binding	TRAF5	USP7	MUL and USP7 are capable of binding in vitro via their TDs to all of the previously identified TRAF family proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, and TRAF6), whereas the TD of SPOP interacts weakly with TRAF1 and TRAF6 only.
432	1432	binding	TRAF6	MUL	MUL and USP7 are capable of binding in vitro via their TDs to all of the previously identified TRAF family proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, and TRAF6), whereas the TD of SPOP interacts weakly with TRAF1 and TRAF6 only.
432	1433	interact	TRAF6	SPOP	MUL and USP7 are capable of binding in vitro via their TDs to all of the previously identified TRAF family proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, and TRAF6), whereas the TD of SPOP interacts weakly with TRAF1 and TRAF6 only.
432	1434	binding	TRAF6	USP7	MUL and USP7 are capable of binding in vitro via their TDs to all of the previously identified TRAF family proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, and TRAF6), whereas the TD of SPOP interacts weakly with TRAF1 and TRAF6 only.
432	1435	binding	USP7	TRAF1	MUL and USP7 are capable of binding in vitro via their TDs to all of the previously identified TRAF family proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, and TRAF6), whereas the TD of SPOP interacts weakly with TRAF1 and TRAF6 only.
432	1436	binding	USP7	TRAF2	MUL and USP7 are capable of binding in vitro via their TDs to all of the previously identified TRAF family proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, and TRAF6), whereas the TD of SPOP interacts weakly with TRAF1 and TRAF6 only.
432	1437	binding	USP7	TRAF3	MUL and USP7 are capable of binding in vitro via their TDs to all of the previously identified TRAF family proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, and TRAF6), whereas the TD of SPOP interacts weakly with TRAF1 and TRAF6 only.
432	1438	binding	USP7	TRAF4	MUL and USP7 are capable of binding in vitro via their TDs to all of the previously identified TRAF family proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, and TRAF6), whereas the TD of SPOP interacts weakly with TRAF1 and TRAF6 only.
432	1439	binding	USP7	TRAF5	MUL and USP7 are capable of binding in vitro via their TDs to all of the previously identified TRAF family proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, and TRAF6), whereas the TD of SPOP interacts weakly with TRAF1 and TRAF6 only.
432	1440	binding	USP7	TRAF6	MUL and USP7 are capable of binding in vitro via their TDs to all of the previously identified TRAF family proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, and TRAF6), whereas the TD of SPOP interacts weakly with TRAF1 and TRAF6 only.
433	1441	bound	Nup358	RanGAP	Mammalian RanGAP is bound to the nuclear pore by a mechanism involving the attachment of small ubiquitin-related modifier protein (SUMO) to its C terminus and the subsequent binding of the SUMOylated domain to the nucleoporin Nup358.
433	1442	bound	RanGAP	Nup358	Mammalian RanGAP is bound to the nuclear pore by a mechanism involving the attachment of small ubiquitin-related modifier protein (SUMO) to its C terminus and the subsequent binding of the SUMOylated domain to the nucleoporin Nup358.
433	1443	attachment	RanGAP	SUMO	Mammalian RanGAP is bound to the nuclear pore by a mechanism involving the attachment of small ubiquitin-related modifier protein (SUMO) to its C terminus and the subsequent binding of the SUMOylated domain to the nucleoporin Nup358.
433	1444	attachment	SUMO	RanGAP	Mammalian RanGAP is bound to the nuclear pore by a mechanism involving the attachment of small ubiquitin-related modifier protein (SUMO) to its C terminus and the subsequent binding of the SUMOylated domain to the nucleoporin Nup358.
434	1445	bind	Mdm2	p53	Mdm2 binds to the N-terminus of p53 and, through its action as an E3 ubiquitin ligase, targets p53 for rapid proteasomal degradation.
434	1446	bind	p53	Mdm2	Mdm2 binds to the N-terminus of p53 and, through its action as an E3 ubiquitin ligase, targets p53 for rapid proteasomal degradation.
435	1447	ubiquitinate	Mdm2	p53	Mdm2 is a ubiquitin-protein ligase known to ubiquitinate p53, promoting its degradation by the ubiquitin-proteasome system.
435	1448	ubiquitinate	p53	Mdm2	Mdm2 is a ubiquitin-protein ligase known to ubiquitinate p53, promoting its degradation by the ubiquitin-proteasome system.
436	1449	interact	STE11	STE5	Measurement of relative binding affinities showed that the STE11 protein tightly interacts with the STE5 protein for its stabilization.
436	1450	interact	STE5	STE11	Measurement of relative binding affinities showed that the STE11 protein tightly interacts with the STE5 protein for its stabilization.
437	1451	interaction	CIN85	Cbl	Monoubiquitination of CIN85 required direct interactions between CIN85 and Cbl, the intact RING finger domain of Cbl and a ubiquitin acceptor site present in the carboxyl terminus of CIN85.
437	1452	interaction	Cbl	CIN85	Monoubiquitination of CIN85 required direct interactions between CIN85 and Cbl, the intact RING finger domain of Cbl and a ubiquitin acceptor site present in the carboxyl terminus of CIN85.
438	1453	modify	IkappaBalpha	SUMO-1	More recent studies have now shown that SUMO-1 covalently modifies a number of target proteins including PML, RanGAP1 and IkappaBalpha and is proposed to play a role in either targeting modified proteins and/or inhibiting their degradation.
438	1454	modify	PML	SUMO-1	More recent studies have now shown that SUMO-1 covalently modifies a number of target proteins including PML, RanGAP1 and IkappaBalpha and is proposed to play a role in either targeting modified proteins and/or inhibiting their degradation.
438	1455	modify	RanGAP1	SUMO-1	More recent studies have now shown that SUMO-1 covalently modifies a number of target proteins including PML, RanGAP1 and IkappaBalpha and is proposed to play a role in either targeting modified proteins and/or inhibiting their degradation.
438	1456	modify	SUMO-1	IkappaBalpha	More recent studies have now shown that SUMO-1 covalently modifies a number of target proteins including PML, RanGAP1 and IkappaBalpha and is proposed to play a role in either targeting modified proteins and/or inhibiting their degradation.
438	1457	modify	SUMO-1	PML	More recent studies have now shown that SUMO-1 covalently modifies a number of target proteins including PML, RanGAP1 and IkappaBalpha and is proposed to play a role in either targeting modified proteins and/or inhibiting their degradation.
438	1458	modify	SUMO-1	RanGAP1	More recent studies have now shown that SUMO-1 covalently modifies a number of target proteins including PML, RanGAP1 and IkappaBalpha and is proposed to play a role in either targeting modified proteins and/or inhibiting their degradation.
439	1459	interaction	Png1p	Rad23p	More recent studies in yeast indicate that Png1p can bind to the 26S proteasome through its interaction with the DNA repair protein Rad23p.
439	1460	interaction	Rad23p	Png1p	More recent studies in yeast indicate that Png1p can bind to the 26S proteasome through its interaction with the DNA repair protein Rad23p.
440	1461	target	LEF1	PIASy	Moreover, PIASy binds to nuclear matrix-associated DNA sequences and targets LEF1 to nuclear bodies, suggesting that PIASy-mediated subnuclear sequestration accounts for the repression of LEF1 activity.
440	1462	target	PIASy	LEF1	Moreover, PIASy binds to nuclear matrix-associated DNA sequences and targets LEF1 to nuclear bodies, suggesting that PIASy-mediated subnuclear sequestration accounts for the repression of LEF1 activity.
441	1463	complex	MMS2	RAD18	Moreover, RAD5 association with RAD18 brings UBC13-MMS2 into contact with the RAD6-RAD18 complex.
441	1464	complex	MMS2	RAD6	Moreover, RAD5 association with RAD18 brings UBC13-MMS2 into contact with the RAD6-RAD18 complex.
441	1465	complex	MMS2	UBC13	Moreover, RAD5 association with RAD18 brings UBC13-MMS2 into contact with the RAD6-RAD18 complex.
441	1466	complex	RAD18	MMS2	Moreover, RAD5 association with RAD18 brings UBC13-MMS2 into contact with the RAD6-RAD18 complex.
441	1467	association	RAD18	RAD5	Moreover, RAD5 association with RAD18 brings UBC13-MMS2 into contact with the RAD6-RAD18 complex.
441	1468	complex	RAD18	RAD6	Moreover, RAD5 association with RAD18 brings UBC13-MMS2 into contact with the RAD6-RAD18 complex.
441	1469	complex	RAD18	UBC13	Moreover, RAD5 association with RAD18 brings UBC13-MMS2 into contact with the RAD6-RAD18 complex.
441	1470	association	RAD5	RAD18	Moreover, RAD5 association with RAD18 brings UBC13-MMS2 into contact with the RAD6-RAD18 complex.
441	1471	complex	RAD6	MMS2	Moreover, RAD5 association with RAD18 brings UBC13-MMS2 into contact with the RAD6-RAD18 complex.
441	1472	complex	RAD6	RAD18	Moreover, RAD5 association with RAD18 brings UBC13-MMS2 into contact with the RAD6-RAD18 complex.
441	1473	complex	RAD6	UBC13	Moreover, RAD5 association with RAD18 brings UBC13-MMS2 into contact with the RAD6-RAD18 complex.
441	1474	complex	UBC13	MMS2	Moreover, RAD5 association with RAD18 brings UBC13-MMS2 into contact with the RAD6-RAD18 complex.
441	1475	complex	UBC13	RAD18	Moreover, RAD5 association with RAD18 brings UBC13-MMS2 into contact with the RAD6-RAD18 complex.
441	1476	complex	UBC13	RAD6	Moreover, RAD5 association with RAD18 brings UBC13-MMS2 into contact with the RAD6-RAD18 complex.
442	1477	associate	Cln3	Ydj1	Moreover, Ydj1 directly associates with Cln3 in close proximity to the segment that is phosphorylated and signals degradation.
442	1478	associate	Ydj1	Cln3	Moreover, Ydj1 directly associates with Cln3 in close proximity to the segment that is phosphorylated and signals degradation.
443	1479	interact	Daxx	PML	Moreover, a PML mutant that can not be modified by the ubiquitin-related SUMO-1 modifier is no more able to interact with Daxx.
443	1480	interact	PML	Daxx	Moreover, a PML mutant that can not be modified by the ubiquitin-related SUMO-1 modifier is no more able to interact with Daxx.
444	1481	interaction	RARs	Stat5	Moreover, coimmunoprecipitation studies indicate an interaction between Stat5 and RARs that is IL-3 dependent.
444	1482	interaction	Stat5	RARs	Moreover, coimmunoprecipitation studies indicate an interaction between Stat5 and RARs that is IL-3 dependent.
445	1483	ubiquitinate	IkappaBalpha	beta-TrCP	Moreover, immunopurified beta-TrCP ubiquitinates phosphorylated IkappaBalpha at specific lysines in the presence of Ub-activating (E1) and -conjugating (Ubch5) enzymes.
445	1484	ubiquitinate	beta-TrCP	IkappaBalpha	Moreover, immunopurified beta-TrCP ubiquitinates phosphorylated IkappaBalpha at specific lysines in the presence of Ub-activating (E1) and -conjugating (Ubch5) enzymes.
446	1485	binding	mHDAC6	ubiquitin	Moreover, in the C-terminal region of mHDAC6, a conserved zinc finger-containing domain named ZnF-UBP, also present in several ubiquitin-specific proteases, was discovered and was shown to mediate the specific binding of ubiquitin by mHDAC6.
446	1486	binding	ubiquitin	mHDAC6	Moreover, in the C-terminal region of mHDAC6, a conserved zinc finger-containing domain named ZnF-UBP, also present in several ubiquitin-specific proteases, was discovered and was shown to mediate the specific binding of ubiquitin by mHDAC6.
447	1487	bind	p62	ubiquitin	Moreover, p62 binds ubiquitin and may act as an adapter linking ubiquitinated species to other proteins.
447	1488	bind	ubiquitin	p62	Moreover, p62 binds ubiquitin and may act as an adapter linking ubiquitinated species to other proteins.
448	1489	phosphorylate	Bub1	Rsk	Moreover, purified p90(Rsk) phosphorylates Bub1 in vitro and increases its protein kinase activity.
448	1490	phosphorylate	Bub1	p90	Moreover, purified p90(Rsk) phosphorylates Bub1 in vitro and increases its protein kinase activity.
448	1491	phosphorylate	Rsk	Bub1	Moreover, purified p90(Rsk) phosphorylates Bub1 in vitro and increases its protein kinase activity.
448	1492	phosphorylate	p90	Bub1	Moreover, purified p90(Rsk) phosphorylates Bub1 in vitro and increases its protein kinase activity.
449	1493	phosphorylate	MKK6	TAK1	Moreover, the activity of TAK1 to phosphorylate MKK6, which activates the JNK-p38 kinase pathway, is directly regulated by K63-linked polyubiquitination.
449	1494	phosphorylate	TAK1	MKK6	Moreover, the activity of TAK1 to phosphorylate MKK6, which activates the JNK-p38 kinase pathway, is directly regulated by K63-linked polyubiquitination.
450	1495	binding	IkappaBalpha	NF-kappaB	Moreover, the putative IkappaBalpha-Ub ligase (IkappaBalpha-E3) present in HeLa cell cytosol associated in vitro with an IKK-phosphorylated recombinant IkappaBalpha, a process independent of NF-kappaB binding to IkappaBalpha or TNFalpha stimulation.
450	1496	binding	NF-kappaB	IkappaBalpha	Moreover, the putative IkappaBalpha-Ub ligase (IkappaBalpha-E3) present in HeLa cell cytosol associated in vitro with an IKK-phosphorylated recombinant IkappaBalpha, a process independent of NF-kappaB binding to IkappaBalpha or TNFalpha stimulation.
451	1497	bind	HIF-1alpha	VHL	Moreover, we demonstrate that Leu-574 of HIF-1alpha is essential for VHL binding to the C-terminal ODD.
451	1498	bind	VHL	HIF-1alpha	Moreover, we demonstrate that Leu-574 of HIF-1alpha is essential for VHL binding to the C-terminal ODD.
452	1499	ubiquitination	E6AP	p53	Mutant forms of E6AP proteins were identified that were catalytically incapable of participating in E6-dependent ubiquitination of p53 and functioned in a dominant-negative manner in that they inhibited the E6-mediated ubiquitination of p53 by the wild-type E6AP in vitro.
452	1500	ubiquitination	p53	E6AP	Mutant forms of E6AP proteins were identified that were catalytically incapable of participating in E6-dependent ubiquitination of p53 and functioned in a dominant-negative manner in that they inhibited the E6-mediated ubiquitination of p53 by the wild-type E6AP in vitro.
453	1501	complex	Srp1p	Sts1p	Mutants of Sts1p that cannot interact with Srp1p are incapable of suppressing srp1-49 defects, strongly suggesting that Sts1p functions in a complex with Srp1p.
453	1502	complex	Sts1p	Srp1p	Mutants of Sts1p that cannot interact with Srp1p are incapable of suppressing srp1-49 defects, strongly suggesting that Sts1p functions in a complex with Srp1p.
454	1503	binding	AIP4	LMP2A	Mutation of both of the LMP2A PY motifs resulted in an absence of binding of AIP4 to LMP2A, which resulted in an increase in the expression of Lyn and the constitutive hyperphosphorylation of LMP2A and an unknown 120-kDa protein.
454	1504	binding	LMP2A	AIP4	Mutation of both of the LMP2A PY motifs resulted in an absence of binding of AIP4 to LMP2A, which resulted in an increase in the expression of Lyn and the constitutive hyperphosphorylation of LMP2A and an unknown 120-kDa protein.
455	1505	binding	ROC1	cullin	Mutations at the conserved Phe79 and His80 residues in the RING finger of ROC1 diminish its binding with cullins, resulting in a loss of cullin protection and ubiquitin ligase activity.
455	1506	binding	cullin	ROC1	Mutations at the conserved Phe79 and His80 residues in the RING finger of ROC1 diminish its binding with cullins, resulting in a loss of cullin protection and ubiquitin ligase activity.
456	1507	conjugate	E3alpha	ubiquitin	Mutations in the destruction signal sequences resulted in changes in the rate at which E3alpha conjugates ubiquitin to the altered 3C protease proteins.
456	1508	conjugate	ubiquitin	E3alpha	Mutations in the destruction signal sequences resulted in changes in the rate at which E3alpha conjugates ubiquitin to the altered 3C protease proteins.
457	1509	bind	N4WBP5	Nedd4	N4WBP5 binds Nedd4 WW domains via the two PPXY motifs present in the amino terminus of the protein.
457	1510	bind	Nedd4	N4WBP5	N4WBP5 binds Nedd4 WW domains via the two PPXY motifs present in the amino terminus of the protein.
458	1511	inhibitor	IkappaB	NF-kappaB	NF-kappaB transcription factor is activated upon ubiquitination and subsequent proteolysis of its inhibitor IkappaB.
458	1512	inhibitor	NF-kappaB	IkappaB	NF-kappaB transcription factor is activated upon ubiquitination and subsequent proteolysis of its inhibitor IkappaB.
459	1513	bind	ENaC	Nedd4	Nedd4 was demonstrated to bind the epithelial sodium channel (alphabetagammaENaC), by association of its WW domains with PY motifs (XPPXY) present in each ENaC subunit, and to regulate the cell surface stability of the channel.
459	1514	bind	Nedd4	ENaC	Nedd4 was demonstrated to bind the epithelial sodium channel (alphabetagammaENaC), by association of its WW domains with PY motifs (XPPXY) present in each ENaC subunit, and to regulate the cell surface stability of the channel.
460	1515	bind	ENaC	Nedd4	Nedd4, a ubiquitin protein ligase, binds to ENaC and targets the channel for endocytosis and degradation.
460	1516	bind	Nedd4	ENaC	Nedd4, a ubiquitin protein ligase, binds to ENaC and targets the channel for endocytosis and degradation.
461	1517	activation	UBA3	ubiquitin	Nevertheless, the protein encoded by UBA3 catalyzes the ATP-dependent activation of ubiquitin in vitro.
461	1518	activation	ubiquitin	UBA3	Nevertheless, the protein encoded by UBA3 catalyzes the ATP-dependent activation of ubiquitin in vitro.
462	1519	bind	isoT	ubiquitin	None of the mutations significantly affected the capacity of isoT to bind ubiquitin and zinc.
462	1520	bind	ubiquitin	isoT	None of the mutations significantly affected the capacity of isoT to bind ubiquitin and zinc.
463	1521	activate	APC	CDH1	Nonphosphorylatable CDH1 mutants constitutively activate APC in vitro and in vivo, whereas mutants mimicking the phosphorylated form of CDH1 are constitutively inactive.
463	1522	activate	CDH1	APC	Nonphosphorylatable CDH1 mutants constitutively activate APC in vitro and in vivo, whereas mutants mimicking the phosphorylated form of CDH1 are constitutively inactive.
464	1523	enhance	PIASy	SUMO-1-modification-EBPalpha	Notably, we find that PIASy has E3like activity and enhances both SUMO-1 and SUMO-3 modification of C/EBPalpha in vivo and in vitro.
464	1524	enhance	PIASy	SUMO-3-modification-EBPalpha	Notably, we find that PIASy has E3like activity and enhances both SUMO-1 and SUMO-3 modification of C/EBPalpha in vivo and in vitro.
464	1525	enhance	SUMO-1-modification-EBPalpha	PIASy	Notably, we find that PIASy has E3like activity and enhances both SUMO-1 and SUMO-3 modification of C/EBPalpha in vivo and in vitro.
464	1526	enhance	SUMO-3-modification-EBPalpha	PIASy	Notably, we find that PIASy has E3like activity and enhances both SUMO-1 and SUMO-3 modification of C/EBPalpha in vivo and in vitro.
465	1527	modification	EBPalpha	SUMO-1	Notably, we find that PIASy has E3like activity and enhances both SUMO-1 and SUMO-3 modification of EBPalpha in vivo and in vitro.
465	1528	modification	EBPalpha	SUMO-3	Notably, we find that PIASy has E3like activity and enhances both SUMO-1 and SUMO-3 modification of EBPalpha in vivo and in vitro.
465	1529	modification	SUMO-1	EBPalpha	Notably, we find that PIASy has E3like activity and enhances both SUMO-1 and SUMO-3 modification of EBPalpha in vivo and in vitro.
465	1530	modification	SUMO-3	EBPalpha	Notably, we find that PIASy has E3like activity and enhances both SUMO-1 and SUMO-3 modification of EBPalpha in vivo and in vitro.
466	1531	modification	PCNA	SUMO	Now, ubiquitin and SUMO modification of proliferating cell nuclear antigen (PCNA) is shown to be induced by DNA damage and linked to components of the RAD6 pathway.
466	1532	modification	PCNA	ubiquitin	Now, ubiquitin and SUMO modification of proliferating cell nuclear antigen (PCNA) is shown to be induced by DNA damage and linked to components of the RAD6 pathway.
466	1533	modification	SUMO	PCNA	Now, ubiquitin and SUMO modification of proliferating cell nuclear antigen (PCNA) is shown to be induced by DNA damage and linked to components of the RAD6 pathway.
466	1534	modification	ubiquitin	PCNA	Now, ubiquitin and SUMO modification of proliferating cell nuclear antigen (PCNA) is shown to be induced by DNA damage and linked to components of the RAD6 pathway.
467	1535	bind	E6	E6AP	Of all four proteins investigated, only HPV16 E6 was able to bind to p53 and E6AP and to induce degradation of the p53 protein in the reticulocyte system.
467	1536	bind	E6	p53	Of all four proteins investigated, only HPV16 E6 was able to bind to p53 and E6AP and to induce degradation of the p53 protein in the reticulocyte system.
467	1537	bind	E6AP	E6	Of all four proteins investigated, only HPV16 E6 was able to bind to p53 and E6AP and to induce degradation of the p53 protein in the reticulocyte system.
467	1538	bind	p53	E6	Of all four proteins investigated, only HPV16 E6 was able to bind to p53 and E6AP and to induce degradation of the p53 protein in the reticulocyte system.
468	1539	bind	E6	p53	Of its gene products, E6 binds to and inactivates p53 tumor suppressor protein by ubiquitin/proteasome-dependent degradation.
468	1540	bind	p53	E6	Of its gene products, E6 binds to and inactivates p53 tumor suppressor protein by ubiquitin/proteasome-dependent degradation.
469	1541	interact	CUL1	SKR-1	Of the 17 SKR proteins examined, eight (SKR-1, -2, -3, -4, -7, -8, -9, and -10) were shown to interact with C. elegans CUL1 by yeast two-hybrid analysis or a coimmunoprecipitation assay in mammalian cells.
469	1542	interact	CUL1	SKR-10	Of the 17 SKR proteins examined, eight (SKR-1, -2, -3, -4, -7, -8, -9, and -10) were shown to interact with C. elegans CUL1 by yeast two-hybrid analysis or a coimmunoprecipitation assay in mammalian cells.
469	1543	interact	CUL1	SKR-2	Of the 17 SKR proteins examined, eight (SKR-1, -2, -3, -4, -7, -8, -9, and -10) were shown to interact with C. elegans CUL1 by yeast two-hybrid analysis or a coimmunoprecipitation assay in mammalian cells.
469	1544	interact	CUL1	SKR-3	Of the 17 SKR proteins examined, eight (SKR-1, -2, -3, -4, -7, -8, -9, and -10) were shown to interact with C. elegans CUL1 by yeast two-hybrid analysis or a coimmunoprecipitation assay in mammalian cells.
469	1545	interact	CUL1	SKR-4	Of the 17 SKR proteins examined, eight (SKR-1, -2, -3, -4, -7, -8, -9, and -10) were shown to interact with C. elegans CUL1 by yeast two-hybrid analysis or a coimmunoprecipitation assay in mammalian cells.
469	1546	interact	CUL1	SKR-7	Of the 17 SKR proteins examined, eight (SKR-1, -2, -3, -4, -7, -8, -9, and -10) were shown to interact with C. elegans CUL1 by yeast two-hybrid analysis or a coimmunoprecipitation assay in mammalian cells.
469	1547	interact	CUL1	SKR-8	Of the 17 SKR proteins examined, eight (SKR-1, -2, -3, -4, -7, -8, -9, and -10) were shown to interact with C. elegans CUL1 by yeast two-hybrid analysis or a coimmunoprecipitation assay in mammalian cells.
469	1548	interact	CUL1	SKR-9	Of the 17 SKR proteins examined, eight (SKR-1, -2, -3, -4, -7, -8, -9, and -10) were shown to interact with C. elegans CUL1 by yeast two-hybrid analysis or a coimmunoprecipitation assay in mammalian cells.
469	1549	interact	SKR-1	CUL1	Of the 17 SKR proteins examined, eight (SKR-1, -2, -3, -4, -7, -8, -9, and -10) were shown to interact with C. elegans CUL1 by yeast two-hybrid analysis or a coimmunoprecipitation assay in mammalian cells.
469	1550	interact	SKR-10	CUL1	Of the 17 SKR proteins examined, eight (SKR-1, -2, -3, -4, -7, -8, -9, and -10) were shown to interact with C. elegans CUL1 by yeast two-hybrid analysis or a coimmunoprecipitation assay in mammalian cells.
469	1551	interact	SKR-2	CUL1	Of the 17 SKR proteins examined, eight (SKR-1, -2, -3, -4, -7, -8, -9, and -10) were shown to interact with C. elegans CUL1 by yeast two-hybrid analysis or a coimmunoprecipitation assay in mammalian cells.
469	1552	interact	SKR-3	CUL1	Of the 17 SKR proteins examined, eight (SKR-1, -2, -3, -4, -7, -8, -9, and -10) were shown to interact with C. elegans CUL1 by yeast two-hybrid analysis or a coimmunoprecipitation assay in mammalian cells.
469	1553	interact	SKR-4	CUL1	Of the 17 SKR proteins examined, eight (SKR-1, -2, -3, -4, -7, -8, -9, and -10) were shown to interact with C. elegans CUL1 by yeast two-hybrid analysis or a coimmunoprecipitation assay in mammalian cells.
469	1554	interact	SKR-7	CUL1	Of the 17 SKR proteins examined, eight (SKR-1, -2, -3, -4, -7, -8, -9, and -10) were shown to interact with C. elegans CUL1 by yeast two-hybrid analysis or a coimmunoprecipitation assay in mammalian cells.
469	1555	interact	SKR-8	CUL1	Of the 17 SKR proteins examined, eight (SKR-1, -2, -3, -4, -7, -8, -9, and -10) were shown to interact with C. elegans CUL1 by yeast two-hybrid analysis or a coimmunoprecipitation assay in mammalian cells.
469	1556	interact	SKR-9	CUL1	Of the 17 SKR proteins examined, eight (SKR-1, -2, -3, -4, -7, -8, -9, and -10) were shown to interact with C. elegans CUL1 by yeast two-hybrid analysis or a coimmunoprecipitation assay in mammalian cells.
470	1557	binding	FWD1	Skp1	On the other hand, the highly conserved residues Pro(149), Ile(160), and Leu(164) in the F-box domain of FWD1 were dispensable for binding to Skp1.
470	1558	binding	Skp1	FWD1	On the other hand, the highly conserved residues Pro(149), Ile(160), and Leu(164) in the F-box domain of FWD1 were dispensable for binding to Skp1.
471	1559	bind	Skp2	p27	One component, the F-box protein Skp2, binds p27 when phosphorylated on Thr187, thus providing substrate specificity for the ligase.
471	1560	bind	p27	Skp2	One component, the F-box protein Skp2, binds p27 when phosphorylated on Thr187, thus providing substrate specificity for the ligase.
472	1561	binding	Cul2	pVHL	One model, which remains to be tested, is that the binding of pVHL to elongins B/C and Cul2 affects the ubiquitination of RNA-binding proteins that regulate the stability of hypoxia-inducible mRNAs.
472	1562	binding	elongin B	pVHL	One model, which remains to be tested, is that the binding of pVHL to elongins B/C and Cul2 affects the ubiquitination of RNA-binding proteins that regulate the stability of hypoxia-inducible mRNAs.
472	1563	binding	elongin C	pVHL	One model, which remains to be tested, is that the binding of pVHL to elongins B/C and Cul2 affects the ubiquitination of RNA-binding proteins that regulate the stability of hypoxia-inducible mRNAs.
472	1564	binding	pVHL	Cul2	One model, which remains to be tested, is that the binding of pVHL to elongins B/C and Cul2 affects the ubiquitination of RNA-binding proteins that regulate the stability of hypoxia-inducible mRNAs.
472	1565	binding	pVHL	elongin B	One model, which remains to be tested, is that the binding of pVHL to elongins B/C and Cul2 affects the ubiquitination of RNA-binding proteins that regulate the stability of hypoxia-inducible mRNAs.
472	1566	binding	pVHL	elongin C	One model, which remains to be tested, is that the binding of pVHL to elongins B/C and Cul2 affects the ubiquitination of RNA-binding proteins that regulate the stability of hypoxia-inducible mRNAs.
473	1567	conjugation	H2A	ubiquitin	One of these activities supported conjugation of ubiquitin to histone H2A, a substrate degraded in the ubiquitin system by a non-N-end rule mechanism.
473	1568	conjugation	ubiquitin	H2A	One of these activities supported conjugation of ubiquitin to histone H2A, a substrate degraded in the ubiquitin system by a non-N-end rule mechanism.
474	1569	binding	Pop1p	Pop2p	Only the F-box of Pop1p is required for SCFPop1p-Pop2p function, while Pop2p seems to be attracted into the complex through binding to Pop1p.
474	1570	binding	Pop2p	Pop1p	Only the F-box of Pop1p is required for SCFPop1p-Pop2p function, while Pop2p seems to be attracted into the complex through binding to Pop1p.
475	1571	complex	elongin B	elongin C	Only when pVHL and elongins B and C (VBC) are present does an interaction with the cullin family member, hCUL-2, occur, forming the heterotetrameric pVHL/elongin BC/hCUL-2 complex.
475	1572	complex	elongin B	hCUL-2	Only when pVHL and elongins B and C (VBC) are present does an interaction with the cullin family member, hCUL-2, occur, forming the heterotetrameric pVHL/elongin BC/hCUL-2 complex.
475	1573	complex	elongin B	pVHL	Only when pVHL and elongins B and C (VBC) are present does an interaction with the cullin family member, hCUL-2, occur, forming the heterotetrameric pVHL/elongin BC/hCUL-2 complex.
475	1574	complex	elongin C	elongin B	Only when pVHL and elongins B and C (VBC) are present does an interaction with the cullin family member, hCUL-2, occur, forming the heterotetrameric pVHL/elongin BC/hCUL-2 complex.
475	1575	complex	elongin C	hCUL-2	Only when pVHL and elongins B and C (VBC) are present does an interaction with the cullin family member, hCUL-2, occur, forming the heterotetrameric pVHL/elongin BC/hCUL-2 complex.
475	1576	complex	elongin C	pVHL	Only when pVHL and elongins B and C (VBC) are present does an interaction with the cullin family member, hCUL-2, occur, forming the heterotetrameric pVHL/elongin BC/hCUL-2 complex.
475	1577	complex	hCUL-2	elongin B	Only when pVHL and elongins B and C (VBC) are present does an interaction with the cullin family member, hCUL-2, occur, forming the heterotetrameric pVHL/elongin BC/hCUL-2 complex.
475	1578	complex	hCUL-2	elongin C	Only when pVHL and elongins B and C (VBC) are present does an interaction with the cullin family member, hCUL-2, occur, forming the heterotetrameric pVHL/elongin BC/hCUL-2 complex.
475	1579	complex	hCUL-2	pVHL	Only when pVHL and elongins B and C (VBC) are present does an interaction with the cullin family member, hCUL-2, occur, forming the heterotetrameric pVHL/elongin BC/hCUL-2 complex.
475	1580	complex	pVHL	elongin B	Only when pVHL and elongins B and C (VBC) are present does an interaction with the cullin family member, hCUL-2, occur, forming the heterotetrameric pVHL/elongin BC/hCUL-2 complex.
475	1581	complex	pVHL	elongin C	Only when pVHL and elongins B and C (VBC) are present does an interaction with the cullin family member, hCUL-2, occur, forming the heterotetrameric pVHL/elongin BC/hCUL-2 complex.
475	1582	complex	pVHL	hCUL-2	Only when pVHL and elongins B and C (VBC) are present does an interaction with the cullin family member, hCUL-2, occur, forming the heterotetrameric pVHL/elongin BC/hCUL-2 complex.
476	1583	modification	PML	SUMO-1	Our findings identify the basic requirements for ND10 formation and suggest a dynamic mechanism for protein recruitment to these nuclear domains controlled by the SUMO-1 modification state of PML.
476	1584	modification	SUMO-1	PML	Our findings identify the basic requirements for ND10 formation and suggest a dynamic mechanism for protein recruitment to these nuclear domains controlled by the SUMO-1 modification state of PML.
477	1585	ubiquitinate	IkappaBalpha	betaTrCP	Our findings indicate that betaTrCP is the adaptor protein required for IkappaBalpha recognition by the SCFbetaTrCP E3 complex that ubiquitinates IkappaBalpha and makes it a substrate for the proteasome.
477	1586	ubiquitinate	betaTrCP	IkappaBalpha	Our findings indicate that betaTrCP is the adaptor protein required for IkappaBalpha recognition by the SCFbetaTrCP E3 complex that ubiquitinates IkappaBalpha and makes it a substrate for the proteasome.
478	1587	conjugation	CUL1	RUB	Our previous studies showed that conjugation of RUB to CUL1 is required for normal SCF(TIR1) function.
478	1588	conjugation	RUB	CUL1	Our previous studies showed that conjugation of RUB to CUL1 is required for normal SCF(TIR1) function.
479	1589	associate	Cul-4A	DDB2	Our previous study indicated that the cullin family protein Cul-4A associates with the DDB2 subunit.
479	1590	associate	DDB2	Cul-4A	Our previous study indicated that the cullin family protein Cul-4A associates with the DDB2 subunit.
480	1591	binding	CDK2	Xic1	Our results also indicate that binding of Xic1 to CDK2-cyclin E is dispensable for Xic1 ubiquitination and degradation.
480	1592	binding	Xic1	CDK2	Our results also indicate that binding of Xic1 to CDK2-cyclin E is dispensable for Xic1 ubiquitination and degradation.
480	1593	binding	Xic1	cyclin E	Our results also indicate that binding of Xic1 to CDK2-cyclin E is dispensable for Xic1 ubiquitination and degradation.
480	1594	binding	cyclin E	Xic1	Our results also indicate that binding of Xic1 to CDK2-cyclin E is dispensable for Xic1 ubiquitination and degradation.
481	1595	transfer	I kappa B alpha	ubiquitin	Our results also suggest that ubiquitin is transferred directly from the Ubc to phospho-I kappa B alpha in a SCF beta-TRCP dependent reaction.
481	1596	transfer	Ubc	ubiquitin	Our results also suggest that ubiquitin is transferred directly from the Ubc to phospho-I kappa B alpha in a SCF beta-TRCP dependent reaction.
481	1597	transfer	ubiquitin	I kappa B alpha	Our results also suggest that ubiquitin is transferred directly from the Ubc to phospho-I kappa B alpha in a SCF beta-TRCP dependent reaction.
481	1598	transfer	ubiquitin	Ubc	Our results also suggest that ubiquitin is transferred directly from the Ubc to phospho-I kappa B alpha in a SCF beta-TRCP dependent reaction.
482	1599	ubiquitinate	Fbx2	N-glycosylated proteins	Our results indicate that SCF(Fbx2) ubiquitinates N-glycosylated proteins that are translocated from the ER to the cytosol by the quality control mechanism.
482	1600	ubiquitinate	N-glycosylated proteins	Fbx2	Our results indicate that SCF(Fbx2) ubiquitinates N-glycosylated proteins that are translocated from the ER to the cytosol by the quality control mechanism.
483	1601	phosphorylation	APC	Cdc2	Our results indicate that p9 directly regulates the phosphorylation of the APC by Cdc2/cyclin B. These studies indicate that the Suc1/Cks protein modulates substrate recognition by a cyclin-dependent kinase.
483	1602	phosphorylation	APC	cyclin B	Our results indicate that p9 directly regulates the phosphorylation of the APC by Cdc2/cyclin B. These studies indicate that the Suc1/Cks protein modulates substrate recognition by a cyclin-dependent kinase.
483	1603	phosphorylation	Cdc2	APC	Our results indicate that p9 directly regulates the phosphorylation of the APC by Cdc2/cyclin B. These studies indicate that the Suc1/Cks protein modulates substrate recognition by a cyclin-dependent kinase.
483	1604	regulate	Cdc2	p9	Our results indicate that p9 directly regulates the phosphorylation of the APC by Cdc2/cyclin B. These studies indicate that the Suc1/Cks protein modulates substrate recognition by a cyclin-dependent kinase.
483	1605	phosphorylation	cyclin B	APC	Our results indicate that p9 directly regulates the phosphorylation of the APC by Cdc2/cyclin B. These studies indicate that the Suc1/Cks protein modulates substrate recognition by a cyclin-dependent kinase.
483	1606	regulate	cyclin B	p9	Our results indicate that p9 directly regulates the phosphorylation of the APC by Cdc2/cyclin B. These studies indicate that the Suc1/Cks protein modulates substrate recognition by a cyclin-dependent kinase.
483	1607	regulate	p9	Cdc2	Our results indicate that p9 directly regulates the phosphorylation of the APC by Cdc2/cyclin B. These studies indicate that the Suc1/Cks protein modulates substrate recognition by a cyclin-dependent kinase.
483	1608	regulate	p9	cyclin B	Our results indicate that p9 directly regulates the phosphorylation of the APC by Cdc2/cyclin B. These studies indicate that the Suc1/Cks protein modulates substrate recognition by a cyclin-dependent kinase.
484	1609	modification	PML	SUMO-1	Our results provide significant insights into the role of SUMO-1 modification of PML in both normal cells and the APL disease state.
484	1610	modification	SUMO-1	PML	Our results provide significant insights into the role of SUMO-1 modification of PML in both normal cells and the APL disease state.
485	1611	interaction	Cdc23	Clb2	Our results provide the first evidence for a direct interaction between an APC/C substrate (Clb2) and an APC/C subunit (Cdc23).
485	1612	interaction	Clb2	Cdc23	Our results provide the first evidence for a direct interaction between an APC/C substrate (Clb2) and an APC/C subunit (Cdc23).
486	1613	phosphorylation	Cdc28p	Far1p	Our results show that Far1p is regulated by ubiquitin-mediated proteolysis and suggest that phosphorylation of Far1p by the Cdc28p-Clnp kinase is part of the recognition signal for ubiquitination.
486	1614	phosphorylation	Clnp	Far1p	Our results show that Far1p is regulated by ubiquitin-mediated proteolysis and suggest that phosphorylation of Far1p by the Cdc28p-Clnp kinase is part of the recognition signal for ubiquitination.
486	1615	phosphorylation	Far1p	Cdc28p	Our results show that Far1p is regulated by ubiquitin-mediated proteolysis and suggest that phosphorylation of Far1p by the Cdc28p-Clnp kinase is part of the recognition signal for ubiquitination.
486	1616	phosphorylation	Far1p	Clnp	Our results show that Far1p is regulated by ubiquitin-mediated proteolysis and suggest that phosphorylation of Far1p by the Cdc28p-Clnp kinase is part of the recognition signal for ubiquitination.
487	1617	interaction	ASK1	UFO	Our results suggest that ASK1 interacts with UFO to control floral organ identity in whorls 2 and 3.
487	1618	interaction	UFO	ASK1	Our results suggest that ASK1 interacts with UFO to control floral organ identity in whorls 2 and 3.
488	1619	interaction	TAF(II)31	p53	Our results suggest that direct interaction of TAF(II)31 and p53 not only mediates p53 transcriptional activation but also protects p53 from mdm2-mediated degradation, thereby resulting in activation of p53 functions.
488	1620	interaction	p53	TAF(II)31	Our results suggest that direct interaction of TAF(II)31 and p53 not only mediates p53 transcriptional activation but also protects p53 from mdm2-mediated degradation, thereby resulting in activation of p53 functions.
489	1621	bound	APC	hCDC20	Our results suggest that the association between hCDH1 and APC is regulated by post-translational mechanisms, whereas the amount of hCDC20 bound to APC may in addition be controlled by hCDC20 synthesis and destruction.
489	1622	associate	APC	hCDH1	Our results suggest that the association between hCDH1 and APC is regulated by post-translational mechanisms, whereas the amount of hCDC20 bound to APC may in addition be controlled by hCDC20 synthesis and destruction.
489	1623	bound	hCDC20	APC	Our results suggest that the association between hCDH1 and APC is regulated by post-translational mechanisms, whereas the amount of hCDC20 bound to APC may in addition be controlled by hCDC20 synthesis and destruction.
489	1624	associate	hCDH1	APC	Our results suggest that the association between hCDH1 and APC is regulated by post-translational mechanisms, whereas the amount of hCDC20 bound to APC may in addition be controlled by hCDC20 synthesis and destruction.
490	1625	associate	Rbx1	SCF	Our results suggest that the cullin specificity of the SCF complex may reflect its ability to associate with Rbx1.
490	1626	associate	SCF	Rbx1	Our results suggest that the cullin specificity of the SCF complex may reflect its ability to associate with Rbx1.
491	1627	bind	TEL	UBC9	Our studies show that UBC9 binds to TEL exclusively through the HLH domain of TEL.
491	1628	bind	UBC9	TEL	Our studies show that UBC9 binds to TEL exclusively through the HLH domain of TEL.
492	1629	binding	BAG-1M	Hsc70	Our study demonstrates that both N-terminal DNA binding site and C-terminal Hsp70/Hsc70 binding site of BAG-1M play an important role in enhancing the CMV promoter activity.
492	1630	binding	BAG-1M	Hsp70	Our study demonstrates that both N-terminal DNA binding site and C-terminal Hsp70/Hsc70 binding site of BAG-1M play an important role in enhancing the CMV promoter activity.
492	1631	binding	Hsc70	BAG-1M	Our study demonstrates that both N-terminal DNA binding site and C-terminal Hsp70/Hsc70 binding site of BAG-1M play an important role in enhancing the CMV promoter activity.
492	1632	binding	Hsp70	BAG-1M	Our study demonstrates that both N-terminal DNA binding site and C-terminal Hsp70/Hsc70 binding site of BAG-1M play an important role in enhancing the CMV promoter activity.
493	1633	disruption	Atrogin-1	PDZ-binding	Overexpression of the Cdk4/6-specific Cdk inhibitor of Cdk4 p16(INK4A) was associated with increased association of p27(KIP1) with Cdk2, concomitant with disruption of D cyclin/Cdk4 complexes.
493	1634	association	Cdk2	KIP1	Overexpression of the Cdk4/6-specific Cdk inhibitor of Cdk4 p16(INK4A) was associated with increased association of p27(KIP1) with Cdk2, concomitant with disruption of D cyclin/Cdk4 complexes.
493	1635	association	Cdk2	p27	Overexpression of the Cdk4/6-specific Cdk inhibitor of Cdk4 p16(INK4A) was associated with increased association of p27(KIP1) with Cdk2, concomitant with disruption of D cyclin/Cdk4 complexes.
493	1636	inhibitor	Cdk4	INK4A	Overexpression of the Cdk4/6-specific Cdk inhibitor of Cdk4 p16(INK4A) was associated with increased association of p27(KIP1) with Cdk2, concomitant with disruption of D cyclin/Cdk4 complexes.
493	1637	complex	Cdk4	cyclin D	Overexpression of the Cdk4/6-specific Cdk inhibitor of Cdk4 p16(INK4A) was associated with increased association of p27(KIP1) with Cdk2, concomitant with disruption of D cyclin/Cdk4 complexes.
493	1638	inhibitor	INK4A	Cdk4	Overexpression of the Cdk4/6-specific Cdk inhibitor of Cdk4 p16(INK4A) was associated with increased association of p27(KIP1) with Cdk2, concomitant with disruption of D cyclin/Cdk4 complexes.
493	1639	association	KIP1	Cdk2	Overexpression of the Cdk4/6-specific Cdk inhibitor of Cdk4 p16(INK4A) was associated with increased association of p27(KIP1) with Cdk2, concomitant with disruption of D cyclin/Cdk4 complexes.
493	1640	disruption	PDZ-binding	Atrogin-1	Overexpression of the Cdk4/6-specific Cdk inhibitor of Cdk4 p16(INK4A) was associated with increased association of p27(KIP1) with Cdk2, concomitant with disruption of D cyclin/Cdk4 complexes.
493	1641	complex	cyclin D	Cdk4	Overexpression of the Cdk4/6-specific Cdk inhibitor of Cdk4 p16(INK4A) was associated with increased association of p27(KIP1) with Cdk2, concomitant with disruption of D cyclin/Cdk4 complexes.
493	1642	association	p27	Cdk2	Overexpression of the Cdk4/6-specific Cdk inhibitor of Cdk4 p16(INK4A) was associated with increased association of p27(KIP1) with Cdk2, concomitant with disruption of D cyclin/Cdk4 complexes.
494	1643	activate	HKDA	PCMB	PCMB, TLCK and TPCK suppress hexokinase and activate HKDA.
494	1644	activate	HKDA	TLCK	PCMB, TLCK and TPCK suppress hexokinase and activate HKDA.
494	1645	activate	HKDA	TPCK	PCMB, TLCK and TPCK suppress hexokinase and activate HKDA.
494	1646	activate	PCMB	HKDA	PCMB, TLCK and TPCK suppress hexokinase and activate HKDA.
494	1647	suppress	PCMB	hexokinase	PCMB, TLCK and TPCK suppress hexokinase and activate HKDA.
494	1648	activate	TLCK	HKDA	PCMB, TLCK and TPCK suppress hexokinase and activate HKDA.
494	1649	suppress	TLCK	hexokinase	PCMB, TLCK and TPCK suppress hexokinase and activate HKDA.
494	1650	activate	TPCK	HKDA	PCMB, TLCK and TPCK suppress hexokinase and activate HKDA.
494	1651	suppress	TPCK	hexokinase	PCMB, TLCK and TPCK suppress hexokinase and activate HKDA.
494	1652	suppress	hexokinase	PCMB	PCMB, TLCK and TPCK suppress hexokinase and activate HKDA.
494	1653	suppress	hexokinase	TLCK	PCMB, TLCK and TPCK suppress hexokinase and activate HKDA.
494	1654	suppress	hexokinase	TPCK	PCMB, TLCK and TPCK suppress hexokinase and activate HKDA.
495	1655	poly-ubiquitinate	MMS2	PCNA	PCNA is mono-ubiquitinated through RAD6 and RAD18, modified by lysine-63-linked multi-ubiquitination which additionally requires MMS2, UBC13 and RAD5, and is conjugated to SUMO by UBC9.
495	1656	poly-ubiquitinate	PCNA	MMS2	PCNA is mono-ubiquitinated through RAD6 and RAD18, modified by lysine-63-linked multi-ubiquitination which additionally requires MMS2, UBC13 and RAD5, and is conjugated to SUMO by UBC9.
495	1657	mono-ubiquitinate	PCNA	RAD18	PCNA is mono-ubiquitinated through RAD6 and RAD18, modified by lysine-63-linked multi-ubiquitination which additionally requires MMS2, UBC13 and RAD5, and is conjugated to SUMO by UBC9.
495	1658	poly-ubiquitinate	PCNA	RAD5	PCNA is mono-ubiquitinated through RAD6 and RAD18, modified by lysine-63-linked multi-ubiquitination which additionally requires MMS2, UBC13 and RAD5, and is conjugated to SUMO by UBC9.
495	1659	mono-ubiquitinate	PCNA	RAD6	PCNA is mono-ubiquitinated through RAD6 and RAD18, modified by lysine-63-linked multi-ubiquitination which additionally requires MMS2, UBC13 and RAD5, and is conjugated to SUMO by UBC9.
495	1660	conjugate	PCNA	SUMO	PCNA is mono-ubiquitinated through RAD6 and RAD18, modified by lysine-63-linked multi-ubiquitination which additionally requires MMS2, UBC13 and RAD5, and is conjugated to SUMO by UBC9.
495	1661	poly-ubiquitinate	PCNA	UBC13	PCNA is mono-ubiquitinated through RAD6 and RAD18, modified by lysine-63-linked multi-ubiquitination which additionally requires MMS2, UBC13 and RAD5, and is conjugated to SUMO by UBC9.
495	1662	mono-ubiquitinate	RAD18	PCNA	PCNA is mono-ubiquitinated through RAD6 and RAD18, modified by lysine-63-linked multi-ubiquitination which additionally requires MMS2, UBC13 and RAD5, and is conjugated to SUMO by UBC9.
