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P53621

- COPA_HUMAN

UniProt

P53621 - COPA_HUMAN

Protein

Coatomer subunit alpha

Gene

COPA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 2 (02 Sep 2008)
      Previous versions | rss
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    Functioni

    The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors By similarity.By similarity
    Xenin stimulates exocrine pancreatic secretion. It inhibits pentagastrin-stimulated secretion of acid, to induce exocrine pancreatic secretion and to affect small and large intestinal motility. In the gut, xenin interacts with the neurotensin receptor.

    GO - Molecular functioni

    1. structural molecule activity Source: InterPro

    GO - Biological processi

    1. COPI coating of Golgi vesicle Source: Reactome
    2. intracellular protein transport Source: InterPro
    3. membrane organization Source: Reactome
    4. pancreatic juice secretion Source: MGI
    5. retrograde vesicle-mediated transport, Golgi to ER Source: Reactome

    Keywords - Molecular functioni

    Hormone

    Keywords - Biological processi

    ER-Golgi transport, Protein transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_11096. COPI Mediated Transport.
    SignaLinkiP53621.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Coatomer subunit alpha
    Alternative name(s):
    Alpha-coat protein
    Short name:
    Alpha-COP
    HEP-COP
    Short name:
    HEPCOP
    Cleaved into the following 2 chains:
    Alternative name(s):
    Xenopsin-related peptide
    Gene namesi
    Name:COPA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:2230. COPA.

    Subcellular locationi

    Cytoplasm By similarity. Golgi apparatus membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cytoplasmic vesicleCOPI-coated vesicle membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
    Note: The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it.By similarity
    Peptide Xenin : Secreted By similarity

    GO - Cellular componenti

    1. COPI vesicle coat Source: UniProtKB
    2. cytoplasm Source: MGI
    3. cytosol Source: Reactome
    4. extracellular space Source: MGI
    5. extracellular vesicular exosome Source: UniProt
    6. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26746.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12241224Coatomer subunit alphaPRO_0000223307Add
    BLAST
    Peptidei1 – 3535ProxeninPRO_0000041400Add
    BLAST
    Peptidei1 – 2525XeninPRO_0000041401Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei173 – 1731Phosphoserine7 Publications
    Modified residuei185 – 1851Phosphothreonine1 Publication
    Modified residuei402 – 4021Phosphoserine2 Publications
    Modified residuei895 – 8951Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP53621.
    PaxDbiP53621.
    PRIDEiP53621.

    PTM databases

    PhosphoSiteiP53621.

    Expressioni

    Tissue specificityi

    Uniformly expressed in a wide range of adult and fetal tissues. Xenin is found in gastric, duodenal and jejunal mucosa. Circulates in the blood. Seems to be confined to specific endocrine cells.

    Developmental stagei

    Xenin is released into the circulation after a meal.

    Gene expression databases

    BgeeiP53621.
    CleanExiHS_COPA.
    GenevestigatoriP53621.

    Organism-specific databases

    HPAiHPA028024.

    Interactioni

    Subunit structurei

    Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. Probably interacts with PEX11A. Interacts with SCYL1 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi107709. 47 interactions.
    IntActiP53621. 23 interactions.
    MINTiMINT-1144184.
    STRINGi9606.ENSP00000357048.

    Structurei

    3D structure databases

    ProteinModelPortaliP53621.
    SMRiP53621. Positions 1-320, 905-1224.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati7 – 3731WD 1Add
    BLAST
    Repeati49 – 7931WD 2Add
    BLAST
    Repeati91 – 12131WD 3Add
    BLAST
    Repeati133 – 16331WD 4Add
    BLAST
    Repeati203 – 23331WD 5Add
    BLAST
    Repeati247 – 27731WD 6Add
    BLAST

