Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P39940 (RSP5_YEAST)

Last modified June 16, 2009. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    E3 ubiquitin-protein ligase RSP5
    EC=6.3.2.-
Alternative name(s):
    Reverses SPT-phenotype protein 5
Gene names
Name: RSP5
Synonyms: MDP1, NPI1
Ordered Locus Names: YER125W
ORF Names: SYGP-ORF41
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length809 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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. Ref.4 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.18

Pathway

Protein modification; protein ubiquitination.

Subunit structure

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. The WW domains interact with the singular VPEY sequence in RCR1. Interacts with HSE1, ROG3 and ROD1. Ref.7 Ref.9 Ref.15 Ref.18 Ref.6 Ref.14 Ref.17

Subcellular location

Cytoplasm Potential. Nucleus Potential.

Post-translational modification

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

Miscellaneous

A cysteine residue is required for ubiquitin-thioester formation.

Sequence similarities

Contains 1 C2 domain.

Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain.

Contains 3 WW domains.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   DomainRepeat
   Molecular functionLigase
   PTMUbl conjugation
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcellular response to UV

Inferred from mutant phenotype. Source: SGD

chromatin assembly or disassembly

Inferred from mutant phenotype. Source: SGD

late endosome to vacuole transport via multivesicular body sorting pathway

Inferred from mutant phenotype. Source: SGD

mitochondrion organization

Inferred from genetic interaction. Source: SGD

positive regulation of fatty acid biosynthetic process

Inferred from mutant phenotype. Source: SGD

positive regulation of receptor-mediated endocytosis

Inferred from mutant phenotype. Source: SGD

positive regulation of specific transcription from RNA polymerase II promoter

Inferred from mutant phenotype. Source: SGD

proteasomal ubiquitin-dependent protein catabolic process

Inferred from physical interaction. Source: SGD

protein monoubiquitination

Inferred from direct assay. Source: SGD

protein polyubiquitination

Inferred from direct assay. Source: SGD

protein ubiquitination during ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype. Source: SGD

