ARPC2

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Actin related protein 2/3 complex, subunit 2, 34kDa
File:PBB Protein ARPC2 image.jpg
PDB rendering based on 1k8k.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols ARPC2 ; ARC34; PNAS-139; PRO2446; p34-Arc
External IDs Template:OMIM5 Template:MGI HomoloGene4187
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Actin related protein 2/3 complex, subunit 2, 34kDa, also known as ARPC2, is a human gene.[1]

This gene encodes one of seven subunits of the human Arp2/3 protein complex. The Arp2/3 protein complex has been implicated in the control of actin polymerization in cells and has been conserved through evolution. The exact role of the protein encoded by this gene, the p34 subunit, has yet to be determined. Two alternatively spliced variants have been characterized to date. Additional alternatively spliced variants have been described but their full length nature has not been determined.[1]

References

  1. 1.0 1.1 "Entrez Gene: ARPC2 actin related protein 2/3 complex, subunit 2, 34kDa".

Further reading

  • Couch FJ, Rommens JM, Neuhausen SL; et al. (1997). "Generation of an integrated transcription map of the BRCA2 region on chromosome 13q12-q13". Genomics. 36 (1): 86–99. PMID 8812419.
  • Welch MD, Iwamatsu A, Mitchison TJ (1997). "Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes". Nature. 385 (6613): 265–9. doi:10.1038/385265a0. PMID 9000076.
  • Welch MD, DePace AH, Verma S; et al. (1997). "The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly". J. Cell Biol. 138 (2): 375–84. PMID 9230079.
  • Machesky LM, Reeves E, Wientjes F; et al. (1998). "Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins". Biochem. J. 328 ( Pt 1): 105–12. PMID 9359840.
  • Näär AM, Beaurang PA, Zhou S; et al. (1999). "Composite co-activator ARC mediates chromatin-directed transcriptional activation". Nature. 398 (6730): 828–32. doi:10.1038/19789. PMID 10235267.
  • Zhao X, Yang Z, Qian M, Zhu X (2001). "Interactions among subunits of human Arp2/3 complex: p20-Arc as the hub". Biochem. Biophys. Res. Commun. 280 (2): 513–7. doi:10.1006/bbrc.2000.4151. PMID 11162547.
  • Robinson RC, Turbedsky K, Kaiser DA; et al. (2001). "Crystal structure of Arp2/3 complex". Science. 294 (5547): 1679–84. doi:10.1126/science.1066333. PMID 11721045.
  • Gournier H, Goley ED, Niederstrasser H; et al. (2002). "Reconstitution of human Arp2/3 complex reveals critical roles of individual subunits in complex structure and activity". Mol. Cell. 8 (5): 1041–52. PMID 11741539.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Gevaert K, Goethals M, Martens L; et al. (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.
  • Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Kaneda A, Kaminishi M, Sugimura T, Ushijima T (2004). "Decreased expression of the seven ARP2/3 complex genes in human gastric cancers". Cancer Lett. 212 (2): 203–10. doi:10.1016/j.canlet.2004.03.020. PMID 15279900.
  • Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
  • Andersen JS, Lam YW, Leung AK; et al. (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
  • Dubois T, Paléotti O, Mironov AA; et al. (2005). "Golgi-localized GAP for Cdc42 functions downstream of ARF1 to control Arp2/3 complex and F-actin dynamics". Nat. Cell Biol. 7 (4): 353–64. doi:10.1038/ncb1244. PMID 15793564.
  • Cai L, Holoweckyj N, Schaller MD, Bear JE (2005). "Phosphorylation of coronin 1B by protein kinase C regulates interaction with Arp2/3 and cell motility". J. Biol. Chem. 280 (36): 31913–23. doi:10.1074/jbc.M504146200. PMID 16027158.
  • Cai L, Marshall TW, Uetrecht AC; et al. (2007). "Coronin 1B coordinates Arp2/3 complex and cofilin activities at the leading edge". Cell. 128 (5): 915–29. doi:10.1016/j.cell.2007.01.031. PMID 17350576.
  • Ewing RM, Chu P, Elisma F; et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMID 17353931.

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