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P39940

- RSP5_YEAST

UniProt

P39940 - RSP5_YEAST

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Protein
E3 ubiquitin-protein ligase RSP5
Gene
RSP5, MDP1, NPI1, YER125W, SYGP-ORF41
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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. Component of a RSP5 ubiquitin ligase complex which specifies polyubiquitination and intracellular trafficking of the general amino acid permease GAP1 as well as other cell surface proteins like GAP1, FUR4, MAL61, PMA1 and STE2. The RSP5-BUL1/2 complex is also necessary for the heat-shock element (HSE)-mediated gene expression, nitrogen starvation GLN3-dependent transcription, pressure-induced differential regulation of the two tryptophan permeases TAT1 and TAT2 and sorting efficiency into multivesicular bodies. Also acts on RBP1. Plays a role in tolerance to o-dinitrobenzene. Involved in actin cytoskeleton organization and dynamics. Ubiquitinates the LAS17-binding proteins LSB1 and PIN3/LSB2 without directing them for degradation and affects LAS17 levels in a SLA1-dependent and LSB1/2-independent manner.12 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei777 – 7771Glycyl thioester intermediate

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. phosphatidylinositol binding Source: SGD
  3. protein binding Source: IntAct
  4. ubiquitin binding Source: SGD
  5. ubiquitin-protein transferase activity Source: SGD
Complete GO annotation...

GO - Biological processi

  1. cellular response to UV Source: SGD
  2. chromatin assembly or disassembly Source: SGD
  3. late endosome to vacuole transport via multivesicular body sorting pathway Source: SGD
  4. mitochondrion organization Source: SGD
  5. positive regulation of endocytosis Source: SGD
  6. positive regulation of fatty acid biosynthetic process Source: SGD
  7. positive regulation of receptor-mediated endocytosis Source: SGD
  8. positive regulation of transcription from RNA polymerase II promoter Source: SGD
  9. proteasome-mediated ubiquitin-dependent protein catabolic process Source: SGD
  10. protein autoubiquitination Source: SGD
  11. protein monoubiquitination Source: SGD
  12. protein polyubiquitination Source: SGD
  13. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: SGD
  14. regulation of actin cytoskeleton organization Source: SGD
  15. regulation of dolichol biosynthetic process Source: SGD
  16. regulation of ergosterol biosynthetic process Source: SGD
  17. regulation of initiation of mating projection growth Source: SGD
  18. regulation of mRNA export from nucleus Source: SGD
  19. regulation of multivesicular body size Source: SGD
  20. regulation of nitrogen utilization Source: SGD
  21. regulation of phosphate metabolic process Source: SGD
  22. regulation of protein localization Source: SGD
  23. regulation of rRNA processing Source: SGD
  24. regulation of ribosomal large subunit export from nucleus Source: SGD
  25. regulation of tRNA export from nucleus Source: SGD
  26. regulation of tRNA processing Source: SGD
  27. regulation of ubiquinone biosynthetic process Source: SGD
  28. response to drug Source: SGD
  29. ribophagy Source: SGD
  30. ubiquitin-dependent endocytosis Source: SGD
  31. ubiquitin-dependent protein catabolic process Source: MGI
  32. ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

BioCyciYEAST:G3O-30288-MONOMER.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RSP5 (EC:6.3.2.-)
Alternative name(s):
Reverses SPT-phenotype protein 5
Gene namesi
Name:RSP5
Synonyms:MDP1, NPI1
Ordered Locus Names:YER125W
ORF Names:SYGP-ORF41
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome V

Organism-specific databases

CYGDiYER125w.
SGDiS000000927. RSP5.

Subcellular locationi

Cytoplasm. Nucleus Reviewed prediction. Cytoplasmcytoskeletonactin patch 1 Publication

