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)

O88339

- EPN1_RAT

UniProt

O88339 - EPN1_RAT

Protein

Epsin-1

Gene

Epn1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations. Regulates receptor-mediated endocytosis.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei8 – 81Phosphatidylinositol lipid headgroup
    Binding sitei11 – 111Phosphatidylinositol lipid headgroup
    Binding sitei25 – 251Phosphatidylinositol lipid headgroup
    Binding sitei30 – 301Phosphatidylinositol lipid headgroup
    Binding sitei63 – 631Phosphatidylinositol lipid headgroup
    Binding sitei73 – 731Phosphatidylinositol lipid headgroup

    GO - Molecular functioni

    1. lipid binding Source: UniProtKB-KW
    2. transcription factor binding Source: RGD

    GO - Biological processi

    1. embryonic organ development Source: Ensembl
    2. endocytosis Source: RGD
    3. female pregnancy Source: Ensembl
    4. in utero embryonic development Source: Ensembl
    5. Notch signaling pathway Source: Ensembl

    Keywords - Biological processi

    Endocytosis

    Keywords - Ligandi

    Lipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Epsin-1
    Alternative name(s):
    EPS-15-interacting protein 1
    Gene namesi
    Name:Epn1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 1

    Organism-specific databases

    RGDi619772. Epn1.

    Subcellular locationi

    Cytoplasm. Cell membrane; Peripheral membrane protein. Nucleus. Membraneclathrin-coated pit
    Note: Associated with the cytoplasmic membrane at sites where clathrin-coated pits are forming. Colocalizes with clathrin and AP-2 in a punctate pattern on the plasma membrane. Colocalizes with clathrin at the Golgi complex. Detected in presynaptic nerve terminals and in synaptosomes. May shuttle to the nucleus when associated with ZBTB16/ZNF145.

    GO - Cellular componenti

    1. coated pit Source: UniProtKB-SubCell
    2. cytoplasm Source: UniProtKB-SubCell
    3. nucleus Source: RGD
    4. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Coated pit, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi6 – 61L → E, H or Q: Reduces lipid binding. 2 Publications
    Mutagenesisi8 – 81R → A: Strongly reduces lipid binding. 2 Publications
    Mutagenesisi63 – 631R → L: Strongly reduces lipid binding. Abolishes lipid binding; when associated with L-73. 3 Publications
    Mutagenesisi72 – 721R → A: Abolishes ZNF145 binding. 2 Publications
    Mutagenesisi73 – 731H → L: Abolishes lipid binding; when associated with L-63. 2 Publications
    Mutagenesisi76 – 761K → A: Strongly reduces lipid binding. 2 Publications
    Mutagenesisi190 – 1901L → A: Abolishes mono-ubiquitination. 2 Publications
    Mutagenesisi257 – 2593LMD → AAA: Strongly reduces clathrin binding. 1 Publication
    Mutagenesisi260 – 2634LADV → AAAA: Strongly reduces clathrin binding. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 575575Epsin-1PRO_0000074515Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei382 – 3821PhosphoserineBy similarity
    Modified residuei418 – 4181PhosphoserineBy similarity
    Modified residuei419 – 4191PhosphoserineBy similarity
    Modified residuei434 – 4341PhosphoserineBy similarity
    Modified residuei453 – 4531PhosphoserineBy similarity
    Modified residuei459 – 4591PhosphothreonineBy similarity
    Modified residuei469 – 4691PhosphothreonineBy similarity
    Modified residuei493 – 4931PhosphothreonineBy similarity

    Post-translational modificationi

    Ubiquitinated.1 Publication
    Phosphorylated on serine and/or threonine residues in mitotic cells. Phosphorylation reduces interaction with REPS2, AP-2 and the membrane fraction. Depolarization of synaptosomes results in dephosphorylation.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiO88339.
    PRIDEiO88339.

    PTM databases

    PhosphoSiteiO88339.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    GenevestigatoriO88339.

    Interactioni

    Subunit structurei

    Monomer. Binds REPS2 and ITSN1 By similarity. Binds EPS15, clathrin, ZBTB16/ZNF145, AP2A1 and AP2A2. Binds ubiquitinated proteins. Interacts with RALBP1 in a complex also containing NUMB and TFAP2A during interphase and mitosis. Interacts with AP2B1.By similarity10 Publications

    Protein-protein interaction databases

    BioGridi250724. 16 interactions.
    IntActiO88339. 2 interactions.
    MINTiMINT-101104.
    STRINGi10116.ENSRNOP00000021286.

