Actin-related protein 2/3 complex subunit 1B

Details

Name
Actin-related protein 2/3 complex subunit 1B
Synonyms
  • ARC41
  • Arp2/3 complex 41 kDa subunit
  • p41-ARC
Gene Name
ARPC1B
Organism
Humans
Amino acid sequence
>lcl|BSEQ0017382|Actin-related protein 2/3 complex subunit 1B
MAYHSFLVEPISCHAWNKDRTQIAICPNNHEVHIYEKSGAKWTKVHELKEHNGQVTGIDW
APESNRIVTCGTDRNAYVWTLKGRTWKPTLVILRINRAARCVRWAPNENKFAVGSGSRVI
SICYFEQENDWWVCKHIKKPIRSTVLSLDWHPNNVLLAAGSCDFKCRIFSAYIKEVEERP
APTPWGSKMPFGELMFESSSSCGWVHGVCFSASGSRVAWVSHDSTVCLADADKKMAVATL
ASETLPLLALTFITDNSLVAAGHDCFPVLFTYDAAAGMLSFGGRLDVPKQSSQRGLTARE
RFQNLDKKASSEGGTAAGAGLDSLHKNSVSQISVLSGGKAKCSQFCTTGMDGGMSIWDVK
SLESALKDLKIK
Number of residues
372
Molecular Weight
40949.415
Theoretical pI
8.44
GO Classification
Functions
structural constituent of cytoskeleton
Processes
Arp2/3 complex-mediated actin nucleation / axon guidance / ephrin receptor signaling pathway / Fc-gamma receptor signaling pathway involved in phagocytosis / innate immune response / movement of cell or subcellular component / small GTPase mediated signal transduction
Components
actin cytoskeleton / Arp2/3 protein complex / cytosol / extracellular exosome / focal adhesion
General Function
Structural constituent of cytoskeleton
Specific Function
Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0017383|Actin-related protein 2/3 complex subunit 1B (ARPC1B)
ATGGCCTACCACAGCTTCCTGGTGGAGCCCATCAGCTGCCACGCCTGGAACAAGGACCGC
ACCCAGATTGCCATCTGCCCCAACAACCATGAGGTGCATATCTATGAAAAGAGCGGTGCC
AAATGGACCAAGGTGCACGAGCTCAAGGAGCACAACGGGCAGGTGACAGGCATCGACTGG
GCCCCCGAGAGTAACCGTATTGTGACCTGCGGCACAGACCGCAACGCCTACGTGTGGACG
CTGAAGGGCCGCACATGGAAGCCCACGCTGGTCATCCTGCGGATCAACCGGGCTGCCCGC
TGCGTGCGCTGGGCCCCCAACGAGAACAAGTTTGCTGTGGGCAGCGGCTCTCGTGTGATC
TCCATCTGTTATTTCGAGCAGGAGAATGACTGGTGGGTTTGCAAGCACATCAAGAAGCCC
ATCCGCTCCACCGTCCTCAGCCTGGACTGGCACCCCAACAATGTGCTGCTGGCTGCCGGC
TCCTGTGACTTCAAGTGTCGGATCTTTTCAGCCTACATCAAGGAGGTGGAGGAACGGCCG
GCACCCACCCCGTGGGGCTCCAAGATGCCCTTTGGGGAACTGATGTTCGAATCCAGCAGT
AGCTGCGGCTGGGTACATGGCGTCTGTTTCTCAGCCAGCGGGAGCCGCGTGGCCTGGGTA
AGCCACGACAGCACCGTCTGCCTGGCTGATGCCGACAAGAAGATGGCCGTCGCGACTCTG
GCCTCTGAAACACTACCACTGCTGGCGCTGACCTTCATCACAGACAACAGCCTGGTGGCA
GCGGGCCACGACTGCTTCCCGGTGCTGTTCACCTATGACGCCGCCGCGGGGATGCTGAGC
TTCGGCGGGCGGCTGGACGTTCCTAAGCAGAGCTCGCAGCGTGGCTTGACGGCCCGCGAG
CGCTTCCAGAACCTGGACAAGAAGGCGAGCTCCGAGGGTGGCACGGCTGCGGGCGCGGGC
CTAGACTCGCTGCACAAGAACAGCGTCAGCCAGATCTCGGTGCTCAGCGGCGGCAAGGCC
AAGTGCTCGCAGTTCTGCACCACTGGCATGGATGGCGGCATGAGTATCTGGGATGTGAAG
AGCTTGGAGTCAGCCTTGAAGGACCTCAAGATCAAATGA
Chromosome Location
7
Locus
7q22.1
External Identifiers
ResourceLink
UniProtKB IDO15143
UniProtKB Entry NameARC1B_HUMAN
GenBank Protein ID2282034
GenBank Gene IDAF006084
HGNC IDHGNC:704
General References
  1. 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]
  2. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [Article]
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  4. 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]
  5. 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]
  6. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [Article]
  7. 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]
  8. 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]
  9. Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal. 2010 Jan 12;3(104):ra3. doi: 10.1126/scisignal.2000475. [Article]
  10. 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]
  11. Rigbolt KT, Prokhorova TA, Akimov V, Henningsen J, Johansen PT, Kratchmarova I, Kassem M, Mann M, Olsen JV, Blagoev B: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Sci Signal. 2011 Mar 15;4(164):rs3. doi: 10.1126/scisignal.2001570. [Article]
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB08235N-[2-(2-methyl-1H-indol-3-yl)ethyl]thiophene-2-carboxamideexperimentalunknownDetails
DB08236(2S)-2-(3-bromophenyl)-3-(5-chloro-2-hydroxyphenyl)-1,3-thiazolidin-4-oneexperimentalunknownDetails