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O14579

- COPE_HUMAN

UniProt

O14579 - COPE_HUMAN

Protein

Coatomer subunit epsilon

Gene

COPE

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      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. The 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 with 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

    GO - Molecular functioni

    1. structural molecule activity Source: InterPro

    GO - Biological processi

    1. COPI coating of Golgi vesicle Source: Reactome
    2. intra-Golgi vesicle-mediated transport Source: UniProtKB
    3. membrane organization Source: Reactome
    4. protein transport Source: UniProtKB-KW
    5. retrograde vesicle-mediated transport, Golgi to ER Source: Reactome

    Keywords - Biological processi

    ER-Golgi transport, Protein transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_11096. COPI Mediated Transport.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Coatomer subunit epsilon
    Alternative name(s):
    Epsilon-coat protein
    Short name:
    Epsilon-COP
    Gene namesi
    Name:COPE
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:2234. COPE.

    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

    GO - Cellular componenti

    1. COPI vesicle coat Source: UniProtKB
    2. cytosol Source: Reactome
    3. Golgi apparatus Source: LIFEdb
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26750.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 308307Coatomer subunit epsilonPRO_0000193851Add
    BLAST

    Post-translational modificationi

    Phosphorylated by PKA.
    Polyubiquitinated by RCHY1 in the presence of androgen, leading to proteasomal degradation.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO14579.
    PaxDbiO14579.
    PRIDEiO14579.

    2D gel databases

    OGPiO14579.

    PTM databases

    PhosphoSiteiO14579.

    Expressioni

    Gene expression databases

    ArrayExpressiO14579.
    BgeeiO14579.
    CleanExiHS_COPE.
    GenevestigatoriO14579.

    Organism-specific databases

    HPAiCAB034345.
    HPA041605.
    HPA043576.

    Interactioni

    Subunit structurei

    Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits.

    Protein-protein interaction databases

    BioGridi116447. 26 interactions.
    IntActiO14579. 8 interactions.
    MINTiMINT-5000768.
    STRINGi9606.ENSP00000262812.

    Structurei

    3D structure databases

    ProteinModelPortaliO14579.
    SMRiO14579. Positions 17-307.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the COPE family.Curated

    Phylogenomic databases

    eggNOGiNOG289253.
    HOGENOMiHOG000205825.
    HOVERGENiHBG002201.
    InParanoidiO14579.
    KOiK17268.
    OrthoDBiEOG7QK0CC.
    PhylomeDBiO14579.
    TreeFamiTF313390.

    Family and domain databases

    Gene3Di1.25.40.10. 1 hit.
    InterProiIPR006822. Coatomer_esu.
    IPR011990. TPR-like_helical.
    [Graphical view]
    PANTHERiPTHR10805. PTHR10805. 1 hit.
    PfamiPF04733. Coatomer_E. 1 hit.
    [Graphical view]
    PIRSFiPIRSF016478. Coatomer_esu. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O14579-1) [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

    MAPPAPGPAS GGSGEVDELF DVKNAFYIGS YQQCINEAQR VKLSSPERDV    50
    ERDVFLYRAY LAQRKFGVVL DEIKPSSAPE LQAVRMFADY LAHESRRDSI 100
    VAELDREMSR SVDVTNTTFL LMAASIYLHD QNPDAALRAL HQGDSLECTA 150
    MTVQILLKLD RLDLARKELK RMQDLDEDAT LTQLATAWVS LATGGEKLQD 200
    AYYIFQEMAD KCSPTLLLLN GQAACHMAQG RWEAAEGLLQ EALDKDSGYP 250
    ETLVNLIVLS QHLGKPPEVT NRYLSQLKDA HRSHPFIKEY QAKENDFDRL 300
    VLQYAPSA 308
    Length:308
    Mass (Da):34,482
    Last modified:January 23, 2007 - v3
    Checksum:iA71146F3332F6BA9
    GO
    Isoform 2 (identifier: O14579-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         97-97: R → S
         98-148: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:257
    Mass (Da):28,797
    Checksum:i0F26BDC0A83D65BF
    GO
    Isoform 3 (identifier: O14579-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         194-245: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:256
    Mass (Da):28,773
    Checksum:i4B35360D41136F1A
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti13 – 131S → C.
    Corresponds to variant rs2231987 [ dbSNP | Ensembl ].
    VAR_054032
    Natural varianti117 – 1171T → I.2 Publications
    Corresponds to variant rs10330 [ dbSNP | Ensembl ].
    VAR_054033

