YEAST:RSP5

Species (Taxon ID)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s)	RSP5 (synonyms: MDP1, NPI1)
Protein Name(s)	E3 ubiquitin-protein ligase RSP5 Reverses SPT-phenotype protein 5
External Links
UniProt	P39940
EMBL	U18916 BK006939
PIR	S43217
RefSeq	NP_011051.3
PDB	3OLM 4LCD
PDBsum	3OLM 4LCD
ProteinModelPortal	P39940
SMR	P39940
BioGrid	36869
DIP	DIP-2238N
IntAct	P39940
MINT	MINT-520379
STRING	4932.YER125W
MaxQB	P39940
PaxDb	P39940
PeptideAtlas	P39940
EnsemblFungi	[example_ID YER125W]
GeneID	856862
KEGG	sce:YER125W
CYGD	YER125w
SGD	S000000927
eggNOG	COG5021
GeneTree	ENSGT00760000118966
HOGENOM	HOG000208451
InParanoid	P39940
KO	K10591
OMA	PNGWERR
OrthoDB	EOG735453
BioCyc	YEAST:G3O-30288-MONOMER
UniPathway	UPA00143
EvolutionaryTrace	P39940
NextBio	983216
PRO	PR:P39940
Proteomes	UP000002311
Genevestigator	P39940
GO	GO:0030479 GO:0005934 GO:0005737 GO:0010008 GO:0031234 GO:0005794 GO:0005634 GO:0000151 GO:0016874 GO:0035091 GO:0043130 GO:0004842 GO:0034644 GO:0006333 GO:0032511 GO:0007005 GO:0045807 GO:0045723 GO:0032436 GO:0048260 GO:0045944 GO:0043161 GO:0051865 GO:0006513 GO:0000209 GO:0016567 GO:0042787 GO:0032956 GO:0010794 GO:0032443 GO:0031384 GO:0010793 GO:0010796 GO:0006808 GO:0019220 GO:0032880 GO:2000203 GO:2000232 GO:2000238 GO:2000235 GO:0010795 GO:0042493 GO:0034517 GO:0070086 GO:0006511 GO:0043162
Gene3D	2.60.40.150
InterPro	IPR000008 IPR024928 IPR000569 IPR001202
Pfam	PF00168 PF00632 PF00397
PIRSF	PIRSF001569
SMART	SM00239 SM00119 SM00456
SUPFAM	SSF49562 SSF51045 SSF56204
PROSITE	PS50004 PS50237 PS01159 PS50020

