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Protein

Epsin-1

Gene

ENT1

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

Binds to membranes enriched in phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) and phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Required for endocytosis and localization of actin. Negatively regulated via phosphorylation.3 Publications

GO - Molecular functioni

  • clathrin binding Source: SGD
  • lipid binding Source: UniProtKB-KW
  • ubiquitin binding Source: SGD

GO - Biological processi

  • actin cortical patch assembly Source: SGD
  • actin filament organization Source: SGD
  • endocytosis Source: SGD
Complete GO annotation...

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29555-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Epsin-1
Gene namesi
Name:ENT1
Ordered Locus Names:YDL161W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL161W.
SGDiS000002320. ENT1.

Subcellular locationi

GO - Cellular componenti

  • early endosome Source: SGD
  • membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi395 – 3951T → A or E: No phosphorylation. 1 Publication
Mutagenesisi415 – 4151T → A or E: No phosphorylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 454454Epsin-1PRO_0000074524Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei160 – 1601PhosphothreonineCombined sources
Modified residuei163 – 1631PhosphoserineCombined sources
Modified residuei180 – 1801PhosphothreonineCombined sources
Modified residuei328 – 3281PhosphoserineCombined sources
Cross-linki357 – 357Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei364 – 3641PhosphothreonineCombined sources
Modified residuei366 – 3661PhosphothreonineCombined sources
Modified residuei384 – 3841PhosphothreonineCombined sources
Modified residuei386 – 3861PhosphothreonineCombined sources
Modified residuei388 – 3881PhosphothreonineCombined sources
Modified residuei395 – 3951Phosphothreonine; by PRK11 Publication
Modified residuei415 – 4151Phosphothreonine; by PRK11 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ12518.

PTM databases

iPTMnetiQ12518.

Interactioni

Subunit structurei

Interacts with EDE1 and PAN1.2 Publications

GO - Molecular functioni

  • clathrin binding Source: SGD
  • ubiquitin binding Source: SGD

Protein-protein interaction databases

BioGridi31902. 27 interactions.
DIPiDIP-957N.
IntActiQ12518. 8 interactions.
MINTiMINT-372554.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5AHVelectron microscopy13.60E1-154[»]
ProteinModelPortaliQ12518.
SMRiQ12518. Positions 1-154.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 143133ENTHPROSITE-ProRule annotationAdd
BLAST
Domaini165 – 18420UIM 1PROSITE-ProRule annotationAdd
BLAST
Domaini189 – 20820UIM 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni447 – 4548Clathrin-binding

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi211 – 349139Gln-richAdd
BLAST

Sequence similaritiesi

Belongs to the epsin family.Curated
Contains 1 ENTH (epsin N-terminal homology) domain.PROSITE-ProRule annotation
Contains 2 UIM (ubiquitin-interacting motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00820000128075.
HOGENOMiHOG000216614.
InParanoidiQ12518.
KOiK12471.
OMAiNPIANFQ.
OrthoDBiEOG7KM63T.

Family and domain databases

Gene3Di1.25.40.90. 1 hit.
InterProiIPR013809. ENTH.
IPR008942. ENTH_VHS.
IPR003903. UIM_dom.
[Graphical view]
PfamiPF01417. ENTH. 1 hit.
[Graphical view]
SMARTiSM00273. ENTH. 1 hit.
SM00726. UIM. 2 hits.
[Graphical view]
SUPFAMiSSF48464. SSF48464. 1 hit.
PROSITEiPS50942. ENTH. 1 hit.
PS50330. UIM. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12518-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKQFVRSAK NLVKGYSSTQ VLVRNATSND NHQVSKDSLI ELAEKSYDSA
60 70 80 90 100
DFFEIMDMLD KRLNDKGKYW RHIAKALTVI DYLIRFGSEN CVLWCRENLY
110 120 130 140 150
IIKTLKEFRH EDDEGIDQGQ IVRVKAKELT ALLSDDERLN EERNMNIKGR
160 170 180 190 200
NRKGRRRRGT GRSDENDDDL QRAISASRLT AEEDERRRKQ DEDYETALQL
210 220 230 240 250
SKEEEELKRL QDLQRMQQQQ GQQQLQQPMY YDIFGNPITP EEYAQFQLQQ
260 270 280 290 300
QQQQQQQQLQ QQPMYYDVFG NPITPEELAQ FQQQQQLQEQ QYLASMQQQQ
310 320 330 340 350
QAMSNNPFAK SEQSSSSPKR NQLVAASSPQ QLQQQKQQEP LIQNRTGNQS
360 370 380 390 400
MTDKYSKLNE LLATGTGIDT FGNVGEARIP AQHTKTGTFI NSQGTGYRQV
410 420 430 440 450
SDDPNHNPFL NSQYTGLPST SVVPTQTGYG FGNQSQQQSQ NNGSNNRGYT