    Structurei

    Secondary structure

    1
    575
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi2 – 1514
    Helixi19 – 279
    Beta strandi30 – 334
    Helixi37 – 4610
    Helixi50 – 6415
    Helixi68 – 703
    Helixi71 – 8717
    Helixi90 – 989
    Helixi100 – 1045
    Helixi105 – 1084
    Helixi120 – 13516
    Helixi137 – 15519

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EDUX-ray1.80A12-160[»]
    1EYHX-ray1.56A15-158[»]
    1H0AX-ray1.70A1-158[»]
    1KY6X-ray2.00P375-381[»]
    DisProtiDP00251.
    ProteinModelPortaliO88339.
    SMRiO88339. Positions 1-158.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO88339.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini12 – 144133ENTHPROSITE-ProRule annotationAdd
    BLAST
    Repeati183 – 20220UIM 1Add
    BLAST
    Repeati208 – 22720UIM 2Add
    BLAST
    Repeati233 – 25220UIM 3Add
    BLAST
    Repeati274 – 27631
    Repeati294 – 29632
    Repeati306 – 30833
    Repeati319 – 32134
    Repeati332 – 33435
    Repeati349 – 35136
    Repeati367 – 36937
    Repeati377 – 37938
    Repeati501 – 50331
    Repeati517 – 51932
    Repeati571 – 57333

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni274 – 3791068 X 3 AA repeats of D-P-WAdd
    BLAST
    Regioni501 – 573733 X 3 AA repeats of N-P-FAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi401 – 41010[DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi267 – 572306Ala/Gly/Pro-richAdd
    BLAST

    Domaini

    The NPF repeat domain is involved in EPS15 binding.
    The DPW repeat domain is involved in AP2A2 and clathrin binding.
    The [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif mediates interaction the AP-2 complex subunit AP2B1.By similarity

    Sequence similaritiesi

    Belongs to the epsin family.Curated
    Contains 1 ENTH (epsin N-terminal homology) domain.PROSITE-ProRule annotation
    Contains 3 UIM (ubiquitin-interacting motif) repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG263730.
    GeneTreeiENSGT00550000074611.
    HOGENOMiHOG000008298.
    HOVERGENiHBG006690.
    InParanoidiO88339.
    KOiK12471.
    OMAiDPWGGTQ.
    OrthoDBiEOG7F511Z.
    PhylomeDBiO88339.

    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.
    PF02809. UIM. 2 hits.
    [Graphical view]
    SMARTiSM00273. ENTH. 1 hit.
    SM00726. UIM. 3 hits.
    [Graphical view]
    SUPFAMiSSF48464. SSF48464. 1 hit.
    PROSITEiPS50942. ENTH. 1 hit.
    PS50330. UIM. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O88339-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTSSLRRQM KNIVHNYSEA EIKVREATSN DPWGPSSSLM SEIADLTYNV    50
    VAFSEIMSMI WKRLNDHGKN WRHVYKAMTL MEYLIKTGSE RVSQQCKENM 100
    YAVQTLKDFQ YVDRDGKDQG VNVREKAKQL VALLRDEDRL REERAHALKT 150
    KEKLAQTATA SSAAVGSGPP PEAEQAWPQS SGEEELQLQL ALAMSKEEAD 200
    QPPSCGPEDD VQLQLALSLS REEHDKEERI RRGDDLRLQM AIEESKRETG 250
    GKEESSLMDL ADVFTTPAPP QASDPWGGPA SVPTAVPVAA AASDPWGAPA 300
    VPPAADPWGG AAPTPASGDP WRPAAPTGPS VDPWGGTPAP AAGEGPTSDP 350
    WGSADGGAPV SGPPSSDPWA PAPAFSDPWG GSPAKPSSNG TAVGGFDTEP 400
    DEFSDFDRLR TALPTSGSST GELELLAGEV PARSPGAFDM SGVGGSLAES 450
    VGSPPPAATP TPTPPTRKTP ESFLGPNAAL VDLDSLVSRP GPTPPGAKAS 500
    NPFLPSGAPA TGPSVTNPFQ PAPPATLTLN QLRLSPVPPV PGAPPTYISP 550
    LGGGPGLPPM MPPGPPAPNT NPFLL 575
    Length:575
    Mass (Da):60,158
    Last modified:November 1, 1998 - v1
    Checksum:iD0B770F3B7AB5DDA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF018261 mRNA. Translation: AAC33823.1.
    RefSeqiNP_476477.1. NM_057136.1.
    UniGeneiRn.30007.

    Genome annotation databases

    EnsembliENSRNOT00000021286; ENSRNOP00000021286; ENSRNOG00000015753.
    GeneIDi117277.
    KEGGirno:117277.
    UCSCiRGD:619772. rat.

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    The bubble's bend - Issue 42 of January 2004

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF018261 mRNA. Translation: AAC33823.1 .
    RefSeqi NP_476477.1. NM_057136.1.
    UniGenei Rn.30007.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EDU X-ray 1.80 A 12-160 [» ]
    1EYH X-ray 1.56 A 15-158 [» ]
    1H0A X-ray 1.70 A 1-158 [» ]
    1KY6 X-ray 2.00 P 375-381 [» ]
    DisProti DP00251.
    ProteinModelPortali O88339.
    SMRi O88339. Positions 1-158.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 250724. 16 interactions.
    IntActi O88339. 2 interactions.
    MINTi MINT-101104.
    STRINGi 10116.ENSRNOP00000021286.

