COPG2

COPG2
Identifiers
Aliases	COPG2 , 2-COP, gamma-2-COP, coatomer protein complex subunit gamma 2, COPI coat complex subunit gamma 2
External IDs	OMIM: 604355; MGI: 1858683; HomoloGene: 56292; GeneCards: COPG2; OMA:COPG2 - orthologs
Gene location (Human) Chr. Chromosome 7 (human) [1] Band 7q32.2 Start 130,506,238 bp [1] End 130,668,748 bp [1]
Gene location (Mouse) Chr. Chromosome 6 (mouse) [2] Band 6|6 A3.3 Start 30,747,553 bp [2] End 30,873,729 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ganglionic eminence ventricular zone right adrenal gland right adrenal cortex left adrenal gland left ovary islet of Langerhans left adrenal cortex right testis right ovary Top expressed in spermatocyte zygote transitional epithelium of urinary bladder secondary oocyte genital tubercle tail of embryo granulocyte lateral hypothalamus medial vestibular nucleus ventromedial nucleus More reference expression data BioGPS n/a
Gene ontology Molecular function structural molecule activity Cellular component cytoplasmic vesicle Golgi membrane transport vesicle cytosol membrane membrane coat cytoplasm COPI vesicle coat Golgi apparatus COPI-coated vesicle membrane endoplasmic reticulum membrane endoplasmic reticulum endoplasmic reticulum-Golgi intermediate compartment Biological process intracellular protein transport vesicle-mediated transport intra-Golgi vesicle-mediated transport endoplasmic reticulum to Golgi vesicle-mediated transport protein transport retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum protein secretion organelle transport along microtubule Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 26958 54160 Ensembl ENSG00000158623 ENSMUSG00000025607 UniProt Q9UBF2 Q9QXK3 RefSeq (mRNA) NM_012133 NM_001290033 NM_017478 RefSeq (protein) NP_001276962 NP_036265 NP_059506 Location (UCSC) Chr 7: 130.51 – 130.67 Mb Chr 6: 30.75 – 30.87 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Coatomer subunit gamma-2 is a protein that in humans is encoded by the COPG2 gene. ^{[5] [6] [7]}

Interactions

COPG2 has been shown to interact with Dopamine receptor D1 ^[8] and COPB1. ^{[9] [10]}

References

1. GRCh38: Ensembl release 89: ENSG00000158623 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000025607 – 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. Blagitko N, Schulz U, Schinzel AA, Ropers HH, Kalscheuer VM (Jan 2000). "gamma2-COP, a novel imprinted gene on chromosome 7q32, defines a new imprinting cluster in the human genome". Hum Mol Genet. 8 (13): 2387–96. doi: 10.1093/hmg/8.13.2387 . PMID   10556286.
6. Yamasaki K, Hayashida S, Miura K, Masuzaki H, Ishimaru T, Niikawa N, Kishino T (Nov 2000). "The novel gene, gamma2-COP (COPG2), in the 7q32 imprinted domain escapes genomic imprinting". Genomics. 68 (3): 330–5. doi:10.1006/geno.2000.6265. PMID   10995575.
7. "Entrez Gene: COPG2 coatomer protein complex, subunit gamma 2".
8. Bermak JC, Li M, Bullock C, Weingarten P, Zhou QY (Feb 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.
9. Takatsu H, Futatsumori M, Yoshino K, Yoshida Y, Shin HW, Nakayama K (Jun 2001). "Similar subunit interactions contribute to assembly of clathrin adaptor complexes and COPI complex: analysis using yeast three-hybrid system". Biochem. Biophys. Res. Commun. 284 (4): 1083–9. doi:10.1006/bbrc.2001.5081. PMID   11409905.
10. Futatsumori M, Kasai K, Takatsu H, Shin HW, Nakayama K (2000). "Identification and characterization of novel isoforms of COP I subunits". J Biochem. 128 (5): 793–801. doi:10.1093/oxfordjournals.jbchem.a022817. PMID   11056392.

External links

• Human COPG2 genome location and COPG2 gene details page in the UCSC Genome Browser .

Further reading

• Pelham HR, Rothman JE (2000). "The debate about transport in the Golgi--two sides of the same coin?". Cell. 102 (6): 713–9. doi: 10.1016/S0092-8674(00)00060-X . PMID   11030615. S2CID   18044044.
• Waters MG, Serafini T, Rothman JE (1991). "'Coatomer': a cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles". Nature. 349 (6306): 248–51. Bibcode:1991Natur.349..248W. doi:10.1038/349248a0. PMID   1898986. S2CID   4342145.
• 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.
• Harter C, Wieland FT (1998). "A single binding site for dilysine retrieval motifs and p23 within the gamma subunit of coatomer". Proc. Natl. Acad. Sci. U.S.A. 95 (20): 11649–54. Bibcode:1998PNAS...9511649H. doi: 10.1073/pnas.95.20.11649 . PMC   21695 . PMID   9751720.
• Zhao L, Helms JB, Brunner J, Wieland FT (1999). "GTP-dependent binding of ADP-ribosylation factor to coatomer in close proximity to the binding site for dilysine retrieval motifs and p23". J. Biol. Chem. 274 (20): 14198–203. doi: 10.1074/jbc.274.20.14198 . PMID   10318838.
• 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.
• Futatsumori M, Kasai K, Takatsu H, Shin HW, Nakayama K (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.
• Takatsu H, Futatsumori M, Yoshino K, Yoshida Y, Shin HW, Nakayama K (2001). "Similar subunit interactions contribute to assembly of clathrin adaptor complexes and COPI complex: analysis using yeast three-hybrid system". Biochem. Biophys. Res. Commun. 284 (4): 1083–9. doi:10.1006/bbrc.2001.5081. PMID   11409905.
• Paulsson KM, Kleijmeer MJ, Griffith J, Jevon M, Chen S, Anderson PO, Sjogren HO, Li S, Wang P (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, Weingarten P, Zhou QY (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.
• Bonora E, Bacchelli E, Levy ER, Blasi F, Marlow A, Monaco AP, Maestrini E (2002). "Mutation screening and imprinting analysis of four candidate genes for autism in the 7q32 region". Mol. Psychiatry. 7 (3): 289–301. doi: 10.1038/sj.mp.4001004 . PMID   11920156.
• Scanlan MJ, Gout I, Gordon CM, Williamson B, Stockert E, Gure AO, Jäger D, Chen YT, Mackay A, O'Hare MJ, Old LJ (2003). "Humoral immunity to human breast cancer: antigen definition and quantitative analysis of mRNA expression". Cancer Immun. 1: 4. PMID   12747765.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID   16189514. S2CID   4427026.
• Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (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.