495	1663	poly-ubiquitinate	RAD5	PCNA	PCNA is mono-ubiquitinated through RAD6 and RAD18, modified by lysine-63-linked multi-ubiquitination which additionally requires MMS2, UBC13 and RAD5, and is conjugated to SUMO by UBC9.
495	1664	mono-ubiquitinate	RAD6	PCNA	PCNA is mono-ubiquitinated through RAD6 and RAD18, modified by lysine-63-linked multi-ubiquitination which additionally requires MMS2, UBC13 and RAD5, and is conjugated to SUMO by UBC9.
495	1665	conjugate	SUMO	PCNA	PCNA is mono-ubiquitinated through RAD6 and RAD18, modified by lysine-63-linked multi-ubiquitination which additionally requires MMS2, UBC13 and RAD5, and is conjugated to SUMO by UBC9.
495	1666	conjugate	SUMO	UBC9	PCNA is mono-ubiquitinated through RAD6 and RAD18, modified by lysine-63-linked multi-ubiquitination which additionally requires MMS2, UBC13 and RAD5, and is conjugated to SUMO by UBC9.
495	1667	poly-ubiquitinate	UBC13	PCNA	PCNA is mono-ubiquitinated through RAD6 and RAD18, modified by lysine-63-linked multi-ubiquitination which additionally requires MMS2, UBC13 and RAD5, and is conjugated to SUMO by UBC9.
495	1668	conjugate	UBC9	SUMO	PCNA is mono-ubiquitinated through RAD6 and RAD18, modified by lysine-63-linked multi-ubiquitination which additionally requires MMS2, UBC13 and RAD5, and is conjugated to SUMO by UBC9.
496	1669	bound	PIAS1	Ubc9	PIAS1 and PIASxalpha bound Ubc9, the E2 enzyme for SUMO-1, in a RING finger-like domain-dependent manner.
496	1670	bound	PIASxalpha	Ubc9	PIAS1 and PIASxalpha bound Ubc9, the E2 enzyme for SUMO-1, in a RING finger-like domain-dependent manner.
496	1671	bound	Ubc9	PIAS1	PIAS1 and PIASxalpha bound Ubc9, the E2 enzyme for SUMO-1, in a RING finger-like domain-dependent manner.
496	1672	bound	Ubc9	PIASxalpha	PIAS1 and PIASxalpha bound Ubc9, the E2 enzyme for SUMO-1, in a RING finger-like domain-dependent manner.
497	1673	interact	PIC1	PML	PIC1 was shown to interact with the PML component of nuclear multiprotein complex that is disrupted in acute promyelocytic leukemia (9).
497	1674	interact	PML	PIC1	PIC1 was shown to interact with the PML component of nuclear multiprotein complex that is disrupted in acute promyelocytic leukemia (9).
498	1675	complexed	XPC	mHR23B	Part of mHR23B is complexed with the XPC protein, and this heterodimer functions as the main damage detector and initiator of global genome NER.
498	1676	complexed	mHR23B	XPC	Part of mHR23B is complexed with the XPC protein, and this heterodimer functions as the main damage detector and initiator of global genome NER.
499	1677	associate	Png1p	Rad23p	Particularly the recently identified inhibition of degradation by mouse Rad23 protein (mHR23) of the associated nucleotide excision repair protein XPC was shown to stimulate DNA repair.Recently, it was shown that Rad23p and the mouse homologue mHR23B also associate with Png1p, a deglycosylation enzyme.
499	1678	associate	Png1p	mHR23B	Particularly the recently identified inhibition of degradation by mouse Rad23 protein (mHR23) of the associated nucleotide excision repair protein XPC was shown to stimulate DNA repair.Recently, it was shown that Rad23p and the mouse homologue mHR23B also associate with Png1p, a deglycosylation enzyme.
499	1679	associate	Rad23p	Png1p	Particularly the recently identified inhibition of degradation by mouse Rad23 protein (mHR23) of the associated nucleotide excision repair protein XPC was shown to stimulate DNA repair.Recently, it was shown that Rad23p and the mouse homologue mHR23B also associate with Png1p, a deglycosylation enzyme.
499	1680	associate	mHR23B	Png1p	Particularly the recently identified inhibition of degradation by mouse Rad23 protein (mHR23) of the associated nucleotide excision repair protein XPC was shown to stimulate DNA repair.Recently, it was shown that Rad23p and the mouse homologue mHR23B also associate with Png1p, a deglycosylation enzyme.
500	1681	binding	BE6	Paxillin	Paxillin binding to BE6 excludes simultaneous binding to E6-AP.
500	1682	binding	Paxillin	BE6	Paxillin binding to BE6 excludes simultaneous binding to E6-AP.
501	1683	modified	NEDD8	Pcu1	Pcu1 assembled on SCF ubiquitin-ligase was completely modified by NEDD8.
501	1684	modified	Pcu1	NEDD8	Pcu1 assembled on SCF ubiquitin-ligase was completely modified by NEDD8.
502	1685	modified	Ned8p	Pcu3p	Pcu3p is modified by Ned8p on Lys 729 and accumulates exclusively in the neddylated form in cells lacking the CSN subunits 1, 3, 4, and 5.
502	1686	modified	Pcu3p	Ned8p	Pcu3p is modified by Ned8p on Lys 729 and accumulates exclusively in the neddylated form in cells lacking the CSN subunits 1, 3, 4, and 5.
503	1687	interact	Pex22p	Pex4p	Pex22p interacts with the ubiquitin-conjugating enzyme Pex4p, a peripheral peroxisomal membrane protein, in vivo, and in a yeast two-hybrid experiment.
503	1688	interact	Pex4p	Pex22p	Pex22p interacts with the ubiquitin-conjugating enzyme Pex4p, a peripheral peroxisomal membrane protein, in vivo, and in a yeast two-hybrid experiment.
504	1689	bind	betaTrCP	p105	Phosphopeptide competition experiments indicate that betaTrCP binds p105 more effectively when both serines 927 and 932 are phosphorylated.
504	1690	bind	p105	betaTrCP	Phosphopeptide competition experiments indicate that betaTrCP binds p105 more effectively when both serines 927 and 932 are phosphorylated.
505	1691	ubiquitinate	Cln1	Grr1	Phosphorylated Cln1 and Cln2 are ubiquitinated by the SCF-Grr1 complex and then degraded by the 26 S proteasome.
505	1692	ubiquitinate	Cln2	Grr1	Phosphorylated Cln1 and Cln2 are ubiquitinated by the SCF-Grr1 complex and then degraded by the 26 S proteasome.
505	1693	ubiquitinate	Grr1	Cln1	Phosphorylated Cln1 and Cln2 are ubiquitinated by the SCF-Grr1 complex and then degraded by the 26 S proteasome.
505	1694	ubiquitinate	Grr1	Cln2	Phosphorylated Cln1 and Cln2 are ubiquitinated by the SCF-Grr1 complex and then degraded by the 26 S proteasome.
506	1695	ubiquitinate	Cln1	Grr1	Phosphorylated Cln1 was ubiquitinated by SCF (Skp1-Cdc53-F-box protein) complexes containing the F-box protein Grr1, Rbx1, and the E2 Cdc34.
506	1696	ubiquitinate	Grr1	Cln1	Phosphorylated Cln1 was ubiquitinated by SCF (Skp1-Cdc53-F-box protein) complexes containing the F-box protein Grr1, Rbx1, and the E2 Cdc34.
507	1697	interaction	APC	Hct1	Phosphorylation of Hct1 by CDKs blocked the Hct1-APC interaction.
507	1698	Phosphorylation	CDKs	Hct1	Phosphorylation of Hct1 by CDKs blocked the Hct1-APC interaction.
507	1699	interaction	Hct1	APC	Phosphorylation of Hct1 by CDKs blocked the Hct1-APC interaction.
507	1700	Phosphorylation	Hct1	CDKs	Phosphorylation of Hct1 by CDKs blocked the Hct1-APC interaction.
508	1701	inhibitor	IkappaB	NF-kappaB	Phosphorylation of NF-kappaB inhibitor (IkappaB) by respective stress-inducible kinases (IKK) is a key event in NF-kappaB activation. beta-TrCP F-box protein mediates ubiquitination of phosphorylated IkappaB via recruitment of SCF(beta-TrCP)-Roc1 E3 ubiquitin ligase complex.
508	1702	inhibitor	NF-kappaB	IkappaB	Phosphorylation of NF-kappaB inhibitor (IkappaB) by respective stress-inducible kinases (IKK) is a key event in NF-kappaB activation. beta-TrCP F-box protein mediates ubiquitination of phosphorylated IkappaB via recruitment of SCF(beta-TrCP)-Roc1 E3 ubiquitin ligase complex.
509	1703	phosphorylation	Cdc28	Pds1	Phosphorylation of Pds1 by Cdc28 is important for efficient binding of Pds1 to Esp1 and for promoting the nuclear localization of Esp1.
509	1704	binding	Esp1	Pds1	Phosphorylation of Pds1 by Cdc28 is important for efficient binding of Pds1 to Esp1 and for promoting the nuclear localization of Esp1.
509	1705	phosphorylation	Pds1	Cdc28	Phosphorylation of Pds1 by Cdc28 is important for efficient binding of Pds1 to Esp1 and for promoting the nuclear localization of Esp1.
509	1706	binding	Pds1	Esp1	Phosphorylation of Pds1 by Cdc28 is important for efficient binding of Pds1 to Esp1 and for promoting the nuclear localization of Esp1.
510	1707	ubiquitinate	H2B	Rad6	Preferential accessibility is independent of the Swi-Snf chromatin remodeling complex, Gcn5 histone acetylase complexes Ada and SAGA, and Rad6, which ubiquitinates histone H2B.
510	1708	ubiquitinate	Rad6	H2B	Preferential accessibility is independent of the Swi-Snf chromatin remodeling complex, Gcn5 histone acetylase complexes Ada and SAGA, and Rad6, which ubiquitinates histone H2B.
511	1709	phosphorylate	APC	Cdc5	Previous reports have shown that the budding yeast Cdc5 homologue, Plk, can also phosphorylate and activate the APC in vitro.
511	1710	phosphorylate	APC	Plk	Previous reports have shown that the budding yeast Cdc5 homologue, Plk, can also phosphorylate and activate the APC in vitro.
511	1711	phosphorylate	Cdc5	APC	Previous reports have shown that the budding yeast Cdc5 homologue, Plk, can also phosphorylate and activate the APC in vitro.
511	1712	phosphorylate	Plk	APC	Previous reports have shown that the budding yeast Cdc5 homologue, Plk, can also phosphorylate and activate the APC in vitro.
512	1713	associate	55K	ND10	Previous studies have shown that, during wild-type infection, 55K associates initially with structures termed ND10, which are sites of localization of the promyelocytic leukaemia protein, and then moves, dependent upon its interaction with Orf6, to the establishing virus replication centres.
512	1714	associate	ND10	55K	Previous studies have shown that, during wild-type infection, 55K associates initially with structures termed ND10, which are sites of localization of the promyelocytic leukaemia protein, and then moves, dependent upon its interaction with Orf6, to the establishing virus replication centres.
513	1715	conjugation	histone	ubiquitin	Protein expressed in Escherichia coli by the E2(23 kDa) cDNA was capable of both thiol ester adduct formation and conjugation of ubiquitin to histones.
513	1716	conjugation	ubiquitin	histone	Protein expressed in Escherichia coli by the E2(23 kDa) cDNA was capable of both thiol ester adduct formation and conjugation of ubiquitin to histones.
514	1717	bind	BubR1	Cdc20	Purified BubR1 binds to recombinant Cdc20 and this interaction is direct.
514	1718	bind	Cdc20	BubR1	Purified BubR1 binds to recombinant Cdc20 and this interaction is direct.
515	1719	activate	APC	Hct1	Purified Hct1 was phosphorylated in vitro at these sites by purified Cdc28-cyclin complexes, and phosphorylation abolished the ability of Hct1 to activate the APC in vitro.
515	1720	phosphorylate	Cdc28	Hct1	Purified Hct1 was phosphorylated in vitro at these sites by purified Cdc28-cyclin complexes, and phosphorylation abolished the ability of Hct1 to activate the APC in vitro.
515	1721	activate	Hct1	APC	Purified Hct1 was phosphorylated in vitro at these sites by purified Cdc28-cyclin complexes, and phosphorylation abolished the ability of Hct1 to activate the APC in vitro.
515	1722	phosphorylate	Hct1	Cdc28	Purified Hct1 was phosphorylated in vitro at these sites by purified Cdc28-cyclin complexes, and phosphorylation abolished the ability of Hct1 to activate the APC in vitro.
516	1723	modify	Cul1	NEDD8	Purified centrosomes also contain Skp1, and Cul1 modified by the ubiquitin-like molecule NEDD8, suggesting a role for NEDD8 in targeting.
516	1724	modify	NEDD8	Cul1	Purified centrosomes also contain Skp1, and Cul1 modified by the ubiquitin-like molecule NEDD8, suggesting a role for NEDD8 in targeting.
517	1725	transfer	DmAos1	DmSUMO-1	Purified recombinant DmUba2/DmAos1 dimer can activate DmSUMO-1 in vitro and transfer DmSUMO-1 to recombinant DmUbc9.
517	1726	transfer	DmSUMO-1	DmAos1	Purified recombinant DmUba2/DmAos1 dimer can activate DmSUMO-1 in vitro and transfer DmSUMO-1 to recombinant DmUbc9.
517	1727	transfer	DmSUMO-1	DmUba2	Purified recombinant DmUba2/DmAos1 dimer can activate DmSUMO-1 in vitro and transfer DmSUMO-1 to recombinant DmUbc9.
517	1728	transfer	DmSUMO-1	DmUbc9	Purified recombinant DmUba2/DmAos1 dimer can activate DmSUMO-1 in vitro and transfer DmSUMO-1 to recombinant DmUbc9.
517	1729	transfer	DmUba2	DmSUMO-1	Purified recombinant DmUba2/DmAos1 dimer can activate DmSUMO-1 in vitro and transfer DmSUMO-1 to recombinant DmUbc9.
517	1730	transfer	DmUbc9	DmSUMO-1	Purified recombinant DmUba2/DmAos1 dimer can activate DmSUMO-1 in vitro and transfer DmSUMO-1 to recombinant DmUbc9.
518	1731	interact	RAD6	UBR1	RAD6 interacts physically with the UBR1 gene product in carrying out the multiubiquitination of amino-end rule proteolytic substrates.
518	1732	interact	UBR1	RAD6	RAD6 interacts physically with the UBR1 gene product in carrying out the multiubiquitination of amino-end rule proteolytic substrates.
519	1733	conjugate	AtCUL1	RUB	RCE1 works together with AXR1-ECR1 to promote formation of a stable RUB conjugate with the Arabidopsis cullin AtCUL1 in vitro.
519	1734	conjugate	RUB	AtCUL1	RCE1 works together with AXR1-ECR1 to promote formation of a stable RUB conjugate with the Arabidopsis cullin AtCUL1 in vitro.
520	1735	interact	APC11	APC2	ROC1 and ROC2 commonly interact with all cullins while APC11 specifically interacts with APC2, a cullin-related APC subunit.
520	1736	interact	APC2	APC11	ROC1 and ROC2 commonly interact with all cullins while APC11 specifically interacts with APC2, a cullin-related APC subunit.
520	1737	interact	ROC1	cullins	ROC1 and ROC2 commonly interact with all cullins while APC11 specifically interacts with APC2, a cullin-related APC subunit.
520	1738	interact	ROC2	cullins	ROC1 and ROC2 commonly interact with all cullins while APC11 specifically interacts with APC2, a cullin-related APC subunit.
520	1739	interact	cullins	ROC1	ROC1 and ROC2 commonly interact with all cullins while APC11 specifically interacts with APC2, a cullin-related APC subunit.
520	1740	interact	cullins	ROC2	ROC1 and ROC2 commonly interact with all cullins while APC11 specifically interacts with APC2, a cullin-related APC subunit.
521	1741	activate	NADPH oxidase	Rac1	Rac1 has been shown to activate a NADPH oxidase complex producing superoxide anions in a variety of mammalian cell types.
521	1742	activate	Rac1	NADPH oxidase	Rac1 has been shown to activate a NADPH oxidase complex producing superoxide anions in a variety of mammalian cell types.
522	1743	interact	26S	Rad23	Rad23 can interact with the 26S proteasome through an N-terminal ubiquitin-like domain, and inhibits the assembly of substrate-linked multi-ubiquitin (multi-Ub) chains in vitro and in vivo.
522	1744	interact	Rad23	26S	Rad23 can interact with the 26S proteasome through an N-terminal ubiquitin-like domain, and inhibits the assembly of substrate-linked multi-ubiquitin (multi-Ub) chains in vitro and in vivo.
523	1745	bind	Rad23	Ub	Rad23 contains a ubiquitin-like domain (UbL(R23)) that interacts with catalytically active proteasomes and two ubiquitin (Ub)-associated (UBA) sequences that bind Ub.
523	1746	bind	Ub	Rad23	Rad23 contains a ubiquitin-like domain (UbL(R23)) that interacts with catalytically active proteasomes and two ubiquitin (Ub)-associated (UBA) sequences that bind Ub.
524	1747	bind	Rad24	Ste11	Rad24 binds preferentially to phosphorylated Ste11, and this binding results in inhibition of the transcriptional activation capacity of Ste11.
524	1748	bind	Ste11	Rad24	Rad24 binds preferentially to phosphorylated Ste11, and this binding results in inhibition of the transcriptional activation capacity of Ste11.
525	1749	association	Rad18	Rad6	Rad6 mediates its DNA repair role via its association with Rad18, whose DNA binding activity may target the Rad6-Rad18 complex to damaged sites in DNA.
525	1750	association	Rad6	Rad18	Rad6 mediates its DNA repair role via its association with Rad18, whose DNA binding activity may target the Rad6-Rad18 complex to damaged sites in DNA.
526	1751	interact	RanBP2	Ubc9	RanBP2 directly interacts with the E2 enzyme Ubc9 and strongly enhances SUMO1-transfer from Ubc9 to the SUMO1 target Sp100.
526	1752	transfer	SUMO1	Sp100	RanBP2 directly interacts with the E2 enzyme Ubc9 and strongly enhances SUMO1-transfer from Ubc9 to the SUMO1 target Sp100.
526	1753	transfer	SUMO1	Ubc9	RanBP2 directly interacts with the E2 enzyme Ubc9 and strongly enhances SUMO1-transfer from Ubc9 to the SUMO1 target Sp100.
526	1754	transfer	Sp100	SUMO1	RanBP2 directly interacts with the E2 enzyme Ubc9 and strongly enhances SUMO1-transfer from Ubc9 to the SUMO1 target Sp100.
526	1755	interact	Ubc9	RanBP2	RanBP2 directly interacts with the E2 enzyme Ubc9 and strongly enhances SUMO1-transfer from Ubc9 to the SUMO1 target Sp100.
526	1756	transfer	Ubc9	SUMO1	RanBP2 directly interacts with the E2 enzyme Ubc9 and strongly enhances SUMO1-transfer from Ubc9 to the SUMO1 target Sp100.
527	1757	associate	RAVE	V-ATPase	Rav1, Rav2 and Skp1 form a complex that we have named 'regulator of the (H+)-ATPase of the vacuolar and endosomal membranes' (RAVE), which associates with the V1 domain of the vacuolar membrane (H+)-ATPase (V-ATPase).
527	1758	complex	Rav1	Rav2	Rav1, Rav2 and Skp1 form a complex that we have named 'regulator of the (H+)-ATPase of the vacuolar and endosomal membranes' (RAVE), which associates with the V1 domain of the vacuolar membrane (H+)-ATPase (V-ATPase).
527	1759	complex	Rav1	Skp1	Rav1, Rav2 and Skp1 form a complex that we have named 'regulator of the (H+)-ATPase of the vacuolar and endosomal membranes' (RAVE), which associates with the V1 domain of the vacuolar membrane (H+)-ATPase (V-ATPase).
527	1760	complex	Rav2	Rav1	Rav1, Rav2 and Skp1 form a complex that we have named 'regulator of the (H+)-ATPase of the vacuolar and endosomal membranes' (RAVE), which associates with the V1 domain of the vacuolar membrane (H+)-ATPase (V-ATPase).
527	1761	complex	Rav2	Skp1	Rav1, Rav2 and Skp1 form a complex that we have named 'regulator of the (H+)-ATPase of the vacuolar and endosomal membranes' (RAVE), which associates with the V1 domain of the vacuolar membrane (H+)-ATPase (V-ATPase).
527	1762	complex	Skp1	Rav1	Rav1, Rav2 and Skp1 form a complex that we have named 'regulator of the (H+)-ATPase of the vacuolar and endosomal membranes' (RAVE), which associates with the V1 domain of the vacuolar membrane (H+)-ATPase (V-ATPase).
527	1763	complex	Skp1	Rav2	Rav1, Rav2 and Skp1 form a complex that we have named 'regulator of the (H+)-ATPase of the vacuolar and endosomal membranes' (RAVE), which associates with the V1 domain of the vacuolar membrane (H+)-ATPase (V-ATPase).
527	1764	associate	V-ATPase	RAVE	Rav1, Rav2 and Skp1 form a complex that we have named 'regulator of the (H+)-ATPase of the vacuolar and endosomal membranes' (RAVE), which associates with the V1 domain of the vacuolar membrane (H+)-ATPase (V-ATPase).
528	1765	interact	Rcy1p	Skp1p	Rcy1p interacted with Skp1p in vivo in an F-box-dependent manner, and both deletion of its F box and loss of Skp1p function impaired recycling.
528	1766	interact	Skp1p	Rcy1p	Rcy1p interacted with Skp1p in vivo in an F-box-dependent manner, and both deletion of its F box and loss of Skp1p function impaired recycling.
529	1767	bind	MDM2	p53	Recent studies indicate that MDM2 can bind p53 and promote its rapid degradation although the molecular basis for this degradation has not been clarified.
529	1768	bind	p53	MDM2	Recent studies indicate that MDM2 can bind p53 and promote its rapid degradation although the molecular basis for this degradation has not been clarified.
530	1769	complex	Skp1	cullin	Recent work has shown that central to the temporal control mechanism is a relationship between newly identified E3 ubiquitin protein ligases, designated SCFs (Skp1-cullin-F-box protein ligase complexes), which confer substrate specificity on ubiquitination reactions and the activities of protein kinases that phosphorylate substrates destined for destruction at specific sites, thereby converting them into preferred targets for ubiquitin modification catalyzed by SCFs.
530	1770	complex	cullin	Skp1	Recent work has shown that central to the temporal control mechanism is a relationship between newly identified E3 ubiquitin protein ligases, designated SCFs (Skp1-cullin-F-box protein ligase complexes), which confer substrate specificity on ubiquitination reactions and the activities of protein kinases that phosphorylate substrates destined for destruction at specific sites, thereby converting them into preferred targets for ubiquitin modification catalyzed by SCFs.
531	1771	linked	Cul-4A	NEDD8	Recently we found that NEDD8, a ubiquitin-like protein, was linked covalently to human cullin-4A (abbreviated Cul-4A) by a new ubiquitin-related pathway that is analogous to but distinct from the ligating system for SUMO1, another ubiquitin-like protein.
531	1772	linked	NEDD8	Cul-4A	Recently we found that NEDD8, a ubiquitin-like protein, was linked covalently to human cullin-4A (abbreviated Cul-4A) by a new ubiquitin-related pathway that is analogous to but distinct from the ligating system for SUMO1, another ubiquitin-like protein.
532	1773	complex	Cul2	elongin C	Recently, a multiprotein complex containing pVHL, elongin C and Cul2 (VEC) was shown to structurally and functionally resemble SCF complexes.
532	1774	complex	Cul2	pVHL	Recently, a multiprotein complex containing pVHL, elongin C and Cul2 (VEC) was shown to structurally and functionally resemble SCF complexes.
532	1775	complex	VEC	elongin C	Recently, a multiprotein complex containing pVHL, elongin C and Cul2 (VEC) was shown to structurally and functionally resemble SCF complexes.
532	1776	complex	VEC	pVHL	Recently, a multiprotein complex containing pVHL, elongin C and Cul2 (VEC) was shown to structurally and functionally resemble SCF complexes.
532	1777	complex	elongin C	Cul2	Recently, a multiprotein complex containing pVHL, elongin C and Cul2 (VEC) was shown to structurally and functionally resemble SCF complexes.
532	1778	complex	elongin C	VEC	Recently, a multiprotein complex containing pVHL, elongin C and Cul2 (VEC) was shown to structurally and functionally resemble SCF complexes.
532	1779	complex	elongin C	pVHL	Recently, a multiprotein complex containing pVHL, elongin C and Cul2 (VEC) was shown to structurally and functionally resemble SCF complexes.
532	1780	complex	pVHL	Cul2	Recently, a multiprotein complex containing pVHL, elongin C and Cul2 (VEC) was shown to structurally and functionally resemble SCF complexes.
532	1781	complex	pVHL	VEC	Recently, a multiprotein complex containing pVHL, elongin C and Cul2 (VEC) was shown to structurally and functionally resemble SCF complexes.
532	1782	complex	pVHL	elongin C	Recently, a multiprotein complex containing pVHL, elongin C and Cul2 (VEC) was shown to structurally and functionally resemble SCF complexes.
533	1783	complex	Cul2	Elongin B	Recently, the VHL-Elongin BC complex was found to interact with a module composed of Cullin family member Cul2 and RING-H2 finger protein Rbx1 to reconstitute a novel E3 ubiquitin ligase that activates ubiquitylation by the E2 ubiquitin-conjugating enzymes Ubc5 and Cdc34.
533	1784	complex	Cul2	Elongin C	Recently, the VHL-Elongin BC complex was found to interact with a module composed of Cullin family member Cul2 and RING-H2 finger protein Rbx1 to reconstitute a novel E3 ubiquitin ligase that activates ubiquitylation by the E2 ubiquitin-conjugating enzymes Ubc5 and Cdc34.
533	1785	complex	Cul2	VHL	Recently, the VHL-Elongin BC complex was found to interact with a module composed of Cullin family member Cul2 and RING-H2 finger protein Rbx1 to reconstitute a novel E3 ubiquitin ligase that activates ubiquitylation by the E2 ubiquitin-conjugating enzymes Ubc5 and Cdc34.
533	1786	complex	Elongin B	Cul2	Recently, the VHL-Elongin BC complex was found to interact with a module composed of Cullin family member Cul2 and RING-H2 finger protein Rbx1 to reconstitute a novel E3 ubiquitin ligase that activates ubiquitylation by the E2 ubiquitin-conjugating enzymes Ubc5 and Cdc34.
533	1787	complex	Elongin B	Elongin C	Recently, the VHL-Elongin BC complex was found to interact with a module composed of Cullin family member Cul2 and RING-H2 finger protein Rbx1 to reconstitute a novel E3 ubiquitin ligase that activates ubiquitylation by the E2 ubiquitin-conjugating enzymes Ubc5 and Cdc34.
533	1788	complex	Elongin B	VHL	Recently, the VHL-Elongin BC complex was found to interact with a module composed of Cullin family member Cul2 and RING-H2 finger protein Rbx1 to reconstitute a novel E3 ubiquitin ligase that activates ubiquitylation by the E2 ubiquitin-conjugating enzymes Ubc5 and Cdc34.
533	1789	complex	Elongin C	Cul2	Recently, the VHL-Elongin BC complex was found to interact with a module composed of Cullin family member Cul2 and RING-H2 finger protein Rbx1 to reconstitute a novel E3 ubiquitin ligase that activates ubiquitylation by the E2 ubiquitin-conjugating enzymes Ubc5 and Cdc34.
533	1790	complex	Elongin C	Elongin B	Recently, the VHL-Elongin BC complex was found to interact with a module composed of Cullin family member Cul2 and RING-H2 finger protein Rbx1 to reconstitute a novel E3 ubiquitin ligase that activates ubiquitylation by the E2 ubiquitin-conjugating enzymes Ubc5 and Cdc34.
533	1791	complex	Elongin C	VHL	Recently, the VHL-Elongin BC complex was found to interact with a module composed of Cullin family member Cul2 and RING-H2 finger protein Rbx1 to reconstitute a novel E3 ubiquitin ligase that activates ubiquitylation by the E2 ubiquitin-conjugating enzymes Ubc5 and Cdc34.
533	1792	complex	VHL	Cul2	Recently, the VHL-Elongin BC complex was found to interact with a module composed of Cullin family member Cul2 and RING-H2 finger protein Rbx1 to reconstitute a novel E3 ubiquitin ligase that activates ubiquitylation by the E2 ubiquitin-conjugating enzymes Ubc5 and Cdc34.
533	1793	complex	VHL	Elongin B	Recently, the VHL-Elongin BC complex was found to interact with a module composed of Cullin family member Cul2 and RING-H2 finger protein Rbx1 to reconstitute a novel E3 ubiquitin ligase that activates ubiquitylation by the E2 ubiquitin-conjugating enzymes Ubc5 and Cdc34.
533	1794	complex	VHL	Elongin C	Recently, the VHL-Elongin BC complex was found to interact with a module composed of Cullin family member Cul2 and RING-H2 finger protein Rbx1 to reconstitute a novel E3 ubiquitin ligase that activates ubiquitylation by the E2 ubiquitin-conjugating enzymes Ubc5 and Cdc34.
534	1795	bound	H2A	ubiquitin	Regardless of protein synthesis, ubiquitin was again bound to H2A when cells entered the G1 phase.
534	1796	bound	ubiquitin	H2A	Regardless of protein synthesis, ubiquitin was again bound to H2A when cells entered the G1 phase.
535	1797	conjugation	CDC53	RUB1	Remarkably, CDC53/cullin, a common subunit of the multifunctional SCF ubiquitin ligase, was found to be a major substrate for RUB1 conjugation.
535	1798	conjugation	RUB1	CDC53	Remarkably, CDC53/cullin, a common subunit of the multifunctional SCF ubiquitin ligase, was found to be a major substrate for RUB1 conjugation.
535	1799	conjugation	RUB1	cullin	Remarkably, CDC53/cullin, a common subunit of the multifunctional SCF ubiquitin ligase, was found to be a major substrate for RUB1 conjugation.
535	1800	conjugation	cullin	RUB1	Remarkably, CDC53/cullin, a common subunit of the multifunctional SCF ubiquitin ligase, was found to be a major substrate for RUB1 conjugation.
536	1801	complex	CUL7	Fbx29	Remarkably, CUL7 assembles an SCF-ROC1-like E3 ubiquitin ligase complex consisting of Skp1, CUL7, the Fbx29 F-box protein, and ROC1.
536	1802	complex	CUL7	ROC1	Remarkably, CUL7 assembles an SCF-ROC1-like E3 ubiquitin ligase complex consisting of Skp1, CUL7, the Fbx29 F-box protein, and ROC1.
536	1803	complex	CUL7	Skp1	Remarkably, CUL7 assembles an SCF-ROC1-like E3 ubiquitin ligase complex consisting of Skp1, CUL7, the Fbx29 F-box protein, and ROC1.
536	1804	complex	Fbx29	CUL7	Remarkably, CUL7 assembles an SCF-ROC1-like E3 ubiquitin ligase complex consisting of Skp1, CUL7, the Fbx29 F-box protein, and ROC1.
536	1805	complex	Fbx29	ROC1	Remarkably, CUL7 assembles an SCF-ROC1-like E3 ubiquitin ligase complex consisting of Skp1, CUL7, the Fbx29 F-box protein, and ROC1.
536	1806	complex	Fbx29	Skp1	Remarkably, CUL7 assembles an SCF-ROC1-like E3 ubiquitin ligase complex consisting of Skp1, CUL7, the Fbx29 F-box protein, and ROC1.
536	1807	complex	ROC1	CUL7	Remarkably, CUL7 assembles an SCF-ROC1-like E3 ubiquitin ligase complex consisting of Skp1, CUL7, the Fbx29 F-box protein, and ROC1.
536	1808	complex	ROC1	Fbx29	Remarkably, CUL7 assembles an SCF-ROC1-like E3 ubiquitin ligase complex consisting of Skp1, CUL7, the Fbx29 F-box protein, and ROC1.
536	1809	complex	ROC1	Skp1	Remarkably, CUL7 assembles an SCF-ROC1-like E3 ubiquitin ligase complex consisting of Skp1, CUL7, the Fbx29 F-box protein, and ROC1.
536	1810	complex	Skp1	CUL7	Remarkably, CUL7 assembles an SCF-ROC1-like E3 ubiquitin ligase complex consisting of Skp1, CUL7, the Fbx29 F-box protein, and ROC1.
536	1811	complex	Skp1	Fbx29	Remarkably, CUL7 assembles an SCF-ROC1-like E3 ubiquitin ligase complex consisting of Skp1, CUL7, the Fbx29 F-box protein, and ROC1.
536	1812	complex	Skp1	ROC1	Remarkably, CUL7 assembles an SCF-ROC1-like E3 ubiquitin ligase complex consisting of Skp1, CUL7, the Fbx29 F-box protein, and ROC1.
537	1813	ubiquitinate	Cdc4	Sic1	Remarkably, SCF(Cdc4) ubiquitin ligase binds and ubiquitinates Sic1 decorated with six, but not five, phosphates.
537	1814	ubiquitinate	Sic1	Cdc4	Remarkably, SCF(Cdc4) ubiquitin ligase binds and ubiquitinates Sic1 decorated with six, but not five, phosphates.
538	1815	interact	C-GLUT4	Daxx	Replacement of alanine and serine for the dileucine pair (Leu(489)-Leu(490)) critical for targeting GLUT4 from the trans-Golgi network to the perinuclear intracellular store as well as for its surface internalization by endocytosis inhibits 2-fold the interaction of C-GLUT4 with Daxx.
538	1816	interact	Daxx	C-GLUT4	Replacement of alanine and serine for the dileucine pair (Leu(489)-Leu(490)) critical for targeting GLUT4 from the trans-Golgi network to the perinuclear intracellular store as well as for its surface internalization by endocytosis inhibits 2-fold the interaction of C-GLUT4 with Daxx.
539	1817	interaction	Rad18	Rad6	Residues important for Rad6 interaction with Ubr1 and Rad18 are on the opposite side of the structure from the active site, indicating that this part of the UBC surface participates in protein-protein interactions that define Rad6 substrate specificity.
539	1818	interaction	Rad6	Rad18	Residues important for Rad6 interaction with Ubr1 and Rad18 are on the opposite side of the structure from the active site, indicating that this part of the UBC surface participates in protein-protein interactions that define Rad6 substrate specificity.
539	1819	interaction	Rad6	Ubr1	Residues important for Rad6 interaction with Ubr1 and Rad18 are on the opposite side of the structure from the active site, indicating that this part of the UBC surface participates in protein-protein interactions that define Rad6 substrate specificity.
539	1820	interaction	Ubr1	Rad6	Residues important for Rad6 interaction with Ubr1 and Rad18 are on the opposite side of the structure from the active site, indicating that this part of the UBC surface participates in protein-protein interactions that define Rad6 substrate specificity.
540	1821	ubiquitinate	Skp2	h0rc1p	Ro106-9920 was observed to inhibit an ubiquitination activity that does not require betaTRCP but associates with IkappaB(alpha) and will ubiquitinate IkappaB(alpha) S32E,S36E (IkappaB(alpha)(ee)) specifically at lysine 21 or 22.
540	1822	ubiquitinate	h0rc1p	Skp2	Ro106-9920 was observed to inhibit an ubiquitination activity that does not require betaTRCP but associates with IkappaB(alpha) and will ubiquitinate IkappaB(alpha) S32E,S36E (IkappaB(alpha)(ee)) specifically at lysine 21 or 22.
541	1823	bind	Rog1	Rsp5	Rog1 binds directly to Rsp5, and their interaction is dependent on GSK-3.
541	1824	bind	Rsp5	Rog1	Rog1 binds directly to Rsp5, and their interaction is dependent on GSK-3.
542	1825	bound	H2A	ubiquitin	SDS-PAGE analysis of fractionated density gradients suggests, however, that newly synthesized ubiquitin becomes bound nonselectively to both new and preexisting H2A molecules.
542	1826	bound	ubiquitin	H2A	SDS-PAGE analysis of fractionated density gradients suggests, however, that newly synthesized ubiquitin becomes bound nonselectively to both new and preexisting H2A molecules.
543	1827	bound	Notch4	SEL-10	SEL-10 bound Notch4 via the WD40 repeats and bound preferentially to a phosphorylated form of Notch4 in cells.
543	1828	bound	SEL-10	Notch4	SEL-10 bound Notch4 via the WD40 repeats and bound preferentially to a phosphorylated form of Notch4 in cells.
544	1829	associate	CUL1	SGT1	SGT1 associates with SKP1 and CUL1, subunits of the SCF (Skp1-Cullin-F-box) ubiquitin ligase complex.
544	1830	associate	SGT1	CUL1	SGT1 associates with SKP1 and CUL1, subunits of the SCF (Skp1-Cullin-F-box) ubiquitin ligase complex.
544	1831	associate	SGT1	SKP1	SGT1 associates with SKP1 and CUL1, subunits of the SCF (Skp1-Cullin-F-box) ubiquitin ligase complex.
544	1832	associate	SKP1	SGT1	SGT1 associates with SKP1 and CUL1, subunits of the SCF (Skp1-Cullin-F-box) ubiquitin ligase complex.
545	1833	interact	SMRZ	SMT3b	SMRZ was found to interact with SMT3b, a ubiquitin-like protein, through the SMRZ-RING domain.
545	1834	interact	SMT3b	SMRZ	SMRZ was found to interact with SMT3b, a ubiquitin-like protein, through the SMRZ-RING domain.
546	1835	bound	IRS1	SOCS1	SOCS1 or SOCS3 bound both recombinant and endogenous IRS1 and IRS2 and promoted their ubiquitination and subsequent degradation in multiple cell types.
546	1836	bound	IRS1	SOCS3	SOCS1 or SOCS3 bound both recombinant and endogenous IRS1 and IRS2 and promoted their ubiquitination and subsequent degradation in multiple cell types.
546	1837	bound	IRS2	SOCS1	SOCS1 or SOCS3 bound both recombinant and endogenous IRS1 and IRS2 and promoted their ubiquitination and subsequent degradation in multiple cell types.
546	1838	bound	IRS2	SOCS3	SOCS1 or SOCS3 bound both recombinant and endogenous IRS1 and IRS2 and promoted their ubiquitination and subsequent degradation in multiple cell types.
546	1839	bound	SOCS1	IRS1	SOCS1 or SOCS3 bound both recombinant and endogenous IRS1 and IRS2 and promoted their ubiquitination and subsequent degradation in multiple cell types.
546	1840	bound	SOCS1	IRS2	SOCS1 or SOCS3 bound both recombinant and endogenous IRS1 and IRS2 and promoted their ubiquitination and subsequent degradation in multiple cell types.
546	1841	bound	SOCS3	IRS1	SOCS1 or SOCS3 bound both recombinant and endogenous IRS1 and IRS2 and promoted their ubiquitination and subsequent degradation in multiple cell types.
546	1842	bound	SOCS3	IRS2	SOCS1 or SOCS3 bound both recombinant and endogenous IRS1 and IRS2 and promoted their ubiquitination and subsequent degradation in multiple cell types.
547	1843	association	Plo1	SPB	SPB association of Plo1 is the earliest fission yeast mitotic event recorded to date.
547	1844	association	SPB	Plo1	SPB association of Plo1 is the earliest fission yeast mitotic event recorded to date.
548	1845	association	Plo1	SPB	SPB association of Plo1 requires mitosis-promoting factor (MPF) activity, whereas its disassociation requires the activity of the anaphase-promoting complex.
548	1846	association	SPB	Plo1	SPB association of Plo1 requires mitosis-promoting factor (MPF) activity, whereas its disassociation requires the activity of the anaphase-promoting complex.
549	1847	interact	RPN11	STS1	STS1 also interacted with the second suppressor, RPN11, a subunit of the 26S proteasome, in the two-hybrid system.
549	1848	interact	STS1	RPN11	STS1 also interacted with the second suppressor, RPN11, a subunit of the 26S proteasome, in the two-hybrid system.
550	1849	modification	IE72	SUMO	SUMO modification of IE72 was confirmed by immunoprecipitation with anti-IE72 and anti-SUMO-1 followed by Western blotting with anti-SUMO-1 and anti-IE72, respectively.
550	1850	modification	SUMO	IE72	SUMO modification of IE72 was confirmed by immunoprecipitation with anti-IE72 and anti-SUMO-1 followed by Western blotting with anti-SUMO-1 and anti-IE72, respectively.
551	1851	modification	SUMO	Sp3	SUMO modification of Sp3 occurs at a single lysine located between the second glutamine-rich activation domain and the DNA-binding domain.
551	1852	modification	Sp3	SUMO	SUMO modification of Sp3 occurs at a single lysine located between the second glutamine-rich activation domain and the DNA-binding domain.
552	1853	interacting	Mdm2	p14ARF	SUMO modification requires residues 2-14 in p14ARF that interact with (H)Mdm2 and residues 82-101 in exon 2 involved in nucleolar localisation of p14ARF.
552	1854	interacting	p14ARF	Mdm2	SUMO modification requires residues 2-14 in p14ARF that interact with (H)Mdm2 and residues 82-101 in exon 2 involved in nucleolar localisation of p14ARF.
553	1855	bind	PR	SUMO-1	SUMO-1 binds PR covalently at (387)IKEE, but only if the C-terminal, liganded, hormone-binding domain is also present.
553	1856	bind	SUMO-1	PR	SUMO-1 binds PR covalently at (387)IKEE, but only if the C-terminal, liganded, hormone-binding domain is also present.
554	1857	linked	RanGAP1	SUMO-1	SUMO-1 is linked to RanGAP1 via glycine 97, indicating that the last 4 amino acids of this 101- amino acid protein are proteolytically removed before its attachment to RanGAP1.
554	1858	linked	SUMO-1	RanGAP1	SUMO-1 is linked to RanGAP1 via glycine 97, indicating that the last 4 amino acids of this 101- amino acid protein are proteolytically removed before its attachment to RanGAP1.
555	1859	modification	PML	SUMO-1	SUMO-1 modification of PML is known to be required for the formation of PML bodies.
555	1860	modification	SUMO-1	PML	SUMO-1 modification of PML is known to be required for the formation of PML bodies.
556	1861	linked	GMP1	RanGAP1	SUMO-1/GMP1 was found to be covalently linked to the Ran GTPase-activating protein RanGAP1, and attachment of SUMO-1 targets the otherwise cytosolic RanGAP1 to the nuclear pore complex.
556	1862	linked	RanGAP1	GMP1	SUMO-1/GMP1 was found to be covalently linked to the Ran GTPase-activating protein RanGAP1, and attachment of SUMO-1 targets the otherwise cytosolic RanGAP1 to the nuclear pore complex.
556	1863	linked	RanGAP1	SUMO-1	SUMO-1/GMP1 was found to be covalently linked to the Ran GTPase-activating protein RanGAP1, and attachment of SUMO-1 targets the otherwise cytosolic RanGAP1 to the nuclear pore complex.
556	1864	linked	SUMO-1	RanGAP1	SUMO-1/GMP1 was found to be covalently linked to the Ran GTPase-activating protein RanGAP1, and attachment of SUMO-1 targets the otherwise cytosolic RanGAP1 to the nuclear pore complex.
557	1865	interact	SVIP	VCP	SVIP and previously identified adaptors p47 and ufd1p interact with VCP/p97 in a mutually exclusive manner.
557	1866	interact	SVIP	p97	SVIP and previously identified adaptors p47 and ufd1p interact with VCP/p97 in a mutually exclusive manner.
557	1867	interact	VCP	SVIP	SVIP and previously identified adaptors p47 and ufd1p interact with VCP/p97 in a mutually exclusive manner.
557	1868	interact	VCP	p47	SVIP and previously identified adaptors p47 and ufd1p interact with VCP/p97 in a mutually exclusive manner.
557	1869	interact	VCP	ufd1p	SVIP and previously identified adaptors p47 and ufd1p interact with VCP/p97 in a mutually exclusive manner.
557	1870	interact	p47	VCP	SVIP and previously identified adaptors p47 and ufd1p interact with VCP/p97 in a mutually exclusive manner.
557	1871	interact	p47	p97	SVIP and previously identified adaptors p47 and ufd1p interact with VCP/p97 in a mutually exclusive manner.
557	1872	interact	p97	SVIP	SVIP and previously identified adaptors p47 and ufd1p interact with VCP/p97 in a mutually exclusive manner.
557	1873	interact	p97	p47	SVIP and previously identified adaptors p47 and ufd1p interact with VCP/p97 in a mutually exclusive manner.
557	1874	interact	p97	ufd1p	SVIP and previously identified adaptors p47 and ufd1p interact with VCP/p97 in a mutually exclusive manner.
557	1875	interact	ufd1p	VCP	SVIP and previously identified adaptors p47 and ufd1p interact with VCP/p97 in a mutually exclusive manner.
557	1876	interact	ufd1p	p97	SVIP and previously identified adaptors p47 and ufd1p interact with VCP/p97 in a mutually exclusive manner.
558	1877	conjugate	iso1-cytochrome c	ubiquitin	Saccharomyces cerevisiae iso-1-cytochrome c was conjugated with ubiquitin (Ub) in vitro in a rabbit reticulocyte extract (Fraction II).
558	1878	conjugate	ubiquitin	iso1-cytochrome c	Saccharomyces cerevisiae iso-1-cytochrome c was conjugated with ubiquitin (Ub) in vitro in a rabbit reticulocyte extract (Fraction II).
559	1879	interaction	E6	E6AP	Screening system based on the interaction between E6AP and E6 may be a promising system in the development of drugs against cervical cancer caused by HPV infection.
559	1880	interaction	E6AP	E6	Screening system based on the interaction between E6AP and E6 may be a promising system in the development of drugs against cervical cancer caused by HPV infection.
560	1881	target	APC	securin	Securin, like mitotic cyclins, is the target of the anaphase promoting complex (APC)/cyclosome and is polyubiquitinated before destruction in a manner dependent upon the destruction sequence.
560	1882	target	securin	APC	Securin, like mitotic cyclins, is the target of the anaphase promoting complex (APC)/cyclosome and is polyubiquitinated before destruction in a manner dependent upon the destruction sequence.
561	1883	interact	APO-1	Sentrin	Sentrin was shown to interact with Fas/APO-1 or the TNF receptor 1 death domain, and the overexpression of sentrin provided protection against both anti-Fas/APO-1 and TNF-induced cell death (11).
561	1884	interact	Fas	Sentrin	Sentrin was shown to interact with Fas/APO-1 or the TNF receptor 1 death domain, and the overexpression of sentrin provided protection against both anti-Fas/APO-1 and TNF-induced cell death (11).
561	1885	interact	Sentrin	APO-1	Sentrin was shown to interact with Fas/APO-1 or the TNF receptor 1 death domain, and the overexpression of sentrin provided protection against both anti-Fas/APO-1 and TNF-induced cell death (11).
561	1886	interact	Sentrin	Fas	Sentrin was shown to interact with Fas/APO-1 or the TNF receptor 1 death domain, and the overexpression of sentrin provided protection against both anti-Fas/APO-1 and TNF-induced cell death (11).
561	1887	interact	Sentrin	TNF receptor 1	Sentrin was shown to interact with Fas/APO-1 or the TNF receptor 1 death domain, and the overexpression of sentrin provided protection against both anti-Fas/APO-1 and TNF-induced cell death (11).
561	1888	interact	TNF receptor 1	Sentrin	Sentrin was shown to interact with Fas/APO-1 or the TNF receptor 1 death domain, and the overexpression of sentrin provided protection against both anti-Fas/APO-1 and TNF-induced cell death (11).
562	1889	associate	Sgt1p	Skp1p	Sgt1p physically associates with Skp1p in vivo and in vitro.
562	1890	associate	Skp1p	Sgt1p	Sgt1p physically associates with Skp1p in vivo and in vitro.
563	1891	activate	Akt	SigD	SigD activates Akt in epithelial cells and indirectly activates Cdc42 through one of its products, inositol 1,4,5,6-tetrakisphosphate.
563	1892	activate	SigD	Akt	SigD activates Akt in epithelial cells and indirectly activates Cdc42 through one of its products, inositol 1,4,5,6-tetrakisphosphate.
564	1893	bind	AEF	amyloid fibrils	Since AEF is known to bind to amyloid fibrils and 'fibril-AEF' on passive transfer induces accelerated amyloidogenesis in the recipient animals, it was of interest to investigate whether ubiquitin binds to amyloid.
