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
Gene location (Human)
Chr.	Chromosome 7 (human)
End	130,668,748 bp
Gene location (Mouse)
Chr.	Chromosome 6 (mouse)
End	30,873,729 bp
RNA expression pattern
	Top expressed in
	ovary; ; hypothalamus; ; kidney;
	More reference expression data
	n/a
Gene ontology
Molecular function	structural molecule activity ;
Cellular component	GO:0016023 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
	26958
	54160
	ENSG00000158623
	ENSMUSG00000025607
	Q9UBF2
	Q9QXK3
	NM_012133 ; NM_001290033
	NM_017478
	NP_001276962 ; NP_036265
	NP_059506
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated April 14, 2022

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]

Related Research Articles

COPI is a coatomer, a protein complex that coats vesicles transporting proteins from the cis end of the Golgi complex back to the rough endoplasmic reticulum (ER), where they were originally synthesized, and between Golgi compartments. This type of transport is retrograde transport, in contrast to the anterograde transport associated with the COPII protein. The name "COPI" refers to the specific coat protein complex that initiates the budding process on the cis-Golgi membrane. The coat consists of large protein subcomplexes that are made of seven different protein subunits, namely α, β, β', γ, δ, ε and ζ.

Vesicular transport adaptor proteins are proteins involved in forming complexes that function in the trafficking of molecules from one subcellular location to another. These complexes concentrate the correct cargo molecules in vesicles that bud or extrude off of one organelle and travel to another location, where the cargo is delivered. While some of the details of how these adaptor proteins achieve their trafficking specificity has been worked out, there is still much to be learned.

ADP-ribosylation factor-binding protein GGA1 is a protein that in humans is encoded by the GGA1 gene.

Coatomer subunit beta is a protein that in humans is encoded by the COPB1 gene.

AP-2 complex subunit alpha-1 is a protein that in humans is encoded by the AP2A1 gene.

ADP-ribosylation factor-binding protein GGA3 is a protein that in humans is encoded by the GGA3 gene.

AP-1 complex subunit gamma-1 is a protein that in humans is encoded by the AP1G1 gene.

AP-1 complex subunit beta-1 is a protein that in humans is encoded by the AP1B1 gene.

Coatomer subunit alpha is a protein that in humans is encoded by the COPA gene.

Coatomer subunit epsilon is a protein that in humans is encoded by the COPE gene.

AP-1 complex subunit sigma-1A is a protein that in humans is encoded by the AP1S1 gene.

Coatomer subunit beta' is a protein that in humans is encoded by the COPB2 gene.

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

AP-1 complex subunit gamma-like 2 is a protein that in humans is encoded by the AP1G2 gene.

AP-1 complex subunit sigma-2 is a protein that in humans is encoded by the AP1S2 gene.

Synergin gamma also known as AP1 subunit gamma-binding protein 1 (AP1GBP1) is a protein that in humans is encoded by the SYNRG gene.

AP-4 complex subunit beta-1 is a protein that in humans is encoded by the AP4B1 gene.

Coatomer subunit zeta-1 is a protein that in humans is encoded by the COPZ1 gene.

AP-4 complex subunit epsilon-1 is a protein that in humans is encoded by the AP4E1 gene.

Clathrin adaptor proteins, also known as adaptins, are vesicular transport adaptor proteins associated with clathrin. These proteins are synthesized in the ribosomes, processed in the endoplasmic reticulum and transported from the Golgi apparatus to the trans-Golgi network, and from there via small carrier vesicles to their final destination compartment. The association between adaptins and clathrin are important for vesicular cargo selection and transporting. Clathrin coats contain both clathrin and adaptor complexes that link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Therefore, adaptor proteins are responsible for the recruitment of cargo molecules into a growing clathrin-coated pits. The two major types of clathrin adaptor complexes are the heterotetrameric vesicular transport adaptor proteins (AP1-5), and the monomeric GGA adaptors. Adaptins are distantly related to the other main type of vesicular transport proteins, the coatomer subunits, sharing between 16% and 26% of their amino acid sequence.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000158623 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000025607 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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.
↑ 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.
↑ "Entrez Gene: COPG2 coatomer protein complex, subunit gamma 2".
↑ 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.
↑ 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.
↑ 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 .

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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000158623 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 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.

[pmid10556286-5] 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.

[pmid10995575-6] 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.

[entrez-7] "Entrez Gene: COPG2 coatomer protein complex, subunit gamma 2".

[pmid11893085-8] 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.

[pmid11409905-9] 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.

[pmid11056392-10] 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.

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COPG2

Contents

Interactions

Related Research Articles

References

External links

Further reading