ID ACTB_HUMAN Reviewed; 375 AA. AC P60709; P02570; P70514; P99021; Q11211; Q64316; Q75MN2; Q96B34; Q96HG5; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1988, sequence version 1. DT 04-NOV-2026, entry version 220. DE RecName: Full=Actin, cytoplasmic 1; DE EC=3.6.4.- {ECO:0000250|UniProtKB:P68137}; DE AltName: Full=Beta-actin; DE Contains: DE RecName: Full=Actin, cytoplasmic 1, N-terminally processed; GN Name=ACTB; 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]. RX PubMed=6322116; DOI=10.1093/nar/12.3.1687; RA Ponte P., Ng S.Y., Engel J., Gunning P., Kedes L.; RT "Evolutionary conservation in the untranslated regions of actin mRNAs: DNA RT sequence of a human beta-actin cDNA."; RL Nucleic Acids Res. 12:1687-1696(1984). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2994062; DOI=10.1073/pnas.82.18.6133; RA Nakajima-Iijima S., Hamada H., Reddy P., Kakunaga T.; RT "Molecular structure of the human cytoplasmic beta-actin gene: interspecies RT homology of sequences in the introns."; RL Proc. Natl. Acad. Sci. U.S.A. 82:6133-6137(1985). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1734024; DOI=10.1083/jcb.116.4.933; RA Ohmori H., Toyama S., Toyama S.; RT "Direct proof that the primary site of action of cytochalasin on cell RT motility processes is actin."; RL J. Cell Biol. 116:933-941(1992). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NIEHS SNPs program; RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, Eye, Kidney, Muscle, Pancreas, Placenta, and Skin; 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 PROTEIN SEQUENCE OF 2-28. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [8] RP PROTEIN SEQUENCE OF 2-18; 29-37; 40-50; 85-95; 148-177; 184-191; 197-206; RP 292-312 AND 316-326, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT RP ASP-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V.; RL Submitted (JUN-2005) to UniProtKB. RN [9] RP PROTEIN SEQUENCE OF 19-62; 85-113; 184-191; 197-206; 216-254; 291-312; RP 316-326 AND 360-372, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 252-375. RX PubMed=6842590; DOI=10.1016/0022-2836(83)90117-1; RA Hanukoglu I., Tanese N., Fuchs E.; RT "Complementary DNA sequence of a human cytoplasmic actin. Interspecies RT divergence of 3' non-coding regions."; RL J. Mol. Biol. 163:673-678(1983). RN [11] RP SUBCELLULAR LOCATION, AND INTERACTION WITH DHX9. RX PubMed=11687588; DOI=10.1074/jbc.m109393200; RA Zhang S., Buder K., Burkhardt C., Schlott B., Goerlach M., Grosse F.; RT "Nuclear DNA helicase II/RNA helicase A binds to filamentous actin."; RL J. Biol. Chem. 277:843-853(2002). RN [12] RP IDENTIFICATION IN A COMPLEX WITH RAN; XPO6 AND PFN1, AND INTERACTION WITH RP XPO6. RX PubMed=14592989; DOI=10.1093/emboj/cdg565; RA Stueven T., Hartmann E., Goerlich D.; RT "Exportin 6: a novel nuclear export receptor that is specific for RT profilin.actin complexes."; RL EMBO J. 22:5928-5940(2003). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [14] RP INTERACTION WITH EMD. RX PubMed=15328537; DOI=10.1371/journal.pbio.0020231; RA Holaska J.M., Kowalski A.K., Wilson K.L.; RT "Emerin caps the pointed end of actin filaments: evidence for an actin RT cortical network at the nuclear inner membrane."; RL PLoS Biol. 2:1354-1362(2004). RN [15] RP ISGYLATION. RX PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132; RA Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., RA Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.; RT "Proteomic identification of proteins conjugated to ISG15 in mouse and RT human cells."; RL Biochem. Biophys. Res. Commun. 336:496-506(2005). RN [16] RP INTERACTION WITH GCSAM. RX PubMed=17823310; DOI=10.1182/blood-2007-04-087775; RA Lu X., Chen J., Malumbres R., Cubedo Gil E., Helfman D.M., Lossos I.S.; RT "HGAL, a lymphoma prognostic biomarker, interacts with the cytoskeleton and RT mediates the effects of IL-6 on cell migration."; RL Blood 110:4268-4277(2007). RN [17] RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS RP SPECTROMETRY, AND SUBCELLULAR LOCATION. RX PubMed=17289661; DOI=10.1074/mcp.m600346-mcp200; RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., RA Johnsen A.H., Christiansen J., Nielsen F.C.; RT "Molecular composition of IMP1 ribonucleoprotein granules."; RL Mol. Cell. Proteomics 6:798-811(2007). RN [18] RP IDENTIFICATION IN THE BAF COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=18765789; DOI=10.1101/gad.471408; RA Lange M., Kaynak B., Forster U.B., Toenjes M., Fischer J.J., Grimm C., RA Schlesinger J., Just S., Dunkel I., Krueger T., Mebus S., Lehrach H., RA Lurz R., Gobom J., Rottbauer W., Abdelilah-Seyfried S., Sperling S.; RT "Regulation of muscle development by DPF3, a novel histone acetylation and RT methylation reader of the BAF chromatin remodeling complex."; RL Genes Dev. 22:2370-2384(2008). RN [19] RP CROSS-LINK BETWEEN LYS-50 AND GLU-270 BY V.CHOLERAE TOXIN RTXA (MICROBIAL RP INFECTION). RX PubMed=19015515; DOI=10.1073/pnas.0808082105; RA Kudryashov D.S., Durer Z.A., Ytterberg A.J., Sawaya M.R., Pashkov I., RA Prochazkova K., Yeates T.O., Loo R.R., Loo J.A., Satchell K.J., Reisler E.; RT "Connecting actin monomers by iso-peptide bond is a toxicity mechanism of RT the Vibrio cholerae MARTX toxin."; RL Proc. Natl. Acad. Sci. U.S.A. 105:18537-18542(2008). RN [20] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ASP-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [21] RP RETRACTED PAPER. RX PubMed=19377461; DOI=10.1038/nature07954; RA Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G., RA Kitagawa H., Kato S.; RT "GlcNAcylation of a histone methyltransferase in retinoic-acid-induced RT granulopoiesis."; RL Nature 459:455-459(2009). RN [22] RP RETRACTION NOTICE OF PUBMED:19377461. RX PubMed=24336203; DOI=10.1038/nature12896; RA Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G., RA Kitagawa H., Kato S.; RL Nature 505:574-574(2014). RN [23] RP INTERACTION WITH FAM107A. RX PubMed=21969592; DOI=10.1073/pnas.1103318108; RA Schmidt M.V., Schuelke J.P., Liebl C., Stiess M., Avrabos C., Bock J., RA Wochnik G.M., Davies H.A., Zimmermann N., Scharf S.H., Truembach D., RA Wurst W., Zieglgaensberger W., Turck C., Holsboer F., Stewart M.G., RA Bradke F., Eder M., Mueller M.B., Rein T.; RT "Tumor suppressor down-regulated in renal cell carcinoma 1 (DRR1) is a RT stress-induced actin bundling factor that modulates synaptic efficacy and RT cognition."; RL Proc. Natl. Acad. Sci. U.S.A. 108:17213-17218(2011). RN [24] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ASP-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [25] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND ASP-2, CLEAVAGE OF RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [26] RP INTERACTION WITH ERBB2. RX PubMed=21555369; DOI=10.1158/0008-5472.can-10-3504; RA Li L.Y., Chen H., Hsieh Y.H., Wang Y.N., Chu H.J., Chen Y.H., Chen H.Y., RA Chien P.J., Ma H.T., Tsai H.C., Lai C.C., Sher Y.P., Lien H.C., Tsai C.H., RA Hung M.C.; RT "Nuclear ErbB2 enhances translation and cell growth by activating RT transcription of ribosomal RNA genes."; RL Cancer Res. 71:4269-4279(2011). RN [27] RP METHYLATION AT LYS-84, AND DEMETHYLATION BY ALKBH4. RX PubMed=23673617; DOI=10.1038/ncomms2863; RA Li M.M., Nilsen A., Shi Y., Fusser M., Ding Y.H., Fu Y., Liu B., Niu Y., RA Wu Y.S., Huang C.M., Olofsson M., Jin K.X., Lv Y., Xu X.Z., He C., RA Dong M.Q., Rendtlew Danielsen J.M., Klungland A., Yang Y.G.; RT "ALKBH4-dependent demethylation of actin regulates actomyosin dynamics."; RL Nat. Commun. 4:1832-1832(2013). RN [28] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ASP-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [29] RP CROSS-LINK BY V.CHOLERAE TOXIN RTXA (MICROBIAL INFECTION). RX PubMed=26228148; DOI=10.1126/science.aab4090; RA Heisler D.B., Kudryashova E., Grinevich D.O., Suarez C., Winkelman J.D., RA Birukov K.G., Kotha S.R., Parinandi N.L., Vavylonis D., Kovar D.R., RA Kudryashov D.S.; RT "ACD toxin-produced actin oligomers poison formin-controlled actin RT polymerization."; RL Science 349:535-539(2015). RN [30] RP INTERACTION WITH FAM107A. RX PubMed=28604741; DOI=10.1038/onc.2017.181; RA Mu P., Akashi T., Lu F., Kishida S., Kadomatsu K.; RT "A novel nuclear complex of DRR1, F-actin and COMMD1 involved in NF-kappaB RT degradation and cell growth suppression in neuroblastoma."; RL Oncogene 36:5745-5756(2017). RN [31] RP ACETYLATION AT ASP-2. RX PubMed=30028079; DOI=10.1111/febs.14605; RA Wiame E., Tahay G., Tyteca D., Vertommen D., Stroobant V., Bommer G.T., RA Van Schaftingen E.; RT "NAT6 acetylates the N-terminus of different forms of actin."; RL FEBS J. 285:3299-3316(2018). RN [32] 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). RN [33] RP FUNCTION, AND ACETYLATION AT ASP-2. RX PubMed=29581253; DOI=10.1073/pnas.1718336115; RA Drazic A., Aksnes H., Marie M., Boczkowska M., Varland S., Timmerman E., RA Foyn H., Glomnes N., Rebowski G., Impens F., Gevaert K., Dominguez R., RA Arnesen T.; RT "NAA80 is actin's N-terminal acetyltransferase and regulates cytoskeleton RT assembly and cell motility."; RL Proc. Natl. Acad. Sci. U.S.A. 115:4399-4404(2018). RN [34] RP METHYLATION AT HIS-73. RX PubMed=30526847; DOI=10.7554/elife.37921; RA Kwiatkowski S., Seliga A.K., Vertommen D., Terreri M., Ishikawa T., RA Grabowska I., Tiebe M., Teleman A.A., Jagielski A.K., Veiga-da-Cunha M., RA Drozak J.; RT "SETD3 protein is the actin-specific histidine N-methyltransferase."; RL Elife 7:0-0(2018). RN [35] RP OXIDATION AT MET-44 AND MET-47. RX PubMed=29343822; DOI=10.1038/s41598-017-17943-5; RA Wu H., Yesilyurt H.G., Yoon J., Terman J.R.; RT "The MICALs are a Family of F-actin Dismantling Oxidoreductases Conserved RT from Drosophila to Humans."; RL Sci. Rep. 8:937-937(2018). RN [36] RP PROTEOLYTIC CLEAVAGE BY ACTMAP, CLEAVAGE OF INITIATOR METHIONINE, AND RP ACETYLATION AT MET-1. RX PubMed=36173861; DOI=10.1126/science.abq5082; RA Haahr P., Galli R.A., van den Hengel L.G., Bleijerveld O.B., RA Kazokaite-Adomaitiene J., Song J.Y., Kroese L.J., Krimpenfort P., RA Baltissen M.P., Vermeulen M., Ottenheijm C.A.C., Brummelkamp T.R.; RT "Actin maturation requires the ACTMAP/C19orf54 protease."; RL Science 377:1533-1537(2022). RN [37] RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH SETD3, METHYLATION AT HIS-73, AND RP MUTAGENESIS OF TYR-69; ILE-71; HIS-73; ASP-80; ASP-81 AND MET-82. RX PubMed=30785395; DOI=10.7554/elife.43676; RA Guo Q., Liao S., Kwiatkowski S., Tomaka W., Yu H., Wu G., Tu X., Min J., RA Drozak J., Xu C.; RT "Structural insights into SETD3-mediated histidine methylation on beta- RT actin."; RL Elife 8:0-0(2019). RN [38] RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH