Med Library . org

Open Source Encyclopedia

COPB2

Welcome to MedLibrary.org. For best results, we recommend beginning with the navigation links at the top of the page, which can guide you through our collection of over 14,000 medication labels and package inserts. For additional information on other topics which are not covered by our database of medications, just enter your topic in the search box below:

Coatomer protein complex, subunit beta 2 (beta prime)
Identifiers
Symbols COPB2; beta'-COP
External IDs OMIM606990 MGI1354962 HomoloGene3499 GeneCards: COPB2 Gene
RNA expression pattern
PBB GE COPB2 201098 at tn.png
More reference expression data
Orthologs
Species Human Mouse
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:
139.07 – 139.11 Mb
Chr 9:
98.56 – 98.59 Mb
PubMed search [1] [2]

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

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 RGS4,[3] PRKCE[4] and COPB1.[5][6]

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. ^ a b "Entrez Gene: COPB2 coatomer protein complex, subunit beta 2 (beta prime)".
  3. ^ Sullivan, B M; Harrison-Lavoie K J, Marshansky V, Lin H Y, Kehrl J H, Ausiello D A, Brown D, Druey K M (September 2000). "RGS4 and RGS2 Bind Coatomer and Inhibit COPI Association with Golgi Membranes and Intracellular Transport". Mol. Biol. Cell (UNITED STATES) 11 (9): 3155–68. ISSN 1059-1524. PMC 14982. PMID 10982407.
  4. ^ England, Karen; Ashford David, Kidd Daniel, Rumsby Martin (June 2002). "PKC epsilon is associated with myosin IIA and actin in fibroblasts". Cell. Signal. (England) 14 (6): 529–36. doi:10.1016/S0898-6568(01)00277-7. ISSN 0898-6568. PMID 11897493.
  5. ^ 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. (ENGLAND) 19 (15): 3905–17. doi:10.1093/emboj/19.15.3905. ISSN 0261-4189. PMC 306616. PMID 10921873.
  6. ^ Lowe, M; Kreis T E (November 1996). "In vivo assembly of coatomer, the COP-I coat precursor". J. Biol. Chem. (UNITED STATES) 271 (48): 30725–30. doi:10.1074/jbc.271.48.30725. ISSN 0021-9258. PMID 8940050.

Further reading