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P42566

- EPS15_HUMAN

UniProt

P42566 - EPS15_HUMAN

Protein

Epidermal growth factor receptor substrate 15

Gene

EPS15

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 162 (01 Oct 2014)
      Sequence version 2 (07 Jun 2005)
      Previous versions | rss
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    Functioni

    Involved in cell growth regulation. May be involved in the regulation of mitogenic signals and control of cell proliferation. Involved in the internalization of ligand-inducible receptors of the receptor tyrosine kinase (RTK) type, in particular EGFR. Plays a role in the assembly of clathrin-coated pits (CCPs). Acts as a clathrin adapter required for post-Golgi trafficking. Seems to be involved in CCPs maturation including invagination or budding. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2.4 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi173 – 184121Add
    BLAST
    Calcium bindingi236 – 247122Add
    BLAST

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. polyubiquitin binding Source: UniProtKB
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell proliferation Source: ProtInc
    2. clathrin coat assembly Source: BHF-UCL
    3. endocytic recycling Source: BHF-UCL
    4. endocytosis Source: UniProtKB-KW
    5. epidermal growth factor receptor signaling pathway Source: Reactome
    6. Golgi to endosome transport Source: UniProtKB
    7. negative regulation of epidermal growth factor receptor signaling pathway Source: Reactome
    8. protein transport Source: UniProtKB-KW
    9. vesicle organization Source: UniProtKB

    Keywords - Biological processi

    Endocytosis, Protein transport, Transport

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_12484. EGFR downregulation.
    SignaLinkiP42566.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Epidermal growth factor receptor substrate 15
    Short name:
    Protein Eps15
    Alternative name(s):
    Protein AF-1p
    Gene namesi
    Name:EPS15
    Synonyms:AF1P
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:3419. EPS15.

    Subcellular locationi

    Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Membraneclathrin-coated pit
    Note: Recruited to the plasma membrane upon EGFR activation and localizes to coated pits.
    Isoform 2 : Early endosome membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication
    Note: Colocalizes with HGS on bilayered clathrin coats on endosomes.

    GO - Cellular componenti

    1. AP-2 adaptor complex Source: Ensembl
    2. ciliary membrane Source: Ensembl
    3. coated pit Source: UniProtKB
    4. cytoplasm Source: HPA
    5. cytosol Source: Reactome
    6. early endosome membrane Source: UniProtKB-SubCell
    7. intracellular membrane-bounded organelle Source: HPA
    8. membrane Source: UniProtKB
    9. plasma membrane Source: HGNC

    Keywords - Cellular componenti

    Cell membrane, Coated pit, Cytoplasm, Endosome, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving EPS15 is found in acute leukemias. Translocation t(1;11)(p32;q23) with KMT2A/MLL1. The result is a rogue activator protein.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi154 – 1541V → E: Loss of interaction with STON2 NPF motifs. 1 Publication
    Mutagenesisi169 – 1691W → A: Loss of interaction with STON2 NPF motifs. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    PharmGKBiPA27838.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 896895Epidermal growth factor receptor substrate 15PRO_0000146116Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei108 – 1081Phosphoserine1 Publication
    Modified residuei140 – 1401Phosphoserine1 Publication
    Modified residuei323 – 3231Phosphoserine3 Publications
    Modified residuei324 – 3241Phosphoserine3 Publications
    Modified residuei467 – 4671Phosphoserine1 Publication
    Modified residuei470 – 4701Phosphoserine1 Publication
    Modified residuei485 – 4851Phosphoserine3 Publications
    Modified residuei777 – 7771PhosphothreonineBy similarity
    Modified residuei790 – 7901Phosphoserine2 Publications
    Modified residuei796 – 7961Phosphoserine3 Publications
    Modified residuei814 – 8141Phosphoserine5 Publications
    Modified residuei849 – 8491Phosphotyrosine; by EGFR1 Publication

    Post-translational modificationi

    Phosphorylation on Tyr-849 is involved in the internalization of EGFR. Not required for membrane translocation after EGF treatment or for targeting to coated pits, but essential for a subsequent step in EGFR endocytosis By similarity. Phosphorylated on serine upon DNA damage, probably by ATM or ATR.By similarity7 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP42566.
    PaxDbiP42566.
    PeptideAtlasiP42566.
    PRIDEiP42566.