    Sequence similaritiesi

    Contains 6 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG2319.
    HOGENOMiHOG000195913.
    HOVERGENiHBG005379.
    KOiK05236.
    OMAiFWVLGAH.
    OrthoDBiEOG78WKQX.
    PhylomeDBiP53621.
    TreeFamiTF105693.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    InterProiIPR016391. Coatomer_asu.
    IPR010714. Coatomer_asu_C.
    IPR006692. Coatomer_WD-assoc_reg.
    IPR020472. G-protein_beta_WD-40_rep.
    IPR011048. Haem_d1.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    PfamiPF04053. Coatomer_WDAD. 1 hit.
    PF06957. COPI_C. 1 hit.
    PF00400. WD40. 6 hits.
    [Graphical view]
    PIRSFiPIRSF003354. Coatomer_alpha_subunit. 1 hit.
    PRINTSiPR00320. GPROTEINBRPT.
    SMARTiSM00320. WD40. 7 hits.
    [Graphical view]
    SUPFAMiSSF50978. SSF50978. 2 hits.
    SSF51004. SSF51004. 3 hits.
    PROSITEiPS00678. WD_REPEATS_1. 1 hit.
    PS50082. WD_REPEATS_2. 6 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [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: P53621-1) [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

    MLTKFETKSA RVKGLSFHPK RPWILTSLHN GVIQLWDYRM CTLIDKFDEH     50
    DGPVRGIDFH KQQPLFVSGG DDYKIKVWNY KLRRCLFTLL GHLDYIRTTF 100
    FHHEYPWILS ASDDQTIRVW NWQSRTCVCV LTGHNHYVMC AQFHPTEDLV 150
    VSASLDQTVR VWDISGLRKK NLSPGAVESD VRGITGVDLF GTTDAVVKHV 200
    LEGHDRGVNW AAFHPTMPLI VSGADDRQVK IWRMNESKAW EVDTCRGHYN 250
    NVSCAVFHPR QELILSNSED KSIRVWDMSK RTGVQTFRRD HDRFWVLAAH 300
    PNLNLFAAGH DGGMIVFKLE RERPAYAVHG NMLHYVKDRF LRQLDFNSSK 350
    DVAVMQLRSG SKFPVFNMSY NPAENAVLLC TRASNLENST YDLYTIPKDA 400
    DSQNPDAPEG KRSSGLTAVW VARNRFAVLD RMHSLLIKNL KNEITKKVQV 450
    PNCDEIFYAG TGNLLLRDAD SITLFDVQQK RTLASVKISK VKYVIWSADM 500
    SHVALLAKHA IVICNRKLDA LCNIHENIRV KSGAWDESGV FIYTTSNHIK 550
    YAVTTGDHGI IRTLDLPIYV TRVKGNNVYC LDRECRPRVL TIDPTEFKFK 600
    LALINRKYDE VLHMVRNAKL VGQSIIAYLQ KKGYPEVALH FVKDEKTRFS 650
    LALECGNIEI ALEAAKALDD KNCWEKLGEV ALLQGNHQIV EMCYQRTKNF 700
    DKLSFLYLIT GNLEKLRKMM KIAEIRKDMS GHYQNALYLG DVSERVRILK 750
    NCGQKSLAYL TAATHGLDEE AESLKETFDP EKETIPDIDP NAKLLQPPAP 800
    IMPLDTNWPL LTVSKGFFEG TIASKGKGGA LAADIDIDTV GTEGWGEDAE 850
    LQLDEDGFVE ATEGLGDDAL GKGQEEGGGW DVEEDLELPP ELDISPGAAG 900
    GAEDGFFVPP TKGTSPTQIW CNNSQLPVDH ILAGSFETAM RLLHDQVGVI 950
    QFGPYKQLFL QTYARGRTTY QALPCLPSMY GYPNRNWKDA GLKNGVPAVG 1000
    LKLNDLIQRL QLCYQLTTVG KFEEAVEKFR SILLSVPLLV VDNKQEIAEA 1050
    QQLITICREY IVGLSVETER KKLPKETLEQ QKRICEMAAY FTHSNLQPVH 1100
    MILVLRTALN LFFKLKNFKT AATFARRLLE LGPKPEVAQQ TRKILSACEK 1150
    NPTDAYQLNY DMHNPFDICA ASYRPIYRGK PVEKCPLSGA CYSPEFKGQI 1200
    CRVTTVTEIG KDVIGLRISP LQFR 1224
    Length:1,224
    Mass (Da):138,346
    Last modified:September 2, 2008 - v2
    Checksum:i5A8BC35CE78F155D
    GO
    Isoform 2 (identifier: P53621-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         509-509: H → HEHSCPLPLT

