Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q05785

- ENT2_YEAST

UniProt

Q05785 - ENT2_YEAST

Protein

Epsin-2

Gene

ENT2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    1. clathrin binding Source: SGD
    2. lipid binding Source: UniProtKB-KW

    GO - Biological processi

    1. actin cortical patch assembly Source: SGD
    2. actin filament organization Source: SGD
    3. endocytosis Source: SGD

    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: Chromosome XII

    Organism-specific databases

    CYGDiYLR206w.
    SGDiS000004196. ENT2.

    Subcellular locationi

    Cytoplasm. Membrane; Peripheral membrane protein
    Note: Localizes in a punctate pattern. Found in the actin cortical patches, although the majority is located at the cell periphery.

    GO - Cellular componenti

    1. actin cortical patch Source: SGD
    2. membrane Source: UniProtKB-SubCell

    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 – 1651Phosphothreonine3 Publications
    Modified residuei167 – 1671Phosphoserine4 Publications
    Modified residuei430 – 4301Phosphothreonine2 Publications
    Modified residuei434 – 4341Phosphoserine2 Publications
    Modified residuei450 – 4501Phosphothreonine2 Publications
    Modified residuei468 – 4681Phosphothreonine3 Publications
    Modified residuei470 – 4701Phosphothreonine2 Publications

    Post-translational modificationi

    Phosphorylated by PRK1.5 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ05785.
    PaxDbiQ05785.
    PeptideAtlasiQ05785.

    Expressioni

    Gene expression databases

    GenevestigatoriQ05785.

    Interactioni

    Protein-protein interaction databases

    BioGridi31474. 56 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 – 269
    Beta strandi29 – 313
    Helixi36 – 4510
    Helixi49 – 6315
    Helixi67 – 693
    Helixi70 – 8617
    Helixi89 – 979
    Helixi99 – 1046
    Helixi105 – 1073
    Helixi120 – 13314
    Helixi136 – 14510

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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
    Repeati175 – 19420UIM 1Add
    BLAST
    Repeati206 – 22520UIM 2Add
    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) repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG263730.
    GeneTreeiENSGT00720000109538.
    HOGENOMiHOG000216614.
    KOiK12471.
    OMAiFRHENES.
    OrthoDBiEOG7KM63T.

    Family and domain databases

    Gene3Di1.25.40.90. 1 hit.
    InterProiIPR008942. ENTH_VHS.
    IPR013809. Epsin-like_N.
    IPR001026. Epsin_dom_N.
    IPR003903. Ubiquitin-int_motif.
    [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

    MSKQFVRSAK NMMKGYSSTQ VLVRDATAND SRTPSIDTLD DLAQRSYDSV    50
    DFFEIMDMLD KRLNDKGKYW RHVAKSLTVL DYLVRFGSEN CVLWCRENFY 100
    VIKTLREFRH ENESGFDEGQ IIRVKAKELV SLLNDEERLR EERSMNTRNR 150
    RANRAARPRP RRQRTRSNPH DSSPSYQDDL EKALEESRIT AQEDEQRRRE 200
    LAQYDDEDPD FQAALQLSKE EEELKQLQEL QRLQKQQQSL SQFQAPLQQQ 250
    QPQQQPAYYD IFGNPISQDE YLQYQYQQDQ EQAMAQQRWL DQQQEQQQLA 300
    EQQYFQQQQQ AAAAASALQQ QQTAANMQQQ QQQPADFQQP LPTGSNNPFS 350
    MDNLERQKQE QQHAQLQRQQ EEARQQQEQL KLQQLQRQQQ EEAQLHQKRQ 400
    EEAQLQQQQA QLLQQQAQFQ QQQPLKQTRT GNQSISDKYS DLNTLLATGT 450
    GIDTFGNTGE ARIPAQHTKT GTFINSQGTG YKQVTNEPKN NPFLSNQYTG 500
    LPSTNIVPTQ TGYGFGNQPQ SPPTNSPQQN PTGISYSQPQ QQQQPQQQPQ 550
    YMQNFQQQQP QYAQNFQQQP QYTQNYQQQP QYIQPHQQQQ QQQQQQQQQQ 600
    GYTPDQGVSL IDL 613
    Length:613
    Mass (Da):71,807
    Last modified:November 1, 1996 - v1
    Checksum:iCEC1B2D04C0F7D86
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U14913 Genomic DNA. Translation: AAB67428.1 .
    BK006945 Genomic DNA. Translation: DAA09523.1 .
    PIRi S48557.
    RefSeqi NP_013307.1. NM_001182093.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4GZC X-ray 1.30 A 1-149 [» ]
    4GZD X-ray 1.75 A 1-149 [» ]
    ProteinModelPortali Q05785.
    SMRi Q05785. Positions 15-146.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31474. 56 interactions.
    DIPi DIP-2698N.
    IntActi Q05785. 16 interactions.
    MINTi MINT-687167.
    STRINGi 4932.YLR206W.

    Proteomic databases

    MaxQBi Q05785.
    PaxDbi Q05785.
    PeptideAtlasi Q05785.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YLR206W ; YLR206W ; YLR206W .
    GeneIDi 850903.
    KEGGi sce:YLR206W.

    Organism-specific databases

    CYGDi YLR206w.
    SGDi S000004196. ENT2.

    Phylogenomic databases

    eggNOGi NOG263730.
    GeneTreei ENSGT00720000109538.
    HOGENOMi HOG000216614.
    KOi K12471.
    OMAi FRHENES.
    OrthoDBi EOG7KM63T.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32324-MONOMER.

    Miscellaneous databases

    NextBioi 967293.

    Gene expression databases

    Genevestigatori Q05785.

    Family and domain databases

    Gene3Di 1.25.40.90. 1 hit.
    InterProi IPR008942. ENTH_VHS.
    IPR013809. Epsin-like_N.
    IPR001026. Epsin_dom_N.
    IPR003903. Ubiquitin-int_motif.
    [Graphical view ]
    Pfami PF01417. ENTH. 1 hit.
    [Graphical view ]
    SMARTi SM00273. ENTH. 1 hit.
    SM00726. UIM. 2 hits.
    [Graphical view ]
    SUPFAMi SSF48464. SSF48464. 1 hit.
    PROSITEi PS50942. ENTH. 1 hit.
    PS50330. UIM. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 120 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