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Q9UBC2

- EP15R_HUMAN

UniProt

Q9UBC2 - EP15R_HUMAN

Protein

Epidermal growth factor receptor substrate 15-like 1

Gene

EPS15L1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Seems to be a constitutive component of clathrin-coated pits that is required for receptor-mediated endocytosis. 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 DAB2.2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi172 – 18413PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. protein binding Source: IntAct

    GO - Biological processi

    1. endocytosis Source: UniProtKB-KW
    2. epidermal growth factor receptor signaling pathway Source: Reactome
    3. negative regulation of epidermal growth factor receptor signaling pathway Source: Reactome

    Keywords - Biological processi

    Endocytosis

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_12484. EGFR downregulation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Epidermal growth factor receptor substrate 15-like 1
    Alternative name(s):
    Eps15-related protein
    Short name:
    Eps15R
    Gene namesi
    Name:EPS15L1
    Synonyms:EPS15R
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:24634. EPS15L1.

    Subcellular locationi

    Cell membrane By similarity; Peripheral membrane protein By similarity. Nucleus By similarity. Membranecoated pit By similarity
    Note: Localized to plasma membrane coated pits.By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell membrane, Coated pit, Membrane, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134906266.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 864863Epidermal growth factor receptor substrate 15-like 1PRO_0000146118Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei74 – 741PhosphotyrosineBy similarity
    Modified residuei108 – 1081PhosphoserineBy similarity
    Modified residuei229 – 2291Phosphoserine1 Publication
    Modified residuei244 – 2441Phosphoserine1 Publication
    Modified residuei255 – 2551Phosphoserine4 Publications
    Modified residuei560 – 5601Phosphoserine1 Publication
    Modified residuei564 – 5641PhosphotyrosineBy similarity
    Modified residuei577 – 5771Phosphothreonine1 Publication
    Modified residuei797 – 7971Phosphothreonine1 Publication

    Post-translational modificationi

    Phosphorylated on tyrosine residues by EGFR.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9UBC2.
    PaxDbiQ9UBC2.
    PRIDEiQ9UBC2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UBC2.
    BgeeiQ9UBC2.
    CleanExiHS_EPS15L1.
    GenevestigatoriQ9UBC2.

    Organism-specific databases

    HPAiHPA019237.

    Interactioni

    Subunit structurei

    Interacts with EPS15, AGFG1/HRB and AGFG2/HRBL. Associates with the clathrin-associated adapter protein complex 2 (AP-2) By similarity. Interacts with FCHO1. Interacts with FCHO2. Interacts (via EH domains) with DAB2.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PRKCDBPQ969G52EBI-2556746,EBI-3893101

    Protein-protein interaction databases

    BioGridi121840. 17 interactions.
    IntActiQ9UBC2. 10 interactions.
    MINTiMINT-1538779.
    STRINGi9606.ENSP00000248070.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UBC2.
    SMRiQ9UBC2. Positions 11-105, 121-214, 269-362, 435-463.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini15 – 10490EH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini127 – 21589EH 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini159 – 19436EF-handPROSITE-ProRule annotationAdd
    BLAST
    Domaini275 – 36591EH 3PROSITE-ProRule annotationAdd
    BLAST
    Repeati618 – 62031
    Repeati640 – 64232
    Repeati645 – 64733
    Repeati650 – 65234
    Repeati656 – 65835
    Repeati661 – 66336
    Repeati667 – 66937
    Repeati685 – 68738
    Repeati690 – 69239
    Repeati709 – 711310
    Repeati728 – 730311
    Repeati754 – 756312
    Repeati806 – 808313
    Repeati812 – 814314
    Repeati833 – 835315

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni15 – 368354Interaction with DAB2By similarityAdd
    BLAST
    Regioni618 – 83521815 X 3 AA repeats of D-P-FAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi750 – 81667Pro-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 EF-hand domain.PROSITE-ProRule annotation
    Contains 3 EH domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG301764.
    HOGENOMiHOG000004804.
    HOVERGENiHBG005591.
    InParanoidiQ9UBC2.
    OMAiMDDPFKN.
    OrthoDBiEOG7JHM68.
    PhylomeDBiQ9UBC2.
    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.
    [Graphical view]
    SMARTiSM00054. EFh. 3 hits.
    SM00027. EH. 3 hits.
    [Graphical view]
    PROSITEiPS00018. EF_HAND_1. 1 hit.
    PS50222. EF_HAND_2. 4 hits.
    PS50031. EH. 3 hits.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UBC2-1) [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