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0006890	retrograde vesicle-mediated transport, Golgi to ER	PMID:22761830^[1]	ECO:0000315			P		Figure 4 shows Rsp4 mutants have impaired retrograde trafficking from Golgi to ER. Figure 7 shows similar evidence.	complete CACAO 8111
	GO:0061630	ubiquitin protein ligase activity	PMID:7708685^[2]	ECO:0000247		UniProtKB:Q05086	F		Fig 1B shows sequence alignment, including highly conserved cysteine residue necessary for Ubiquitin thioester formation.	complete CACAO 10316
	GO:0061630	ubiquitin protein ligase activity	PMID:7708685^[2]	ECO:0000315			F		Fig3 shows evidence for E3 Ubiquitin-protein ligase activty	complete CACAO 10317
part_of	GO:0005739	mitochondrion	PMID:24769239^[3]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:16823961^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:14576278^[5]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0016567	protein ubiquitination	PMID:29444958^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	part_of:(GO:0043328) has_direct_input:(UniProtKB:P27614)	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:16622836^[7]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0016973	poly(A)+ mRNA export from nucleus	PMID:27385342^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0072671	mitochondria-associated ubiquitin-dependent protein catabolic process	PMID:21070972^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_input:(UniProtKB:P07213)\|has_input:(UniProtKB:P53083)\|has_input:(UniProtKB:P28737)	Seeded From UniProt	complete
enables	GO:0004842	ubiquitin-protein transferase activity	PMID:27694912^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	has_direct_input:(UniProtKB:O94742)	Seeded From UniProt	complete
enables	GO:0004842	ubiquitin-protein transferase activity	PMID:27694912^[10]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:O94742)	Seeded From UniProt	complete
enables	GO:0061630	ubiquitin protein ligase activity	PMID:7708685^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006511	ubiquitin-dependent protein catabolic process	PMID:25344756^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	happens_during:(GO:0034605) occurs_in:(GO:0005829)	Seeded From UniProt	complete
involved_in	GO:0032436	positive regulation of proteasomal ubiquitin-dependent protein catabolic process	PMID:24962567^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	happens_during:(GO:0034605)	Seeded From UniProt	complete
involved_in	GO:0016567	protein ubiquitination	PMID:23443663^[13]	ECO:0000314	direct assay evidence used in manual assertion		P	has_direct_input:(UniProtKB:P38356)	Seeded From UniProt	complete
enables	GO:0004842	ubiquitin-protein transferase activity	PMID:23443663^[13]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:Q04195)	Seeded From UniProt	complete
enables	GO:0004842	ubiquitin-protein transferase activity	PMID:23443663^[13]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:Q12216)	Seeded From UniProt	complete
enables	GO:0004842	ubiquitin-protein transferase activity	PMID:23443663^[13]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:P38356)	Seeded From UniProt	complete
involved_in	GO:0016567	protein ubiquitination	PMID:23443663^[13]	ECO:0000314	direct assay evidence used in manual assertion		P	has_direct_input:(UniProtKB:Q12216)	Seeded From UniProt	complete
involved_in	GO:0016567	protein ubiquitination	PMID:23443663^[13]	ECO:0000314	direct assay evidence used in manual assertion		P	has_direct_input:(UniProtKB:Q04195)	Seeded From UniProt	complete
involved_in	GO:2000238	regulation of tRNA export from nucleus	PMID:14608372^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2000235	regulation of tRNA processing	PMID:14608372^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2000232	regulation of rRNA processing	PMID:14608372^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2000203	regulation of ribosomal large subunit export from nucleus	PMID:14608372^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0070086	ubiquitin-dependent endocytosis	PMID:17344478^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051865	protein autoubiquitination	PMID:24069405^[16]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000005650	P		Seeded From UniProt	complete
involved_in	GO:0048260	positive regulation of receptor-mediated endocytosis	PMID:11179425^[17]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:11007476^[18]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045807	positive regulation of endocytosis	PMID:12654912^[19]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045723	positive regulation of fatty acid biosynthetic process	PMID:11007476^[18]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043162	ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway	PMID:17344478^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043161	proteasome-mediated ubiquitin-dependent protein catabolic process	PMID:15713680^[20]	ECO:0000353	physical interaction evidence used in manual assertion	SGD:S000002545	P		Seeded From UniProt	complete