rRNA processing

Inferred from mutant phenotype. Source: SGD

regulation of actin cytoskeleton organization

Inferred from genetic interaction. Source: SGD

regulation of dolichol biosynthetic process

Inferred from genetic interaction. Source: SGD

regulation of ergosterol biosynthetic process

Inferred from genetic interaction. Source: SGD

regulation of mRNA export from nucleus

Inferred from physical interaction. Source: SGD

regulation of multivesicular body size

Inferred from mutant phenotype. Source: SGD

regulation of nitrogen utilization Ref.12

Inferred from genetic interaction. Source: SGD

regulation of phosphate metabolic process

Inferred from genetic interaction. Source: SGD

regulation of protein localization

Inferred from mutant phenotype. Source: SGD

regulation of ubiquinone biosynthetic process

Inferred from genetic interaction. Source: SGD

response to drug Ref.9

Inferred from mutant phenotype. Source: SGD

ribophagy

Inferred from genetic interaction. Source: SGD

ribosomal large subunit export from nucleus

Inferred from mutant phenotype. Source: SGD

tRNA export from nucleus

Inferred from mutant phenotype. Source: SGD

tRNA processing

Inferred from mutant phenotype. Source: SGD

ubiquitin-dependent endocytosis

Inferred from mutant phenotype. Source: SGD

ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway

Inferred from mutant phenotype. Source: SGD

   Cellular componentGolgi apparatus

Inferred from direct assay. Source: SGD

cellular bud tip

Inferred from direct assay. Source: SGD

endosome membrane

Inferred from direct assay. Source: SGD

extrinsic to internal side of plasma membrane

Inferred from direct assay. Source: SGD

mitochondrion

Inferred from direct assay. Source: SGD

nucleus

Inferred from direct assay. Source: SGD

plasma membrane enriched fraction

Inferred from direct assay. Source: SGD

ubiquitin ligase complex Ref.7

Inferred from direct assay. Source: MGI

   Molecular functionidentical protein binding

Inferred from physical interaction. Source: IntAct

phosphoinositide binding

Inferred from direct assay. Source: SGD

ubiquitin binding

Inferred from direct assay. Source: SGD

ubiquitin-protein ligase activity

Inferred from direct assay. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself1EBI-16219,EBI-16219
O135311EBI-16219,EBI-35836
O135501EBI-16219,EBI-35936
P186341EBI-16219,EBI-27197
P255611EBI-16219,EBI-21696
P283211EBI-16219,EBI-26790
P360691EBI-16219,EBI-26862
P360881EBI-16219,EBI-26738
P361171EBI-16219,EBI-26358
P361401EBI-16219,EBI-26441
P380811EBI-16219,EBI-21453
P387161EBI-16219,EBI-24682
P387411EBI-16219,EBI-24341
P387581EBI-16219,EBI-24443
P403251EBI-16219,EBI-23614
P408921EBI-16219,EBI-26263
P470292EBI-16219,EBI-25974
P470661EBI-16219,EBI-25816
P471371EBI-16219,EBI-25572
P531831EBI-16219,EBI-23747
Q028311EBI-16219,EBI-31828
Q043361EBI-16219,EBI-27435
Q086861EBI-16219,EBI-19264
Q089091EBI-16219,EBI-36654
Q122981EBI-16219,EBI-34580
ACK1Q076221EBI-16219,EBI-38674
ADE12P802101EBI-16219,EBI-14267
ADE17P380091EBI-16219,EBI-14223
ADH2P003311EBI-16219,EBI-2222
ADK1P071701EBI-16219,EBI-9447
AIP1P466801EBI-16219,EBI-2406
ALA1P408251EBI-16219,EBI-18648
AMD1P152741EBI-16219,EBI-2548
ARA2Q042121EBI-16219,EBI-28073
ARP2P323811EBI-16219,EBI-2927
ART5P532442EBI-16219,EBI-23201
ASF1P324471EBI-16219,EBI-3003
BNA5Q059791EBI-16219,EBI-10016
CMD1P067871EBI-16219,EBI-3976
CRN1Q064401EBI-16219,EBI-4950
CSR2Q127341EBI-16219,EBI-32379
CTA1P152021EBI-16219,EBI-4061
CTF4Q014541EBI-16219,EBI-5209
DFR1P078071EBI-16219,EBI-6247
DIA1P540052EBI-16219,EBI-27668
DUS1P537591EBI-16219,EBI-27885
ECM21P381671EBI-16219,EBI-21359
EHT1P382951EBI-16219,EBI-20890
ELP2P429351EBI-16219,EBI-23459
ENO2P009251EBI-16219,EBI-6475
FMP40Q089681EBI-16219,EBI-29375
FMP46P361411EBI-16219,EBI-26445
FSP2P530511EBI-16219,EBI-10464
GCN5Q033301EBI-16219,EBI-7458
GND1P387201EBI-16219,EBI-1965
GON7P469841EBI-16219,EBI-26178
GPH1P067381EBI-16219,EBI-13389
GSF2Q046971EBI-16219,EBI-27807
GSY2P274721EBI-16219,EBI-8036
GUS1P466551EBI-16219,EBI-18665
HCR1Q057751EBI-16219,EBI-8944
HEM12P323471EBI-16219,EBI-5711
HSP104P315391EBI-16219,EBI-8050
IDI1P154961EBI-16219,EBI-8902
IDP3P539821EBI-16219,EBI-8892
IPP1P008171EBI-16219,EBI-9338
LAH1P333991EBI-16219,EBI-10046
LDB19Q125022EBI-16219,EBI-2113927
LSB1P532811EBI-16219,EBI-23329
LYS1P389981EBI-16219,EBI-10264
LYS4P493671EBI-16219,EBI-10276
MAL32P381581EBI-16219,EBI-10326
MCR1P360601EBI-16219,EBI-10565
MDH3P324191EBI-16219,EBI-10598
MDM34P530831EBI-16219,EBI-24154
MEF1P250391EBI-16219,EBI-6353
MET12P461511EBI-16219,EBI-11567
MLS1P309521EBI-16219,EBI-10428
MSE1P485251EBI-16219,EBI-18669
MVP1P409591EBI-16219,EBI-11636
NOB1Q084441EBI-16219,EBI-29777
NPL3Q015601EBI-16219,EBI-12114
NPT1P396831EBI-16219,EBI-12218
OYE2Q035581EBI-16219,EBI-12729
OYE3P418161EBI-16219,EBI-12734
PCK1P109631EBI-16219,EBI-13770
PDI1P179671EBI-16219,EBI-13012
PFK2P168621EBI-16219,EBI-9435
PRE10P212421EBI-16219,EBI-13963
PRP2P200951EBI-16219,EBI-13820
PTP1P250441EBI-16219,EBI-14183
PYC1P111541EBI-16219,EBI-14358
RCR1P382123EBI-16219,EBI-21381
RCR2Q034461EBI-16219,EBI-18180
RGM1Q004531EBI-16219,EBI-15073
ROD1Q028052EBI-16219,EBI-15679
ROG3P436023EBI-16219,EBI-22976
RPB8P204361EBI-16219,EBI-15794
RPL8AP170761EBI-16219,EBI-15431
RUB1Q039191EBI-16219,EBI-37695
SDO1Q079531EBI-16219,EBI-27124
SGN1P405611EBI-16219,EBI-25362
SIP2P341641EBI-16219,EBI-17187
SNA3P143591EBI-16219,EBI-26122
SNA4Q075491EBI-16219,EBI-22078
SNO2P538231EBI-16219,EBI-28424
SPT4P329141EBI-16219,EBI-17928
SSH4P323431EBI-16219,EBI-26858
STM1P390151EBI-16219,EBI-11238
STR3P531011EBI-16219,EBI-24097
THI13Q077481EBI-16219,EBI-36080
THI21Q089751EBI-16219,EBI-30327
THI5P435341EBI-16219,EBI-19221
THI80P352021EBI-16219,EBI-19195
TIF34P402171EBI-16219,EBI-8951
TKL1P232541EBI-16219,EBI-19291
TRM82Q037741EBI-16219,EBI-19486
TY1A-AO135281EBI-16219,EBI-37069
TY1A-DR6Q121621EBI-16219,EBI-36658
TY1A-OLQ923921EBI-16219,EBI-32813
TY1A-PR3Q6Q5H11EBI-16219,EBI-937891
TY2B-DR1Q124721EBI-16219,EBI-35737
UBC6P332961EBI-16219,EBI-19745
UBX3Q122291EBI-16219,EBI-35335
UME1Q030101EBI-16219,EBI-20070
VPS66Q065081EBI-16219,EBI-36961
YDL086WQ075051EBI-16219,EBI-5951
YIP5P531081EBI-16219,EBI-24051
YJR149WP471771EBI-16219,EBI-25740
YMR315WQ048691EBI-16219,EBI-27664
YNL045WQ107401EBI-16219,EBI-10175