GO - Cellular componenti

  1. Golgi apparatus Source: SGD
  2. actin cortical patch Source: UniProtKB-SubCell
  3. cellular bud tip Source: SGD
  4. cytoplasm Source: SGD
  5. endosome membrane Source: SGD
  6. extrinsic component of cytoplasmic side of plasma membrane Source: SGD
  7. nucleus Source: SGD
  8. ubiquitin ligase complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi516 – 5161Y → A: Has subtle defects on both initial ubiquitination and chain elongation of substrate proteins.
Mutagenesisi521 – 5211Y → A: Has defects on both initial ubiquitination and chain elongation of substrate proteins.
Mutagenesisi537 – 5371I → D: Has defects on both initial ubiquitination and chain elongation of substrate proteins.
Mutagenesisi618 – 6181F → D: Has defects on both initial ubiquitination and chain elongation of substrate proteins.
Mutagenesisi733 – 7331L → S in RSP5-1; impairs ubiquitin-thioester formation and catalysis of substrate ubiquitination. 1 Publication
Mutagenesisi777 – 7771C → A: Loss of ubiquitination. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 809809E3 ubiquitin-protein ligase RSP5
PRO_0000120335Add
BLAST

Post-translational modificationi

The ubiquitination appears to be the result of an intramolecular transfer of ubiquitin.

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiP39940.
PaxDbiP39940.
PeptideAtlasiP39940.

Expressioni

Gene expression databases

GenevestigatoriP39940.

Interactioni

Subunit structurei

Component of the RSP5-BUL1/2 ubiquitin ligase complex composed of at least RSP5 and BUL1 or BUL2. Forms also a ternary complex with RUP1 and UBP2. Interacts (via WW domains) with LSB1, PIN3/LSB2 and RCR1 (via PY motifs). Interacts with HSE1, LAS17, ROG3, ROD1 and RVS167.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ACK1Q076222EBI-16219,EBI-38674
ADE12P802102EBI-16219,EBI-14267
ALY1P361174EBI-16219,EBI-26358
ALY2P470295EBI-16219,EBI-25974
ART10P186344EBI-16219,EBI-27197
ART5P532444EBI-16219,EBI-23201
BNA5Q059792EBI-16219,EBI-10016
CDC14Q006842EBI-16219,EBI-4192
CSR2Q127342EBI-16219,EBI-32379
CTA1P152022EBI-16219,EBI-4061
DIA1P540054EBI-16219,EBI-27668
DUS1P537592EBI-16219,EBI-27885
ECM21P381672EBI-16219,EBI-21359
ENO2P009252EBI-16219,EBI-6475
FMP46P361412EBI-16219,EBI-26445
GPH1P067382EBI-16219,EBI-13389
HEM12P323472EBI-16219,EBI-5711
IMA1P530512EBI-16219,EBI-10464
IPP1P008172EBI-16219,EBI-9338
LDB19Q125023EBI-16219,EBI-2113927
LYS1P389983EBI-16219,EBI-10264
LYS4P493672EBI-16219,EBI-10276
MCR1P360602EBI-16219,EBI-10565
MLS1P309523EBI-16219,EBI-10428
NPL3Q015602EBI-16219,EBI-12114
NPT1P396832EBI-16219,EBI-12218
PCK1P109632EBI-16219,EBI-13770
PFK2P168623EBI-16219,EBI-9435
PMU1P360692EBI-16219,EBI-26862
PTP1P250442EBI-16219,EBI-14183
PYC1P111542EBI-16219,EBI-14358
RCR1P382123EBI-16219,EBI-21381
RCR2Q034462EBI-16219,EBI-18180
RGM1Q004532EBI-16219,EBI-15073
ROD1Q028053EBI-16219,EBI-15679
ROG3P436023EBI-16219,EBI-22976
RPB8P204363EBI-16219,EBI-15794
SNA3P143592EBI-16219,EBI-26122
SNA4Q075492EBI-16219,EBI-22078
STM1P390153EBI-16219,EBI-11238
THI13Q077482EBI-16219,EBI-36080
THI5P435342EBI-16219,EBI-19221
TKL1P232542EBI-16219,EBI-19291
TRE1Q089193EBI-16219,EBI-31915
TY1A-PLQ121622EBI-16219,EBI-36658
TY2B-DR1Q124722EBI-16219,EBI-35737
UBC6P332962EBI-16219,EBI-19745
YBR056WP380813EBI-16219,EBI-21453
YCL021WP255613EBI-16219,EBI-21696
YHR131CP388353EBI-16219,EBI-24724
YIP5P531082EBI-16219,EBI-24051
YJL218WP408922EBI-16219,EBI-26263
YJR096WP471373EBI-16219,EBI-25572
YKR047WP361402EBI-16219,EBI-26441