SETD3, METHYLATION AT HIS-73, AND RP MUTAGENESIS OF ILE-71; GLY-74 AND TRP-79. RX PubMed=30626964; DOI=10.1038/s41586-018-0821-8; RA Wilkinson A.W., Diep J., Dai S., Liu S., Ooi Y.S., Song D., Li T.M., RA Horton J.R., Zhang X., Liu C., Trivedi D.V., Ruppel K.M., RA Vilches-Moure J.G., Casey K.M., Mak J., Cowan T., Elias J.E., RA Nagamine C.M., Spudich J.A., Cheng X., Carette J.E., Gozani O.; RT "SETD3 is an actin histidine methyltransferase that prevents primary RT dystocia."; RL Nature 565:372-376(2019). RN [39] {ECO:0007744|PDB:6OX0, ECO:0007744|PDB:6OX1, ECO:0007744|PDB:6OX2, ECO:0007744|PDB:6OX3, ECO:0007744|PDB:6OX4, ECO:0007744|PDB:6OX5} RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH SETD3, METHYLATION AT HIS-73, AND RP MUTAGENESIS OF HIS-73. RX PubMed=31388018; DOI=10.1038/s41467-019-11554-6; RA Dai S., Horton J.R., Woodcock C.B., Wilkinson A.W., Zhang X., Gozani O., RA Cheng X.; RT "Structural basis for the target specificity of actin histidine RT methyltransferase SETD3."; RL Nat. Commun. 10:3541-3541(2019). RN [40] {ECO:0007744|PDB:6WK1, ECO:0007744|PDB:6WK2} RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH SETD3, AND MUTAGENESIS OF HIS-73. RX PubMed=32503840; DOI=10.1074/jbc.ra120.014072; RA Dai S., Holt M.V., Horton J.R., Woodcock C.B., Patel A., Zhang X., RA Young N.L., Wilkinson A.W., Cheng X.; RT "Characterization of SETD3 methyltransferase-mediated protein methionine RT methylation."; RL J. Biol. Chem. 295:10901-10910(2020). RN [41] {ECO:0007744|PDB:6V62, ECO:0007744|PDB:6V63} RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH SETD3. RX PubMed=31911441; DOI=10.1074/jbc.ra119.012319; RA Dai S., Horton J.R., Wilkinson A.W., Gozani O., Zhang X., Cheng X.; RT "An engineered variant of SETD3 methyltransferase alters target specificity RT from histidine to lysine methylation."; RL J. Biol. Chem. 295:2582-2589(2020). RN [42] {ECO:0007744|PDB:8RX1} RP STRUCTURE BY ELECTRON MICROSCOPY IN COMPLEX WITH MZT1; MZT2A; CDK5RAP2 AND RP THE GAMMA-TUBULIN RING COMPLEX, FUNCTION, AND SUBUNIT. RX PubMed=39321809; DOI=10.1016/j.devcel.2024.09.001; RA Serna M., Zimmermann F., Vineethakumari C., Gonzalez-Rodriguez N., RA Llorca O., Luders J.; RT "CDK5RAP2 activates microtubule nucleator gammaTuRC by facilitating RT template formation and actin release."; RL Dev. Cell 59:3175-3188.e8(2024). RN [43] {ECO:0007744|PDB:8VRD, ECO:0007744|PDB:8VRJ, ECO:0007744|PDB:8VRK} RP STRUCTURE BY ELECTRON MICROSCOPY IN COMPLEXES WITH MZT1; TUBA1B; TUBB3 AND RP THE GAMMA-TUBULIN RING COMPLEX, FUNCTION, AND SUBUNIT. RX PubMed=38609661; DOI=10.1038/s41594-024-01264-z; RA Aher A., Urnavicius L., Xue A., Neselu K., Kapoor T.M.; RT "Structure of the gamma-tubulin ring complex-capped microtubule."; RL Nat. Struct. Mol. Biol. 31:1124-1133(2024). RN [44] RP VARIANT THC8 LYS-364, INVOLVEMENT IN THC8, AND INTERACTION WITH PFN1. RX PubMed=10411937; DOI=10.1073/pnas.96.15.8693; RA Nunoi H., Yamazaki T., Tsuchiya H., Kato S., Malech H.L., Matsuda I., RA Kanegasaki S.; RT "A heterozygous mutation of beta-actin associated with neutrophil RT dysfunction and recurrent infection."; RL Proc. Natl. Acad. Sci. U.S.A. 96:8693-8698(1999). RN [45] RP VARIANT DDS1 TRP-183, AND CHARACTERIZATION OF VARIANT DDS1 TRP-183. RX PubMed=16685646; DOI=10.1086/504271; RA Procaccio V., Salazar G., Ono S., Styers M.L., Gearing M., Davila A., RA Jimenez R., Juncos J., Gutekunst C.-A., Meroni G., Fontanella B., RA Sontag E., Sontag J.-M., Faundez V., Wainer B.H.; RT "A mutation of beta -actin that alters depolymerization dynamics is RT associated with autosomal dominant developmental malformations, deafness, RT and dystonia."; RL Am. J. Hum. Genet. 78:947-960(2006). RN [46] RP VARIANTS BRWS1 ASP-12; VAL-65; CYS-196 AND HIS-196. RX PubMed=22366783; DOI=10.1038/ng.1091; RA Riviere J.B., van Bon B.W., Hoischen A., Kholmanskikh S.S., O'Roak B.J., RA Gilissen C., Gijsen S., Sullivan C.T., Christian S.L., Abdul-Rahman O.A., RA Atkin J.F., Chassaing N., Drouin-Garraud V., Fry A.E., Fryns J.P., RA Gripp K.W., Kempers M., Kleefstra T., Mancini G.M., Nowaczyk M.J., RA van Ravenswaaij-Arts C.M., Roscioli T., Marble M., Rosenfeld J.A., RA Siu V.M., de Vries B.B., Shendure J., Verloes A., Veltman J.A., RA Brunner H.G., Ross M.E., Pilz D.T., Dobyns W.B.; RT "De novo mutations in the actin genes ACTB and ACTG1 cause Baraitser-Winter RT syndrome."; RL Nat. Genet. 44:440-444(2012). RN [47] RP CHARACTERIZATION OF VARIANT DDS1 TRP-183, CHARACTERIZATION OF VARIANT THC8 RP LYS-364, CATALYTIC ACTIVITY, FUNCTION, AND INTERACTION WITH PFN1. RX PubMed=25255767; DOI=10.1111/febs.13068; RA Hundt N., Preller M., Swolski O., Ang A.M., Mannherz H.G., Manstein D.J., RA Mueller M.; RT "Molecular mechanisms of disease-related human beta-actin mutations p.R183W RT and p.E364K."; RL FEBS J. 281:5279-5291(2014). RN [48] RP VARIANT DDS1 TRP-183. RX PubMed=28487785; DOI=10.1155/2017/9184265; RA Conboy E., Vairo F., Waggoner D., Ober C., Das S., Dhamija R., Klee E.W., RA Pichurin P.; RT "Pathogenic Variant in ACTB, p.Arg183Trp, Causes Juvenile-Onset Dystonia, RT Hearing Loss, and Developmental Delay without Midline Malformation."; RL Case Rep. Genet. 