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P42567

- EPS15_MOUSE

UniProt

P42567 - EPS15_MOUSE

Protein

Epidermal growth factor receptor substrate 15

Gene

Eps15

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      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.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi173 – 184121PROSITE-ProRule annotationAdd
    BLAST
    Calcium bindingi236 – 247122PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

    1. clathrin coat assembly Source: Ensembl
    2. endocytosis Source: UniProtKB-KW
    3. Golgi to endosome transport Source: UniProtKB
    4. protein transport Source: UniProtKB-KW

    Keywords - Biological processi

    Endocytosis, Protein transport, Transport

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_203917. EGFR downregulation.

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:104583. 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 By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
    Note: Colocalizes with HGS on bilayered clathrin coats on endosomes.By similarity

    GO - Cellular componenti

    1. AP-2 adaptor complex Source: UniProtKB
    2. ciliary membrane Source: MGI
    3. clathrin-coated vesicle Source: UniProtKB
    4. clathrin coat of coated pit Source: MGI
    5. coated pit Source: MGI
    6. early endosome membrane Source: UniProtKB-SubCell
    7. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Coated pit, Cytoplasm, Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi850 – 8501Y → F: Inefficient EGFR internalization. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 897896Epidermal growth factor receptor substrate 15PRO_0000146117Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei108 – 1081PhosphoserineBy similarity
    Modified residuei140 – 1401PhosphoserineBy similarity
    Modified residuei323 – 3231PhosphoserineBy similarity
    Modified residuei324 – 3241Phosphoserine1 Publication
    Modified residuei467 – 4671PhosphoserineBy similarity
    Modified residuei470 – 4701PhosphoserineBy similarity
    Modified residuei485 – 4851PhosphoserineBy similarity
    Modified residuei779 – 7791Phosphothreonine1 Publication
    Modified residuei798 – 7981PhosphoserineBy similarity
    Modified residuei816 – 8161PhosphoserineBy similarity
    Modified residuei850 – 8501Phosphotyrosine; by EGFR1 Publication

    Post-translational modificationi

    Phosphorylated on serine upon DNA damage, probably by ATM or ATR By similarity. Phosphorylation on Tyr-850 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 similarity3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP42567.
    PaxDbiP42567.
    PRIDEiP42567.

    PTM databases

    PhosphoSiteiP42567.

    Expressioni

    Gene expression databases

    ArrayExpressiP42567.
    BgeeiP42567.
    GenevestigatoriP42567.

    Interactioni

    Subunit structurei

    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 (via UIM repeats) with CORO7 (when ubiquitinated at 'Lys-472') By similarity. Interacts with FCHO1 By similarity. Interacts with FCHO2. Interacts with SGIP1. Interacts (via EH domains) with DAB2.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-443923,EBI-443923
    Dab2P980782EBI-443923,EBI-1391846
    Eps15l1Q609022EBI-443923,EBI-443931
    REPS2Q8NFH810EBI-443923,EBI-7067016From a different organism.

    Protein-protein interaction databases

    BioGridi199489. 16 interactions.
    DIPiDIP-29052N.
    IntActiP42567. 7 interactions.
    MINTiMINT-86610.

    Structurei

    Secondary structure

    1
    897
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 124
    Turni13 – 153
    Helixi18 – 269
    Helixi37 – 448
    Beta strandi46 – 483
    Helixi50 – 6011
    Beta strandi63 – 675
    Helixi71 – 8313
    Turni84 – 863
    Helixi91 – 933

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KYFX-ray1.22P627-632[»]
    1KYUX-ray1.80P627-632[»]
    1QJTNMR-A7-105[»]
    ProteinModelPortaliP42567.
    SMRiP42567. Positions 7-105, 121-215, 217-311, 336-391, 440-478.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP42567.

