COPE (gene)

Coatomer subunit epsilon is a protein that in humans is encoded by the COPE gene.[5][6]

COPE
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCOPE, epsilon-COP, coatomer protein complex subunit epsilon, COPI coat complex subunit epsilon
External IDsOMIM: 606942 MGI: 1891702 HomoloGene: 5254 GeneCards: COPE
Gene location (Human)
Chr.Chromosome 19 (human)[1]
Band19p13.11Start18,899,514 bp[1]
End18,919,387 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

11316

59042

Ensembl

ENSG00000105669

ENSMUSG00000055681

UniProt

O14579

O89079

RefSeq (mRNA)

NM_007263
NM_199442
NM_199444
NM_001330469

NM_021538

RefSeq (protein)

NP_001317398
NP_009194
NP_955474
NP_955476

NP_067513

Location (UCSC)Chr 19: 18.9 – 18.92 MbChr 8: 70.3 – 70.31 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function

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.[6]

Interactions

COPE (gene) has been shown to interact with COPA.[7][8][9]

References

  1. GRCh38: Ensembl release 89: ENSG00000105669 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000055681 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. 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. S2CID 16182290.
  6. "Entrez Gene: COPE coatomer protein complex, subunit epsilon".
  7. Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (September 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.
  8. 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. 19 (15): 3905–17. doi:10.1093/emboj/19.15.3905. PMC 306616. PMID 10921873.
  9. Faulstich D, Auerbach S, Orci L, Ravazzola M, Wegchingel S, Lottspeich F, Stenbeck G, Harter C, Wieland FT, Tschochner H (October 1996). "Architecture of coatomer: molecular characterization of delta-COP and protein interactions within the complex". J. Cell Biol. 135 (1): 53–61. doi:10.1083/jcb.135.1.53. PMC 2121028. PMID 8858162.

Further reading


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