enables	GO:0043130	ubiquitin binding	PMID:19252184^[21]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006511	ubiquitin-dependent protein catabolic process	PMID:9614172^[22]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042493	response to drug	PMID:12163175^[23]	ECO:0000353	physical interaction evidence used in manual assertion	SGD:S000005544	P		Seeded From UniProt	complete
involved_in	GO:0042493	response to drug	PMID:12163175^[23]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0035091	phosphatidylinositol binding	PMID:15078904^[24]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0034644	cellular response to UV	PMID:10490634^[25]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034517	ribophagy	PMID:18670191^[26]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000000953	P		Seeded From UniProt	complete
involved_in	GO:0032956	regulation of actin cytoskeleton organization	PMID:15855235^[27]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000005028	P		Seeded From UniProt	complete
involved_in	GO:0032880	regulation of protein localization	PMID:12867034^[28]	ECO:0000353	physical interaction evidence used in manual assertion	SGD:S000001472	P		Seeded From UniProt	complete
involved_in	GO:0032880	regulation of protein localization	PMID:12867034^[28]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032511	late endosome to vacuole transport via multivesicular body sorting pathway	PMID:17182849^[29]	ECO:0000353	physical interaction evidence used in manual assertion	SGD:S000003687	P		Seeded From UniProt	complete
involved_in	GO:0032511	late endosome to vacuole transport via multivesicular body sorting pathway	PMID:17182849^[29]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032443	regulation of ergosterol biosynthetic process	PMID:18771750^[30]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000001472 SGD:S000001503	P		Seeded From UniProt	complete
involved_in	GO:0032443	regulation of ergosterol biosynthetic process	PMID:18771750^[30]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031384	regulation of initiation of mating projection growth	PMID:21685393^[31]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	part_of:(GO:0000749)	Seeded From UniProt	complete
part_of	GO:0031234	extrinsic component of cytoplasmic side of plasma membrane	PMID:15078904^[24]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0019220	regulation of phosphate metabolic process	PMID:18165238^[32]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000001930	P		Seeded From UniProt	complete
involved_in	GO:0010796	regulation of multivesicular body size	PMID:17182850^[33]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010795	regulation of ubiquinone biosynthetic process	PMID:18771750^[30]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000001472 SGD:S000001503	P		Seeded From UniProt	complete
involved_in	GO:0010795	regulation of ubiquinone biosynthetic process	PMID:18771750^[30]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010794	regulation of dolichol biosynthetic process	PMID:18771750^[30]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000001472 SGD:S000001503	P		Seeded From UniProt	complete
involved_in	GO:0010794	regulation of dolichol biosynthetic process	PMID:18771750^[30]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010793	regulation of mRNA export from nucleus	PMID:15713680^[20]	ECO:0000353	physical interaction evidence used in manual assertion	SGD:S000002545	P		Seeded From UniProt	complete
involved_in	GO:0010793	regulation of mRNA export from nucleus	PMID:14608372^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0010008	endosome membrane	PMID:14657247^[34]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0007005	mitochondrion organization	PMID:10366593^[35]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000004572	P		Seeded From UniProt	complete
involved_in	GO:0007005	mitochondrion organization	PMID:10366593^[35]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006808	regulation of nitrogen utilization	PMID:15247235^[36]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000005127	P		Seeded From UniProt	complete
involved_in	GO:0006513	protein monoubiquitination	PMID:19176477^[37]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000001047	P		Seeded From UniProt	complete
involved_in	GO:0006513	protein monoubiquitination	PMID:14761940^[38]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000002796	P		Seeded From UniProt	complete
involved_in	GO:0006513	protein monoubiquitination	PMID:21685393^[31]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	part_of:(GO:0000749)	Seeded From UniProt	complete
involved_in	GO:0006513	protein monoubiquitination	PMID:19176477^[37]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006513	protein monoubiquitination	PMID:14761940^[38]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006513	protein monoubiquitination	PMID:21685393^[31]	ECO:0000314	direct assay evidence used in manual assertion		P	has_direct_input:(UniProtKB:P18851)	Seeded From UniProt	complete
