RefGenome Electronic Jamboree 2008-10 NEDD4

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Orthoset

Ortholog set at PPOD

Participants

Name	Group	Organism(s)/Genome(s)	Notes
Rachael Huntley	GOA	Human	UniProtKB:P46934
Susan Tweedie	flyBase	D. melanogaster	FBgn0259174
Ruth Lovering	BHF-UCL	Human	UniProtKB:P46934
Varsha Khodiyar	BHF-UCL	Human	UniProtKB:P46934
Emily Dimmer	GOA	Human	UniProtKB:P46934
Kimberly Van Auken	WormBase	C. elegans	NEDD4 = Y92H12A.2 = WBGene00022358
Julie Park	SGD	S. cerevisiae	NEDD4 = RSP5 = S000000927 (Although this gene is not in the stated orthogroup, the body of literature for RSP5 supports that it is the ortholog of NEDD4)
Alexander Diehl	MGI	Mouse	UniProtKB:P46935
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NEDD4

<ejamb> 573c5f77b3a094817c4e1c4a6f9b2c99.260434.M48e666180c35f

NEDD4</ejamb>

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Group	Organism	Gene	Qualifier	GO ID	GO term name	Reference(s)	Evidence Code	with/from	Aspect	Notes	Status
BHF-UCL	Human	P46934		GO:0034644	cellular response to UV	PMID:17996703^[1]	IMP: Inferred from Mutant Phenotype		P		complete
BHF-UCL	Human	P46934		GO:0042787	protein ubiquitination during ubiquitin-dependent protein catabolic process	PMID:17996703^[1]	IMP: Inferred from Mutant Phenotype		P		complete
BHF-UCL	Human	P46934		GO:0042921	glucocorticoid receptor signaling pathway	PMID:8649367^[2]	IDA: Inferred from Direct Assay		P		complete
BHF-UCL	Human	P46934		GO:0050847	progesterone receptor signaling pathway	PMID:8649367^[2]	IDA: Inferred from Direct Assay		P		complete
BHF-UCL	Human	P46934		GO:0031175	neurite development	PMID:9990509^[3]	IEP: Inferred from Expression Pattern		P		complete
BHF-UCL	Human	P46934		GO:0014068	positive regulation of phosphoinositide 3-kinase cascade	PMID:17218260^[4]	IMP: Inferred from Mutant Phenotype		P		complete
BHF-UCL	Human	P46934		GO:0042787	protein ubiquitination during ubiquitin-dependent protein catabolic process	PMID:17218260^[4]	IMP: Inferred from Mutant Phenotype		P		complete
BHF-UCL	Human	P46934		GO:0046824	positive regulation of nucleocytoplasmic transport	PMID:17218261^[5]	IDA: Inferred from Direct Assay		P		complete
GOA	Human	P46934		GO:0007041	lysosomal transport	PMID:18544533^[6]	IDA: Inferred from Direct Assay		P
GOA	Human	P46934		GO:0031623	receptor internalization	PMID:18544533^[6]	IDA: Inferred from Direct Assay		P
GOA	Human	P46934		GO:0032801	receptor catabolic process	PMID:18544533^[6]	IDA: Inferred from Direct Assay		P
GOA	Human	P46934		GO:0006622	protein targeting to lysosome	PMID:17116753^[7]	IDA: Inferred from Direct Assay		P
GOA	Human	P46934		GO:0010766	negative regulation of sodium ion transport	PMID:10642508^[8]	IDA: Inferred from Direct Assay		P		complete
BHF-UCL	Human	P46934		GO:0010768	negative regulation of transcription from RNA polymerase II promoter in response to UV-induced DNA damage	PMID:17996703^[1]	IMP: Inferred from Mutant Phenotype		P		complete
FlyBase	Drosophila	FBgn0259174		GO:0005737	cytoplasm	PMID:17074801^[9]	IDA: Inferred from Direct Assay		C		complete
BHF-UCL	Human	P46934		GO:0004842	ubiquitin-protein ligase activity	PMID:17996703^[1]	IDA: Inferred from Direct Assay		F		complete
FlyBase	Drosophila	FBgn0259174		GO:0016567	protein ubiquitination	PMID:17074801^[9]	IMP: Inferred from Mutant Phenotype		P		complete
BHF-UCL	Human	P46934		GO:0043130	ubiquitin binding	PMID:17996703^[1]	IC: Inferred by Curator	GO:0004842	F		complete
FlyBase	Drosophila	FBgn0259174		GO:0045807	positive regulation of endocytosis	PMID:17074801^[9]	IMP: Inferred from Mutant Phenotype		P	Do we need term to indicate endocytosis of a specific protein (other than receptor)?	complete
BHF-UCL	Human	P46934		GO:0005515	protein binding	PMID:9305852^[10]	IPI: Inferred from Physical Interaction	Q16621	F		complete
FlyBase	Drosophila	FBgn0259174		GO:0051965	positive regulation of synaptogenesis	PMID:17074801^[9]	IMP: Inferred from Mutant Phenotype		P	NTR: reg of neuromuscular synaptogenesis?	complete
BHF-UCL	Human	P46934		GO:0043130	ubiquitin binding	PMID:9990509^[3]	IDA: Inferred from Direct Assay		F		complete
BHF-UCL	Human	P46934		GO:0005515	protein binding	PMID:12796489^[11]	IPI: Inferred from Physical Interaction	Q9NV92	F		complete
BHF-UCL	Human	P46934		GO:0005515	protein binding	PMID:10642508^[8]	IPI: Inferred from Physical Interaction	P37088	F		complete
FlyBase	Drosophila	FBgn0259174		GO:0019904	protein domain specific binding	PMID:16531238^[12]	IPI: Inferred from Physical Interaction	FB:FBgn0010105	F	NTR: PY motif binding?	complete