LIDL
Length:454
Mass (Da):52,352
Last modified:November 1, 1996 - v1
Checksum:i37447FB4A6449256
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z74210 Genomic DNA. Translation: CAA98736.1.
Z67750 Genomic DNA. Translation: CAA91585.1.
BK006938 Genomic DNA. Translation: DAA11698.1.
PIRiS61052.
RefSeqiNP_010120.1. NM_001180221.1.

Genome annotation databases

EnsemblFungiiYDL161W; YDL161W; YDL161W.
GeneIDi851392.
KEGGisce:YDL161W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z74210 Genomic DNA. Translation: CAA98736.1.
Z67750 Genomic DNA. Translation: CAA91585.1.
BK006938 Genomic DNA. Translation: DAA11698.1.
PIRiS61052.
RefSeqiNP_010120.1. NM_001180221.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5AHVelectron microscopy13.60E1-154[»]
ProteinModelPortaliQ12518.
SMRiQ12518. Positions 1-154.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31902. 27 interactions.
DIPiDIP-957N.
IntActiQ12518. 8 interactions.
MINTiMINT-372554.

PTM databases

iPTMnetiQ12518.

Proteomic databases

MaxQBiQ12518.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL161W; YDL161W; YDL161W.
GeneIDi851392.
KEGGisce:YDL161W.

Organism-specific databases

EuPathDBiFungiDB:YDL161W.
SGDiS000002320. ENT1.

Phylogenomic databases

GeneTreeiENSGT00820000128075.
HOGENOMiHOG000216614.
InParanoidiQ12518.
KOiK12471.
OMAiNPIANFQ.
OrthoDBiEOG7KM63T.

Enzyme and pathway databases

BioCyciYEAST:G3O-29555-MONOMER.

Miscellaneous databases

PROiQ12518.

Family and domain databases

Gene3Di1.25.40.90. 1 hit.
InterProiIPR013809. ENTH.
IPR008942. ENTH_VHS.
IPR003903. UIM_dom.
[Graphical view]
PfamiPF01417. ENTH. 1 hit.
[Graphical view]
SMARTiSM00273. ENTH. 1 hit.
SM00726. UIM. 2 hits.
[Graphical view]
SUPFAMiSSF48464. SSF48464. 1 hit.
PROSITEiPS50942. ENTH. 1 hit.
PS50330. UIM. 2 hits.
[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. "Yeast epsins contain an essential N-terminal ENTH domain, bind clathrin and are required for endocytosis."
    Wendland B., Steece K.E., Emr S.D.
    EMBO J. 18:4383-4393(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN CLATHRIN BINDING.
  4. "In vivo role for actin-regulating kinases in endocytosis and yeast epsin phosphorylation."
    Watson H.A., Cope M.J.T.V., Groen A.C., Drubin D.G., Wendland B.
    Mol. Biol. Cell 12:3668-3679(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PAN1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-395 AND THR-415 BY PRK1, MUTAGENESIS OF THR-395 AND THR-415.
  5. "The yeast Epsin Ent1 is recruited to membranes through multiple independent interactions."
    Aguilar R.C., Watson H.A., Wendland B.
    J. Biol. Chem. 278:10737-10743(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EDE1, SUBCELLULAR LOCATION.
  6. "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 THR-366 AND THR-384, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  7. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-160; SER-163; THR-180; THR-364 AND THR-366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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-163; SER-328; THR-364; THR-366; THR-386 AND THR-388, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-357, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiENT1_YEAST
AccessioniPrimary (citable) accession number: Q12518
Secondary accession number(s): D6VRI8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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