    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
    Repeati665 – 66738
    Repeati673 – 67539
    Repeati693 – 695310
    Repeati711 – 713311
    Repeati806 – 808312
    Repeati827 – 829313
    Repeati852 – 87120UIM 1Add
    BLAST
    Repeati878 – 89720UIM 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 330329Interaction with DAB2Add
    BLAST
    Regioni599 – 82923113 X 3 AA repeats of D-P-FAdd
    BLAST

    Domaini

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

    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.
    GeneTreeiENSGT00750000117388.
    HOGENOMiHOG000004804.
    HOVERGENiHBG005591.
    InParanoidiP42567.
    KOiK12472.
    OrthoDBiEOG7JHM68.
    PhylomeDBiP42567.
    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. 4 hits.
    SM00027. EH. 3 hits.
    SM00726. UIM. 2 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: P42567-1) [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 KYYRQVEAGN TGRVLALDAA AFLKKSGLPD    50
    LILGKIWDLA DTDGKGVLSK QEFFVALRLV ACAQNGLEVS LSSLSLAVPP 100
    PRFHDSSSPL LTSGPSVAEL PWAVKSEDKA KYDAIFDSLS PVDGFLSGDK 150
    VKPVLLNSKL PVEILGRVWE LSDIDHDGKL DRDEFAVAMF LVYCALEKEP 200
    VPMSLPPALV PPSKRKTWVV SPAEKAKYDE IFLKTDKDMD GYVSGLEVRE 250
    TFLKTGLPSA LLAHIWSLCD TKGCGKLSKD QFALAFHLIN QKLIKGIDPP 300
    HSLTPEMIPP SDRSSLQKNI TGSSPVADFS AIKELDTLNN EIVDLQREKN 350
    NVEQDLKEKE DTVKQRTSEV QDLQDEVQRE SINLQKLQAQ KQQVQELLGE 400
    LDEQKAQLEE QLQEVRKKCA EEAQLISSLK AEITSQESQI SSYEEELLKA 450
    REELSRLQQE TAQLEESVES GKAQLEPLQQ HLQESQQEIS SMQMRLEMKD 500
    LETDNNQSNW SSSPQSVLVN GATDYCSLST SSSETANFNE HAEGQNNLES 550
    EPTHQESSVR SSPEIAPSDV TDESEAVTVA GNEKVTPRFD DDKHSKEEDP 600
    FNVESSSLTD AVADTNLDFF QSDPFVGSDP FKDDPFGKID PFGGDPFKGS 650
    DPFASDCFFK QTSTDPFTTS STDPFSASSN SSNTSVETWK HNDPFAPGGT 700
    VVAAASDSAT DPFASVFGNE SFGDGFADFS TLSKVNNEDA FNPTISSSTS 750
    SVTIAKPMLE ETASKSEDVP PALPPKVGTP TRPCPPPPGK RPINKLDSSD 800
    PLKLNDPFQP FPGNDSPKEK DPDMFCDPFT SSTTTNKEAD PSNFANFSAY 850
    PSEEDMIEWA KRESEREEEQ RLARLNQQEQ EDLELAIALS KSEISEA 897
    Length:897
    Mass (Da):98,471
    Last modified:November 1, 1995 - v1
    Checksum:i08A0C0D423F873C2
    GO
    Isoform 2 (identifier: P42567-2) [UniParc]FASTAAdd to Basket

    Also known as: Eps15b

    The sequence of this isoform differs from the canonical sequence as follows:
         2-314: Missing.
         315-346: SLQKNITGSSPVADFSAIKELDTLNNEIVDLQ → MYSDSGLGGWIAIPAVADVLRYSCIVCWSS

    Show »
    Length:582
    Mass (Da):64,203
    Checksum:iD5951681ED54F90C
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 314313Missing in isoform 2. 1 PublicationVSP_036170Add
    BLAST
    Alternative sequencei315 – 34632SLQKN…IVDLQ → MYSDSGLGGWIAIPAVADVL RYSCIVCWSS in isoform 2. 1 PublicationVSP_036171Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L21768 mRNA. Translation: AAA02912.1.
    AK083176 mRNA. Translation: BAC38796.1.
    AL669905 Genomic DNA. Translation: CAM13653.1.
    CCDSiCCDS18462.1. [P42567-1]
    PIRiA54696.
    RefSeqiNP_001153436.1. NM_001159964.1.
    NP_031969.1. NM_007943.3. [P42567-1]
    UniGeneiMm.318250.