564	1894	bind	amyloid fibrils	AEF	Since AEF is known to bind to amyloid fibrils and 'fibril-AEF' on passive transfer induces accelerated amyloidogenesis in the recipient animals, it was of interest to investigate whether ubiquitin binds to amyloid.
565	1895	complex	Cdk2	Skp1	Skp1 interacts with cullins, F-box containing proteins, and forms a complex with cyclin A-Cdk2 in mammalian cells.
565	1896	complex	Cdk2	cyclin A	Skp1 interacts with cullins, F-box containing proteins, and forms a complex with cyclin A-Cdk2 in mammalian cells.
565	1897	complex	Skp1	Cdk2	Skp1 interacts with cullins, F-box containing proteins, and forms a complex with cyclin A-Cdk2 in mammalian cells.
565	1898	complex	Skp1	cyclin A	Skp1 interacts with cullins, F-box containing proteins, and forms a complex with cyclin A-Cdk2 in mammalian cells.
565	1899	complex	cyclin A	Cdk2	Skp1 interacts with cullins, F-box containing proteins, and forms a complex with cyclin A-Cdk2 in mammalian cells.
565	1900	complex	cyclin A	Skp1	Skp1 interacts with cullins, F-box containing proteins, and forms a complex with cyclin A-Cdk2 in mammalian cells.
566	1901	complex	Cdc4	Cdc53	Skp1, Cdc53, and the F-box protein Cdc4 form a complex, SCFCdc4, which functions as a Sic1 ubiquitin-ligase (E3) in combination with the ubiquitin conjugating enzyme (E2) Cdc34 and E1.
566	1902	ubiquitinate	Cdc4	Sic1	Skp1, Cdc53, and the F-box protein Cdc4 form a complex, SCFCdc4, which functions as a Sic1 ubiquitin-ligase (E3) in combination with the ubiquitin conjugating enzyme (E2) Cdc34 and E1.
566	1903	complex	Cdc4	Skp1	Skp1, Cdc53, and the F-box protein Cdc4 form a complex, SCFCdc4, which functions as a Sic1 ubiquitin-ligase (E3) in combination with the ubiquitin conjugating enzyme (E2) Cdc34 and E1.
566	1904	complex	Cdc53	Cdc4	Skp1, Cdc53, and the F-box protein Cdc4 form a complex, SCFCdc4, which functions as a Sic1 ubiquitin-ligase (E3) in combination with the ubiquitin conjugating enzyme (E2) Cdc34 and E1.
566	1905	complex	Cdc53	Skp1	Skp1, Cdc53, and the F-box protein Cdc4 form a complex, SCFCdc4, which functions as a Sic1 ubiquitin-ligase (E3) in combination with the ubiquitin conjugating enzyme (E2) Cdc34 and E1.
566	1906	ubiquitinate	Sic1	Cdc4	Skp1, Cdc53, and the F-box protein Cdc4 form a complex, SCFCdc4, which functions as a Sic1 ubiquitin-ligase (E3) in combination with the ubiquitin conjugating enzyme (E2) Cdc34 and E1.
566	1907	complex	Skp1	Cdc4	Skp1, Cdc53, and the F-box protein Cdc4 form a complex, SCFCdc4, which functions as a Sic1 ubiquitin-ligase (E3) in combination with the ubiquitin conjugating enzyme (E2) Cdc34 and E1.
566	1908	complex	Skp1	Cdc53	Skp1, Cdc53, and the F-box protein Cdc4 form a complex, SCFCdc4, which functions as a Sic1 ubiquitin-ligase (E3) in combination with the ubiquitin conjugating enzyme (E2) Cdc34 and E1.
567	1909	phophorylated	Cdk2	Skp2	Skp2 is phosphorylated by cyclin A-Cdk2 on residue Ser76, but nonphosphorylatable mutants of Skp2 can still inhibit the kinase activity of cyclin A-Cdk2 toward histone H1.
567	1910	phophorylated	Skp2	Cdk2	Skp2 is phosphorylated by cyclin A-Cdk2 on residue Ser76, but nonphosphorylatable mutants of Skp2 can still inhibit the kinase activity of cyclin A-Cdk2 toward histone H1.
567	1911	phophorylated	Skp2	cyclin A	Skp2 is phosphorylated by cyclin A-Cdk2 on residue Ser76, but nonphosphorylatable mutants of Skp2 can still inhibit the kinase activity of cyclin A-Cdk2 toward histone H1.
567	1912	phophorylated	cyclin A	Skp2	Skp2 is phosphorylated by cyclin A-Cdk2 on residue Ser76, but nonphosphorylatable mutants of Skp2 can still inhibit the kinase activity of cyclin A-Cdk2 toward histone H1.
568	1913	interact	Smad7	Smurf1	Smad ubiquitin regulatory factor 1 (Smurf1), a HECT type E3 ubiquitin ligase, interacts with inhibitory Smad7 and induces translocation of Smad7 to the cytoplasm.
568	1914	interact	Smurf1	Smad7	Smad ubiquitin regulatory factor 1 (Smurf1), a HECT type E3 ubiquitin ligase, interacts with inhibitory Smad7 and induces translocation of Smad7 to the cytoplasm.
569	1915	interact	Smad7	Smurf1	Smad ubiquitin regulatory factor 1 (Smurf1), a HECT-type E3 ubiquitin ligase, interacts with inhibitory Smad7 and induces cytoplasmic localization of Smad7.
569	1916	interact	Smurf1	Smad7	Smad ubiquitin regulatory factor 1 (Smurf1), a HECT-type E3 ubiquitin ligase, interacts with inhibitory Smad7 and induces cytoplasmic localization of Smad7.
570	1917	activated	Smad2	TGF-beta	Smad2 is phosphorylated and activated by TGF-beta, resulting in the antiproliferative effects of TGF-beta signaling.
570	1918	activated	TGF-beta	Smad2	Smad2 is phosphorylated and activated by TGF-beta, resulting in the antiproliferative effects of TGF-beta signaling.
571	1919	interact	APC	Smad2	Smad3 and to a lesser extent, Smad2, interact with both the APC and SnoN, resulting in the recruitment of the APC to SnoN and subsequent ubiquitination of SnoN in a destruction box (D box)-dependent manner.
571	1920	interact	APC	Smad3	Smad3 and to a lesser extent, Smad2, interact with both the APC and SnoN, resulting in the recruitment of the APC to SnoN and subsequent ubiquitination of SnoN in a destruction box (D box)-dependent manner.
571	1921	recruitment	APC	SnoN	Smad3 and to a lesser extent, Smad2, interact with both the APC and SnoN, resulting in the recruitment of the APC to SnoN and subsequent ubiquitination of SnoN in a destruction box (D box)-dependent manner.
571	1922	interact	Smad2	APC	Smad3 and to a lesser extent, Smad2, interact with both the APC and SnoN, resulting in the recruitment of the APC to SnoN and subsequent ubiquitination of SnoN in a destruction box (D box)-dependent manner.
571	1923	interact	Smad2	SnoN	Smad3 and to a lesser extent, Smad2, interact with both the APC and SnoN, resulting in the recruitment of the APC to SnoN and subsequent ubiquitination of SnoN in a destruction box (D box)-dependent manner.
571	1924	interact	Smad3	APC	Smad3 and to a lesser extent, Smad2, interact with both the APC and SnoN, resulting in the recruitment of the APC to SnoN and subsequent ubiquitination of SnoN in a destruction box (D box)-dependent manner.
571	1925	interact	Smad3	SnoN	Smad3 and to a lesser extent, Smad2, interact with both the APC and SnoN, resulting in the recruitment of the APC to SnoN and subsequent ubiquitination of SnoN in a destruction box (D box)-dependent manner.
571	1926	recruitment	SnoN	APC	Smad3 and to a lesser extent, Smad2, interact with both the APC and SnoN, resulting in the recruitment of the APC to SnoN and subsequent ubiquitination of SnoN in a destruction box (D box)-dependent manner.
571	1927	interact	SnoN	Smad2	Smad3 and to a lesser extent, Smad2, interact with both the APC and SnoN, resulting in the recruitment of the APC to SnoN and subsequent ubiquitination of SnoN in a destruction box (D box)-dependent manner.
571	1928	interact	SnoN	Smad3	Smad3 and to a lesser extent, Smad2, interact with both the APC and SnoN, resulting in the recruitment of the APC to SnoN and subsequent ubiquitination of SnoN in a destruction box (D box)-dependent manner.
572	1929	activation	Aos1p	Smt3p	Smt3p undergoes ATP-dependent activation by a novel heterodimeric enzyme consisting of Uba2p, a previously identified 71 kDa protein similar to the C-terminus of ubiquitin-activating enzymes (E1s), and Aos1p (activation of Smt3p), a 40 kDa protein similar to the N-terminus of E1s.
572	1930	activation	Smt3p	Aos1p	Smt3p undergoes ATP-dependent activation by a novel heterodimeric enzyme consisting of Uba2p, a previously identified 71 kDa protein similar to the C-terminus of ubiquitin-activating enzymes (E1s), and Aos1p (activation of Smt3p), a 40 kDa protein similar to the N-terminus of E1s.
572	1931	activation	Smt3p	Uba2p	Smt3p undergoes ATP-dependent activation by a novel heterodimeric enzyme consisting of Uba2p, a previously identified 71 kDa protein similar to the C-terminus of ubiquitin-activating enzymes (E1s), and Aos1p (activation of Smt3p), a 40 kDa protein similar to the N-terminus of E1s.
572	1932	activation	Uba2p	Smt3p	Smt3p undergoes ATP-dependent activation by a novel heterodimeric enzyme consisting of Uba2p, a previously identified 71 kDa protein similar to the C-terminus of ubiquitin-activating enzymes (E1s), and Aos1p (activation of Smt3p), a 40 kDa protein similar to the N-terminus of E1s.
573	1933	interact	SMADs	Smurf1	Smurf1 selectively interacts with receptor-regulated SMADs specific for the BMP pathway in order to trigger their ubiquitination and degradation, and hence their inactivation.
573	1934	interact	Smurf1	SMADs	Smurf1 selectively interacts with receptor-regulated SMADs specific for the BMP pathway in order to trigger their ubiquitination and degradation, and hence their inactivation.
574	1935	associate	Smurf1	TbR-I	Smurf1 then associates with transforming growth factor (TGF)-b type I receptor (TbR-I) and enhances turnover of it.
574	1936	associate	TbR-I	Smurf1	Smurf1 then associates with transforming growth factor (TGF)-b type I receptor (TbR-I) and enhances turnover of it.
575	1937	associate	Smurf1	TbetaR-I	Smurf1 then associates with transforming growth factor-beta type I receptor (TbetaR-I) and enhances the turnover of this receptor.
575	1938	associate	TbetaR-I	Smurf1	Smurf1 then associates with transforming growth factor-beta type I receptor (TbetaR-I) and enhances the turnover of this receptor.
576	1939	bind	Rpn2p	Ubr1p	Specifically, Ubr1p is shown to bind to the Rpn2p, Rpt1p, and Rpt6p proteins of the 19S particle, and Ufd4p is shown to bind to Rpt6p.
576	1940	bind	Rpt1p	Ubr1p	Specifically, Ubr1p is shown to bind to the Rpn2p, Rpt1p, and Rpt6p proteins of the 19S particle, and Ufd4p is shown to bind to Rpt6p.
576	1941	bind	Rpt6p	Ubr1p	Specifically, Ubr1p is shown to bind to the Rpn2p, Rpt1p, and Rpt6p proteins of the 19S particle, and Ufd4p is shown to bind to Rpt6p.
576	1942	bind	Rpt6p	Ufd4p	Specifically, Ubr1p is shown to bind to the Rpn2p, Rpt1p, and Rpt6p proteins of the 19S particle, and Ufd4p is shown to bind to Rpt6p.
576	1943	bind	Ubr1p	Rpn2p	Specifically, Ubr1p is shown to bind to the Rpn2p, Rpt1p, and Rpt6p proteins of the 19S particle, and Ufd4p is shown to bind to Rpt6p.
576	1944	bind	Ubr1p	Rpt1p	Specifically, Ubr1p is shown to bind to the Rpn2p, Rpt1p, and Rpt6p proteins of the 19S particle, and Ufd4p is shown to bind to Rpt6p.
576	1945	bind	Ubr1p	Rpt6p	Specifically, Ubr1p is shown to bind to the Rpn2p, Rpt1p, and Rpt6p proteins of the 19S particle, and Ufd4p is shown to bind to Rpt6p.
576	1946	bind	Ufd4p	Rpt6p	Specifically, Ubr1p is shown to bind to the Rpn2p, Rpt1p, and Rpt6p proteins of the 19S particle, and Ufd4p is shown to bind to Rpt6p.
577	1947	inhibited	7alpha-hydroxylase	Fbw1a	Stable expression of two different plasmids that encode either rat or human 7alpha-hydroxylase inhibited the ubiquitin conjugation of apoB and its subsequent degradation by the proteasome.
577	1948	inhibited	Fbw1a	7alpha-hydroxylase	Stable expression of two different plasmids that encode either rat or human 7alpha-hydroxylase inhibited the ubiquitin conjugation of apoB and its subsequent degradation by the proteasome.
577	1949	conjugation	apoB	ubiquitin	Stable expression of two different plasmids that encode either rat or human 7alpha-hydroxylase inhibited the ubiquitin conjugation of apoB and its subsequent degradation by the proteasome.
577	1950	conjugation	ubiquitin	apoB	Stable expression of two different plasmids that encode either rat or human 7alpha-hydroxylase inhibited the ubiquitin conjugation of apoB and its subsequent degradation by the proteasome.
578	1951	interaction	RPS0A	TOM1	Strains with mutant alleles of TOM1 are defective in multiple steps in rRNA processing, and interactions between RPS0A/B and TOM1 stem, in part, from their roles in the maturation of ribosomal subunits.
578	1952	interaction	RPS0B	TOM1	Strains with mutant alleles of TOM1 are defective in multiple steps in rRNA processing, and interactions between RPS0A/B and TOM1 stem, in part, from their roles in the maturation of ribosomal subunits.
578	1953	interaction	TOM1	RPS0A	Strains with mutant alleles of TOM1 are defective in multiple steps in rRNA processing, and interactions between RPS0A/B and TOM1 stem, in part, from their roles in the maturation of ribosomal subunits.
578	1954	interaction	TOM1	RPS0B	Strains with mutant alleles of TOM1 are defective in multiple steps in rRNA processing, and interactions between RPS0A/B and TOM1 stem, in part, from their roles in the maturation of ribosomal subunits.
579	1955	modification	IkappaBalpha	SUMO	Structure-based mutagenesis and biochemical analysis of Ubc9 and RanGAP1 reveal distinct motifs required for substrate binding and SUMO modification of p53, IkappaBalpha, and RanGAP1.
579	1956	modification	RanGAP1	SUMO	Structure-based mutagenesis and biochemical analysis of Ubc9 and RanGAP1 reveal distinct motifs required for substrate binding and SUMO modification of p53, IkappaBalpha, and RanGAP1.
579	1957	modification	SUMO	IkappaBalpha	Structure-based mutagenesis and biochemical analysis of Ubc9 and RanGAP1 reveal distinct motifs required for substrate binding and SUMO modification of p53, IkappaBalpha, and RanGAP1.
579	1958	modification	SUMO	RanGAP1	Structure-based mutagenesis and biochemical analysis of Ubc9 and RanGAP1 reveal distinct motifs required for substrate binding and SUMO modification of p53, IkappaBalpha, and RanGAP1.
579	1959	modification	SUMO	p53	Structure-based mutagenesis and biochemical analysis of Ubc9 and RanGAP1 reveal distinct motifs required for substrate binding and SUMO modification of p53, IkappaBalpha, and RanGAP1.
579	1960	modification	p53	SUMO	Structure-based mutagenesis and biochemical analysis of Ubc9 and RanGAP1 reveal distinct motifs required for substrate binding and SUMO modification of p53, IkappaBalpha, and RanGAP1.
580	1961	binding	Jak1	gp130	Substitution of Tyr(107) to alanine, a residue conserved among Jaks and involved in hydrophobic core interactions of the proposed beta-grasp domain, abrogated binding of full-length Jak1 to gp130 in COS-7 transfectants.
580	1962	binding	gp130	Jak1	Substitution of Tyr(107) to alanine, a residue conserved among Jaks and involved in hydrophobic core interactions of the proposed beta-grasp domain, abrogated binding of full-length Jak1 to gp130 in COS-7 transfectants.
581	1963	interaction	ENaC	Nedd4-2	Such phosphorylation reduces the interaction between Nedd4-2 and ENaC, leading to elevated ENaC cell surface expression.
581	1964	interaction	Nedd4-2	ENaC	Such phosphorylation reduces the interaction between Nedd4-2 and ENaC, leading to elevated ENaC cell surface expression.
582	1965	Sumoylation	PIC1	p53	Sumoylation of p53 by the ubiquitin-like protein, SUMO-1/sentrin/PIC1, has been shown to stimulate its transcriptional activation activity.
582	1966	Sumoylation	p53	PIC1	Sumoylation of p53 by the ubiquitin-like protein, SUMO-1/sentrin/PIC1, has been shown to stimulate its transcriptional activation activity.
583	1967	phosphorylation	CDK2	cyclin E	Surprising, in marked contrast to cyclin E, where phosphorylation of Thr-380 by CDK2 is required for proteolysis, degradation of cyclin A was not affected by Ser-154 phosphorylation.
583	1968	phosphorylation	cyclin E	CDK2	Surprising, in marked contrast to cyclin E, where phosphorylation of Thr-380 by CDK2 is required for proteolysis, degradation of cyclin A was not affected by Ser-154 phosphorylation.
584	1969	interaction	Gag	TSG101	TSG-5' is incorporated into virions, confirming the Gag/TSG101 interaction in virus-producing cells.
584	1970	interaction	TSG101	Gag	TSG-5' is incorporated into virions, confirming the Gag/TSG101 interaction in virus-producing cells.
585	1971	conjugation	Cul-2	NEDD8	Taken together, the VBC complex appears to have ligase activity in the conjugation of NEDD8 to Cul-2.
585	1972	conjugation	NEDD8	Cul-2	Taken together, the VBC complex appears to have ligase activity in the conjugation of NEDD8 to Cul-2.
586	1973	modify	PML	SUMO-1	Taken together, these results argue that SUMO-1 modified PML can derepress Pax3 transcriptional activity through sequestration of the Daxx repressor into the NBs and suggest a role for these nuclear structures in the transcriptional control by Pax proteins.
586	1974	modify	SUMO-1	PML	Taken together, these results argue that SUMO-1 modified PML can derepress Pax3 transcriptional activity through sequestration of the Daxx repressor into the NBs and suggest a role for these nuclear structures in the transcriptional control by Pax proteins.
587	1975	bind	MDM2	p53	Taken together, these results support a model whereby MDM2 binding-deficient forms of p53 can bind MDM2 indirectly through oligomerization with wild-type p53 and are subsequently targeted for ubiquitination, nuclear export, and degradation.
587	1976	bind	p53	MDM2	Taken together, these results support a model whereby MDM2 binding-deficient forms of p53 can bind MDM2 indirectly through oligomerization with wild-type p53 and are subsequently targeted for ubiquitination, nuclear export, and degradation.
588	1977	ubiquitinate	Ste2p	rsp5	Temperature-sensitive rsp5 mutants were unable to ubiquitinate or to internalize Ste2p at the nonpermissive temperature.
588	1978	ubiquitinate	rsp5	Ste2p	Temperature-sensitive rsp5 mutants were unable to ubiquitinate or to internalize Ste2p at the nonpermissive temperature.
589	1979	target	SCF	Sic1p	Temperature-sensitive yrb1-51 mutants are defective in APC-mediated degradation of the anaphase inhibitor protein Pds1p and in degradation of the cyclin-dependent kinase inhibitor Sic1p, a target of SCF.
589	1980	target	Sic1p	SCF	Temperature-sensitive yrb1-51 mutants are defective in APC-mediated degradation of the anaphase inhibitor protein Pds1p and in degradation of the cyclin-dependent kinase inhibitor Sic1p, a target of SCF.
590	1981	modified	Pmt3	Rad22	The 83 kDa species is observed when extracts are prepared under both native and denaturing conditions, and is also observed when myc + His-tagged Rad22 and Pmt3 are expressed at wild type levels, suggesting that Rad22 is modified by Pmt3 in vivo.
590	1982	modified	Rad22	Pmt3	The 83 kDa species is observed when extracts are prepared under both native and denaturing conditions, and is also observed when myc + His-tagged Rad22 and Pmt3 are expressed at wild type levels, suggesting that Rad22 is modified by Pmt3 in vivo.
591	1983	activated	APC	CDC20	The APC is activated in mitosis and G1 by CDC20 and CDH1, and inhibited by the checkpoint protein MAD2, a specific inhibitor of CDC20.
591	1984	activated	APC	CDH1	The APC is activated in mitosis and G1 by CDC20 and CDH1, and inhibited by the checkpoint protein MAD2, a specific inhibitor of CDC20.
591	1985	inhibited	APC	MAD2	The APC is activated in mitosis and G1 by CDC20 and CDH1, and inhibited by the checkpoint protein MAD2, a specific inhibitor of CDC20.
591	1986	activated	CDC20	APC	The APC is activated in mitosis and G1 by CDC20 and CDH1, and inhibited by the checkpoint protein MAD2, a specific inhibitor of CDC20.
591	1987	inhibitor	CDC20	MAD2	The APC is activated in mitosis and G1 by CDC20 and CDH1, and inhibited by the checkpoint protein MAD2, a specific inhibitor of CDC20.
591	1988	activated	CDH1	APC	The APC is activated in mitosis and G1 by CDC20 and CDH1, and inhibited by the checkpoint protein MAD2, a specific inhibitor of CDC20.
591	1989	inhibited	MAD2	APC	The APC is activated in mitosis and G1 by CDC20 and CDH1, and inhibited by the checkpoint protein MAD2, a specific inhibitor of CDC20.
591	1990	inhibitor	MAD2	CDC20	The APC is activated in mitosis and G1 by CDC20 and CDH1, and inhibited by the checkpoint protein MAD2, a specific inhibitor of CDC20.
592	1991	interact	AhR	hsp90	The AhR mediated transcription is tightly regulated through, at least, two mechanisms: (a) the cytoplasmic AhR interacts with hsp90 and an immunophilin chaperone AIP for proper folding and receptivity, and (b) the agonist-activated, nuclear AhR is degraded through the ubiquitin-26S proteasome mediated protein turnover, such that the transcription by AhR is controlled at a physiologically adequate level.
592	1992	interact	hsp90	AhR	The AhR mediated transcription is tightly regulated through, at least, two mechanisms: (a) the cytoplasmic AhR interacts with hsp90 and an immunophilin chaperone AIP for proper folding and receptivity, and (b) the agonist-activated, nuclear AhR is degraded through the ubiquitin-26S proteasome mediated protein turnover, such that the transcription by AhR is controlled at a physiologically adequate level.
593	1993	interact	MURF-1	titin	The COOH-terminal A168-170 region of the giant sarcomeric protein titin interacts with muscle-specific RING finger-1 (MURF-1).
593	1994	interact	titin	MURF-1	The COOH-terminal A168-170 region of the giant sarcomeric protein titin interacts with muscle-specific RING finger-1 (MURF-1).
594	1995	associate	LIN-12	SEL-10	The Caenorhabditis elegans F-box- and WD40-repeat-containing protein SEL-10 functionally and physically associates with LIN-12 and SEL-12, orthologues of mammalian Notch and presenilin, respectively.
594	1996	associate	SEL-10	LIN-12	The Caenorhabditis elegans F-box- and WD40-repeat-containing protein SEL-10 functionally and physically associates with LIN-12 and SEL-12, orthologues of mammalian Notch and presenilin, respectively.
594	1997	associate	SEL-10	SEL-12	The Caenorhabditis elegans F-box- and WD40-repeat-containing protein SEL-10 functionally and physically associates with LIN-12 and SEL-12, orthologues of mammalian Notch and presenilin, respectively.
594	1998	associate	SEL-12	SEL-10	The Caenorhabditis elegans F-box- and WD40-repeat-containing protein SEL-10 functionally and physically associates with LIN-12 and SEL-12, orthologues of mammalian Notch and presenilin, respectively.
595	1999	associate	CDK	Cks	The Cks/Suc1 proteins associate with CDK/cyclin complexes, but their precise function(s) is not well defined.
595	2000	associate	CDK	Suc1	The Cks/Suc1 proteins associate with CDK/cyclin complexes, but their precise function(s) is not well defined.
595	2001	associate	Cks	CDK	The Cks/Suc1 proteins associate with CDK/cyclin complexes, but their precise function(s) is not well defined.
595	2002	associate	Cks	cyclin	The Cks/Suc1 proteins associate with CDK/cyclin complexes, but their precise function(s) is not well defined.
595	2003	associate	Suc1	CDK	The Cks/Suc1 proteins associate with CDK/cyclin complexes, but their precise function(s) is not well defined.
595	2004	associate	Suc1	cyclin	The Cks/Suc1 proteins associate with CDK/cyclin complexes, but their precise function(s) is not well defined.
595	2005	associate	cyclin	Cks	The Cks/Suc1 proteins associate with CDK/cyclin complexes, but their precise function(s) is not well defined.
595	2006	associate	cyclin	Suc1	The Cks/Suc1 proteins associate with CDK/cyclin complexes, but their precise function(s) is not well defined.
596	2007	interact	APC/C	E4orf4	The E4orf4-PP2A complex physically interacts with the APC/C, suggesting that E4orf4 functions by directly targeting PP2A to the APC/C, thereby leading to its inactivation.
596	2008	interact	APC/C	PP2A	The E4orf4-PP2A complex physically interacts with the APC/C, suggesting that E4orf4 functions by directly targeting PP2A to the APC/C, thereby leading to its inactivation.
596	2009	interact	E4orf4	APC/C	The E4orf4-PP2A complex physically interacts with the APC/C, suggesting that E4orf4 functions by directly targeting PP2A to the APC/C, thereby leading to its inactivation.
596	2010	complex	E4orf4	PP2A	The E4orf4-PP2A complex physically interacts with the APC/C, suggesting that E4orf4 functions by directly targeting PP2A to the APC/C, thereby leading to its inactivation.
596	2011	interact	PP2A	APC/C	The E4orf4-PP2A complex physically interacts with the APC/C, suggesting that E4orf4 functions by directly targeting PP2A to the APC/C, thereby leading to its inactivation.
596	2012	complex	PP2A	E4orf4	The E4orf4-PP2A complex physically interacts with the APC/C, suggesting that E4orf4 functions by directly targeting PP2A to the APC/C, thereby leading to its inactivation.
597	2013	bind	E6	p53	The E6 protein is able to bind to host p53 causing inactivation of its function through the mechanism of ubiquitin-dependent degradation.
597	2014	bind	p53	E6	The E6 protein is able to bind to host p53 causing inactivation of its function through the mechanism of ubiquitin-dependent degradation.
598	2015	interact	E6	p53	The E6-E6-AP complex specifically interacts with p53, resulting in the rapid ubiquitin-dependent degradation of p53.
598	2016	interact	E6-AP	p53	The E6-E6-AP complex specifically interacts with p53, resulting in the rapid ubiquitin-dependent degradation of p53.
598	2017	interact	p53	E6	The E6-E6-AP complex specifically interacts with p53, resulting in the rapid ubiquitin-dependent degradation of p53.
598	2018	interact	p53	E6-AP	The E6-E6-AP complex specifically interacts with p53, resulting in the rapid ubiquitin-dependent degradation of p53.
599	2019	bind	E6	p53	The E6/E6-AP complex binds to and targets the p53 tumor-suppressor protein for ubiquitin-mediated proteolysis.
599	2020	bind	E6-AP	p53	The E6/E6-AP complex binds to and targets the p53 tumor-suppressor protein for ubiquitin-mediated proteolysis.
599	2021	bind	p53	E6	The E6/E6-AP complex binds to and targets the p53 tumor-suppressor protein for ubiquitin-mediated proteolysis.
599	2022	bind	p53	E6-AP	The E6/E6-AP complex binds to and targets the p53 tumor-suppressor protein for ubiquitin-mediated proteolysis.
600	2023	binding	Cdk2	Skp2	The F box of Skp2 is required for binding to Skp1, and both the N-terminal and C-terminal regions of Skp2 are involved in binding to cyclin A-Cdk2.
600	2024	binding	Skp1	Skp2	The F box of Skp2 is required for binding to Skp1, and both the N-terminal and C-terminal regions of Skp2 are involved in binding to cyclin A-Cdk2.
600	2025	binding	Skp2	Cdk2	The F box of Skp2 is required for binding to Skp1, and both the N-terminal and C-terminal regions of Skp2 are involved in binding to cyclin A-Cdk2.
600	2026	binding	Skp2	Skp1	The F box of Skp2 is required for binding to Skp1, and both the N-terminal and C-terminal regions of Skp2 are involved in binding to cyclin A-Cdk2.
600	2027	binding	Skp2	cyclin A	The F box of Skp2 is required for binding to Skp1, and both the N-terminal and C-terminal regions of Skp2 are involved in binding to cyclin A-Cdk2.
600	2028	binding	cyclin A	Skp2	The F box of Skp2 is required for binding to Skp1, and both the N-terminal and C-terminal regions of Skp2 are involved in binding to cyclin A-Cdk2.
601	2029	interact	ASK1	ORE9	The F-box motif of ORE9 interacts with ASK1 (Arabidopsis Skp1-like 1), a component of the plant SCF complex.
601	2030	interact	ORE9	ASK1	The F-box motif of ORE9 interacts with ASK1 (Arabidopsis Skp1-like 1), a component of the plant SCF complex.
602	2031	interaction	ASK1	At5g48990	The F-box motif of the At5g48990 gene product, a member of the family, was shown to be functionally active by its ability to mediate the in vitro interaction between At5g48990 and ASK1 proteins.
602	2032	interaction	At5g48990	ASK1	The F-box motif of the At5g48990 gene product, a member of the family, was shown to be functionally active by its ability to mediate the in vitro interaction between At5g48990 and ASK1 proteins.
603	2033	associate	Skp2	cyclin D1	The F-box protein Skp2 is a component of an SCF ubiquitin ligase complex and can associate with cyclin D1 and the cdk inhibitor p21 .
603	2034	associate	Skp2	p21	The F-box protein Skp2 is a component of an SCF ubiquitin ligase complex and can associate with cyclin D1 and the cdk inhibitor p21 .
603	2035	associate	cyclin D1	Skp2	The F-box protein Skp2 is a component of an SCF ubiquitin ligase complex and can associate with cyclin D1 and the cdk inhibitor p21 .
603	2036	associate	p21	Skp2	The F-box protein Skp2 is a component of an SCF ubiquitin ligase complex and can associate with cyclin D1 and the cdk inhibitor p21 .
604	2037	binds	Cdk2	Skp2	The F-box protein Skp2 is important for S phase entry and binds to Skp1 and the cyclin A-Cdk2 complex.
604	2038	complex	Cdk2	cyclin A	The F-box protein Skp2 is important for S phase entry and binds to Skp1 and the cyclin A-Cdk2 complex.
604	2039	bind	Skp1	Skp2	The F-box protein Skp2 is important for S phase entry and binds to Skp1 and the cyclin A-Cdk2 complex.
604	2040	binds	Skp2	Cdk2	The F-box protein Skp2 is important for S phase entry and binds to Skp1 and the cyclin A-Cdk2 complex.
604	2041	bind	Skp2	Skp1	The F-box protein Skp2 is important for S phase entry and binds to Skp1 and the cyclin A-Cdk2 complex.
604	2042	binds	Skp2	cyclin A	The F-box protein Skp2 is important for S phase entry and binds to Skp1 and the cyclin A-Cdk2 complex.
604	2043	complex	cyclin A	Cdk2	The F-box protein Skp2 is important for S phase entry and binds to Skp1 and the cyclin A-Cdk2 complex.
604	2044	binds	cyclin A	Skp2	The F-box protein Skp2 is important for S phase entry and binds to Skp1 and the cyclin A-Cdk2 complex.
605	2045	interaction	Cdc13	Rum1	The G1/S transition is controlled by interactions of Cdc13/Cdc2 and its stoichiometric inhibitor, Rum1.
605	2046	interaction	Cdc2	Rum1	The G1/S transition is controlled by interactions of Cdc13/Cdc2 and its stoichiometric inhibitor, Rum1.
605	2047	interaction	Rum1	Cdc13	The G1/S transition is controlled by interactions of Cdc13/Cdc2 and its stoichiometric inhibitor, Rum1.
605	2048	interaction	Rum1	Cdc2	The G1/S transition is controlled by interactions of Cdc13/Cdc2 and its stoichiometric inhibitor, Rum1.
606	2049	interact	GABA(A)R	GABARAP	The GABA(A) receptor-associated protein GABARAP interacts with the gamma2 subunit of GABA(A)Rs and displays high homology to proteins involved in membrane fusion underlying Golgi transport and autophagic processes.
606	2050	interact	GABARAP	GABA(A)R	The GABA(A) receptor-associated protein GABARAP interacts with the gamma2 subunit of GABA(A)Rs and displays high homology to proteins involved in membrane fusion underlying Golgi transport and autophagic processes.
607	2051	bind	HDAC1	MDM2	The HDAC1 complex binds MDM2 in a p53-independent manner and deacetylates p53 at all known acetylated lysines in vivo.
607	2052	deacetylates	HDAC1	p53	The HDAC1 complex binds MDM2 in a p53-independent manner and deacetylates p53 at all known acetylated lysines in vivo.
607	2053	bind	MDM2	HDAC1	The HDAC1 complex binds MDM2 in a p53-independent manner and deacetylates p53 at all known acetylated lysines in vivo.
607	2054	deacetylates	p53	HDAC1	The HDAC1 complex binds MDM2 in a p53-independent manner and deacetylates p53 at all known acetylated lysines in vivo.
608	2055	bind	E6	p53	The HPV E6 protein from high-risk types binds p53 and mediates its degradation by the ubiquitin pathway.
608	2056	bind	p53	E6	The HPV E6 protein from high-risk types binds p53 and mediates its degradation by the ubiquitin pathway.
609	2057	complex	Cullin-1	Skp1	The IkappaB alpha ubiquitin-ligase activity associated with phosphorylated IkappaB alpha (pIkappaB alpha) in HeLa cells was almost completely lost by washing under stringent conditions including 1 M NaCl; nevertheless, an SCF(betaTrCP) complex containing Skp1, Cullin-1, and F-box/WD40 protein betaTrCP was still bound to pIkappaB alpha, suggesting the existence of a putative factor that is loosely associated with pIkappaB alpha and may collaborate with SCF(betaTrCP).
609	2058	complex	Cullin-1	betaTrCP	The IkappaB alpha ubiquitin-ligase activity associated with phosphorylated IkappaB alpha (pIkappaB alpha) in HeLa cells was almost completely lost by washing under stringent conditions including 1 M NaCl; nevertheless, an SCF(betaTrCP) complex containing Skp1, Cullin-1, and F-box/WD40 protein betaTrCP was still bound to pIkappaB alpha, suggesting the existence of a putative factor that is loosely associated with pIkappaB alpha and may collaborate with SCF(betaTrCP).
609	2059	complex	Skp1	Cullin-1	The IkappaB alpha ubiquitin-ligase activity associated with phosphorylated IkappaB alpha (pIkappaB alpha) in HeLa cells was almost completely lost by washing under stringent conditions including 1 M NaCl; nevertheless, an SCF(betaTrCP) complex containing Skp1, Cullin-1, and F-box/WD40 protein betaTrCP was still bound to pIkappaB alpha, suggesting the existence of a putative factor that is loosely associated with pIkappaB alpha and may collaborate with SCF(betaTrCP).
609	2060	complex	Skp1	betaTrCP	The IkappaB alpha ubiquitin-ligase activity associated with phosphorylated IkappaB alpha (pIkappaB alpha) in HeLa cells was almost completely lost by washing under stringent conditions including 1 M NaCl; nevertheless, an SCF(betaTrCP) complex containing Skp1, Cullin-1, and F-box/WD40 protein betaTrCP was still bound to pIkappaB alpha, suggesting the existence of a putative factor that is loosely associated with pIkappaB alpha and may collaborate with SCF(betaTrCP).
609	2061	complex	betaTrCP	Cullin-1	The IkappaB alpha ubiquitin-ligase activity associated with phosphorylated IkappaB alpha (pIkappaB alpha) in HeLa cells was almost completely lost by washing under stringent conditions including 1 M NaCl; nevertheless, an SCF(betaTrCP) complex containing Skp1, Cullin-1, and F-box/WD40 protein betaTrCP was still bound to pIkappaB alpha, suggesting the existence of a putative factor that is loosely associated with pIkappaB alpha and may collaborate with SCF(betaTrCP).
609	2062	complex	betaTrCP	Skp1	The IkappaB alpha ubiquitin-ligase activity associated with phosphorylated IkappaB alpha (pIkappaB alpha) in HeLa cells was almost completely lost by washing under stringent conditions including 1 M NaCl; nevertheless, an SCF(betaTrCP) complex containing Skp1, Cullin-1, and F-box/WD40 protein betaTrCP was still bound to pIkappaB alpha, suggesting the existence of a putative factor that is loosely associated with pIkappaB alpha and may collaborate with SCF(betaTrCP).
610	2063	binding	FWD1	IkappaBalpha	The IkappaBalpha mutant D31E still exhibited binding to FWD1 and underwent ubiquitination.
610	2064	binding	IkappaBalpha	FWD1	The IkappaBalpha mutant D31E still exhibited binding to FWD1 and underwent ubiquitination.
611	2065	bind	BE6	paxillin	The LD motifs of paxillin that bind BE6 share homology with the E6 binding site of E6-AP, a ubiquitin ligase that together with 16E6 targets the degradation of the p53 tumor suppressor.
611	2066	binding	E6	E6-AP	The LD motifs of paxillin that bind BE6 share homology with the E6 binding site of E6-AP, a ubiquitin ligase that together with 16E6 targets the degradation of the p53 tumor suppressor.
611	2067	binding	E6-AP	E6	The LD motifs of paxillin that bind BE6 share homology with the E6 binding site of E6-AP, a ubiquitin ligase that together with 16E6 targets the degradation of the p53 tumor suppressor.
611	2068	target	E6-AP	p53	The LD motifs of paxillin that bind BE6 share homology with the E6 binding site of E6-AP, a ubiquitin ligase that together with 16E6 targets the degradation of the p53 tumor suppressor.
611	2069	target	p53	E6-AP	The LD motifs of paxillin that bind BE6 share homology with the E6 binding site of E6-AP, a ubiquitin ligase that together with 16E6 targets the degradation of the p53 tumor suppressor.
611	2070	bind	paxillin	BE6	The LD motifs of paxillin that bind BE6 share homology with the E6 binding site of E6-AP, a ubiquitin ligase that together with 16E6 targets the degradation of the p53 tumor suppressor.
612	2071	modified	RanGAP1	SUMO-1	The NPC-associated form of RanGAP1 is covalently modified by the small ubiquitin-like protein, SUMO-1, and we have recently proposed that SUMO-1 modification functions to target RanGAP1 to the NPC.
612	2072	modified	SUMO-1	RanGAP1	The NPC-associated form of RanGAP1 is covalently modified by the small ubiquitin-like protein, SUMO-1, and we have recently proposed that SUMO-1 modification functions to target RanGAP1 to the NPC.
613	2073	binding	EBNA-2	RBP-Jkappa	The RBP-Jkappa binding sites of EBNA-2 and the LMP1 promoter are not required for EBNA-3C coactivation, whereas the PU1 site in the LMP1 promoter is required for EBNA-2-mediated activation and EBNA-3C coactivation.
613	2074	binding	RBP-Jkappa	EBNA-2	The RBP-Jkappa binding sites of EBNA-2 and the LMP1 promoter are not required for EBNA-3C coactivation, whereas the PU1 site in the LMP1 promoter is required for EBNA-2-mediated activation and EBNA-3C coactivation.
614	2075	interact	RAD5	UBC13-MMS2	The RING finger protein RAD5 interacts and cooperates with the UBC13-MMS2 ubiquitin-conjugating enzyme in postreplication DNA damage repair in yeast.
614	2076	interact	UBC13-MMS2	RAD5	The RING finger protein RAD5 interacts and cooperates with the UBC13-MMS2 ubiquitin-conjugating enzyme in postreplication DNA damage repair in yeast.
615	2077	complex	Cdc53	F-box protein	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2078	complex	Cdc53	Rbx1	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2079	complex	Cdc53	Skp1	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2080	complex	Cul1	F-box protein	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2081	complex	Cul1	Rbx1	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2082	complex	Cul1	Skp1	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2083	complex	Cul2	Rbx1	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2084	complex	Cul2	VHL	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2085	complex	Cul2	elongin B	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2086	complex	Cul2	elongin C	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2087	complex	F-box protein	Cdc53	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2088	complex	F-box protein	Cul1	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2089	complex	F-box protein	Rbx1	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2090	complex	F-box protein	Skp1	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2091	complex	Rbx1	Cdc53	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2092	complex	Rbx1	Cul1	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2093	complex	Rbx1	Cul2	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2094	complex	Rbx1	F-box protein	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2095	complex	Rbx1	Skp1	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2096	complex	Rbx1	VHL	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2097	complex	Rbx1	elongin B	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2098	complex	Rbx1	elongin C	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2099	complex	Skp1	Cdc53	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2100	complex	Skp1	Cul1	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2101	complex	Skp1	F-box protein	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2102	complex	Skp1	Rbx1	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2103	complex	VHL	Cul2	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2104	complex	VHL	Rbx1	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2105	complex	VHL	elongin B	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2106	complex	VHL	elongin C	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2107	complex	elongin B	Cul2	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2108	complex	elongin B	Rbx1	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2109	complex	elongin B	VHL	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2110	complex	elongin B	elongin C	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2111	complex	elongin C	Cul2	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2112	complex	elongin C	Rbx1	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2113	complex	elongin C	VHL	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
615	2114	complex	elongin C	elongin B	The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5.
616	2115	complex	Cul1	FWD1	The SCF complex containing Skp1, Cul1, and the F-box protein FWD1 (the mouse homologue of Drosophila Slimb and Xenopus beta-TrCP) functions as the ubiquitin ligase for IkappaBalpha.
616	2116	complex	Cul1	Skp1	The SCF complex containing Skp1, Cul1, and the F-box protein FWD1 (the mouse homologue of Drosophila Slimb and Xenopus beta-TrCP) functions as the ubiquitin ligase for IkappaBalpha.
616	2117	complex	FWD1	Cul1	The SCF complex containing Skp1, Cul1, and the F-box protein FWD1 (the mouse homologue of Drosophila Slimb and Xenopus beta-TrCP) functions as the ubiquitin ligase for IkappaBalpha.
616	2118	complex	FWD1	Skp1	The SCF complex containing Skp1, Cul1, and the F-box protein FWD1 (the mouse homologue of Drosophila Slimb and Xenopus beta-TrCP) functions as the ubiquitin ligase for IkappaBalpha.
616	2119	complex	Skp1	Cul1	The SCF complex containing Skp1, Cul1, and the F-box protein FWD1 (the mouse homologue of Drosophila Slimb and Xenopus beta-TrCP) functions as the ubiquitin ligase for IkappaBalpha.
616	2120	complex	Skp1	FWD1	The SCF complex containing Skp1, Cul1, and the F-box protein FWD1 (the mouse homologue of Drosophila Slimb and Xenopus beta-TrCP) functions as the ubiquitin ligase for IkappaBalpha.
617	2121	interact	AR	Ubc9	The SUMO-1-conjugating enzyme Ubc9 interacts with androgen receptor (AR), a ligand-activated transcription factor belonging to the steroid receptor superfamily.
617	2122	interact	Ubc9	AR	The SUMO-1-conjugating enzyme Ubc9 interacts with androgen receptor (AR), a ligand-activated transcription factor belonging to the steroid receptor superfamily.
618	2123	ubiquitinate	AhR	TCDD	The TCDD-induced degradation of AhR involves ubiquitination of the AhR protein, because (a) TCDD induces formation of high molecular weight, ubiquitinated AhR and (b) degradation of AhR is inhibited in ts20 cells, which bear a temperature-sensitive mutation in the ubiquitin-activating enzyme E1, at a nonpermissive temperature.
618	2124	ubiquitinate	TCDD	AhR	The TCDD-induced degradation of AhR involves ubiquitination of the AhR protein, because (a) TCDD induces formation of high molecular weight, ubiquitinated AhR and (b) degradation of AhR is inhibited in ts20 cells, which bear a temperature-sensitive mutation in the ubiquitin-activating enzyme E1, at a nonpermissive temperature.
619	2125	interact	TNF-alpha	TRAF-C	The TRAF-C region interacts with TNF-alpha receptors and TNF-receptor associated death-domain (TRADD) proteins; however, our findings indicate that these interactions are unlikely to be mimicked by Siah.
619	2126	interact	TRAF-C	TNF-alpha	The TRAF-C region interacts with TNF-alpha receptors and TNF-receptor associated death-domain (TRADD) proteins; however, our findings indicate that these interactions are unlikely to be mimicked by Siah.
620	2127	bind	Gag	Tsg101	The UEV domain of Tsg101 binds to an essential tetrapeptide (PTAP) motif within the p6 domain of the structural Gag protein and also to ubiquitin.
620	2128	bind	Tsg101	Gag	The UEV domain of Tsg101 binds to an essential tetrapeptide (PTAP) motif within the p6 domain of the structural Gag protein and also to ubiquitin.
620	2129	bind	Tsg101	ubiquitin	The UEV domain of Tsg101 binds to an essential tetrapeptide (PTAP) motif within the p6 domain of the structural Gag protein and also to ubiquitin.
620	2130	bind	ubiquitin	Tsg101	The UEV domain of Tsg101 binds to an essential tetrapeptide (PTAP) motif within the p6 domain of the structural Gag protein and also to ubiquitin.
621	2131	bind	APC/C	CDC	The WD-repeat protein called p55(CDC)(Cdc20) directly binds to and activates APC/C.
621	2132	bind	APC/C	Cdc20	The WD-repeat protein called p55(CDC)(Cdc20) directly binds to and activates APC/C.
621	2133	bind	APC/C	p55	The WD-repeat protein called p55(CDC)(Cdc20) directly binds to and activates APC/C.
621	2134	bind	CDC	APC/C	The WD-repeat protein called p55(CDC)(Cdc20) directly binds to and activates APC/C.
621	2135	bind	Cdc20	APC/C	The WD-repeat protein called p55(CDC)(Cdc20) directly binds to and activates APC/C.
621	2136	bind	p55	APC/C	The WD-repeat protein called p55(CDC)(Cdc20) directly binds to and activates APC/C.
622	2137	binding	Cdc4	Sic1	The WD40 repeat domain of Cdc4 binds with high affinity to a consensus phosphopeptide motif (the Cdc4 phospho-degron, CPD), yet Sic1 itself has many sub-optimal CPD motifs that act in concert to mediate Cdc4 binding.
622	2138	binding	Sic1	Cdc4	The WD40 repeat domain of Cdc4 binds with high affinity to a consensus phosphopeptide motif (the Cdc4 phospho-degron, CPD), yet Sic1 itself has many sub-optimal CPD motifs that act in concert to mediate Cdc4 binding.
623	2139	complex	ERCC1	PIC2	The XPF.ERCC1 complex bound to PIC2, forming PIC3, which led to dual incisions and the release of the excised oligomer.
623	2140	complex	ERCC1	XPF	The XPF.ERCC1 complex bound to PIC2, forming PIC3, which led to dual incisions and the release of the excised oligomer.
623	2141	complex	PIC2	ERCC1	The XPF.ERCC1 complex bound to PIC2, forming PIC3, which led to dual incisions and the release of the excised oligomer.
623	2142	complex	PIC2	XPF	The XPF.ERCC1 complex bound to PIC2, forming PIC3, which led to dual incisions and the release of the excised oligomer.
623	2143	complex	XPF	ERCC1	The XPF.ERCC1 complex bound to PIC2, forming PIC3, which led to dual incisions and the release of the excised oligomer.
623	2144	complex	XPF	PIC2	The XPF.ERCC1 complex bound to PIC2, forming PIC3, which led to dual incisions and the release of the excised oligomer.
624	2145	interaction	Commissureless	DNedd4	The ability of Commissureless to regulate Robo in the embryo also requires a Commissureless/DNedd4 interaction.
624	2146	interaction	DNedd4	Commissureless	The ability of Commissureless to regulate Robo in the embryo also requires a Commissureless/DNedd4 interaction.
625	2147	bind	p62	ubiquitin	The ability of p62 to bind noncovalently to ubiquitin and to several signalling proteins suggests that p62 may play a regulatory role connected to the ubiquitin system.
