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Q9Y6I3

- EPN1_HUMAN

UniProt

Q9Y6I3 - EPN1_HUMAN

Protein

Epsin-1

Gene

EPN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (03 May 2011)
      Previous versions | rss
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    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 By similarity. Regulates receptor-mediated endocytosis.By similarity1 Publication

    Sites

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

    GO - Molecular functioni

    1. lipid binding Source: UniProtKB-KW

    GO - Biological processi

    1. embryonic organ development Source: Ensembl
    2. endocytosis Source: ProtInc
    3. epidermal growth factor receptor signaling pathway Source: Reactome
    4. female pregnancy Source: Ensembl
    5. in utero embryonic development Source: Ensembl
    6. negative regulation of epidermal growth factor receptor signaling pathway Source: Reactome
    7. Notch signaling pathway Source: Ensembl

    Keywords - Biological processi

    Endocytosis

    Keywords - Ligandi

    Lipid-binding

    Enzyme and pathway databases

    ReactomeiREACT_12484. EGFR downregulation.
    SignaLinkiQ9Y6I3.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Epsin-1
    Alternative name(s):
    EH domain-binding mitotic phosphoprotein
    EPS-15-interacting protein 1
    Gene namesi
    Name:EPN1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:21604. EPN1.

    Subcellular locationi

    Cytoplasm By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity. Nucleus By similarity. Membraneclathrin-coated pit By similarity
    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. Detected in presynaptic nerve terminals and in Golgi stacks. May shuttle to the nucleus when associated with ZBTB16/ZNF145 By similarity.By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell membrane, Coated pit, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi382 – 3821S → A: Abolishes phosphorylation by CDK1. 1 Publication
    Mutagenesisi382 – 3821S → D: Abolishes phosphorylation by CDK1 and reduces REPS2 binding. 1 Publication
    Mutagenesisi404 – 4041F → A: Reduces interaction with AP2B1. 1 Publication

    Organism-specific databases

    PharmGKBiPA134860916.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 576576Epsin-1PRO_0000074513Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei382 – 3821Phosphoserine; by CDK11 Publication
    Modified residuei419 – 4191Phosphoserine1 Publication
    Modified residuei420 – 4201Phosphoserine1 Publication
    Modified residuei435 – 4351Phosphoserine3 Publications
    Modified residuei454 – 4541Phosphoserine4 Publications
    Modified residuei460 – 4601Phosphothreonine4 Publications
    Modified residuei470 – 4701Phosphothreonine1 Publication
    Modified residuei494 – 4941Phosphothreonine3 Publications

    Post-translational modificationi

    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.6 Publications
    Ubiquitinated.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9Y6I3.
    PaxDbiQ9Y6I3.
    PRIDEiQ9Y6I3.

    PTM databases

    PhosphoSiteiQ9Y6I3.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Y6I3.
    BgeeiQ9Y6I3.
    CleanExiHS_EPN1.
    GenevestigatoriQ9Y6I3.

    Organism-specific databases

    HPAiCAB009729.

    Interactioni

    Subunit structurei

    Monomer. Binds clathrin, ZBTB16/ZNF145 and ITSN1. Binds ubiquitinated proteins By similarity. Binds REPS2, EPS15, AP2A1 and AP2A2. Interacts with RALBP1 in a complex also containing NUMB and TFAP2A during interphase and mitosis. Interacts with AP2B1.By similarity4 Publications

    Protein-protein interaction databases

    BioGridi118965. 41 interactions.
    IntActiQ9Y6I3. 10 interactions.
    MINTiMINT-110599.
    STRINGi9606.ENSP00000406209.

    Structurei

    Secondary structure

    1
    576
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi20 – 278
    Helixi39 – 479
    Helixi51 – 6212
    Helixi63 – 653
    Helixi72 – 8615
    Helixi90 – 989
    Helixi100 – 1089
    Helixi121 – 13414

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1INZNMR-A1-144[»]
    ProteinModelPortaliQ9Y6I3.
    SMRiQ9Y6I3. Positions 1-158.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y6I3.

    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
    Repeati502 – 50431
    Repeati518 – 52032
    Repeati572 – 57433

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni274 – 3791068 X 3 AA repeats of [ED]-P-WAdd
    BLAST
    Regioni502 – 574733 X 3 AA repeats of N-P-FAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi402 – 41110[DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi267 – 573307Ala/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 with 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.
    HOGENOMiHOG000008298.
    HOVERGENiHBG006690.
    KOiK12471.
    OMAiDPWGGTQ.
    OrthoDBiEOG7F511Z.
    TreeFamiTF313361.

