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Protein

Epsin-5

Gene

ENT5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the recruitment of clathrin to the Golgi network and endosomes to form clathrin coated vesicles. Plays a role in the trafficking of clathrin between the Golgi network and endosomes. Binds to membranes enriched in phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2) and, in association with VPS27, is involved in protein sorting at the multivesicular body (MVB).2 Publications

GO - Molecular functioni

  • clathrin binding Source: SGD
  • phosphatidylinositol-3,5-bisphosphate binding Source: SGD

GO - Biological processi

  • early endosome to Golgi transport Source: SGD
  • Golgi to endosome transport Source: SGD
  • late endosome to vacuole transport via multivesicular body sorting pathway Source: SGD
  • protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29747-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Epsin-5
Gene namesi
Name:ENT5
Ordered Locus Names:YDR153C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR153C.
SGDiS000002560. ENT5.

Subcellular locationi

GO - Cellular componenti

  • clathrin vesicle coat Source: SGD
  • cytosol Source: GOC
  • endosome Source: SGD
  • endosome membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi331 – 3311F → A: Reduced binding to GGA2. 1 Publication
Mutagenesisi334 – 3341F → A: Reduced binding to GGA2. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 411411Epsin-5PRO_0000074528Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei322 – 3221PhosphoserineCombined sources
Modified residuei324 – 3241PhosphoserineCombined sources
Modified residuei363 – 3631PhosphoserineCombined sources
Modified residuei368 – 3681PhosphothreonineCombined sources
Modified residuei394 – 3941PhosphoserineCombined sources
Modified residuei401 – 4011PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ03769.

PTM databases

iPTMnetiQ03769.

Interactioni

Subunit structurei

Interacts with the clathrin adapter GGA2 and the clathrin adapter complex AP-1.2 Publications

GO - Molecular functioni

  • clathrin binding Source: SGD

Protein-protein interaction databases

BioGridi32206. 93 interactions.
IntActiQ03769. 1 interaction.
MINTiMINT-2780845.

Structurei

3D structure databases

ProteinModelPortaliQ03769.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 184160ENTHPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi304 – 32320Asn-richAdd
BLAST

Sequence similaritiesi

Contains 1 ENTH (epsin N-terminal homology) domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000112379.
InParanoidiQ03769.
OMAiWRVVLKC.
OrthoDBiEOG7RJQ2G.

Family and domain databases

Gene3Di1.25.40.90. 1 hit.
InterProiIPR013809. ENTH.
IPR008942. ENTH_VHS.
[Graphical view]
PfamiPF01417. ENTH. 1 hit.
[Graphical view]
SMARTiSM00273. ENTH. 1 hit.
[Graphical view]
SUPFAMiSSF48464. SSF48464. 1 hit.
PROSITEiPS50942. ENTH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q03769-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSLSKKIQN LGIHDIRNAA RFAQNVIVQY EPYQIDIRRA TNTDAWGPTP
60 70 80 90 100
KHLAKVLRNR YQVPLYLMTE YTLKRLVDHI ATRPKNLYEK ARKDYVNYGS
110 120 130 140 150
EWRVVLKCLV VIEFLLLNVD TGDELNQIRS CLLTHKHILT REIAQFKVKF
160 170 180 190 200
SNDGKMEIHE RGIRKKGELI LQYLEDSQFL KKERAKNKKN ALKIRQQGES
210 220 230 240 250
SIYNANQIST SASYDNIDDD EFDADADGFD SEMDANNVTN FNVPVETEAN
260 270 280 290 300
SNTRRRSHME EQRRQRREIL REQIKNKEQQ RKRKQQQDSI PDLIDLDDST
310 320 330 340 350
STTNNITIDN GNNDNKNNNI NSNSDDDDDE FGDFQSETSP DTTAPKTSNS
360 370 380 390 400
KIDDLLDWDG PKSDTDTTAA AQTSLPFAEK KQQKARPQAT KDKSKGNDAF
410
SDLFSYSKSL V
Length:411
Mass (Da):47,321
Last modified:November 1, 1996 - v1
Checksum:i8802816008D9A4CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z50046 Genomic DNA. Translation: CAA90375.1.
AY557702 Genomic DNA. Translation: AAS56028.1.
BK006938 Genomic DNA. Translation: DAA11995.1.
PIRiS57979.
RefSeqiNP_010437.3. NM_001180460.3.

Genome annotation databases

EnsemblFungiiYDR153C; YDR153C; YDR153C.
GeneIDi851731.
KEGGisce:YDR153C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z50046 Genomic DNA. Translation: CAA90375.1.
AY557702 Genomic DNA. Translation: AAS56028.1.
BK006938 Genomic DNA. Translation: DAA11995.1.
PIRiS57979.
RefSeqiNP_010437.3. NM_001180460.3.

3D structure databases

ProteinModelPortaliQ03769.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32206. 93 interactions.
IntActiQ03769. 1 interaction.
MINTiMINT-2780845.

PTM databases

iPTMnetiQ03769.

Proteomic databases

MaxQBiQ03769.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR153C; YDR153C; YDR153C.
GeneIDi851731.
KEGGisce:YDR153C.

Organism-specific databases

EuPathDBiFungiDB:YDR153C.
SGDiS000002560. ENT5.

Phylogenomic databases

HOGENOMiHOG000112379.
InParanoidiQ03769.
OMAiWRVVLKC.
OrthoDBiEOG7RJQ2G.

Enzyme and pathway databases

BioCyciYEAST:G3O-29747-MONOMER.

Miscellaneous databases

PROiQ03769.

Family and domain databases

Gene3Di1.25.40.90. 1 hit.
InterProiIPR013809. ENTH.
IPR008942. ENTH_VHS.
[Graphical view]
PfamiPF01417. ENTH. 1 hit.
[Graphical view]
SMARTiSM00273. ENTH. 1 hit.
[Graphical view]
SUPFAMiSSF48464. SSF48464. 1 hit.
PROSITEiPS50942. ENTH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "Yeast epsin-related proteins required for Golgi-endosome traffic define a gamma-adaptin ear-binding motif."
    Duncan M.C., Costaguta G., Payne G.S.
    Nat. Cell Biol. 5:77-81(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GGA2 AND AP-1, SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-331 AND PHE-334.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Ent5p is required with Ent3p and Vps27p for ubiquitin-dependent protein sorting into the multivesicular body."
    Eugster A., Pecheur E.-I., Michel F., Winsor B., Letourneur F., Friant S.
    Mol. Biol. Cell 15:3031-3041(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH VPS27, SUBCELLULAR LOCATION.
  7. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  8. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322; SER-324; SER-363; THR-368; SER-394 AND SER-401, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiENT5_YEAST
AccessioniPrimary (citable) accession number: Q03769
Secondary accession number(s): D6VSD5, Q6Q5U2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 8100 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.