625	2148	bind	ubiquitin	p62	The ability of p62 to bind noncovalently to ubiquitin and to several signalling proteins suggests that p62 may play a regulatory role connected to the ubiquitin system.
626	2149	conjugation	H2A	ubiquitin	The ability of this protein to catalyze the conjugation of ubiquitin to histone H2A and H2B was also examined.
626	2150	conjugation	H2B	ubiquitin	The ability of this protein to catalyze the conjugation of ubiquitin to histone H2A and H2B was also examined.
626	2151	conjugation	ubiquitin	H2A	The ability of this protein to catalyze the conjugation of ubiquitin to histone H2A and H2B was also examined.
626	2152	conjugation	ubiquitin	H2B	The ability of this protein to catalyze the conjugation of ubiquitin to histone H2A and H2B was also examined.
627	2153	transfer	SAE2	SUMO-1	The addition of the SUMO-1-conjugating enzyme Ubch9 resulted in efficient transfer of the thioester-linked SUMO-1 from SAE2 to Ubch9.
627	2154	transfer	SUMO-1	SAE2	The addition of the SUMO-1-conjugating enzyme Ubch9 resulted in efficient transfer of the thioester-linked SUMO-1 from SAE2 to Ubch9.
627	2155	transfer	SUMO-1	Ubch9	The addition of the SUMO-1-conjugating enzyme Ubch9 resulted in efficient transfer of the thioester-linked SUMO-1 from SAE2 to Ubch9.
627	2156	transfer	Ubch9	SUMO-1	The addition of the SUMO-1-conjugating enzyme Ubch9 resulted in efficient transfer of the thioester-linked SUMO-1 from SAE2 to Ubch9.
628	2157	activate	APC	Cdc20	The anaphase-promoting complex/cyclosome (APC) ubiquitin ligase is activated by Cdc20 and Cdh1 and inhibited by Mad2 and the spindle assembly checkpoint complex, Mad2B, and the early mitotic inhibitor Emi1.
628	2158	activate	APC	Cdh1	The anaphase-promoting complex/cyclosome (APC) ubiquitin ligase is activated by Cdc20 and Cdh1 and inhibited by Mad2 and the spindle assembly checkpoint complex, Mad2B, and the early mitotic inhibitor Emi1.
628	2159	inhibit	APC	Emi1	The anaphase-promoting complex/cyclosome (APC) ubiquitin ligase is activated by Cdc20 and Cdh1 and inhibited by Mad2 and the spindle assembly checkpoint complex, Mad2B, and the early mitotic inhibitor Emi1.
628	2160	inhibit	APC	Mad2	The anaphase-promoting complex/cyclosome (APC) ubiquitin ligase is activated by Cdc20 and Cdh1 and inhibited by Mad2 and the spindle assembly checkpoint complex, Mad2B, and the early mitotic inhibitor Emi1.
628	2161	inhibit	APC	Mad2B	The anaphase-promoting complex/cyclosome (APC) ubiquitin ligase is activated by Cdc20 and Cdh1 and inhibited by Mad2 and the spindle assembly checkpoint complex, Mad2B, and the early mitotic inhibitor Emi1.
628	2162	activate	Cdc20	APC	The anaphase-promoting complex/cyclosome (APC) ubiquitin ligase is activated by Cdc20 and Cdh1 and inhibited by Mad2 and the spindle assembly checkpoint complex, Mad2B, and the early mitotic inhibitor Emi1.
628	2163	activate	Cdh1	APC	The anaphase-promoting complex/cyclosome (APC) ubiquitin ligase is activated by Cdc20 and Cdh1 and inhibited by Mad2 and the spindle assembly checkpoint complex, Mad2B, and the early mitotic inhibitor Emi1.
628	2164	inhibit	Emi1	APC	The anaphase-promoting complex/cyclosome (APC) ubiquitin ligase is activated by Cdc20 and Cdh1 and inhibited by Mad2 and the spindle assembly checkpoint complex, Mad2B, and the early mitotic inhibitor Emi1.
628	2165	inhibit	Mad2	APC	The anaphase-promoting complex/cyclosome (APC) ubiquitin ligase is activated by Cdc20 and Cdh1 and inhibited by Mad2 and the spindle assembly checkpoint complex, Mad2B, and the early mitotic inhibitor Emi1.
628	2166	inhibit	Mad2B	APC	The anaphase-promoting complex/cyclosome (APC) ubiquitin ligase is activated by Cdc20 and Cdh1 and inhibited by Mad2 and the spindle assembly checkpoint complex, Mad2B, and the early mitotic inhibitor Emi1.
629	2167	transfer	Rsc1083	ubiquitin	The assay measures the transfer of ubiquitin from Ubc4 to HECT protein Rsc 1083.
629	2168	transfer	Ubc4	ubiquitin	The assay measures the transfer of ubiquitin from Ubc4 to HECT protein Rsc 1083.
629	2169	transfer	ubiquitin	Rsc1083	The assay measures the transfer of ubiquitin from Ubc4 to HECT protein Rsc 1083.
629	2170	transfer	ubiquitin	Ubc4	The assay measures the transfer of ubiquitin from Ubc4 to HECT protein Rsc 1083.
630	2171	association	MITF	hUBC9	The association of MITF with hUBC9 was further confirmed by an in vitro GST pull-down assay.
630	2172	association	hUBC9	MITF	The association of MITF with hUBC9 was further confirmed by an in vitro GST pull-down assay.
631	2173	binding	Mdm2	p53	The binding of Mdm2 to p53 is essential for ubiquitination, but p53's tertiary structure and/or C-terminal region may also be important for this reaction.
631	2174	binding	p53	Mdm2	The binding of Mdm2 to p53 is essential for ubiquitination, but p53's tertiary structure and/or C-terminal region may also be important for this reaction.
632	2175	complex	CDC53p	SKP1	The budding yeast gene product, CDC53p, forms E3-like SCF complexes with SKP1 and F-box-containing proteins to mediate the ubiquitin-dependent degradation of G1 cyclins and cyclin-dependent kinase (CDK) inhibitors.
632	2176	complex	SKP1	CDC53p	The budding yeast gene product, CDC53p, forms E3-like SCF complexes with SKP1 and F-box-containing proteins to mediate the ubiquitin-dependent degradation of G1 cyclins and cyclin-dependent kinase (CDK) inhibitors.
633	2177	bind	Rad23	Rad4	The carboxy terminus of Rad23 binds to the Rad4 DNA repair protein and creates a link between the DNA repair and proteasome pathways.
633	2178	bind	Rad4	Rad23	The carboxy terminus of Rad23 binds to the Rad4 DNA repair protein and creates a link between the DNA repair and proteasome pathways.
634	2179	interact	ARF1	p619	The carboxy-terminal RCC1-like domain of p619 interacts specifically with myristoylated ARF1, a small GTP binding protein also located in the Golgi.
634	2180	interact	p619	ARF1	The carboxy-terminal RCC1-like domain of p619 interacts specifically with myristoylated ARF1, a small GTP binding protein also located in the Golgi.
635	2181	interaction	ENaC	Nedd4	The carboxyl terminus of each ENaC subunit contains a PPXY motif that is believed to be important for interaction with the WW domains of the ubiquitin-protein ligases, Nedd4 and Nedd4-2.
635	2182	interaction	ENaC	Nedd4-2	The carboxyl terminus of each ENaC subunit contains a PPXY motif that is believed to be important for interaction with the WW domains of the ubiquitin-protein ligases, Nedd4 and Nedd4-2.
635	2183	interaction	Nedd4	ENaC	The carboxyl terminus of each ENaC subunit contains a PPXY motif that is believed to be important for interaction with the WW domains of the ubiquitin-protein ligases, Nedd4 and Nedd4-2.
635	2184	interaction	Nedd4-2	ENaC	The carboxyl terminus of each ENaC subunit contains a PPXY motif that is believed to be important for interaction with the WW domains of the ubiquitin-protein ligases, Nedd4 and Nedd4-2.
636	2185	target	SKP2	kip1	The cell cycle inhibitor p27(kip1) is a known target of the SCF(SKP2) complex, and Myc-induced Cul1 expression matched well with the kinetics of declining p27(kip1) protein.
636	2186	target	SKP2	p27	The cell cycle inhibitor p27(kip1) is a known target of the SCF(SKP2) complex, and Myc-induced Cul1 expression matched well with the kinetics of declining p27(kip1) protein.
636	2187	target	kip1	SKP2	The cell cycle inhibitor p27(kip1) is a known target of the SCF(SKP2) complex, and Myc-induced Cul1 expression matched well with the kinetics of declining p27(kip1) protein.
636	2188	target	p27	SKP2	The cell cycle inhibitor p27(kip1) is a known target of the SCF(SKP2) complex, and Myc-induced Cul1 expression matched well with the kinetics of declining p27(kip1) protein.
637	2189	target	Cln2p	SCF	The cells displayed multiple genetic interactions with mutations in known SCF components and were defective for the degradation of several SCF targets including Gic2p, Far1p, Sic1p, and Cln2p.
637	2190	target	Far1p	SCF	The cells displayed multiple genetic interactions with mutations in known SCF components and were defective for the degradation of several SCF targets including Gic2p, Far1p, Sic1p, and Cln2p.
637	2191	target	Gic2p	SCF	The cells displayed multiple genetic interactions with mutations in known SCF components and were defective for the degradation of several SCF targets including Gic2p, Far1p, Sic1p, and Cln2p.
637	2192	target	SCF	Cln2p	The cells displayed multiple genetic interactions with mutations in known SCF components and were defective for the degradation of several SCF targets including Gic2p, Far1p, Sic1p, and Cln2p.
637	2193	target	SCF	Far1p	The cells displayed multiple genetic interactions with mutations in known SCF components and were defective for the degradation of several SCF targets including Gic2p, Far1p, Sic1p, and Cln2p.
637	2194	target	SCF	Gic2p	The cells displayed multiple genetic interactions with mutations in known SCF components and were defective for the degradation of several SCF targets including Gic2p, Far1p, Sic1p, and Cln2p.
637	2195	target	SCF	Sic1p	The cells displayed multiple genetic interactions with mutations in known SCF components and were defective for the degradation of several SCF targets including Gic2p, Far1p, Sic1p, and Cln2p.
637	2196	target	Sic1p	SCF	The cells displayed multiple genetic interactions with mutations in known SCF components and were defective for the degradation of several SCF targets including Gic2p, Far1p, Sic1p, and Cln2p.
638	2197	bind	TAF(II)31	p53	The coactivator protein TAF(II)31 binds to p53 at the amino-terminal region that is also required for interaction with mdm2.
638	2198	interaction	mdm2	p53	The coactivator protein TAF(II)31 binds to p53 at the amino-terminal region that is also required for interaction with mdm2.
638	2199	bind	p53	TAF(II)31	The coactivator protein TAF(II)31 binds to p53 at the amino-terminal region that is also required for interaction with mdm2.
638	2200	interaction	p53	mdm2	The coactivator protein TAF(II)31 binds to p53 at the amino-terminal region that is also required for interaction with mdm2.
639	2201	bind	CLB5	SIC1	The complementary C-terminal segment of SIC1 binds to the S-phase cyclin CLB5, indicating a modular structure for SIC1.
639	2202	bind	SIC1	CLB5	The complementary C-terminal segment of SIC1 binds to the S-phase cyclin CLB5, indicating a modular structure for SIC1.
640	2203	interact	E6	p53	The complex of E6 and E6-AP specifically interacts with p53 and induces the ubiquitination of p53 in a reaction which requires the ubiquitin-activating enzyme (E1) and a cellular fraction thought to contain a mammalian ubiquitin-conjugating enzyme (E2).
640	2204	interact	E6-AP	p53	The complex of E6 and E6-AP specifically interacts with p53 and induces the ubiquitination of p53 in a reaction which requires the ubiquitin-activating enzyme (E1) and a cellular fraction thought to contain a mammalian ubiquitin-conjugating enzyme (E2).
640	2205	interact	p53	E6	The complex of E6 and E6-AP specifically interacts with p53 and induces the ubiquitination of p53 in a reaction which requires the ubiquitin-activating enzyme (E1) and a cellular fraction thought to contain a mammalian ubiquitin-conjugating enzyme (E2).
640	2206	interact	p53	E6-AP	The complex of E6 and E6-AP specifically interacts with p53 and induces the ubiquitination of p53 in a reaction which requires the ubiquitin-activating enzyme (E1) and a cellular fraction thought to contain a mammalian ubiquitin-conjugating enzyme (E2).
641	2207	interact	E6	p53	The complex of E6-AP and E6 specifically interacts with p53 and mediates ubiquitination of p53 in concert with the E1 ubiquitin-activating enzyme and the E2 ubiquitin-conjugating enzyme UbcH5.
641	2208	interact	E6-AP	p53	The complex of E6-AP and E6 specifically interacts with p53 and mediates ubiquitination of p53 in concert with the E1 ubiquitin-activating enzyme and the E2 ubiquitin-conjugating enzyme UbcH5.
641	2209	interact	p53	E6	The complex of E6-AP and E6 specifically interacts with p53 and mediates ubiquitination of p53 in concert with the E1 ubiquitin-activating enzyme and the E2 ubiquitin-conjugating enzyme UbcH5.
641	2210	interact	p53	E6-AP	The complex of E6-AP and E6 specifically interacts with p53 and mediates ubiquitination of p53 in concert with the E1 ubiquitin-activating enzyme and the E2 ubiquitin-conjugating enzyme UbcH5.
642	2211	conjugation	H2A	ubiquitin	The conjugation of ubiquitin to histones H2A and H2B has been established in higher eukaryotes and has been related to changes in chromatin organization.
642	2212	conjugation	H2B	ubiquitin	The conjugation of ubiquitin to histones H2A and H2B has been established in higher eukaryotes and has been related to changes in chromatin organization.
642	2213	conjugation	ubiquitin	H2A	The conjugation of ubiquitin to histones H2A and H2B has been established in higher eukaryotes and has been related to changes in chromatin organization.
642	2214	conjugation	ubiquitin	H2B	The conjugation of ubiquitin to histones H2A and H2B has been established in higher eukaryotes and has been related to changes in chromatin organization.
643	2215	bound	HIF-1 alpha	elongin B	The crystal structure of a hydroxylated HIF-1 alpha peptide bound to VCB (pVHL, elongins C and B) and solution binding assays reveal a single, conserved hydroxyproline-binding pocket in pVHL.
643	2216	bound	HIF-1 alpha	elongin C	The crystal structure of a hydroxylated HIF-1 alpha peptide bound to VCB (pVHL, elongins C and B) and solution binding assays reveal a single, conserved hydroxyproline-binding pocket in pVHL.
643	2217	bound	HIF-1 alpha	pVHL	The crystal structure of a hydroxylated HIF-1 alpha peptide bound to VCB (pVHL, elongins C and B) and solution binding assays reveal a single, conserved hydroxyproline-binding pocket in pVHL.
643	2218	bound	elongin B	HIF-1 alpha	The crystal structure of a hydroxylated HIF-1 alpha peptide bound to VCB (pVHL, elongins C and B) and solution binding assays reveal a single, conserved hydroxyproline-binding pocket in pVHL.
643	2219	bound	elongin C	HIF-1 alpha	The crystal structure of a hydroxylated HIF-1 alpha peptide bound to VCB (pVHL, elongins C and B) and solution binding assays reveal a single, conserved hydroxyproline-binding pocket in pVHL.
643	2220	bound	pVHL	HIF-1 alpha	The crystal structure of a hydroxylated HIF-1 alpha peptide bound to VCB (pVHL, elongins C and B) and solution binding assays reveal a single, conserved hydroxyproline-binding pocket in pVHL.
644	2221	complex	CUL-1	SKP1	The data presented here imply that the p45(SKP2)-CUL-1-p19(SKP1) complex may be a human representative of an SCF-type E3 ubiquitin protein ligase.
644	2222	complex	CUL-1	SKP2	The data presented here imply that the p45(SKP2)-CUL-1-p19(SKP1) complex may be a human representative of an SCF-type E3 ubiquitin protein ligase.
644	2223	complex	CUL-1	p19	The data presented here imply that the p45(SKP2)-CUL-1-p19(SKP1) complex may be a human representative of an SCF-type E3 ubiquitin protein ligase.
644	2224	complex	CUL-1	p45	The data presented here imply that the p45(SKP2)-CUL-1-p19(SKP1) complex may be a human representative of an SCF-type E3 ubiquitin protein ligase.
644	2225	complex	SKP1	CUL-1	The data presented here imply that the p45(SKP2)-CUL-1-p19(SKP1) complex may be a human representative of an SCF-type E3 ubiquitin protein ligase.
644	2226	complex	SKP1	SKP2	The data presented here imply that the p45(SKP2)-CUL-1-p19(SKP1) complex may be a human representative of an SCF-type E3 ubiquitin protein ligase.
644	2227	complex	SKP1	p45	The data presented here imply that the p45(SKP2)-CUL-1-p19(SKP1) complex may be a human representative of an SCF-type E3 ubiquitin protein ligase.
644	2228	complex	SKP2	CUL-1	The data presented here imply that the p45(SKP2)-CUL-1-p19(SKP1) complex may be a human representative of an SCF-type E3 ubiquitin protein ligase.
644	2229	complex	SKP2	SKP1	The data presented here imply that the p45(SKP2)-CUL-1-p19(SKP1) complex may be a human representative of an SCF-type E3 ubiquitin protein ligase.
644	2230	complex	SKP2	p19	The data presented here imply that the p45(SKP2)-CUL-1-p19(SKP1) complex may be a human representative of an SCF-type E3 ubiquitin protein ligase.
644	2231	complex	p19	CUL-1	The data presented here imply that the p45(SKP2)-CUL-1-p19(SKP1) complex may be a human representative of an SCF-type E3 ubiquitin protein ligase.
644	2232	complex	p19	SKP2	The data presented here imply that the p45(SKP2)-CUL-1-p19(SKP1) complex may be a human representative of an SCF-type E3 ubiquitin protein ligase.
644	2233	complex	p19	p45	The data presented here imply that the p45(SKP2)-CUL-1-p19(SKP1) complex may be a human representative of an SCF-type E3 ubiquitin protein ligase.
644	2234	complex	p45	CUL-1	The data presented here imply that the p45(SKP2)-CUL-1-p19(SKP1) complex may be a human representative of an SCF-type E3 ubiquitin protein ligase.
644	2235	complex	p45	SKP1	The data presented here imply that the p45(SKP2)-CUL-1-p19(SKP1) complex may be a human representative of an SCF-type E3 ubiquitin protein ligase.
644	2236	complex	p45	p19	The data presented here imply that the p45(SKP2)-CUL-1-p19(SKP1) complex may be a human representative of an SCF-type E3 ubiquitin protein ligase.
645	2237	complex	SKP1	SKP2	The dependency of p45(SKP2)-p19(SKP1) complex formation on cyclin A-CDK2 may ensure tight coordination of the activities of the cell cycle clock with those of a potential ubiquitin conjugation pathway.
645	2238	complex	SKP1	p45	The dependency of p45(SKP2)-p19(SKP1) complex formation on cyclin A-CDK2 may ensure tight coordination of the activities of the cell cycle clock with those of a potential ubiquitin conjugation pathway.
645	2239	complex	SKP2	SKP1	The dependency of p45(SKP2)-p19(SKP1) complex formation on cyclin A-CDK2 may ensure tight coordination of the activities of the cell cycle clock with those of a potential ubiquitin conjugation pathway.
645	2240	complex	SKP2	p19	The dependency of p45(SKP2)-p19(SKP1) complex formation on cyclin A-CDK2 may ensure tight coordination of the activities of the cell cycle clock with those of a potential ubiquitin conjugation pathway.
645	2241	complex	p19	SKP2	The dependency of p45(SKP2)-p19(SKP1) complex formation on cyclin A-CDK2 may ensure tight coordination of the activities of the cell cycle clock with those of a potential ubiquitin conjugation pathway.
645	2242	complex	p19	p45	The dependency of p45(SKP2)-p19(SKP1) complex formation on cyclin A-CDK2 may ensure tight coordination of the activities of the cell cycle clock with those of a potential ubiquitin conjugation pathway.
645	2243	complex	p45	SKP1	The dependency of p45(SKP2)-p19(SKP1) complex formation on cyclin A-CDK2 may ensure tight coordination of the activities of the cell cycle clock with those of a potential ubiquitin conjugation pathway.
645	2244	complex	p45	p19	The dependency of p45(SKP2)-p19(SKP1) complex formation on cyclin A-CDK2 may ensure tight coordination of the activities of the cell cycle clock with those of a potential ubiquitin conjugation pathway.
646	2245	interaction	UIP	UbcM4	The effects of L2 mutations on UbcM4/UIP interaction are different for each UIP, indicating that RING finger domains can vary considerably in their structural requirements for binding to E2 enzymes.
646	2246	interaction	UbcM4	UIP	The effects of L2 mutations on UbcM4/UIP interaction are different for each UIP, indicating that RING finger domains can vary considerably in their structural requirements for binding to E2 enzymes.
647	2247	complex	elongin B	elongin C	The elongin BC dimer acts as a bridge between pVHL and hCUL-2 because pVHL and hCUL-2 can form distinct complexes with elongins B and C.
647	2248	complex	elongin B	hCUL-2	The elongin BC dimer acts as a bridge between pVHL and hCUL-2 because pVHL and hCUL-2 can form distinct complexes with elongins B and C.
647	2249	complex	elongin B	pVHL	The elongin BC dimer acts as a bridge between pVHL and hCUL-2 because pVHL and hCUL-2 can form distinct complexes with elongins B and C.
647	2250	complex	elongin C	elongin B	The elongin BC dimer acts as a bridge between pVHL and hCUL-2 because pVHL and hCUL-2 can form distinct complexes with elongins B and C.
647	2251	complex	elongin C	hCUL-2	The elongin BC dimer acts as a bridge between pVHL and hCUL-2 because pVHL and hCUL-2 can form distinct complexes with elongins B and C.
647	2252	complex	elongin C	pVHL	The elongin BC dimer acts as a bridge between pVHL and hCUL-2 because pVHL and hCUL-2 can form distinct complexes with elongins B and C.
647	2253	complex	hCUL-2	elongin B	The elongin BC dimer acts as a bridge between pVHL and hCUL-2 because pVHL and hCUL-2 can form distinct complexes with elongins B and C.
647	2254	complex	hCUL-2	elongin C	The elongin BC dimer acts as a bridge between pVHL and hCUL-2 because pVHL and hCUL-2 can form distinct complexes with elongins B and C.
647	2255	complex	hCUL-2	pVHL	The elongin BC dimer acts as a bridge between pVHL and hCUL-2 because pVHL and hCUL-2 can form distinct complexes with elongins B and C.
647	2256	complex	pVHL	elongin B	The elongin BC dimer acts as a bridge between pVHL and hCUL-2 because pVHL and hCUL-2 can form distinct complexes with elongins B and C.
647	2257	complex	pVHL	elongin C	The elongin BC dimer acts as a bridge between pVHL and hCUL-2 because pVHL and hCUL-2 can form distinct complexes with elongins B and C.
647	2258	complex	pVHL	hCUL-2	The elongin BC dimer acts as a bridge between pVHL and hCUL-2 because pVHL and hCUL-2 can form distinct complexes with elongins B and C.
648	2259	phosphorylate	IKK	IkappaB	The essential features of this cascade are that a mitogen-activated protein kinase kinase kinase (MAP3K) activates an IkappaB kinase (IKK) that site-specifically phosphorylates IkappaB.
648	2260	activate	IKK	MAP3K	The essential features of this cascade are that a mitogen-activated protein kinase kinase kinase (MAP3K) activates an IkappaB kinase (IKK) that site-specifically phosphorylates IkappaB.
648	2261	phosphorylate	IkappaB	IKK	The essential features of this cascade are that a mitogen-activated protein kinase kinase kinase (MAP3K) activates an IkappaB kinase (IKK) that site-specifically phosphorylates IkappaB.
648	2262	activate	MAP3K	IKK	The essential features of this cascade are that a mitogen-activated protein kinase kinase kinase (MAP3K) activates an IkappaB kinase (IKK) that site-specifically phosphorylates IkappaB.
649	2263	interaction	VBC	hCUL-2	The first amino-terminal 108 aa of hCUL-2 are necessary for interaction with the VBC complex.
649	2264	interaction	hCUL-2	VBC	The first amino-terminal 108 aa of hCUL-2 are necessary for interaction with the VBC complex.
650	2265	activation	AXR1	RUB	The first step in the pathway is RUB activation by a bipartite enzyme composed of the AXR1 and ECR1 proteins.
650	2266	activation	ECR1	RUB	The first step in the pathway is RUB activation by a bipartite enzyme composed of the AXR1 and ECR1 proteins.
650	2267	activation	RUB	AXR1	The first step in the pathway is RUB activation by a bipartite enzyme composed of the AXR1 and ECR1 proteins.
650	2268	activation	RUB	ECR1	The first step in the pathway is RUB activation by a bipartite enzyme composed of the AXR1 and ECR1 proteins.
651	2269	interaction	sel-10	sel-12	The functional and physical interaction between sel-10 and sel-12 therefore offers an approach to understanding how presenilin levels are normally regulated.
651	2270	interaction	sel-12	sel-10	The functional and physical interaction between sel-10 and sel-12 therefore offers an approach to understanding how presenilin levels are normally regulated.
652	2271	interact	Cullin	hFBH1	The hFBH1 enzyme interacted with human SKP1 and formed an SCF (SKP1/Cullin/F-box) complex together with human Cullin and ROC1.
652	2272	interact	ROC1	hFBH1	The hFBH1 enzyme interacted with human SKP1 and formed an SCF (SKP1/Cullin/F-box) complex together with human Cullin and ROC1.
652	2273	interact	SKP1	hFBH1	The hFBH1 enzyme interacted with human SKP1 and formed an SCF (SKP1/Cullin/F-box) complex together with human Cullin and ROC1.
652	2274	interact	hFBH1	Cullin	The hFBH1 enzyme interacted with human SKP1 and formed an SCF (SKP1/Cullin/F-box) complex together with human Cullin and ROC1.
652	2275	interact	hFBH1	ROC1	The hFBH1 enzyme interacted with human SKP1 and formed an SCF (SKP1/Cullin/F-box) complex together with human Cullin and ROC1.
652	2276	interact	hFBH1	SKP1	The hFBH1 enzyme interacted with human SKP1 and formed an SCF (SKP1/Cullin/F-box) complex together with human Cullin and ROC1.
653	2277	interact	PIC1	PML	The human ubiquitin-homology domain protein PIC1 interacts with the acute promyelocytic leukemia protein PML, and both proteins form part of the large, nuclear, multiprotein complexes known as PML nuclear bodies.
653	2278	interact	PML	PIC1	The human ubiquitin-homology domain protein PIC1 interacts with the acute promyelocytic leukemia protein PML, and both proteins form part of the large, nuclear, multiprotein complexes known as PML nuclear bodies.
654	2279	complex	CDC53	F-box	The identification of CUL-1 as a member of the complex raises the possibility that the p19(SKP1)/p45(SKP2)/CUL-1 complex may function as the yeast SKP1-CDC53-F-box (SCF) protein complex that acts as a ubiquitin E3 ligase to regulate the G1/S transition.
654	2280	complex	CDC53	SKP1	The identification of CUL-1 as a member of the complex raises the possibility that the p19(SKP1)/p45(SKP2)/CUL-1 complex may function as the yeast SKP1-CDC53-F-box (SCF) protein complex that acts as a ubiquitin E3 ligase to regulate the G1/S transition.
654	2281	complex	CUL-1	SKP1	The identification of CUL-1 as a member of the complex raises the possibility that the p19(SKP1)/p45(SKP2)/CUL-1 complex may function as the yeast SKP1-CDC53-F-box (SCF) protein complex that acts as a ubiquitin E3 ligase to regulate the G1/S transition.
654	2282	complex	CUL-1	SKP2	The identification of CUL-1 as a member of the complex raises the possibility that the p19(SKP1)/p45(SKP2)/CUL-1 complex may function as the yeast SKP1-CDC53-F-box (SCF) protein complex that acts as a ubiquitin E3 ligase to regulate the G1/S transition.
654	2283	complex	CUL-1	p19	The identification of CUL-1 as a member of the complex raises the possibility that the p19(SKP1)/p45(SKP2)/CUL-1 complex may function as the yeast SKP1-CDC53-F-box (SCF) protein complex that acts as a ubiquitin E3 ligase to regulate the G1/S transition.
654	2284	complex	CUL-1	p45	The identification of CUL-1 as a member of the complex raises the possibility that the p19(SKP1)/p45(SKP2)/CUL-1 complex may function as the yeast SKP1-CDC53-F-box (SCF) protein complex that acts as a ubiquitin E3 ligase to regulate the G1/S transition.
654	2285	complex	F-box	CDC53	The identification of CUL-1 as a member of the complex raises the possibility that the p19(SKP1)/p45(SKP2)/CUL-1 complex may function as the yeast SKP1-CDC53-F-box (SCF) protein complex that acts as a ubiquitin E3 ligase to regulate the G1/S transition.
654	2286	complex	F-box	SKP1	The identification of CUL-1 as a member of the complex raises the possibility that the p19(SKP1)/p45(SKP2)/CUL-1 complex may function as the yeast SKP1-CDC53-F-box (SCF) protein complex that acts as a ubiquitin E3 ligase to regulate the G1/S transition.
654	2287	complex	SKP1	CDC53	The identification of CUL-1 as a member of the complex raises the possibility that the p19(SKP1)/p45(SKP2)/CUL-1 complex may function as the yeast SKP1-CDC53-F-box (SCF) protein complex that acts as a ubiquitin E3 ligase to regulate the G1/S transition.
654	2288	complex	SKP1	CUL-1	The identification of CUL-1 as a member of the complex raises the possibility that the p19(SKP1)/p45(SKP2)/CUL-1 complex may function as the yeast SKP1-CDC53-F-box (SCF) protein complex that acts as a ubiquitin E3 ligase to regulate the G1/S transition.
654	2289	complex	SKP1	F-box	The identification of CUL-1 as a member of the complex raises the possibility that the p19(SKP1)/p45(SKP2)/CUL-1 complex may function as the yeast SKP1-CDC53-F-box (SCF) protein complex that acts as a ubiquitin E3 ligase to regulate the G1/S transition.
654	2290	complex	SKP1	SKP2	The identification of CUL-1 as a member of the complex raises the possibility that the p19(SKP1)/p45(SKP2)/CUL-1 complex may function as the yeast SKP1-CDC53-F-box (SCF) protein complex that acts as a ubiquitin E3 ligase to regulate the G1/S transition.
654	2291	complex	SKP1	p45	The identification of CUL-1 as a member of the complex raises the possibility that the p19(SKP1)/p45(SKP2)/CUL-1 complex may function as the yeast SKP1-CDC53-F-box (SCF) protein complex that acts as a ubiquitin E3 ligase to regulate the G1/S transition.
654	2292	complex	SKP2	CUL-1	The identification of CUL-1 as a member of the complex raises the possibility that the p19(SKP1)/p45(SKP2)/CUL-1 complex may function as the yeast SKP1-CDC53-F-box (SCF) protein complex that acts as a ubiquitin E3 ligase to regulate the G1/S transition.
654	2293	complex	SKP2	SKP1	The identification of CUL-1 as a member of the complex raises the possibility that the p19(SKP1)/p45(SKP2)/CUL-1 complex may function as the yeast SKP1-CDC53-F-box (SCF) protein complex that acts as a ubiquitin E3 ligase to regulate the G1/S transition.
654	2294	complex	SKP2	p19	The identification of CUL-1 as a member of the complex raises the possibility that the p19(SKP1)/p45(SKP2)/CUL-1 complex may function as the yeast SKP1-CDC53-F-box (SCF) protein complex that acts as a ubiquitin E3 ligase to regulate the G1/S transition.
654	2295	complex	p19	CUL-1	The identification of CUL-1 as a member of the complex raises the possibility that the p19(SKP1)/p45(SKP2)/CUL-1 complex may function as the yeast SKP1-CDC53-F-box (SCF) protein complex that acts as a ubiquitin E3 ligase to regulate the G1/S transition.
654	2296	complex	p19	SKP2	The identification of CUL-1 as a member of the complex raises the possibility that the p19(SKP1)/p45(SKP2)/CUL-1 complex may function as the yeast SKP1-CDC53-F-box (SCF) protein complex that acts as a ubiquitin E3 ligase to regulate the G1/S transition.
654	2297	complex	p19	p45	The identification of CUL-1 as a member of the complex raises the possibility that the p19(SKP1)/p45(SKP2)/CUL-1 complex may function as the yeast SKP1-CDC53-F-box (SCF) protein complex that acts as a ubiquitin E3 ligase to regulate the G1/S transition.
654	2298	complex	p45	CUL-1	The identification of CUL-1 as a member of the complex raises the possibility that the p19(SKP1)/p45(SKP2)/CUL-1 complex may function as the yeast SKP1-CDC53-F-box (SCF) protein complex that acts as a ubiquitin E3 ligase to regulate the G1/S transition.
654	2299	complex	p45	SKP1	The identification of CUL-1 as a member of the complex raises the possibility that the p19(SKP1)/p45(SKP2)/CUL-1 complex may function as the yeast SKP1-CDC53-F-box (SCF) protein complex that acts as a ubiquitin E3 ligase to regulate the G1/S transition.
654	2300	complex	p45	p19	The identification of CUL-1 as a member of the complex raises the possibility that the p19(SKP1)/p45(SKP2)/CUL-1 complex may function as the yeast SKP1-CDC53-F-box (SCF) protein complex that acts as a ubiquitin E3 ligase to regulate the G1/S transition.
655	2301	interaction	DAP-1	TNF-R1	The in vivo interaction between DAP-1 and TNF-R1 was further confirmed in mammalian cells.
655	2302	interaction	TNF-R1	DAP-1	The in vivo interaction between DAP-1 and TNF-R1 was further confirmed in mammalian cells.
656	2303	interaction	DCC	Siah	The in vivo interaction between Sina/Siah and DCC was confirmed through studies of transgenic Drosophila lines in which DCC and Sina were ectopically expressed in the eye.
656	2304	interaction	DCC	Sina	The in vivo interaction between Sina/Siah and DCC was confirmed through studies of transgenic Drosophila lines in which DCC and Sina were ectopically expressed in the eye.
656	2305	interaction	Siah	DCC	The in vivo interaction between Sina/Siah and DCC was confirmed through studies of transgenic Drosophila lines in which DCC and Sina were ectopically expressed in the eye.
656	2306	interaction	Sina	DCC	The in vivo interaction between Sina/Siah and DCC was confirmed through studies of transgenic Drosophila lines in which DCC and Sina were ectopically expressed in the eye.
657	2307	complex	CUL1	HOS	The initial ubiquitin transfer and subsequent polymerization steps of this reaction require the coordinated action of Cdc34 and the SCF(HOS/beta-TRCP)-ROC1 E3 ligase complex, comprised of four subunits (Skp1, cullin 1 [CUL1], HOS/beta-TRCP, and ROC1).
657	2308	complex	CUL1	ROC1	The initial ubiquitin transfer and subsequent polymerization steps of this reaction require the coordinated action of Cdc34 and the SCF(HOS/beta-TRCP)-ROC1 E3 ligase complex, comprised of four subunits (Skp1, cullin 1 [CUL1], HOS/beta-TRCP, and ROC1).
657	2309	complex	CUL1	Skp1	The initial ubiquitin transfer and subsequent polymerization steps of this reaction require the coordinated action of Cdc34 and the SCF(HOS/beta-TRCP)-ROC1 E3 ligase complex, comprised of four subunits (Skp1, cullin 1 [CUL1], HOS/beta-TRCP, and ROC1).
657	2310	complex	CUL1	beta-TRCP	The initial ubiquitin transfer and subsequent polymerization steps of this reaction require the coordinated action of Cdc34 and the SCF(HOS/beta-TRCP)-ROC1 E3 ligase complex, comprised of four subunits (Skp1, cullin 1 [CUL1], HOS/beta-TRCP, and ROC1).
657	2311	complex	HOS	CUL1	The initial ubiquitin transfer and subsequent polymerization steps of this reaction require the coordinated action of Cdc34 and the SCF(HOS/beta-TRCP)-ROC1 E3 ligase complex, comprised of four subunits (Skp1, cullin 1 [CUL1], HOS/beta-TRCP, and ROC1).
657	2312	complex	HOS	ROC1	The initial ubiquitin transfer and subsequent polymerization steps of this reaction require the coordinated action of Cdc34 and the SCF(HOS/beta-TRCP)-ROC1 E3 ligase complex, comprised of four subunits (Skp1, cullin 1 [CUL1], HOS/beta-TRCP, and ROC1).
657	2313	complex	HOS	Skp1	The initial ubiquitin transfer and subsequent polymerization steps of this reaction require the coordinated action of Cdc34 and the SCF(HOS/beta-TRCP)-ROC1 E3 ligase complex, comprised of four subunits (Skp1, cullin 1 [CUL1], HOS/beta-TRCP, and ROC1).
657	2314	complex	HOS	cullin 1	The initial ubiquitin transfer and subsequent polymerization steps of this reaction require the coordinated action of Cdc34 and the SCF(HOS/beta-TRCP)-ROC1 E3 ligase complex, comprised of four subunits (Skp1, cullin 1 [CUL1], HOS/beta-TRCP, and ROC1).
657	2315	complex	ROC1	CUL1	The initial ubiquitin transfer and subsequent polymerization steps of this reaction require the coordinated action of Cdc34 and the SCF(HOS/beta-TRCP)-ROC1 E3 ligase complex, comprised of four subunits (Skp1, cullin 1 [CUL1], HOS/beta-TRCP, and ROC1).
657	2316	complex	ROC1	HOS	The initial ubiquitin transfer and subsequent polymerization steps of this reaction require the coordinated action of Cdc34 and the SCF(HOS/beta-TRCP)-ROC1 E3 ligase complex, comprised of four subunits (Skp1, cullin 1 [CUL1], HOS/beta-TRCP, and ROC1).
657	2317	complex	ROC1	Skp1	The initial ubiquitin transfer and subsequent polymerization steps of this reaction require the coordinated action of Cdc34 and the SCF(HOS/beta-TRCP)-ROC1 E3 ligase complex, comprised of four subunits (Skp1, cullin 1 [CUL1], HOS/beta-TRCP, and ROC1).
657	2318	complex	ROC1	beta-TRCP	The initial ubiquitin transfer and subsequent polymerization steps of this reaction require the coordinated action of Cdc34 and the SCF(HOS/beta-TRCP)-ROC1 E3 ligase complex, comprised of four subunits (Skp1, cullin 1 [CUL1], HOS/beta-TRCP, and ROC1).
657	2319	complex	ROC1	cullin 1	The initial ubiquitin transfer and subsequent polymerization steps of this reaction require the coordinated action of Cdc34 and the SCF(HOS/beta-TRCP)-ROC1 E3 ligase complex, comprised of four subunits (Skp1, cullin 1 [CUL1], HOS/beta-TRCP, and ROC1).
657	2320	complex	Skp1	CUL1	The initial ubiquitin transfer and subsequent polymerization steps of this reaction require the coordinated action of Cdc34 and the SCF(HOS/beta-TRCP)-ROC1 E3 ligase complex, comprised of four subunits (Skp1, cullin 1 [CUL1], HOS/beta-TRCP, and ROC1).
657	2321	complex	Skp1	HOS	The initial ubiquitin transfer and subsequent polymerization steps of this reaction require the coordinated action of Cdc34 and the SCF(HOS/beta-TRCP)-ROC1 E3 ligase complex, comprised of four subunits (Skp1, cullin 1 [CUL1], HOS/beta-TRCP, and ROC1).
657	2322	complex	Skp1	ROC1	The initial ubiquitin transfer and subsequent polymerization steps of this reaction require the coordinated action of Cdc34 and the SCF(HOS/beta-TRCP)-ROC1 E3 ligase complex, comprised of four subunits (Skp1, cullin 1 [CUL1], HOS/beta-TRCP, and ROC1).
657	2323	complex	Skp1	beta-TrCP	The initial ubiquitin transfer and subsequent polymerization steps of this reaction require the coordinated action of Cdc34 and the SCF(HOS/beta-TRCP)-ROC1 E3 ligase complex, comprised of four subunits (Skp1, cullin 1 [CUL1], HOS/beta-TRCP, and ROC1).
657	2324	complex	Skp1	cullin 1	The initial ubiquitin transfer and subsequent polymerization steps of this reaction require the coordinated action of Cdc34 and the SCF(HOS/beta-TRCP)-ROC1 E3 ligase complex, comprised of four subunits (Skp1, cullin 1 [CUL1], HOS/beta-TRCP, and ROC1).
657	2325	complex	beta-TRCP	CUL1	The initial ubiquitin transfer and subsequent polymerization steps of this reaction require the coordinated action of Cdc34 and the SCF(HOS/beta-TRCP)-ROC1 E3 ligase complex, comprised of four subunits (Skp1, cullin 1 [CUL1], HOS/beta-TRCP, and ROC1).
657	2326	complex	beta-TRCP	ROC1	The initial ubiquitin transfer and subsequent polymerization steps of this reaction require the coordinated action of Cdc34 and the SCF(HOS/beta-TRCP)-ROC1 E3 ligase complex, comprised of four subunits (Skp1, cullin 1 [CUL1], HOS/beta-TRCP, and ROC1).
657	2327	complex	beta-TRCP	cullin 1	The initial ubiquitin transfer and subsequent polymerization steps of this reaction require the coordinated action of Cdc34 and the SCF(HOS/beta-TRCP)-ROC1 E3 ligase complex, comprised of four subunits (Skp1, cullin 1 [CUL1], HOS/beta-TRCP, and ROC1).
657	2328	complex	beta-TrCP	Skp1	The initial ubiquitin transfer and subsequent polymerization steps of this reaction require the coordinated action of Cdc34 and the SCF(HOS/beta-TRCP)-ROC1 E3 ligase complex, comprised of four subunits (Skp1, cullin 1 [CUL1], HOS/beta-TRCP, and ROC1).
657	2329	complex	cullin 1	HOS	The initial ubiquitin transfer and subsequent polymerization steps of this reaction require the coordinated action of Cdc34 and the SCF(HOS/beta-TRCP)-ROC1 E3 ligase complex, comprised of four subunits (Skp1, cullin 1 [CUL1], HOS/beta-TRCP, and ROC1).
657	2330	complex	cullin 1	ROC1	The initial ubiquitin transfer and subsequent polymerization steps of this reaction require the coordinated action of Cdc34 and the SCF(HOS/beta-TRCP)-ROC1 E3 ligase complex, comprised of four subunits (Skp1, cullin 1 [CUL1], HOS/beta-TRCP, and ROC1).
657	2331	complex	cullin 1	Skp1	The initial ubiquitin transfer and subsequent polymerization steps of this reaction require the coordinated action of Cdc34 and the SCF(HOS/beta-TRCP)-ROC1 E3 ligase complex, comprised of four subunits (Skp1, cullin 1 [CUL1], HOS/beta-TRCP, and ROC1).
657	2332	complex	cullin 1	beta-TRCP	The initial ubiquitin transfer and subsequent polymerization steps of this reaction require the coordinated action of Cdc34 and the SCF(HOS/beta-TRCP)-ROC1 E3 ligase complex, comprised of four subunits (Skp1, cullin 1 [CUL1], HOS/beta-TRCP, and ROC1).
658	2333	ubiquitinate	APC	cyclin B	The initiation of anaphase and exit from mitosis require the activation of a proteolytic system that ubiquitinates and degrades cyclin B. The regulated component of this system is a large ubiquitin ligase complex, termed the anaphase-promoting complex (APC) or cyclosome.
658	2334	ubiquitinate	cyclin B	APC	The initiation of anaphase and exit from mitosis require the activation of a proteolytic system that ubiquitinates and degrades cyclin B. The regulated component of this system is a large ubiquitin ligase complex, termed the anaphase-promoting complex (APC) or cyclosome.
659	2335	interaction	Grb10	Nedd4	The interaction between Grb10 and Nedd4 was also reproduced in vivo in mouse embryo fibroblasts, where endogenous Nedd4 co-immunoprecipitated constitutively with both the endogenous and an overexpressed Grb10.
659	2336	interaction	Nedd4	Grb10	The interaction between Grb10 and Nedd4 was also reproduced in vivo in mouse embryo fibroblasts, where endogenous Nedd4 co-immunoprecipitated constitutively with both the endogenous and an overexpressed Grb10.
660	2337	interaction	MDM2	hsp90	The interaction between MDM2 and hsp90 is disrupted by the 2A10 antibody, which recognizes a site on MDM2 important for binding to alternative reading frame (ARF).
660	2338	interaction	hsp90	MDM2	The interaction between MDM2 and hsp90 is disrupted by the 2A10 antibody, which recognizes a site on MDM2 important for binding to alternative reading frame (ARF).
661	2339	interaction	FMRP	UBC9	The interaction between UBC9 and FMRP is supported both by similarity search of the amino acid sequences of the mouse and human UBC9 and by expression characteristics of the two proteins.
661	2340	interaction	UBC9	FMRP	The interaction between UBC9 and FMRP is supported both by similarity search of the amino acid sequences of the mouse and human UBC9 and by expression characteristics of the two proteins.
662	2341	interaction	Ubc9	sentrin	The interaction between sentrin and Ubc9 required the ubiquitin domain and the C-terminal Gly-Gly residues of sentrin.
662	2342	interaction	sentrin	Ubc9	The interaction between sentrin and Ubc9 required the ubiquitin domain and the C-terminal Gly-Gly residues of sentrin.
663	2343	interaction	SUMO-1	yUbc9	The interaction between yUbc9 and SUMO-1 was abolished by deleting the C-terminal Gly residue of SUMO-1, which is reportedly required for the formation of Ubc9-SUMO-1 thioester linkage.
663	2344	interaction	yUbc9	SUMO-1	The interaction between yUbc9 and SUMO-1 was abolished by deleting the C-terminal Gly residue of SUMO-1, which is reportedly required for the formation of Ubc9-SUMO-1 thioester linkage.
664	2345	interaction	SALL1	UBE2I	The interaction of SALL1 and UBE2I was confirmed in a glutathione S-transferase (GST) pull-down experiment.
664	2346	interaction	UBE2I	SALL1	The interaction of SALL1 and UBE2I was confirmed in a glutathione S-transferase (GST) pull-down experiment.
665	2347	conjugated	H2A	ubiquitin	The low level of deposition that is observed has characteristics similar to the deposition of uH2A and uH2B, and it is proposed that conjugation of H2A and H2B by ubiquitin occurs when these proteins are in a free pool within the nucleus.
665	2348	conjugation	H2B	ubiquitin	The low level of deposition that is observed has characteristics similar to the deposition of uH2A and uH2B, and it is proposed that conjugation of H2A and H2B by ubiquitin occurs when these proteins are in a free pool within the nucleus.
665	2349	conjugated	ubiquitin	H2A	The low level of deposition that is observed has characteristics similar to the deposition of uH2A and uH2B, and it is proposed that conjugation of H2A and H2B by ubiquitin occurs when these proteins are in a free pool within the nucleus.
665	2350	conjugation	ubiquitin	H2B	The low level of deposition that is observed has characteristics similar to the deposition of uH2A and uH2B, and it is proposed that conjugation of H2A and H2B by ubiquitin occurs when these proteins are in a free pool within the nucleus.
666	2351	bind	GLUT1	mUbc9	The mUbc9 enzyme was found to bind directly to GLUT4 and GLUT1 through an 11-aa sequence common to the two transporters and to modify both transporters covalently by conjugation with the mUbc9 substrate, sentrin.
666	2352	bind	GLUT4	mUbc9	The mUbc9 enzyme was found to bind directly to GLUT4 and GLUT1 through an 11-aa sequence common to the two transporters and to modify both transporters covalently by conjugation with the mUbc9 substrate, sentrin.
666	2353	bind	mUbc9	GLUT1	The mUbc9 enzyme was found to bind directly to GLUT4 and GLUT1 through an 11-aa sequence common to the two transporters and to modify both transporters covalently by conjugation with the mUbc9 substrate, sentrin.
666	2354	bind	mUbc9	GLUT4	The mUbc9 enzyme was found to bind directly to GLUT4 and GLUT1 through an 11-aa sequence common to the two transporters and to modify both transporters covalently by conjugation with the mUbc9 substrate, sentrin.
667	2355	interaction	52Ro	UnpEL	The mammalian 2-hybrid assay confirmed the interaction between full-length 52Ro and UnpEL.
667	2356	interaction	UnpEL	52Ro	The mammalian 2-hybrid assay confirmed the interaction between full-length 52Ro and UnpEL.