2017:9184265-9184265(2017). RN [49] RP VARIANT BNS CYS-147, VARIANT SER-147, AND INVOLVEMENT IN BNS. RX PubMed=28347698; DOI=10.1016/j.jid.2017.03.017; RA Cai E.D., Sun B.K., Chiang A., Rogers A., Bernet L., Cheng B., Teng J., RA Rieger K.E., Sarin K.Y.; RT "Postzygotic Mutations in Beta-Actin Are Associated with Becker's Nevus and RT Becker's Nevus Syndrome."; RL J. Invest. Dermatol. 137:1795-1798(2017). RN [50] RP VARIANT DDS1 TRP-183. RX PubMed=29788902; DOI=10.1186/s11689-018-9235-z; RA Skogseid I.M., Roesby O., Konglund A., Connelly J.P., Nedregaard B., RA Jablonski G.E., Kvernmo N., Stray-Pedersen A., Glover J.C.; RT "Dystonia-deafness syndrome caused by ACTB p.Arg183Trp heterozygosity shows RT striatal dopaminergic dysfunction and response to pallidal stimulation."; RL J. Neurodev. Disord. 10:17-17(2018). RN [51] RP VARIANTS THC8 ARG-313 AND 338-SER--ILE-341 DEL, AND INVOLVEMENT IN THC8. RX PubMed=30315159; DOI=10.1038/s41467-018-06713-0; RA Latham S.L., Ehmke N., Reinke P.Y.A., Taft M.H., Eicke D., Reindl T., RA Stenzel W., Lyons M.J., Friez M.J., Lee J.A., Hecker R., Fruehwald M.C., RA Becker K., Neuhann T.M., Horn D., Schrock E., Niehaus I., Sarnow K., RA Gruetzmann K., Gawehn L., Klink B., Rump A., Chaponnier C., Figueiredo C., RA Knoefler R., Manstein D.J., Di Donato N.; RT "Variants in exons 5 and 6 of ACTB cause syndromic thrombocytopenia."; RL Nat. Commun. 9:4250-4250(2018). RN [52] RP ERRATUM OF PUBMED:30315159. RX PubMed=30451859; DOI=10.1038/s41467-018-07404-6; RA Latham S.L., Ehmke N., Reinke P.Y.A., Taft M.H., Eicke D., Reindl T., RA Stenzel W., Lyons M.J., Friez M.J., Lee J.A., Hecker R., Fruehwald M.C., RA Becker K., Neuhann T.M., Horn D., Schrock E., Niehaus I., Sarnow K., RA Gruetzmann K., Gawehn L., Klink B., Rump A., Chaponnier C., Figueiredo C., RA Knoefler R., Manstein D.J., Di Donato N.; RL Nat. Commun. 9:4930-4930(2018). RN [53] RP VARIANT BRWS1 ALA-70, AND VARIANT THC8 PHE-171. RX PubMed=30733661; DOI=10.1159/000492267; RA Sandestig A., Green A., Jonasson J., Vogt H., Wahlstroem J., Pepler A., RA Ellnebo K., Biskup S., Stefanova M.; RT "Could Dissimilar Phenotypic Effects of ACTB Missense Mutations Reflect the RT Actin Conformational Change? Two Novel Mutations and Literature Review."; RL Mol. Syndromol. 9:259-265(2019). RN [54] RP VARIANTS CSMH ASP-111; HIS-137; ALA-146; VAL-146; ASP-146; SER-146; SER-147 RP AND CYS-147, AND INVOLVEMENT IN CSMH. RX PubMed=32170967; DOI=10.1111/cup.13683; RA Atzmony L., Ugwu N., Zaki T.D., Antaya R.J., Choate K.A.; RT "Post-zygotic ACTB mutations underlie congenital smooth muscle RT hamartomas."; RL J. Cutan. Pathol. 47:681-685(2020). RN [55] RP VARIANT DDS1 TRP-183. RX PubMed=35005077; DOI=10.1002/mdc3.13358; RA Zavala L., Ziegler G., Moron D.G., Garretto N.; RT "Dystonia-Deafness Syndrome: ACTB Pathogenic Variant in an Argentinean RT Family."; RL Mov. Disord. Clin. Pract. 9:122-124(2022). CC -!- FUNCTION: Actin is a highly conserved protein that polymerizes to CC produce filaments that form cross-linked networks in the cytoplasm of CC cells (PubMed:25255767, PubMed:29581253). Actin exists in both CC monomeric (G-actin) and polymeric (F-actin) forms, both forms playing CC key functions, such as cell motility and contraction (PubMed:29581253). CC In addition to their role in the cytoplasmic cytoskeleton, G- and F- CC actin also localize in the nucleus, and regulate gene transcription and CC motility and repair of damaged DNA (PubMed:29925947). Plays a role in CC the assembly of the gamma-tubulin ring complex (gTuRC), which regulates CC the minus-end nucleation of alpha-beta tubulin heterodimers that grow CC into microtubule protafilaments (PubMed:39321809, PubMed:38609661). CC Part of the ACTR1A/ACTB filament around which the dynactin complex is CC built (By similarity). The dynactin multiprotein complex activates the CC molecular motor dynein for ultra-processive transport along CC microtubules (By similarity). {ECO:0000250|UniProtKB:Q6QAQ1, CC ECO:0000269|PubMed:25255767, ECO:0000269|PubMed:29581253, CC ECO:0000269|PubMed:29925947, ECO:0000269|PubMed:38609661, CC ECO:0000269|PubMed:39321809}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:25255767}; CC -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a CC structural filament (F-actin) in the form of a two-stranded helix CC (PubMed:16685646, PubMed:28604741). Each actin can bind to 4 others CC (PubMed:16685646, PubMed:28604741). Identified in a IGF2BP1-dependent CC mRNP granule complex containing untranslated mRNAs (PubMed:17289661). CC Component of the BAF complex, which includes at least actin (ACTB), CC ARID1A, ARID1B/BAF250, SMARCA2, SMARCA4/BRG1, ACTL6A/BAF53, CC ACTL6B/BAF53B, SMARCE1/BAF57 SMARCC1/BAF155, SMARCC2/BAF170, CC SMARCB1/SNF5/INI1, and one or more of SMARCD1/BAF60A, SMARCD2/BAF60B, CC or SMARCD3/BAF60C (PubMed:18765789). In muscle cells, the BAF complex CC also contains DPF3 (PubMed:18765789). Found in a complex with XPO6, CC Ran, ACTB and PFN1 (PubMed:14592989). Interacts with PFN1 CC (PubMed:10411937, PubMed:25255767). Interacts with XPO6 and EMD CC (PubMed:15328537). Interacts with ERBB2 (PubMed:21555369). Interacts CC with GCSAM (PubMed:17823310). Interacts with TBC1D21 (By similarity). CC Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain) (By CC similarity). Interacts with DHX9 (via C-terminus); this interaction is CC direct and mediates the attachment to nuclear ribonucleoprotein CC complexes (PubMed:11687588). Interacts with FAM107A (PubMed:21969592, CC