ARP2_HUMAN
ID ARP2_HUMAN Reviewed; 394 AA.
AC P61160; B2RCP5; D6W5F4; E9PF41; O15142; Q96C82;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Actin-related protein 2;
DE AltName: Full=Actin-like protein 2;
GN Name=ACTR2; Synonyms=ARP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX 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 subunits
RT and is localized to cellular regions of dynamic actin filament assembly.";
RL J. Cell Biol. 138:375-384(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Liver;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PARTIAL 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 surface
RT of Listeria monocytogenes.";
RL Nature 385:265-269(1997).
RN [8]
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 [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17220302; DOI=10.1074/jbc.m607596200;
RA Yoo Y., Wu X., Guan J.L.;
RT "A novel role of the actin-nucleating Arp2/3 complex in the regulation of
RT RNA polymerase II-dependent transcription.";
RL J. Biol. Chem. 282:7616-7623(2007).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-299 AND LYS-322, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
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).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP FUNCTION, AND INTERACTION WITH AVIL.
RX PubMed=29058690; DOI=10.1172/jci94138;
RA Rao J., Ashraf S., Tan W., van der Ven A.T., Gee H.Y., Braun D.A.,
RA Feher K., George S.P., Esmaeilniakooshkghazi A., Choi W.I.,
RA Jobst-Schwan T., Schneider R., Schmidt J.M., Widmeier E., Warejko J.K.,
RA Hermle T., Schapiro D., Lovric S., Shril S., Daga A., Nayir A., Shenoy M.,
RA Tse Y., Bald M., Helmchen U., Mir S., Berdeli A., Kari J.A., El Desoky S.,
RA Soliman N.A., Bagga A., Mane S., Jairajpuri M.A., Lifton R.P., Khurana S.,
RA Martins J.C., Hildebrandt F.;
RT "Advillin acts upstream of phospholipase C 1 in steroid-resistant nephrotic
RT syndrome.";
RL J. Clin. Invest. 127:4257-4269(2017).
RN [15]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=29925947; DOI=10.1038/s41586-018-0237-5;
RA Schrank B.R., Aparicio T., Li Y., Chang W., Chait B.T., Gundersen G.G.,
RA Gottesman M.E., Gautier J.;
RT "Nuclear ARP2/3 drives DNA break clustering for homology-directed repair.";
RL Nature 559:61-66(2018).
CC -!- FUNCTION: ATP-binding component of the Arp2/3 complex, a multiprotein
CC complex that mediates actin polymerization upon stimulation by
CC nucleation-promoting factor (NPF) (PubMed:9000076). The Arp2/3 complex
CC mediates the formation of branched actin networks in the cytoplasm,
CC providing the force for cell motility (PubMed:9000076). Seems to
CC contact the pointed end of the daughter actin filament
CC (PubMed:9000076). In podocytes, required for the formation of
CC lamellipodia downstream of AVIL and PLCE1 regulation (PubMed:29058690).
CC In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3
CC complex also promotes actin polymerization in the nucleus, thereby
CC regulating gene transcription and repair of damaged DNA
CC (PubMed:17220302, PubMed:29925947). The Arp2/3 complex promotes
CC homologous recombination (HR) repair in response to DNA damage by
CC promoting nuclear actin polymerization, leading to drive motility of
CC double-strand breaks (DSBs) (PubMed:29925947).
CC {ECO:0000269|PubMed:17220302, ECO:0000269|PubMed:29058690,
CC ECO:0000269|PubMed:29925947, ECO:0000269|PubMed:9000076}.
CC -!- SUBUNIT: Component of the Arp2/3 complex composed of ACTR2/ARP2,
CC ACTR3/ARP3, ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC
CC and ARPC5/p16-ARC. Interacts with AVIL (PubMed:29058690).
CC {ECO:0000269|PubMed:11741539, ECO:0000269|PubMed:29058690,
CC ECO:0000269|PubMed:9000076}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:9000076}. Cell projection
CC {ECO:0000269|PubMed:9000076}. Nucleus {ECO:0000269|PubMed:17220302,
CC ECO:0000269|PubMed:29925947}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P61160-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P61160-2; Sequence=VSP_046178;
CC -!- SIMILARITY: Belongs to the actin family. ARP2 subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=On mar and motion - Issue
CC 208 of November 2018;
CC URL="https://web.expasy.org/spotlight/back_issues/208/";
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DR EMBL; AF006082; AAB64187.1; -; mRNA.
DR EMBL; AK315205; BAG37642.1; -; mRNA.
DR EMBL; BX649080; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC007318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471053; EAW99908.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99910.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99912.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99913.1; -; Genomic_DNA.
DR EMBL; BC014546; AAH14546.1; -; mRNA.
DR CCDS; CCDS1881.1; -. [P61160-1]
DR CCDS; CCDS46307.1; -. [P61160-2]
DR RefSeq; NP_001005386.1; NM_001005386.2. [P61160-2]
DR RefSeq; NP_005713.1; NM_005722.3. [P61160-1]
DR PDB; 6UHC; EM; 3.90 A; B=1-394.
DR PDB; 6YW6; EM; 4.20 A; B=1-394.
DR PDB; 6YW7; EM; 4.50 A; B=1-394.
DR PDBsum; 6UHC; -.
DR PDBsum; 6YW6; -.
DR PDBsum; 6YW7; -.
DR AlphaFoldDB; P61160; -.
DR SMR; P61160; -.
DR BioGRID; 115404; 231.
DR CORUM; P61160; -.
DR DIP; DIP-33165N; -.
DR IntAct; P61160; 103.
DR MINT; P61160; -.
DR STRING; 9606.ENSP00000367220; -.
DR BindingDB; P61160; -.
DR ChEMBL; CHEMBL6090; -.