    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]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y6I3-2) [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

    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 AQLQLALSLS REEHDKEERI RRGDDLRLQM AIEESKRETG 250
    GKEESSLMDL ADVFTAPAPA PTTDPWGGPA PMAAAVPTAA PTSDPWGGPP 300
    VPPAADPWGG PAPTPASGDP WRPAAPAGPS VDPWGGTPAP AAGEGPTPDP 350
    WGSSDGGVPV SGPSASDPWT PAPAFSDPWG GSPAKPSTNG TTAAGGFDTE 400
    PDEFSDFDRL RTALPTSGSS AGELELLAGE VPARSPGAFD MSGVRGSLAE 450
    AVGSPPPAAT PTPTPPTRKT PESFLGPNAA LVDLDSLVSR PGPTPPGAKA 500
    SNPFLPGGGP ATGPSVTNPF QPAPPATLTL NQLRLSPVPP VPGAPPTYIS 550
    PLGGGPGLPP MMPPGPPAPN TNPFLL 576
    Length:576
    Mass (Da):60,293
    Last modified:May 3, 2011 - v2
    Checksum:i68DD433F3168E975
    GO
    Isoform 2 (identifier: Q9Y6I3-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MGDQSWLWNQ...CPLLLQPGTM
         202-226: Missing.

    Show »
    Length:662
    Mass (Da):69,040
    Checksum:iBE8DD37499E2DB6A
    GO
    Isoform 3 (identifier: Q9Y6I3-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         202-226: Missing.
         393-393: Missing.

    Note: May be due to a competing donor splice site. No experimental confirmation available.

    Show »
    Length:550
    Mass (Da):57,504
    Checksum:iDC8BA5EBEB1D5111
    GO

    Sequence cautioni

    Isoform 2 : The sequence AAD38326.1 differs from that shown. Reason: Frameshift at position 98.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MGDQSWLWNQAAPGVRSPVF ACSVEKGNVPLVLSEHLAHS RDPGSGAVRFLISPEPWASA ILGTSGLLASPVLPAALDAV TCQHLPQPSSGSRPISPRIG ALCPLLLQPGTM in isoform 2. 1 PublicationVSP_041010
    Alternative sequencei202 – 22625Missing in isoform 2 and isoform 3. 2 PublicationsVSP_041011Add
    BLAST
    Alternative sequencei393 – 3931Missing in isoform 3. 1 PublicationVSP_041012

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF073727 mRNA. Translation: AAD38326.1. Frameshift.
    AK022454 mRNA. Translation: BAB14041.1.
    AC008735 Genomic DNA. No translation available.
    AC010525 Genomic DNA. No translation available.
    BC044651 mRNA. Translation: AAH44651.1.
    CCDSiCCDS46198.1. [Q9Y6I3-1]
    CCDS46199.1. [Q9Y6I3-2]
    CCDS46200.1. [Q9Y6I3-3]
    RefSeqiNP_001123543.1. NM_001130071.1. [Q9Y6I3-1]
    NP_001123544.1. NM_001130072.1. [Q9Y6I3-2]
    NP_037465.2. NM_013333.3. [Q9Y6I3-3]
    XP_005258886.1. XM_005258829.1. [Q9Y6I3-2]
    UniGeneiHs.279953.

    Genome annotation databases

    EnsembliENST00000085079; ENSP00000085079; ENSG00000063245. [Q9Y6I3-3]
    ENST00000270460; ENSP00000270460; ENSG00000063245. [Q9Y6I3-2]
    ENST00000411543; ENSP00000406209; ENSG00000063245. [Q9Y6I3-1]
    GeneIDi29924.
    KEGGihsa:29924.
    UCSCiuc002qlv.3. human. [Q9Y6I3-3]
    uc002qlw.3. human. [Q9Y6I3-2]
    uc002qlx.3. human. [Q9Y6I3-1]

    Polymorphism databases

    DMDMi332278179.

    Keywords - Coding sequence diversityi

    Alternative splicing

    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
    AF073727 mRNA. Translation: AAD38326.1 . Frameshift.
    AK022454 mRNA. Translation: BAB14041.1 .
    AC008735 Genomic DNA. No translation available.
    AC010525 Genomic DNA. No translation available.
    BC044651 mRNA. Translation: AAH44651.1 .
    CCDSi CCDS46198.1. [Q9Y6I3-1 ]
    CCDS46199.1. [Q9Y6I3-2 ]
    CCDS46200.1. [Q9Y6I3-3 ]
    RefSeqi NP_001123543.1. NM_001130071.1. [Q9Y6I3-1 ]
    NP_001123544.1. NM_001130072.1. [Q9Y6I3-2 ]
    NP_037465.2. NM_013333.3. [Q9Y6I3-3 ]
    XP_005258886.1. XM_005258829.1. [Q9Y6I3-2 ]
    UniGenei Hs.279953.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1INZ NMR - A 1-144 [» ]
    ProteinModelPortali Q9Y6I3.
    SMRi Q9Y6I3. Positions 1-158.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118965. 41 interactions.
    IntActi Q9Y6I3. 10 interactions.
    MINTi MINT-110599.
    STRINGi 9606.ENSP00000406209.