    2D gel databases

    OGPiP42566.

    PTM databases

    PhosphoSiteiP42566.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.

    Gene expression databases

    ArrayExpressiP42566.
    BgeeiP42566.
    CleanExiHS_EPS15.
    GenevestigatoriP42566.

    Organism-specific databases

    HPAiCAB010164.
    HPA008451.

    Interactioni

    Subunit structurei

    Interacts with SGIP1 By similarity. Interacts with HGS; the interaction bridges the interaction of STAM or STAM2 with EPS15. Isoform 2 interacts with HGS and AP2A2. Part of a complex at least composed of EPS15, HGS, and either STAM1 or STAM2. Binds AP2A2. Interacts with AP2B1; clathrin competes with EPS15. Binds STON2 and EPN1. Interacts (via its SH3-binding sites) with CRK. Interacts with SH3BP4/TTP. Interacts with ERBB2. Interacts with FCHO1. Interacts with FCHO2. Interacts (via EH domains) with DAB2. Interacts (via UIM repeats) with CORO7 (when ubiquitinated at 'Lys-472').By similarity16 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FCHO2Q0JRZ93EBI-396684,EBI-2609756
    Fcho2Q3UQN23EBI-396684,EBI-6094986From a different organism.
    NCK1P163332EBI-396684,EBI-389883
    STON2Q8WXE917EBI-396684,EBI-539742
    UBQLN1Q9UMX05EBI-396684,EBI-741480

    Protein-protein interaction databases

    BioGridi108374. 113 interactions.
    DIPiDIP-33064N.
    IntActiP42566. 39 interactions.
    MINTiMINT-107223.
    STRINGi9606.ENSP00000360798.

    Structurei

    Secondary structure

    1
    896
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi126 – 13611
    Beta strandi142 – 1443
    Beta strandi145 – 1473
    Helixi148 – 1569
    Turni157 – 1593
    Helixi162 – 17211
    Beta strandi177 – 1793
    Helixi182 – 19716
    Turni207 – 2093
    Helixi212 – 2143
    Helixi223 – 23513
    Beta strandi240 – 2434
    Helixi245 – 2539
    Turni254 – 2563
    Helixi259 – 26911
    Beta strandi274 – 2785
    Turni279 – 2813
    Helixi282 – 29312
    Turni305 – 3073
    Helixi723 – 7264

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1C07NMR-A217-311[»]
    1EH2NMR-A121-218[»]
    1F8HNMR-A121-215[»]
    1FF1NMR-A121-215[»]
    2IV9X-ray1.90P723-730[»]
    2JXCNMR-A121-215[»]
    ProteinModelPortaliP42566.
    SMRiP42566. Positions 7-105, 121-215, 217-311, 371-420, 448-475.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP42566.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini15 – 10490EH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini128 – 21689EH 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini160 – 19536EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini223 – 25836EF-hand 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini224 – 31491EH 3PROSITE-ProRule annotationAdd
    BLAST
    Repeati599 – 60131
    Repeati623 – 62532
    Repeati629 – 63133
    Repeati634 – 63634
    Repeati640 – 64235
    Repeati645 – 64736
    Repeati651 – 65337
    Repeati664 – 66638
    Repeati672 – 67439
    Repeati692 – 694310
    Repeati709 – 711311
    Repeati737 – 739312
    Repeati798 – 800313
    Repeati804 – 806314
    Repeati825 – 827315
    Repeati851 – 87020UIM 1Add
    BLAST
    Repeati877 – 89620UIM 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 330329Interaction with DAB2By similarityAdd
    BLAST
    Regioni599 – 82722915 X 3 AA repeats of D-P-FAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi768 – 7747SH3-binding