BHF-UCL	Human	P46934		GO:0005515	protein binding	PMID:10642508^[8]	IPI: Inferred from Physical Interaction	P51168	F		complete
BHF-UCL	Human	P46934		GO:0005515	protein binding	PMID:10642508^[8]	IPI: Inferred from Physical Interaction	P51170	F		complete
BHF-UCL	Human	P46934		GO:0019871	sodium channel inhibitor activity	PMID:10642508^[8]	IDA: Inferred from Direct Assay		F		complete
BHF-UCL	Human	P46934		GO:0005515	protein binding	PMID:9990509^[3]	IPI: Inferred from Physical Interaction	P68036	F		complete
BHF-UCL	Human	P46934		GO:0005886	plasma membrane	PMID:15126635^[13]	IMP: Inferred from Mutant Phenotype		C		complete
GOA	Human	P46934		GO:0031698	beta-2 adrenergic receptor binding	PMID:18544533^[6]	IDA: Inferred from Direct Assay		F		complete
GOA	Human	P46934		GO:0019904	protein domain specific binding	PMID:12907594^[14]	IPI: Inferred from Physical Interaction	Q969W9	F		complete
BHF-UCL	Human	P46934		GO:0070063	RNA polymerase binding	PMID:17996703^[1]	IPI: Inferred from Physical Interaction	P24928	F		complete
BHF-UCL	Human	P46934		GO:0070064	proline-rich region binding	PMID:15126635^[13]	IMP: Inferred from Mutant Phenotype		F		complete
GOA	Human	P46934		GO:0070064	proline-rich region binding	PMID:11342538^[15]	IPI: Inferred from Physical Interaction	Q15038	F		complete
BHF-UCL	Human	P46934		GO:0005737	cytoplasm	PMID:12796489^[11]	IDA: Inferred from Direct Assay		C		complete
BHF-UCL	Human	P46934		GO:0005938	cell cortex	PMID:9990509^[3]	IDA: Inferred from Direct Assay		C		complete
BHF-UCL	Human	P46934		GO:0048471	perinuclear region of cytoplasm	PMID:9990509^[3]	IDA: Inferred from Direct Assay		C		complete
BHF-UCL	Human	P46934		GO:0000785	chromatin	PMID:17996703^[1]	IDA: Inferred from Direct Assay		C		complete
FlyBase	Drosophila	FBgn0259174		GO:0002092	positive regulation of receptor internalization	PMID:15620649^[16]	IMP: Inferred from Mutant Phenotype		P		complete
FlyBase	Drosophila	FBgn0259174		GO:0045746	negative regulation of Notch signaling pathway	PMID:15620649^[16]	IGI: Inferred from Genetic Interaction	FB:FBgn0004647	P		complete
FlyBase	Drosophila	FBgn0259174		GO:0005938	cell cortex	PMID:15620649^[16]	IDA: Inferred from Direct Assay		C		complete
FlyBase	Drosophila	FBgn0259174		GO:0016567	protein ubiquitination	PMID:15620649^[16]	IMP: Inferred from Mutant Phenotype		P		complete
DictyBase	Dicty									no ortholog in Dicty	required field missing
FlyBase	Drosophila	FBgn0259174		GO:0019904	protein domain specific binding	PMID:15620649^[16]	IPI: Inferred from Physical Interaction	FB:FBgn0004647	F		complete
SGD	S. cerevisiae	RSP5		GO:0004842	ubiquitin-protein ligase activity	PMID:9108033^[17]	IDA: Inferred from Direct Assay		F		complete
WormBase	C.elegans	NEDD4 = Y92H12A.2 = WBGene000223358								No experimental annotations available.	required field missing
SGD	S. cerevisiae	RSP5		GO:0035091	phosphoinositide binding	PMID:15078904^[18]	IDA: Inferred from Direct Assay		F		complete
SGD	S. cerevisiae	RSP5		GO:0000209	protein polyubiquitination	PMID:9108033^[17]	IDA: Inferred from Direct Assay		P		complete
SGD	S. cerevisiae	RSP5		GO:0006513	protein monoubiquitination	PMID:14761940^[19]	IGI: Inferred from Genetic Interaction	RVS167	P		complete
SGD	S. cerevisiae	RSP5		GO:0042787	protein ubiquitination during ubiquitin-dependent protein catabolic process	PMID:9614172^[20]	IMP: Inferred from Mutant Phenotype		P		complete
SGD	S. cerevisiae	RSP5		GO:0043162	ubiquitin-dependent protein catabolic process via the multivesicular body pathway	PMID:17344478^[21]	IMP: Inferred from Mutant Phenotype		P		complete
SGD	S. cerevisiae	RSP5		GO:0043161	proteasomal ubiquitin-dependent protein catabolic process	PMID:15713680^[22]	IPI: Inferred from Physical Interaction	HPR1	P		complete
SGD	S. cerevisiae	RSP5		GO:0032511	late endosome to vacuole transport via multivesicular body sorting pathway	PMID:17182849^[23]	IMP: Inferred from Mutant Phenotype		P		complete
SGD	S. cerevisiae	RSP5		GO:0032880	regulation of protein localization	PMID:12867034^[24]	IMP: Inferred from Mutant Phenotype		P		complete
SGD	S. cerevisiae	RSP5		GO:0048260	positive regulation of receptor-mediated endocytosis	PMID:11179425^[25]	IMP: Inferred from Mutant Phenotype		P		complete
SGD	S. cerevisiae	RSP5		GO:0045807	positive regulation of endocytosis	PMID:12654912^[26]	IDA: Inferred from Direct Assay		P		complete
SGD	S. cerevisiae	RSP5		GO:0045723	positive regulation of fatty acid biosynthetic process	PMID:11007476^[27]	IMP: Inferred from Mutant Phenotype		P		complete