668	2357	bind	TAP	p15	The middle domain of TAP binds directly to p15, a protein related to the nuclear transport factor 2 (NTF2), whereas its C-terminal domain interacts with various nucleoporins, the components of the nuclear pore complex (NPC).
668	2358	bind	p15	TAP	The middle domain of TAP binds directly to p15, a protein related to the nuclear transport factor 2 (NTF2), whereas its C-terminal domain interacts with various nucleoporins, the components of the nuclear pore complex (NPC).
669	2359	interaction	Skp2	p27	The molecular mechanisms by which Cks1 promotes the interaction of the Skp2 ubiquitin ligase subunit to p27 remained obscure.
669	2360	interaction	p27	Skp2	The molecular mechanisms by which Cks1 promotes the interaction of the Skp2 ubiquitin ligase subunit to p27 remained obscure.
670	2361	bind	GH receptor	GH	The multiple actions of GH start when GH binds to the cell surface-expressed GH receptor.
670	2362	bind	GH	GH receptor	The multiple actions of GH start when GH binds to the cell surface-expressed GH receptor.
671	2363	interaction	AIP4	LMP2A	The mutation of both PY motifs completely abolished binding activity of these proteins to LMP2A and the interaction of AIP4 and WWP2 with LMP2A was confirmed in cell lines expressing LMP2A, WWP2, and AIP4.
671	2364	interaction	LMP2A	AIP4	The mutation of both PY motifs completely abolished binding activity of these proteins to LMP2A and the interaction of AIP4 and WWP2 with LMP2A was confirmed in cell lines expressing LMP2A, WWP2, and AIP4.
671	2365	interaction	LMP2A	WWP2	The mutation of both PY motifs completely abolished binding activity of these proteins to LMP2A and the interaction of AIP4 and WWP2 with LMP2A was confirmed in cell lines expressing LMP2A, WWP2, and AIP4.
671	2366	interaction	WWP2	LMP2A	The mutation of both PY motifs completely abolished binding activity of these proteins to LMP2A and the interaction of AIP4 and WWP2 with LMP2A was confirmed in cell lines expressing LMP2A, WWP2, and AIP4.
672	2367	inhibitory	NF-kappaB	p100	The nf-kb2 gene encodes the cytoplasmic NF-kappaB inhibitory protein p100 from which the active p52 NF-kappaB subunit is derived by proteasome-mediated proteolysis.
672	2368	inhibitory	p100	NF-kappaB	The nf-kb2 gene encodes the cytoplasmic NF-kappaB inhibitory protein p100 from which the active p52 NF-kappaB subunit is derived by proteasome-mediated proteolysis.
673	2369	interaction	RNA14p	RNA15p	The observation that both proteins are found in the nucleus is in agreement with previous genetic data which suggest an interaction between RNA14p and RNA15p.
673	2370	interaction	RNA15p	RNA14p	The observation that both proteins are found in the nucleus is in agreement with previous genetic data which suggest an interaction between RNA14p and RNA15p.
674	2371	ubiquitinate	hdm2	p53	The oncoprotein hdm2 ubiquitinates p53, resulting in the rapid degradation of p53 through the ubiquitin (Ub)-proteasome pathway.
674	2372	ubiquitinate	p53	hdm2	The oncoprotein hdm2 ubiquitinates p53, resulting in the rapid degradation of p53 through the ubiquitin (Ub)-proteasome pathway.
675	2373	bind	GH receptors	SOCS-2	The overexpressed SOCS-2 was found to bind to endogenous GH receptors in a number of mouse organs, while phosphopeptide binding studies with recombinant SOCS-2 defined phosphorylated tyrosine 595 on the GH receptor as the site of interaction.
675	2374	bind	SOCS-2	GH receptors	The overexpressed SOCS-2 was found to bind to endogenous GH receptors in a number of mouse organs, while phosphopeptide binding studies with recombinant SOCS-2 defined phosphorylated tyrosine 595 on the GH receptor as the site of interaction.
676	2375	bind	hsp90	p50cdc37	The p50cdc37 binds to hsp90 at a site that is close to but different from the TPR binding site of the immunophilins, and like the immunophilins, p50cdc37 is thought to be involved in targeting and trafficking of the protein kinases.
676	2376	bind	p50cdc37	hsp90	The p50cdc37 binds to hsp90 at a site that is close to but different from the TPR binding site of the immunophilins, and like the immunophilins, p50cdc37 is thought to be involved in targeting and trafficking of the protein kinases.
677	2377	interaction	ICP0	cdc34	The physical interaction of cdc34 and ICP0 leads to its degradation.
677	2378	interaction	cdc34	ICP0	The physical interaction of cdc34 and ICP0 leads to its degradation.
678	2379	interaction	Cdc11	Cdc5	The polo-box-dependent interactions between Cdc5 and septins (Cdc11 and Cdc12) and genetic interactions between the dominant-negative cdc5DeltaN and Cyk2/Hof1 or Myo1 suggest that direct interactions between cdc5DeltaN and septins resulted in inhibition of Cyk2/Hof1- and Myo1-mediated cytokinetic pathways.
678	2380	interaction	Cdc12	Cdc5	The polo-box-dependent interactions between Cdc5 and septins (Cdc11 and Cdc12) and genetic interactions between the dominant-negative cdc5DeltaN and Cyk2/Hof1 or Myo1 suggest that direct interactions between cdc5DeltaN and septins resulted in inhibition of Cyk2/Hof1- and Myo1-mediated cytokinetic pathways.
678	2381	interaction	Cdc5	Cdc11	The polo-box-dependent interactions between Cdc5 and septins (Cdc11 and Cdc12) and genetic interactions between the dominant-negative cdc5DeltaN and Cyk2/Hof1 or Myo1 suggest that direct interactions between cdc5DeltaN and septins resulted in inhibition of Cyk2/Hof1- and Myo1-mediated cytokinetic pathways.
678	2382	interaction	Cdc5	Cdc12	The polo-box-dependent interactions between Cdc5 and septins (Cdc11 and Cdc12) and genetic interactions between the dominant-negative cdc5DeltaN and Cyk2/Hof1 or Myo1 suggest that direct interactions between cdc5DeltaN and septins resulted in inhibition of Cyk2/Hof1- and Myo1-mediated cytokinetic pathways.
679	2383	modification	PML	SUMO-1	The precise molecular role for the SUMO-1 modification of PML is unclear, and the specific lysine residues within PML that are targeted for modification and the PML sub-domains necessary for mediating the modification in vivo are unknown.
679	2384	modification	SUMO-1	PML	The precise molecular role for the SUMO-1 modification of PML is unclear, and the specific lysine residues within PML that are targeted for modification and the PML sub-domains necessary for mediating the modification in vivo are unknown.
680	2385	binding	YUH1	ubiquitin	The presence of several hydrophobic clusters in the ubiquitin binding interface of YUH1 suggests that hydrophobic interactions are equally important as ionic interactions in contacting ubiquitin.
680	2386	binding	ubiquitin	YUH1	The presence of several hydrophobic clusters in the ubiquitin binding interface of YUH1 suggests that hydrophobic interactions are equally important as ionic interactions in contacting ubiquitin.
681	2387	destruction	APC	cyclin B	The progression of cytokinesis requires cyclin B destruction by the anaphase promoting complex (APC/C) and, in fission yeast, activation of the septation initiation network (SIN) is also essential.
681	2388	destruction	cyclin B	APC	The progression of cytokinesis requires cyclin B destruction by the anaphase promoting complex (APC/C) and, in fission yeast, activation of the septation initiation network (SIN) is also essential.
682	2389	interaction	SCON2	SCON3	The protein-protein interaction detected between SCON2 and SCON3 represents the initial demonstration in a filamentous fungus of functional interaction between putative core components of a SCF complex.
682	2390	interaction	SCON3	SCON2	The protein-protein interaction detected between SCON2 and SCON3 represents the initial demonstration in a filamentous fungus of functional interaction between putative core components of a SCF complex.
683	2391	modified	PIC1	PML	The recent finding that PIC1/SUMO-1, a small ubiquitin-like protein, is covalently linked to the RanGAP1 protein of the nuclear pore complex and also binds PML in yeast cells led us to determine whether PML is covalently modified by PIC1/SUMO-1 and whether the same is true for Sp100.
683	2392	linked	PIC1	RanGAP1	The recent finding that PIC1/SUMO-1, a small ubiquitin-like protein, is covalently linked to the RanGAP1 protein of the nuclear pore complex and also binds PML in yeast cells led us to determine whether PML is covalently modified by PIC1/SUMO-1 and whether the same is true for Sp100.
683	2393	modified	PML	PIC1	The recent finding that PIC1/SUMO-1, a small ubiquitin-like protein, is covalently linked to the RanGAP1 protein of the nuclear pore complex and also binds PML in yeast cells led us to determine whether PML is covalently modified by PIC1/SUMO-1 and whether the same is true for Sp100.
683	2394	modified	PML	SUMO-1	The recent finding that PIC1/SUMO-1, a small ubiquitin-like protein, is covalently linked to the RanGAP1 protein of the nuclear pore complex and also binds PML in yeast cells led us to determine whether PML is covalently modified by PIC1/SUMO-1 and whether the same is true for Sp100.
683	2395	linked	RanGAP1	PIC1	The recent finding that PIC1/SUMO-1, a small ubiquitin-like protein, is covalently linked to the RanGAP1 protein of the nuclear pore complex and also binds PML in yeast cells led us to determine whether PML is covalently modified by PIC1/SUMO-1 and whether the same is true for Sp100.
683	2396	linked	RanGAP1	SUMO-1	The recent finding that PIC1/SUMO-1, a small ubiquitin-like protein, is covalently linked to the RanGAP1 protein of the nuclear pore complex and also binds PML in yeast cells led us to determine whether PML is covalently modified by PIC1/SUMO-1 and whether the same is true for Sp100.
683	2397	modified	SUMO-1	PML	The recent finding that PIC1/SUMO-1, a small ubiquitin-like protein, is covalently linked to the RanGAP1 protein of the nuclear pore complex and also binds PML in yeast cells led us to determine whether PML is covalently modified by PIC1/SUMO-1 and whether the same is true for Sp100.
683	2398	linked	SUMO-1	RanGAP1	The recent finding that PIC1/SUMO-1, a small ubiquitin-like protein, is covalently linked to the RanGAP1 protein of the nuclear pore complex and also binds PML in yeast cells led us to determine whether PML is covalently modified by PIC1/SUMO-1 and whether the same is true for Sp100.
684	2399	complex	Sua1p	hUba2p	The recombinant proteins, Sua1p and hUba2p, formed a complex.
684	2400	complex	hUba2p	Sua1p	The recombinant proteins, Sua1p and hUba2p, formed a complex.
685	2401	interaction	HIF-1 alpha	VHL	The region of VHL mediating interaction with HIF-1 alpha overlapped with a putative macromolecular binding site observed within the crystal structure of VHL.
685	2402	interaction	VHL	HIF-1 alpha	The region of VHL mediating interaction with HIF-1 alpha overlapped with a putative macromolecular binding site observed within the crystal structure of VHL.
686	2403	complex	Cdc28p	Cdc6p	The replication initiation protein Cdc6p forms a tight complex with Cdc28p, specifically with forms of the kinase that are competent to promote replication initiation.
686	2404	complex	Cdc6p	Cdc28p	The replication initiation protein Cdc6p forms a tight complex with Cdc28p, specifically with forms of the kinase that are competent to promote replication initiation.
687	2405	interaction	CaM	Siah-1A	The results demonstrate a direct interaction between group 1 mGluRs and Siah-1A and suggest a novel modulatory mechanism mediated by a competitive interaction between Ca2+/CaM and Siah-1A.
687	2406	interaction	Siah-1A	CaM	The results demonstrate a direct interaction between group 1 mGluRs and Siah-1A and suggest a novel modulatory mechanism mediated by a competitive interaction between Ca2+/CaM and Siah-1A.
687	2407	interaction	Siah-1A	mGluR	The results demonstrate a direct interaction between group 1 mGluRs and Siah-1A and suggest a novel modulatory mechanism mediated by a competitive interaction between Ca2+/CaM and Siah-1A.
687	2408	interaction	mGluR	Siah-1A	The results demonstrate a direct interaction between group 1 mGluRs and Siah-1A and suggest a novel modulatory mechanism mediated by a competitive interaction between Ca2+/CaM and Siah-1A.
688	2409	monoubiquitinate	E214K	histone	The results show the following. 1) No E2 exhibits strong specificity for H2A over the other histones. 2) For a given histone, kinetics of formation of its monoubiquitinated adduct do not differ strongly among the E2s; sigmoid kinetics (nH = 2) are generally observed, with values of K 0.5 ranging from 2-6 microM. 3) E214K catalyzes primarily monoubiquitination. 4) E220K catalyzes multiple ubiquitination (up to three ubiquitin/histone) by a processive mechanism that involves joining of ubiquitin carboxyl termini to multiple histone lysine residues. 5) E235K also catalyzes processive ubiquitination, with formation of polyubiquitinated products exhibiting a lag phase.
688	2410	polyubiquitinate	E220K	histone	The results show the following. 1) No E2 exhibits strong specificity for H2A over the other histones. 2) For a given histone, kinetics of formation of its monoubiquitinated adduct do not differ strongly among the E2s; sigmoid kinetics (nH = 2) are generally observed, with values of K 0.5 ranging from 2-6 microM. 3) E214K catalyzes primarily monoubiquitination. 4) E220K catalyzes multiple ubiquitination (up to three ubiquitin/histone) by a processive mechanism that involves joining of ubiquitin carboxyl termini to multiple histone lysine residues. 5) E235K also catalyzes processive ubiquitination, with formation of polyubiquitinated products exhibiting a lag phase.
688	2411	ubiquitinate	E235K	histone	The results show the following. 1) No E2 exhibits strong specificity for H2A over the other histones. 2) For a given histone, kinetics of formation of its monoubiquitinated adduct do not differ strongly among the E2s; sigmoid kinetics (nH = 2) are generally observed, with values of K 0.5 ranging from 2-6 microM. 3) E214K catalyzes primarily monoubiquitination. 4) E220K catalyzes multiple ubiquitination (up to three ubiquitin/histone) by a processive mechanism that involves joining of ubiquitin carboxyl termini to multiple histone lysine residues. 5) E235K also catalyzes processive ubiquitination, with formation of polyubiquitinated products exhibiting a lag phase.
688	2412	monoubiquitinate	histone	E214K	The results show the following. 1) No E2 exhibits strong specificity for H2A over the other histones. 2) For a given histone, kinetics of formation of its monoubiquitinated adduct do not differ strongly among the E2s; sigmoid kinetics (nH = 2) are generally observed, with values of K 0.5 ranging from 2-6 microM. 3) E214K catalyzes primarily monoubiquitination. 4) E220K catalyzes multiple ubiquitination (up to three ubiquitin/histone) by a processive mechanism that involves joining of ubiquitin carboxyl termini to multiple histone lysine residues. 5) E235K also catalyzes processive ubiquitination, with formation of polyubiquitinated products exhibiting a lag phase.
688	2413	polyubiquitinate	histone	E220K	The results show the following. 1) No E2 exhibits strong specificity for H2A over the other histones. 2) For a given histone, kinetics of formation of its monoubiquitinated adduct do not differ strongly among the E2s; sigmoid kinetics (nH = 2) are generally observed, with values of K 0.5 ranging from 2-6 microM. 3) E214K catalyzes primarily monoubiquitination. 4) E220K catalyzes multiple ubiquitination (up to three ubiquitin/histone) by a processive mechanism that involves joining of ubiquitin carboxyl termini to multiple histone lysine residues. 5) E235K also catalyzes processive ubiquitination, with formation of polyubiquitinated products exhibiting a lag phase.
688	2414	ubiquitinate	histone	E235K	The results show the following. 1) No E2 exhibits strong specificity for H2A over the other histones. 2) For a given histone, kinetics of formation of its monoubiquitinated adduct do not differ strongly among the E2s; sigmoid kinetics (nH = 2) are generally observed, with values of K 0.5 ranging from 2-6 microM. 3) E214K catalyzes primarily monoubiquitination. 4) E220K catalyzes multiple ubiquitination (up to three ubiquitin/histone) by a processive mechanism that involves joining of ubiquitin carboxyl termini to multiple histone lysine residues. 5) E235K also catalyzes processive ubiquitination, with formation of polyubiquitinated products exhibiting a lag phase.
689	2415	activate	APC	MPF	The same antibodies suppressed M phase-promoting factor (MPF)-dependent activation of the APC/cyclosome in interphase egg extracts, although they did not appear to alter the pattern or extent of MPF-dependent phosphorylation of APC/cyclosome subunits.
689	2416	activate	MPF	APC	The same antibodies suppressed M phase-promoting factor (MPF)-dependent activation of the APC/cyclosome in interphase egg extracts, although they did not appear to alter the pattern or extent of MPF-dependent phosphorylation of APC/cyclosome subunits.
690	2417	interact	HsUbc9	Rad51	The sequence of UBC-FAP is identical to that of HsUbc9, a UBC recently shown to interact with Rad51.
690	2418	interact	Rad51	HsUbc9	The sequence of UBC-FAP is identical to that of HsUbc9, a UBC recently shown to interact with Rad51.
691	2419	interaction	Mns1p	Rer1p	The split-ubiquitin system was used to determine if there is an interaction between Mns1p and Rer1p in vivo.
691	2420	interaction	Rer1p	Mns1p	The split-ubiquitin system was used to determine if there is an interaction between Mns1p and Rer1p in vivo.
692	2421	interaction	Avp	Ubal	The structural model of the Ubal-Avp interaction revealed some similarity between S1-S4 substrate binding sites of Avp and ubiquitin hydrolases.
692	2422	interaction	Ubal	Avp	The structural model of the Ubal-Avp interaction revealed some similarity between S1-S4 substrate binding sites of Avp and ubiquitin hydrolases.
693	2423	binding	SIP	Siah1	The structural prediction was confirmed by site-directed mutagenesis of these electronegative residues, resulting in loss of binding of Siah1 to SIP in vitro and in cells.
693	2424	binding	Siah1	SIP	The structural prediction was confirmed by site-directed mutagenesis of these electronegative residues, resulting in loss of binding of Siah1 to SIP in vitro and in cells.
694	2425	interaction	IkappaBalpha	Skp1	The structural requirements for the interactions of FWD1 with IkappaBalpha and with Skp1 have now been investigated further.
694	2426	interaction	Skp1	IkappaBalpha	The structural requirements for the interactions of FWD1 with IkappaBalpha and with Skp1 have now been investigated further.
695	2427	bind	ENaC	Nedd4	The tryptophan-bounded WW domains ofNedd4 bind to the proline-tyrosine (PY) motifs contained in the C-terminal cytoplasmic region of the beta and gamma subunits of the rat amiloride-sensitive sodium channel (ENaC).
695	2428	bind	Nedd4	ENaC	The tryptophan-bounded WW domains ofNedd4 bind to the proline-tyrosine (PY) motifs contained in the C-terminal cytoplasmic region of the beta and gamma subunits of the rat amiloride-sensitive sodium channel (ENaC).
696	2429	polyubiquitinate	MDM2	p53	The tumor suppressor p53 is degraded by the ubiquitin-proteasome system. p53 was polyubiquitinated in the presence of E1, UbcH5 as E2 and MDM2 oncoprotein.
696	2430	polyubiquitinate	p53	MDM2	The tumor suppressor p53 is degraded by the ubiquitin-proteasome system. p53 was polyubiquitinated in the presence of E1, UbcH5 as E2 and MDM2 oncoprotein.
697	2431	modified	PML	SUMO-1	The two NB proteins PML and SP100 are covalently modified by the ubiquitin-related SUMO-1 modifier, and recent work indicates that this modification is critical for the regulation of NB dynamics.
697	2432	modified	SP100	SUMO-1	The two NB proteins PML and SP100 are covalently modified by the ubiquitin-related SUMO-1 modifier, and recent work indicates that this modification is critical for the regulation of NB dynamics.
697	2433	modified	SUMO-1	PML	The two NB proteins PML and SP100 are covalently modified by the ubiquitin-related SUMO-1 modifier, and recent work indicates that this modification is critical for the regulation of NB dynamics.
697	2434	modified	SUMO-1	SP100	The two NB proteins PML and SP100 are covalently modified by the ubiquitin-related SUMO-1 modifier, and recent work indicates that this modification is critical for the regulation of NB dynamics.
698	2435	interaction	C-Daxx	C-GLUT4	The two-hybrid interaction between C-GLUT4 and C-Daxx is validated by the ability of in vitro translated C-GLUT4 to interact with in vitro translated full-length Daxx and C-Daxx.
698	2436	interaction	C-GLUT4	C-Daxx	The two-hybrid interaction between C-GLUT4 and C-Daxx is validated by the ability of in vitro translated C-GLUT4 to interact with in vitro translated full-length Daxx and C-Daxx.
698	2437	interact	C-GLUT4	Daxx	The two-hybrid interaction between C-GLUT4 and C-Daxx is validated by the ability of in vitro translated C-GLUT4 to interact with in vitro translated full-length Daxx and C-Daxx.
698	2438	interact	Daxx	C-GLUT4	The two-hybrid interaction between C-GLUT4 and C-Daxx is validated by the ability of in vitro translated C-GLUT4 to interact with in vitro translated full-length Daxx and C-Daxx.
699	2439	conjugate	PIC1	ubc-9	The ubiquitin conjugating (ubc) E2 enzyme ubc-9 conjugates the ubiquitin-like peptide sentrin/SUMO-1/PIC1 to target proteins which include the Fas antigen.
699	2440	conjugate	SUMO-1	ubc-9	The ubiquitin conjugating (ubc) E2 enzyme ubc-9 conjugates the ubiquitin-like peptide sentrin/SUMO-1/PIC1 to target proteins which include the Fas antigen.
699	2441	conjugate	sentrin	ubc-9	The ubiquitin conjugating (ubc) E2 enzyme ubc-9 conjugates the ubiquitin-like peptide sentrin/SUMO-1/PIC1 to target proteins which include the Fas antigen.
699	2442	conjugate	ubc-9	PIC1	The ubiquitin conjugating (ubc) E2 enzyme ubc-9 conjugates the ubiquitin-like peptide sentrin/SUMO-1/PIC1 to target proteins which include the Fas antigen.
699	2443	conjugate	ubc-9	SUMO-1	The ubiquitin conjugating (ubc) E2 enzyme ubc-9 conjugates the ubiquitin-like peptide sentrin/SUMO-1/PIC1 to target proteins which include the Fas antigen.
699	2444	conjugate	ubc-9	sentrin	The ubiquitin conjugating (ubc) E2 enzyme ubc-9 conjugates the ubiquitin-like peptide sentrin/SUMO-1/PIC1 to target proteins which include the Fas antigen.
700	2445	associate	IkappaBalpha	VCP	The ubiquitinated IkappaBalpha conjugates readily associate with VCP both in vivo and in vitro, and this complex appears dissociated from NF-kappaB.
700	2446	associate	VCP	IkappaBalpha	The ubiquitinated IkappaBalpha conjugates readily associate with VCP both in vivo and in vitro, and this complex appears dissociated from NF-kappaB.
701	2447	complex	Grb2	c-Cbl	The underlying mechanism seems to involve recruitment of a Grb2 c-Cbl complex to Grb2-specific docking sites of EGFR, and concurrent acceleration of receptor ubiquitylation and desensitization.
701	2448	complex	c-Cbl	Grb2	The underlying mechanism seems to involve recruitment of a Grb2 c-Cbl complex to Grb2-specific docking sites of EGFR, and concurrent acceleration of receptor ubiquitylation and desensitization.
702	2449	interact	Nup153	SENP2	The unique amino-terminal domain of SENP2 interacts with the FG repeat domain of Nup153, indicating that SENP2 associates with the nucleoplasmic basket of the NPC.
702	2450	interact	SENP2	Nup153	The unique amino-terminal domain of SENP2 interacts with the FG repeat domain of Nup153, indicating that SENP2 associates with the nucleoplasmic basket of the NPC.
703	2451	association	IP3 receptor	ubiquitin	Then samples of cells or pancreata were probed for IP3 receptor content and distribution as well as for ubiquitin association with IP3 receptors.
703	2452	association	ubiquitin	IP3 receptor	Then samples of cells or pancreata were probed for IP3 receptor content and distribution as well as for ubiquitin association with IP3 receptors.
704	2453	modification	SUMO-1	TEL	Therefore, SUMO-1 modification of TEL could be a critical signal necessary for normal functioning of the protein.
704	2454	modification	TEL	SUMO-1	Therefore, SUMO-1 modification of TEL could be a critical signal necessary for normal functioning of the protein.
705	2455	activated	NF-kappaB	TNF-alpha	These data demonstrate that TNF-alpha directly induces skeletal muscle protein loss, that NF-kappaB is rapidly activated by TNF-alpha in differentiated skeletal muscle cells, and that TNF-alpha/NF-kappaB signaling in skeletal muscle is regulated by endogenous reactive oxygen species.
705	2456	activated	TNF-alpha	NF-kappaB	These data demonstrate that TNF-alpha directly induces skeletal muscle protein loss, that NF-kappaB is rapidly activated by TNF-alpha in differentiated skeletal muscle cells, and that TNF-alpha/NF-kappaB signaling in skeletal muscle is regulated by endogenous reactive oxygen species.
706	2457	interaction	Hsp70	Hsp90	These data indicate a model for protein quality control in which the interaction of Hsp70 and Hsp90 with co-chaperones that have either folding or degradatory activity helps to determine the fate of non-native cellular proteins.
706	2458	interaction	Hsp90	Hsp70	These data indicate a model for protein quality control in which the interaction of Hsp70 and Hsp90 with co-chaperones that have either folding or degradatory activity helps to determine the fate of non-native cellular proteins.
707	2459	modification	SUMO-1	p53	These data indicate that SUMO-1 modification of p53 at lysine 386 may not be essential for p53's cellular localization, transcriptional activation, or growth regulation.
707	2460	modification	p53	SUMO-1	These data indicate that SUMO-1 modification of p53 at lysine 386 may not be essential for p53's cellular localization, transcriptional activation, or growth regulation.
708	2461	activated	HDM2	p63	These data indicate that p63 can be activated by HDM2 under conditions in which p53 is inhibited.
708	2462	activated	p63	HDM2	These data indicate that p63 can be activated by HDM2 under conditions in which p53 is inhibited.
709	2463	interact	Kri1p	Krr1p	These data lead us to conclude that Krr1p physically and functionally interacts with Kri1p to form a complex which is required for 40S ribosome biogenesis in the nucleolus.
709	2464	interact	Krr1p	Kri1p	These data lead us to conclude that Krr1p physically and functionally interacts with Kri1p to form a complex which is required for 40S ribosome biogenesis in the nucleolus.
710	2465	interaction	ENaC	WW2	These data provides the first determination of association, dissociation and equilibrium constants for the interactions between WW2 and beta or gammaENaC.
710	2466	interaction	WW2	ENaC	These data provides the first determination of association, dissociation and equilibrium constants for the interactions between WW2 and beta or gammaENaC.
711	2467	bind	GMEB-1	MURF-1	These data suggest that the interaction of titin with MURF-1 is important for the stability of the sarcomeric M-line region.MURF-1 also binds to ubiquitin-conjugating enzyme-9 and isopeptidase T-3, enzymes involved in small ubiquitin-related modifier-mediated nuclear import, and with glucocorticoid modulatory element binding protein-1 (GMEB-1), a transcriptional regulator.
711	2468	bind	MURF-1	GMEB-1	These data suggest that the interaction of titin with MURF-1 is important for the stability of the sarcomeric M-line region.MURF-1 also binds to ubiquitin-conjugating enzyme-9 and isopeptidase T-3, enzymes involved in small ubiquitin-related modifier-mediated nuclear import, and with glucocorticoid modulatory element binding protein-1 (GMEB-1), a transcriptional regulator.
711	2469	bind	MURF-1	isopeptidase T-3	These data suggest that the interaction of titin with MURF-1 is important for the stability of the sarcomeric M-line region.MURF-1 also binds to ubiquitin-conjugating enzyme-9 and isopeptidase T-3, enzymes involved in small ubiquitin-related modifier-mediated nuclear import, and with glucocorticoid modulatory element binding protein-1 (GMEB-1), a transcriptional regulator.
711	2470	interact	MURF-1	titin	These data suggest that the interaction of titin with MURF-1 is important for the stability of the sarcomeric M-line region.MURF-1 also binds to ubiquitin-conjugating enzyme-9 and isopeptidase T-3, enzymes involved in small ubiquitin-related modifier-mediated nuclear import, and with glucocorticoid modulatory element binding protein-1 (GMEB-1), a transcriptional regulator.
711	2471	bind	MURF-1	ubiquitin conjugating enzyme 9	These data suggest that the interaction of titin with MURF-1 is important for the stability of the sarcomeric M-line region.MURF-1 also binds to ubiquitin-conjugating enzyme-9 and isopeptidase T-3, enzymes involved in small ubiquitin-related modifier-mediated nuclear import, and with glucocorticoid modulatory element binding protein-1 (GMEB-1), a transcriptional regulator.
711	2472	bind	isopeptidase T-3	MURF-1	These data suggest that the interaction of titin with MURF-1 is important for the stability of the sarcomeric M-line region.MURF-1 also binds to ubiquitin-conjugating enzyme-9 and isopeptidase T-3, enzymes involved in small ubiquitin-related modifier-mediated nuclear import, and with glucocorticoid modulatory element binding protein-1 (GMEB-1), a transcriptional regulator.
711	2473	interact	titin	MURF-1	These data suggest that the interaction of titin with MURF-1 is important for the stability of the sarcomeric M-line region.MURF-1 also binds to ubiquitin-conjugating enzyme-9 and isopeptidase T-3, enzymes involved in small ubiquitin-related modifier-mediated nuclear import, and with glucocorticoid modulatory element binding protein-1 (GMEB-1), a transcriptional regulator.
711	2474	bind	ubiquitin conjugating enzyme 9	MURF-1	These data suggest that the interaction of titin with MURF-1 is important for the stability of the sarcomeric M-line region.MURF-1 also binds to ubiquitin-conjugating enzyme-9 and isopeptidase T-3, enzymes involved in small ubiquitin-related modifier-mediated nuclear import, and with glucocorticoid modulatory element binding protein-1 (GMEB-1), a transcriptional regulator.
712	2475	modification	PML	SUMO-1	These findings identify the basic requirements for ND10 formation and suggest a dynamic mechanism for protein recruitment to these nuclear domains controlled by the SUMO-1 modification state of PML.
712	2476	modification	SUMO-1	PML	These findings identify the basic requirements for ND10 formation and suggest a dynamic mechanism for protein recruitment to these nuclear domains controlled by the SUMO-1 modification state of PML.
713	2477	interact	A68	ACT	These findings suggest that A68 may interact with beta A4, ubiquitin, and ACT in neuronal perikarya as well as in the extracellular space after release of A68 from degenerating neurons.
713	2478	interact	A68	beta A4	These findings suggest that A68 may interact with beta A4, ubiquitin, and ACT in neuronal perikarya as well as in the extracellular space after release of A68 from degenerating neurons.
713	2479	interact	A68	ubiquitin	These findings suggest that A68 may interact with beta A4, ubiquitin, and ACT in neuronal perikarya as well as in the extracellular space after release of A68 from degenerating neurons.
713	2480	interact	ACT	A68	These findings suggest that A68 may interact with beta A4, ubiquitin, and ACT in neuronal perikarya as well as in the extracellular space after release of A68 from degenerating neurons.
713	2481	interact	beta A4	A68	These findings suggest that A68 may interact with beta A4, ubiquitin, and ACT in neuronal perikarya as well as in the extracellular space after release of A68 from degenerating neurons.
713	2482	interact	ubiquitin	A68	These findings suggest that A68 may interact with beta A4, ubiquitin, and ACT in neuronal perikarya as well as in the extracellular space after release of A68 from degenerating neurons.
714	2483	bound	H2A	ubiquitin	These fractions included three subfractions of linker histones (H1a, H1b, H1(0)), four nucleosomal core histones (H2A, H2B, H3, H4), and the modified core histone, A24 (uH2A), comprised of H2A covalently bound to the non-histone protein, ubiquitin.
714	2484	bound	ubiquitin	H2A	These fractions included three subfractions of linker histones (H1a, H1b, H1(0)), four nucleosomal core histones (H2A, H2B, H3, H4), and the modified core histone, A24 (uH2A), comprised of H2A covalently bound to the non-histone protein, ubiquitin.
715	2485	association	Swi6p	TFIID	These interactions include association between TBP and the RSC chromatin remodeling complex, the TAF17p-dependent association of the Swi6p transactivator protein with TFIID, and the identification of three novel subunits of the SAGA acetyltransferase complex, including a putative ubiquitin-specific protease component.
715	2486	association	TFIID	Swi6p	These interactions include association between TBP and the RSC chromatin remodeling complex, the TAF17p-dependent association of the Swi6p transactivator protein with TFIID, and the identification of three novel subunits of the SAGA acetyltransferase complex, including a putative ubiquitin-specific protease component.
716	2487	bind	ENaC	rNedd4	These results demonstrate that the WW domains of rNedd4 bind to the PY motifs deleted from beta or gammaENaC in Liddle's syndrome patients, and suggest that Nedd4 may be a regulator (suppressor) of the epithelial Na+ channel.
716	2488	bind	rNedd4	ENaC	These results demonstrate that the WW domains of rNedd4 bind to the PY motifs deleted from beta or gammaENaC in Liddle's syndrome patients, and suggest that Nedd4 may be a regulator (suppressor) of the epithelial Na+ channel.
717	2489	interact	Mms2	ubiquitin	These results have identified a surface of untethered ubiquitin that interacts with Mms2 in the monomeric and heterodimeric form.
717	2490	interact	ubiquitin	Mms2	These results have identified a surface of untethered ubiquitin that interacts with Mms2 in the monomeric and heterodimeric form.
718	2491	attachment	H2A	ubiquitin	These results indicate that attachment of ubiquitin to H2A has little effect on the ability of nucleosomal arrays to form higher order folded structures in the ionic conditions tested.
718	2492	attachment	ubiquitin	H2A	These results indicate that attachment of ubiquitin to H2A has little effect on the ability of nucleosomal arrays to form higher order folded structures in the ionic conditions tested.
719	2493	complex	betaTrCP1	betaTrCP2	These results indicate that not only betaTrCP1 but also betaTrCP2 participates in the ubiquitination-dependent destruction of IkappaBalpha by forming SCF(betaTrCP1-betaTrCP1) and SCF(betaTrCP2-betaTrCP2) ubiquitin-ligase complexes.
719	2494	complex	betaTrCP2	betaTrCP1	These results indicate that not only betaTrCP1 but also betaTrCP2 participates in the ubiquitination-dependent destruction of IkappaBalpha by forming SCF(betaTrCP1-betaTrCP1) and SCF(betaTrCP2-betaTrCP2) ubiquitin-ligase complexes.
720	2495	interact	IE1	PML-bodies	These results indicate that the HHV-6 IE1 protein interacts with PML-bodies yet, unlike other herpesviruses, HHV-6 appears to have no requirement or mechanism to induce PML-body dispersal during lytic replication.
720	2496	interact	PML-bodies	IE1	These results indicate that the HHV-6 IE1 protein interacts with PML-bodies yet, unlike other herpesviruses, HHV-6 appears to have no requirement or mechanism to induce PML-body dispersal during lytic replication.
721	2497	interact	Apg12p	Apg7p	These results indicated that Apg12p interacts with Apg7p via a thioester bond.
721	2498	interact	Apg7p	Apg12p	These results indicated that Apg12p interacts with Apg7p via a thioester bond.
722	2499	conjugate	AtCUL1	RUB	These results provide strong support for a model in which RUB conjugation of AtCUL1 affects the function of SCF E3s that are required for auxin response.
722	2500	conjugate	RUB	AtCUL1	These results provide strong support for a model in which RUB conjugation of AtCUL1 affects the function of SCF E3s that are required for auxin response.
723	2501	activate	APC	Cdc28	These results show that Cdc28 activates the APC in budding yeast to trigger anaphase.
723	2502	activate	Cdc28	APC	These results show that Cdc28 activates the APC in budding yeast to trigger anaphase.
724	2503	interact	Cdc48	Hsc70	These results show that Cdc48 possesses chaperone-like activities and can functionally interact with Hsc70.
724	2504	interact	Hsc70	Cdc48	These results show that Cdc48 possesses chaperone-like activities and can functionally interact with Hsc70.
725	2505	interact	E2-p38	PKR	These results show that E2-p38 is the form of E2 that interacts with PKR in the cytosol and may contribute to the resistance of HCV to IFN-alpha.
725	2506	interact	PKR	E2-p38	These results show that E2-p38 is the form of E2 that interacts with PKR in the cytosol and may contribute to the resistance of HCV to IFN-alpha.
726	2507	association	Grr1	Skp1	These results strongly suggest that Grr1 functions in the ubiquitin pathway through association with Skp1.
726	2508	association	Skp1	Grr1	These results strongly suggest that Grr1 functions in the ubiquitin pathway through association with Skp1.
727	2509	modifies	HsUbc9	RanGAP1	These results suggest that HsUbc9 is a component of a novel enzymatic cascade that modifies RanGAP1, and possibly other substrates, with SUMO-1.
727	2510	modifies	RanGAP1	HsUbc9	These results suggest that HsUbc9 is a component of a novel enzymatic cascade that modifies RanGAP1, and possibly other substrates, with SUMO-1.
728	2511	activate	NADPH oxidase	Rac1	These results suggest that Rac1 activation of NADPH oxidase is necessary for the proteolytic degradation of Rac1 itself.
728	2512	activate	Rac1	NADPH oxidase	These results suggest that Rac1 activation of NADPH oxidase is necessary for the proteolytic degradation of Rac1 itself.
729	2513	phosphorylation	Cdk2	p27	These results suggest that if phosphorylation of p27 by Cdk2/Cyclin E is involved in its ubiquitin-dependent degradation, as previously suggested, then the target for such event is the phosphorylated p27 bound to Cdk2/Cyclin E and not free p27.
729	2514	phosphorylation	Cyclin E	p27	These results suggest that if phosphorylation of p27 by Cdk2/Cyclin E is involved in its ubiquitin-dependent degradation, as previously suggested, then the target for such event is the phosphorylated p27 bound to Cdk2/Cyclin E and not free p27.
729	2515	phosphorylation	p27	Cdk2	These results suggest that if phosphorylation of p27 by Cdk2/Cyclin E is involved in its ubiquitin-dependent degradation, as previously suggested, then the target for such event is the phosphorylated p27 bound to Cdk2/Cyclin E and not free p27.
729	2516	phosphorylation	p27	Cyclin E	These results suggest that if phosphorylation of p27 by Cdk2/Cyclin E is involved in its ubiquitin-dependent degradation, as previously suggested, then the target for such event is the phosphorylated p27 bound to Cdk2/Cyclin E and not free p27.
730	2517	interaction	Rod1	Rsp5	These results suggest that interaction of Rod1 and Rsp5 is important for drug resistance.
730	2518	interaction	Rsp5	Rod1	These results suggest that interaction of Rod1 and Rsp5 is important for drug resistance.
731	2519	ubiquitinate	cdc25	pub1	These results suggest that pub1 directly ubiquitinates cdc25 in vivo.
731	2520	ubiquitinate	pub1	cdc25	These results suggest that pub1 directly ubiquitinates cdc25 in vivo.
732	2521	conjugation	ubiquitin	ubiquitin	These results suggest that the conjugation of ubiquitin to ubiquitin during polyubiquitin synthesis involves a specific conjugation system that recognizes ubiquitin and some of its derivatives, but not general proteolysis substrates, as ubiquitin acceptors.
733	2522	bind	CUL1	ROC1	These results suggest the mode of action of SCF-ROC1, where CUL1 serves as a dual-function molecule that recruits an F-box protein for substrate targeting through Skp1 at its N terminus, while the C terminus of CUL1 binds ROC1 to assemble a core ubiquitin ligase.
733	2523	bind	ROC1	CUL1	These results suggest the mode of action of SCF-ROC1, where CUL1 serves as a dual-function molecule that recruits an F-box protein for substrate targeting through Skp1 at its N terminus, while the C terminus of CUL1 binds ROC1 to assemble a core ubiquitin ligase.
734	2524	interact	AhR	Nedd8	These studies demonstrate that the AhR interacts with Nedd8 and suggest that this interaction enhances the transcriptional activity of the receptor, perhaps involving increased nuclear accumulation or retention.
734	2525	interact	Nedd8	AhR	These studies demonstrate that the AhR interacts with Nedd8 and suggest that this interaction enhances the transcriptional activity of the receptor, perhaps involving increased nuclear accumulation or retention.
735	2526	interaction	CUL1	SKP1	This CUL1-SKP1 interaction is mediated by the NH2-terminal domains of both proteins, and the association appears to be required for the interaction of CUL1 with SKP2, an essential element of the S-phase cyclin A-CDK2 kinase.
735	2527	interaction	CUL1	SKP2	This CUL1-SKP1 interaction is mediated by the NH2-terminal domains of both proteins, and the association appears to be required for the interaction of CUL1 with SKP2, an essential element of the S-phase cyclin A-CDK2 kinase.
735	2528	interaction	SKP1	CUL1	This CUL1-SKP1 interaction is mediated by the NH2-terminal domains of both proteins, and the association appears to be required for the interaction of CUL1 with SKP2, an essential element of the S-phase cyclin A-CDK2 kinase.
735	2529	interaction	SKP2	CUL1	This CUL1-SKP1 interaction is mediated by the NH2-terminal domains of both proteins, and the association appears to be required for the interaction of CUL1 with SKP2, an essential element of the S-phase cyclin A-CDK2 kinase.
736	2530	interaction	E6	E6-AP	This S. pombe based system represents a candidate screen for novel antiviral agents that act by disrupting the E6/E6-AP/p53 interaction.
736	2531	interaction	E6	p53	This S. pombe based system represents a candidate screen for novel antiviral agents that act by disrupting the E6/E6-AP/p53 interaction.
736	2532	interaction	E6-AP	E6	This S. pombe based system represents a candidate screen for novel antiviral agents that act by disrupting the E6/E6-AP/p53 interaction.
736	2533	interaction	E6-AP	p53	This S. pombe based system represents a candidate screen for novel antiviral agents that act by disrupting the E6/E6-AP/p53 interaction.
736	2534	interaction	p53	E6	This S. pombe based system represents a candidate screen for novel antiviral agents that act by disrupting the E6/E6-AP/p53 interaction.
736	2535	interaction	p53	E6-AP	This S. pombe based system represents a candidate screen for novel antiviral agents that act by disrupting the E6/E6-AP/p53 interaction.
737	2536	interaction	EDD	PR	This activity is comparable with that of the coactivator SRC-1, but, in contrast, the interaction between EDD and PR does not appear to involve an LXXLL receptor-binding motif.
737	2537	interaction	PR	EDD	This activity is comparable with that of the coactivator SRC-1, but, in contrast, the interaction between EDD and PR does not appear to involve an LXXLL receptor-binding motif.
738	2538	binding	HDM2	p53	This activity is dependent on binding of p53 to HDM2, and requires an intact p53 NES, but is independent of the HDM2 NES.
738	2539	binding	p53	HDM2	This activity is dependent on binding of p53 to HDM2, and requires an intact p53 NES, but is independent of the HDM2 NES.
739	2540	interacting	BAG-1L	Hsc70	This activity is unique to BAG-1M in that other isoforms, BAG-1S and BAG-1L, are much weaker in this activity, although all of the isoforms share common ubiquitin-like domain and BAG domain interacting with Hsp70/Hsc70.
739	2541	interacting	BAG-1L	Hsp70	This activity is unique to BAG-1M in that other isoforms, BAG-1S and BAG-1L, are much weaker in this activity, although all of the isoforms share common ubiquitin-like domain and BAG domain interacting with Hsp70/Hsc70.
739	2542	interacting	BAG-1M	Hsc70	This activity is unique to BAG-1M in that other isoforms, BAG-1S and BAG-1L, are much weaker in this activity, although all of the isoforms share common ubiquitin-like domain and BAG domain interacting with Hsp70/Hsc70.
739	2543	interacting	BAG-1M	Hsp70	This activity is unique to BAG-1M in that other isoforms, BAG-1S and BAG-1L, are much weaker in this activity, although all of the isoforms share common ubiquitin-like domain and BAG domain interacting with Hsp70/Hsc70.
739	2544	interacting	BAG-1S	Hsc70	This activity is unique to BAG-1M in that other isoforms, BAG-1S and BAG-1L, are much weaker in this activity, although all of the isoforms share common ubiquitin-like domain and BAG domain interacting with Hsp70/Hsc70.
739	2545	interacting	BAG-1S	Hsp70	This activity is unique to BAG-1M in that other isoforms, BAG-1S and BAG-1L, are much weaker in this activity, although all of the isoforms share common ubiquitin-like domain and BAG domain interacting with Hsp70/Hsc70.
739	2546	interacting	Hsc70	BAG-1L	This activity is unique to BAG-1M in that other isoforms, BAG-1S and BAG-1L, are much weaker in this activity, although all of the isoforms share common ubiquitin-like domain and BAG domain interacting with Hsp70/Hsc70.
739	2547	interacting	Hsc70	BAG-1M	This activity is unique to BAG-1M in that other isoforms, BAG-1S and BAG-1L, are much weaker in this activity, although all of the isoforms share common ubiquitin-like domain and BAG domain interacting with Hsp70/Hsc70.
739	2548	interacting	Hsc70	BAG-1S	This activity is unique to BAG-1M in that other isoforms, BAG-1S and BAG-1L, are much weaker in this activity, although all of the isoforms share common ubiquitin-like domain and BAG domain interacting with Hsp70/Hsc70.
739	2549	interacting	Hsp70	BAG-1L	This activity is unique to BAG-1M in that other isoforms, BAG-1S and BAG-1L, are much weaker in this activity, although all of the isoforms share common ubiquitin-like domain and BAG domain interacting with Hsp70/Hsc70.
739	2550	interacting	Hsp70	BAG-1M	This activity is unique to BAG-1M in that other isoforms, BAG-1S and BAG-1L, are much weaker in this activity, although all of the isoforms share common ubiquitin-like domain and BAG domain interacting with Hsp70/Hsc70.
739	2551	interacting	Hsp70	BAG-1S	This activity is unique to BAG-1M in that other isoforms, BAG-1S and BAG-1L, are much weaker in this activity, although all of the isoforms share common ubiquitin-like domain and BAG domain interacting with Hsp70/Hsc70.
740	2552	complex	Cdc2p	Cdc6p	This activity of Cdc6p is entirely contained within a short N-terminal peptide, which forms a tight complex with Cdc2p and the F-box/WD-repeat protein Sud1p/Pop2p, a component of the SCF(Pop) ubiquitin ligase in fission yeast.
740	2553	complex	Cdc2p	Pop2p	This activity of Cdc6p is entirely contained within a short N-terminal peptide, which forms a tight complex with Cdc2p and the F-box/WD-repeat protein Sud1p/Pop2p, a component of the SCF(Pop) ubiquitin ligase in fission yeast.
740	2554	complex	Cdc2p	Sud1p	This activity of Cdc6p is entirely contained within a short N-terminal peptide, which forms a tight complex with Cdc2p and the F-box/WD-repeat protein Sud1p/Pop2p, a component of the SCF(Pop) ubiquitin ligase in fission yeast.
740	2555	complex	Cdc6p	Cdc2p	This activity of Cdc6p is entirely contained within a short N-terminal peptide, which forms a tight complex with Cdc2p and the F-box/WD-repeat protein Sud1p/Pop2p, a component of the SCF(Pop) ubiquitin ligase in fission yeast.
740	2556	complex	Cdc6p	Pop2p	This activity of Cdc6p is entirely contained within a short N-terminal peptide, which forms a tight complex with Cdc2p and the F-box/WD-repeat protein Sud1p/Pop2p, a component of the SCF(Pop) ubiquitin ligase in fission yeast.
740	2557	complex	Cdc6p	Sud1p	This activity of Cdc6p is entirely contained within a short N-terminal peptide, which forms a tight complex with Cdc2p and the F-box/WD-repeat protein Sud1p/Pop2p, a component of the SCF(Pop) ubiquitin ligase in fission yeast.
740	2558	complex	Pop2p	Cdc2p	This activity of Cdc6p is entirely contained within a short N-terminal peptide, which forms a tight complex with Cdc2p and the F-box/WD-repeat protein Sud1p/Pop2p, a component of the SCF(Pop) ubiquitin ligase in fission yeast.
