Actin-related protein 2/3 complex subunit 3
Details
- Name
- Actin-related protein 2/3 complex subunit 3
- Kind
- protein
- Synonyms
- ARC21
- Arp2/3 complex 21 kDa subunit
- p21-ARC
- Gene Name
- ARPC3
- UniProtKB Entry
- O15145Swiss-Prot
- Organism
- Humans
- NCBI Taxonomy ID
- 9606
- Amino acid sequence
>lcl|BSEQ0017380|Actin-related protein 2/3 complex subunit 3 MPAYHSSLMDPDTKLIGNMALLPIRSQFKGPAPRETKDTDIVDEAIYYFKANVFFKNYEI KNEADRTLIYITLYISECLKKLQKCNSKSQGEKEMYTLGITNFPIPGEPGFPLNAIYAKP ANKQEDEVMRAYLQQLRQETGLRLCEKVFDPQNDKPSKWWTCFVKRQFMNKSLSGPGQ
- Number of residues
- 178
- Molecular Weight
- 20546.505
- Theoretical pI
- 8.83
- GO Classification
- Functionsstructural constituent of cytoskeletonProcessesArp2/3 complex-mediated actin nucleationComponentsactin cytoskeleton / Arp2/3 protein complex / cytosol / extracellular exosome / focal adhesion / lamellipodium / membrane
- General Function
- Component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF) (PubMed:9230079). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (PubMed:9230079). In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA (PubMed:29925947). The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs) (PubMed:29925947)
- Specific Function
- actin binding
- Pfam Domain Function
- P21-Arc (PF04062)
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm, cytoskeleton
- Gene sequence
>lcl|BSEQ0017381|Actin-related protein 2/3 complex subunit 3 (ARPC3) ATGCCGGCTTACCACTCTTCTCTCATGGATCCTGATACCAAACTCATCGGAAACATGGCA CTGTTGCCTATCAGAAGTCAATTCAAAGGACCTGCCCCCAGAGAGACAAAAGATACAGAT ATTGTGGATGAAGCCATCTATTACTTCAAGGCCAATGTCTTCTTCAAAAACTATGAAATT AAGAATGAAGCTGATAGGACCTTGATATATATAACTCTCTACATTTCTGAATGTCTGAAG AAACTGCAAAAGTGCAATTCCAAAAGCCAAGGTGAGAAAGAAATGTATACGCTGGGAATC ACTAATTTTCCCATTCCTGGAGAGCCTGGTTTTCCACTTAACGCAATTTATGCCAAACCT GCAAACAAACAGGAAGATGAAGTGATGAGAGCCTATTTACAACAGCTAAGGCAAGAGACT GGACTGAGACTTTGTGAGAAAGTTTTCGACCCTCAGAATGATAAACCCAGCAAGTGGTGG ACTTGCTTTGTGAAGAGACAGTTCATGAACAAGAGTCTTTCAGGACCTGGACAGTGA
- Chromosome Location
- 12
- Locus
- 12q24.11
- External Identifiers
Resource Link UniProtKB ID O15145 UniProtKB Entry Name ARPC3_HUMAN GenBank Protein ID 2209347 GenBank Gene ID AF004561 GeneCard ID ARPC3 HGNC ID HGNC:706 PDB ID(s) 6UHC, 6YW6, 6YW7, 8P94 KEGG ID hsa:10094 NCBI Gene ID 10094 - General References
- Machesky LM, Reeves E, Wientjes F, Mattheyse FJ, Grogan A, Totty NF, Burlingame AL, Hsuan JJ, Segal AW: Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins. Biochem J. 1997 Nov 15;328 ( Pt 1):105-12. [Article]
- Welch MD, DePace AH, Verma S, Iwamatsu A, Mitchison TJ: 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. 1997 Jul 28;138(2):375-84. [Article]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [Article]
- Gournier H, Goley ED, Niederstrasser H, Trinh T, Welch MD: Reconstitution of human Arp2/3 complex reveals critical roles of individual subunits in complex structure and activity. Mol Cell. 2001 Nov;8(5):1041-52. [Article]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [Article]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [Article]
- Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
- Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
- Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details N-[2-(2-methyl-1H-indol-3-yl)ethyl]thiophene-2-carboxamide experimental unknown target Details (2S)-2-(3-bromophenyl)-3-(5-chloro-2-hydroxyphenyl)-1,3-thiazolidin-4-one experimental unknown target Details