COPB1

Protein-coding gene in humans
COPB1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

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

Identifiers
AliasesCOPB1, COPB, coatomer protein complex subunit beta 1, COPI coat complex subunit beta 1, BARMACS
External IDsOMIM: 600959 MGI: 1917599 HomoloGene: 5664 GeneCards: COPB1
Gene location (Human)
Chromosome 11 (human)
Chr.Chromosome 11 (human)[1]
Chromosome 11 (human)
Genomic location for COPB1
Genomic location for COPB1
Band11p15.2Start14,443,440 bp[1]
End14,500,027 bp[1]
Gene location (Mouse)
Chromosome 7 (mouse)
Chr.Chromosome 7 (mouse)[2]
Chromosome 7 (mouse)
Genomic location for COPB1
Genomic location for COPB1
Band7 F1|7 59.31 cMStart113,814,794 bp[2]
End113,853,946 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • pancreatic ductal cell

  • corpus epididymis

  • caput epididymis

  • endothelial cell

  • germinal epithelium

  • tibia

  • jejunal mucosa

  • parotid gland

  • bronchial epithelial cell

  • visceral pleura
Top expressed in
  • parotid gland

  • basilar part of occipital bone

  • secondary oocyte

  • dermis

  • molar

  • calvaria

  • islet of Langerhans

  • endocardial cushion

  • submandibular gland

  • atrioventricular valve
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • structural molecule activity
  • protein binding
Cellular component
  • Golgi apparatus
  • membrane
  • intracellular membrane-bounded organelle
  • Golgi membrane
  • COPI-coated vesicle membrane
  • transport vesicle
  • Golgi-associated vesicle
  • membrane coat
  • cytoplasmic vesicle
  • COPI-coated vesicle
  • endoplasmic reticulum-Golgi intermediate compartment
  • endoplasmic reticulum membrane
  • cytoplasm
  • cytosol
  • plasma membrane
  • COPI vesicle coat
  • secretory granule membrane
  • tertiary granule membrane
  • ficolin-1-rich granule membrane
Biological process
  • protein transport
  • intracellular protein transport
  • viral process
  • vesicle-mediated transport
  • endoplasmic reticulum to Golgi vesicle-mediated transport
  • retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum
  • intra-Golgi vesicle-mediated transport
  • neutrophil degranulation
  • transport
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

1315

70349

Ensembl

ENSG00000129083

ENSMUSG00000030754

UniProt

P53618

Q9JIF7

RefSeq (mRNA)

NM_016451
NM_001144061
NM_001144062

NM_033370

RefSeq (protein)

NP_001137533
NP_001137534
NP_057535

NP_203534

Location (UCSC)Chr 11: 14.44 – 14.5 MbChr 7: 113.81 – 113.85 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Coatomer subunit beta is a protein that in humans is encoded by the COPB1 gene.[5]

See also

  • COPI coatomer, a protein complex

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000129083 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000030754 – 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. ^ Benichou S, Bomsel M, Bodeus M, Durand H, Doute M, Letourneur F, Camonis J, Benarous R (Dec 1994). "Physical interaction of the HIV-1 Nef protein with beta-COP, a component of non-clathrin-coated vesicles essential for membrane traffic". J Biol Chem. 269 (48): 30073–6. doi:10.1016/S0021-9258(18)43773-8. PMID 7982906.

Further reading

  • Benichou S, Liu LX, Erdtmann L, et al. (1997). "Use of the two-hybrid system to identify cellular partners of the HIV1 Nef protein". Res. Virol. 148 (1): 71–3. doi:10.1016/S0923-2516(97)81918-8. PMID 9017839.
  • Geyer M, Fackler OT, Peterlin BM (2001). "Structure–function relationships in HIV-1 Nef". EMBO Rep. 2 (7): 580–5. doi:10.1093/embo-reports/kve141. PMC 1083955. PMID 11463741.
  • Duden R, Griffiths G, Frank R, et al. (1991). "Beta-COP, a 110 kd protein associated with non-clathrin-coated vesicles and the Golgi complex, shows homology to beta-adaptin". Cell. 64 (3): 649–65. doi:10.1016/0092-8674(91)90248-W. PMID 1840503. S2CID 54293222.
  • 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.
  • Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins from the cytosol". Nature. 364 (6439): 732–4. Bibcode:1993Natur.364..732O. doi:10.1038/364732a0. PMID 8355790. S2CID 4348442.
  • Aniento F, Gu F, Parton RG, Gruenberg J (1996). "An endosomal beta COP is involved in the pH-dependent formation of transport vesicles destined for late endosomes" (PDF). J. Cell Biol. 133 (1): 29–41. doi:10.1083/jcb.133.1.29. PMC 2120778. PMID 8601610.
  • 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.
  • Hansen K, Rönnstrand L, Rorsman C, et al. (1997). "Association of coatomer proteins with the beta-receptor for platelet-derived growth factor". Biochem. Biophys. Res. Commun. 235 (3): 455–60. doi:10.1006/bbrc.1997.6821. PMID 9207175.
  • Pavel J, Harter C, Wieland FT (1998). "Reversible dissociation of coatomer: Functional characterization of a β/δ-coat protein subcomplex". Proc. Natl. Acad. Sci. U.S.A. 95 (5): 2140–5. Bibcode:1998PNAS...95.2140P. doi:10.1073/pnas.95.5.2140. PMC 19276. PMID 9482852.
  • Piguet V, Gu F, Foti M, et al. (1999). "Nef-induced CD4 degradation: a diacidic-based motif in Nef functions as a lysosomal targeting signal through the binding of beta-COP in endosomes". Cell. 97 (1): 63–73. doi:10.1016/S0092-8674(00)80715-1. PMID 10199403. S2CID 14793848.
  • 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.
  • Fischer KD, Helms JB, Zhao L, Wieland FT (2000). "Site-specific photocrosslinking to probe interactions of Arf1 with proteins involved in budding of COPI vesicles". Methods. 20 (4): 455–64. doi:10.1006/meth.2000.0958. PMID 10720466.
  • Allan BB, Moyer BD, Balch WE (2000). "Rab1 recruitment of p115 into a cis-SNARE complex: programming budding COPII vesicles for fusion". Science. 289 (5478): 444–8. Bibcode:2000Sci...289..444A. doi:10.1126/science.289.5478.444. PMID 10903204.
  • 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, et al. (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.
  • Futatsumori M, Kasai K, Takatsu H, et al. (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.
  • Hartley JL, Temple GF, Brasch MA (2001). "DNA Cloning Using In Vitro Site-Specific Recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
  • Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a Catalog of Human Genes and Proteins: Sequencing and Analysis of 500 Novel Complete Protein Coding Human cDNAs". Genome Res. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.

External links

  • Human COPB1 genome location and COPB1 gene details page in the UCSC Genome Browser.
  • PDBe-KB provides an overview of all the structure information available in the PDB for Mouse Coatomer subunit beta


  • v
  • t
  • e
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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