740	2559	complex	Pop2p	Cdc6p	This activity of Cdc6p is entirely contained within a short N-terminal peptide, which forms a tight complex with Cdc2p and the F-box/WD-repeat protein Sud1p/Pop2p, a component of the SCF(Pop) ubiquitin ligase in fission yeast.
740	2560	complex	Sud1p	Cdc2p	This activity of Cdc6p is entirely contained within a short N-terminal peptide, which forms a tight complex with Cdc2p and the F-box/WD-repeat protein Sud1p/Pop2p, a component of the SCF(Pop) ubiquitin ligase in fission yeast.
740	2561	complex	Sud1p	Cdc6p	This activity of Cdc6p is entirely contained within a short N-terminal peptide, which forms a tight complex with Cdc2p and the F-box/WD-repeat protein Sud1p/Pop2p, a component of the SCF(Pop) ubiquitin ligase in fission yeast.
741	2562	linkage	CUL1	Nedd8	This covalent linkage of Nedd8 to CUL1 is both necessary and sufficient to markedly enhance the ability of the ROC1-CUL1 complex to promote ubiquitin polymerization.
741	2563	linkage	Nedd8	CUL1	This covalent linkage of Nedd8 to CUL1 is both necessary and sufficient to markedly enhance the ability of the ROC1-CUL1 complex to promote ubiquitin polymerization.
742	2564	interaction	Mdm2	p53	This degradation requires interaction between p53 and Mdm2 and the subsequent ubiquitination and nuclear export of p53.
742	2565	interaction	p53	Mdm2	This degradation requires interaction between p53 and Mdm2 and the subsequent ubiquitination and nuclear export of p53.
743	2566	interaction	CUP9	UBR1	This dissociation, which allows the interaction between UBR1 and CUP9, is strongly increased only if both type 1- and type 2-binding sites of UBR1 are occupied by dipeptides.
743	2567	interaction	UBR1	CUP9	This dissociation, which allows the interaction between UBR1 and CUP9, is strongly increased only if both type 1- and type 2-binding sites of UBR1 are occupied by dipeptides.
744	2568	binding	HIF	VHL	This increased stability is due to the absence of proline hydroxylation, which in normoxia promotes binding of HIF to the von Hippel-Lindau (VHL tumor suppressor) ubiquitin ligase.
744	2569	binding	VHL	HIF	This increased stability is due to the absence of proline hydroxylation, which in normoxia promotes binding of HIF to the von Hippel-Lindau (VHL tumor suppressor) ubiquitin ligase.
745	2570	interact	UbcH5B	sentrin	This interaction appears to be specific because sentrin could only interact weakly with UbcH5B, but could not interact with HHR6B, UbcH6 nor E2-EPF.
745	2571	interact	sentrin	UbcH5B	This interaction appears to be specific because sentrin could only interact weakly with UbcH5B, but could not interact with HHR6B, UbcH6 nor E2-EPF.
746	2572	conjugated	RanGAP1	SUMO-1	This interaction requires the ATP-dependent posttranslational conjugation of RanGAP1 with SUMO-1 (for small ubiquitin-related modifier), a novel protein of 101 amino acids that contains low but significant homology to ubiquitin.
746	2573	conjugated	SUMO-1	RanGAP1	This interaction requires the ATP-dependent posttranslational conjugation of RanGAP1 with SUMO-1 (for small ubiquitin-related modifier), a novel protein of 101 amino acids that contains low but significant homology to ubiquitin.
747	2574	bind	Ddi1	ubiquitin	This observation, coupled with the findings that Rad23 and Ddi1 UBA domains bind ubiquitin and that dimerization of Rad23 blocks ubiquitin binding, suggests a possible mechanism for regulating Rad23 and Ddi1 function.
747	2575	bind	Rad23	ubiquitin	This observation, coupled with the findings that Rad23 and Ddi1 UBA domains bind ubiquitin and that dimerization of Rad23 blocks ubiquitin binding, suggests a possible mechanism for regulating Rad23 and Ddi1 function.
747	2576	bind	ubiquitin	Ddi1	This observation, coupled with the findings that Rad23 and Ddi1 UBA domains bind ubiquitin and that dimerization of Rad23 blocks ubiquitin binding, suggests a possible mechanism for regulating Rad23 and Ddi1 function.
747	2577	bind	ubiquitin	Rad23	This observation, coupled with the findings that Rad23 and Ddi1 UBA domains bind ubiquitin and that dimerization of Rad23 blocks ubiquitin binding, suggests a possible mechanism for regulating Rad23 and Ddi1 function.
748	2578	bound	Apg12	Apg5	This process requires a ubiquitin-like protein conjugation system, in which Apg12 is covalently bound to Apg5.
748	2579	bound	Apg5	Apg12	This process requires a ubiquitin-like protein conjugation system, in which Apg12 is covalently bound to Apg5.
749	2580	conjugated	CUL1	Nedd8	This report describes that the CUL1 subunit of the bacterially expressed, unmodified ROC1-CUL1 complex is conjugated with Nedd8 at Lys-720 by HeLa cell extracts or by a purified Nedd8 conjugation system (consisting of APP-BP1/Uba3, Ubc12, and Nedd8).
749	2581	conjugated	Nedd8	CUL1	This report describes that the CUL1 subunit of the bacterially expressed, unmodified ROC1-CUL1 complex is conjugated with Nedd8 at Lys-720 by HeLa cell extracts or by a purified Nedd8 conjugation system (consisting of APP-BP1/Uba3, Ubc12, and Nedd8).
750	2582	activate	APC	Cdc20p	This review describes the known components and substrates of the mitotic ubiquitination machinery and discusses how a new subfamily of proteins that contain the WD40 repeat (the Fizzy/Cdc20p family) might activate the APC/C to allow temporal differences in substrate ubiquitination during progression through mitosis.
750	2583	activate	APC	Fizzy	This review describes the known components and substrates of the mitotic ubiquitination machinery and discusses how a new subfamily of proteins that contain the WD40 repeat (the Fizzy/Cdc20p family) might activate the APC/C to allow temporal differences in substrate ubiquitination during progression through mitosis.
750	2584	activate	Cdc20p	APC	This review describes the known components and substrates of the mitotic ubiquitination machinery and discusses how a new subfamily of proteins that contain the WD40 repeat (the Fizzy/Cdc20p family) might activate the APC/C to allow temporal differences in substrate ubiquitination during progression through mitosis.
750	2585	activate	Fizzy	APC	This review describes the known components and substrates of the mitotic ubiquitination machinery and discusses how a new subfamily of proteins that contain the WD40 repeat (the Fizzy/Cdc20p family) might activate the APC/C to allow temporal differences in substrate ubiquitination during progression through mitosis.
751	2586	interact	EDD	importin alpha 5	This study shows that EDD interacts with importin alpha 5 through consensus basic nuclear localization signals and is localized in cell nuclei.
751	2587	interact	importin alpha 5	EDD	This study shows that EDD interacts with importin alpha 5 through consensus basic nuclear localization signals and is localized in cell nuclei.
752	2588	binding	VBC	hCUL-2	This system was then used to map the binding region of hCUL-2 for the VBC complex.
752	2589	binding	hCUL-2	VBC	This system was then used to map the binding region of hCUL-2 for the VBC complex.
753	2590	association	Src-beta2-AR	beta-arrestin-1-Src	This was associated with a decrease in beta-arrestin-1 association with the beta2-AR as well as a decrease in beta-arrestin-1-Src and Src-beta2-AR association.
753	2591	association	beta-arrestin-1	beta2-AR	This was associated with a decrease in beta-arrestin-1 association with the beta2-AR as well as a decrease in beta-arrestin-1-Src and Src-beta2-AR association.
753	2592	association	beta-arrestin-1-Src	Src-beta2-AR	This was associated with a decrease in beta-arrestin-1 association with the beta2-AR as well as a decrease in beta-arrestin-1-Src and Src-beta2-AR association.
753	2593	association	beta2-AR	beta-arrestin-1	This was associated with a decrease in beta-arrestin-1 association with the beta2-AR as well as a decrease in beta-arrestin-1-Src and Src-beta2-AR association.
754	2594	modification	HSF1	SUMO-1	This work implicates SUMO-1 modification as an important modulator of HSF1 function in response to stress.
754	2595	modification	SUMO-1	HSF1	This work implicates SUMO-1 modification as an important modulator of HSF1 function in response to stress.
755	2596	bind	RNase A	hsc73	Three lines of evidence indicate that prp73 is the heat shock cognate protein of 73 kDa (hsc73): (a) among five hsp70s tested, hsc73 binds to RNase S-peptide most avidly, (b) both prp73 and hsc73 also bind to RNase A and aspartate aminotransferase but not to ovalbumin, lysozyme, or ubiquitin, and (c) both prp73 and hsc73 promote uptake and degradation of [3H] RNase S-peptide by lysosomes in vitro, while three other hsp70s are without activity in this assay.
755	2597	bind	RNase A	prp73	Three lines of evidence indicate that prp73 is the heat shock cognate protein of 73 kDa (hsc73): (a) among five hsp70s tested, hsc73 binds to RNase S-peptide most avidly, (b) both prp73 and hsc73 also bind to RNase A and aspartate aminotransferase but not to ovalbumin, lysozyme, or ubiquitin, and (c) both prp73 and hsc73 promote uptake and degradation of [3H] RNase S-peptide by lysosomes in vitro, while three other hsp70s are without activity in this assay.
755	2598	bind	aspartate aminotransferase	hsc73	Three lines of evidence indicate that prp73 is the heat shock cognate protein of 73 kDa (hsc73): (a) among five hsp70s tested, hsc73 binds to RNase S-peptide most avidly, (b) both prp73 and hsc73 also bind to RNase A and aspartate aminotransferase but not to ovalbumin, lysozyme, or ubiquitin, and (c) both prp73 and hsc73 promote uptake and degradation of [3H] RNase S-peptide by lysosomes in vitro, while three other hsp70s are without activity in this assay.
755	2599	bind	aspartate aminotransferase	prp73	Three lines of evidence indicate that prp73 is the heat shock cognate protein of 73 kDa (hsc73): (a) among five hsp70s tested, hsc73 binds to RNase S-peptide most avidly, (b) both prp73 and hsc73 also bind to RNase A and aspartate aminotransferase but not to ovalbumin, lysozyme, or ubiquitin, and (c) both prp73 and hsc73 promote uptake and degradation of [3H] RNase S-peptide by lysosomes in vitro, while three other hsp70s are without activity in this assay.
755	2600	bind	hsc73	RNase A	Three lines of evidence indicate that prp73 is the heat shock cognate protein of 73 kDa (hsc73): (a) among five hsp70s tested, hsc73 binds to RNase S-peptide most avidly, (b) both prp73 and hsc73 also bind to RNase A and aspartate aminotransferase but not to ovalbumin, lysozyme, or ubiquitin, and (c) both prp73 and hsc73 promote uptake and degradation of [3H] RNase S-peptide by lysosomes in vitro, while three other hsp70s are without activity in this assay.
755	2601	bind	hsc73	aspartate aminotransferase	Three lines of evidence indicate that prp73 is the heat shock cognate protein of 73 kDa (hsc73): (a) among five hsp70s tested, hsc73 binds to RNase S-peptide most avidly, (b) both prp73 and hsc73 also bind to RNase A and aspartate aminotransferase but not to ovalbumin, lysozyme, or ubiquitin, and (c) both prp73 and hsc73 promote uptake and degradation of [3H] RNase S-peptide by lysosomes in vitro, while three other hsp70s are without activity in this assay.
755	2602	bind	prp73	RNase A	Three lines of evidence indicate that prp73 is the heat shock cognate protein of 73 kDa (hsc73): (a) among five hsp70s tested, hsc73 binds to RNase S-peptide most avidly, (b) both prp73 and hsc73 also bind to RNase A and aspartate aminotransferase but not to ovalbumin, lysozyme, or ubiquitin, and (c) both prp73 and hsc73 promote uptake and degradation of [3H] RNase S-peptide by lysosomes in vitro, while three other hsp70s are without activity in this assay.
755	2603	bind	prp73	aspartate aminotransferase	Three lines of evidence indicate that prp73 is the heat shock cognate protein of 73 kDa (hsc73): (a) among five hsp70s tested, hsc73 binds to RNase S-peptide most avidly, (b) both prp73 and hsc73 also bind to RNase A and aspartate aminotransferase but not to ovalbumin, lysozyme, or ubiquitin, and (c) both prp73 and hsc73 promote uptake and degradation of [3H] RNase S-peptide by lysosomes in vitro, while three other hsp70s are without activity in this assay.
756	2604	modification	GR	SUMO-1	Thus SUMO-1 modification of GR influences receptor function in a promoter context-dependent fashion.
756	2605	modification	SUMO-1	GR	Thus SUMO-1 modification of GR influences receptor function in a promoter context-dependent fashion.
757	2606	interact	Ulp1	nucleoporins	Thus Ulp1 associates with nucleoporins and may interact with septin rings in the telophase.
757	2607	interact	Ulp1	septin	Thus Ulp1 associates with nucleoporins and may interact with septin rings in the telophase.
757	2608	interact	nucleoporins	Ulp1	Thus Ulp1 associates with nucleoporins and may interact with septin rings in the telophase.
757	2609	interact	septin	Ulp1	Thus Ulp1 associates with nucleoporins and may interact with septin rings in the telophase.
758	2610	activate	CHUK	NIK	Thus, CHUK is a NIK-activated IkappaB-alpha kinase that links TNF- and IL-1-induced kinase cascades to NF-kappaB activation.
758	2611	activate	NIK	CHUK	Thus, CHUK is a NIK-activated IkappaB-alpha kinase that links TNF- and IL-1-induced kinase cascades to NF-kappaB activation.
759	2612	linked	HDAC6	ubiquitin	Thus, HDAC6 is linked to the ubiquitin system via ubiquitin conjugation, polyubiquitin binding, and copurification with deubiquitinating enzymes.
759	2613	linked	ubiquitin	HDAC6	Thus, HDAC6 is linked to the ubiquitin system via ubiquitin conjugation, polyubiquitin binding, and copurification with deubiquitinating enzymes.
760	2614	target	APC	Clb2	Thus, RPN3 function is required for the degradation of the G(1)-phase cyclin Cln2 targeted by SCF; the S-phase cyclin Clb5, whose ubiquitination is likely to involve a combination of E3 (ubiquitin protein ligase) enzymes; and anaphase-promoting complex targets, such as the B-type cyclin Clb2 and the anaphase inhibitor Pds1.
760	2615	target	APC	Pds1	Thus, RPN3 function is required for the degradation of the G(1)-phase cyclin Cln2 targeted by SCF; the S-phase cyclin Clb5, whose ubiquitination is likely to involve a combination of E3 (ubiquitin protein ligase) enzymes; and anaphase-promoting complex targets, such as the B-type cyclin Clb2 and the anaphase inhibitor Pds1.
760	2616	target	Clb2	APC	Thus, RPN3 function is required for the degradation of the G(1)-phase cyclin Cln2 targeted by SCF; the S-phase cyclin Clb5, whose ubiquitination is likely to involve a combination of E3 (ubiquitin protein ligase) enzymes; and anaphase-promoting complex targets, such as the B-type cyclin Clb2 and the anaphase inhibitor Pds1.
760	2617	target	Cln2	SCF	Thus, RPN3 function is required for the degradation of the G(1)-phase cyclin Cln2 targeted by SCF; the S-phase cyclin Clb5, whose ubiquitination is likely to involve a combination of E3 (ubiquitin protein ligase) enzymes; and anaphase-promoting complex targets, such as the B-type cyclin Clb2 and the anaphase inhibitor Pds1.
760	2618	target	Pds1	APC	Thus, RPN3 function is required for the degradation of the G(1)-phase cyclin Cln2 targeted by SCF; the S-phase cyclin Clb5, whose ubiquitination is likely to involve a combination of E3 (ubiquitin protein ligase) enzymes; and anaphase-promoting complex targets, such as the B-type cyclin Clb2 and the anaphase inhibitor Pds1.
760	2619	target	SCF	Cln2	Thus, RPN3 function is required for the degradation of the G(1)-phase cyclin Cln2 targeted by SCF; the S-phase cyclin Clb5, whose ubiquitination is likely to involve a combination of E3 (ubiquitin protein ligase) enzymes; and anaphase-promoting complex targets, such as the B-type cyclin Clb2 and the anaphase inhibitor Pds1.
761	2620	interaction	ENaC	hNedd4	Thus, WW domains 2-4 each participate in the functional interaction between hNedd4 and ENaC in intact cells.
761	2621	interaction	hNedd4	ENaC	Thus, WW domains 2-4 each participate in the functional interaction between hNedd4 and ENaC in intact cells.
762	2622	modified	CREB	SUMO-1	Thus, in prolonged hypoxia, CREB is modified by association with SUMO-1.
762	2623	modified	SUMO-1	CREB	Thus, in prolonged hypoxia, CREB is modified by association with SUMO-1.
763	2624	complex	elongin B	elongin C	Thus, it seems possible that pVHL/elongin BC/hCUL-2 complex will possess ubiquitin ligase activity targeting specific proteins for degradation by the proteasome.
763	2625	complex	elongin B	hCUL-2	Thus, it seems possible that pVHL/elongin BC/hCUL-2 complex will possess ubiquitin ligase activity targeting specific proteins for degradation by the proteasome.
763	2626	complex	elongin B	pVHL	Thus, it seems possible that pVHL/elongin BC/hCUL-2 complex will possess ubiquitin ligase activity targeting specific proteins for degradation by the proteasome.
763	2627	complex	elongin C	elongin B	Thus, it seems possible that pVHL/elongin BC/hCUL-2 complex will possess ubiquitin ligase activity targeting specific proteins for degradation by the proteasome.
763	2628	complex	elongin C	hCUL-2	Thus, it seems possible that pVHL/elongin BC/hCUL-2 complex will possess ubiquitin ligase activity targeting specific proteins for degradation by the proteasome.
763	2629	complex	elongin C	pVHL	Thus, it seems possible that pVHL/elongin BC/hCUL-2 complex will possess ubiquitin ligase activity targeting specific proteins for degradation by the proteasome.
763	2630	complex	hCUL-2	elongin B	Thus, it seems possible that pVHL/elongin BC/hCUL-2 complex will possess ubiquitin ligase activity targeting specific proteins for degradation by the proteasome.
763	2631	complex	hCUL-2	elongin C	Thus, it seems possible that pVHL/elongin BC/hCUL-2 complex will possess ubiquitin ligase activity targeting specific proteins for degradation by the proteasome.
763	2632	complex	hCUL-2	pVHL	Thus, it seems possible that pVHL/elongin BC/hCUL-2 complex will possess ubiquitin ligase activity targeting specific proteins for degradation by the proteasome.
763	2633	complex	pVHL	elongin B	Thus, it seems possible that pVHL/elongin BC/hCUL-2 complex will possess ubiquitin ligase activity targeting specific proteins for degradation by the proteasome.
763	2634	complex	pVHL	elongin C	Thus, it seems possible that pVHL/elongin BC/hCUL-2 complex will possess ubiquitin ligase activity targeting specific proteins for degradation by the proteasome.
763	2635	complex	pVHL	hCUL-2	Thus, it seems possible that pVHL/elongin BC/hCUL-2 complex will possess ubiquitin ligase activity targeting specific proteins for degradation by the proteasome.
764	2636	modified	HIPK2	SUMO-1	Thus, our results provide firm evidence that the nuclear protein kinase HIPK2 can be covalently modified by SUMO-1, which directs its localization to nuclear speckles (dots).
764	2637	modified	SUMO-1	HIPK2	Thus, our results provide firm evidence that the nuclear protein kinase HIPK2 can be covalently modified by SUMO-1, which directs its localization to nuclear speckles (dots).
765	2638	bind	p62	ubiquitin	Thus, p62 binds to ubiquitin noncovalently.
765	2639	bind	ubiquitin	p62	Thus, p62 binds to ubiquitin noncovalently.
766	2640	binding	ICP0	cdc34	Thus, substitution of ICP0 aspartate 199 with alanine attenuates the degradation of cdc34 and its binding to the ICP0 ring finger domain. (ii) Substitution of residue 620 reported to abolish the interaction with a ubiquitin-specific protease has no effect on the function of ubiquitin ligase. (iii) ICP0 contains an additional distinct E3 ligase activity specific for the UbcH5a- and UbcH6 E2-conjugating enzymes mapping to the ring finger domain.
766	2641	binding	cdc34	ICP0	Thus, substitution of ICP0 aspartate 199 with alanine attenuates the degradation of cdc34 and its binding to the ICP0 ring finger domain. (ii) Substitution of residue 620 reported to abolish the interaction with a ubiquitin-specific protease has no effect on the function of ubiquitin ligase. (iii) ICP0 contains an additional distinct E3 ligase activity specific for the UbcH5a- and UbcH6 E2-conjugating enzymes mapping to the ring finger domain.
767	2642	conjugate	Cdc3	Smt3	Thus, we conclude that Smt3 was conjugated to Cdc3 in septin rings localized at the mother-bud neck.
767	2643	conjugate	Smt3	Cdc3	Thus, we conclude that Smt3 was conjugated to Cdc3 in septin rings localized at the mother-bud neck.
768	2644	bind	ND10	Sp100	To determine whether Sp100 binds to ND10 through hetero- or oligomerization, Sp100 deletion variants fused with GFP were transfected into cells with and without endogenous Sp100, and the localization of the GFP-labeled fragments was determined relative to ND10.
768	2645	bind	Sp100	ND10	To determine whether Sp100 binds to ND10 through hetero- or oligomerization, Sp100 deletion variants fused with GFP were transfected into cells with and without endogenous Sp100, and the localization of the GFP-labeled fragments was determined relative to ND10.
769	2646	interact	E6	p53	To determine whether the ability of E6 to interact with p53 leads to a disruption of cell cycle control, mutated E6 proteins were tested for p53 binding and p53 degradation targeting in vitro, the ability to reduce intracellular p53 levels in vivo, and the ability to abrogate actinomycin D-induced growth arrest in human keratinocytes.
769	2647	interact	p53	E6	To determine whether the ability of E6 to interact with p53 leads to a disruption of cell cycle control, mutated E6 proteins were tested for p53 binding and p53 degradation targeting in vitro, the ability to reduce intracellular p53 levels in vivo, and the ability to abrogate actinomycin D-induced growth arrest in human keratinocytes.
770	2648	accepted	E6AP	ubiquitin	To identify the ubiquitination pathway that is linked to Nedd4, we demonstrated that specific E2 enzymes, including human Ubc4, UbcH5B, UbcH5C, UbcH6 and UbcH7, could transfer ubiquitin molecules to Nedd4 at the active cysteine residue, whereas E6AP accepted ubiquitins from Ubc4, UbcH5B, UbcH5C and UbcH7.
770	2649	transfer	Nedd4	ubiquitin	To identify the ubiquitination pathway that is linked to Nedd4, we demonstrated that specific E2 enzymes, including human Ubc4, UbcH5B, UbcH5C, UbcH6 and UbcH7, could transfer ubiquitin molecules to Nedd4 at the active cysteine residue, whereas E6AP accepted ubiquitins from Ubc4, UbcH5B, UbcH5C and UbcH7.
770	2650	transfer	Ubc4	ubiquitin	To identify the ubiquitination pathway that is linked to Nedd4, we demonstrated that specific E2 enzymes, including human Ubc4, UbcH5B, UbcH5C, UbcH6 and UbcH7, could transfer ubiquitin molecules to Nedd4 at the active cysteine residue, whereas E6AP accepted ubiquitins from Ubc4, UbcH5B, UbcH5C and UbcH7.
770	2651	transfer	UbcH5B	ubiquitin	To identify the ubiquitination pathway that is linked to Nedd4, we demonstrated that specific E2 enzymes, including human Ubc4, UbcH5B, UbcH5C, UbcH6 and UbcH7, could transfer ubiquitin molecules to Nedd4 at the active cysteine residue, whereas E6AP accepted ubiquitins from Ubc4, UbcH5B, UbcH5C and UbcH7.
770	2652	transfer	UbcH5C	ubiquitin	To identify the ubiquitination pathway that is linked to Nedd4, we demonstrated that specific E2 enzymes, including human Ubc4, UbcH5B, UbcH5C, UbcH6 and UbcH7, could transfer ubiquitin molecules to Nedd4 at the active cysteine residue, whereas E6AP accepted ubiquitins from Ubc4, UbcH5B, UbcH5C and UbcH7.
770	2653	transfer	UbcH6	ubiquitin	To identify the ubiquitination pathway that is linked to Nedd4, we demonstrated that specific E2 enzymes, including human Ubc4, UbcH5B, UbcH5C, UbcH6 and UbcH7, could transfer ubiquitin molecules to Nedd4 at the active cysteine residue, whereas E6AP accepted ubiquitins from Ubc4, UbcH5B, UbcH5C and UbcH7.
770	2654	transfer	UbcH7	ubiquitin	To identify the ubiquitination pathway that is linked to Nedd4, we demonstrated that specific E2 enzymes, including human Ubc4, UbcH5B, UbcH5C, UbcH6 and UbcH7, could transfer ubiquitin molecules to Nedd4 at the active cysteine residue, whereas E6AP accepted ubiquitins from Ubc4, UbcH5B, UbcH5C and UbcH7.
770	2655	accepted	ubiquitin	E6AP	To identify the ubiquitination pathway that is linked to Nedd4, we demonstrated that specific E2 enzymes, including human Ubc4, UbcH5B, UbcH5C, UbcH6 and UbcH7, could transfer ubiquitin molecules to Nedd4 at the active cysteine residue, whereas E6AP accepted ubiquitins from Ubc4, UbcH5B, UbcH5C and UbcH7.
770	2656	transfer	ubiquitin	Nedd4	To identify the ubiquitination pathway that is linked to Nedd4, we demonstrated that specific E2 enzymes, including human Ubc4, UbcH5B, UbcH5C, UbcH6 and UbcH7, could transfer ubiquitin molecules to Nedd4 at the active cysteine residue, whereas E6AP accepted ubiquitins from Ubc4, UbcH5B, UbcH5C and UbcH7.
770	2657	transfer	ubiquitin	Ubc4	To identify the ubiquitination pathway that is linked to Nedd4, we demonstrated that specific E2 enzymes, including human Ubc4, UbcH5B, UbcH5C, UbcH6 and UbcH7, could transfer ubiquitin molecules to Nedd4 at the active cysteine residue, whereas E6AP accepted ubiquitins from Ubc4, UbcH5B, UbcH5C and UbcH7.
770	2658	transfer	ubiquitin	UbcH5B	To identify the ubiquitination pathway that is linked to Nedd4, we demonstrated that specific E2 enzymes, including human Ubc4, UbcH5B, UbcH5C, UbcH6 and UbcH7, could transfer ubiquitin molecules to Nedd4 at the active cysteine residue, whereas E6AP accepted ubiquitins from Ubc4, UbcH5B, UbcH5C and UbcH7.
770	2659	transfer	ubiquitin	UbcH5C	To identify the ubiquitination pathway that is linked to Nedd4, we demonstrated that specific E2 enzymes, including human Ubc4, UbcH5B, UbcH5C, UbcH6 and UbcH7, could transfer ubiquitin molecules to Nedd4 at the active cysteine residue, whereas E6AP accepted ubiquitins from Ubc4, UbcH5B, UbcH5C and UbcH7.
770	2660	transfer	ubiquitin	UbcH6	To identify the ubiquitination pathway that is linked to Nedd4, we demonstrated that specific E2 enzymes, including human Ubc4, UbcH5B, UbcH5C, UbcH6 and UbcH7, could transfer ubiquitin molecules to Nedd4 at the active cysteine residue, whereas E6AP accepted ubiquitins from Ubc4, UbcH5B, UbcH5C and UbcH7.
770	2661	transfer	ubiquitin	UbcH7	To identify the ubiquitination pathway that is linked to Nedd4, we demonstrated that specific E2 enzymes, including human Ubc4, UbcH5B, UbcH5C, UbcH6 and UbcH7, could transfer ubiquitin molecules to Nedd4 at the active cysteine residue, whereas E6AP accepted ubiquitins from Ubc4, UbcH5B, UbcH5C and UbcH7.
771	2662	modified	HDAC1	SUMO-1	Together, the results demonstrate that HDAC1 is modified by SUMO-1, and this modification can dramatically affect HDAC1 activity in a number of surrogate biological assays.
771	2663	modified	SUMO-1	HDAC1	Together, the results demonstrate that HDAC1 is modified by SUMO-1, and this modification can dramatically affect HDAC1 activity in a number of surrogate biological assays.
772	2664	interaction	FWD1	IkappaBalpha	Together, these data delineate the structural requirements for the interactions among IkappaBalpha, FWD1, and Skp1 that underlie substrate recognition by the SCF ubiquitin ligase complex.
772	2665	interaction	FWD1	Skp1	Together, these data delineate the structural requirements for the interactions among IkappaBalpha, FWD1, and Skp1 that underlie substrate recognition by the SCF ubiquitin ligase complex.
772	2666	interaction	IkappaBalpha	FWD1	Together, these data delineate the structural requirements for the interactions among IkappaBalpha, FWD1, and Skp1 that underlie substrate recognition by the SCF ubiquitin ligase complex.
772	2667	interaction	IkappaBalpha	Skp1	Together, these data delineate the structural requirements for the interactions among IkappaBalpha, FWD1, and Skp1 that underlie substrate recognition by the SCF ubiquitin ligase complex.
772	2668	interaction	Skp1	FWD1	Together, these data delineate the structural requirements for the interactions among IkappaBalpha, FWD1, and Skp1 that underlie substrate recognition by the SCF ubiquitin ligase complex.
772	2669	interaction	Skp1	IkappaBalpha	Together, these data delineate the structural requirements for the interactions among IkappaBalpha, FWD1, and Skp1 that underlie substrate recognition by the SCF ubiquitin ligase complex.
773	2670	binding	Nup358	RanGAP1	Together, these findings indicate that SUMO-1 modification targets RanGAP1 to the NPC by exposing, or creating, a Nup358 binding site in the COOH-terminal domain of RanGAP1.
773	2671	binding	RanGAP1	Nup358	Together, these findings indicate that SUMO-1 modification targets RanGAP1 to the NPC by exposing, or creating, a Nup358 binding site in the COOH-terminal domain of RanGAP1.
774	2672	interact	AtGRH1	AtSKP1a	Two-hybrid experiments revealed that AtGRH1 can interact with AtSKP1a and AtSKP1b, two recently identified SKP1 homologues in Arabidopsis.
774	2673	interact	AtGRH1	AtSKP1b	Two-hybrid experiments revealed that AtGRH1 can interact with AtSKP1a and AtSKP1b, two recently identified SKP1 homologues in Arabidopsis.
774	2674	interact	AtSKP1a	AtGRH1	Two-hybrid experiments revealed that AtGRH1 can interact with AtSKP1a and AtSKP1b, two recently identified SKP1 homologues in Arabidopsis.
774	2675	interact	AtSKP1b	AtGRH1	Two-hybrid experiments revealed that AtGRH1 can interact with AtSKP1a and AtSKP1b, two recently identified SKP1 homologues in Arabidopsis.
775	2676	complexed	Rad18	Rad6	UBC2(Rad6) is complexed with the ring finger DNA-binding protein Rad18, and we find that Ho is stabilized in rad18 mutants.
775	2677	complexed	Rad18	UBC2	UBC2(Rad6) is complexed with the ring finger DNA-binding protein Rad18, and we find that Ho is stabilized in rad18 mutants.
775	2678	complexed	Rad6	Rad18	UBC2(Rad6) is complexed with the ring finger DNA-binding protein Rad18, and we find that Ho is stabilized in rad18 mutants.
775	2679	complexed	UBC2	Rad18	UBC2(Rad6) is complexed with the ring finger DNA-binding protein Rad18, and we find that Ho is stabilized in rad18 mutants.
776	2680	bind	DIAP1	Rpr	UBCD1 and Rpr specifically bind to DIAP1 and stimulate DIAP1 auto-ubiquitination in vitro.
776	2681	bind	DIAP1	UBCD1	UBCD1 and Rpr specifically bind to DIAP1 and stimulate DIAP1 auto-ubiquitination in vitro.
776	2682	bind	Rpr	DIAP1	UBCD1 and Rpr specifically bind to DIAP1 and stimulate DIAP1 auto-ubiquitination in vitro.
776	2683	bind	UBCD1	DIAP1	UBCD1 and Rpr specifically bind to DIAP1 and stimulate DIAP1 auto-ubiquitination in vitro.
777	2684	associate	RAD51	UBL1	UBL1 was found to associate with human RAD51/RAD52 proteins involved in DNA recombination and DNA double-strand break repair (10).
777	2685	associate	RAD52	UBL1	UBL1 was found to associate with human RAD51/RAD52 proteins involved in DNA recombination and DNA double-strand break repair (10).
777	2686	associate	UBL1	RAD51	UBL1 was found to associate with human RAD51/RAD52 proteins involved in DNA recombination and DNA double-strand break repair (10).
777	2687	associate	UBL1	RAD52	UBL1 was found to associate with human RAD51/RAD52 proteins involved in DNA recombination and DNA double-strand break repair (10).
778	2688	bind	UCaM Syn-F2	calmodulin	UCaM Syn-F2, which binds to calmodulin-Sepharose in a Ca2+-dependent manner, has been purified over 3500-fold in seven steps from rabbit reticulocytes and has a native molecular mass of approximately 620 kDa.
778	2689	bind	calmodulin	UCaM Syn-F2	UCaM Syn-F2, which binds to calmodulin-Sepharose in a Ca2+-dependent manner, has been purified over 3500-fold in seven steps from rabbit reticulocytes and has a native molecular mass of approximately 620 kDa.
779	2690	function	Aos1p	Uba2p	Uba2p functions together with a second protein, Aos1p.
779	2691	function	Uba2p	Aos1p	Uba2p functions together with a second protein, Aos1p.
780	2692	bound	PDGF receptor	Ubiquitin	Ubiquitin is covalently bound to the purified PDGF receptor, the human gene for which is on chromosome 5.
780	2693	bound	Ubiquitin	PDGF receptor	Ubiquitin is covalently bound to the purified PDGF receptor, the human gene for which is on chromosome 5.
781	2694	ubiquitinate	H2B	Rad6	Ubiquitinated H2B (uH2B) has been identified in the yeast Saccharomyces cerevisiae, and mutation of the conserved ubiquitination site is shown to confer defects in mitotic cell growth and meiosis. uH2B was not detected in rad6 mutants, which are defective for the ubiquitin-conjugating enzyme Ubc2, thus identifying Rad6 as the major cellular activity that ubiquitinates H2B in yeast.
781	2695	ubiquitinate	Rad6	H2B	Ubiquitinated H2B (uH2B) has been identified in the yeast Saccharomyces cerevisiae, and mutation of the conserved ubiquitination site is shown to confer defects in mitotic cell growth and meiosis. uH2B was not detected in rad6 mutants, which are defective for the ubiquitin-conjugating enzyme Ubc2, thus identifying Rad6 as the major cellular activity that ubiquitinates H2B in yeast.
782	2696	associate	Cul-1	Skp2	Ubiquitinylation of p27 requires its phosphorylation at Thr 187 and subsequent recognition by S-phase kinase associated protein 2 (Skp2), a member of the F-box family of proteins that associates with Skp1, Cul-1 and ROC1/Rbx1 to form an SCF ubiquitin ligase complex.
782	2697	associate	ROC1	Skp2	Ubiquitinylation of p27 requires its phosphorylation at Thr 187 and subsequent recognition by S-phase kinase associated protein 2 (Skp2), a member of the F-box family of proteins that associates with Skp1, Cul-1 and ROC1/Rbx1 to form an SCF ubiquitin ligase complex.
782	2698	associate	Rbx1	Skp2	Ubiquitinylation of p27 requires its phosphorylation at Thr 187 and subsequent recognition by S-phase kinase associated protein 2 (Skp2), a member of the F-box family of proteins that associates with Skp1, Cul-1 and ROC1/Rbx1 to form an SCF ubiquitin ligase complex.
782	2699	associate	Skp1	Skp2	Ubiquitinylation of p27 requires its phosphorylation at Thr 187 and subsequent recognition by S-phase kinase associated protein 2 (Skp2), a member of the F-box family of proteins that associates with Skp1, Cul-1 and ROC1/Rbx1 to form an SCF ubiquitin ligase complex.
782	2700	associate	Skp2	Cul-1	Ubiquitinylation of p27 requires its phosphorylation at Thr 187 and subsequent recognition by S-phase kinase associated protein 2 (Skp2), a member of the F-box family of proteins that associates with Skp1, Cul-1 and ROC1/Rbx1 to form an SCF ubiquitin ligase complex.
782	2701	associate	Skp2	ROC1	Ubiquitinylation of p27 requires its phosphorylation at Thr 187 and subsequent recognition by S-phase kinase associated protein 2 (Skp2), a member of the F-box family of proteins that associates with Skp1, Cul-1 and ROC1/Rbx1 to form an SCF ubiquitin ligase complex.
782	2702	associate	Skp2	Rbx1	Ubiquitinylation of p27 requires its phosphorylation at Thr 187 and subsequent recognition by S-phase kinase associated protein 2 (Skp2), a member of the F-box family of proteins that associates with Skp1, Cul-1 and ROC1/Rbx1 to form an SCF ubiquitin ligase complex.
782	2703	associate	Skp2	Skp1	Ubiquitinylation of p27 requires its phosphorylation at Thr 187 and subsequent recognition by S-phase kinase associated protein 2 (Skp2), a member of the F-box family of proteins that associates with Skp1, Cul-1 and ROC1/Rbx1 to form an SCF ubiquitin ligase complex.
783	2704	recognize	Rpn1	Ubp6	Ubp6 recognizes the proteasome base and its subunit Rpn1, suggesting that proteasome binding positions Ubp6 proximally to the substrate translocation channel.
783	2705	recognize	Ubp6	Rpn1	Ubp6 recognizes the proteasome base and its subunit Rpn1, suggesting that proteasome binding positions Ubp6 proximally to the substrate translocation channel.
784	2706	interact	Hsp70	apoB	Under these conditions, apoB is partially translocated, interacts with cytosolic Hsp70, and undergoes rapid degradation.
784	2707	interact	apoB	Hsp70	Under these conditions, apoB is partially translocated, interacts with cytosolic Hsp70, and undergoes rapid degradation.
785	2708	activation	NF-kappaB	c-Src	Underscoring the physiological significance of c-Src activation of NF-kappaB, TNF induction of IL-6, which is an NF-kappaB mediated event, is substantially diminished in c-src-/- BMMs.
785	2709	activation	c-Src	NF-kappaB	Underscoring the physiological significance of c-Src activation of NF-kappaB, TNF induction of IL-6, which is an NF-kappaB mediated event, is substantially diminished in c-src-/- BMMs.
786	2710	activation	CNF1	Rho GTPases	Unexpectedly, we measured in bladder cells a transient CNF1-induced activation of Rho GTPases, maximal for Rac.
786	2711	activation	Rho GTPases	CNF1	Unexpectedly, we measured in bladder cells a transient CNF1-induced activation of Rho GTPases, maximal for Rac.
787	2712	modification	IkappaBalpha	SUMO-1	Unlike ubiquitin modification, which requires phosphorylation of S32 and S36, SUMO-1 modification of IkappaBalpha is inhibited by phosphorylation.
787	2713	modification	SUMO-1	IkappaBalpha	Unlike ubiquitin modification, which requires phosphorylation of S32 and S36, SUMO-1 modification of IkappaBalpha is inhibited by phosphorylation.
788	2714	complex	Bub3	BubR1	Upon checkpoint activation, the BubR1-Bub3 complex interacts with Cdc20.
788	2715	interact	Bub3	Cdc20	Upon checkpoint activation, the BubR1-Bub3 complex interacts with Cdc20.
788	2716	complex	BubR1	Bub3	Upon checkpoint activation, the BubR1-Bub3 complex interacts with Cdc20.
788	2717	interact	BubR1	Cdc20	Upon checkpoint activation, the BubR1-Bub3 complex interacts with Cdc20.
788	2718	interact	Cdc20	Bub3	Upon checkpoint activation, the BubR1-Bub3 complex interacts with Cdc20.
788	2719	interact	Cdc20	BubR1	Upon checkpoint activation, the BubR1-Bub3 complex interacts with Cdc20.
789	2720	bind	mDac	mUbc9	Using a yeast two hybrid system and pull-down assays we demonstrate that mouse Dac (mDac) specifically binds to mouse ubiquitin-conjugating enzyme mUbc9.
789	2721	bind	mUbc9	mDac	Using a yeast two hybrid system and pull-down assays we demonstrate that mouse Dac (mDac) specifically binds to mouse ubiquitin-conjugating enzyme mUbc9.
790	2722	modification	Cul-1	NEDD8	Using an in vitro reconstituted system, we report here that NEDD8 modification of Cul-1 enhances recruitment of Ub-conjugating enzyme Ubc4 (E2) to the SCF complex (E3).
790	2723	modification	NEDD8	Cul-1	Using an in vitro reconstituted system, we report here that NEDD8 modification of Cul-1 enhances recruitment of Ub-conjugating enzyme Ubc4 (E2) to the SCF complex (E3).
790	2724	recruitment	SCF	Ubc4	Using an in vitro reconstituted system, we report here that NEDD8 modification of Cul-1 enhances recruitment of Ub-conjugating enzyme Ubc4 (E2) to the SCF complex (E3).
790	2725	recruitment	Ubc4	SCF	Using an in vitro reconstituted system, we report here that NEDD8 modification of Cul-1 enhances recruitment of Ub-conjugating enzyme Ubc4 (E2) to the SCF complex (E3).
791	2726	transfer	UbcH4	ubiquitin	Using an in vitro reconstitution, specific E2 (ubiquitin-conjugating) enzymes (human UbcH4, UbcH5B, and UbcH5C) transferred ubiquitin molecules to hHYD, leading to the ubiquitination of TopBP1.
791	2727	transfer	UbcH5B	ubiquitin	Using an in vitro reconstitution, specific E2 (ubiquitin-conjugating) enzymes (human UbcH4, UbcH5B, and UbcH5C) transferred ubiquitin molecules to hHYD, leading to the ubiquitination of TopBP1.
791	2728	transfer	UbcH5C	ubiquitin	Using an in vitro reconstitution, specific E2 (ubiquitin-conjugating) enzymes (human UbcH4, UbcH5B, and UbcH5C) transferred ubiquitin molecules to hHYD, leading to the ubiquitination of TopBP1.
791	2729	transfer	hHYD	ubiquitin	Using an in vitro reconstitution, specific E2 (ubiquitin-conjugating) enzymes (human UbcH4, UbcH5B, and UbcH5C) transferred ubiquitin molecules to hHYD, leading to the ubiquitination of TopBP1.
791	2730	transfer	ubiquitin	UbcH4	Using an in vitro reconstitution, specific E2 (ubiquitin-conjugating) enzymes (human UbcH4, UbcH5B, and UbcH5C) transferred ubiquitin molecules to hHYD, leading to the ubiquitination of TopBP1.
791	2731	transfer	ubiquitin	UbcH5B	Using an in vitro reconstitution, specific E2 (ubiquitin-conjugating) enzymes (human UbcH4, UbcH5B, and UbcH5C) transferred ubiquitin molecules to hHYD, leading to the ubiquitination of TopBP1.
791	2732	transfer	ubiquitin	UbcH5C	Using an in vitro reconstitution, specific E2 (ubiquitin-conjugating) enzymes (human UbcH4, UbcH5B, and UbcH5C) transferred ubiquitin molecules to hHYD, leading to the ubiquitination of TopBP1.
791	2733	transfer	ubiquitin	hHYD	Using an in vitro reconstitution, specific E2 (ubiquitin-conjugating) enzymes (human UbcH4, UbcH5B, and UbcH5C) transferred ubiquitin molecules to hHYD, leading to the ubiquitination of TopBP1.
792	2734	associate	RanBP2	Ubc9p	Using antibodies directed against Xenopus Ubc9p, we have confirmed that Ubc9p associates with p340(RanBP2) in Xenopus extracts.
792	2735	associate	Ubc9p	RanBP2	Using antibodies directed against Xenopus Ubc9p, we have confirmed that Ubc9p associates with p340(RanBP2) in Xenopus extracts.
792	2736	associate	Ubc9p	p340	Using antibodies directed against Xenopus Ubc9p, we have confirmed that Ubc9p associates with p340(RanBP2) in Xenopus extracts.
792	2737	associate	p340	Ubc9p	Using antibodies directed against Xenopus Ubc9p, we have confirmed that Ubc9p associates with p340(RanBP2) in Xenopus extracts.
793	2738	interact	Mdm2	p19(ARF)	Using bacterially produced ARF polypeptides and chemically synthesized peptides conjugated to Sepharose, residues 1 to 14 and 26 to 37 of mouse p19(ARF) were found to interact independently and cooperatively with Mdm2, while residues 15 to 25 were dispensable for binding.
793	2739	interact	p19(ARF)	Mdm2	Using bacterially produced ARF polypeptides and chemically synthesized peptides conjugated to Sepharose, residues 1 to 14 and 26 to 37 of mouse p19(ARF) were found to interact independently and cooperatively with Mdm2, while residues 15 to 25 were dispensable for binding.
794	2740	bound	E6	p53	Using glutathione S-transferase (GST) fusion proteins, we found that HPV E6 bound human p53 and that the relative efficiency of binding varied such that the GST-HPV type 16 E6 (16E6) protein bound p53 with highest affinity, followed by GST-31E6, GST-18E6, and GST-11E6.
794	2741	bound	p53	E6	Using glutathione S-transferase (GST) fusion proteins, we found that HPV E6 bound human p53 and that the relative efficiency of binding varied such that the GST-HPV type 16 E6 (16E6) protein bound p53 with highest affinity, followed by GST-31E6, GST-18E6, and GST-11E6.
795	2742	ubiquitinate	EGF 	c-Cbl	Using low temperature and a dynamin mutant, we find that c-Cbl associates with and ubiquitinates the activated epidermal growth factor (EGF) receptor at the plasma membrane in the absence of endocytosis.
795	2743	ubiquitinate	c-Cbl	EGF 	Using low temperature and a dynamin mutant, we find that c-Cbl associates with and ubiquitinates the activated epidermal growth factor (EGF) receptor at the plasma membrane in the absence of endocytosis.
796	2744	interact	RAD51	UBE2I	Using the human RAD52 protein as the bait in a yeast two-hybrid system, we have identified a human homolog of yeast UBC9, designated UBE2I, that interacts with RAD52, RAD51, p53, and a ubiquitin-like protein UBL1.
796	2745	interact	RAD52	UBE2I	Using the human RAD52 protein as the bait in a yeast two-hybrid system, we have identified a human homolog of yeast UBC9, designated UBE2I, that interacts with RAD52, RAD51, p53, and a ubiquitin-like protein UBL1.
796	2746	interact	UBE2I	RAD51	Using the human RAD52 protein as the bait in a yeast two-hybrid system, we have identified a human homolog of yeast UBC9, designated UBE2I, that interacts with RAD52, RAD51, p53, and a ubiquitin-like protein UBL1.
796	2747	interact	UBE2I	RAD52	Using the human RAD52 protein as the bait in a yeast two-hybrid system, we have identified a human homolog of yeast UBC9, designated UBE2I, that interacts with RAD52, RAD51, p53, and a ubiquitin-like protein UBL1.
796	2748	interact	UBE2I	UBL1	Using the human RAD52 protein as the bait in a yeast two-hybrid system, we have identified a human homolog of yeast UBC9, designated UBE2I, that interacts with RAD52, RAD51, p53, and a ubiquitin-like protein UBL1.
796	2749	interact	UBE2I	p53	Using the human RAD52 protein as the bait in a yeast two-hybrid system, we have identified a human homolog of yeast UBC9, designated UBE2I, that interacts with RAD52, RAD51, p53, and a ubiquitin-like protein UBL1.
796	2750	interact	UBL1	UBE2I	Using the human RAD52 protein as the bait in a yeast two-hybrid system, we have identified a human homolog of yeast UBC9, designated UBE2I, that interacts with RAD52, RAD51, p53, and a ubiquitin-like protein UBL1.
796	2751	interact	p53	UBE2I	Using the human RAD52 protein as the bait in a yeast two-hybrid system, we have identified a human homolog of yeast UBC9, designated UBE2I, that interacts with RAD52, RAD51, p53, and a ubiquitin-like protein UBL1.
797	2752	bind	USP7	ataxin-1	Using the yeast two-hybrid system, we have found that USP7, a ubiquitin-specific protease, binds to ataxin-1.
797	2753	bind	ataxin-1	USP7	Using the yeast two-hybrid system, we have found that USP7, a ubiquitin-specific protease, binds to ataxin-1.