PubMed:28604741). Associates with the gamma-tubulin ring complex CC (gTuRC) consisting of TUBGCP2, TUBGCP3, TUBGCP4, TUBGCP5 and TUBGCP6 CC and gamma-tubulin TUBG1 or TUBG2; within the complex, interacts with CC TUBGCP3 and TUBGCP6 to form a luminal bridge with MZT1 that stabilizes CC the initial structure during complex assembly (PubMed:39321809, CC PubMed:38609661). Part of the ACTR1A/ACTB filament around which the CC dynactin complex is built (By similarity). The filament contains 8 CC copies of ACTR1A and 1 ACTB (By similarity). Interacts with TPRN which CC forms ring-like structures in the stereocilium taper region; the CC interaction may stabilize stereocilia in inner ear hair cells (By CC similarity). Interacts with AMOTL2 (via N-terminus), the interaction CC facilitates binding of cell junction complexes to actin fibers in CC endothelial cells (By similarity). {ECO:0000250|UniProtKB:O18840, CC ECO:0000250|UniProtKB:P60710, ECO:0000250|UniProtKB:Q6QAQ1, CC ECO:0000269|PubMed:10411937, ECO:0000269|PubMed:11687588, CC ECO:0000269|PubMed:14592989, ECO:0000269|PubMed:15328537, CC ECO:0000269|PubMed:16685646, ECO:0000269|PubMed:17289661, CC ECO:0000269|PubMed:17823310, ECO:0000269|PubMed:18765789, CC ECO:0000269|PubMed:21555369, ECO:0000269|PubMed:21969592, CC ECO:0000269|PubMed:25255767, ECO:0000269|PubMed:28604741, CC ECO:0000269|PubMed:38609661, ECO:0000269|PubMed:39321809}. CC -!- INTERACTION: CC P60709; P60709: ACTB; NbExp=16; IntAct=EBI-353944, EBI-353944; CC P60709; P63261: ACTG1; NbExp=16; IntAct=EBI-353944, EBI-351292; CC P60709; P05067: APP; NbExp=8; IntAct=EBI-353944, EBI-77613; CC P60709; Q9UQB8: BAIAP2; NbExp=2; IntAct=EBI-353944, EBI-525456; CC P60709; P40123: CAP2; NbExp=9; IntAct=EBI-353944, EBI-1051165; CC P60709; Q16543: CDC37; NbExp=3; IntAct=EBI-353944, EBI-295634; CC P60709; P23528: CFL1; NbExp=11; IntAct=EBI-353944, EBI-352733; CC P60709; Q549N0: CFL2; NbExp=3; IntAct=EBI-353944, EBI-10201319; CC P60709; Q9Y281: CFL2; NbExp=11; IntAct=EBI-353944, EBI-351218; CC P60709; P13569: CFTR; NbExp=6; IntAct=EBI-353944, EBI-349854; CC P60709; P60981: DSTN; NbExp=10; IntAct=EBI-353944, EBI-745191; CC P60709; Q8WTR2: DUSP19; NbExp=4; IntAct=EBI-353944, EBI-8654968; CC P60709; Q08426: EHHADH; NbExp=4; IntAct=EBI-353944, EBI-2339219; CC P60709; P50402: EMD; NbExp=2; IntAct=EBI-353944, EBI-489887; CC P60709; P04626: ERBB2; NbExp=11; IntAct=EBI-353944, EBI-641062; CC P60709; Q8TCJ0-2: FBXO25; NbExp=3; IntAct=EBI-353944, EBI-6264551; CC P60709; P11142: HSPA8; NbExp=2; IntAct=EBI-353944, EBI-351896; CC P60709; P83110: HTRA3; NbExp=5; IntAct=EBI-353944, EBI-2867394; CC P60709; P42858: HTT; NbExp=3; IntAct=EBI-353944, EBI-466029; CC P60709; O14950: MYL12B; NbExp=3; IntAct=EBI-353944, EBI-1642165; CC P60709; P14598: NCF1; NbExp=3; IntAct=EBI-353944, EBI-395044; CC P60709; P29474: NOS3; NbExp=3; IntAct=EBI-353944, EBI-1391623; CC P60709; Q92636: NSMAF; NbExp=2; IntAct=EBI-353944, EBI-2947053; CC P60709; Q96HA8: NTAQ1; NbExp=6; IntAct=EBI-353944, EBI-741158; CC P60709; P07737: PFN1; NbExp=3; IntAct=EBI-353944, EBI-713780; CC P60709; P78317: RNF4; NbExp=3; IntAct=EBI-353944, EBI-2340927; CC P60709; P37802: TAGLN2; NbExp=3; IntAct=EBI-353944, EBI-1056740; CC P60709; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-353944, EBI-717399; CC P60709; P13693: TPT1; NbExp=4; IntAct=EBI-353944, EBI-1783169; CC P60709; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-353944, EBI-10180829; CC P60709; Q9UBQ0-2: VPS29; NbExp=3; IntAct=EBI-353944, EBI-11141397; CC P60709; O75083: WDR1; NbExp=2; IntAct=EBI-353944, EBI-351917; CC P60709; P63104: YWHAZ; NbExp=3; IntAct=EBI-353944, EBI-347088; CC P60709; P08413: Camk2b; Xeno; NbExp=4; IntAct=EBI-353944, EBI-916155; CC P60709; Q8K4J6: Mrtfa; Xeno; NbExp=3; IntAct=EBI-353944, EBI-8291665; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:11687588, ECO:0000269|PubMed:17289661}. Nucleus CC {ECO:0000269|PubMed:11687588, ECO:0000269|PubMed:29925947}. CC Note=Localized in cytoplasmic mRNP granules containing untranslated CC mRNAs. {ECO:0000269|PubMed:17289661}. CC -!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}. CC -!- PTM: Oxidation of Met-44 and Met-47 by MICALs (MICAL1, MICAL2 or CC MICAL3) to form methionine sulfoxide promotes actin filament CC depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The CC (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promote actin CC repolymerization. {ECO:0000269|PubMed:29343822}. CC -!- PTM: Monomethylation at Lys-84 (K84me1) regulates actin-myosin CC interaction and actomyosin-dependent processes (PubMed:23673617). CC Demethylation by ALKBH4 is required for maintaining actomyosin dynamics CC supporting normal cleavage furrow ingression during cytokinesis and CC cell migration (PubMed:23673617). {ECO:0000269|PubMed:23673617}. CC -!- PTM: Methylated at His-73 by SETD3 (PubMed:30526847, PubMed:30626964, CC PubMed:30785395, PubMed:31388018). Methylation at His-73 is required CC for smooth muscle contraction of the laboring uterus during delivery CC (By similarity). {ECO:0000250|UniProtKB:P60710, CC ECO:0000269|PubMed:30526847, ECO:0000269|PubMed:30626964, CC ECO:0000269|PubMed:30785395, ECO:0000269|PubMed:31388018}. CC -!- PTM: [Actin, cytoplasmic 1]: N-terminal cleavage of acetylated CC methionine of immature cytoplasmic actin by ACTMAP. CC {ECO:0000269|PubMed:36173861}. CC -!