Protein-protein interaction databases

BioGridi36869. 399 interactions.
DIPiDIP-2238N.
IntActiP39940. 172 interactions.
MINTiMINT-520379.
STRINGi4932.YER125W.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi393 – 3964
Beta strandi405 – 4073
Turni408 – 4114
Beta strandi412 – 4165
Helixi430 – 44314
Helixi446 – 4483
Beta strandi455 – 4606
Helixi461 – 4633
Helixi464 – 47411
Helixi477 – 4804
Beta strandi484 – 4896
Helixi502 – 51110
Helixi514 – 5163
Beta strandi517 – 52610
Beta strandi529 – 5313
Helixi533 – 5375
Helixi541 – 55717
Helixi568 – 5747
Helixi581 – 5877
Helixi589 – 59810
Turni604 – 6063
Beta strandi610 – 6178
Beta strandi620 – 6278
Helixi630 – 6323
Beta strandi633 – 6353
Turni637 – 6393
Helixi640 – 65213
Turni653 – 6564
Helixi657 – 66812
Helixi673 – 6764
Helixi681 – 6888
Helixi696 – 7016
Beta strandi703 – 7075
Helixi713 – 72412
Helixi727 – 73812
Helixi748 – 7503
Beta strandi754 – 7574
Beta strandi760 – 7634
Beta strandi773 – 7753
Helixi776 – 7783
Beta strandi780 – 7823
Helixi789 – 80214

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3OLMX-ray2.50A384-809[»]
4LCDX-ray3.10A/B383-809[»]
ProteinModelPortaliP39940.
SMRiP39940. Positions 3-135, 227-291, 329-806.

Miscellaneous databases

EvolutionaryTraceiP39940.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8888C2
Add
BLAST
Domaini229 – 26234WW 1
Add
BLAST
Domaini331 – 36434WW 2
Add
BLAST
Domaini387 – 42034WW 3
Add
BLAST
Domaini705 – 809105HECT
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi315 – 3228Poly-Ala

Sequence similaritiesi

Contains 1 C2 domain.
Contains 3 WW domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5021.
GeneTreeiENSGT00570000078756.
HOGENOMiHOG000208451.
KOiK10591.
OMAiMHTGATT.
OrthoDBiEOG735453.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
IPR024928. E3_ub_ligase_SMURF1.
IPR000569. HECT.
IPR001202. WW_dom.
[Graphical view]
PfamiPF00168. C2. 1 hit.
PF00632. HECT. 1 hit.
PF00397. WW. 3 hits.
[Graphical view]
PIRSFiPIRSF001569. E3_ub_ligase_SMURF1. 1 hit.
SMARTiSM00239. C2. 1 hit.
SM00119. HECTc. 1 hit.
SM00456. WW. 3 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF51045. SSF51045. 3 hits.
SSF56204. SSF56204. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS50237. HECT. 1 hit.
PS01159. WW_DOMAIN_1. 3 hits.
PS50020. WW_DOMAIN_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39940-1 [UniParc]FASTAAdd to Basket

« Hide

MPSSISVKLV AAESLYKRDV FRSPDPFAVL TIDGYQTKST SAAKKTLNPY    50
WNETFKFDDI NENSILTIQV FDQKKFKKKD QGFLGVVNVR VGDVLGHLDE 100
DTATSSGRPR EETITRDLKK SNDGMAVSGR LIVVLSKLPS SSPHSQAPSG 150
HTASSSTNTS STTRTNGHST SSTRNHSTSH PSRGTAQAVE STLQSGTTAA 200
TNTATTSHRS TNSTSSATRQ YSSFEDQYGR LPPGWERRTD NFGRTYYVDH 250
NTRTTTWKRP TLDQTEAERG NQLNANTELE RRQHRGRTLP GGSSDNSSVT 300
VQVGGGSNIP PVNGAAAAAF AATGGTTSGL GELPSGWEQR FTPEGRAYFV 350
DHNTRTTTWV DPRRQQYIRT YGPTNTTIQQ QPVSQLGPLP SGWEMRLTNT 400
ARVYFVDHNT KTTTWDDPRL PSSLDQNVPQ YKRDFRRKVI YFRSQPALRI 450
LPGQCHIKVR RKNIFEDAYQ EIMRQTPEDL KKRLMIKFDG EEGLDYGGVS 500
REFFFLLSHE MFNPFYCLFE YSAYDNYTIQ INPNSGINPE HLNYFKFIGR 550
VVGLGVFHRR FLDAFFVGAL YKMMLRKKVV LQDMEGVDAE VYNSLNWMLE 600
NSIDGVLDLT FSADDERFGE VVTVDLKPDG RNIEVTDGNK KEYVELYTQW 650
RIVDRVQEQF KAFMDGFNEL IPEDLVTVFD ERELELLIGG IAEIDIEDWK 700
KHTDYRGYQE SDEVIQWFWK CVSEWDNEQR ARLLQFTTGT SRIPVNGFKD 750
LQGSDGPRRF TIEKAGEVQQ LPKSHTCFNR VDLPQYVDYD SMKQKLTLAV 800
EETIGFGQE 809
Length:809
Mass (Da):91,816
Last modified:February 1, 1995 - v1
Checksum:i6F1836384479E70F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U18916 Genomic DNA. Translation: AAC03223.1.
BK006939 Genomic DNA. Translation: DAA07785.1.
PIRiS43217.
RefSeqiNP_011051.3. NM_001179015.3.