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei97 – 971R → S in isoform 2. 1 PublicationVSP_042770
    Alternative sequencei98 – 14851Missing in isoform 2. 1 PublicationVSP_042771Add
    BLAST
    Alternative sequencei194 – 24552Missing in isoform 3. 1 PublicationVSP_045070Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ131182 mRNA. Translation: CAA10316.1.
    AJ249366 mRNA. Translation: CAB55628.1.
    AL136928 mRNA. Translation: CAB66862.1.
    AK126476 mRNA. Translation: BAG54333.1.
    AK315281 mRNA. Translation: BAG37690.1.
    CR456886 mRNA. Translation: CAG33167.1.
    AC002985 Genomic DNA. Translation: AAB81543.1.
    AC005197 Genomic DNA. Translation: AAC24612.1.
    CH471106 Genomic DNA. Translation: EAW84749.1.
    CH471106 Genomic DNA. Translation: EAW84752.1.
    CH471106 Genomic DNA. Translation: EAW84756.1.
    BC003155 mRNA. Translation: AAH03155.1.
    BC007250 mRNA. Translation: AAH07250.1.
    BC017285 mRNA. Translation: AAH17285.1.
    BM454494 mRNA. No translation available.
    CCDSiCCDS12387.1. [O14579-1]
    CCDS12388.1. [O14579-2]
    CCDS12389.1. [O14579-3]
    RefSeqiNP_009194.2. NM_007263.3. [O14579-1]
    NP_955474.1. NM_199442.1. [O14579-2]
    NP_955476.1. NM_199444.1. [O14579-3]
    UniGeneiHs.10326.

    Genome annotation databases

    EnsembliENST00000262812; ENSP00000262812; ENSG00000105669. [O14579-1]
    ENST00000349893; ENSP00000343134; ENSG00000105669. [O14579-3]
    ENST00000351079; ENSP00000345674; ENSG00000105669. [O14579-2]
    GeneIDi11316.
    KEGGihsa:11316.
    UCSCiuc002nkk.3. human. [O14579-1]
    uc002nkl.3. human. [O14579-2]
    uc002nkm.3. human.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ131182 mRNA. Translation: CAA10316.1 .
    AJ249366 mRNA. Translation: CAB55628.1 .
    AL136928 mRNA. Translation: CAB66862.1 .
    AK126476 mRNA. Translation: BAG54333.1 .
    AK315281 mRNA. Translation: BAG37690.1 .
    CR456886 mRNA. Translation: CAG33167.1 .
    AC002985 Genomic DNA. Translation: AAB81543.1 .
    AC005197 Genomic DNA. Translation: AAC24612.1 .
    CH471106 Genomic DNA. Translation: EAW84749.1 .
    CH471106 Genomic DNA. Translation: EAW84752.1 .
    CH471106 Genomic DNA. Translation: EAW84756.1 .
    BC003155 mRNA. Translation: AAH03155.1 .
    BC007250 mRNA. Translation: AAH07250.1 .
    BC017285 mRNA. Translation: AAH17285.1 .
    BM454494 mRNA. No translation available.
    CCDSi CCDS12387.1. [O14579-1 ]
    CCDS12388.1. [O14579-2 ]
    CCDS12389.1. [O14579-3 ]
    RefSeqi NP_009194.2. NM_007263.3. [O14579-1 ]
    NP_955474.1. NM_199442.1. [O14579-2 ]
    NP_955476.1. NM_199444.1. [O14579-3 ]
    UniGenei Hs.10326.