- PTM: [Actin, cytoplasmic 1, N-terminally processed]: N-terminal CC acetylation by NAA80 affects actin filament depolymerization and CC elongation, including elongation driven by formins (PubMed:29581253). CC In contrast, filament nucleation by the Arp2/3 complex is not affected CC (PubMed:29581253). {ECO:0000269|PubMed:29581253}. CC -!- PTM: (Microbial infection) Monomeric actin is cross-linked by CC V.cholerae toxins RtxA and VgrG1 in case of infection: bacterial toxins CC mediate the cross-link between Lys-50 of one monomer and Glu-270 of CC another actin monomer, resulting in formation of highly toxic actin CC oligomers that cause cell rounding (PubMed:19015515). The toxin can be CC highly efficient at very low concentrations by acting on formin CC homology family proteins: toxic actin oligomers bind with high affinity CC to formins and adversely affect both nucleation and elongation CC abilities of formins, causing their potent inhibition in both profilin- CC dependent and independent manners (PubMed:26228148). CC {ECO:0000305|PubMed:19015515, ECO:0000305|PubMed:26228148}. CC -!- DISEASE: Dystonia-deafness syndrome 1 (DDS1) [MIM:607371]: An autosomal CC dominant form of dystonia with juvenile onset, associated with CC congenital or childhood-onset sensorineural deafness. Dystonia is CC defined by the presence of sustained involuntary muscle contraction, CC often leading to abnormal postures. Some DDS1 patients have dysmorphic CC features, skeletal anomalies, and/or mild developmental delay with CC impaired intellectual development. {ECO:0000269|PubMed:16685646, CC ECO:0000269|PubMed:25255767, ECO:0000269|PubMed:28487785, CC ECO:0000269|PubMed:29788902, ECO:0000269|PubMed:35005077}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Baraitser-Winter syndrome 1 (BRWS1) [MIM:243310]: A rare CC developmental disorder characterized by the combination of congenital CC ptosis, high-arched eyebrows, hypertelorism, ocular colobomata, and a CC brain malformation consisting of anterior-predominant lissencephaly. CC Other typical features include postnatal short stature and CC microcephaly, intellectual disability, seizures, and hearing loss. CC {ECO:0000269|PubMed:22366783, ECO:0000269|PubMed:30733661}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Thrombocytopenia 8, with dysmorphic features and developmental CC delay (THC8) [MIM:620475]: A form of thrombocytopenia, a hematologic CC disorder defined by a decrease in the number of platelets in CC circulating blood, resulting in the potential for increased bleeding CC and decreased ability for clotting. THC8 is an autosomal dominant form CC characterized by early-childhood onset of thrombocytopenia with CC platelet anisotropy. Affected individuals also have dysmorphic facial CC features and variable developmental delay with speech delay and mildly CC impaired intellectual development. {ECO:0000269|PubMed:10411937, CC ECO:0000269|PubMed:25255767, ECO:0000269|PubMed:30315159, CC ECO:0000269|PubMed:30733661}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Becker nevus syndrome (BNS) [MIM:604919]: A syndrome CC characterized by the association of Becker nevi with musculoskeletal CC abnormalities, unilateral breast hypoplasia, intellectual disability, CC developmental delay, and cardiomyopathy. Becker nevus is a cutaneous CC hamartoma that appears in childhood as a unilateral tan patch and CC increases in thickness, pigmentation, and hair growth during CC adolescence. Histologically, epidermal acanthosis is accompanied by CC irregularly dispersed ectopic smooth muscle bundles and increased CC terminal hair follicles. Most cases are sporadic. CC {ECO:0000269|PubMed:28347698}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Congenital smooth muscle hamartoma, with or without CC hemihypertrophy (CSMH) [MIM:620470]: A benign skin lesion that usually CC presents as an indurated, slightly pigmented or flesh-colored plaque CC with perifollicular papules or coarse hair. Histopathologically, there CC is excessive proliferation of ectopic smooth muscle within the dermis. CC Hair follicles are normal in number and hyperkeratosis, acanthosis and CC hyperpigmentation of the basal cell layer can sometimes be seen. CC Rarely, CSMH is associated with hemihypertrophy. CC {ECO:0000269|PubMed:32170967}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms, alpha, CC beta and gamma have been identified. The alpha actins are found in CC muscle tissues and are a major constituent of the contractile CC apparatus. The beta and gamma actins coexist in most cell types as CC components of the cytoskeleton and as mediators of internal cell CC motility. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}. CC -!- CAUTION: Was originally thought to be part of the MLL5-L complex, at CC least composed of KMT2E, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and CC OGT (PubMed:19377461). However, the corresponding article has been CC retracted (PubMed:24336203). {ECO:0000269|PubMed:19377461, CC ECO:0000269|PubMed:24336203}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/42959/ACTB"; CC -!