    MAAPLIPLSQ QIPTGNSLYE SYYKQVDPAY TGRVGASEAA LFLKKSGLSD    50
    IILGKIWDLA DPEGKGFLDK QGFYVALRLV ACAQSGHEVT LSNLNLSMPP 100
    PKFHDTSSPL MVTPPSAEAH WAVRVEEKAK FDGIFESLLP INGLLSGDKV 150
    KPVLMNSKLP LDVLGRVWDL SDIDKDGHLD RDEFAVAMHL VYRALEKEPV 200
    PSALPPSLIP PSKRKKTVFP GAVPVLPASP PPKDSLRSTP SHGSVSSLNS 250
    TGSLSPKHSL KQTQPTVNWV VPVADKMRFD EIFLKTDLDL DGYVSGQEVK 300
    EIFMHSGLTQ NLLAHIWALA DTRQTGKLSK DQFALAMYFI QQKVSKGIDP 350
    PQVLSPDMVP PSERGTPGPD SSGSLGSGEF TGVKELDDIS QEIAQLQREK 400
    YSLEQDIREK EEAIRQKTSE VQELQNDLDR ETSSLQELEA QKQDAQDRLD 450
    EMDQQKAKLR DMLSDVRQKC QDETQMISSL KTQIQSQESD LKSQEDDLNR 500
    AKSELNRLQQ EETQLEQSIQ AGRVQLETII KSLKSTQDEI NQARSKLSQL 550
    HESRQEAHRS LEQYDQVLDG AHGASLTDLA NLSEGVSLAE RGSFGAMDDP 600
    FKNKALLFSN NTQELHPDPF QTEDPFKSDP FKGADPFKGD PFQNDPFAEQ 650
    QTTSTDPFGG DPFKESDPFR GSATDDFFKK QTKNDPFTSD PFTKNPSLPS 700
    KLDPFESSDP FSSSSVSSKG SDPFGTLDPF GSGSFNSAEG FADFSQMSKP 750
    PPSGPFTSSL GGAGFSDDPF KSKQDTPALP PKKPAPPRPK PPSGKSTPVS 800
    QLGSADFPEA PDPFQPLGAD SGDPFQSKKG FGDPFSGKDP FVPSSAAKPS 850
    KASASGFADF TSVS 864
    Length:864
    Mass (Da):94,255
    Last modified:May 1, 2000 - v1
    Checksum:iF4126069F6E00387
    GO
    Isoform 2 (identifier: Q9UBC2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         863-864: VS → FGNEEQQLAWAKRESEKAEQERLARLRRQEQEDLELAIALSKADMPAA

    Show »
    Length:910
    Mass (Da):99,606
    Checksum:iF56CC554F539B5FE
    GO
    Isoform 3 (identifier: Q9UBC2-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         750-864: PPPSGPFTSS...SGFADFTSVS → VKVHL

    Show »
    Length:754
    Mass (Da):83,248
    Checksum:i5FFC0740FA78FC8B
    GO
    Isoform 4 (identifier: Q9UBC2-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         598-601: DDPF → VKVE
         602-864: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:601
    Mass (Da):66,479
    Checksum:i9709A5D16D1E126A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti680 – 6801K → E in BAG59115. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei598 – 6014DDPF → VKVE in isoform 4. 1 PublicationVSP_046904
    Alternative sequencei602 – 864263Missing in isoform 4. 1 PublicationVSP_046905Add
    BLAST
    Alternative sequencei750 – 864115PPPSG…FTSVS → VKVHL in isoform 3. 2 PublicationsVSP_045429Add
    BLAST
    Alternative sequencei863 – 8642VS → FGNEEQQLAWAKRESEKAEQ ERLARLRRQEQEDLELAIAL SKADMPAA in isoform 2. 1 PublicationVSP_042200

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF110265 mRNA. Translation: AAF21930.1.
    AB015346 mRNA. Translation: BAA88118.1.
    AK024166 mRNA. Translation: BAG51266.1.
    AK296473 mRNA. Translation: BAG59115.1.
    AC008764 Genomic DNA. No translation available.
    AC020917 Genomic DNA. No translation available.
    CH471106 Genomic DNA. Translation: EAW84542.1.
    BC131590 mRNA. Translation: AAI31591.1.
    BC142716 mRNA. Translation: AAI42717.1.
    CCDSiCCDS32944.1. [Q9UBC2-1]
    CCDS58653.1. [Q9UBC2-3]
    CCDS58654.1. [Q9UBC2-2]
    CCDS59363.1. [Q9UBC2-4]
    RefSeqiNP_001245303.1. NM_001258374.1. [Q9UBC2-2]
    NP_001245304.1. NM_001258375.1. [Q9UBC2-3]
    NP_001245305.1. NM_001258376.1. [Q9UBC2-4]
    NP_067058.1. NM_021235.2. [Q9UBC2-1]
    UniGeneiHs.654639.
    Hs.744842.

