ID ARP3_HUMAN Reviewed; 418 AA. AC P61158; P32391; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 05-OCT-2010, entry version 78. DE RecName: Full=Actin-related protein 3; DE AltName: Full=Actin-like protein 3; GN Name=ACTR3; Synonyms=ARP3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN THE ARP2/2 COMPLEX, AND RP SUBCELLULAR LOCATION. RX MEDLINE=97375667; PubMed=9230079; DOI=10.1083/jcb.138.2.375; RA Welch M.D., Depace A.H., Verma S., Iwamatsu A., Mitchison T.J.; RT "The human Arp2/3 complex is composed of evolutionarily conserved RT subunits and is localized to cellular regions of dynamic actin RT filament assembly."; RL J. Cell Biol. 138:375-384(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Szelei J., Soto A.M., Geck P., Desronvil M., Prechtl N., Weill B., RA Sonnenschein C.; RT "Identification of human estrogen-inducible transcripts from a serum RT resistant variant of breast cancer MCF7 cells."; RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE, FUNCTION OF THE ARP2/3 COMPLEX, IDENTIFICATION IN RP THE ARP2/3 COMPLEX, AND SUBCELLULAR LOCATION. RX PubMed=9000076; DOI=10.1038/385265a0; RA Welch M.D., Iwamatsu A., Mitchison T.J.; RT "Actin polymerization is induced by Arp2/3 protein complex at the RT surface of Listeria monocytogenes."; RL Nature 385:265-269(1997). RN [5] RP PROTEIN SEQUENCE OF 2-17, CLEAVAGE OF INITIATOR METHIONINE, RP ACETYLATION AT ALA-2, AND MASS SPECTROMETRY. RC TISSUE=T-cell; RA Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.; RL Submitted (MAY-2006) to UniProtKB. RN [6] RP PROTEIN SEQUENCE OF 103-123 AND 199-209, AND MASS SPECTROMETRY. RC TISSUE=Brain, and Cajal-Retzius cell; RA Lubec G., Afjehi-Sadat L.; RL Submitted (MAR-2007) to UniProtKB. RN [7] RP RECONSTITUTION OF THE ARP2/3 COMPLEX. RX PubMed=11741539; DOI=10.1016/S1097-2765(01)00393-8; RA Gournier H., Goley E.D., Niederstrasser H., Trinh T., Welch M.D.; RT "Reconstitution of human Arp2/3 complex reveals critical roles of RT individual subunits in complex structure and activity."; RL Mol. Cell 8:1041-1052(2001). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-231, AND MASS RP SPECTROMETRY. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer RT cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-16; TYR-202 AND TYR-231, RP AND MASS SPECTROMETRY. RC TISSUE=Lung carcinoma; RX PubMed=18083107; DOI=10.1016/j.cell.2007.11.025; RA Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., RA Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., RA Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., RA Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., RA Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; RT "Global survey of phosphotyrosine signaling identifies oncogenic RT kinases in lung cancer."; RL Cell 131:1190-1203(2007). RN [10] RP INTERACTION WITH WHDC1. RX PubMed=18614018; DOI=10.1016/j.cell.2008.05.032; RA Campellone K.G., Webb N.J., Znameroski E.A., Welch M.D.; RT "WHAMM is an Arp2/3 complex activator that binds microtubules and RT functions in ER to Golgi transport."; RL Cell 134:148-161(2008). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY. RC TISSUE=Embryonic kidney; RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-240; LYS-244; LYS-251 AND RP LYS-254, AND MASS SPECTROMETRY. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). CC -!