ARPC5

Actin related protein 2/3 complex, subunit 5, 16kDa
File:PBB Protein ARPC5 image.jpg PDB rendering based on 1k8k.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1k8k​, 1tyq​, 1u2v​, 2p9i​, 2p9k​, 2p9l​, 2p9n​, 2p9p​, 2p9s​, 2p9u​
Identifiers
Symbols	ARPC5 ; ARC16; dJ127C7.3; p16-Arc
External IDs	Template:OMIM5 Template:MGI HomoloGene: 4176
Gene ontology Molecular function Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO
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 5, 16kDa, also known as ARPC5, is a human gene.

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 p16 subunit, has yet to be determined.

Further reading

• 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.CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Millard TH, Behrendt B, Launay S; et al. (2003). "Identification and characterisation of a novel human isoform of Arp2/3 complex subunit p16-ARC/ARPC5". Cell Motil. Cytoskeleton. 54 (1): 81–90. doi:10.1002/cm.10087. PMID 12451597.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Singh S, Powell DW, Rane MJ; et al. (2003). "Identification of the p16-Arc subunit of the Arp 2/3 complex as a substrate of MAPK-activated protein kinase 2 by proteomic analysis". J. Biol. Chem. 278 (38): 36410–7. doi:10.1074/jbc.M306428200. PMID 12829704.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Gregory SG, Barlow KF, McLay KE; et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)