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi768 – 85083Pro-richAdd
    BLAST

    Domaini

    The EH domain interacts with Asn-Pro-Phe (NPF) motifs of target proteins.1 Publication
    The UIM (ubiquitin-interacting motif) repeats specifically bind 'Lys-33'-linked ubiquitin.2 Publications

    Sequence similaritiesi

    Contains 2 EF-hand domains.PROSITE-ProRule annotation
    Contains 3 EH domains.PROSITE-ProRule annotation
    Contains 2 UIM (ubiquitin-interacting motif) repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, SH3-binding

    Phylogenomic databases

    eggNOGiNOG301764.
    HOGENOMiHOG000004804.
    HOVERGENiHBG005591.
    InParanoidiP42566.
    KOiK12472.
    OMAiPPPRFHD.
    PhylomeDBiP42566.
    TreeFamiTF324293.

    Family and domain databases

    Gene3Di1.10.238.10. 3 hits.
    InterProiIPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR000261. EPS15_homology.
    IPR003903. Ubiquitin-int_motif.
    [Graphical view]
    SMARTiSM00054. EFh. 3 hits.
    SM00027. EH. 3 hits.
    SM00726. UIM. 3 hits.
    [Graphical view]
    PROSITEiPS00018. EF_HAND_1. 2 hits.
    PS50222. EF_HAND_2. 4 hits.
    PS50031. EH. 3 hits.
    PS50330. UIM. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P42566-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAAAAQLSLT QLSSGNPVYE KYYRQVDTGN TGRVLASDAA AFLKKSGLPD    50
    LILGKIWDLA DTDGKGILNK QEFFVALRLV ACAQNGLEVS LSSLNLAVPP 100
    PRFHDTSSPL LISGTSAAEL PWAVKPEDKA KYDAIFDSLS PVNGFLSGDK 150
    VKPVLLNSKL PVDILGRVWE LSDIDHDGML DRDEFAVAMF LVYCALEKEP 200
    VPMSLPPALV PPSKRKTWVV SPAEKAKYDE IFLKTDKDMD GFVSGLEVRE 250
    IFLKTGLPST LLAHIWSLCD TKDCGKLSKD QFALAFHLIS QKLIKGIDPP 300
    HVLTPEMIPP SDRASLQKNI IGSSPVADFS AIKELDTLNN EIVDLQREKN 350
    NVEQDLKEKE DTIKQRTSEV QDLQDEVQRE NTNLQKLQAQ KQQVQELLDE 400
    LDEQKAQLEE QLKEVRKKCA EEAQLISSLK AELTSQESQI STYEEELAKA 450
    REELSRLQQE TAELEESVES GKAQLEPLQQ HLQDSQQEIS SMQMKLMEMK 500
    DLENHNSQLN WCSSPHSILV NGATDYCSLS TSSSETANLN EHVEGQSNLE 550
    SEPIHQESPA RSSPELLPSG VTDENEVTTA VTEKVCSELD NNRHSKEEDP 600
    FNVDSSSLTG PVADTNLDFF QSDPFVGSDP FKDDPFGKID PFGGDPFKGS 650
    DPFASDCFFR QSTDPFATSS TDPFSAANNS SITSVETLKH NDPFAPGGTV 700
    VAASDSATDP FASVFGNESF GGGFADFSTL SKVNNEDPFR SATSSSVSNV 750
    VITKNVFEET SVKSEDEPPA LPPKIGTPTR PCPLPPGKRS INKLDSPDPF 800
    KLNDPFQPFP GNDSPKEKDP EIFCDPFTSA TTTTNKEADP SNFANFSAYP 850
    SEEDMIEWAK RESEREEEQR LARLNQQEQE DLELAIALSK SEISEA 896
    Length:896
    Mass (Da):98,656
    Last modified:June 7, 2005 - v2
    Checksum:iA1B9FE15B47ABAFF
    GO
    Isoform 2 (identifier: P42566-2) [UniParc]FASTAAdd to Basket