SGD	S. cerevisiae	RSP5		GO:0006333	chromatin assembly or disassembly	PMID:12399376^[28]	IMP: Inferred from Mutant Phenotype		P		complete
SGD	S. cerevisiae	RSP5		GO:0034517	ribophagy	PMID:18670191^[29]	IGI: Inferred from Genetic Interaction	UBP3	P		complete
SGD	S. cerevisiae	RSP5		GO:0000055	ribosomal large subunit export from nucleus	PMID:14608372^[30]	IMP: Inferred from Mutant Phenotype		P		complete
SGD	S. cerevisiae	RSP5		GO:0006409	tRNA export from nucleus	PMID:14608372^[30]	IMP: Inferred from Mutant Phenotype		P		complete
SGD	S. cerevisiae	RSP5		GO:0008033	tRNA processing	PMID:14608372^[30]	IMP: Inferred from Mutant Phenotype		P		complete
SGD	S. cerevisiae	RSP5		GO:0006364	rRNA processing	PMID:14608372^[30]	IMP: Inferred from Mutant Phenotype		P		complete
SGD	S. cerevisiae	RSP5		GO:0034644	cellular response to UV	PMID:10490634^[31]	IMP: Inferred from Mutant Phenotype		P		complete
SGD	S. cerevisiae	RSP5		GO:0042493	response to drug	PMID:12163175^[32]	IPI: Inferred from Physical Interaction	ROD1	P		complete
SGD	S. cerevisiae	RSP5		GO:0007005	mitochondrion organization	PMID:10366593^[33]	IGI: Inferred from Genetic Interaction	MDM1	P		complete
SGD	S. cerevisiae	RSP5		GO:0032443	regulation of ergosterol biosynthetic process	PMID:18771750^[34]	IGI: Inferred from Genetic Interaction	SPT23\|MGA2	P		complete
SGD	S. cerevisiae	RSP5		GO:0032956	regulation of actin cytoskeleton organization and biogenesis	PMID:15855235^[35]	IGI: Inferred from Genetic Interaction	END3	P		complete
SGD	S. cerevisiae	RSP5		GO:0006808	regulation of nitrogen utilization	PMID:15247235^[36]	IGI: Inferred from Genetic Interaction	NPR1	P		complete
SGD	S. cerevisiae	RSP5		GO:0019220	regulation of phosphate metabolic process	PMID:18165238^[37]	IGI: Inferred from Genetic Interaction	PHO4	P		complete
SGD	S. cerevisiae	RSP5		GO:0000151	ubiquitin ligase complex	PMID:9931424^[38]	IPI: Inferred from Physical Interaction	BUL1	C		complete
SGD	S. cerevisiae	RSP5		GO:0005739	mitochondrion	PMID:16823961^[39] PMID:14576278^[40]	IDA: Inferred from Direct Assay		C		complete
SGD	S. cerevisiae	RSP5		GO:0005737	cytoplasm	PMID:14657247^[41] PMID:15078904^[18]	IDA: Inferred from Direct Assay		C		complete
SGD	S. cerevisiae	RSP5		GO:0010008	endosome membrane	PMID:14657247^[41]	IDA: Inferred from Direct Assay		C		complete
SGD	S. cerevisiae	RSP5		GO:0005794	Golgi apparatus	PMID:14657247^[41]	IDA: Inferred from Direct Assay		C		complete
SGD	S. cerevisiae	RSP5		GO:0031234	extrinsic to internal side of plasma membrane	PMID:15078904^[18]	IDA: Inferred from Direct Assay		C		complete
SGD	S. cerevisiae	RSP5		GO:0005634	nucleus	PMID:14608372^[30]	IDA: Inferred from Direct Assay		C		complete
SGD	S. cerevisiae	RSP5		GO:0005934	cellular bud tip	PMID:14608372^[30]	IDA: Inferred from Direct Assay		C		complete
FlyBase	Drosophila	FBgn0259174		GO:0045746	negative regulation of Notch signaling pathway	PMID:15620650^[42]	IMP: Inferred from Mutant Phenotype		P		complete
FlyBase	Drosophila	FBgn0259174		GO:0005515	protein binding	PMID:12165468^[43]	IPI: Inferred from Physical Interaction	FB:FBgn0010105	F		complete
FlyBase	Drosophila	FBgn0259174		GO:0016567	protein ubiquitination	PMID:12165468^[43]	IDA: Inferred from Direct Assay		P		complete
FlyBase	Drosophila	FBgn0259174	NOT	GO:0007411	axon guidance	PMID:15657595^[44]	IMP: Inferred from Mutant Phenotype		P		complete
FlyBase	Drosophila	FBgn0259174		GO:0007411	axon guidance	PMID:12165468^[43]	IMP: Inferred from Mutant Phenotype		P		complete
BHF-UCL	Human	P46934		GO:0009405	pathogenesis	PMID:15126635^[13]	IMP: Inferred from Mutant Phenotype		P		complete
FlyBase	Drosophila	FBgn0259174		GO:0045807	positive regulation of endocytosis	PMID:12165468^[43]	IMP: Inferred from Mutant Phenotype		P		complete
BHF-UCL	Human	P46934		GO:0019089	transmission of virus	PMID:15126635^[13]	IMP: Inferred from Mutant Phenotype		P		complete
BHF-UCL	Human	P46934		GO:0052171	growth or development during symbiotic interaction	PMID:15126635^[13]	IMP: Inferred from Mutant Phenotype		P		complete
MGI	Mouse	Nedd4		GO:0005515	protein binding	PMID:10446181^[45]	IPI: Inferred from Physical Interaction	UniProtKB:Q60760	F		complete
MGI	Mouse	Nedd4		GO:0004842	ubiquitin-protein ligase activity	PMID:9182527^[46]	IDA: Inferred from Direct Assay		F		complete
MGI	Mouse	Nedd4		GO:0005829	cytosol	PMID:9182527^[46]	IDA: Inferred from Direct Assay		C		complete
MGI	Mouse	Nedd4		GO:0000151	ubiquitin ligase complex	PMID:11042109^[47]	IPI: Inferred from Physical Interaction	UniProtKB:Q9QYK7	C		complete
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Notes