Genome annotation databases

EnsemblFungiiYER125W; YER125W; YER125W.
GeneIDi856862.
KEGGisce:YER125W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U18916 Genomic DNA. Translation: AAC03223.1 .
BK006939 Genomic DNA. Translation: DAA07785.1 .
PIRi S43217.
RefSeqi NP_011051.3. NM_001179015.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3OLM X-ray 2.50 A 384-809 [» ]
4LCD X-ray 3.10 A/B 383-809 [» ]
ProteinModelPortali P39940.
SMRi P39940. Positions 3-135, 227-291, 329-806.
ModBasei Search...

Protein-protein interaction databases

BioGridi 36869. 399 interactions.
DIPi DIP-2238N.
IntActi P39940. 172 interactions.
MINTi MINT-520379.
STRINGi 4932.YER125W.

Proteomic databases

MaxQBi P39940.
PaxDbi P39940.
PeptideAtlasi P39940.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YER125W ; YER125W ; YER125W .
GeneIDi 856862.
KEGGi sce:YER125W.

Organism-specific databases

CYGDi YER125w.
SGDi S000000927. RSP5.

Phylogenomic databases

eggNOGi COG5021.
GeneTreei ENSGT00570000078756.
HOGENOMi HOG000208451.
KOi K10591.
OMAi MHTGATT.
OrthoDBi EOG735453.

Enzyme and pathway databases

UniPathwayi UPA00143 .
BioCyci YEAST:G3O-30288-MONOMER.

Miscellaneous databases

EvolutionaryTracei P39940.
NextBioi 983216.
PROi P39940.

Gene expression databases

Genevestigatori P39940.