DR DrugBank; DB08236; (2S)-2-(3-bromophenyl)-3-(5-chloro-2-hydroxyphenyl)-1,3-thiazolidin-4-one.
DR DrugBank; DB08235; N-[2-(2-methyl-1H-indol-3-yl)ethyl]thiophene-2-carboxamide.
DR iPTMnet; P61160; -.
DR MetOSite; P61160; -.
DR PhosphoSitePlus; P61160; -.
DR SwissPalm; P61160; -.
DR BioMuta; ACTR2; -.
DR DMDM; 47117648; -.
DR SWISS-2DPAGE; P61160; -.
DR EPD; P61160; -.
DR jPOST; P61160; -.
DR MassIVE; P61160; -.
DR MaxQB; P61160; -.
DR PaxDb; P61160; -.
DR PeptideAtlas; P61160; -.
DR PRIDE; P61160; -.
DR ProteomicsDB; 20021; -.
DR ProteomicsDB; 57269; -. [P61160-1]
DR Antibodypedia; 3912; 301 antibodies from 36 providers.
DR DNASU; 10097; -.
DR Ensembl; ENST00000260641.10; ENSP00000260641.5; ENSG00000138071.15. [P61160-1]
DR Ensembl; ENST00000377982.8; ENSP00000367220.4; ENSG00000138071.15. [P61160-2]
DR GeneID; 10097; -.
DR KEGG; hsa:10097; -.
DR MANE-Select; ENST00000260641.10; ENSP00000260641.5; NM_005722.4; NP_005713.1.
DR UCSC; uc002sdp.4; human. [P61160-1]
DR CTD; 10097; -.
DR DisGeNET; 10097; -.
DR GeneCards; ACTR2; -.
DR HGNC; HGNC:169; ACTR2.
DR HPA; ENSG00000138071; Low tissue specificity.
DR MIM; 604221; gene.
DR neXtProt; NX_P61160; -.
DR OpenTargets; ENSG00000138071; -.
DR PharmGKB; PA24488; -.
DR VEuPathDB; HostDB:ENSG00000138071; -.
DR eggNOG; KOG0677; Eukaryota.
DR GeneTree; ENSGT00940000154556; -.
DR InParanoid; P61160; -.
DR OMA; WEDMQHL; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; P61160; -.
DR TreeFam; TF300467; -.
DR PathwayCommons; P61160; -.
DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-HSA-3928662; EPHB-mediated forward signaling.
DR Reactome; R-HSA-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR SignaLink; P61160; -.
DR SIGNOR; P61160; -.
DR BioGRID-ORCS; 10097; 759 hits in 1023 CRISPR screens.
DR ChiTaRS; ACTR2; human.
DR GeneWiki; ACTR2; -.
DR GenomeRNAi; 10097; -.
DR Pharos; P61160; Tchem.
DR PRO; PR:P61160; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P61160; protein.
DR Bgee; ENSG00000138071; Expressed in monocyte and 214 other tissues.
DR ExpressionAtlas; P61160; baseline and differential.
DR Genevisible; P61160; HS.
DR GO; GO:0030478; C:actin cap; IEA:Ensembl.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:UniProtKB.
DR GO; GO:0005885; C:Arp2/3 protein complex; IDA:UniProtKB.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0061825; C:podosome core; IEA:Ensembl.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:FlyBase.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IDA:UniProtKB.
DR GO; GO:0008306; P:associative learning; IEA:Ensembl.
DR GO; GO:0008356; P:asymmetric cell division; IEA:Ensembl.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
DR GO; GO:0035984; P:cellular response to trichostatin A; IEA:Ensembl.
DR GO; GO:0060271; P:cilium assembly; IMP:MGI.
DR GO; GO:0016482; P:cytosolic transport; IEA:Ensembl.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IEA:Ensembl.
DR GO; GO:0016344; P:meiotic chromosome movement towards spindle pole; IEA:Ensembl.
DR GO; GO:0033206; P:meiotic cytokinesis; IEA:Ensembl.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IEA:Ensembl.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IDA:UniProtKB.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl.
DR GO; GO:0051653; P:spindle localization; IEA:Ensembl.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR PRINTS; PR00190; ACTIN.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Alternative splicing;
KW ATP-binding; Cell projection; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..394
FT /note="Actin-related protein 2"
FT /id="PRO_0000089067"
FT BINDING 160..162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A7MB62"
FT BINDING 214..218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A7MB62"
FT BINDING 305..310
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A7MB62"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:25944712"
FT MOD_RES 299
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 322
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 53
FT /note="K -> KNNKKM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_046178"
FT CONFLICT 67
FT /note="M -> T (in Ref. 6; AAH14546)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="G -> S (in Ref. 6; AAH14546)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 394 AA; 44761 MW; 1BFA6B442ED1A797 CRC64;
MDSQGRKVVV CDNGTGFVKC GYAGSNFPEH IFPALVGRPI IRSTTKVGNI EIKDLMVGDE
ASELRSMLEV NYPMENGIVR NWDDMKHLWD YTFGPEKLNI DTRNCKILLT EPPMNPTKNR
EKIVEVMFET YQFSGVYVAI QAVLTLYAQG LLTGVVVDSG DGVTHICPVY EGFSLPHLTR
RLDIAGRDIT RYLIKLLLLR GYAFNHSADF ETVRMIKEKL CYVGYNIEQE QKLALETTVL
VESYTLPDGR IIKVGGERFE APEALFQPHL INVEGVGVAE LLFNTIQAAD IDTRSEFYKH
IVLSGGSTMY PGLPSRLERE LKQLYLERVL KGDVEKLSKF KIRIEDPPRR KHMVFLGGAV
LADIMKDKDN FWMTRQEYQE KGVRVLEKLG VTVR