    PTM databases

    PhosphoSitei Q9Y6I3.

    Polymorphism databases

    DMDMi 332278179.

    Proteomic databases

    MaxQBi Q9Y6I3.
    PaxDbi Q9Y6I3.
    PRIDEi Q9Y6I3.

    Protocols and materials databases

    DNASUi 29924.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000085079 ; ENSP00000085079 ; ENSG00000063245 . [Q9Y6I3-3 ]
    ENST00000270460 ; ENSP00000270460 ; ENSG00000063245 . [Q9Y6I3-2 ]
    ENST00000411543 ; ENSP00000406209 ; ENSG00000063245 . [Q9Y6I3-1 ]
    GeneIDi 29924.
    KEGGi hsa:29924.
    UCSCi uc002qlv.3. human. [Q9Y6I3-3 ]
    uc002qlw.3. human. [Q9Y6I3-2 ]
    uc002qlx.3. human. [Q9Y6I3-1 ]

    Organism-specific databases

    CTDi 29924.
    GeneCardsi GC19P056186.
    H-InvDB HIX0202721.
    HGNCi HGNC:21604. EPN1.
    HPAi CAB009729.
    MIMi 607262. gene.
    neXtProti NX_Q9Y6I3.
    PharmGKBi PA134860916.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG263730.
    HOGENOMi HOG000008298.
    HOVERGENi HBG006690.
    KOi K12471.
    OMAi DPWGGTQ.
    OrthoDBi EOG7F511Z.
    TreeFami TF313361.

    Enzyme and pathway databases

    Reactomei REACT_12484. EGFR downregulation.
    SignaLinki Q9Y6I3.

    Miscellaneous databases

    EvolutionaryTracei Q9Y6I3.
    GeneWikii EPN1.
    GenomeRNAii 29924.
    NextBioi 52535.
    PROi Q9Y6I3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y6I3.
    Bgeei Q9Y6I3.
    CleanExi HS_EPN1.
    Genevestigatori Q9Y6I3.

    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 binds to the EH domain of POB1 and regulates receptor-mediated endocytosis."
      Morinaka K., Koyama S., Nakashima S., Hinoi T., Okawa K., Iwamatsu A., Kikuchi A.
      Oncogene 18:5915-5922(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH REPS2.
      Tissue: Brain.
    2. "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: Mammary gland.
    3. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Brain.
    5. "Regulation of complex formation of POB1/epsin/adaptor protein complex 2 by mitotic phosphorylation."
      Kariya K., Koyama S., Nakashima S., Oshiro T., Morinaka K., Kikuchi A.
      J. Biol. Chem. 275:18399-18406(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-382, MUTAGENESIS OF SER-382, INTERACTION WITH REPS2; EPS15 AND AP-2 ALPHA SUBUNIT.
    6. "RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to phosphorylate epsin during the switch off of endocytosis in mitosis."
      Rosse C., L'Hoste S., Offner N., Picard A., Camonis J.
      J. Biol. Chem. 278:30597-30604(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RALBP1.
    7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-494, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Molecular switches involving the AP-2 beta2 appendage regulate endocytic cargo selection and clathrin coat assembly."
      Edeling M.A., Mishra S.K., Keyel P.A., Steinhauser A.L., Collins B.M., Roth R., Heuser J.E., Owen D.J., Traub L.M.
      Dev. Cell 10:329-342(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AP2B1, MUTAGENESIS OF PHE-404.
    9. "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-454 AND THR-460, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435; SER-454; THR-460 AND THR-494, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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-419; SER-420; SER-435; SER-454; THR-460 AND THR-470, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "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-435; SER-454; THR-460 AND THR-494, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Solution structure of the epsin N-terminal homology (ENTH) domain of human epsin."
      Koshiba S., Kigawa T., Kikuchi A., Yokoyama S.
      J. Struct. Funct. Genomics 2:1-8(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-144.

    Entry informationi

    Entry nameiEPN1_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y6I3
    Secondary accession number(s): Q86ST3, Q9HA18
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 16, 2004
    Last sequence update: May 3, 2011
    Last modified: October 1, 2014
    This is version 136 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3