    Genome annotation databases

    GeneIDi58513.
    KEGGihsa:58513.
    UCSCiuc002ndx.4. human. [Q9UBC2-2]
    uc002ndz.2. human. [Q9UBC2-1]
    uc002nea.2. human.
    uc002nec.2. human.

    Polymorphism databases

    DMDMi61223942.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF110265 mRNA. Translation: AAF21930.1 .
    AB015346 mRNA. Translation: BAA88118.1 .
    AK024166 mRNA. Translation: BAG51266.1 .
    AK296473 mRNA. Translation: BAG59115.1 .
    AC008764 Genomic DNA. No translation available.
    AC020917 Genomic DNA. No translation available.
    CH471106 Genomic DNA. Translation: EAW84542.1 .
    BC131590 mRNA. Translation: AAI31591.1 .
    BC142716 mRNA. Translation: AAI42717.1 .
    CCDSi CCDS32944.1. [Q9UBC2-1 ]
    CCDS58653.1. [Q9UBC2-3 ]
    CCDS58654.1. [Q9UBC2-2 ]
    CCDS59363.1. [Q9UBC2-4 ]
    RefSeqi NP_001245303.1. NM_001258374.1. [Q9UBC2-2 ]
    NP_001245304.1. NM_001258375.1. [Q9UBC2-3 ]
    NP_001245305.1. NM_001258376.1. [Q9UBC2-4 ]
    NP_067058.1. NM_021235.2. [Q9UBC2-1 ]
    UniGenei Hs.654639.
    Hs.744842.

    3D structure databases

    ProteinModelPortali Q9UBC2.
    SMRi Q9UBC2. Positions 11-105, 121-214, 269-362, 435-463.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121840. 17 interactions.
    IntActi Q9UBC2. 10 interactions.
    MINTi MINT-1538779.
    STRINGi 9606.ENSP00000248070.

    Polymorphism databases

    DMDMi 61223942.

    Proteomic databases

    MaxQBi Q9UBC2.
    PaxDbi Q9UBC2.
    PRIDEi Q9UBC2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 58513.
    KEGGi hsa:58513.
    UCSCi uc002ndx.4. human. [Q9UBC2-2 ]
    uc002ndz.2. human. [Q9UBC2-1 ]
    uc002nea.2. human.
    uc002nec.2. human.

    Organism-specific databases

    CTDi 58513.
    GeneCardsi GC19M016466.
    HGNCi HGNC:24634. EPS15L1.
    HPAi HPA019237.
    neXtProti NX_Q9UBC2.
    PharmGKBi PA134906266.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG301764.
    HOGENOMi HOG000004804.
    HOVERGENi HBG005591.
    InParanoidi Q9UBC2.
    OMAi MDDPFKN.
    OrthoDBi EOG7JHM68.
    PhylomeDBi Q9UBC2.
    TreeFami TF324293.

    Enzyme and pathway databases

    Reactomei REACT_12484. EGFR downregulation.

    Miscellaneous databases

    ChiTaRSi EPS15L1. human.
    GeneWikii EPS15L1.
    GenomeRNAii 58513.
    NextBioi 65055.
    PROi Q9UBC2.

    Gene expression databases

    ArrayExpressi Q9UBC2.
    Bgeei Q9UBC2.
    CleanExi HS_EPS15L1.
    Genevestigatori Q9UBC2.

    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.
    [Graphical view ]
    SMARTi SM00054. EFh. 3 hits.
    SM00027. EH. 3 hits.
    [Graphical view ]
    PROSITEi PS00018. EF_HAND_1. 1 hit.
    PS50222. EF_HAND_2. 4 hits.
    PS50031. EH. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Nakashima S., Morinaka K., Ikeda M., Kishida S., Koyama S., Kikuchi A.
      Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "Selection system for genes encoding nuclear-targeted proteins."
      Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.
      Nat. Biotechnol. 16:1338-1342(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], SUBCELLULAR LOCATION.
      Tissue: Fetal brain.
    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] (ISOFORMS 2 AND 3).
      Tissue: Thalamus.
    4. "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].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORMS 3 AND 4).
    7. "eps15 and eps15R are essential components of the endocytic pathway."
      Carbone R., Fre S., Iannolo G., Belleudi F., Mancini P., Pelicci P.G., Torrisi M.R., Di Fiore P.P.
      Cancer Res. 57:5498-5504(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    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-229, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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].
    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-244; SER-255; SER-560; THR-577 AND THR-797, 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-255, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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-255, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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.
    18. "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.

    Entry informationi

    Entry nameiEP15R_HUMAN
    AccessioniPrimary (citable) accession number: Q9UBC2
    Secondary accession number(s): A2RRF3, A5PL29, B4DKA3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2004
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 128 of the entry and version 1 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3