- WEB RESOURCE: Name=Mendelian genes actin, beta (ACTB); Note=Leiden Open CC Variation Database (LOVD); CC URL="https://databases.lovd.nl/shared/genes/ACTB"; CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=On mar and motion - Issue CC 208 of November 2018; CC URL="https://www.proteinspotlight.org/back_issues/208/"; 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; X00351; CAA25099.1; -; mRNA. DR EMBL; M10277; AAA51567.1; -; Genomic_DNA. DR EMBL; X63432; CAA45026.1; -; mRNA. DR EMBL; AY582799; AAS79319.1; -; Genomic_DNA. DR EMBL; AC006483; AAP22343.1; -; Genomic_DNA. DR EMBL; BC001301; AAH01301.1; -; mRNA. DR EMBL; BC002409; AAH02409.1; -; mRNA. DR EMBL; BC004251; AAH04251.1; -; mRNA. DR EMBL; BC008633; AAH08633.1; -; mRNA. DR EMBL; BC012854; AAH12854.1; -; mRNA. DR EMBL; BC013380; AAH13380.1; -; mRNA. DR EMBL; BC014861; AAH14861.1; -; mRNA. DR EMBL; BC016045; AAH16045.1; -; mRNA. DR EMBL; V00478; CAA23745.1; -; mRNA. DR CCDS; CCDS5341.1; -. DR PIR; A25168; ATHUB. DR RefSeq; NP_001092.1; NM_001101.5. DR PDB; 21VV; EM; 4.70 A; J=1-375. DR PDB; 3BYH; EM; 12.00 A; A=2-375. DR PDB; 3D2U; X-ray; 2.21 A; C/G=170-178. DR PDB; 3J82; EM; 7.70 A; B/C/D=2-375. DR PDB; 3LUE; EM; -; A/B/C/D/E/F/G/H/I/J=2-375. DR PDB; 6ANU; EM; 7.00 A; A/B/C/D/E/F=1-375. DR PDB; 6ICT; X-ray; 1.95 A; E/G/H/I=66-88. DR PDB; 6ICV; X-ray; 2.15 A; C/D=66-88. DR PDB; 6LTJ; EM; 3.70 A; K=1-375. DR PDB; 6MBJ; X-ray; 1.78 A; Y/Z=66-80. DR PDB; 6MBK; X-ray; 1.69 A; Y/Z=66-80. DR PDB; 6MBL; X-ray; 2.20 A; Y=66-80. DR PDB; 6NBW; X-ray; 2.50 A; A=2-375. DR PDB; 6OX0; X-ray; 1.75 A; Y/Z=66-80. DR PDB; 6OX1; X-ray; 1.95 A; Y/Z=66-80. DR PDB; 6OX2; X-ray; 2.09 A; Y/Z=66-80. DR PDB; 6OX3; X-ray; 1.78 A; Y/Z=66-84. DR PDB; 6OX4; X-ray; 2.29 A; Y/Z=66-80. DR PDB; 6OX5; X-ray; 2.10 A; Y=66-83. DR PDB; 6V62; X-ray; 2.36 A; Y=66-88. DR PDB; 6V63; X-ray; 2.02 A; Y/Z=66-88. DR PDB; 6WK1; X-ray; 1.89 A; Y/Z=66-88. DR PDB; 6WK2; X-ray; 1.76 A; C/Y=66-88. DR PDB; 7AS4; EM; 4.13 A; 7=2-375. DR PDB; 7P1H; EM; 3.90 A; B=4-375. DR PDB; 7QJ6; EM; 7.80 A; e=1-375. DR PDB; 7QJ9; EM; 8.10 A; e=1-375. DR PDB; 7VDV; EM; 3.40 A; P=1-375. DR PDB; 7W28; X-ray; 1.79 A; P=66-81. DR PDB; 7W29; X-ray; 2.90 A; P=66-81. DR PDB; 7Y8R; EM; 4.40 A; J=1-375. DR PDB; 7ZTC; EM; 3.90 A; A/B/C/D/E/F/G/H=1-375. DR PDB; 7ZTD; EM; 4.60 A; A/B/C/D/E/F/G/H=1-375. DR PDB; 8COG; EM; 3.50 A; F=2-375. DR PDB; 8DNH; EM; 2.99 A; A/B/C/D=2-375. DR PDB; 8IB8; EM; 4.42 A; S=1-375. DR PDB; 8OI8; EM; 2.28 A; A/B/C/D/E=1-375. DR PDB; 8OID; EM; 2.30 A; A/B/C/D/E=1-375. DR PDB; 8QR1; EM; 2.40 A; B/G=1-375. DR PDB; 8RTT; EM; 3.56 A; A/B/C/D=1-375. DR PDB; 8RTY; EM; 6.25 A; A/B/C/D=2-375. DR PDB; 8RU2; EM; 3.49 A; B/C/D=2-375. DR PDB; 8RX1; EM; 3.57 A; 7=2-375. DR PDB; 8UAU; EM; 5.70 A; S=3-14. DR PDB; 8VRD; EM; 7.00 A; S=1-375. DR PDB; 8VRJ; EM; 7.70 A; 9=1-375. DR PDB; 8VRK; EM; 8.50 A; 9=1-375. DR PDB; 8X15; EM; 3.20 A; S/U=1-375. DR PDB; 8X19; EM; 3.20 A; S/U=1-375. DR PDB; 8X1C; EM; 3.20 A; S/U=1-375. DR PDB; 8XVG; EM; 9.40 A; K=1-375. DR PDB; 8XVT; EM; 3.20 A; K=1-375. DR PDB; 9B2Z; EM; 2.83 A; B=1-375. DR PDB; 9B7J; EM; 3.49 A; H=1-375. DR PDB; 9B85; EM; 3.47 A; H=1-375. DR PDB; 9C57; EM; 2.75 A; J=1-375. DR PDB; 9C62; EM; 5.28 A; J=1-375. DR PDB; 9C6N; EM; 3.29 A; J=1-375. DR PDB; 9CAC; EM; 3.43 A; K/L=1-375. DR PDB; 9CAE; EM; 3.07 A; L=1-375. DR PDB; 9FJM; EM; 3.65 A; A/B/C/D=2-375. DR PDB; 9GXI; EM; 9.00 A; B/C/D/E/F/G=1-375. DR PDB; 9I8G; EM; 22.40 A; U=2-375. DR PDB; 9I8H; EM; 23.20 A; U=2-375. DR PDB; 9P1I; EM; 3.00 A; Q/R/S/T/U/V/W/X/Y/Z/a/b=1-375. DR PDB; 9QEW; EM; 2.18 A; A/B/C/D/E=2-375. DR PDB; 9QEY; EM; 2.74 A; A/B/C/D/E=2-375. DR PDB; 9QF2; EM; 2.42 A; A/B/C/D/E=2-375. DR PDB; 9QFB; EM; 2.74 A; A/B/C/D/E/F/G=2-375. DR PDB; 9QFD; EM; 2.61 A; A/B/C/D/E/F/G=2-375. DR PDB; 9QFE; EM; 3.12 A; A/B/C/D/E/F/G=2-375. DR PDB; 9QFG; EM; 3.49 A; A/B/C/D/E/F/G=2-375. DR PDB; 9QFJ; EM; 2.31 A; A/B/C/D/E=2-375. DR PDB; 9QFK; EM; 3.99 A; A/B/C/D/E/F/G=2-375. DR PDB; 9QFO; EM; 2.96 A; A/B/C/D/E/F=2-375. DR PDB; 9QFQ; EM; 2.76 A; A/B/C/D/E=2-375. DR PDB; 9QFW; EM; 3.16 A; A/B/C/D/E=2-375. DR PDB; 9QVM; EM; 6.80 A; Z=1-375. DR PDB; 9QVN; EM; 4.70 A; Z=1-375. DR PDB; 9RL4; EM; 3.50 A; K=1-375. DR PDB; 9RMC; EM; 4.20 A; K=1-375. DR PDB; 9RN1; EM; 5.90 A; K=1-375. DR PDB; 9RN2; EM; 4.10 A; K=1-375. DR PDB; 9UXA; EM; 3.28 A; I=2-375. DR PDB; 9UXB; EM; 2.92 A; B=2-375. DR PDB; 9UXC; EM; 2.74 A; B=2-375. DR PDB; 9WBZ; EM; 2.90 A; L=1-375. DR PDB; 9WC1; EM; 3.40 A; A=1-375. DR AlphaFoldDB; P60709; -. DR EMDB; EMD-0974; -. DR EMDB; EMD-11888; -. DR EMDB; EMD-13159; -. DR EMDB; EMD-16776; -. DR EMDB; EMD-16888; -. DR EMDB; EMD-16889; -. DR EMDB; EMD-18581; -. DR EMDB; EMD-18591; -. DR EMDB; EMD-18597; -. DR EMDB; EMD-18598; -. DR EMDB; EMD-18611; -. DR EMDB; EMD-18794; -. DR EMDB; EMD-19496; -. DR EMDB; EMD-19497; -. DR EMDB; EMD-19499; -. DR EMDB; EMD-19503; -. DR EMDB; EMD-19570; -. DR EMDB; EMD-27572; -. DR EMDB; EMD-31926; -. DR EMDB; EMD-37984; -. DR EMDB; EMD-37988; -. DR EMDB; EMD-37990; -. DR EMDB; EMD-38718; -. DR EMDB; EMD-43481; -. DR EMDB; EMD-43482; -. DR EMDB; EMD-43483; -. DR EMDB; EMD-44118; -. DR EMDB; EMD-44306; -. DR EMDB; EMD-44333; -. DR EMDB; EMD-45206; -. DR EMDB; EMD-45240; -. DR EMDB; EMD-45252; -. DR EMDB; EMD-45386; -. DR EMDB; EMD-45388; -. DR EMDB; EMD-50506; -. DR EMDB; EMD-51662; -. DR EMDB; EMD-52718; -. DR EMDB; EMD-52719; -. DR EMDB; EMD-53093; -. DR EMDB; EMD-53094; -. DR EMDB; EMD-53096; -. DR EMDB; EMD-53105; -. DR EMDB; EMD-53106; -. DR EMDB; EMD-53107; -. DR EMDB; EMD-53108; -. DR EMDB; EMD-53110; -. DR