    Also known as: Eps15b

    The sequence of this isoform differs from the canonical sequence as follows:
         1-314: Missing.
         315-346: SLQKNIIGSSPVADFSAIKELDTLNNEIVDLQ → MYLKSDSGLGGWITIPAVADVLKYSCIVCWSS

    Show »
    Length:582
    Mass (Da):64,376
    Checksum:i2A7BACA24604E8CA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti446 – 4461Missing in BX647676. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti822 – 8221I → M.1 Publication
    Corresponds to variant rs17567 [ dbSNP | Ensembl ].
    VAR_016142

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 314314Missing in isoform 2. 1 PublicationVSP_036168Add
    BLAST
    Alternative sequencei315 – 34632SLQKN…IVDLQ → MYLKSDSGLGGWITIPAVAD VLKYSCIVCWSS in isoform 2. 1 PublicationVSP_036169Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U07707 mRNA. Translation: AAA52101.1.
    Z29064 mRNA. Translation: CAA82305.1.
    AK313396 mRNA. Translation: BAG36194.1.
    DQ367924 mRNA. Translation: ABD34786.1.
    BX647676 mRNA. No translation available.
    AL671986, AC104170 Genomic DNA. Translation: CAI13030.1.
    CH471059 Genomic DNA. Translation: EAX06823.1.
    CCDSiCCDS557.1. [P42566-1]
    PIRiS43074.
    RefSeqiNP_001153441.1. NM_001159969.1. [P42566-2]
    NP_001972.1. NM_001981.2. [P42566-1]
    UniGeneiHs.83722.

    Genome annotation databases

    EnsembliENST00000371733; ENSP00000360798; ENSG00000085832. [P42566-1]
    GeneIDi2060.
    KEGGihsa:2060.
    UCSCiuc001csp.3. human. [P42566-2]
    uc001csq.1. human. [P42566-1]

    Polymorphism databases

    DMDMi67476728.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U07707 mRNA. Translation: AAA52101.1 .
    Z29064 mRNA. Translation: CAA82305.1 .
    AK313396 mRNA. Translation: BAG36194.1 .
    DQ367924 mRNA. Translation: ABD34786.1 .
    BX647676 mRNA. No translation available.
    AL671986 , AC104170 Genomic DNA. Translation: CAI13030.1 .
    CH471059 Genomic DNA. Translation: EAX06823.1 .
    CCDSi CCDS557.1. [P42566-1 ]
    PIRi S43074.
    RefSeqi NP_001153441.1. NM_001159969.1. [P42566-2 ]
    NP_001972.1. NM_001981.2. [P42566-1 ]
    UniGenei Hs.83722.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1C07 NMR - A 217-311 [» ]
    1EH2 NMR - A 121-218 [» ]
    1F8H NMR - A 121-215 [» ]
    1FF1 NMR - A 121-215 [» ]
    2IV9 X-ray 1.90 P 723-730 [» ]
    2JXC NMR - A 121-215 [» ]
    ProteinModelPortali P42566.
    SMRi P42566. Positions 7-105, 121-215, 217-311, 371-420, 448-475.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108374. 113 interactions.
    DIPi DIP-33064N.
    IntActi P42566. 39 interactions.
    MINTi MINT-107223.
    STRINGi 9606.ENSP00000360798.

    PTM databases

    PhosphoSitei P42566.

    Polymorphism databases

    DMDMi 67476728.

    2D gel databases

    OGPi P42566.