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 809809E3 ubiquitin-protein ligase RSP5
PRO_0000120335

Regions

Domain1 – 8888C2
Domain229 – 26234WW 1
Domain331 – 36434WW 2
Domain387 – 42034WW 3
Domain705 – 809105HECT
Compositional bias315 – 3228Poly-Ala

Sites

Active site7771Glycyl thioester intermediate

Experimental info

Mutagenesis7331L → S in RSP5-1; impairs ubiquitin-thioester formation and catalysis of substrate ubiquitination. Ref.8
Mutagenesis7771C → A: Loss of ubiquitination. Ref.8

Sequences

Sequence LengthMass (Da)Tools
P39940-1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 6F1836384479E70F

FASTA80991,816
        10         20         30         40         50         60 
MPSSISVKLV AAESLYKRDV FRSPDPFAVL TIDGYQTKST SAAKKTLNPY WNETFKFDDI 

        70         80         90        100        110        120 
NENSILTIQV FDQKKFKKKD QGFLGVVNVR VGDVLGHLDE DTATSSGRPR EETITRDLKK 

       130        140        150        160        170        180 
SNDGMAVSGR LIVVLSKLPS SSPHSQAPSG HTASSSTNTS STTRTNGHST SSTRNHSTSH 

       190        200        210        220        230        240 
PSRGTAQAVE STLQSGTTAA TNTATTSHRS TNSTSSATRQ YSSFEDQYGR LPPGWERRTD 

       250        260        270        280        290        300 
NFGRTYYVDH NTRTTTWKRP TLDQTEAERG NQLNANTELE RRQHRGRTLP GGSSDNSSVT 

