Biology:ARPC3
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Revision as of 21:23, 11 October 2021 by imported>NBrushPhys (change)
Generic protein structure example |
ARP2/3 complex ARPC3 (21 kDa) subunit | |||||||||
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crystal structure of arp2/3 complex with bound adp and calcium | |||||||||
Identifiers | |||||||||
Symbol | P21-Arc | ||||||||
Pfam | PF04062 | ||||||||
InterPro | IPR007204 | ||||||||
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Actin-related protein 2/3 complex subunit 3 is a protein that in humans is encoded by the ARPC3 gene.[1][2][3]
This gene encodes one of seven subunits of the 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 p21 subunit, has yet to be determined.[3]
References
- ↑ "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. Aug 1997. doi:10.1083/jcb.138.2.375. PMID 9230079.
- ↑ "Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins". Biochem J 328 (1): 105–12. Jan 1998. doi:10.1042/bj3280105. PMID 9359840.
- ↑ 3.0 3.1 "Entrez Gene: ARPC3 actin related protein 2/3 complex, subunit 3, 21kDa". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10094.
Further reading
- "Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes.". Nature 385 (6613): 265–9. 1997. doi:10.1038/385265a0. PMID 9000076.
- "Interaction of WASP/Scar proteins with actin and vertebrate Arp2/3 complex.". Nat. Cell Biol. 3 (1): 76–82. 2001. doi:10.1038/35050590. PMID 11146629.
- "Interactions among subunits of human Arp2/3 complex: p20-Arc as the hub.". Biochem. Biophys. Res. Commun. 280 (2): 513–7. 2001. doi:10.1006/bbrc.2000.4151. PMID 11162547.
- "Crystal structure of Arp2/3 complex.". Science 294 (5547): 1679–84. 2001. doi:10.1126/science.1066333. PMID 11721045.
- "Reconstitution of human Arp2/3 complex reveals critical roles of individual subunits in complex structure and activity.". Mol. Cell 8 (5): 1041–52. 2002. doi:10.1016/S1097-2765(01)00393-8. PMID 11741539.
- "Directed proteomic analysis of the human nucleolus.". Curr. Biol. 12 (1): 1–11. 2002. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298.
- "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. 2003. doi:10.1073/pnas.242603899. PMID 12477932.
- "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.". Nat. Biotechnol. 21 (5): 566–9. 2004. doi:10.1038/nbt810. PMID 12665801.
- "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. 2004. doi:10.1101/gr.2596504. PMID 15489334.
- "Nucleolar proteome dynamics.". Nature 433 (7021): 77–83. 2005. doi:10.1038/nature03207. PMID 15635413.
- "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. 2005. doi:10.1038/ncb1244. PMID 15793564.
- "A human protein-protein interaction network: a resource for annotating the proteome.". Cell 122 (6): 957–68. 2005. doi:10.1016/j.cell.2005.08.029. PMID 16169070.
- "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3 (1): 89. 2007. doi:10.1038/msb4100134. PMID 17353931.
External links
- ARPC3 human gene location in the UCSC Genome Browser.
- ARPC3 human gene details in the UCSC Genome Browser.