    3D structure databases

    ProteinModelPortali O14579.
    SMRi O14579. Positions 17-307.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116447. 26 interactions.
    IntActi O14579. 8 interactions.
    MINTi MINT-5000768.
    STRINGi 9606.ENSP00000262812.

    PTM databases

    PhosphoSitei O14579.

    2D gel databases

    OGPi O14579.

    Proteomic databases

    MaxQBi O14579.
    PaxDbi O14579.
    PRIDEi O14579.

    Protocols and materials databases

    DNASUi 11316.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262812 ; ENSP00000262812 ; ENSG00000105669 . [O14579-1 ]
    ENST00000349893 ; ENSP00000343134 ; ENSG00000105669 . [O14579-3 ]
    ENST00000351079 ; ENSP00000345674 ; ENSG00000105669 . [O14579-2 ]
    GeneIDi 11316.
    KEGGi hsa:11316.
    UCSCi uc002nkk.3. human. [O14579-1 ]
    uc002nkl.3. human. [O14579-2 ]
    uc002nkm.3. human.

    Organism-specific databases

    CTDi 11316.
    GeneCardsi GC19M019010.
    HGNCi HGNC:2234. COPE.
    HPAi CAB034345.
    HPA041605.
    HPA043576.
    MIMi 606942. gene.
    neXtProti NX_O14579.
    PharmGKBi PA26750.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG289253.
    HOGENOMi HOG000205825.
    HOVERGENi HBG002201.
    InParanoidi O14579.
    KOi K17268.
    OrthoDBi EOG7QK0CC.
    PhylomeDBi O14579.
    TreeFami TF313390.

    Enzyme and pathway databases

    Reactomei REACT_11096. COPI Mediated Transport.

    Miscellaneous databases

    ChiTaRSi COPE. human.
    GeneWikii COPE_(gene).
    GenomeRNAii 11316.
    NextBioi 42987.
    PROi O14579.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O14579.
    Bgeei O14579.
    CleanExi HS_COPE.
    Genevestigatori O14579.

    Family and domain databases

    Gene3Di 1.25.40.10. 1 hit.
    InterProi IPR006822. Coatomer_esu.
    IPR011990. TPR-like_helical.
    [Graphical view ]
    PANTHERi PTHR10805. PTHR10805. 1 hit.
    Pfami PF04733. Coatomer_E. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF016478. Coatomer_esu. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Segregation of COPI-rich and anterograde-cargo-rich domains in endoplasmic-reticulum-to-Golgi transport complexes."
      Shima D.T., Scales S.J., Kreis T.E., Pepperkok R.
      Curr. Biol. 9:821-824(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-117.
      Tissue: Brain.
    2. "Cloning, expression, and phosphorylation by protein kinase A of human epsilon-COP."
      Baehr C., Herzog A., Haeussermann S., Marks F., Gschwendt M.
      Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Uterus.
    4. "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 1 AND 2), VARIANT ILE-117.
      Tissue: Testis and Uterus.
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. "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].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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 1 AND 3).
      Tissue: Brain, Embryonic carcinoma, Lymph and Skin.
    9. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-23; 66-85 AND 172-211, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryonic kidney.
    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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Ubiquitylation of epsilon-COP by PIRH2 and regulation of the secretion of PSA."
      Maruyama S., Miyajima N., Bohgaki M., Tsukiyama T., Shigemura M., Nonomura K., Hatakeyama S.
      Mol. Cell. Biochem. 307:73-82(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION BY RCHY1.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCOPE_HUMAN
    AccessioniPrimary (citable) accession number: O14579
    Secondary accession number(s): A6NE29
    , A6NKA3, O76097, Q6IBB8, Q9UGP6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 127 of the entry and version 3 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 19
      Human chromosome 19: 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