COPB2

Protein-coding gene in humans
COPB2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

5A1U, 5A1V, 5A1W, 5A1X, 5A1Y

Identifiers
AliasesCOPB2, beta'-COP, coatomer protein complex subunit beta 2, MCPH19, COPI coat complex subunit beta 2
External IDsOMIM: 606990; MGI: 1354962; HomoloGene: 3499; GeneCards: COPB2; OMA:COPB2 - orthologs
Gene location (Human)
Chromosome 3 (human)
Chr.Chromosome 3 (human)[1]
Chromosome 3 (human)
Genomic location for COPB2
Genomic location for COPB2
Band3q23Start139,353,946 bp[1]
End139,389,736 bp[1]
Gene location (Mouse)
Chromosome 9 (mouse)
Chr.Chromosome 9 (mouse)[2]
Chromosome 9 (mouse)
Genomic location for COPB2
Genomic location for COPB2
Band9|9 E3.3Start98,445,774 bp[2]
End98,470,435 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • parotid gland

  • stromal cell of endometrium

  • beta cell

  • oral cavity

  • body of pancreas

  • mucosa of sigmoid colon

  • bronchial epithelial cell

  • smooth muscle tissue

  • Achilles tendon

  • rectum
Top expressed in
  • ascending aorta

  • aortic valve

  • lobe of prostate

  • Paneth cell

  • Rostral migratory stream

  • vas deferens

  • fossa

  • seminal vesicula

  • calvaria

  • pituitary gland
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • structural molecule activity
  • protein binding
Cellular component
  • cytoplasm
  • cytosol
  • Golgi apparatus
  • membrane
  • Golgi membrane
  • COPI-coated vesicle membrane
  • transport vesicle
  • membrane coat
  • COPI vesicle coat
  • cytoplasmic vesicle
  • endoplasmic reticulum membrane
Biological process
  • retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum
  • toxin transport
  • endoplasmic reticulum to Golgi vesicle-mediated transport
  • protein transport
  • intracellular protein transport
  • intra-Golgi vesicle-mediated transport
  • vesicle-mediated transport
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

9276

50797

Ensembl

ENSG00000184432

ENSMUSG00000032458

UniProt

P35606

O55029

RefSeq (mRNA)

NM_004766

NM_015827

RefSeq (protein)

NP_004757

NP_056642

Location (UCSC)Chr 3: 139.35 – 139.39 MbChr 9: 98.45 – 98.47 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Coatomer subunit beta is a protein that is encoded by the COPB2 gene in humans.[5][6]

Function

The Golgi coatomer complex (see MIM 601924) constitutes the coat of non-clathrin-coated vesicles and is essential for Golgi budding and vesicular trafficking. It consists of 7 protein subunits, including COPB2.[supplied by OMIM][6]

Interactions

COPB2 has been shown to interact with:

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000184432 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000032458 – 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. ^ De Baere E, Speleman F, Van Roy N, De Paepe A, Messiaen L (February 1999). "Assignment of the cellular retinol-binding protein 1 gene (RBP1) and of the coatomer beta subunit gene (COPB2) to human chromosome band 3q23 by in situ hybridization". Cytogenet Cell Genet. 82 (3–4): 226–7. doi:10.1159/000015107. PMID 9858824. S2CID 46851294.
  6. ^ a b "Entrez Gene: COPB2 coatomer protein complex, subunit beta 2 (beta prime)".
  7. ^ 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.
  8. ^ Lowe M, Kreis TE (November 1996). "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.
  9. ^ England K, Ashford D, Kidd D, Rumsby M (June 2002). "PKC epsilon is associated with myosin IIA and actin in fibroblasts". Cell. Signal. 14 (6): 529–36. doi:10.1016/s0898-6568(01)00277-7. PMID 11897493.
  10. ^ Sullivan BM, Harrison-Lavoie KJ, Marshansky V, Lin HY, Kehrl JH, Ausiello DA, Brown D, Druey KM (September 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.

External links

  • Human COPB2 genome location and COPB2 gene details page in the UCSC Genome Browser.
  • Overview of all the structural information available in the PDB for UniProt: O55029 (Mouse Coatomer subunit beta') at the PDBe-KB.

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.
  • Stenbeck G, Harter C, Brecht A, Herrmann D, Lottspeich F, Orci L, Wieland FT (1993). "beta'-COP, a novel subunit of coatomer". EMBO J. 12 (7): 2841–5. doi:10.1002/j.1460-2075.1993.tb05945.x. PMC 413534. PMID 8334999.
  • Harrison-Lavoie KJ, Lewis VA, Hynes GM, Collison KS, Nutland E, Willison KR (1993). "A 102 kDa subunit of a Golgi-associated particle has homology to beta subunits of trimeric G proteins". EMBO J. 12 (7): 2847–53. doi:10.1002/j.1460-2075.1993.tb05946.x. PMC 413536. PMID 8335000.
  • Lowe M, Kreis TE (1996). "In vitro assembly and disassembly of coatomer". J. Biol. Chem. 270 (52): 31364–71. doi:10.1074/jbc.270.52.31364. PMID 8537409.
  • 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.
  • Csukai M, Chen CH, De Matteis MA, Mochly-Rosen D (1997). "The coatomer protein beta'-COP, a selective binding protein (RACK) for protein kinase Cepsilon". J. Biol. Chem. 272 (46): 29200–6. doi:10.1074/jbc.272.46.29200. PMID 9360998.
  • 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.
  • Sullivan BM, Harrison-Lavoie KJ, Marshansky V, Lin HY, Kehrl JH, Ausiello DA, Brown D, Druey KM (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.
  • Zhang T, Hong W (2001). "Ykt6 forms a SNARE complex with syntaxin 5, GS28, and Bet1 and participates in a late stage in endoplasmic reticulum-Golgi transport". J. Biol. Chem. 276 (29): 27480–7. doi:10.1074/jbc.M102786200. PMID 11323436.
  • 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" (PDF). Mol. Biol. Cell. 13 (10): 3493–507. doi:10.1091/mbc.E02-01-0004. PMC 129961. PMID 12388752.
  • Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801. S2CID 23783563.
  • Rohde HM, Cheong FY, Konrad G, Paiha K, Mayinger P, Boehmelt G (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.
  • Bouwmeester T, Bauch A, Ruffner H, Angrand PO, Bergamini G, Croughton K, Cruciat C, Eberhard D, Gagneur J, Ghidelli S, Hopf C, Huhse B, Mangano R, Michon AM, Schirle M, Schlegl J, Schwab M, Stein MA, Bauer A, Casari G, Drewes G, Gavin AC, Jackson DB, Joberty G, Neubauer G, Rick J, Kuster B, Superti-Furga G (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216. S2CID 11683986.
  • 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.
  • Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.
  • Tu LC, Yan X, Hood L, Lin B (2007). "Proteomics analysis of the interactome of N-myc downstream regulated gene 1 and its interactions with the androgen response program in prostate cancer cells". Mol. Cell. Proteomics. 6 (4): 575–88. doi:10.1074/mcp.M600249-MCP200. PMID 17220478. S2CID 7203032.
  • v
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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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