COPB2

Coatomer protein complex, subunit beta 2 (beta prime)
Identifiers
SymbolsCOPB2 ; beta'-COP
External IDsOMIM: 606990 MGI: 1354962 HomoloGene: 3499 GeneCards: COPB2 Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez927650797
EnsemblENSG00000184432ENSMUSG00000032458
UniProtP35606O55029
RefSeq (mRNA)NM_004766NM_015827
RefSeq (protein)NP_004757NP_056642
Location (UCSC)Chr 3:
139.07 – 139.11 Mb
Chr 9:
98.56 – 98.59 Mb
PubMed search

Coatomer subunit beta' is a protein that in humans is encoded by the COPB2 gene.[1][2]

Function

The Golgi coatomer complex (see MIM 601924) constitutes the coat of nonclathrin-coated vesicles and is essential for Golgi budding and vesicular trafficking. It consists of 7 protein subunits, including COPB2.[supplied by OMIM][2]

Interactions


COPB2 has been shown to interact with:

References

  1. 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.
  2. 2.0 2.1 "Entrez Gene: COPB2 coatomer protein complex, subunit beta 2 (beta prime)".
  3. 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.
  4. 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.
  5. 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.
  6. Sullivan BM, Harrison-Lavoie KJ, Marshansky V, Lin HY, Kehrl JH, Ausiello DA et al. (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.

Further reading