798	2754	complex	Cks1	Skp2	Using this assay, we have determined the dissociation constant of the Skp2-Cks1 complex (Kd=140+/-14 nM) and have shown that Skp2 binds phosphorylated p27 peptide with high affinity only in the presence of Cks1 (Kd=37+/-2 nM).
798	2755	complex	Skp2	Cks1	Using this assay, we have determined the dissociation constant of the Skp2-Cks1 complex (Kd=140+/-14 nM) and have shown that Skp2 binds phosphorylated p27 peptide with high affinity only in the presence of Cks1 (Kd=37+/-2 nM).
798	2756	bind	Skp2	p27	Using this assay, we have determined the dissociation constant of the Skp2-Cks1 complex (Kd=140+/-14 nM) and have shown that Skp2 binds phosphorylated p27 peptide with high affinity only in the presence of Cks1 (Kd=37+/-2 nM).
798	2757	bind	p27	Skp2	Using this assay, we have determined the dissociation constant of the Skp2-Cks1 complex (Kd=140+/-14 nM) and have shown that Skp2 binds phosphorylated p27 peptide with high affinity only in the presence of Cks1 (Kd=37+/-2 nM).
799	2758	complex	SOCS1	VAV	VAV and SOCS1 form a protein complex through interactions between the VAV NH(2)-terminal regulatory region and the SH2 domain of SOCS1 in a phosphotyrosine-independent manner.
799	2759	complex	VAV	SOCS1	VAV and SOCS1 form a protein complex through interactions between the VAV NH(2)-terminal regulatory region and the SH2 domain of SOCS1 in a phosphotyrosine-independent manner.
800	2760	binding	alphaENaC	hNedd4	WW domain 3 (but not the other WW domains) was both necessary and sufficient for the binding of hNedd4 to alphaENaC.
800	2761	binding	hNedd4	alphaENaC	WW domain 3 (but not the other WW domains) was both necessary and sufficient for the binding of hNedd4 to alphaENaC.
801	2762	interaction	Slmb	UbcD1	We also describe the direct interaction of the UbcH5 related protein UbcD1 with dCul1 and Slmb.
801	2763	interaction	UbcD1	Slmb	We also describe the direct interaction of the UbcH5 related protein UbcD1 with dCul1 and Slmb.
801	2764	interaction	UbcD1	dCul1	We also describe the direct interaction of the UbcH5 related protein UbcD1 with dCul1 and Slmb.
801	2765	interaction	dCul1	UbcD1	We also describe the direct interaction of the UbcH5 related protein UbcD1 with dCul1 and Slmb.
802	2766	associate	p100	pVHL	We also found that pVHL associates with two proteins, p100 and p220, which migrate at a similar molecular weight as two major bands in the ubiquitination assay.
802	2767	associate	p220	pVHL	We also found that pVHL associates with two proteins, p100 and p220, which migrate at a similar molecular weight as two major bands in the ubiquitination assay.
802	2768	associate	pVHL	p100	We also found that pVHL associates with two proteins, p100 and p220, which migrate at a similar molecular weight as two major bands in the ubiquitination assay.
802	2769	associate	pVHL	p220	We also found that pVHL associates with two proteins, p100 and p220, which migrate at a similar molecular weight as two major bands in the ubiquitination assay.
803	2770	associate	Mad2	p55Cdc	We also show that Mad2 associates with the APC regulatory protein p55Cdc in mammalian cells as has been reported in yeast.
803	2771	associate	p55Cdc	Mad2	We also show that Mad2 associates with the APC regulatory protein p55Cdc in mammalian cells as has been reported in yeast.
804	2772	interact	UFD2a	VCP	We also show that UFD2a interacts with VCP (a AAA-family ATPase) that is thought to mediate protein folding.
804	2773	interact	VCP	UFD2a	We also show that UFD2a interacts with VCP (a AAA-family ATPase) that is thought to mediate protein folding.
805	2774	transfer	E2-25K	Nedd8	We also show that recombinant human NEDD8 protein is activated, albeit inefficiently, by the ubiquitin-activating (E1) enzyme and that NEDD8 can be transferred from E1 to the ubiquitin conjugating enzyme E2-25K.
805	2775	transfer	Nedd8	E2-25K	We also show that recombinant human NEDD8 protein is activated, albeit inefficiently, by the ubiquitin-activating (E1) enzyme and that NEDD8 can be transferred from E1 to the ubiquitin conjugating enzyme E2-25K.
806	2776	interact	Ede1	Ent1	We also show that the Ent1 ENTH domain binds to phosphoinositides in vitro, and that Ent1 NPF motifs interact with the EH-domain containing proteins Ede1 and Pan1.
806	2777	interact	Ent1	Ede1	We also show that the Ent1 ENTH domain binds to phosphoinositides in vitro, and that Ent1 NPF motifs interact with the EH-domain containing proteins Ede1 and Pan1.
806	2778	interact	Ent1	Pan1	We also show that the Ent1 ENTH domain binds to phosphoinositides in vitro, and that Ent1 NPF motifs interact with the EH-domain containing proteins Ede1 and Pan1.
806	2779	interact	Pan1	Ent1	We also show that the Ent1 ENTH domain binds to phosphoinositides in vitro, and that Ent1 NPF motifs interact with the EH-domain containing proteins Ede1 and Pan1.
807	2780	linked	influenza NP	ubiquitin	We also show that the effect of lactacystin on antigen presentation correlates with the block of breakdown of a rapidly degraded form of the influenza NP linked to ubiquitin.
807	2781	linked	ubiquitin	influenza NP	We also show that the effect of lactacystin on antigen presentation correlates with the block of breakdown of a rapidly degraded form of the influenza NP linked to ubiquitin.
808	2782	modified	AML1	SUMO-1	We also show that the leukemia-associated fusion protein TEL/AML1 is modified by SUMO-1 and found in the TEL bodies, in a pattern quite different from what we observe and report for AML1.
808	2783	modified	SUMO-1	AML1	We also show that the leukemia-associated fusion protein TEL/AML1 is modified by SUMO-1 and found in the TEL bodies, in a pattern quite different from what we observe and report for AML1.
808	2784	modified	SUMO-1	TEL	We also show that the leukemia-associated fusion protein TEL/AML1 is modified by SUMO-1 and found in the TEL bodies, in a pattern quite different from what we observe and report for AML1.
808	2785	modified	TEL	SUMO-1	We also show that the leukemia-associated fusion protein TEL/AML1 is modified by SUMO-1 and found in the TEL bodies, in a pattern quite different from what we observe and report for AML1.
809	2786	interact	GLD-1	fog-2	We cloned fog-2 by finding that its gene product physically interacts with GLD-1, forming a FOG-2/GLD-1/tra-2 3'untranslated region ternary complex.
809	2787	interact	fog-2	GLD-1	We cloned fog-2 by finding that its gene product physically interacts with GLD-1, forming a FOG-2/GLD-1/tra-2 3'untranslated region ternary complex.
810	2788	activate	MAP3Ks	NF-kappaB	We conclude that a distinct subset of MAP3Ks can activate NF-kappaB.
810	2789	activate	NF-kappaB	MAP3Ks	We conclude that a distinct subset of MAP3Ks can activate NF-kappaB.
811	2790	associate	UNP	p107	We conclude that within cells UNP does physically associate with pRb, and can also associate with p107 and p130.
811	2791	associate	UNP	p130	We conclude that within cells UNP does physically associate with pRb, and can also associate with p107 and p130.
811	2792	associate	UNP	pRb	We conclude that within cells UNP does physically associate with pRb, and can also associate with p107 and p130.
811	2793	associate	p107	UNP	We conclude that within cells UNP does physically associate with pRb, and can also associate with p107 and p130.
811	2794	associate	p130	UNP	We conclude that within cells UNP does physically associate with pRb, and can also associate with p107 and p130.
811	2795	associate	pRb	UNP	We conclude that within cells UNP does physically associate with pRb, and can also associate with p107 and p130.
812	2796	interaction	Hsa-AIP4	Hsa-CBLC	We confirmed the interaction between Hsa-CBLC and Hsa-AIP4 by a combination of glutathione S-transferase pull-down, co-immunoprecipitation, and colocalization experiments.
812	2797	interaction	Hsa-CBLC	Hsa-AIP4	We confirmed the interaction between Hsa-CBLC and Hsa-AIP4 by a combination of glutathione S-transferase pull-down, co-immunoprecipitation, and colocalization experiments.
813	2798	interact	UbcH7	c-Cbl	We demonstrate here, using the yeast two-hybrid system and an in vitro binding assay, that the c-Cbl RING finger domain interacts with UbcH7, a ubiquitin-conjugating enzyme (E2).
813	2799	interact	c-Cbl	UbcH7	We demonstrate here, using the yeast two-hybrid system and an in vitro binding assay, that the c-Cbl RING finger domain interacts with UbcH7, a ubiquitin-conjugating enzyme (E2).
814	2800	associate	SCF beta-TRCP	Ubc3	We demonstrate specific ubiquitination of I kappa B alpha by Ubc3 and Ubc4 in a phosphorylation and SCF beta-TRCP dependent manner and that both are capable of associating with the SCF beta-TRCP complex isolated from human cells.
814	2801	associate	SCF beta-TRCP	Ubc4	We demonstrate specific ubiquitination of I kappa B alpha by Ubc3 and Ubc4 in a phosphorylation and SCF beta-TRCP dependent manner and that both are capable of associating with the SCF beta-TRCP complex isolated from human cells.
814	2802	associate	Ubc3	SCF beta-TRCP	We demonstrate specific ubiquitination of I kappa B alpha by Ubc3 and Ubc4 in a phosphorylation and SCF beta-TRCP dependent manner and that both are capable of associating with the SCF beta-TRCP complex isolated from human cells.
814	2803	associate	Ubc4	SCF beta-TRCP	We demonstrate specific ubiquitination of I kappa B alpha by Ubc3 and Ubc4 in a phosphorylation and SCF beta-TRCP dependent manner and that both are capable of associating with the SCF beta-TRCP complex isolated from human cells.
815	2804	bind	ENaC	KIAA0439	We demonstrate that KIAA0439 WW domains bind all three ENaC subunits.
815	2805	bind	KIAA0439	ENaC	We demonstrate that KIAA0439 WW domains bind all three ENaC subunits.
816	2806	interact	Cdc35p	Sgt1p	We demonstrate that Sgt1p and Cyrlp/Cdc35p physically interact and that the activity of the cAMP pathway is affected in an sgt1 conditional mutant.
816	2807	interact	Cyrlp	Sgt1p	We demonstrate that Sgt1p and Cyrlp/Cdc35p physically interact and that the activity of the cAMP pathway is affected in an sgt1 conditional mutant.
816	2808	interact	Sgt1p	Cdc35p	We demonstrate that Sgt1p and Cyrlp/Cdc35p physically interact and that the activity of the cAMP pathway is affected in an sgt1 conditional mutant.
816	2809	interact	Sgt1p	Cyrlp	We demonstrate that Sgt1p and Cyrlp/Cdc35p physically interact and that the activity of the cAMP pathway is affected in an sgt1 conditional mutant.
817	2810	conjugation	Ttk69	dSmt3	We demonstrate that Tramtrack 69 (Ttk69), a repressor of neuronal differentiation, is a bona fide in vivo substrate for dSmt3 conjugation.
817	2811	conjugation	dSmt3	Ttk69	We demonstrate that Tramtrack 69 (Ttk69), a repressor of neuronal differentiation, is a bona fide in vivo substrate for dSmt3 conjugation.
818	2812	complexed	IkappaB alpha	c-Rel	We demonstrate that all IkappaB alpha is found complexed with c-Rel protein in the cytoplasm.
818	2813	complexed	c-Rel	IkappaB alpha	We demonstrate that all IkappaB alpha is found complexed with c-Rel protein in the cytoplasm.
819	2814	interact	IkappaBbeta	beta-TrCP	We demonstrate that beta-TrCP interacts specifically with IkappaBbeta, and such interaction is dependent on prior phosphorylation of IkappaBbeta on serines 19 and 23.
819	2815	interact	beta-TrCP	IkappaBbeta	We demonstrate that beta-TrCP interacts specifically with IkappaBbeta, and such interaction is dependent on prior phosphorylation of IkappaBbeta on serines 19 and 23.
820	2816	modification	Ned8p	Pcu3p	We demonstrate that multiple CSN subunits control Ned8p modification of Pcu3p, another fission yeast cullin, which, in complex with the RING domain protein Pip1p, forms a ubiquitin ligase that functions in cellular stress response.
820	2817	modification	Pcu3p	Ned8p	We demonstrate that multiple CSN subunits control Ned8p modification of Pcu3p, another fission yeast cullin, which, in complex with the RING domain protein Pip1p, forms a ubiquitin ligase that functions in cellular stress response.
820	2818	complex	Pcu3p	Pip1p	We demonstrate that multiple CSN subunits control Ned8p modification of Pcu3p, another fission yeast cullin, which, in complex with the RING domain protein Pip1p, forms a ubiquitin ligase that functions in cellular stress response.
820	2819	complex	Pip1p	Pcu3p	We demonstrate that multiple CSN subunits control Ned8p modification of Pcu3p, another fission yeast cullin, which, in complex with the RING domain protein Pip1p, forms a ubiquitin ligase that functions in cellular stress response.
821	2820	modification	DmSmt3	septins	We did not observe any concentration of DmUba2 at sites where the septins are concentrated, and we could not detect DmSmt3 modification of the three Drosophila septins tested.
821	2821	modification	septins	DmSmt3	We did not observe any concentration of DmUba2 at sites where the septins are concentrated, and we could not detect DmSmt3 modification of the three Drosophila septins tested.
822	2822	targets	Cln1	Grr1	We discovered that Grr1 physically interacts with Skp1, a protein that has been implicated in a ubiquitin-conjugating enzyme complex that targets for degradation the cell cycle regulators Cln1 and Cln2, and the cyclin-dependent kinase inhibitor Sic1.
822	2823	targets	Cln2	Grr1	We discovered that Grr1 physically interacts with Skp1, a protein that has been implicated in a ubiquitin-conjugating enzyme complex that targets for degradation the cell cycle regulators Cln1 and Cln2, and the cyclin-dependent kinase inhibitor Sic1.
822	2824	targets	Grr1	Cln1	We discovered that Grr1 physically interacts with Skp1, a protein that has been implicated in a ubiquitin-conjugating enzyme complex that targets for degradation the cell cycle regulators Cln1 and Cln2, and the cyclin-dependent kinase inhibitor Sic1.
822	2825	targets	Grr1	Cln2	We discovered that Grr1 physically interacts with Skp1, a protein that has been implicated in a ubiquitin-conjugating enzyme complex that targets for degradation the cell cycle regulators Cln1 and Cln2, and the cyclin-dependent kinase inhibitor Sic1.
822	2826	targets	Grr1	Sic1	We discovered that Grr1 physically interacts with Skp1, a protein that has been implicated in a ubiquitin-conjugating enzyme complex that targets for degradation the cell cycle regulators Cln1 and Cln2, and the cyclin-dependent kinase inhibitor Sic1.
822	2827	interact	Grr1	Skp1	We discovered that Grr1 physically interacts with Skp1, a protein that has been implicated in a ubiquitin-conjugating enzyme complex that targets for degradation the cell cycle regulators Cln1 and Cln2, and the cyclin-dependent kinase inhibitor Sic1.
822	2828	targets	Sic1	Grr1	We discovered that Grr1 physically interacts with Skp1, a protein that has been implicated in a ubiquitin-conjugating enzyme complex that targets for degradation the cell cycle regulators Cln1 and Cln2, and the cyclin-dependent kinase inhibitor Sic1.
822	2829	interact	Skp1	Grr1	We discovered that Grr1 physically interacts with Skp1, a protein that has been implicated in a ubiquitin-conjugating enzyme complex that targets for degradation the cell cycle regulators Cln1 and Cln2, and the cyclin-dependent kinase inhibitor Sic1.
823	2830	function	Bul1	Rsp5	We discuss the possibility that Bul1 functions together with Rsp5 in protein ubiquitination.
823	2831	function	Rsp5	Bul1	We discuss the possibility that Bul1 functions together with Rsp5 in protein ubiquitination.
824	2832	interaction	Ubc2p	Ubr1p	We dissected physical and functional interactions between the ubiquitin-conjugating (E2) enzyme Ubc2p and Ubr1p, the E3 component of the N-end rule pathway in Saccharomyces cerevisiae.
824	2833	interaction	Ubr1p	Ubc2p	We dissected physical and functional interactions between the ubiquitin-conjugating (E2) enzyme Ubc2p and Ubr1p, the E3 component of the N-end rule pathway in Saccharomyces cerevisiae.
825	2834	bound	APC/C	Cdc20	We do not know what determines the release of Cdc14 and enables it to promote Cdk1 inactivation, but it is known to be dependent on APC/C bound by Cdc20 (APC(Cdc20)).
825	2835	bound	Cdc20	APC/C	We do not know what determines the release of Cdc14 and enables it to promote Cdk1 inactivation, but it is known to be dependent on APC/C bound by Cdc20 (APC(Cdc20)).
826	2836	association	PHF-tau	p62	We examined the immunoreactivity of ubiquitin-binding protein p62 and its association with ubiquitin (Ub), alpha-synuclein, and paired helical filament (PHF)-tau in the affected brain areas of human tauopathies and synucleinopathies.
826	2837	association	alpha-synuclein	p62	We examined the immunoreactivity of ubiquitin-binding protein p62 and its association with ubiquitin (Ub), alpha-synuclein, and paired helical filament (PHF)-tau in the affected brain areas of human tauopathies and synucleinopathies.
826	2838	association	p62	PHF-tau	We examined the immunoreactivity of ubiquitin-binding protein p62 and its association with ubiquitin (Ub), alpha-synuclein, and paired helical filament (PHF)-tau in the affected brain areas of human tauopathies and synucleinopathies.
826	2839	association	p62	alpha-synuclein	We examined the immunoreactivity of ubiquitin-binding protein p62 and its association with ubiquitin (Ub), alpha-synuclein, and paired helical filament (PHF)-tau in the affected brain areas of human tauopathies and synucleinopathies.
826	2840	association	p62	ubiquitin	We examined the immunoreactivity of ubiquitin-binding protein p62 and its association with ubiquitin (Ub), alpha-synuclein, and paired helical filament (PHF)-tau in the affected brain areas of human tauopathies and synucleinopathies.
826	2841	association	ubiquitin	p62	We examined the immunoreactivity of ubiquitin-binding protein p62 and its association with ubiquitin (Ub), alpha-synuclein, and paired helical filament (PHF)-tau in the affected brain areas of human tauopathies and synucleinopathies.
827	2842	associate	Skp2	cyclin D3	We extend this observation and show that cyclin D3 can also associate with Skp2 suggesting that cyclins D1, D3 and p21 may share the same SCF complex.
827	2843	associate	cyclin D3	Skp2	We extend this observation and show that cyclin D3 can also associate with Skp2 suggesting that cyclins D1, D3 and p21 may share the same SCF complex.
828	2844	interact	Cdc53	Skp1	We find that Skp1 interacts with Cdc53 in vivo, and that Skp1 bridges Cdc53 to three different F-box proteins, Cdc4, Met30, and Grr1.
828	2845	interact	Skp1	Cdc53	We find that Skp1 interacts with Cdc53 in vivo, and that Skp1 bridges Cdc53 to three different F-box proteins, Cdc4, Met30, and Grr1.
829	2846	interact	Notch 1	mSel-10	We find that mSel-10 localizes to the cell nucleus, and that it physically interacts with the Notch 1 intracellular domain (IC) and reduces Notch 1 IC-mediated activation of the HES 1 promoter.
829	2847	interact	mSel-10	Notch 1	We find that mSel-10 localizes to the cell nucleus, and that it physically interacts with the Notch 1 intracellular domain (IC) and reduces Notch 1 IC-mediated activation of the HES 1 promoter.
830	2848	conjugated	H2A	ubiquitin	We find that newly synthesized H2A is rapidly conjugated to ubiquitin.
830	2849	conjugated	ubiquitin	H2A	We find that newly synthesized H2A is rapidly conjugated to ubiquitin.
831	2850	phosphorylation	ApC	MAP kinase	We find that phosphorylation of ApC/EBP by mitogen-activated protein (MAP) kinase is essential for binding.
831	2851	phosphorylation	EBP	MAP kinase	We find that phosphorylation of ApC/EBP by mitogen-activated protein (MAP) kinase is essential for binding.
831	2852	phosphorylation	MAP kinase	ApC	We find that phosphorylation of ApC/EBP by mitogen-activated protein (MAP) kinase is essential for binding.
831	2853	phosphorylation	MAP kinase	EBP	We find that phosphorylation of ApC/EBP by mitogen-activated protein (MAP) kinase is essential for binding.
832	2854	phosphorylate	IKK	TAK1	We find that the TAK1 kinase complex phosphorylates and activates IKK in a manner that depends on TRAF6 and Ubc13-Uev1A.
832	2855	phosphorylate	TAK1	IKK	We find that the TAK1 kinase complex phosphorylates and activates IKK in a manner that depends on TRAF6 and Ubc13-Uev1A.
833	2856	modify	Cul1	Nedd8	We found that Nedd8 modifies Cul1 in Drosophila.
833	2857	modify	Nedd8	Cul1	We found that Nedd8 modifies Cul1 in Drosophila.
834	2858	complex	Cdk2	cyclin A	We found that Skp2 can inhibit the kinase activity of cyclin A-Cdk2 in vitro, both by direct inhibition of cyclin A-Cdk2 and by inhibition of the activation of Cdk2 by cyclin-dependent kinase (CDK)-activating kinase phosphorylation.
834	2859	inhibit	Rad24	Skp2	We found that Skp2 can inhibit the kinase activity of cyclin A-Cdk2 in vitro, both by direct inhibition of cyclin A-Cdk2 and by inhibition of the activation of Cdk2 by cyclin-dependent kinase (CDK)-activating kinase phosphorylation.
834	2860	inhibit	Skp2	Rad24	We found that Skp2 can inhibit the kinase activity of cyclin A-Cdk2 in vitro, both by direct inhibition of cyclin A-Cdk2 and by inhibition of the activation of Cdk2 by cyclin-dependent kinase (CDK)-activating kinase phosphorylation.
834	2861	complex	cyclin A	Cdk2	We found that Skp2 can inhibit the kinase activity of cyclin A-Cdk2 in vitro, both by direct inhibition of cyclin A-Cdk2 and by inhibition of the activation of Cdk2 by cyclin-dependent kinase (CDK)-activating kinase phosphorylation.
835	2862	interact	Srp1p	Sts1p	We found that Sts1p interacts directly with Srp1p in vitro and also in vivo, as judged by coimmunoprecipitation and two-hybrid analyses.
835	2863	interact	Sts1p	Srp1p	We found that Sts1p interacts directly with Srp1p in vitro and also in vivo, as judged by coimmunoprecipitation and two-hybrid analyses.
836	2864	conjugated	CaMKII	DmSUMO-1	We found that at least one isoform of Drosophila neuronal CaMKII is conjugated to DmSUMO-1 in vivo.
836	2865	conjugated	DmSUMO-1	CaMKII	We found that at least one isoform of Drosophila neuronal CaMKII is conjugated to DmSUMO-1 in vivo.
837	2866	interact	Apc11p	Ubc4	We found that the integrity of the Apc11p RING-H2 finger was essential for budding yeast cell viability, Using purified, recombinant proteins we showed that Apc11p interacted directly with the Ubc4 ubiquitin conjugating enzyme (E2).
837	2867	interact	Ubc4	Apc11p	We found that the integrity of the Apc11p RING-H2 finger was essential for budding yeast cell viability, Using purified, recombinant proteins we showed that Apc11p interacted directly with the Ubc4 ubiquitin conjugating enzyme (E2).
838	2868	bind	APC10	APC3	We further provide biochemical evidence that the C-terminus of APC10 binds to CDC27/APC3, an APC subunit that contains multiple tetratrico peptide repeats.
838	2869	bind	APC10	CDC27	We further provide biochemical evidence that the C-terminus of APC10 binds to CDC27/APC3, an APC subunit that contains multiple tetratrico peptide repeats.
838	2870	bind	APC3	APC10	We further provide biochemical evidence that the C-terminus of APC10 binds to CDC27/APC3, an APC subunit that contains multiple tetratrico peptide repeats.
838	2871	bind	CDC27	APC10	We further provide biochemical evidence that the C-terminus of APC10 binds to CDC27/APC3, an APC subunit that contains multiple tetratrico peptide repeats.
839	2872	modify	RanGAP1	sentrin-1	We further showed that both sentrin-1 and sentrin-2 could covalently modify RanGAP1, a Ran GTPase-activating protein critically involved in nuclear transport.
839	2873	modify	RanGAP1	sentrin-2	We further showed that both sentrin-1 and sentrin-2 could covalently modify RanGAP1, a Ran GTPase-activating protein critically involved in nuclear transport.
839	2874	modify	sentrin-1	RanGAP1	We further showed that both sentrin-1 and sentrin-2 could covalently modify RanGAP1, a Ran GTPase-activating protein critically involved in nuclear transport.
839	2875	modify	sentrin-2	RanGAP1	We further showed that both sentrin-1 and sentrin-2 could covalently modify RanGAP1, a Ran GTPase-activating protein critically involved in nuclear transport.
840	2876	interact	Cdc5p	Dbf4p	We had previously shown that Dbf4p interacts with the M phase polo-like kinase Cdc5p, a key regulator of the APC late in mitosis.
840	2877	interact	Dbf4p	Cdc5p	We had previously shown that Dbf4p interacts with the M phase polo-like kinase Cdc5p, a key regulator of the APC late in mitosis.
841	2878	binding	S5a	SUMO-1	We have also compared the S5a binding properties of ubiquitin, SUMO-1, and the ubl domains of hPLIC-2 and hHR23a and have identified the residues on their respective S5a contact surfaces.
841	2879	binding	S5a	hHR23a	We have also compared the S5a binding properties of ubiquitin, SUMO-1, and the ubl domains of hPLIC-2 and hHR23a and have identified the residues on their respective S5a contact surfaces.
841	2880	binding	S5a	hPLIC-2	We have also compared the S5a binding properties of ubiquitin, SUMO-1, and the ubl domains of hPLIC-2 and hHR23a and have identified the residues on their respective S5a contact surfaces.
841	2881	binding	S5a	ubiquitin	We have also compared the S5a binding properties of ubiquitin, SUMO-1, and the ubl domains of hPLIC-2 and hHR23a and have identified the residues on their respective S5a contact surfaces.
841	2882	binding	SUMO-1	S5a	We have also compared the S5a binding properties of ubiquitin, SUMO-1, and the ubl domains of hPLIC-2 and hHR23a and have identified the residues on their respective S5a contact surfaces.
841	2883	binding	hHR23a	S5a	We have also compared the S5a binding properties of ubiquitin, SUMO-1, and the ubl domains of hPLIC-2 and hHR23a and have identified the residues on their respective S5a contact surfaces.
841	2884	binding	hPLIC-2	S5a	We have also compared the S5a binding properties of ubiquitin, SUMO-1, and the ubl domains of hPLIC-2 and hHR23a and have identified the residues on their respective S5a contact surfaces.
841	2885	binding	ubiquitin	S5a	We have also compared the S5a binding properties of ubiquitin, SUMO-1, and the ubl domains of hPLIC-2 and hHR23a and have identified the residues on their respective S5a contact surfaces.
842	2886	bind	Nup153	SENP2	We have also shown that SENP2 binds to Nup153, a nucleoporin that is localized to the nucleoplasmic face of the pore.
842	2887	bind	SENP2	Nup153	We have also shown that SENP2 binds to Nup153, a nucleoporin that is localized to the nucleoplasmic face of the pore.
843	2888	interaction	VDU1	pVHL	We have determined that the VDU1-interacting region in pVHL is located in its beta-domain, and several naturally occurring mutations located in this domain disrupt the interaction between pVHL and VDU1 protein.
843	2889	interaction	pVHL	VDU1	We have determined that the VDU1-interacting region in pVHL is located in its beta-domain, and several naturally occurring mutations located in this domain disrupt the interaction between pVHL and VDU1 protein.
844	2890	interact	26S	Ubc1	We have discovered that E2 proteins, including Ubc1, Ubc2, Ubc4, and Ubc5, can interact with the 26S proteasome.
844	2891	interact	26S	Ubc2	We have discovered that E2 proteins, including Ubc1, Ubc2, Ubc4, and Ubc5, can interact with the 26S proteasome.
844	2892	interact	26S	Ubc4	We have discovered that E2 proteins, including Ubc1, Ubc2, Ubc4, and Ubc5, can interact with the 26S proteasome.
844	2893	interact	26S	Ubc5	We have discovered that E2 proteins, including Ubc1, Ubc2, Ubc4, and Ubc5, can interact with the 26S proteasome.
844	2894	interact	Ubc1	26S	We have discovered that E2 proteins, including Ubc1, Ubc2, Ubc4, and Ubc5, can interact with the 26S proteasome.
844	2895	interact	Ubc2	26S	We have discovered that E2 proteins, including Ubc1, Ubc2, Ubc4, and Ubc5, can interact with the 26S proteasome.
844	2896	interact	Ubc4	26S	We have discovered that E2 proteins, including Ubc1, Ubc2, Ubc4, and Ubc5, can interact with the 26S proteasome.
844	2897	interact	Ubc5	26S	We have discovered that E2 proteins, including Ubc1, Ubc2, Ubc4, and Ubc5, can interact with the 26S proteasome.
845	2898	phosphorylate	IKK	IkappaB	We have examined the possibility that IKK can phosphorylate the p65 NF-kappaB subunit as well as IkappaB in the cytokine-induced NF-kappaB activation.
845	2899	phosphorylate	IKK	NF-kappaB	We have examined the possibility that IKK can phosphorylate the p65 NF-kappaB subunit as well as IkappaB in the cytokine-induced NF-kappaB activation.
845	2900	phosphorylate	IkappaB	IKK	We have examined the possibility that IKK can phosphorylate the p65 NF-kappaB subunit as well as IkappaB in the cytokine-induced NF-kappaB activation.
845	2901	phosphorylate	NF-kappaB	IKK	We have examined the possibility that IKK can phosphorylate the p65 NF-kappaB subunit as well as IkappaB in the cytokine-induced NF-kappaB activation.
846	2902	interact	KIAA0439	alpha-ENaC	We have found that KIAA0439 is expressed in mouse mandibular ducts and interacts with the PY motifs of the alpha-, beta-, and gamma-subunits of ENaC in vitro.
846	2903	interact	KIAA0439	beta-ENaC	We have found that KIAA0439 is expressed in mouse mandibular ducts and interacts with the PY motifs of the alpha-, beta-, and gamma-subunits of ENaC in vitro.
846	2904	interact	KIAA0439	gamma-ENaC	We have found that KIAA0439 is expressed in mouse mandibular ducts and interacts with the PY motifs of the alpha-, beta-, and gamma-subunits of ENaC in vitro.
846	2905	interact	alpha-ENaC	KIAA0439	We have found that KIAA0439 is expressed in mouse mandibular ducts and interacts with the PY motifs of the alpha-, beta-, and gamma-subunits of ENaC in vitro.
846	2906	interact	beta-ENaC	KIAA0439	We have found that KIAA0439 is expressed in mouse mandibular ducts and interacts with the PY motifs of the alpha-, beta-, and gamma-subunits of ENaC in vitro.
846	2907	interact	gamma-ENaC	KIAA0439	We have found that KIAA0439 is expressed in mouse mandibular ducts and interacts with the PY motifs of the alpha-, beta-, and gamma-subunits of ENaC in vitro.
847	2908	interaction	Cdc34	ubiquitin	We have further demonstrated that separate regions within the human Cdc34 C-terminal tail are responsible for multiubiquitin chain assembly and for physical interactions with the Nedd8-conjugated ROC1-CUL1 to assemble extensive ubiquitin polymers.
847	2909	interaction	ubiquitin	Cdc34	We have further demonstrated that separate regions within the human Cdc34 C-terminal tail are responsible for multiubiquitin chain assembly and for physical interactions with the Nedd8-conjugated ROC1-CUL1 to assemble extensive ubiquitin polymers.
848	2910	complex	Pcu1p	Pip1p	We have identified Psh1p and Pip1p, the fission yeast homologues of human SKP1 and HRT1/RBX1/ROC1, and show that both associate with Pop1p, Pop2p, and Pcu1p into a ~500 kDa SCFPop1p-Pop2p complex, which supports polyubiquitylation of Rum1p.
848	2911	complex	Pcu1p	Pop1p	We have identified Psh1p and Pip1p, the fission yeast homologues of human SKP1 and HRT1/RBX1/ROC1, and show that both associate with Pop1p, Pop2p, and Pcu1p into a ~500 kDa SCFPop1p-Pop2p complex, which supports polyubiquitylation of Rum1p.
848	2912	complex	Pcu1p	Pop2p	We have identified Psh1p and Pip1p, the fission yeast homologues of human SKP1 and HRT1/RBX1/ROC1, and show that both associate with Pop1p, Pop2p, and Pcu1p into a ~500 kDa SCFPop1p-Pop2p complex, which supports polyubiquitylation of Rum1p.
848	2913	complex	Pcu1p	Psh1p	We have identified Psh1p and Pip1p, the fission yeast homologues of human SKP1 and HRT1/RBX1/ROC1, and show that both associate with Pop1p, Pop2p, and Pcu1p into a ~500 kDa SCFPop1p-Pop2p complex, which supports polyubiquitylation of Rum1p.
848	2914	complex	Pip1p	Pcu1p	We have identified Psh1p and Pip1p, the fission yeast homologues of human SKP1 and HRT1/RBX1/ROC1, and show that both associate with Pop1p, Pop2p, and Pcu1p into a ~500 kDa SCFPop1p-Pop2p complex, which supports polyubiquitylation of Rum1p.
848	2915	complex	Pip1p	Pop1p	We have identified Psh1p and Pip1p, the fission yeast homologues of human SKP1 and HRT1/RBX1/ROC1, and show that both associate with Pop1p, Pop2p, and Pcu1p into a ~500 kDa SCFPop1p-Pop2p complex, which supports polyubiquitylation of Rum1p.
848	2916	complex	Pip1p	Pop2p	We have identified Psh1p and Pip1p, the fission yeast homologues of human SKP1 and HRT1/RBX1/ROC1, and show that both associate with Pop1p, Pop2p, and Pcu1p into a ~500 kDa SCFPop1p-Pop2p complex, which supports polyubiquitylation of Rum1p.
848	2917	complex	Pip1p	Psh1p	We have identified Psh1p and Pip1p, the fission yeast homologues of human SKP1 and HRT1/RBX1/ROC1, and show that both associate with Pop1p, Pop2p, and Pcu1p into a ~500 kDa SCFPop1p-Pop2p complex, which supports polyubiquitylation of Rum1p.
848	2918	complex	Pop1p	Pcu1p	We have identified Psh1p and Pip1p, the fission yeast homologues of human SKP1 and HRT1/RBX1/ROC1, and show that both associate with Pop1p, Pop2p, and Pcu1p into a ~500 kDa SCFPop1p-Pop2p complex, which supports polyubiquitylation of Rum1p.
848	2919	complex	Pop1p	Pip1p	We have identified Psh1p and Pip1p, the fission yeast homologues of human SKP1 and HRT1/RBX1/ROC1, and show that both associate with Pop1p, Pop2p, and Pcu1p into a ~500 kDa SCFPop1p-Pop2p complex, which supports polyubiquitylation of Rum1p.
848	2920	complex	Pop1p	Pop2p	We have identified Psh1p and Pip1p, the fission yeast homologues of human SKP1 and HRT1/RBX1/ROC1, and show that both associate with Pop1p, Pop2p, and Pcu1p into a ~500 kDa SCFPop1p-Pop2p complex, which supports polyubiquitylation of Rum1p.
848	2921	complex	Pop1p	Psh1p	We have identified Psh1p and Pip1p, the fission yeast homologues of human SKP1 and HRT1/RBX1/ROC1, and show that both associate with Pop1p, Pop2p, and Pcu1p into a ~500 kDa SCFPop1p-Pop2p complex, which supports polyubiquitylation of Rum1p.
848	2922	complex	Pop2p	Pcu1p	We have identified Psh1p and Pip1p, the fission yeast homologues of human SKP1 and HRT1/RBX1/ROC1, and show that both associate with Pop1p, Pop2p, and Pcu1p into a ~500 kDa SCFPop1p-Pop2p complex, which supports polyubiquitylation of Rum1p.
848	2923	complex	Pop2p	Pip1p	We have identified Psh1p and Pip1p, the fission yeast homologues of human SKP1 and HRT1/RBX1/ROC1, and show that both associate with Pop1p, Pop2p, and Pcu1p into a ~500 kDa SCFPop1p-Pop2p complex, which supports polyubiquitylation of Rum1p.
848	2924	complex	Pop2p	Pop1p	We have identified Psh1p and Pip1p, the fission yeast homologues of human SKP1 and HRT1/RBX1/ROC1, and show that both associate with Pop1p, Pop2p, and Pcu1p into a ~500 kDa SCFPop1p-Pop2p complex, which supports polyubiquitylation of Rum1p.
848	2925	complex	Pop2p	Psh1p	We have identified Psh1p and Pip1p, the fission yeast homologues of human SKP1 and HRT1/RBX1/ROC1, and show that both associate with Pop1p, Pop2p, and Pcu1p into a ~500 kDa SCFPop1p-Pop2p complex, which supports polyubiquitylation of Rum1p.
848	2926	complex	Psh1p	Pcu1p	We have identified Psh1p and Pip1p, the fission yeast homologues of human SKP1 and HRT1/RBX1/ROC1, and show that both associate with Pop1p, Pop2p, and Pcu1p into a ~500 kDa SCFPop1p-Pop2p complex, which supports polyubiquitylation of Rum1p.
848	2927	complex	Psh1p	Pip1p	We have identified Psh1p and Pip1p, the fission yeast homologues of human SKP1 and HRT1/RBX1/ROC1, and show that both associate with Pop1p, Pop2p, and Pcu1p into a ~500 kDa SCFPop1p-Pop2p complex, which supports polyubiquitylation of Rum1p.
848	2928	complex	Psh1p	Pop1p	We have identified Psh1p and Pip1p, the fission yeast homologues of human SKP1 and HRT1/RBX1/ROC1, and show that both associate with Pop1p, Pop2p, and Pcu1p into a ~500 kDa SCFPop1p-Pop2p complex, which supports polyubiquitylation of Rum1p.
848	2929	complex	Psh1p	Pop2p	We have identified Psh1p and Pip1p, the fission yeast homologues of human SKP1 and HRT1/RBX1/ROC1, and show that both associate with Pop1p, Pop2p, and Pcu1p into a ~500 kDa SCFPop1p-Pop2p complex, which supports polyubiquitylation of Rum1p.
849	2930	ubiquitinate	Rpb1	Rsp5	We have previously shown that Rsp5 binds and ubiquitinates the largest subunit of RNA polymerase II, Rpb1, in vitro.
849	2931	ubiquitinate	Rsp5	Rpb1	We have previously shown that Rsp5 binds and ubiquitinates the largest subunit of RNA polymerase II, Rpb1, in vitro.
850	2932	modified	Cul-2	NEDD8	We have previously shown that human cullin-2 (Cul-2) is covalently modified at Lys-689 by NEDD8.
850	2933	modified	NEDD8	Cul-2	We have previously shown that human cullin-2 (Cul-2) is covalently modified at Lys-689 by NEDD8.
851	2934	interact	Mx1	PKM	We have previously shown that the hamster equivalent of HIPK-2 (named PKM) interacts with the interferon-induced antiviral GTPase Mx1 and associates with ND10 in interferon-treated cells.
851	2935	associate	ND10	PKM	We have previously shown that the hamster equivalent of HIPK-2 (named PKM) interacts with the interferon-induced antiviral GTPase Mx1 and associates with ND10 in interferon-treated cells.
851	2936	interact	PKM	Mx1	We have previously shown that the hamster equivalent of HIPK-2 (named PKM) interacts with the interferon-induced antiviral GTPase Mx1 and associates with ND10 in interferon-treated cells.
851	2937	associate	PKM	ND10	We have previously shown that the hamster equivalent of HIPK-2 (named PKM) interacts with the interferon-induced antiviral GTPase Mx1 and associates with ND10 in interferon-treated cells.
852	2938	interaction	ENaC	Nedd4	We have recently identified the ubiquitin-protein ligase Nedd4 as an interacting protein with ENaC and demonstrated that Nedd4 binds by its WW domains to the proline-rich PY motifs of ENaC.
852	2939	interaction	Nedd4	ENaC	We have recently identified the ubiquitin-protein ligase Nedd4 as an interacting protein with ENaC and demonstrated that Nedd4 binds by its WW domains to the proline-rich PY motifs of ENaC.
853	2940	associate	Cul1	Skp2	We have reported previously that the degradation of p27 requires its phosphorylation on Thr-187 and is mediated by Skp2, an F-box protein that associates with Skp1, Cul1, and Roc1/Rbx1 to form the SCF(Skp2) ubiquitin ligase complex.
853	2941	associate	Rbx1	Skp2	We have reported previously that the degradation of p27 requires its phosphorylation on Thr-187 and is mediated by Skp2, an F-box protein that associates with Skp1, Cul1, and Roc1/Rbx1 to form the SCF(Skp2) ubiquitin ligase complex.
853	2942	associate	Roc1	Skp2	We have reported previously that the degradation of p27 requires its phosphorylation on Thr-187 and is mediated by Skp2, an F-box protein that associates with Skp1, Cul1, and Roc1/Rbx1 to form the SCF(Skp2) ubiquitin ligase complex.
853	2943	associate	Skp1	Skp2	We have reported previously that the degradation of p27 requires its phosphorylation on Thr-187 and is mediated by Skp2, an F-box protein that associates with Skp1, Cul1, and Roc1/Rbx1 to form the SCF(Skp2) ubiquitin ligase complex.
853	2944	associate	Skp2	Cul1	We have reported previously that the degradation of p27 requires its phosphorylation on Thr-187 and is mediated by Skp2, an F-box protein that associates with Skp1, Cul1, and Roc1/Rbx1 to form the SCF(Skp2) ubiquitin ligase complex.
853	2945	associate	Skp2	Rbx1	We have reported previously that the degradation of p27 requires its phosphorylation on Thr-187 and is mediated by Skp2, an F-box protein that associates with Skp1, Cul1, and Roc1/Rbx1 to form the SCF(Skp2) ubiquitin ligase complex.
853	2946	associate	Skp2	Roc1	We have reported previously that the degradation of p27 requires its phosphorylation on Thr-187 and is mediated by Skp2, an F-box protein that associates with Skp1, Cul1, and Roc1/Rbx1 to form the SCF(Skp2) ubiquitin ligase complex.
853	2947	associate	Skp2	Skp1	We have reported previously that the degradation of p27 requires its phosphorylation on Thr-187 and is mediated by Skp2, an F-box protein that associates with Skp1, Cul1, and Roc1/Rbx1 to form the SCF(Skp2) ubiquitin ligase complex.
854	2948	interact	E6	E6TP1	We have reported previously that the high-risk human papillomavirus (HPV) E6 oncoprotein interacts with E6TP1, a novel Rap GTPase-activating protein (RapGAP).
854	2949	interact	E6TP1	E6	We have reported previously that the high-risk human papillomavirus (HPV) E6 oncoprotein interacts with E6TP1, a novel Rap GTPase-activating protein (RapGAP).
855	2950	interaction	Fbx4	aB-crystallin	We here describe the interaction of aB-crystallin with Fbx4, an F-box containing protein which is a component of the E3 ubiquitin-ligase SCF (Skp1/Cullin/F-box).
855	2951	interaction	aB-crystallin	Fbx4	We here describe the interaction of aB-crystallin with Fbx4, an F-box containing protein which is a component of the E3 ubiquitin-ligase SCF (Skp1/Cullin/F-box).
856	2952	ubiquitinate	alpha-synuclein	parkin	We hypothesized that these two gene products interact functionally, namely, that parkin ubiquitinates alpha-synuclein normally and that this process is altered in autosomal recessive PD.
856	2953	ubiquitinate	parkin	alpha-synuclein	We hypothesized that these two gene products interact functionally, namely, that parkin ubiquitinates alpha-synuclein normally and that this process is altered in autosomal recessive PD.
857	2954	interaction	PIAS1	Sp3	We identified the protein inhibitor of activated STAT1 (PIAS1) as an interaction partner of Sp3 and Ubc9.
857	2955	interaction	PIAS1	Ubc9	We identified the protein inhibitor of activated STAT1 (PIAS1) as an interaction partner of Sp3 and Ubc9.
857	2956	interaction	Sp3	PIAS1	We identified the protein inhibitor of activated STAT1 (PIAS1) as an interaction partner of Sp3 and Ubc9.
857	2957	interaction	Ubc9	PIAS1	We identified the protein inhibitor of activated STAT1 (PIAS1) as an interaction partner of Sp3 and Ubc9.
858	2958	conjugated	IE72	SUMO-1	We now demonstrate that IE72 is covalently conjugated to the small ubiquitin-like modifier (SUMO-1).
858	2959	conjugated	SUMO-1	IE72	We now demonstrate that IE72 is covalently conjugated to the small ubiquitin-like modifier (SUMO-1).
859	2960	bound	LRP	alpha2M	We now report that ubiquitinylation of the LRP heavy chain occurred when either Pseudomonas exotoxin A or alpha2M bound to LRP on macrophages.
859	2961	bound	LRP	exotoxin A	We now report that ubiquitinylation of the LRP heavy chain occurred when either Pseudomonas exotoxin A or alpha2M bound to LRP on macrophages.
859	2962	bound	alpha2M	LRP	We now report that ubiquitinylation of the LRP heavy chain occurred when either Pseudomonas exotoxin A or alpha2M bound to LRP on macrophages.
859	2963	bound	exotoxin A	LRP	We now report that ubiquitinylation of the LRP heavy chain occurred when either Pseudomonas exotoxin A or alpha2M bound to LRP on macrophages.
860	2964	associates	KK3	MHC class I	We now show that KK3 associates with MHC class I molecules and promotes ubiquitylation of class I after export from the endoplasmic reticulum.
860	2965	associates	MHC class I	KK3	We now show that KK3 associates with MHC class I molecules and promotes ubiquitylation of class I after export from the endoplasmic reticulum.
861	2966	activate	IKK-alpha	MEKK2	We now show that MEKK2 and MEKK3 can in vivo activate IKK-alpha and IKK-beta, induce site-specific IkappaBalpha phosphorylation, and, relatively modestly, activate an NF-kappaB reporter gene.
861	2967	activate	IKK-alpha	MEKK3	We now show that MEKK2 and MEKK3 can in vivo activate IKK-alpha and IKK-beta, induce site-specific IkappaBalpha phosphorylation, and, relatively modestly, activate an NF-kappaB reporter gene.
861	2968	activate	IKK-beta	MEKK2	We now show that MEKK2 and MEKK3 can in vivo activate IKK-alpha and IKK-beta, induce site-specific IkappaBalpha phosphorylation, and, relatively modestly, activate an NF-kappaB reporter gene.
861	2969	activate	IKK-beta	MEKK3	We now show that MEKK2 and MEKK3 can in vivo activate IKK-alpha and IKK-beta, induce site-specific IkappaBalpha phosphorylation, and, relatively modestly, activate an NF-kappaB reporter gene.
861	2970	phosphorylation	IkappaBalpha	MEKK2	We now show that MEKK2 and MEKK3 can in vivo activate IKK-alpha and IKK-beta, induce site-specific IkappaBalpha phosphorylation, and, relatively modestly, activate an NF-kappaB reporter gene.
861	2971	phosphorylation	IkappaBalpha	MEKK3	We now show that MEKK2 and MEKK3 can in vivo activate IKK-alpha and IKK-beta, induce site-specific IkappaBalpha phosphorylation, and, relatively modestly, activate an NF-kappaB reporter gene.
861	2972	activate	MEKK2	IKK-alpha	We now show that MEKK2 and MEKK3 can in vivo activate IKK-alpha and IKK-beta, induce site-specific IkappaBalpha phosphorylation, and, relatively modestly, activate an NF-kappaB reporter gene.
861	2973	activate	MEKK2	IKK-beta	We now show that MEKK2 and MEKK3 can in vivo activate IKK-alpha and IKK-beta, induce site-specific IkappaBalpha phosphorylation, and, relatively modestly, activate an NF-kappaB reporter gene.