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NEDD4

SGD: receptor-mediated endocytosis vs. ubiquitin-mediated endocytosis Should these be two different processes in GO? Are they different enough? The definition of RME in GO refers to ligand binding, but this doesn't always happen.

Action Item: SGD will submit a new term request to SourceForge for ubiquitin- mediated endocytosis.

SGD: RSP5/NEDD4, a ubiquitin ligase, directly ubiquitinates many targets that are involved in many different processes. Should RSP5 be annotated, then, to regulation of each of these processes?

For example, ergosterol biosynthesis. If a mutation in RSP5 results in loss of ergosterol biosynthesis, then it seems reasonable to annotate RSP5 to regulation of ergosterol biosynthesis with an IMP evidence code.

High throughput experiments show many proteins ubiquitinated by RSP5. Without other experiments, is it appropriate to annotate RSP5 to regulation of any of the processes in which the target proteins are involved?

Consensus seemed to be no; in the absence of other experimental data (i.e. mutant phenotypes) making this type of annotation wouldn't be appropriate.

GOA: If NEDD4 ubiquitinates a protein, is it appropriate to annotate to protein binding to capture the target?

Some groups capture targets in comments, but should targets be captured more explicitly with the MF annotation?

An analogous situation would be capturing enzyme and substrate interactions with a binding term.

In the past, there's been an understanding that if a physical interaction was transient, for example, an enzyme substrate interaction, then we haven't captured that binding interaction in GO.

However, how does this differ from a kinases being annotated to ATP binding, an annotation that *is* made in GO? (see InterPro2GO mappings, also)

Couldn't the relationship between kinase activity and ATP binding be captured in the ontology, i.e. kinase activity would be a child term of ATP binding?

Since not all kinases bind ATP, such a relationship would violate the true path rule.

But if we are going to annotate kinases that bind ATP to that MF term, we need to be consistent with other binding annotations.

Action Item: Put the issue of consistently annotating to binding terms on the agenda for the Montreal meeting.

Human and yeast NEDD4 proteins were annotated to many different BP terms. What are the appropriate terms for other groups to consider making ISS annotations?

Generally, MF and CC terms are more easily transferred for ISS annotations, but curators need to use discretion when making ISS annotations to BP terms. For example, it would be approrpiate to annotate a kinase to the BP term phosphorylation, but other processes would need to be assessed in the context of each organism and its biology.

The issue of automatic ISS annotations was raised. What is really meant by 'automatic ISS' and are these annotations ever appropriate?

The October 2008 electronic jamboree also annotated PFKL.