    Proteomic databases

    MaxQBi P42566.
    PaxDbi P42566.
    PeptideAtlasi P42566.
    PRIDEi P42566.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371733 ; ENSP00000360798 ; ENSG00000085832 . [P42566-1 ]
    GeneIDi 2060.
    KEGGi hsa:2060.
    UCSCi uc001csp.3. human. [P42566-2 ]
    uc001csq.1. human. [P42566-1 ]

    Organism-specific databases

    CTDi 2060.
    GeneCardsi GC01M051819.
    HGNCi HGNC:3419. EPS15.
    HPAi CAB010164.
    HPA008451.
    MIMi 600051. gene.
    neXtProti NX_P42566.
    PharmGKBi PA27838.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG301764.
    HOGENOMi HOG000004804.
    HOVERGENi HBG005591.
    InParanoidi P42566.
    KOi K12472.
    OMAi PPPRFHD.
    PhylomeDBi P42566.
    TreeFami TF324293.

    Enzyme and pathway databases

    Reactomei REACT_12484. EGFR downregulation.
    SignaLinki P42566.

    Miscellaneous databases

    ChiTaRSi EPS15. human.
    EvolutionaryTracei P42566.
    GeneWikii EPS15.
    GenomeRNAii 2060.
    NextBioi 8377.
    PROi P42566.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P42566.
    Bgeei P42566.
    CleanExi HS_EPS15.
    Genevestigatori P42566.