861	2974	phosphorylation	MEKK2	IkappaBalpha	We now show that MEKK2 and MEKK3 can in vivo activate IKK-alpha and IKK-beta, induce site-specific IkappaBalpha phosphorylation, and, relatively modestly, activate an NF-kappaB reporter gene.
861	2975	activate	MEKK3	IKK-alpha	We now show that MEKK2 and MEKK3 can in vivo activate IKK-alpha and IKK-beta, induce site-specific IkappaBalpha phosphorylation, and, relatively modestly, activate an NF-kappaB reporter gene.
861	2976	activate	MEKK3	IKK-beta	We now show that MEKK2 and MEKK3 can in vivo activate IKK-alpha and IKK-beta, induce site-specific IkappaBalpha phosphorylation, and, relatively modestly, activate an NF-kappaB reporter gene.
861	2977	phosphorylation	MEKK3	IkappaBalpha	We now show that MEKK2 and MEKK3 can in vivo activate IKK-alpha and IKK-beta, induce site-specific IkappaBalpha phosphorylation, and, relatively modestly, activate an NF-kappaB reporter gene.
862	2978	inhibitor	IkappaB beta	NF-kappaB	We observed that IkappaB beta, another NF-kappaB inhibitor, is also complexed with c-Rel but slowly degraded by a proteasome-dependent process in WEHI231 cells.
862	2979	complexed	IkappaB beta	c-Rel	We observed that IkappaB beta, another NF-kappaB inhibitor, is also complexed with c-Rel but slowly degraded by a proteasome-dependent process in WEHI231 cells.
862	2980	inhibitor	NF-kappaB	IkappaB beta	We observed that IkappaB beta, another NF-kappaB inhibitor, is also complexed with c-Rel but slowly degraded by a proteasome-dependent process in WEHI231 cells.
862	2981	complexed	c-Rel	IkappaB beta	We observed that IkappaB beta, another NF-kappaB inhibitor, is also complexed with c-Rel but slowly degraded by a proteasome-dependent process in WEHI231 cells.
863	2982	interact	Ppr1p	Tup1p	We performed a split-ubiquitin screen with Tup1p as bait, and we found that the global repressor Tup1p interacts with the transcriptional activator Ppr1p both in vivo and in vitro.
863	2983	interact	Tup1p	Ppr1p	We performed a split-ubiquitin screen with Tup1p as bait, and we found that the global repressor Tup1p interacts with the transcriptional activator Ppr1p both in vivo and in vitro.
864	2984	interact	HBX	PSMA7	We previously identified a proteasome subunit PSMA7 that interacts specifically with HBX in the Saccharomyces cerevisiae two-hybrid system.
864	2985	interact	PSMA7	HBX	We previously identified a proteasome subunit PSMA7 that interacts specifically with HBX in the Saccharomyces cerevisiae two-hybrid system.
865	2986	modify	ND10	PKM	We propose that PKM is able to modify ND10 structure by inducing changes in the posttranslational modification of PML and by interacting with SUMO-1 modification pathways.
865	2987	modify	PKM	ND10	We propose that PKM is able to modify ND10 structure by inducing changes in the posttranslational modification of PML and by interacting with SUMO-1 modification pathways.
866	2988	conjugation	IkappaBalpha	mE2	We propose that mE2 is directly involved in the ubiquitin conjugation of IkappaBalpha, a pivotal step in its degradation pathway.
866	2989	conjugation	mE2	IkappaBalpha	We propose that mE2 is directly involved in the ubiquitin conjugation of IkappaBalpha, a pivotal step in its degradation pathway.
867	2990	activation	CSN	JUN	We propose that the broad spectrum of activities previously attributed to CSN subunits, including repression of photomorphogenesis, activation of JUN, and activation of p27 nuclear export, underscores the importance of dynamic cycles of NEDD8 attachment and removal in biological regulation.
867	2991	activation	CSN	p27	We propose that the broad spectrum of activities previously attributed to CSN subunits, including repression of photomorphogenesis, activation of JUN, and activation of p27 nuclear export, underscores the importance of dynamic cycles of NEDD8 attachment and removal in biological regulation.
867	2992	activation	JUN	CSN	We propose that the broad spectrum of activities previously attributed to CSN subunits, including repression of photomorphogenesis, activation of JUN, and activation of p27 nuclear export, underscores the importance of dynamic cycles of NEDD8 attachment and removal in biological regulation.
867	2993	activation	p27	CSN	We propose that the broad spectrum of activities previously attributed to CSN subunits, including repression of photomorphogenesis, activation of JUN, and activation of p27 nuclear export, underscores the importance of dynamic cycles of NEDD8 attachment and removal in biological regulation.
868	2994	complex	Cullin-5	E1B-55K	We propose that these newly identified binding partners (Cullin-5, Elongins B and C, and Rbx1) complex with E1B-55K and E4-orf6 during Ad infection to form part of an E3 ubiquitin ligase that targets specific protein substrates for degradation.
868	2995	complex	Cullin-5	E4-orf6	We propose that these newly identified binding partners (Cullin-5, Elongins B and C, and Rbx1) complex with E1B-55K and E4-orf6 during Ad infection to form part of an E3 ubiquitin ligase that targets specific protein substrates for degradation.
868	2996	complex	Cullin-5	Elongin B	We propose that these newly identified binding partners (Cullin-5, Elongins B and C, and Rbx1) complex with E1B-55K and E4-orf6 during Ad infection to form part of an E3 ubiquitin ligase that targets specific protein substrates for degradation.
868	2997	complex	Cullin-5	Elongin C	We propose that these newly identified binding partners (Cullin-5, Elongins B and C, and Rbx1) complex with E1B-55K and E4-orf6 during Ad infection to form part of an E3 ubiquitin ligase that targets specific protein substrates for degradation.
868	2998	complex	Cullin-5	Rbx1	We propose that these newly identified binding partners (Cullin-5, Elongins B and C, and Rbx1) complex with E1B-55K and E4-orf6 during Ad infection to form part of an E3 ubiquitin ligase that targets specific protein substrates for degradation.
868	2999	complex	E1B-55K	Cullin-5	We propose that these newly identified binding partners (Cullin-5, Elongins B and C, and Rbx1) complex with E1B-55K and E4-orf6 during Ad infection to form part of an E3 ubiquitin ligase that targets specific protein substrates for degradation.
868	3000	complex	E1B-55K	E4-orf6	We propose that these newly identified binding partners (Cullin-5, Elongins B and C, and Rbx1) complex with E1B-55K and E4-orf6 during Ad infection to form part of an E3 ubiquitin ligase that targets specific protein substrates for degradation.
868	3001	complex	E1B-55K	Elongin B	We propose that these newly identified binding partners (Cullin-5, Elongins B and C, and Rbx1) complex with E1B-55K and E4-orf6 during Ad infection to form part of an E3 ubiquitin ligase that targets specific protein substrates for degradation.
868	3002	complex	E1B-55K	Elongin C	We propose that these newly identified binding partners (Cullin-5, Elongins B and C, and Rbx1) complex with E1B-55K and E4-orf6 during Ad infection to form part of an E3 ubiquitin ligase that targets specific protein substrates for degradation.
868	3003	complex	E1B-55K	Rbx1	We propose that these newly identified binding partners (Cullin-5, Elongins B and C, and Rbx1) complex with E1B-55K and E4-orf6 during Ad infection to form part of an E3 ubiquitin ligase that targets specific protein substrates for degradation.
868	3004	complex	E4-orf6	Cullin-5	We propose that these newly identified binding partners (Cullin-5, Elongins B and C, and Rbx1) complex with E1B-55K and E4-orf6 during Ad infection to form part of an E3 ubiquitin ligase that targets specific protein substrates for degradation.
868	3005	complex	E4-orf6	E1B-55K	We propose that these newly identified binding partners (Cullin-5, Elongins B and C, and Rbx1) complex with E1B-55K and E4-orf6 during Ad infection to form part of an E3 ubiquitin ligase that targets specific protein substrates for degradation.
868	3006	complex	E4-orf6	Elongin B	We propose that these newly identified binding partners (Cullin-5, Elongins B and C, and Rbx1) complex with E1B-55K and E4-orf6 during Ad infection to form part of an E3 ubiquitin ligase that targets specific protein substrates for degradation.
868	3007	complex	E4-orf6	Elongin C	We propose that these newly identified binding partners (Cullin-5, Elongins B and C, and Rbx1) complex with E1B-55K and E4-orf6 during Ad infection to form part of an E3 ubiquitin ligase that targets specific protein substrates for degradation.
868	3008	complex	E4-orf6	Rbx1	We propose that these newly identified binding partners (Cullin-5, Elongins B and C, and Rbx1) complex with E1B-55K and E4-orf6 during Ad infection to form part of an E3 ubiquitin ligase that targets specific protein substrates for degradation.
868	3009	complex	Elongin B	Cullin-5	We propose that these newly identified binding partners (Cullin-5, Elongins B and C, and Rbx1) complex with E1B-55K and E4-orf6 during Ad infection to form part of an E3 ubiquitin ligase that targets specific protein substrates for degradation.
868	3010	complex	Elongin B	E1B-55K	We propose that these newly identified binding partners (Cullin-5, Elongins B and C, and Rbx1) complex with E1B-55K and E4-orf6 during Ad infection to form part of an E3 ubiquitin ligase that targets specific protein substrates for degradation.
868	3011	complex	Elongin B	E4-orf6	We propose that these newly identified binding partners (Cullin-5, Elongins B and C, and Rbx1) complex with E1B-55K and E4-orf6 during Ad infection to form part of an E3 ubiquitin ligase that targets specific protein substrates for degradation.
868	3012	complex	Elongin B	Elongin C	We propose that these newly identified binding partners (Cullin-5, Elongins B and C, and Rbx1) complex with E1B-55K and E4-orf6 during Ad infection to form part of an E3 ubiquitin ligase that targets specific protein substrates for degradation.
868	3013	complex	Elongin B	Rbx1	We propose that these newly identified binding partners (Cullin-5, Elongins B and C, and Rbx1) complex with E1B-55K and E4-orf6 during Ad infection to form part of an E3 ubiquitin ligase that targets specific protein substrates for degradation.
868	3014	complex	Elongin C	Cullin-5	We propose that these newly identified binding partners (Cullin-5, Elongins B and C, and Rbx1) complex with E1B-55K and E4-orf6 during Ad infection to form part of an E3 ubiquitin ligase that targets specific protein substrates for degradation.
868	3015	complex	Elongin C	E1B-55K	We propose that these newly identified binding partners (Cullin-5, Elongins B and C, and Rbx1) complex with E1B-55K and E4-orf6 during Ad infection to form part of an E3 ubiquitin ligase that targets specific protein substrates for degradation.
868	3016	complex	Elongin C	E4-orf6	We propose that these newly identified binding partners (Cullin-5, Elongins B and C, and Rbx1) complex with E1B-55K and E4-orf6 during Ad infection to form part of an E3 ubiquitin ligase that targets specific protein substrates for degradation.
868	3017	complex	Elongin C	Elongin B	We propose that these newly identified binding partners (Cullin-5, Elongins B and C, and Rbx1) complex with E1B-55K and E4-orf6 during Ad infection to form part of an E3 ubiquitin ligase that targets specific protein substrates for degradation.
868	3018	complex	Elongin C	Rbx1	We propose that these newly identified binding partners (Cullin-5, Elongins B and C, and Rbx1) complex with E1B-55K and E4-orf6 during Ad infection to form part of an E3 ubiquitin ligase that targets specific protein substrates for degradation.
868	3019	complex	Rbx1	Cullin-5	We propose that these newly identified binding partners (Cullin-5, Elongins B and C, and Rbx1) complex with E1B-55K and E4-orf6 during Ad infection to form part of an E3 ubiquitin ligase that targets specific protein substrates for degradation.
868	3020	complex	Rbx1	E1B-55K	We propose that these newly identified binding partners (Cullin-5, Elongins B and C, and Rbx1) complex with E1B-55K and E4-orf6 during Ad infection to form part of an E3 ubiquitin ligase that targets specific protein substrates for degradation.
868	3021	complex	Rbx1	E4-orf6	We propose that these newly identified binding partners (Cullin-5, Elongins B and C, and Rbx1) complex with E1B-55K and E4-orf6 during Ad infection to form part of an E3 ubiquitin ligase that targets specific protein substrates for degradation.
868	3022	complex	Rbx1	Elongin B	We propose that these newly identified binding partners (Cullin-5, Elongins B and C, and Rbx1) complex with E1B-55K and E4-orf6 during Ad infection to form part of an E3 ubiquitin ligase that targets specific protein substrates for degradation.
868	3023	complex	Rbx1	Elongin C	We propose that these newly identified binding partners (Cullin-5, Elongins B and C, and Rbx1) complex with E1B-55K and E4-orf6 during Ad infection to form part of an E3 ubiquitin ligase that targets specific protein substrates for degradation.
869	3024	activate	NF-kappaB	TNF-alpha	We recently reported that tumor necrosis factor-alpha (TNF-alpha) rapidly activates NF-kappaB in differentiated skeletal muscle myotubes and that TNF-alpha acts directly on the muscle cell to induce protein degradation.
869	3025	activate	TNF-alpha	NF-kappaB	We recently reported that tumor necrosis factor-alpha (TNF-alpha) rapidly activates NF-kappaB in differentiated skeletal muscle myotubes and that TNF-alpha acts directly on the muscle cell to induce protein degradation.
870	3026	bind	HHARI	UbcH7	We recently reported the identification of a RING finger-containing protein, HHARI (human homologue of Drosophila ariadne), which binds to the human ubiquitin-conjugating enzyme UbcH7 in vitro.
870	3027	bind	UbcH7	HHARI	We recently reported the identification of a RING finger-containing protein, HHARI (human homologue of Drosophila ariadne), which binds to the human ubiquitin-conjugating enzyme UbcH7 in vitro.
871	3028	bind	E6	E6BP	We recently showed the cellular protein ERC-55/E6BP binds BPV-1 E6 as well as the cancer-related human papillomavirus (HPV) E6 proteins.
871	3029	bind	E6	ERC-55	We recently showed the cellular protein ERC-55/E6BP binds BPV-1 E6 as well as the cancer-related human papillomavirus (HPV) E6 proteins.
871	3030	bind	E6BP	E6	We recently showed the cellular protein ERC-55/E6BP binds BPV-1 E6 as well as the cancer-related human papillomavirus (HPV) E6 proteins.
871	3031	bind	ERC-55	E6	We recently showed the cellular protein ERC-55/E6BP binds BPV-1 E6 as well as the cancer-related human papillomavirus (HPV) E6 proteins.
872	3032	bind	IkappaBalpha	beta-TrCP	We report here the identification of an IkappaB-ubiquitin (Ub) ligase complex containing the F-box/WD40-repeat protein, beta-TrCP, a vertebrate homolog of Drosophila Slimb. beta-TrCP binds to IkappaBalpha only when the latter is specifically phosphorylated by an IkappaB kinase complex.
872	3033	bind	beta-TrCP	IkappaBalpha	We report here the identification of an IkappaB-ubiquitin (Ub) ligase complex containing the F-box/WD40-repeat protein, beta-TrCP, a vertebrate homolog of Drosophila Slimb. beta-TrCP binds to IkappaBalpha only when the latter is specifically phosphorylated by an IkappaB kinase complex.
873	3034	interaction	Cdc20	Mad2	We report the solution structure of human Mad2 and its interaction with Cdc20.
873	3035	interaction	Mad2	Cdc20	We report the solution structure of human Mad2 and its interaction with Cdc20.
874	3036	modified	AR	SUMO-1	We show here that AR is covalently modified by SUMO-1 (sumoylated) in an androgen-enhanced fashion and identify the principal acceptor site in the N-terminal domain of AR.
874	3037	modified	SUMO-1	AR	We show here that AR is covalently modified by SUMO-1 (sumoylated) in an androgen-enhanced fashion and identify the principal acceptor site in the N-terminal domain of AR.
875	3038	complex	Cd53p	Skp1p	We show here that Cdc4p, Cdc53p, and Skp1p assemble into a ubiquitin ligase complex named SCFCdc4p.
875	3039	complex	Cdc4p	Cdc53p	We show here that Cdc4p, Cdc53p, and Skp1p assemble into a ubiquitin ligase complex named SCFCdc4p.
875	3040	complex	Cdc4p	Skp1p	We show here that Cdc4p, Cdc53p, and Skp1p assemble into a ubiquitin ligase complex named SCFCdc4p.
875	3041	complex	Cdc53p	Cdc4p	We show here that Cdc4p, Cdc53p, and Skp1p assemble into a ubiquitin ligase complex named SCFCdc4p.
875	3042	complex	Skp1p	Cd53p	We show here that Cdc4p, Cdc53p, and Skp1p assemble into a ubiquitin ligase complex named SCFCdc4p.
875	3043	complex	Skp1p	Cdc4p	We show here that Cdc4p, Cdc53p, and Skp1p assemble into a ubiquitin ligase complex named SCFCdc4p.
876	3044	interact	Rad22	Rhp51	We show here that Rad22 interacts with Rhp51 and Rpa70 (the fission yeast homologues of Rad51 and the large subunit of RPA, respectively), but that neither of these proteins appears to be responsible for the 83 kDa species.
876	3045	interact	Rad22	Rpa70	We show here that Rad22 interacts with Rhp51 and Rpa70 (the fission yeast homologues of Rad51 and the large subunit of RPA, respectively), but that neither of these proteins appears to be responsible for the 83 kDa species.
876	3046	interact	Rhp51	Rad22	We show here that Rad22 interacts with Rhp51 and Rpa70 (the fission yeast homologues of Rad51 and the large subunit of RPA, respectively), but that neither of these proteins appears to be responsible for the 83 kDa species.
876	3047	interact	Rpa70	Rad22	We show here that Rad22 interacts with Rhp51 and Rpa70 (the fission yeast homologues of Rad51 and the large subunit of RPA, respectively), but that neither of these proteins appears to be responsible for the 83 kDa species.
877	3048	modified	SUMO-1	TDG	We show here that TDG interacts with and is covalently modified by the ubiquitin-like proteins SUMO-1 and SUMO-2/3.
877	3049	modified	SUMO-2	TDG	We show here that TDG interacts with and is covalently modified by the ubiquitin-like proteins SUMO-1 and SUMO-2/3.
877	3050	modified	SUMO-3	TDG	We show here that TDG interacts with and is covalently modified by the ubiquitin-like proteins SUMO-1 and SUMO-2/3.
877	3051	modified	TDG	SUMO-1	We show here that TDG interacts with and is covalently modified by the ubiquitin-like proteins SUMO-1 and SUMO-2/3.
877	3052	modified	TDG	SUMO-2	We show here that TDG interacts with and is covalently modified by the ubiquitin-like proteins SUMO-1 and SUMO-2/3.
877	3053	modified	TDG	SUMO-3	We show here that TDG interacts with and is covalently modified by the ubiquitin-like proteins SUMO-1 and SUMO-2/3.
878	3054	bind	CAND1	CUL1	We show here that p120(CAND1) selectively binds to unneddylated CUL1 and is dissociated by CUL1 neddylation.
878	3055	bind	CUL1	CAND1	We show here that p120(CAND1) selectively binds to unneddylated CUL1 and is dissociated by CUL1 neddylation.
878	3056	bind	CUL1	p120	We show here that p120(CAND1) selectively binds to unneddylated CUL1 and is dissociated by CUL1 neddylation.
878	3057	bind	p120	CUL1	We show here that p120(CAND1) selectively binds to unneddylated CUL1 and is dissociated by CUL1 neddylation.
879	3058	interact	APP-BP1	hUba3	We show here that, in vivo in mammalian cells, APP-BP1 interacts with hUba3, its presumptive partner in the NEDD8 activation pathway, and that the APP-BP1 binding site for hUba3 is within amino acids 443-479.
879	3059	interact	hUba3	APP-BP1	We show here that, in vivo in mammalian cells, APP-BP1 interacts with hUba3, its presumptive partner in the NEDD8 activation pathway, and that the APP-BP1 binding site for hUba3 is within amino acids 443-479.
880	3060	phosphorylate	IKK-alpha	IkappaB	We show herein that recombinant IKK-alpha and IKK-beta can, in fact, directly phosphorylate IkappaB alpha at Ser-32 and Ser-36, as well as homologous residues in IkappaB beta in vitro, and thus are bona fide IkappaB kinases.
880	3061	phosphorylate	IKK-beta	IkappaB	We show herein that recombinant IKK-alpha and IKK-beta can, in fact, directly phosphorylate IkappaB alpha at Ser-32 and Ser-36, as well as homologous residues in IkappaB beta in vitro, and thus are bona fide IkappaB kinases.
880	3062	phosphorylate	IkappaB	IKK-alpha	We show herein that recombinant IKK-alpha and IKK-beta can, in fact, directly phosphorylate IkappaB alpha at Ser-32 and Ser-36, as well as homologous residues in IkappaB beta in vitro, and thus are bona fide IkappaB kinases.
880	3063	phosphorylate	IkappaB	IKK-beta	We show herein that recombinant IKK-alpha and IKK-beta can, in fact, directly phosphorylate IkappaB alpha at Ser-32 and Ser-36, as well as homologous residues in IkappaB beta in vitro, and thus are bona fide IkappaB kinases.
881	3064	activated	APC	hCDC20	We show that APC is activated during mitosis and G1 by two regulatory factors, hCDC20 and hCDH1.
881	3065	activated	APC	hCDH1	We show that APC is activated during mitosis and G1 by two regulatory factors, hCDC20 and hCDH1.
881	3066	activated	hCDC20	APC	We show that APC is activated during mitosis and G1 by two regulatory factors, hCDC20 and hCDH1.
881	3067	activated	hCDH1	APC	We show that APC is activated during mitosis and G1 by two regulatory factors, hCDC20 and hCDH1.
882	3068	ubiquitinated	MetAP-2	beta-TRCP	We show that MetAP-2 can be tethered to SCF(beta-TRCP), ubiquitinated, and degraded in a Protac-1-dependent manner.
882	3069	ubiquitinated	beta-TRCP	MetAP-2	We show that MetAP-2 can be tethered to SCF(beta-TRCP), ubiquitinated, and degraded in a Protac-1-dependent manner.
883	3070	interact	APC	plo1	We show that Plo1 kinase physically interacts with the anaphase-promoting complex (APC)/cyclosome through the noncatalytic domain of Plo1 and the tetratricopeptide repeat domain of the subunit, Cut23.
883	3071	interact	Cut23	Plo1	We show that Plo1 kinase physically interacts with the anaphase-promoting complex (APC)/cyclosome through the noncatalytic domain of Plo1 and the tetratricopeptide repeat domain of the subunit, Cut23.
883	3072	interact	Plo1	Cut23	We show that Plo1 kinase physically interacts with the anaphase-promoting complex (APC)/cyclosome through the noncatalytic domain of Plo1 and the tetratricopeptide repeat domain of the subunit, Cut23.
883	3073	interact	plo1	APC	We show that Plo1 kinase physically interacts with the anaphase-promoting complex (APC)/cyclosome through the noncatalytic domain of Plo1 and the tetratricopeptide repeat domain of the subunit, Cut23.
884	3074	interact	Pup1	Pup3	We show that Pup1 interacts with Pup3 in each beta subunit ring.
884	3075	interact	Pup3	Pup1	We show that Pup1 interacts with Pup3 in each beta subunit ring.
885	3076	transfer	H2b	ubiquitin	We show that Rad6 protein expressed in metastatic tumor lines is wild type and functional, because it is able to catalyze the transfer of ubiquitin to histone H2b and is predominantly localized in the nucleus as compared with cytoplasmic localization in normal or nonmetastatic mammary cells.
885	3077	transfer	Rad6	ubiquitin	We show that Rad6 protein expressed in metastatic tumor lines is wild type and functional, because it is able to catalyze the transfer of ubiquitin to histone H2b and is predominantly localized in the nucleus as compared with cytoplasmic localization in normal or nonmetastatic mammary cells.
885	3078	transfer	ubiquitin	H2b	We show that Rad6 protein expressed in metastatic tumor lines is wild type and functional, because it is able to catalyze the transfer of ubiquitin to histone H2b and is predominantly localized in the nucleus as compared with cytoplasmic localization in normal or nonmetastatic mammary cells.
885	3079	transfer	ubiquitin	Rad6	We show that Rad6 protein expressed in metastatic tumor lines is wild type and functional, because it is able to catalyze the transfer of ubiquitin to histone H2b and is predominantly localized in the nucleus as compared with cytoplasmic localization in normal or nonmetastatic mammary cells.
886	3080	interact	Sec61p	Sec63p	We show that Sec63p interacts with Sec62p and Sec61p in vivo.
886	3081	interact	Sec62p	Sec63p	We show that Sec63p interacts with Sec62p and Sec61p in vivo.
886	3082	interact	Sec63p	Sec61p	We show that Sec63p interacts with Sec62p and Sec61p in vivo.
886	3083	interact	Sec63p	Sec62p	We show that Sec63p interacts with Sec62p and Sec61p in vivo.
887	3084	bind	Skp1	Skp2	We show that Skp1 can bind to Skp2 in vitro using recombinant proteins, and in vivo using the yeast two-hybrid system.
887	3085	bind	Skp2	Skp1	We show that Skp1 can bind to Skp2 in vitro using recombinant proteins, and in vivo using the yeast two-hybrid system.
888	3086	interact	TEL	UBC9	We show that a protein, UBC9, interacts specifically with TEL in vitro and in vivo.
888	3087	interact	UBC9	TEL	We show that a protein, UBC9, interacts specifically with TEL in vitro and in vivo.
889	3088	binding	Cln2	SCF(Grr1)	We show that binding of Cln2 by SCF(Grr1) was dependent upon its leucine-rich repeat (LRR) domain and its carboxy terminus.
889	3089	binding	SCF(Grr1)	Cln2	We show that binding of Cln2 by SCF(Grr1) was dependent upon its leucine-rich repeat (LRR) domain and its carboxy terminus.
890	3090	binding	E2F-1	pRb	We show that binding of E2F-1 to pRb or E2F-4 to p107 or p130 protects E2Fs from degradation, causing the complexes to be stable.
890	3091	binding	E2F-4	p107	We show that binding of E2F-1 to pRb or E2F-4 to p107 or p130 protects E2Fs from degradation, causing the complexes to be stable.
890	3092	binding	E2F-4	p130	We show that binding of E2F-1 to pRb or E2F-4 to p107 or p130 protects E2Fs from degradation, causing the complexes to be stable.
890	3093	binding	p107	E2F-4	We show that binding of E2F-1 to pRb or E2F-4 to p107 or p130 protects E2Fs from degradation, causing the complexes to be stable.
890	3094	binding	p130	E2F-4	We show that binding of E2F-1 to pRb or E2F-4 to p107 or p130 protects E2Fs from degradation, causing the complexes to be stable.
890	3095	binding	pRb	E2F-1	We show that binding of E2F-1 to pRb or E2F-4 to p107 or p130 protects E2Fs from degradation, causing the complexes to be stable.
891	3096	bind	Cln2	Grr1	We show that point mutations that converted the basic residues on the concave surface but not those on the convex surface to neutral or acidic residues interfered with the capacity of Grr1 to bind to Cln2.
891	3097	bind	Grr1	Cln2	We show that point mutations that converted the basic residues on the concave surface but not those on the convex surface to neutral or acidic residues interfered with the capacity of Grr1 to bind to Cln2.
892	3098	interact	Slmb	dRbx1	We show that putative Drosophila SCF core subunits dSkpA and dRbx1 both interact directly with dCu11 and the F-box protein Slmb.
892	3099	interact	Slmb	dSkpA	We show that putative Drosophila SCF core subunits dSkpA and dRbx1 both interact directly with dCu11 and the F-box protein Slmb.
892	3100	interact	dCu11	dRbx1	We show that putative Drosophila SCF core subunits dSkpA and dRbx1 both interact directly with dCu11 and the F-box protein Slmb.
892	3101	interact	dCu11	dSkpA	We show that putative Drosophila SCF core subunits dSkpA and dRbx1 both interact directly with dCu11 and the F-box protein Slmb.
892	3102	interact	dRbx1	Slmb	We show that putative Drosophila SCF core subunits dSkpA and dRbx1 both interact directly with dCu11 and the F-box protein Slmb.
892	3103	interact	dRbx1	dCu11	We show that putative Drosophila SCF core subunits dSkpA and dRbx1 both interact directly with dCu11 and the F-box protein Slmb.
892	3104	interact	dSkpA	Slmb	We show that putative Drosophila SCF core subunits dSkpA and dRbx1 both interact directly with dCu11 and the F-box protein Slmb.
892	3105	interact	dSkpA	dCu11	We show that putative Drosophila SCF core subunits dSkpA and dRbx1 both interact directly with dCu11 and the F-box protein Slmb.
893	3106	interact	NbRar1	NbSGT1	We show that the NbRar1 protein interacts with NbSGT1, a highly conserved component of the SCF (Skp1/Cullin/F-box protein)-type E3 ubiquitin ligase complex involved in protein degradation.
893	3107	interact	NbSGT1	NbRar1	We show that the NbRar1 protein interacts with NbSGT1, a highly conserved component of the SCF (Skp1/Cullin/F-box protein)-type E3 ubiquitin ligase complex involved in protein degradation.
894	3108	targeted	Scul(Cdc4)	p58Ctf13	We show that the function of p23Skp1 in Cbf3p is to activate p58Ctf13 by phosphorylation. p58Ctf13 is an unstable protein that is targeted to the proteosome, probably by Scul(Cdc4)-mediated ubiquitination.
894	3109	activate	p23Skp1	p58Ctf13	We show that the function of p23Skp1 in Cbf3p is to activate p58Ctf13 by phosphorylation. p58Ctf13 is an unstable protein that is targeted to the proteosome, probably by Scul(Cdc4)-mediated ubiquitination.
894	3110	targeted	p58Ctf13	Scul(Cdc4)	We show that the function of p23Skp1 in Cbf3p is to activate p58Ctf13 by phosphorylation. p58Ctf13 is an unstable protein that is targeted to the proteosome, probably by Scul(Cdc4)-mediated ubiquitination.
894	3111	activate	p58Ctf13	p23Skp1	We show that the function of p23Skp1 in Cbf3p is to activate p58Ctf13 by phosphorylation. p58Ctf13 is an unstable protein that is targeted to the proteosome, probably by Scul(Cdc4)-mediated ubiquitination.
895	3112	interact	CNOT4	E2s	We show that the unique C4C4 RING domain of CNOT4 interacts with a subset of ubiquitin-conjugating enzymes (E2s).
895	3113	interact	E2s	CNOT4	We show that the unique C4C4 RING domain of CNOT4 interacts with a subset of ubiquitin-conjugating enzymes (E2s).
896	3114	modified	GR	SUMO-1	We showed that the GR is covalently modified by the small ubiquitin-related modifier-1 (SUMO-1) peptide in mammalian cells.
896	3115	modified	SUMO-1	GR	We showed that the GR is covalently modified by the small ubiquitin-related modifier-1 (SUMO-1) peptide in mammalian cells.
897	3116	transfer	APC	ubiquitin	We suggest that Apc11p is responsible for recruiting E2s to the APC and for mediating the subsequent transfer of ubiquitin to APC substrates in vivo.
897	3117	transfer	ubiquitin	APC	We suggest that Apc11p is responsible for recruiting E2s to the APC and for mediating the subsequent transfer of ubiquitin to APC substrates in vivo.
898	3118	association	Bub3	Cdc20	We suggest that Bub3 could serve as a platform for interactions between kinetochore checkpoint proteins, and its association with Mad2, Mad3 and Cdc20 might be instrumental for checkpoint activation.
898	3119	association	Bub3	Mad2	We suggest that Bub3 could serve as a platform for interactions between kinetochore checkpoint proteins, and its association with Mad2, Mad3 and Cdc20 might be instrumental for checkpoint activation.
898	3120	association	Bub3	Mad3	We suggest that Bub3 could serve as a platform for interactions between kinetochore checkpoint proteins, and its association with Mad2, Mad3 and Cdc20 might be instrumental for checkpoint activation.
898	3121	association	Cdc20	Bub3	We suggest that Bub3 could serve as a platform for interactions between kinetochore checkpoint proteins, and its association with Mad2, Mad3 and Cdc20 might be instrumental for checkpoint activation.
898	3122	association	Mad2	Bub3	We suggest that Bub3 could serve as a platform for interactions between kinetochore checkpoint proteins, and its association with Mad2, Mad3 and Cdc20 might be instrumental for checkpoint activation.
898	3123	association	Mad3	Bub3	We suggest that Bub3 could serve as a platform for interactions between kinetochore checkpoint proteins, and its association with Mad2, Mad3 and Cdc20 might be instrumental for checkpoint activation.
899	3124	interaction	PhLP	SUG1	We suggest that PhLP/SUG1 interaction may target PhLP for proteasomal degradation.
899	3125	interaction	SUG1	PhLP	We suggest that PhLP/SUG1 interaction may target PhLP for proteasomal degradation.
900	3126	interact	HR6A	RFPL4	We used a yeast two-hybrid model to demonstrate that RFPL4 interacts with the E2 ubiquitin-conjugating enzyme HR6A, proteasome subunit beta type 1, ubiquitin B, as well as a degradation target protein, cyclin B1.
900	3127	interact	RFPL4	HR6A	We used a yeast two-hybrid model to demonstrate that RFPL4 interacts with the E2 ubiquitin-conjugating enzyme HR6A, proteasome subunit beta type 1, ubiquitin B, as well as a degradation target protein, cyclin B1.
900	3128	interact	RFPL4	cyclin B1	We used a yeast two-hybrid model to demonstrate that RFPL4 interacts with the E2 ubiquitin-conjugating enzyme HR6A, proteasome subunit beta type 1, ubiquitin B, as well as a degradation target protein, cyclin B1.
900	3129	interact	RFPL4	ubiquitin	We used a yeast two-hybrid model to demonstrate that RFPL4 interacts with the E2 ubiquitin-conjugating enzyme HR6A, proteasome subunit beta type 1, ubiquitin B, as well as a degradation target protein, cyclin B1.
900	3130	interact	cyclin B1	RFPL4	We used a yeast two-hybrid model to demonstrate that RFPL4 interacts with the E2 ubiquitin-conjugating enzyme HR6A, proteasome subunit beta type 1, ubiquitin B, as well as a degradation target protein, cyclin B1.
900	3131	interact	ubiquitin	RFPL4	We used a yeast two-hybrid model to demonstrate that RFPL4 interacts with the E2 ubiquitin-conjugating enzyme HR6A, proteasome subunit beta type 1, ubiquitin B, as well as a degradation target protein, cyclin B1.
901	3132	conjugation	AAV-2	ubiquitin	Western blot assays of immunoprecipitated viral capsid proteins from infected HeLa cell lysates and in vitro reconstitution experiments revealed evidence for ubiquitin conjugation of both AAV-2 and AAV-5 capsids.
901	3133	conjugation	AAV-5	ubiquitin	Western blot assays of immunoprecipitated viral capsid proteins from infected HeLa cell lysates and in vitro reconstitution experiments revealed evidence for ubiquitin conjugation of both AAV-2 and AAV-5 capsids.
901	3134	conjugation	ubiquitin	AAV-2	Western blot assays of immunoprecipitated viral capsid proteins from infected HeLa cell lysates and in vitro reconstitution experiments revealed evidence for ubiquitin conjugation of both AAV-2 and AAV-5 capsids.
901	3135	conjugation	ubiquitin	AAV-5	Western blot assays of immunoprecipitated viral capsid proteins from infected HeLa cell lysates and in vitro reconstitution experiments revealed evidence for ubiquitin conjugation of both AAV-2 and AAV-5 capsids.
902	3136	bind	Ubc9	Vsx-1	When a yeast two-hybrid assay is used, deletion analysis of the interacting domain on Vsx-1 shows that Ubc9 binds to a nuclear localization signal (NLS) at the NH(2) terminus of the homeodomain.
902	3137	bind	Vsx-1	Ubc9	When a yeast two-hybrid assay is used, deletion analysis of the interacting domain on Vsx-1 shows that Ubc9 binds to a nuclear localization signal (NLS) at the NH(2) terminus of the homeodomain.
903	3138	ubiquitinate	Cln2HA	Grr1	When bound to Cdc28-43244, Cln2HA was recognized and polyubiquitinated by SCF-Grr1.
903	3139	ubiquitinate	Grr1	Cln2HA	When bound to Cdc28-43244, Cln2HA was recognized and polyubiquitinated by SCF-Grr1.
904	3140	catalyzed	A-Cdk2	CDC34	When produced in Escherichia coli, the CDC34 gene product catalyzed the covalent attachment of ubiquitin to histones H2A and H2B in vitro, demonstrating that the CDC34 protein is another distinct member of the family of ubiquitin-conjugating enzymes.
904	3141	catalyzed	CDC34	A-Cdk2	When produced in Escherichia coli, the CDC34 gene product catalyzed the covalent attachment of ubiquitin to histones H2A and H2B in vitro, demonstrating that the CDC34 protein is another distinct member of the family of ubiquitin-conjugating enzymes.
904	3142	catalyzed	CDC34	FBL2	When produced in Escherichia coli, the CDC34 gene product catalyzed the covalent attachment of ubiquitin to histones H2A and H2B in vitro, demonstrating that the CDC34 protein is another distinct member of the family of ubiquitin-conjugating enzymes.
904	3143	catalyzed	FBL2	CDC34	When produced in Escherichia coli, the CDC34 gene product catalyzed the covalent attachment of ubiquitin to histones H2A and H2B in vitro, demonstrating that the CDC34 protein is another distinct member of the family of ubiquitin-conjugating enzymes.
904	3144	attachment	H2A	ubiquitin	When produced in Escherichia coli, the CDC34 gene product catalyzed the covalent attachment of ubiquitin to histones H2A and H2B in vitro, demonstrating that the CDC34 protein is another distinct member of the family of ubiquitin-conjugating enzymes.
904	3145	attachment	H2B	ubiquitin	When produced in Escherichia coli, the CDC34 gene product catalyzed the covalent attachment of ubiquitin to histones H2A and H2B in vitro, demonstrating that the CDC34 protein is another distinct member of the family of ubiquitin-conjugating enzymes.
904	3146	attachment	ubiquitin	H2A	When produced in Escherichia coli, the CDC34 gene product catalyzed the covalent attachment of ubiquitin to histones H2A and H2B in vitro, demonstrating that the CDC34 protein is another distinct member of the family of ubiquitin-conjugating enzymes.
904	3147	attachment	ubiquitin	H2B	When produced in Escherichia coli, the CDC34 gene product catalyzed the covalent attachment of ubiquitin to histones H2A and H2B in vitro, demonstrating that the CDC34 protein is another distinct member of the family of ubiquitin-conjugating enzymes.
905	3148	interaction	Aut1p	Aut7p	While this novel processing event is essential for Aut7p membrane binding, Aut7p must undergo additional physical interactions with Aut1p and the autophagy (Apg) conjugation complex before recruitment to the membrane.
905	3149	interaction	Aut7p	Aut1p	While this novel processing event is essential for Aut7p membrane binding, Aut7p must undergo additional physical interactions with Aut1p and the autophagy (Apg) conjugation complex before recruitment to the membrane.
906	3150	ubiquitinate	CDC4	Far1p	Wild-type Far1p, but not Far1-22p, was readily ubiquitinated in vitro in a CDC34- and CDC4-dependent manner.
906	3151	ubiquitinate	Far1p	CDC4	Wild-type Far1p, but not Far1-22p, was readily ubiquitinated in vitro in a CDC34- and CDC4-dependent manner.
907	3152	binding	GR	Ubc9	With high concentrations of Ubc9 and GR, Ubc9 binding to GR appears to be sufficient to permit Ubc9 to act independently of the GME.
907	3153	binding	Ubc9	GR	With high concentrations of Ubc9 and GR, Ubc9 binding to GR appears to be sufficient to permit Ubc9 to act independently of the GME.
908	3154	ubiquitinate	EGF receptor	c-Cbl	With the aid of confocal microscopy and immunogold electron microscopy, we could demonstrate that c-Cbl associates with the EGF receptor at the plasma membrane prior to receptor recruitment into clathrin-coated pits and remains associated throughout the clathrin-mediated endocytic pathway.
908	3155	ubiquitinate	c-Cbl	EGF receptor	With the aid of confocal microscopy and immunogold electron microscopy, we could demonstrate that c-Cbl associates with the EGF receptor at the plasma membrane prior to receptor recruitment into clathrin-coated pits and remains associated throughout the clathrin-mediated endocytic pathway.
909	3156	modify	H2B	Rad6	With the recent finding that the E2 ubiquitin conjugase Rad6 modifies histone H2B, we examined the role of Rad6 in the regulation of ARG1 transcription.
909	3157	modify	Rad6	H2B	With the recent finding that the E2 ubiquitin conjugase Rad6 modifies histone H2B, we examined the role of Rad6 in the regulation of ARG1 transcription.
910	3158	activation	SUMO	Uba2p	Yeast Uba2p and Ubc9p are involved in the activation and conjugation, respectively, of the ubiquitin-like protein Smt3p/SUMO, which becomes conjugated to a variety of proteins through this pathway.
910	3159	conjugation	SUMO	Ubc9p	Yeast Uba2p and Ubc9p are involved in the activation and conjugation, respectively, of the ubiquitin-like protein Smt3p/SUMO, which becomes conjugated to a variety of proteins through this pathway.
910	3160	activation	Smt3p	Uba2p	Yeast Uba2p and Ubc9p are involved in the activation and conjugation, respectively, of the ubiquitin-like protein Smt3p/SUMO, which becomes conjugated to a variety of proteins through this pathway.
910	3161	conjugation	Smt3p	Ubc9p	Yeast Uba2p and Ubc9p are involved in the activation and conjugation, respectively, of the ubiquitin-like protein Smt3p/SUMO, which becomes conjugated to a variety of proteins through this pathway.
910	3162	activation	Uba2p	SUMO	Yeast Uba2p and Ubc9p are involved in the activation and conjugation, respectively, of the ubiquitin-like protein Smt3p/SUMO, which becomes conjugated to a variety of proteins through this pathway.
910	3163	activation	Uba2p	Smt3p	Yeast Uba2p and Ubc9p are involved in the activation and conjugation, respectively, of the ubiquitin-like protein Smt3p/SUMO, which becomes conjugated to a variety of proteins through this pathway.
910	3164	conjugation	Ubc9p	SUMO	Yeast Uba2p and Ubc9p are involved in the activation and conjugation, respectively, of the ubiquitin-like protein Smt3p/SUMO, which becomes conjugated to a variety of proteins through this pathway.
910	3165	conjugation	Ubc9p	Smt3p	Yeast Uba2p and Ubc9p are involved in the activation and conjugation, respectively, of the ubiquitin-like protein Smt3p/SUMO, which becomes conjugated to a variety of proteins through this pathway.
911	3166	interaction	E6	p73	Yeast two-hybrid and GST pull-down assays indicate a physical interaction between p73 and either HPV-16 or HPV-11 E6 proteins in vivo and in vitro, respectively.
911	3167	interaction	p73	E6	Yeast two-hybrid and GST pull-down assays indicate a physical interaction between p73 and either HPV-16 or HPV-11 E6 proteins in vivo and in vitro, respectively.
912	3168	interact	ERalpha	Uba3	Yeast two-hybrid and glutathione-S-transferase pull-down assays demonstrated that Uba3 directly interacts with ligand-occupied ERalpha and ERbeta.
912	3169	interact	ERbeta	Uba3	Yeast two-hybrid and glutathione-S-transferase pull-down assays demonstrated that Uba3 directly interacts with ligand-occupied ERalpha and ERbeta.
912	3170	interact	Uba3	ERalpha	Yeast two-hybrid and glutathione-S-transferase pull-down assays demonstrated that Uba3 directly interacts with ligand-occupied ERalpha and ERbeta.
912	3171	interact	Uba3	ERbeta	Yeast two-hybrid and glutathione-S-transferase pull-down assays demonstrated that Uba3 directly interacts with ligand-occupied ERalpha and ERbeta.
913	3172	interact	CED-3	ceBNIP3	ceBNIP3 interacts with CED-3 but co-expression of CED-3 and ceBNIP3 does not significantly enhance induction of cell death in the presence or absence of CED-4.
913	3173	interact	ceBNIP3	CED-3	ceBNIP3 interacts with CED-3 but co-expression of CED-3 and ceBNIP3 does not significantly enhance induction of cell death in the presence or absence of CED-4.
914	3174	interact	BCL-XL	ceBNIP3	ceBNIP3 protein interacts with CED-9 and BCL-XL, but unlike other pro-apoptotic BCL-2 family members, the BH3-like domain does not participate in dimerization.
914	3175	interact	CED-9	ceBNIP3	ceBNIP3 protein interacts with CED-9 and BCL-XL, but unlike other pro-apoptotic BCL-2 family members, the BH3-like domain does not participate in dimerization.
914	3176	interact	ceBNIP3	BCL-XL	ceBNIP3 protein interacts with CED-9 and BCL-XL, but unlike other pro-apoptotic BCL-2 family members, the BH3-like domain does not participate in dimerization.
914	3177	interact	ceBNIP3	CED-9	ceBNIP3 protein interacts with CED-9 and BCL-XL, but unlike other pro-apoptotic BCL-2 family members, the BH3-like domain does not participate in dimerization.
915	3178	phosphorylate	c-Abl	gamma-PAK	gamma-PAK phosphorylates c-Abl on sites located in the kinase domain, in a region that is implicated in protein-protein interactions and in subcellular localization.
915	3179	phosphorylate	gamma-PAK	c-Abl	gamma-PAK phosphorylates c-Abl on sites located in the kinase domain, in a region that is implicated in protein-protein interactions and in subcellular localization.
916	3180	interact	c-Cbl	hSpry2	hSpry2 interacts specifically with the c-Cbl RING finger domain and displaces UbcH7 from its binding site on the E3 ligase.
916	3181	interact	hSpry2	c-Cbl	hSpry2 interacts specifically with the c-Cbl RING finger domain and displaces UbcH7 from its binding site on the E3 ligase.
917	3182	interact	TAP	mK3	mK3 failed to regulate class I in TAP- or tapasin-deficient cells, and mK3 interacted with TAP/tapasin, even in the absence of class I.
917	3183	interact	mK3	TAP	mK3 failed to regulate class I in TAP- or tapasin-deficient cells, and mK3 interacted with TAP/tapasin, even in the absence of class I.
917	3184	interact	mK3	tapasin	mK3 failed to regulate class I in TAP- or tapasin-deficient cells, and mK3 interacted with TAP/tapasin, even in the absence of class I.
917	3185	interact	tapasin	mK3	mK3 failed to regulate class I in TAP- or tapasin-deficient cells, and mK3 interacted with TAP/tapasin, even in the absence of class I.
918	3186	interacting	Mdm2	p14ARF	p14ARF tumour suppressor stabilises and activates p53 by directly interacting with (H)Mdm2 [(human) murine double minute 2 homologue] and inhibiting its E3 ubiquitin ligase activity.
918	3187	interacting	p14ARF	Mdm2	p14ARF tumour suppressor stabilises and activates p53 by directly interacting with (H)Mdm2 [(human) murine double minute 2 homologue] and inhibiting its E3 ubiquitin ligase activity.
918	3188	activate	p14ARF	p53	p14ARF tumour suppressor stabilises and activates p53 by directly interacting with (H)Mdm2 [(human) murine double minute 2 homologue] and inhibiting its E3 ubiquitin ligase activity.
918	3189	activate	p53	p14ARF	p14ARF tumour suppressor stabilises and activates p53 by directly interacting with (H)Mdm2 [(human) murine double minute 2 homologue] and inhibiting its E3 ubiquitin ligase activity.
919	3190	interact	CSN subunit 5	p53	p53 interacts via its N-terminus with CSN subunit 5/Jab1 as shown by far-western and pull-down assays.
919	3191	interact	Jab1	p53	p53 interacts via its N-terminus with CSN subunit 5/Jab1 as shown by far-western and pull-down assays.
919	3192	interact	p53	CSN subunit 5	p53 interacts via its N-terminus with CSN subunit 5/Jab1 as shown by far-western and pull-down assays.
919	3193	interact	p53	Jab1	p53 interacts via its N-terminus with CSN subunit 5/Jab1 as shown by far-western and pull-down assays.
920	3194	bind	MDM2	p53	p53 proteins mutated in their MDM2 binding domains were unable to bind MDM2 directly and were resistant to MDM2-mediated ubiquitination, nuclear export, and degradation when expressed with MDM2 alone.
920	3195	bind	p53	MDM2	p53 proteins mutated in their MDM2 binding domains were unable to bind MDM2 directly and were resistant to MDM2-mediated ubiquitination, nuclear export, and degradation when expressed with MDM2 alone.