    PTM databases

    PhosphoSitei O88339.

    Proteomic databases

    PaxDbi O88339.
    PRIDEi O88339.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000021286 ; ENSRNOP00000021286 ; ENSRNOG00000015753 .
    GeneIDi 117277.
    KEGGi rno:117277.
    UCSCi RGD:619772. rat.

    Organism-specific databases

    CTDi 29924.
    RGDi 619772. Epn1.

    Phylogenomic databases

    eggNOGi NOG263730.
    GeneTreei ENSGT00550000074611.
    HOGENOMi HOG000008298.
    HOVERGENi HBG006690.
    InParanoidi O88339.
    KOi K12471.
    OMAi DPWGGTQ.
    OrthoDBi EOG7F511Z.
    PhylomeDBi O88339.

    Miscellaneous databases

    EvolutionaryTracei O88339.
    NextBioi 620217.
    PROi O88339.

    Gene expression databases

    Genevestigatori O88339.

    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.
    PF02809. UIM. 2 hits.
    [Graphical view ]
    SMARTi SM00273. ENTH. 1 hit.
    SM00726. UIM. 3 hits.
    [Graphical view ]
    SUPFAMi SSF48464. SSF48464. 1 hit.
    PROSITEi PS50942. ENTH. 1 hit.
    PS50330. UIM. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis."
      Chen H., Fre S., Slepnev V.I., Capua M.R., Takei K., Butler M.H., Di Fiore P.P., De Camilli P.
      Nature 394:793-797(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH EPS15; AP2A1 AND AP2A2.
      Strain: Wistar.
      Tissue: Brain.
    2. "A structural explanation for the binding of multiple ligands by the alpha-adaptin appendage domain."
      Owen D.J., Vallis Y., Noble M.E.M., Hunter J.B., Dafforn T.R., Evans P.R., McMahon H.T.
      Cell 97:805-815(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AP2A2.
    3. "The interaction of epsin and Eps15 with the clathrin adaptor AP-2 is inhibited by mitotic phosphorylation and enhanced by stimulation-dependent dephosphorylation in nerve terminals."
      Chen H., Slepnev V.I., Di Fiore P.P., De Camilli P.
      J. Biol. Chem. 274:3257-3260(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, INTERACTION WITH AP-2.
    4. "Crystal structure of the alpha appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly."
      Traub L.M., Downs M.A., Westrich J.L., Fremont D.H.
      Proc. Natl. Acad. Sci. U.S.A. 96:8907-8912(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AP2A2.
    5. "The structure and function of the beta 2-adaptin appendage domain."
      Owen D.J., Vallis Y., Pearse B.M.F., McMahon H.T., Evans P.R.
      EMBO J. 19:4216-4227(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AP2B1.
    6. "Epsin binds to clathrin by associating directly with the clathrin-terminal domain. Evidence for cooperative binding through two discrete sites."
      Drake M.T., Downs M.A., Traub L.M.
      J. Biol. Chem. 275:6479-6489(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF 257-LEU--ASP-259 AND 260-LEU--VAL-263, SUBCELLULAR LOCATION, INTERACTION WITH CLATHRIN HEAVY CHAIN AND AP-2.
    7. "Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis."
      Itoh T., Koshiba S., Kigawa T., Kikuchi A., Yokoyama S., Takenawa T.
      Science 291:1047-1051(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ZBTB16, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-8; ARG-63; ARG-72 AND LYS-76.
    8. "A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins."
      Polo S., Sigismund S., Faretta M., Guidi M., Capua M.R., Bossi G., Chen H., De Camilli P., Di Fiore P.P.
      Nature 416:451-455(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LEU-190, UBIQUITINATION.
    9. "Epsin 1 undergoes nucleocytosolic shuttling and its eps15 interactor NH(2)-terminal homology (ENTH) domain, structurally similar to Armadillo and Heat repeats, interacts with the transcription factor promyelocytic leukemia Zn(2)+ finger protein (PLZF)."
      Hyman J., Chen H., Di Fiore P.P., De Camilli P., Brunger A.T.
      J. Cell Biol. 149:537-546(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 12-160, SUBCELLULAR LOCATION, INTERACTION WITH ZNF145.
    10. Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-158 IN COMPLEX WITH INOSITOL-1,4,5-TRIPHOSPHATE, FUNCTION, MUTAGENESIS OF LEU-6; ARG-63 AND HIS-73.
    11. "Accessory protein recruitment motifs in clathrin-mediated endocytosis."
      Brett T.J., Traub L.M., Fremont D.H.
      Structure 10:797-809(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 375-381 IN COMPLEX WITH AP2A2.

    Entry informationi

    Entry nameiEPN1_RAT
    AccessioniPrimary (citable) accession number: O88339
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 16, 2004
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 121 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata 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. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3