involved_in	GO:0006513	protein monoubiquitination	PMID:19176477^[37]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006333	chromatin assembly or disassembly	PMID:12399376^[39]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005934	cellular bud tip	PMID:14608372^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005794	Golgi apparatus	PMID:14657247^[34]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:14657247^[34]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:15078904^[24]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:14608372^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004842	ubiquitin-protein transferase activity	PMID:21685393^[31]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	has_direct_input:(UniProtKB:P18851)	Seeded From UniProt	complete
enables	GO:0004842	ubiquitin-protein transferase activity	PMID:9108033^[40]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004842	ubiquitin-protein transferase activity	PMID:21685393^[31]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:P18851)	Seeded From UniProt	complete
enables	GO:0004842	ubiquitin-protein transferase activity	PMID:9108033^[40]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:P04050)	Seeded From UniProt	complete
involved_in	GO:0000209	protein polyubiquitination	PMID:9108033^[40]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000209	protein polyubiquitination	PMID:9108033^[40]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0000151	ubiquitin ligase complex	PMID:9931424^[41]	ECO:0000353	physical interaction evidence used in manual assertion	SGD:S000004888	C		Seeded From UniProt	complete
enables	GO:0061630	ubiquitin protein ligase activity	PMID:21873635^[42]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0259174 MGI:MGI:1861728 MGI:MGI:1914144 MGI:MGI:1933754 MGI:MGI:97297 PANTHER:PTN000134256 PomBase:SPAC11G7.02 PomBase:SPAC1805.15c UniProtKB:P46934 UniProtKB:Q96J02 UniProtKB:Q9HCE7	F		Seeded From UniProt	complete
involved_in	GO:0045732	positive regulation of protein catabolic process	PMID:21873635^[42]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1202301 MGI:MGI:97297 PANTHER:PTN000134745 RGD:735047 UniProtKB:P46934	P		Seeded From UniProt	complete
involved_in	GO:0043328	protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway	PMID:21873635^[42]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000882953 UniProtKB:Q5BDP1	P		Seeded From UniProt	complete
involved_in	GO:0043161	proteasome-mediated ubiquitin-dependent protein catabolic process	PMID:21873635^[42]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1861728 MGI:MGI:1914144 PANTHER:PTN000134745 SGD:S000000927 UniProtKB:O00308 UniProtKB:Q96PU5 UniProtKB:Q9HCE7	P		Seeded From UniProt	complete
involved_in	GO:0016567	protein ubiquitination	PMID:21873635^[42]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0259174 MGI:MGI:1861728 MGI:MGI:1914144 MGI:MGI:1923038 MGI:MGI:97297 PANTHER:PTN000134256 SGD:S000000927 SGD:S000002865 TAIR:locus:2135630 UniProtKB:O00308 UniProtKB:P46934 UniProtKB:Q5BDP1 UniProtKB:Q8IYU2 UniProtKB:Q96J02 UniProtKB:Q96PU5 UniProtKB:Q9HCE7 WB:WBGene00007009	P		Seeded From UniProt	complete
involved_in	GO:0006511	ubiquitin-dependent protein catabolic process	PMID:21873635^[42]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0029006 MGI:MGI:1202301 MGI:MGI:97297 PANTHER:PTN000134745 PomBase:SPAC11G7.02 SGD:S000000927 UniProtKB:O15033 UniProtKB:P46934 UniProtKB:Q96J02 UniProtKB:Q96PU5 UniProtKB:Q9HAU4 UniProtKB:Q9HCE7	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21873635^[42]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0003557 FB:FBgn0259174 MGI:MGI:1202301 MGI:MGI:1914144 MGI:MGI:97297 PANTHER:PTN000134256 PomBase:SPAC11G7.02 PomBase:SPAC1805.15c SGD:S000000927 TAIR:locus:2135630 UniProtKB:P46934 UniProtKB:Q7Z6Z7 UniProtKB:Q9HCE7 WB:WBGene00007009	C		Seeded From UniProt	complete
involved_in	GO:0000209	protein polyubiquitination	PMID:21873635^[42]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1202301 PANTHER:PTN000134745 SGD:S000000927 UniProtKB:Q9HCE7	P		Seeded From UniProt	complete
enables	GO:0061630	ubiquitin protein ligase activity	PMID:9462742^[43]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006511	ubiquitin-dependent protein catabolic process	PMID:9462742^[43]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0000151	ubiquitin ligase complex	PMID:9462742^[43]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004842	ubiquitin-protein transferase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000569 InterPro:IPR035983	F		Seeded From UniProt	complete
involved_in	GO:0006511	ubiquitin-dependent protein catabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR024928	P		Seeded From UniProt	complete
enables	GO:0061630	ubiquitin protein ligase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR024928	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F		Seeded From UniProt	complete
part_of	GO:0005856	cytoskeleton	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0206	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
part_of	GO:0030479	actin cortical patch	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0008	C		Seeded From UniProt	complete
involved_in	GO:0016567	protein ubiquitination	GO_REF:0000041	ECO:0000322	imported manually asserted information used in automatic assertion	UniPathway:UPA00143	P		Seeded From UniProt	complete
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Notes