References

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See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 ^1.6 Anindya, R et al. (2007) Damage-induced ubiquitylation of human RNA polymerase II by the ubiquitin ligase Nedd4, but not Cockayne syndrome proteins or BRCA1. Mol. Cell 28 386-97 PubMed GONUTS page
↑ ^2.0 ^2.1 Imhof, MO & McDonnell, DP (1996) Yeast RSP5 and its human homolog hRPF1 potentiate hormone-dependent activation of transcription by human progesterone and glucocorticoid receptors. Mol. Cell. Biol. 16 2594-605 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 Anan, T et al. (1998) Human ubiquitin-protein ligase Nedd4: expression, subcellular localization and selective interaction with ubiquitin-conjugating enzymes. Genes Cells 3 751-63 PubMed GONUTS page
↑ ^4.0 ^4.1 Wang, X et al. (2007) NEDD4-1 is a proto-oncogenic ubiquitin ligase for PTEN. Cell 128 129-39 PubMed GONUTS page
↑ Trotman, LC et al. (2007) Ubiquitination regulates PTEN nuclear import and tumor suppression. Cell 128 141-56 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 ^6.3 Shenoy, SK et al. (2008) Nedd4 mediates agonist-dependent ubiquitination, lysosomal targeting, and degradation of the beta2-adrenergic receptor. J. Biol. Chem. 283 22166-76 PubMed GONUTS page
↑ Pak, Y et al. (2006) Transport of LAPTM5 to lysosomes requires association with the ubiquitin ligase Nedd4, but not LAPTM5 ubiquitination. J. Cell Biol. 175 631-45 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 ^8.4 Farr, TJ et al. (2000) Human Nedd4 interacts with the human epithelial Na+ channel: WW3 but not WW1 binds to Na+-channel subunits. Biochem. J. 345 Pt 3 503-9 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 ^9.3 Ing, B et al. (2007) Regulation of Commissureless by the ubiquitin ligase DNedd4 is required for neuromuscular synaptogenesis in Drosophila melanogaster. Mol. Cell. Biol. 27 481-96 PubMed GONUTS page
↑ Gavva, NR et al. (1997) Interaction of WW domains with hematopoietic transcription factor p45/NF-E2 and RNA polymerase II. J. Biol. Chem. 272 24105-8 PubMed GONUTS page
↑ ^11.0 ^11.1 Cristillo, AD et al. (2003) Cloning and characterization of N4WBP5A, an inducible, cyclosporine-sensitive, Nedd4-binding protein in human T lymphocytes. J. Biol. Chem. 278 34587-97 PubMed GONUTS page
↑ Kanelis, V et al. (2006) Structural determinants for high-affinity binding in a Nedd4 WW3* domain-Comm PY motif complex. Structure 14 543-53 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 ^13.3 ^13.4 Blot, V et al. (2004) Nedd4.1-mediated ubiquitination and subsequent recruitment of Tsg101 ensure HTLV-1 Gag trafficking towards the multivesicular body pathway prior to virus budding. J. Cell. Sci. 117 2357-67 PubMed GONUTS page
↑ Xu, LL et al. (2003) PMEPA1, an androgen-regulated NEDD4-binding protein, exhibits cell growth inhibitory function and decreased expression during prostate cancer progression. Cancer Res. 63 4299-304 PubMed GONUTS page
↑ Hamilton, MH et al. (2001) Nuclear import/export of hRPF1/Nedd4 regulates the ubiquitin-dependent degradation of its nuclear substrates. J. Biol. Chem. 276 26324-31 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 ^16.3 ^16.4 Sakata, T et al. (2004) Drosophila Nedd4 regulates endocytosis of notch and suppresses its ligand-independent activation. Curr. Biol. 14 2228-36 PubMed GONUTS page
↑ ^17.0 ^17.1 Huibregtse, JM et al. (1997) The large subunit of RNA polymerase II is a substrate of the Rsp5 ubiquitin-protein ligase. Proc. Natl. Acad. Sci. U.S.A. 94 3656-61 PubMed GONUTS page
↑ ^18.0 ^18.1 ^18.2 Dunn, R et al. (2004) The C2 domain of the Rsp5 ubiquitin ligase binds membrane phosphoinositides and directs ubiquitination of endosomal cargo. J. Cell Biol. 165 135-44 PubMed GONUTS page
↑ Stamenova, SD et al. (2004) The Rsp5 ubiquitin ligase binds to and ubiquitinates members of the yeast CIN85-endophilin complex, Sla1-Rvs167. J. Biol. Chem. 279 16017-25 PubMed GONUTS page
↑ Springael, JY & André, B (1998) Nitrogen-regulated ubiquitination of the Gap1 permease of Saccharomyces cerevisiae. Mol. Biol. Cell 9 1253-63 PubMed GONUTS page
↑ Kim, Y et al. (2007) GGA2- and ubiquitin-dependent trafficking of Arn1, the ferrichrome transporter of Saccharomyces cerevisiae. Mol. Biol. Cell 18 1790-802 PubMed GONUTS page
↑ Gwizdek, C et al. (2005) The mRNA nuclear export factor Hpr1 is regulated by Rsp5-mediated ubiquitylation. J. Biol. Chem. 280 13401-5 PubMed GONUTS page