    Show »
    Length:1,233
    Mass (Da):139,324
    Checksum:iF43D084894C9AD98
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti703 – 7031L → V in AAB70879. (PubMed:8647451)Curated

    RNA editingi

    Edited at about 31%.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti164 – 1641I → V in RNA edited version.
    VAR_066525
    Natural varianti1040 – 10401V → G.
    Corresponds to variant rs34997807 [ dbSNP | Ensembl ].
    VAR_033803

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei509 – 5091H → HEHSCPLPLT in isoform 2. 1 PublicationVSP_035043

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U24105 mRNA. Translation: AAB70879.1.
    AL513282, AL445230 Genomic DNA. Translation: CAI12454.1.
    AL513282, AL445230 Genomic DNA. Translation: CAI12455.1.
    AL445230, AL513282 Genomic DNA. Translation: CAI15004.1.
    AL445230, AL513282 Genomic DNA. Translation: CAI15005.1.
    CH471121 Genomic DNA. Translation: EAW52723.1.
    CH471121 Genomic DNA. Translation: EAW52725.1.
    BC038447 mRNA. Translation: AAH38447.1.
    CCDSiCCDS1202.1. [P53621-1]
    CCDS41424.1. [P53621-2]
    PIRiJC4668. ERHUAH.
    RefSeqiNP_001091868.1. NM_001098398.1. [P53621-2]
    NP_004362.2. NM_004371.3. [P53621-1]
    UniGeneiHs.162121.
    Hs.685025.

    Genome annotation databases

    EnsembliENST00000241704; ENSP00000241704; ENSG00000122218. [P53621-1]
    ENST00000368069; ENSP00000357048; ENSG00000122218. [P53621-2]
    GeneIDi1314.
    KEGGihsa:1314.
    UCSCiuc001fvv.4. human. [P53621-2]
    uc009wti.3. human. [P53621-1]

    Polymorphism databases

    DMDMi205371746.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism, RNA editing

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Xenin entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U24105 mRNA. Translation: AAB70879.1 .
    AL513282 , AL445230 Genomic DNA. Translation: CAI12454.1 .
    AL513282 , AL445230 Genomic DNA. Translation: CAI12455.1 .
    AL445230 , AL513282 Genomic DNA. Translation: CAI15004.1 .
    AL445230 , AL513282 Genomic DNA. Translation: CAI15005.1 .
    CH471121 Genomic DNA. Translation: EAW52723.1 .
    CH471121 Genomic DNA. Translation: EAW52725.1 .
    BC038447 mRNA. Translation: AAH38447.1 .
    CCDSi CCDS1202.1. [P53621-1 ]
    CCDS41424.1. [P53621-2 ]
    PIRi JC4668. ERHUAH.
    RefSeqi NP_001091868.1. NM_001098398.1. [P53621-2 ]
    NP_004362.2. NM_004371.3. [P53621-1 ]
    UniGenei Hs.162121.
    Hs.685025.

    3D structure databases

    ProteinModelPortali P53621.
    SMRi P53621. Positions 1-320, 905-1224.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107709. 47 interactions.
    IntActi P53621. 23 interactions.
    MINTi MINT-1144184.
    STRINGi 9606.ENSP00000357048.