References

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

↑ Jarmoszewicz, K et al. (2012) Rsp5 ubiquitin ligase is required for protein trafficking in Saccharomyces cerevisiae COPI mutants. PLoS ONE 7 e39582 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Huibregtse, JM et al. (1995) A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. Proc. Natl. Acad. Sci. U.S.A. 92 2563-7 PubMed GONUTS page
↑ Renvoisé, M et al. (2014) Quantitative variations of the mitochondrial proteome and phosphoproteome during fermentative and respiratory growth in Saccharomyces cerevisiae. J Proteomics 106 140-50 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
↑ Kama, R et al. (2018) Cdc48 and ubiquilins confer selective anterograde protein sorting and entry into the multivesicular body in yeast. Mol. Biol. Cell 29 948-963 PubMed GONUTS page
↑ Delom, F et al. (2006) The plasma membrane proteome of Saccharomyces cerevisiae and its response to the antifungal calcofluor. Proteomics 6 3029-39 PubMed GONUTS page
↑ Paul, B & Montpetit, B (2016) Altered RNA processing and export lead to retention of mRNAs near transcription sites and nuclear pore complexes or within the nucleolus. Mol. Biol. Cell 27 2742-56 PubMed GONUTS page
↑ Heo, JM et al. (2010) A stress-responsive system for mitochondrial protein degradation. Mol. Cell 40 465-80 PubMed GONUTS page
↑ ^10.0 ^10.1 Levin-Kravets, O et al. (2016) A bacterial genetic selection system for ubiquitylation cascade discovery. Nat. Methods 13 945-952 PubMed GONUTS page
↑ Fang, NN et al. (2014) Rsp5/Nedd4 is the main ubiquitin ligase that targets cytosolic misfolded proteins following heat stress. Nat. Cell Biol. 16 1227-37 PubMed GONUTS page
↑ Kimura, Y et al. (2014) The ESCRT-III adaptor protein Bro1 controls functions of regulator for free ubiquitin chains 1 (Rfu1) in ubiquitin homeostasis. J. Biol. Chem. 289 21760-9 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 ^13.3 ^13.4 ^13.5 Novoselova, TV et al. (2013) SUMOylation regulates the homologous to E6-AP carboxyl terminus (HECT) ubiquitin ligase Rsp5p. J. Biol. Chem. 288 10308-17 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 ^14.3 ^14.4 ^14.5 ^14.6 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
↑ ^15.0 ^15.1 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
↑ Lam, MH & Emili, A (2013) Ubp2 regulates Rsp5 ubiquitination activity in vivo and in vitro. PLoS ONE 8 e75372 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
↑ ^18.0 ^18.1 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
↑ 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
↑ ^20.0 ^20.1 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
↑ French, ME et al. (2009) Regulation of the RSP5 ubiquitin ligase by an intrinsic ubiquitin-binding site. J. Biol. Chem. 284 12071-9 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
↑ ^23.0 ^23.1 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
↑ ^24.0 ^24.1 ^24.2 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
↑ 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
↑ Kraft, C & Peter, M (2008) Is the Rsp5 ubiquitin ligase involved in the regulation of ribophagy? Autophagy 4 838-40 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
↑ ^28.0 ^28.1 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
↑ ^29.0 ^29.1 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
↑ ^30.0 ^30.1 ^30.2 ^30.3 ^30.4 ^30.5 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
↑ ^31.0 ^31.1 ^31.2 ^31.3 ^31.4 Zhu, M et al. (2011) Pheromone- and RSP5-dependent ubiquitination of the G protein beta subunit Ste4 in yeast. J. Biol. Chem. 286 27147-55 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
↑ McNatt, MW et al. (2007) Direct binding to Rsp5 mediates ubiquitin-independent sorting of Sna3 via the multivesicular body pathway. Mol. Biol. Cell 18 697-706 PubMed GONUTS page
↑ ^34.0 ^34.1 ^34.2 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
↑ ^35.0 ^35.1 Fisk, HA & Yaffe, MP (1999) A role for ubiquitination in mitochondrial inheritance in Saccharomyces cerevisiae. J. Cell Biol. 145 1199-208 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
↑ ^37.0 ^37.1 ^37.2 Torres, MP et al. (2009) G Protein Mono-ubiquitination by the Rsp5 Ubiquitin Ligase. J. Biol. Chem. 284 8940-50 PubMed GONUTS page
↑ ^38.0 ^38.1 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
↑ 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
↑ ^40.0 ^40.1 ^40.2 ^40.3 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
↑ 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
↑ ^42.0 ^42.1 ^42.2 ^42.3 ^42.4 ^42.5 ^42.6 ^42.7 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^43.0 ^43.1 ^43.2 Perry, WL et al. (1998) The itchy locus encodes a novel ubiquitin protein ligase that is disrupted in a18H mice. Nat. Genet. 18 143-6 PubMed GONUTS page

[PMID:22761830-1] Jarmoszewicz, K et al. (2012) Rsp5 ubiquitin ligase is required for protein trafficking in Saccharomyces cerevisiae COPI mutants. PLoS ONE 7 e39582 PubMed GONUTS page

[PMID:7708685-2] 2.0 ^2.1 ^2.2 Huibregtse, JM et al. (1995) A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. Proc. Natl. Acad. Sci. U.S.A. 92 2563-7 PubMed GONUTS page

[PMID:24769239-3] Renvoisé, M et al. (2014) Quantitative variations of the mitochondrial proteome and phosphoproteome during fermentative and respiratory growth in Saccharomyces cerevisiae. J Proteomics 106 140-50 PubMed GONUTS page

[PMID:16823961-4] 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:14576278-5] 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:29444958-6] Kama, R et al. (2018) Cdc48 and ubiquilins confer selective anterograde protein sorting and entry into the multivesicular body in yeast. Mol. Biol. Cell 29 948-963 PubMed GONUTS page

[PMID:16622836-7] Delom, F et al. (2006) The plasma membrane proteome of Saccharomyces cerevisiae and its response to the antifungal calcofluor. Proteomics 6 3029-39 PubMed GONUTS page