↑ Oestreich, AJ et al. (2007) Characterization of multiple multivesicular body sorting determinants within Sna3: a role for the ubiquitin ligase Rsp5. Mol. Biol. Cell 18 707-20 PubMed GONUTS page
↑ Shcherbik, N et al. (2003) Rsp5p is required for ER bound Mga2p120 polyubiquitination and release of the processed/tethered transactivator Mga2p90. Curr. Biol. 13 1227-33 PubMed GONUTS page
↑ Dunn, R & Hicke, L (2001) Domains of the Rsp5 ubiquitin-protein ligase required for receptor-mediated and fluid-phase endocytosis. Mol. Biol. Cell 12 421-35 PubMed GONUTS page
↑ Davies, BA et al. (2003) Vps9p CUE domain ubiquitin binding is required for efficient endocytic protein traffic. J. Biol. Chem. 278 19826-33 PubMed GONUTS page
↑ Hoppe, T et al. (2000) Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing. Cell 102 577-86 PubMed GONUTS page
↑ Harkness, TA et al. (2002) The ubiquitin-dependent targeting pathway in Saccharomyces cerevisiae plays a critical role in multiple chromatin assembly regulatory steps. Genetics 162 615-32 PubMed GONUTS page
↑ Kraft, C & Peter, M (2008) Is the Rsp5 ubiquitin ligase involved in the regulation of ribophagy? Autophagy 4 838-40 PubMed GONUTS page
↑ ^30.0 ^30.1 ^30.2 ^30.3 ^30.4 ^30.5 Neumann, S et al. (2003) Formation and nuclear export of tRNA, rRNA and mRNA is regulated by the ubiquitin ligase Rsp5p. EMBO Rep. 4 1156-62 PubMed GONUTS page
↑ Beaudenon, SL et al. (1999) Rsp5 ubiquitin-protein ligase mediates DNA damage-induced degradation of the large subunit of RNA polymerase II in Saccharomyces cerevisiae. Mol. Cell. Biol. 19 6972-9 PubMed GONUTS page
↑ Andoh, T et al. (2002) PY motifs of Rod1 are required for binding to Rsp5 and for drug resistance. FEBS Lett. 525 131-4 PubMed GONUTS page
↑ Fisk, HA & Yaffe, MP (1999) A role for ubiquitination in mitochondrial inheritance in Saccharomyces cerevisiae. J. Cell Biol. 145 1199-208 PubMed GONUTS page
↑ Kaliszewski, P et al. (2008) Rsp5p ubiquitin ligase and the transcriptional activators Spt23p and Mga2p are involved in co-regulation of biosynthesis of end products of the mevalonate pathway and triacylglycerol in yeast Saccharomyces cerevisiae. Biochim. Biophys. Acta 1781 627-34 PubMed GONUTS page
↑ Gourlay, CW & Ayscough, KR (2005) Identification of an upstream regulatory pathway controlling actin-mediated apoptosis in yeast. J. Cell. Sci. 118 2119-32 PubMed GONUTS page
↑ Crespo, JL et al. (2004) NPR1 kinase and RSP5-BUL1/2 ubiquitin ligase control GLN3-dependent transcription in Saccharomyces cerevisiae. J. Biol. Chem. 279 37512-7 PubMed GONUTS page
↑ Estrella, LA et al. (2008) The Rsp5 E3 ligase mediates turnover of low affinity phosphate transporters in Saccharomyces cerevisiae. J. Biol. Chem. 283 5327-34 PubMed GONUTS page
↑ Yashiroda, H et al. (1998) The PY-motif of Bul1 protein is essential for growth of Saccharomyces cerevisiae under various stress conditions. Gene 225 39-46 PubMed GONUTS page
↑ Reinders, J et al. (2006) Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J. Proteome Res. 5 1543-54 PubMed GONUTS page
↑ Sickmann, A et al. (2003) The proteome of Saccharomyces cerevisiae mitochondria. Proc. Natl. Acad. Sci. U.S.A. 100 13207-12 PubMed GONUTS page
↑ ^41.0 ^41.1 ^41.2 Katzmann, DJ et al. (2004) Multivesicular body sorting: ubiquitin ligase Rsp5 is required for the modification and sorting of carboxypeptidase S. Mol. Biol. Cell 15 468-80 PubMed GONUTS page
↑ Wilkin, MB et al. (2004) Regulation of notch endosomal sorting and signaling by Drosophila Nedd4 family proteins. Curr. Biol. 14 2237-44 PubMed GONUTS page
↑ ^43.0 ^43.1 ^43.2 ^43.3 Myat, A et al. (2002) Drosophila Nedd4, a ubiquitin ligase, is recruited by Commissureless to control cell surface levels of the roundabout receptor. Neuron 35 447-59 PubMed GONUTS page
↑ Keleman, K et al. (2005) Comm function in commissural axon guidance: cell-autonomous sorting of Robo in vivo. Nat. Neurosci. 8 156-63 PubMed GONUTS page
↑ Morrione, A et al. (1999) mGrb10 interacts with Nedd4. J. Biol. Chem. 274 24094-9 PubMed GONUTS page
↑ ^46.0 ^46.1 Hatakeyama, S et al. (1997) Subcellular localization and ubiquitin-conjugating enzyme (E2) interactions of mammalian HECT family ubiquitin protein ligases. J. Biol. Chem. 272 15085-92 PubMed GONUTS page
↑ Jolliffe, CN et al. (2000) Identification of multiple proteins expressed in murine embryos as binding partners for the WW domains of the ubiquitin-protein ligase Nedd4. Biochem. J. 351 Pt 3 557-65 PubMed GONUTS page

[PMID:17996703-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 ^1.6 Anindya, R et al. (2007) Damage-induced ubiquitylation of human RNA polymerase II by the ubiquitin ligase Nedd4, but not Cockayne syndrome proteins or BRCA1. Mol. Cell 28 386-97 PubMed GONUTS page

[PMID:8649367-2] 2.0 ^2.1 Imhof, MO & McDonnell, DP (1996) Yeast RSP5 and its human homolog hRPF1 potentiate hormone-dependent activation of transcription by human progesterone and glucocorticoid receptors. Mol. Cell. Biol. 16 2594-605 PubMed GONUTS page

[PMID:9990509-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 Anan, T et al. (1998) Human ubiquitin-protein ligase Nedd4: expression, subcellular localization and selective interaction with ubiquitin-conjugating enzymes. Genes Cells 3 751-63 PubMed GONUTS page

[PMID:17218260-4] 4.0 ^4.1 Wang, X et al. (2007) NEDD4-1 is a proto-oncogenic ubiquitin ligase for PTEN. Cell 128 129-39 PubMed GONUTS page

[PMID:17218261-5] Trotman, LC et al. (2007) Ubiquitination regulates PTEN nuclear import and tumor suppression. Cell 128 141-56 PubMed GONUTS page

[PMID:18544533-6] 6.0 ^6.1 ^6.2 ^6.3 Shenoy, SK et al. (2008) Nedd4 mediates agonist-dependent ubiquitination, lysosomal targeting, and degradation of the beta2-adrenergic receptor. J. Biol. Chem. 283 22166-76 PubMed GONUTS page

[PMID:17116753-7] Pak, Y et al. (2006) Transport of LAPTM5 to lysosomes requires association with the ubiquitin ligase Nedd4, but not LAPTM5 ubiquitination. J. Cell Biol. 175 631-45 PubMed GONUTS page

[PMID:10642508-8] 8.0 ^8.1 ^8.2 ^8.3 ^8.4 Farr, TJ et al. (2000) Human Nedd4 interacts with the human epithelial Na+ channel: WW3 but not WW1 binds to Na+-channel subunits. Biochem. J. 345 Pt 3 503-9 PubMed GONUTS page

[PMID:17074801-9] 9.0 ^9.1 ^9.2 ^9.3 Ing, B et al. (2007) Regulation of Commissureless by the ubiquitin ligase DNedd4 is required for neuromuscular synaptogenesis in Drosophila melanogaster. Mol. Cell. Biol. 27 481-96 PubMed GONUTS page

[PMID:9305852-10] Gavva, NR et al. (1997) Interaction of WW domains with hematopoietic transcription factor p45/NF-E2 and RNA polymerase II. J. Biol. Chem. 272 24105-8 PubMed GONUTS page

[PMID:12796489-11] 11.0 ^11.1 Cristillo, AD et al. (2003) Cloning and characterization of N4WBP5A, an inducible, cyclosporine-sensitive, Nedd4-binding protein in human T lymphocytes. J. Biol. Chem. 278 34587-97 PubMed GONUTS page

[PMID:16531238-12] Kanelis, V et al. (2006) Structural determinants for high-affinity binding in a Nedd4 WW3* domain-Comm PY motif complex. Structure 14 543-53 PubMed GONUTS page

[PMID:15126635-13] 13.0 ^13.1 ^13.2 ^13.3 ^13.4 Blot, V et al. (2004) Nedd4.1-mediated ubiquitination and subsequent recruitment of Tsg101 ensure HTLV-1 Gag trafficking towards the multivesicular body pathway prior to virus budding. J. Cell. Sci. 117 2357-67 PubMed GONUTS page

[PMID:12907594-14] Xu, LL et al. (2003) PMEPA1, an androgen-regulated NEDD4-binding protein, exhibits cell growth inhibitory function and decreased expression during prostate cancer progression. Cancer Res. 63 4299-304 PubMed GONUTS page

[PMID:11342538-15] Hamilton, MH et al. (2001) Nuclear import/export of hRPF1/Nedd4 regulates the ubiquitin-dependent degradation of its nuclear substrates. J. Biol. Chem. 276 26324-31 PubMed GONUTS page

[PMID:15620649-16] 16.0 ^16.1 ^16.2 ^16.3 ^16.4 Sakata, T et al. (2004) Drosophila Nedd4 regulates endocytosis of notch and suppresses its ligand-independent activation. Curr. Biol. 14 2228-36 PubMed GONUTS page

[PMID:9108033-17] 17.0 ^17.1 Huibregtse, JM et al. (1997) The large subunit of RNA polymerase II is a substrate of the Rsp5 ubiquitin-protein ligase. Proc. Natl. Acad. Sci. U.S.A. 94 3656-61 PubMed GONUTS page

[PMID:15078904-18] 18.0 ^18.1 ^18.2 Dunn, R et al. (2004) The C2 domain of the Rsp5 ubiquitin ligase binds membrane phosphoinositides and directs ubiquitination of endosomal cargo. J. Cell Biol. 165 135-44 PubMed GONUTS page

[PMID:14761940-19] Stamenova, SD et al. (2004) The Rsp5 ubiquitin ligase binds to and ubiquitinates members of the yeast CIN85-endophilin complex, Sla1-Rvs167. J. Biol. Chem. 279 16017-25 PubMed GONUTS page

[PMID:9614172-20] Springael, JY & André, B (1998) Nitrogen-regulated ubiquitination of the Gap1 permease of Saccharomyces cerevisiae. Mol. Biol. Cell 9 1253-63 PubMed GONUTS page

[PMID:17344478-21] Kim, Y et al. (2007) GGA2- and ubiquitin-dependent trafficking of Arn1, the ferrichrome transporter of Saccharomyces cerevisiae. Mol. Biol. Cell 18 1790-802 PubMed GONUTS page

[PMID:15713680-22] Gwizdek, C et al. (2005) The mRNA nuclear export factor Hpr1 is regulated by Rsp5-mediated ubiquitylation. J. Biol. Chem. 280 13401-5 PubMed GONUTS page

[PMID:17182849-23] Oestreich, AJ et al. (2007) Characterization of multiple multivesicular body sorting determinants within Sna3: a role for the ubiquitin ligase Rsp5. Mol. Biol. Cell 18 707-20 PubMed GONUTS page

[PMID:12867034-24] Shcherbik, N et al. (2003) Rsp5p is required for ER bound Mga2p120 polyubiquitination and release of the processed/tethered transactivator Mga2p90. Curr. Biol. 13 1227-33 PubMed GONUTS page

[PMID:11179425-25] Dunn, R & Hicke, L (2001) Domains of the Rsp5 ubiquitin-protein ligase required for receptor-mediated and fluid-phase endocytosis. Mol. Biol. Cell 12 421-35 PubMed GONUTS page