    PTM databases

    PhosphoSitei P53621.

    Polymorphism databases

    DMDMi 205371746.

    Proteomic databases

    MaxQBi P53621.
    PaxDbi P53621.
    PRIDEi P53621.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000241704 ; ENSP00000241704 ; ENSG00000122218 . [P53621-1 ]
    ENST00000368069 ; ENSP00000357048 ; ENSG00000122218 . [P53621-2 ]
    GeneIDi 1314.
    KEGGi hsa:1314.
    UCSCi uc001fvv.4. human. [P53621-2 ]
    uc009wti.3. human. [P53621-1 ]

    Organism-specific databases

    CTDi 1314.
    GeneCardsi GC01M160258.
    HGNCi HGNC:2230. COPA.
    HPAi HPA028024.
    MIMi 601924. gene.
    neXtProti NX_P53621.
    PharmGKBi PA26746.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2319.
    HOGENOMi HOG000195913.
    HOVERGENi HBG005379.
    KOi K05236.
    OMAi FWVLGAH.
    OrthoDBi EOG78WKQX.
    PhylomeDBi P53621.
    TreeFami TF105693.

    Enzyme and pathway databases

    Reactomei REACT_11096. COPI Mediated Transport.
    SignaLinki P53621.

    Miscellaneous databases

    ChiTaRSi COPA. human.
    GeneWikii COPA_(gene).
    GenomeRNAii 1314.
    NextBioi 5373.
    PROi P53621.
    SOURCEi Search...

    Gene expression databases

    Bgeei P53621.
    CleanExi HS_COPA.
    Genevestigatori P53621.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    InterProi IPR016391. Coatomer_asu.
    IPR010714. Coatomer_asu_C.
    IPR006692. Coatomer_WD-assoc_reg.
    IPR020472. G-protein_beta_WD-40_rep.
    IPR011048. Haem_d1.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    Pfami PF04053. Coatomer_WDAD. 1 hit.
    PF06957. COPI_C. 1 hit.
    PF00400. WD40. 6 hits.
    [Graphical view ]
    PIRSFi PIRSF003354. Coatomer_alpha_subunit. 1 hit.
    PRINTSi PR00320. GPROTEINBRPT.
    SMARTi SM00320. WD40. 7 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 2 hits.
    SSF51004. SSF51004. 3 hits.
    PROSITEi PS00678. WD_REPEATS_1. 1 hit.
    PS50082. WD_REPEATS_2. 6 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "HEP-COP, a novel human gene whose product is highly homologous to the alpha-subunit of the yeast coatomer protein complex."
      Chow V.T.K., Quek H.H.
      Gene 169:223-227(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "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].
    3. 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 2).
      Tissue: Uterus.
    5. "Identification of xenin, a xenopsin-related peptide, in the human gastric mucosa and its effect on exocrine pancreatic secretion."
      Feurle G.E., Hamscher G., Kusiek R., Meyer H.E., Metzger J.W.
      J. Biol. Chem. 267:22305-22309(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-25 (XENIN).
      Tissue: Gastric mucosa.
    6. "Alpha coat protein COPA (HEP-COP): presence of an Alu repeat in cDNA and identity of the amino terminus to xenin."
      Chow V.T.K., Quek H.H.
      Ann. Hum. Genet. 61:369-373(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING OF COPA TO PRODUCE XENIN.
    7. Cited for: REVIEW ON XENIN.
    8. "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 SER-173, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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-173, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-895, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-402, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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-173, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "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-173 AND THR-185, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: RNA EDITING OF POSITION 164.
    17. "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-173 AND SER-402, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCOPA_HUMAN
    AccessioniPrimary (citable) accession number: P53621
    Secondary accession number(s): Q5T201, Q8IXZ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: September 2, 2008
    Last modified: October 1, 2014
    This is version 152 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

    Complete proteome, Direct protein sequencing, 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3