    Family and domain databases

    Gene3Di 1.10.238.10. 3 hits.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR000261. EPS15_homology.
    IPR003903. Ubiquitin-int_motif.
    [Graphical view ]
    SMARTi SM00054. EFh. 3 hits.
    SM00027. EH. 3 hits.
    SM00726. UIM. 3 hits.
    [Graphical view ]
    PROSITEi PS00018. EF_HAND_1. 2 hits.
    PS50222. EF_HAND_2. 4 hits.
    PS50031. EH. 3 hits.
    PS50330. UIM. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The human eps15 gene, encoding a tyrosine kinase substrate, is conserved in evolution and maps to 1p31-p32."
      Wong W.T., Kraus M.H., Carlomagno F., Zelano A., Druck T., Croce C.M., Huebner K., di Fiore P.P.
      Oncogene 9:1591-1597(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-822.
      Tissue: Melanoma.
    2. "A novel gene, AF-1p, fused to HRX in t(1;11)(p32;q23), is not related to AF-4, AF-9 nor ENL."
      Bernard O.A., Mauchauffe M., Mecucci C., van den Berghe H., Berger R.
      Oncogene 9:1039-1045(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Trachea.
    4. "Eps15 in human umbilical vein endothelial cells."
      Kronstein R., Grossklaus S., Schnittler H.-J.
      Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    6. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "Interaction between the amino-terminal SH3 domain of CRK and its natural target proteins."
      Matsuda M., Ota S., Tanimura R., Nakamura H., Matuoka K., Takenawa T., Nagashima K., Kurata T.
      J. Biol. Chem. 271:14468-14472(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CRK.
    9. "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: INTERACTION WITH EPN1.
    10. "STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes."
      Bache K.G., Raiborg C., Mehlum A., Stenmark H.
      J. Biol. Chem. 278:12513-12521(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HGS AND STAM2.
    11. "TTP specifically regulates the internalization of the transferrin receptor."
      Tosoni D., Puri C., Confalonieri S., Salcini A.E., De Camilli P., Tacchetti C., Di Fiore P.P.
      Cell 123:875-888(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SH3BP4.
    12. "Endosomal transport of ErbB-2: mechanism for nuclear entry of the cell surface receptor."
      Giri D.K., Ali-Seyed M., Li L.Y., Lee D.F., Ling P., Bartholomeusz G., Wang S.C., Hung M.C.
      Mol. Cell. Biol. 25:11005-11018(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ERBB2.
    13. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-485, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    15. "An endosomally localized isoform of Eps15 interacts with Hrs to mediate degradation of epidermal growth factor receptor."
      Roxrud I., Raiborg C., Pedersen N.M., Stang E., Stenmark H.
      J. Cell Biol. 180:1205-1218(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ALTERNATIVE SPLICING (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), INTERACTION WITH HSG AND AP2A2.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-796 AND SER-814, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    17. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-323; SER-485 AND SER-814, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    20. "Endocytic accessory proteins are functionally distinguished by their differential effects on the maturation of clathrin-coated pits."
      Mettlen M., Stoeber M., Loerke D., Antonescu C.N., Danuser G., Schmid S.L.
      Mol. Biol. Cell 20:3251-3260(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    21. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-323; SER-324; SER-814 AND TYR-849, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    22. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324; SER-467; SER-470; SER-790; SER-796 AND SER-814, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    23. "FCHo proteins are nucleators of clathrin-mediated endocytosis."
      Henne W.M., Boucrot E., Meinecke M., Evergren E., Vallis Y., Mittal R., McMahon H.T.
      Science 328:1281-1284(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FCHO2.
    24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "Characterization of the EFC/F-BAR domain protein, FCHO2."
      Uezu A., Umeda K., Tsujita K., Suetsugu S., Takenawa T., Nakanishi H.
      Genes Cells 16:868-878(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FCHO2.
    26. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324; SER-485; SER-790; SER-796 AND SER-814, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "The clathrin adaptor Dab2 recruits EH domain scaffold proteins to regulate integrin beta1 endocytosis."
      Teckchandani A., Mulkearns E.E., Randolph T.W., Toida N., Cooper J.A.
      Mol. Biol. Cell 23:2905-2916(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DAB2.
    28. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "Distinct and separable activities of the endocytic clathrin-coat components Fcho1/2 and AP-2 in developmental patterning."
      Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B., Tsang M., Traub L.M.
      Nat. Cell Biol. 14:488-501(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FCHO1.
    30. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. "K33-linked polyubiquitination of coronin 7 by Cul3-KLHL20 ubiquitin E3 ligase regulates protein trafficking."
      Yuan W.C., Lee Y.R., Lin S.Y., Chang L.Y., Tan Y.P., Hung C.C., Kuo J.C., Liu C.H., Lin M.Y., Xu M., Chen Z.J., Chen R.H.
      Mol. Cell 54:586-600(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CORO7.
    32. "Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain."
      de Beer T., Carter R.E., Lobel-Rice K.E., Sorkin A., Overduin M.
      Science 281:1357-1360(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 121-215 IN COMPLEX WITH CALCIUM IONS.
    33. "Solution structure of Eps15's third EH domain reveals coincident Phe-Trp and Asn-Pro-Phe binding sites."
      Enmon J.L., de Beer T., Overduin M.
      Biochemistry 39:4309-4319(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 217-311 IN COMPLEX WITH CALCIUM IONS.
    34. Cited for: STRUCTURE BY NMR OF 121-215 IN COMPLEX WITH PEPTIDE LIGAND AND CALCIUM IONS, DOMAIN.
    35. "Role of the AP2 beta-appendage hub in recruiting partners for clathrin-coated vesicle assembly."
      Schmid E.M., Ford M.G.J., Burtey A., Praefcke G.J.K., Peak-Chew S.-Y., Mills I.G., Benmerah A., McMahon H.T.
      PLoS Biol. 4:E262-E262(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 719-730 IN COMPLEX WITH AP2B1, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, FUNCTION.
    36. "Structure of the Eps15-stonin2 complex provides a molecular explanation for EH-domain ligand specificity."
      Rumpf J., Simon B., Jung N., Maritzen T., Haucke V., Sattler M., Groemping Y.
      EMBO J. 27:558-569(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 121-215 IN COMPLEX WITH STON2 AND CALCIUM IONS, MUTAGENESIS OF VAL-154 AND TRP-169, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiEPS15_HUMAN
    AccessioniPrimary (citable) accession number: P42566
    Secondary accession number(s): B2R8J7, D3DPJ2, Q5SRH4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: June 7, 2005
    Last modified: October 1, 2014
    This is version 162 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Caution

    Studies in clathrin-mediated endocytosis of ITGB1 and TFR used a siRNA mixture of EPS15 and EPS15L1, and a Dab2 mutant with impaired binding to EH domain-containing proteins EPS15 and ITSN1 suggesting a partially overlapping role of the EH domain-containing proteins.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3