       310        320        330        340        350        360 
VQVGGGSNIP PVNGAAAAAF AATGGTTSGL GELPSGWEQR FTPEGRAYFV DHNTRTTTWV 

       370        380        390        400        410        420 
DPRRQQYIRT YGPTNTTIQQ QPVSQLGPLP SGWEMRLTNT ARVYFVDHNT KTTTWDDPRL 

       430        440        450        460        470        480 
PSSLDQNVPQ YKRDFRRKVI YFRSQPALRI LPGQCHIKVR RKNIFEDAYQ EIMRQTPEDL 

       490        500        510        520        530        540 
KKRLMIKFDG EEGLDYGGVS REFFFLLSHE MFNPFYCLFE YSAYDNYTIQ INPNSGINPE 

       550        560        570        580        590        600 
HLNYFKFIGR VVGLGVFHRR FLDAFFVGAL YKMMLRKKVV LQDMEGVDAE VYNSLNWMLE 

       610        620        630        640        650        660 
NSIDGVLDLT FSADDERFGE VVTVDLKPDG RNIEVTDGNK KEYVELYTQW RIVDRVQEQF 

       670        680        690        700        710        720 
KAFMDGFNEL IPEDLVTVFD ERELELLIGG IAEIDIEDWK KHTDYRGYQE SDEVIQWFWK 

       730        740        750        760        770        780 
CVSEWDNEQR ARLLQFTTGT SRIPVNGFKD LQGSDGPRRF TIEKAGEVQQ LPKSHTCFNR 

       790        800 
VDLPQYVDYD SMKQKLTLAV EETIGFGQE 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome V."
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(1997) [PubMed: 9169868] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[2]Winston F.
Unpublished observations (FEB-1993)
Cited for: IDENTIFICATION.
[3]"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: 8596462] [Abstract]
Cited for: CHARACTERIZATION.
Strain: Sigma 1278B.
[4]"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: 7708685] [Abstract]
Cited for: FUNCTION.
[5]Erratum
Huibregtse J.M., Scheffner M., Beaudenon S., Howley P.M.
Proc. Natl. Acad. Sci. U.S.A. 92:5249-5249(1995) [PubMed: 7761480] [Abstract]
[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: 8668140] [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: 9931424] [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: 9858558] [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: 12163175] [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: 12821147] [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: 14560004] [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: 15247235] [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: 15020711] [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: 15086794] [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: 15933713] [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: 16864574] [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: 17213653] [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: 17079730] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HSE1.
+Additional computationally mapped references.

Cross-references

Sequence databases

U18916 Genomic DNA. Translation: AAC03223.1.
PIRS43217.
RefSeqNP_011051.1.

3D structure databases

HSSPHSSP built from PDB template 1I5H based on UniProtKB Q62940.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:2238N.
IntActP39940. 154 interactions.

Proteomic databases

PeptideAtlasP39940.
PRIDEP39940.

Genome annotation databases

EnsemblYER125W. Saccharomyces cerevisiae. [Contig view]
GeneID856862.
GenomeReviewsGene locus YER125W in contig U00092_GR.
KEGGsce:YER125W.
NMPDRfig|4932.3.peg.2127.

Organism-specific databases

CYGDYER125w.
SGDS000000927. RSP5.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMP39940.
OMAP39940. VLQDMEG.

Gene expression databases

ArrayExpressP39940.
GermOnlineYER125W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR000008. C2_Ca-dep.
IPR018029. C2_membr_targeting.
IPR000569. HECT.
IPR001202. WW_Rsp5_WWP.
[Graphical view]
PfamPF00168. C2. 1 hit.
PF00632. HECT. 1 hit.
PF00397. WW. 3 hits.
[Graphical view]
SMARTSM00239. C2. 1 hit.
SM00119. HECTc. 1 hit.
SM00456. WW. 3 hits.
[Graphical view]
PROSITEPS50004. C2. 1 hit.
PS50237. HECT. 1 hit.
PS01159. WW_DOMAIN_1. 3 hits.
PS50020. WW_DOMAIN_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio983216.

Entry information

Entry nameRSP5_YEAST
AccessionPrimary (citable) accession number: P39940
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 16, 2009
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome V

Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents