COPG2

Protein-coding gene in humans
COPG2
Identifiers
AliasesCOPG2, 2-COP, gamma-2-COP, coatomer protein complex subunit gamma 2, COPI coat complex subunit gamma 2
External IDsOMIM: 604355; MGI: 1858683; HomoloGene: 56292; GeneCards: COPG2; OMA:COPG2 - orthologs
Gene location (Human)
Chromosome 7 (human)
Chr.Chromosome 7 (human)[1]
Chromosome 7 (human)
Genomic location for COPG2
Genomic location for COPG2
Band7q32.2Start130,506,238 bp[1]
End130,668,748 bp[1]
Gene location (Mouse)
Chromosome 6 (mouse)
Chr.Chromosome 6 (mouse)[2]
Chromosome 6 (mouse)
Genomic location for COPG2
Genomic location for COPG2
Band6|6 A3.3Start30,747,553 bp[2]
End30,873,729 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
SpeciesHumanMouse
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 MbChr 6: 30.75 – 30.87 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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. ^ a b c GRCh38: Ensembl release 89: ENSG00000158623 – Ensembl, May 2017
  2. ^ a b c 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

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.
  • v
  • t
  • e
Synaptic vesicle
SNARE
Q-SNARE
R-SNARE
Synaptotagmin
Other
COPICOPIIRME/Clathrin
CaveolaeOther/ungrouped
Vesicle formation
Adaptor protein complex 1:
Adaptor protein complex 2:
Adaptor protein complex 3:
Adaptor protein complex 4:
BLOC-1:
BLOC-2:
BLOC-3:
Coats:
Small GTPase
Other
See also vesicular transport protein disorders


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