    Genome annotation databases

    EnsembliENSMUST00000030281; ENSMUSP00000030281; ENSMUSG00000028552.
    ENSMUST00000102729; ENSMUSP00000099790; ENSMUSG00000028552. [P42567-1]
    GeneIDi13858.
    KEGGimmu:13858.
    UCSCiuc008ucf.2. mouse. [P42567-1]
    uc008ucg.2. mouse. [P42567-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L21768 mRNA. Translation: AAA02912.1 .
    AK083176 mRNA. Translation: BAC38796.1 .
    AL669905 Genomic DNA. Translation: CAM13653.1 .
    CCDSi CCDS18462.1. [P42567-1 ]
    PIRi A54696.
    RefSeqi NP_001153436.1. NM_001159964.1.
    NP_031969.1. NM_007943.3. [P42567-1 ]
    UniGenei Mm.318250.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KYF X-ray 1.22 P 627-632 [» ]
    1KYU X-ray 1.80 P 627-632 [» ]
    1QJT NMR - A 7-105 [» ]
    ProteinModelPortali P42567.
    SMRi P42567. Positions 7-105, 121-215, 217-311, 336-391, 440-478.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199489. 16 interactions.
    DIPi DIP-29052N.
    IntActi P42567. 7 interactions.
    MINTi MINT-86610.

    PTM databases

    PhosphoSitei P42567.

    Proteomic databases

    MaxQBi P42567.
    PaxDbi P42567.
    PRIDEi P42567.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000030281 ; ENSMUSP00000030281 ; ENSMUSG00000028552 .
    ENSMUST00000102729 ; ENSMUSP00000099790 ; ENSMUSG00000028552 . [P42567-1 ]
    GeneIDi 13858.
    KEGGi mmu:13858.
    UCSCi uc008ucf.2. mouse. [P42567-1 ]
    uc008ucg.2. mouse. [P42567-2 ]

    Organism-specific databases

    CTDi 2060.
    MGIi MGI:104583. Eps15.

    Phylogenomic databases

    eggNOGi NOG301764.
    GeneTreei ENSGT00750000117388.
    HOGENOMi HOG000004804.
    HOVERGENi HBG005591.
    InParanoidi P42567.
    KOi K12472.
    OrthoDBi EOG7JHM68.
    PhylomeDBi P42567.
    TreeFami TF324293.

    Enzyme and pathway databases

    Reactomei REACT_203917. EGFR downregulation.

    Miscellaneous databases

    EvolutionaryTracei P42567.
    NextBioi 284734.
    PROi P42567.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P42567.
    Bgeei P42567.
    Genevestigatori P42567.

    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. 4 hits.
    SM00027. EH. 3 hits.
    SM00726. UIM. 2 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. "eps15, a novel tyrosine kinase substrate, exhibits transforming activity."
      Fazioli F., Minichiello L., Matoskova B., Wong W.T., di Fiore P.P.
      Mol. Cell. Biol. 13:5814-5828(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fibroblast.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Strain: C57BL/6J.
      Tissue: Hippocampus.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. Lubec G., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 838-862, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: OF1.
      Tissue: Hippocampus.
    5. "Tyrosine phosphorylation of Eps15 is required for ligand-regulated, but not constitutive, endocytosis."
      Confalonieri S., Salcini A.E., Puri C., Tacchetti C., Di Fiore P.P.
      J. Cell Biol. 150:905-912(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-850 BY EGFR, MUTAGENESIS OF TYR-850.
    6. "SGIP1alpha is an endocytic protein that directly interacts with phospholipids and Eps15."
      Uezu A., Horiuchi A., Kanda K., Kikuchi N., Umeda K., Tsujita K., Suetsugu S., Araki N., Yamamoto H., Takenawa T., Nakanishi H.
      J. Biol. Chem. 282:26481-26489(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SGIP1.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-779, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    8. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    10. "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.
    11. "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.
    12. "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: INTERACTION WITH DAB2.
    13. "The EH1 domain of Eps15 is structurally classified as a member of the S100 subclass of EF-hand-containing proteins."
      Whitehead B., Tessari M., Carotenuto A., van Bergen en Henegouwen P.M., Vuister G.W.
      Biochemistry 38:11271-11277(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 7-105.
    14. "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 (1.22 ANGSTROMS) OF 628-632 IN COMPLEX WITH AP2A2.

    Entry informationi

    Entry nameiEPS15_MOUSE
    AccessioniPrimary (citable) accession number: P42567
    Secondary accession number(s): Q8C431
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 145 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, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3