[PMID:27385342-8] Paul, B & Montpetit, B (2016) Altered RNA processing and export lead to retention of mRNAs near transcription sites and nuclear pore complexes or within the nucleolus. Mol. Biol. Cell 27 2742-56 PubMed GONUTS page

[PMID:21070972-9] Heo, JM et al. (2010) A stress-responsive system for mitochondrial protein degradation. Mol. Cell 40 465-80 PubMed GONUTS page

[PMID:27694912-10] 10.0 ^10.1 Levin-Kravets, O et al. (2016) A bacterial genetic selection system for ubiquitylation cascade discovery. Nat. Methods 13 945-952 PubMed GONUTS page

[PMID:25344756-11] Fang, NN et al. (2014) Rsp5/Nedd4 is the main ubiquitin ligase that targets cytosolic misfolded proteins following heat stress. Nat. Cell Biol. 16 1227-37 PubMed GONUTS page

[PMID:24962567-12] Kimura, Y et al. (2014) The ESCRT-III adaptor protein Bro1 controls functions of regulator for free ubiquitin chains 1 (Rfu1) in ubiquitin homeostasis. J. Biol. Chem. 289 21760-9 PubMed GONUTS page

[PMID:23443663-13] 13.0 ^13.1 ^13.2 ^13.3 ^13.4 ^13.5 Novoselova, TV et al. (2013) SUMOylation regulates the homologous to E6-AP carboxyl terminus (HECT) ubiquitin ligase Rsp5p. J. Biol. Chem. 288 10308-17 PubMed GONUTS page

[PMID:14608372-14] 14.0 ^14.1 ^14.2 ^14.3 ^14.4 ^14.5 ^14.6 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:17344478-15] 15.0 ^15.1 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:24069405-16] Lam, MH & Emili, A (2013) Ubp2 regulates Rsp5 ubiquitination activity in vivo and in vitro. PLoS ONE 8 e75372 PubMed GONUTS page

[PMID:11179425-17] 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:11007476-18] 18.0 ^18.1 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:12654912-19] 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:15713680-20] 20.0 ^20.1 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:19252184-21] French, ME et al. (2009) Regulation of the RSP5 ubiquitin ligase by an intrinsic ubiquitin-binding site. J. Biol. Chem. 284 12071-9 PubMed GONUTS page

[PMID:9614172-22] 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:12163175-23] 23.0 ^23.1 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:15078904-24] 24.0 ^24.1 ^24.2 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:10490634-25] 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:18670191-26] Kraft, C & Peter, M (2008) Is the Rsp5 ubiquitin ligase involved in the regulation of ribophagy? Autophagy 4 838-40 PubMed GONUTS page

[PMID:15855235-27] 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:12867034-28] 28.0 ^28.1 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:17182849-29] 29.0 ^29.1 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:18771750-30] 30.0 ^30.1 ^30.2 ^30.3 ^30.4 ^30.5 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:21685393-31] 31.0 ^31.1 ^31.2 ^31.3 ^31.4 Zhu, M et al. (2011) Pheromone- and RSP5-dependent ubiquitination of the G protein beta subunit Ste4 in yeast. J. Biol. Chem. 286 27147-55 PubMed GONUTS page

[PMID:18165238-32] 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:17182850-33] McNatt, MW et al. (2007) Direct binding to Rsp5 mediates ubiquitin-independent sorting of Sna3 via the multivesicular body pathway. Mol. Biol. Cell 18 697-706 PubMed GONUTS page

[PMID:14657247-34] 34.0 ^34.1 ^34.2 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:10366593-35] 35.0 ^35.1 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: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:19176477-37] 37.0 ^37.1 ^37.2 Torres, MP et al. (2009) G Protein Mono-ubiquitination by the Rsp5 Ubiquitin Ligase. J. Biol. Chem. 284 8940-50 PubMed GONUTS page

[PMID:14761940-38] 38.0 ^38.1 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:12399376-39] 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:9108033-40] 40.0 ^40.1 ^40.2 ^40.3 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:9931424-41] 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:21873635-42] 42.0 ^42.1 ^42.2 ^42.3 ^42.4 ^42.5 ^42.6 ^42.7 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:9462742-43] 43.0 ^43.1 ^43.2 Perry, WL et al. (1998) The itchy locus encodes a novel ubiquitin protein ligase that is disrupted in a18H mice. Nat. Genet. 18 143-6 PubMed GONUTS page

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