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Protein

Epsin-2

Gene

ENT2

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.1 Publication

GO - Molecular functioni

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

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-32324-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Epsin-2
Gene namesi
Name:ENT2
Ordered Locus Names:YLR206W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XII

Organism-specific databases

CYGDiYLR206w.
EuPathDBiFungiDB:YLR206W.
SGDiS000004196. ENT2.

Subcellular locationi

GO - Cellular componenti

  • actin cortical patch Source: SGD
  • membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 613613Epsin-2PRO_0000074525Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei165 – 1651Phosphothreonine2 Publications
Modified residuei167 – 1671Phosphoserine3 Publications
Modified residuei430 – 4301Phosphothreonine1 Publication
Modified residuei434 – 4341Phosphoserine1 Publication
Modified residuei450 – 4501Phosphothreonine1 Publication
Modified residuei468 – 4681Phosphothreonine2 Publications
Modified residuei470 – 4701Phosphothreonine1 Publication

Post-translational modificationi

Phosphorylated by PRK1.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ05785.
PaxDbiQ05785.
PeptideAtlasiQ05785.

Interactioni

Protein-protein interaction databases

BioGridi31474. 57 interactions.
DIPiDIP-2698N.
IntActiQ05785. 16 interactions.
MINTiMINT-687167.
STRINGi4932.YLR206W.

Structurei

Secondary structure

1
613
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi18 – 269Combined sources
Beta strandi29 – 313Combined sources
Helixi36 – 4510Combined sources
Helixi49 – 6315Combined sources
Helixi67 – 693Combined sources
Helixi70 – 8617Combined sources
Helixi89 – 979Combined sources
Helixi99 – 1046Combined sources
Helixi105 – 1073Combined sources
Helixi120 – 13314Combined sources
Helixi136 – 14510Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GZCX-ray1.30A1-149[»]
4GZDX-ray1.75A1-149[»]
ProteinModelPortaliQ05785.
SMRiQ05785. Positions 15-146.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 143133ENTHPROSITE-ProRule annotationAdd
BLAST
Domaini175 – 19420UIM 1PROSITE-ProRule annotationAdd
BLAST
Domaini206 – 22520UIM 2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi138 – 16629Arg-richAdd
BLAST
Compositional biasi192 – 606415Gln-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

eggNOGiNOG263730.
GeneTreeiENSGT00720000109538.
HOGENOMiHOG000216614.
InParanoidiQ05785.
KOiK12471.
OMAiGFVQPQA.
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.

Q05785-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKQFVRSAK NMMKGYSSTQ VLVRDATAND SRTPSIDTLD DLAQRSYDSV
60 70 80 90 100
DFFEIMDMLD KRLNDKGKYW RHVAKSLTVL DYLVRFGSEN CVLWCRENFY
110 120 130 140 150
VIKTLREFRH ENESGFDEGQ IIRVKAKELV SLLNDEERLR EERSMNTRNR
160 170 180 190 200
RANRAARPRP RRQRTRSNPH DSSPSYQDDL EKALEESRIT AQEDEQRRRE
210 220 230 240 250
LAQYDDEDPD FQAALQLSKE EEELKQLQEL QRLQKQQQSL SQFQAPLQQQ
260 270 280 290 300
QPQQQPAYYD IFGNPISQDE YLQYQYQQDQ EQAMAQQRWL DQQQEQQQLA
310 320 330 340 350
EQQYFQQQQQ AAAAASALQQ QQTAANMQQQ QQQPADFQQP LPTGSNNPFS
360 370 380 390 400
MDNLERQKQE QQHAQLQRQQ EEARQQQEQL KLQQLQRQQQ EEAQLHQKRQ
410 420 430 440 450
EEAQLQQQQA QLLQQQAQFQ QQQPLKQTRT GNQSISDKYS DLNTLLATGT
460 470 480 490 500
GIDTFGNTGE ARIPAQHTKT GTFINSQGTG YKQVTNEPKN NPFLSNQYTG
510 520 530 540 550
LPSTNIVPTQ TGYGFGNQPQ SPPTNSPQQN PTGISYSQPQ QQQQPQQQPQ
560 570 580 590 600
YMQNFQQQQP QYAQNFQQQP QYTQNYQQQP QYIQPHQQQQ QQQQQQQQQQ
610
GYTPDQGVSL IDL
Length:613
Mass (Da):71,807
Last modified:November 1, 1996 - v1
Checksum:iCEC1B2D04C0F7D86
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14913 Genomic DNA. Translation: AAB67428.1.
BK006945 Genomic DNA. Translation: DAA09523.1.
PIRiS48557.
RefSeqiNP_013307.1. NM_001182093.1.

Genome annotation databases

EnsemblFungiiYLR206W; YLR206W; YLR206W.
GeneIDi850903.
KEGGisce:YLR206W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14913 Genomic DNA. Translation: AAB67428.1.
BK006945 Genomic DNA. Translation: DAA09523.1.
PIRiS48557.
RefSeqiNP_013307.1. NM_001182093.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GZCX-ray1.30A1-149[»]
4GZDX-ray1.75A1-149[»]
ProteinModelPortaliQ05785.
SMRiQ05785. Positions 15-146.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31474. 57 interactions.
DIPiDIP-2698N.
IntActiQ05785. 16 interactions.
MINTiMINT-687167.
STRINGi4932.YLR206W.

Proteomic databases

MaxQBiQ05785.
PaxDbiQ05785.
PeptideAtlasiQ05785.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR206W; YLR206W; YLR206W.
GeneIDi850903.
KEGGisce:YLR206W.

Organism-specific databases

CYGDiYLR206w.
EuPathDBiFungiDB:YLR206W.
SGDiS000004196. ENT2.

Phylogenomic databases

eggNOGiNOG263730.
GeneTreeiENSGT00720000109538.
HOGENOMiHOG000216614.
InParanoidiQ05785.
KOiK12471.
OMAiGFVQPQA.
OrthoDBiEOG7KM63T.

Enzyme and pathway databases

BioCyciYEAST:G3O-32324-MONOMER.

Miscellaneous databases

NextBioi967293.
PROiQ05785.

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 XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(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.
  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: SUBCELLULAR LOCATION, PHOSPHORYLATION.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  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-165; SER-167 AND THR-468, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  7. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-430 AND SER-434, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167 AND THR-450, 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 THR-165; SER-167; THR-468 AND THR-470, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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].

Entry informationi

Entry nameiENT2_YEAST
AccessioniPrimary (citable) accession number: Q05785
Secondary accession number(s): D6VYK7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: November 1, 1996
Last modified: June 24, 2015
This is version 128 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 1970 molecules/cell in log phase SD medium.1 Publication

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

External Data

Dasty 3

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 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.