- FUNCTION: Functions as ATP-binding component of the Arp2/3 complex CC which is involved in regulation of actin polymerization and CC together with an activating nucleation-promoting factor (NPF) CC mediates the formation of branched actin networks. Seems to CC contact the pointed end of the daughter actin filament. CC -!- SUBUNIT: Component of the Arp2/3 complex composed of ARP2, ARP3, CC ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC and CC ARPC5/p16-ARC. Interacts with WHDC1. CC -!- INTERACTION: CC O60739:EIF1B; NbExp=1; IntAct=EBI-351428, EBI-1043343; CC P17535:JUND; NbExp=1; IntAct=EBI-351428, EBI-2682803; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection. CC -!- SIMILARITY: Belongs to the actin family. ARP3 subfamily. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF006083; AAB64188.1; -; mRNA. DR EMBL; AF127773; AAD51904.1; -; mRNA. DR EMBL; BC044590; AAH44590.1; -; mRNA. DR IPI; IPI00028091; -. DR RefSeq; NP_005712.1; -. DR UniGene; Hs.433512; -. DR ProteinModelPortal; P61158; -. DR SMR; P61158; 3-417. DR DIP; DIP-33140N; -. DR IntAct; P61158; 11. DR STRING; P61158; -. DR PhosphoSite; P61158; -. DR OGP; P32391; -. DR PeptideAtlas; P61158; -. DR PRIDE; P61158; -. DR Ensembl; ENST00000263238; ENSP00000263238; ENSG00000115091. DR GeneID; 10096; -. DR KEGG; hsa:10096; -. DR UCSC; uc002tkx.1; human. DR CTD; 10096; -. DR GeneCards; GC02P114647; -. DR H-InvDB; HIX0017317; -. DR HGNC; HGNC:170; ACTR3. DR HPA; CAB005085; -. DR MIM; 604222; gene. DR PharmGKB; PA24489; -. DR eggNOG; prNOG12759; -. DR HOGENOM; HBG559892; -. DR HOVERGEN; HBG003771; -. DR InParanoid; P61158; -. DR OMA; KYPIRHG; -. DR PhylomeDB; P61158; -. DR NextBio; 38185; -. DR PMAP-CutDB; P61158; -. DR ArrayExpress; P61158; -. DR Bgee; P61158; -. DR CleanEx; HS_ACTR3; -. DR Genevestigator; P61158; -. DR GermOnline; ENSG00000115091; Homo sapiens. DR GO; GO:0005885; C:Arp2/3 protein complex; TAS:UniProtKB. DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0006928; P:cellular component movement; TAS:UniProtKB. DR InterPro; IPR004000; Actin-like. DR InterPro; IPR020902; Actin/actin-like_CS. DR InterPro; IPR015623; Arp3. DR PANTHER; PTHR11937; Actin_like; 1. DR PANTHER; PTHR11937:SF31; Arp3; 1. DR Pfam; PF00022; Actin; 1. DR SMART; SM00268; ACTIN; 1. DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. PE 1: Evidence at protein level; KW Acetylation; Actin-binding; ATP-binding; Cell projection; KW Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; KW Nucleotide-binding; Phosphoprotein. FT INIT_MET 1 1 Removed. FT CHAIN 2 418 Actin-related protein 3. FT /FTId=PRO_0000089079. FT MOD_RES 2 2 N-acetylalanine. FT MOD_RES 16 16 Phosphotyrosine. FT MOD_RES 202 202 Phosphotyrosine. FT MOD_RES 231 231 Phosphotyrosine. FT MOD_RES 240 240 N6-acetyllysine. FT MOD_RES 244 244 N6-acetyllysine. FT MOD_RES 251 251 N6-acetyllysine. FT MOD_RES 254 254 N6-acetyllysine. FT MOD_RES 418 418 Phosphoserine (By similarity). SQ SEQUENCE 418 AA; 47371 MW; 23E5564198B81C63 CRC64; MAGRLPACVV DCGTGYTKLG YAGNTEPQFI IPSCIAIKES AKVGDQAQRR VMKGVDDLDF FIGDEAIEKP TYATKWPIRH GIVEDWDLME RFMEQVIFKY LRAEPEDHYF LLTEPPLNTP ENREYTAEIM FESFNVPGLY IAVQAVLALA ASWTSRQVGE RTLTGTVIDS GDGVTHVIPV AEGYVIGSCI KHIPIAGRDI TYFIQQLLRD REVGIPPEQS LETAKAVKER YSYVCPDLVK EFNKYDTDGS KWIKQYTGIN AISKKEFSID VGYERFLGPE IFFHPEFANP DFTQPISEVV DEVIQNCPID VRRPLYKNIV LSGGSTMFRD FGRRLQRDLK RTVDARLKLS EELSGGRLKP KPIDVQVITH HMQRYAVWFG GSMLASTPEF YQVCHTKKDY EEIGPSICRH NPVFGVMS //