COPG

COPG1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1R4X
Identifiers
Aliases	COPG1, COPG, coatomer protein complex subunit gamma 1, COPI coat complex subunit gamma 1
External IDs	OMIM: 615525; MGI: 1858696; HomoloGene: 56745; GeneCards: COPG1; OMA:COPG1 - orthologs
Gene location (Human) Chr. Chromosome 3 (human)[1] Band 3q21.3 Start 129,249,606 bp[1] End 129,277,773 bp[1]
Gene location (Mouse) Chr. Chromosome 6 (mouse)[2] Band 6 D1|6 39.13 cM Start 87,864,796 bp[2] End 87,890,577 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in stromal cell of endometrium anterior pituitary body of pancreas mucosa of transverse colon islet of Langerhans minor salivary glands right lobe of thyroid gland body of stomach right adrenal gland rectum Top expressed in yolk sac dentate gyrus of hippocampal formation granule cell molar superior frontal gyrus supraoptic nucleus pituitary gland dermis central gray substance of midbrain islet of Langerhans crypt of lieberkuhn of small intestine More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding structural molecule activity Cellular component cytoplasm membrane coat COPI-coated vesicle membrane membrane transport vesicle cytosol cytoplasmic vesicle Golgi apparatus Golgi membrane COPI vesicle coat endoplasmic reticulum membrane endoplasmic reticulum endoplasmic reticulum-Golgi intermediate compartment Biological process retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum protein transport organelle transport along microtubule intracellular protein transport establishment of Golgi localization endoplasmic reticulum to Golgi vesicle-mediated transport vesicle-mediated transport intra-Golgi vesicle-mediated transport protein secretion Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 22820 54161 Ensembl ENSG00000181789 ENSMUSG00000030058 UniProt Q9Y678 Q9QZE5 RefSeq (mRNA) NM_016128 NM_017477 NM_201244 RefSeq (protein) NP_057212 NP_059505 NP_957696 Location (UCSC) Chr 3: 129.25 – 129.28 Mb Chr 6: 87.86 – 87.89 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Coatomer subunit gamma is a protein that in humans is encoded by the COPG gene.^[5][6] It is one of seven proteins in the COPI coatomer complex that coats vesicles as they bud from the Golgi complex.^[5]

Interactions

COPG has been shown to interact with Dopamine receptor D1,^[7] COPZ1^[5][8] and COPB1.^[5][9]

References

1. GRCh38: Ensembl release 89: ENSG00000181789 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000030058 – 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. Futatsumori M, Kasai K, Takatsu H, Shin HW, Nakayama K (February 2001). "Identification and characterization of novel isoforms of COP I subunits". J Biochem. 128 (5): 793–801. doi:10.1093/oxfordjournals.jbchem.a022817. PMID 11056392.
6. "Entrez Gene: COPG coatomer protein complex, subunit gamma".
7. Bermak, Jason C; Li Ming; Bullock Clayton; Weingarten Paul; Zhou Qun-Yong (February 2002). "Interaction of gamma-COP with a transport motif in the D1 receptor C-terminus". Eur. J. Cell Biol. 81 (2). Germany: 77–85. doi:10.1078/0171-9335-00222. ISSN 0171-9335. PMID 11893085.
8. 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" (PDF). J. Cell Biol. 135 (1). UNITED STATES: 53–61. doi:10.1083/jcb.135.1.53. ISSN 0021-9525. PMC 2121028. PMID 8858162.
9. Lowe, M; Kreis T E (November 1996). "In vivo assembly of coatomer, the COP-I coat precursor". J. Biol. Chem. 271 (48). UNITED STATES: 30725–30. doi:10.1074/jbc.271.48.30725. ISSN 0021-9258. PMID 8940050.

External links

• Human COPG1 genome location and COPG1 gene details page in the UCSC Genome Browser.

Further reading

• Lowe M, Kreis TE (1997). "In vivo assembly of coatomer, the COP-I coat precursor". J. Biol. Chem. 271 (48): 30725–30. doi:10.1074/jbc.271.48.30725. PMID 8940050.
• Pavel J, Harter C, Wieland FT (1998). "Reversible dissociation of coatomer: functional characterization of a beta/delta-coat protein subcomplex". Proc. Natl. Acad. Sci. U.S.A. 95 (5): 2140–5. Bibcode:1998PNAS...95.2140P. doi:10.1073/pnas.95.5.2140. PMC 19276. PMID 9482852.
• Fischer KD, Helms JB, Zhao L, Wieland FT (2000). "Site-specific photocrosslinking to probe interactions of Arf1 with proteins involved in budding of COPI vesicles". Methods. 20 (4): 455–64. doi:10.1006/meth.2000.0958. PMID 10720466.
• Eugster A, Frigerio G, Dale M, Duden R (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.
• Hu RM, Han ZG, Song HD, et al. (2000). "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning". Proc. Natl. Acad. Sci. U.S.A. 97 (17): 9543–8. Bibcode:2000PNAS...97.9543H. doi:10.1073/pnas.160270997. PMC 16901. PMID 10931946.
• Sullivan BM, Harrison-Lavoie KJ, Marshansky V, et al. (2000). "RGS4 and RGS2 bind coatomer and inhibit COPI association with Golgi membranes and intracellular transport". Mol. Biol. Cell. 11 (9): 3155–68. doi:10.1091/mbc.11.9.3155. PMC 14982. PMID 10982407.
• Hahn Y, Lee YJ, Yun JH, et al. (2000). "Duplication of genes encoding non-clathrin coat protein gamma-COP in vertebrate, insect and plant evolution". FEBS Lett. 482 (1–2): 31–6. doi:10.1016/S0014-5793(00)02033-0. PMID 11018518. S2CID 36356269.
• Paulsson KM, Kleijmeer MJ, Griffith J, et al. (2002). "Association of tapasin and COPI provides a mechanism for the retrograde transport of major histocompatibility complex (MHC) class I molecules from the Golgi complex to the endoplasmic reticulum". J. Biol. Chem. 277 (21): 18266–71. doi:10.1074/jbc.M201388200. PMID 11884415.
• Bermak JC, Li M, Bullock C, et al. (2002). "Interaction of gamma-COP with a transport motif in the D1 receptor C-terminus". Eur. J. Cell Biol. 81 (2): 77–85. doi:10.1078/0171-9335-00222. PMID 11893085.
• Kanzaki M, Watson RT, Hou JC, et al. (2003). "Small GTP-binding protein TC10 differentially regulates two distinct populations of filamentous actin in 3T3L1 adipocytes". Mol. Biol. Cell. 13 (7): 2334–46. doi:10.1091/mbc.01-10-0490. PMC 117317. PMID 12134073.
• Xu Y, Martin S, James DE, Hong W (2003). "GS15 forms a SNARE complex with syntaxin 5, GS28, and Ykt6 and is implicated in traffic in the early cisternae of the Golgi apparatus". Mol. Biol. Cell. 13 (10): 3493–507. doi:10.1091/mbc.E02-01-0004. PMC 129961. PMID 12388752.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Rohde HM, Cheong FY, Konrad G, et al. (2004). "The human phosphatidylinositol phosphatase SAC1 interacts with the coatomer I complex". J. Biol. Chem. 278 (52): 52689–99. doi:10.1074/jbc.M307983200. PMID 14527956.
• Watson PJ, Frigerio G, Collins BM, et al. (2004). "Gamma-COP appendage domain - structure and function". Traffic. 5 (2): 79–88. doi:10.1111/j.1600-0854.2004.00158.x. PMID 14690497. S2CID 24249308.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.