Family and domain databases

Gene3Di 2.60.40.150. 1 hit.
InterProi IPR000008. C2_dom.
IPR024928. E3_ub_ligase_SMURF1.
IPR000569. HECT.
IPR001202. WW_dom.
[Graphical view ]
Pfami PF00168. C2. 1 hit.
PF00632. HECT. 1 hit.
PF00397. WW. 3 hits.
[Graphical view ]
PIRSFi PIRSF001569. E3_ub_ligase_SMURF1. 1 hit.
SMARTi SM00239. C2. 1 hit.
SM00119. HECTc. 1 hit.
SM00456. WW. 3 hits.
[Graphical view ]
SUPFAMi SSF49562. SSF49562. 1 hit.
SSF51045. SSF51045. 3 hits.
SSF56204. SSF56204. 1 hit.
PROSITEi PS50004. C2. 1 hit.
PS50237. HECT. 1 hit.
PS01159. WW_DOMAIN_1. 3 hits.
PS50020. WW_DOMAIN_2. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Winston F.
    Unpublished observations (FEB-1993)
    Cited for: IDENTIFICATION.
  4. "NPI1, an essential yeast gene involved in induced degradation of Gap1 and Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase."
    Hein C., Springael J.-Y., Volland C., Haguenauer-Tsapis R., Andre B.
    Mol. Microbiol. 18:77-87(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: Sigma 1278B.
  5. "A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase."
    Huibregtse J.M., Scheffner M., Beaudenon S., Howley P.M.
    Proc. Natl. Acad. Sci. U.S.A. 92:2563-2567(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Bul1, a new protein that binds to the Rsp5 ubiquitin ligase in Saccharomyces cerevisiae."
    Yashiroda H., Oguchi T., Yasuda Y., Toh-e A., Kikuchi Y.
    Mol. Cell. Biol. 16:3255-3263(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BUL1.
  7. "The PY-motif of Bul1 protein is essential for growth of Saccharomyces cerevisiae under various stress conditions."
    Yashiroda H., Kaida D., Toh-e A., Kikuchi Y.
    Gene 225:39-46(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BUL1 AND BUL2.
  8. "Functional domains of the rsp5 ubiquitin-protein ligase."
    Wang G., Yang J., Huibregtse J.M.
    Mol. Cell. Biol. 19:342-352(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF LEU-733 AND CYS-777.
    Strain: S288c / FY56.
  9. "PY motifs of Rod1 are required for binding to Rsp5 and for drug resistance."
    Andoh T., Hirata Y., Kikuchi A.
    FEBS Lett. 525:131-134(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ROD1 AND ROG3.
  10. "Rsp5-Bul1/2 complex is necessary for the HSE-mediated gene expression in budding yeast."
    Kaida D., Toh-e A., Kikuchi Y.
    Biochem. Biophys. Res. Commun. 306:1037-1041(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
  11. "Pressure-induced differential regulation of the two tryptophan permeases Tat1 and Tat2 by ubiquitin ligase Rsp5 and its binding proteins, Bul1 and Bul2."
    Abe F., Iida H.
    Mol. Cell. Biol. 23:7566-7584(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
  12. "NPR1 kinase and RSP5-BUL1/2 ubiquitin ligase control GLN3-dependent transcription in Saccharomyces cerevisiae."
    Crespo J.L., Helliwell S.B., Wiederkehr C., Demougin P., Fowler B., Primig M., Hall M.N.
    J. Biol. Chem. 279:37512-37517(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
  13. "Ubiquitin-mediated targeting of a mutant plasma membrane ATPase, Pma1-7, to the endosomal/vacuolar system in yeast."
    Pizzirusso M., Chang A.
    Mol. Biol. Cell 15:2401-2409(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
  14. "Protein-protein interactions of ESCRT complexes in the yeast Saccharomyces cerevisiae."
    Bowers K., Lottridge J., Helliwell S.B., Goldthwaite L.M., Luzio J.P., Stevens T.H.
    Traffic 5:194-210(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSE1.
  15. "The Rsp5 ubiquitin ligase is coupled to and antagonized by the Ubp2 deubiquitinating enzyme."
    Kee Y., Lyon N., Huibregtse J.M.
    EMBO J. 24:2414-2424(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RUP1 AND UBP2.
  16. "Transduction of the nitrogen signal activating Gln3-mediated transcription is independent of Npr1 kinase and Rsp5-Bul1/2 ubiquitin ligase in Saccharomyces cerevisiae."
    Feller A., Boeckstaens M., Marini A.-M., Dubois E.
    J. Biol. Chem. 281:28546-28554(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
  17. "Peculiar protein-protein interactions of the novel endoplasmic reticulum membrane protein Rcr1 and ubiquitin ligase Rsp5."
    Imai K., Noda Y., Adachi H., Yoda K.
    Biosci. Biotechnol. Biochem. 71:249-252(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RCR1.
  18. "Hse1, a component of the yeast Hrs-STAM ubiquitin-sorting complex, associates with ubiquitin peptidases and a ligase to control sorting efficiency into multivesicular bodies."
    Ren J., Kee Y., Huibregtse J.M., Piper R.C.
    Mol. Biol. Cell 18:324-335(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HSE1.
  19. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. Cited for: FUNCTION, INTERACTION WITH LAS17; LSB1; LSB2 AND RVS167, SUBCELLULAR LOCATION.
  21. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Structure and function of a HECT domain ubiquitin-binding site."
    Kim H.C., Steffen A.M., Oldham M.L., Chen J., Huibregtse J.M.
    EMBO Rep. 12:334-341(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 384-809 IN COMPLEX WITH UBIQUITIN.

Entry informationi

Entry nameiRSP5_YEAST
AccessioniPrimary (citable) accession number: P39940
Secondary accession number(s): D3DM31
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: September 3, 2014
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

A cysteine residue is required for ubiquitin-thioester formation.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

External Data

Dasty 3

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