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

COPB2
Available structures
PDBOrtholog search: PDBe RCSB
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
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
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

Function

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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

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COPB2 has been shown to interact with:

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000184432Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000032458Ensembl, 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.
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Further reading

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