[PMID:12654912-26] Davies, BA et al. (2003) Vps9p CUE domain ubiquitin binding is required for efficient endocytic protein traffic. J. Biol. Chem. 278 19826-33 PubMed GONUTS page

[PMID:11007476-27] Hoppe, T et al. (2000) Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing. Cell 102 577-86 PubMed GONUTS page

[PMID:12399376-28] Harkness, TA et al. (2002) The ubiquitin-dependent targeting pathway in Saccharomyces cerevisiae plays a critical role in multiple chromatin assembly regulatory steps. Genetics 162 615-32 PubMed GONUTS page

[PMID:18670191-29] Kraft, C & Peter, M (2008) Is the Rsp5 ubiquitin ligase involved in the regulation of ribophagy? Autophagy 4 838-40 PubMed GONUTS page

[PMID:14608372-30] 30.0 ^30.1 ^30.2 ^30.3 ^30.4 ^30.5 Neumann, S et al. (2003) Formation and nuclear export of tRNA, rRNA and mRNA is regulated by the ubiquitin ligase Rsp5p. EMBO Rep. 4 1156-62 PubMed GONUTS page

[PMID:10490634-31] Beaudenon, SL et al. (1999) Rsp5 ubiquitin-protein ligase mediates DNA damage-induced degradation of the large subunit of RNA polymerase II in Saccharomyces cerevisiae. Mol. Cell. Biol. 19 6972-9 PubMed GONUTS page

[PMID:12163175-32] Andoh, T et al. (2002) PY motifs of Rod1 are required for binding to Rsp5 and for drug resistance. FEBS Lett. 525 131-4 PubMed GONUTS page

[PMID:10366593-33] Fisk, HA & Yaffe, MP (1999) A role for ubiquitination in mitochondrial inheritance in Saccharomyces cerevisiae. J. Cell Biol. 145 1199-208 PubMed GONUTS page

[PMID:18771750-34] Kaliszewski, P et al. (2008) Rsp5p ubiquitin ligase and the transcriptional activators Spt23p and Mga2p are involved in co-regulation of biosynthesis of end products of the mevalonate pathway and triacylglycerol in yeast Saccharomyces cerevisiae. Biochim. Biophys. Acta 1781 627-34 PubMed GONUTS page

[PMID:15855235-35] Gourlay, CW & Ayscough, KR (2005) Identification of an upstream regulatory pathway controlling actin-mediated apoptosis in yeast. J. Cell. Sci. 118 2119-32 PubMed GONUTS page

[PMID:15247235-36] Crespo, JL et al. (2004) NPR1 kinase and RSP5-BUL1/2 ubiquitin ligase control GLN3-dependent transcription in Saccharomyces cerevisiae. J. Biol. Chem. 279 37512-7 PubMed GONUTS page

[PMID:18165238-37] Estrella, LA et al. (2008) The Rsp5 E3 ligase mediates turnover of low affinity phosphate transporters in Saccharomyces cerevisiae. J. Biol. Chem. 283 5327-34 PubMed GONUTS page

[PMID:9931424-38] Yashiroda, H et al. (1998) The PY-motif of Bul1 protein is essential for growth of Saccharomyces cerevisiae under various stress conditions. Gene 225 39-46 PubMed GONUTS page

[PMID:16823961-39] Reinders, J et al. (2006) Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J. Proteome Res. 5 1543-54 PubMed GONUTS page

[PMID:14576278-40] Sickmann, A et al. (2003) The proteome of Saccharomyces cerevisiae mitochondria. Proc. Natl. Acad. Sci. U.S.A. 100 13207-12 PubMed GONUTS page

[PMID:14657247-41] 41.0 ^41.1 ^41.2 Katzmann, DJ et al. (2004) Multivesicular body sorting: ubiquitin ligase Rsp5 is required for the modification and sorting of carboxypeptidase S. Mol. Biol. Cell 15 468-80 PubMed GONUTS page

[PMID:15620650-42] Wilkin, MB et al. (2004) Regulation of notch endosomal sorting and signaling by Drosophila Nedd4 family proteins. Curr. Biol. 14 2237-44 PubMed GONUTS page

[PMID:12165468-43] 43.0 ^43.1 ^43.2 ^43.3 Myat, A et al. (2002) Drosophila Nedd4, a ubiquitin ligase, is recruited by Commissureless to control cell surface levels of the roundabout receptor. Neuron 35 447-59 PubMed GONUTS page

[PMID:15657595-44] Keleman, K et al. (2005) Comm function in commissural axon guidance: cell-autonomous sorting of Robo in vivo. Nat. Neurosci. 8 156-63 PubMed GONUTS page

[PMID:10446181-45] Morrione, A et al. (1999) mGrb10 interacts with Nedd4. J. Biol. Chem. 274 24094-9 PubMed GONUTS page

[PMID:9182527-46] 46.0 ^46.1 Hatakeyama, S et al. (1997) Subcellular localization and ubiquitin-conjugating enzyme (E2) interactions of mammalian HECT family ubiquitin protein ligases. J. Biol. Chem. 272 15085-92 PubMed GONUTS page

[PMID:11042109-47] Jolliffe, CN et al. (2000) Identification of multiple proteins expressed in murine embryos as binding partners for the WW domains of the ubiquitin-protein ligase Nedd4. Biochem. J. 351 Pt 3 557-65 PubMed GONUTS page

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RefGenome Electronic Jamboree 2008-10 NEDD4

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