COPE (gene)

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Coatomer protein complex, subunit epsilon
Identifiers
Symbols COPE ; epsilon-COP
External IDs OMIM606942 MGI1891702 HomoloGene5254 GeneCards: COPE Gene
RNA expression pattern
PBB GE COPE 201264 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 11316 59042
Ensembl ENSG00000105669 ENSMUSG00000055681
UniProt O14579 O89079
RefSeq (mRNA) NM_007263 NM_021538
RefSeq (protein) NP_009194 NP_067513
Location (UCSC) Chr 19:
19.01 – 19.03 Mb
Chr 8:
70.3 – 70.31 Mb
PubMed search [1] [2]

Coatomer subunit epsilon is a protein that in humans is encoded by the COPE gene.[1][2]

The product of this gene is an epsilon subunit of coatomer protein complex. Coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles. It is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. Coatomer complex consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. Alternatively spliced transcript variants encoding different isoforms have been identified.[2]

Interactions[edit]

COPE (gene) has been shown to interact with COPA.[3][4][5]

References[edit]

  1. ^ Shima DT, Scales SJ, Kreis TE, Pepperkok R (November 1999). "Segregation of COPI-rich and anterograde-cargo-rich domains in endoplasmic-reticulum-to-Golgi transport complexes". Curr Biol 9 (15): 821–4. doi:10.1016/S0960-9822(99)80365-0. PMID 10469566. 
  2. ^ a b "Entrez Gene: COPE coatomer protein complex, subunit epsilon". 
  3. ^ Stelzl, Ulrich; Worm Uwe, Lalowski Maciej, Haenig Christian, Brembeck Felix H, Goehler Heike, Stroedicke Martin, Zenkner Martina, Schoenherr Anke, Koeppen Susanne, Timm Jan, Mintzlaff Sascha, Abraham Claudia, Bock Nicole, Kietzmann Silvia, Goedde Astrid, Toksöz Engin, Droege Anja, Krobitsch Sylvia, Korn Bernhard, Birchmeier Walter, Lehrach Hans, Wanker Erich E (September 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell (United States) 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. ISSN 0092-8674. PMID 16169070. 
  4. ^ Eugster, A; Frigerio G; Dale M; Duden R (August 2000). "COP I domains required for coatomer integrity, and novel interactions with ARF and ARF-GAP". EMBO J. (ENGLAND) 19 (15): 3905–17. doi:10.1093/emboj/19.15.3905. ISSN 0261-4189. PMC 306616. PMID 10921873. 
  5. ^ Faulstich, D; Auerbach S; Orci L; Ravazzola M; Wegchingel S; Lottspeich F; Stenbeck G; Harter C; Wieland F T; Tschochner H (October 1996). "Architecture of coatomer: molecular characterization of delta-COP and protein interactions within the complex". J. Cell Biol. (UNITED STATES) 135 (1): 53–61. doi:10.1083/jcb.135.1.53. ISSN 0021-9525. PMC 2121028. PMID 8858162. 

Further reading[edit]