EMDB; EMD-53111; -. DR EMDB; EMD-53112; -. DR EMDB; EMD-53113; -. DR EMDB; EMD-53114; -. DR EMDB; EMD-53118; -. DR EMDB; EMD-53119; -. DR EMDB; EMD-53121; -. DR EMDB; EMD-53122; -. DR EMDB; EMD-53399; -. DR EMDB; EMD-53400; -. DR EMDB; EMD-54030; -. DR EMDB; EMD-54056; -. DR EMDB; EMD-54077; -. DR EMDB; EMD-54078; -. DR EMDB; EMD-64578; -. DR EMDB; EMD-64579; -. DR EMDB; EMD-64580; -. DR EMDB; EMD-65851; -. DR EMDB; EMD-65854; -. DR EMDB; EMD-68033; -. DR EMDB; EMD-68034; -. DR EMDB; EMD-68040; -. DR EMDB; EMD-71108; -. DR EMDB; EMD-8886; -. DR SASBDB; P60709; -. DR SMR; P60709; -. DR BioGRID; 106575; 1266. DR ComplexPortal; CPX-1164; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant. DR ComplexPortal; CPX-1194; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant. DR ComplexPortal; CPX-1195; Embryonic stem cell-specific SWI/SNF ATP-dependent chromatin remodeling complex. DR ComplexPortal; CPX-1196; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B variant. DR ComplexPortal; CPX-1199; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A variant. DR ComplexPortal; CPX-1201; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant. DR ComplexPortal; CPX-1202; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant. DR ComplexPortal; CPX-1203; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant. DR ComplexPortal; CPX-1204; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant. DR ComplexPortal; CPX-1205; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant. DR ComplexPortal; CPX-1206; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant. DR ComplexPortal; CPX-1207; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant. DR ComplexPortal; CPX-1209; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant. DR ComplexPortal; CPX-1210; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant. DR ComplexPortal; CPX-1211; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant. DR ComplexPortal; CPX-1212; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant. DR ComplexPortal; CPX-1213; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant. DR ComplexPortal; CPX-1215; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant. DR ComplexPortal; CPX-1216; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant. DR ComplexPortal; CPX-1217; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant. DR ComplexPortal; CPX-1218; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant. DR ComplexPortal; CPX-1219; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant. DR ComplexPortal; CPX-1220; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant. DR ComplexPortal; CPX-1221; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant. DR ComplexPortal; CPX-1222; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant. DR ComplexPortal; CPX-1223; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant. DR ComplexPortal; CPX-1224; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant. DR ComplexPortal; CPX-1225; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant. DR ComplexPortal; CPX-1226; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant. DR ComplexPortal; CPX-1227; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant. DR ComplexPortal; CPX-1228; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant. DR ComplexPortal; CPX-26352; Dynactin complex. DR ComplexPortal; CPX-26416; Gamma tubulin ring complex. DR ComplexPortal; CPX-4084; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA2 variant. DR ComplexPortal; CPX-4203; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA2 variant. DR ComplexPortal; CPX-4206; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA4 variant. DR ComplexPortal; CPX-4207; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA4 variant. DR ComplexPortal; CPX-4223; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA2 variant. DR ComplexPortal; CPX-4224; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA2 variant. DR ComplexPortal; CPX-4225; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA4 variant. DR ComplexPortal; CPX-4226; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA4 variant. DR ComplexPortal; CPX-978; NuA4 histone acetyltransferase complex. DR CORUM; P60709; -. DR DIP; DIP-29686N; -. DR FunCoup; P60709; 2855. DR IntAct; P60709; 525. DR NDEx; IQUERY-CP-ACTB; 14 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000494750; -. DR BindingDB; P60709; -. DR ChEMBL; CHEMBL2062353; -. DR DrugBank; DB12695; Phenethyl Isothiocyanate. DR DrugBank; DB04216; Quercetin. DR CarbonylDB; P60709; -. DR GlyCosmos; P60709; 11 sites, 3 glycans. DR GlyGen; P60709; 12 sites, 1 N-linked glycan (1 site), 2 O-linked glycans (11 sites). DR iPTMnet; P60709; -. DR MetOSite; P60709; -. DR PhosphoSitePlus; P60709; -. DR SwissPalm; P60709; -. DR BioMuta; ACTB; -. DR DMDM; 46397333; -. DR REPRODUCTION-2DPAGE; P60709; -. DR jPOST; P60709; -. DR MassIVE; P60709; -. DR PaxDb; 9606-ENSP00000494750; -. DR PeptideAtlas; P60709; -. DR PRIDE; P60709; -. DR ProteomicsDB; 57224; -. DR Pumba; P60709; -. DR TopDownProteomics; P60709; -. DR ABCD; P60709; 4 sequenced antibodies. DR Antibodypedia; 3623; 2262 antibodies from 62 providers. DR DNASU; 60; -. DR Ensembl; ENST00000493945.6; ENSP00000494269.1; ENSG00000075624.18. DR Ensembl; ENST00000642480.2; ENSP00000495995.2; ENSG00000075624.18. DR Ensembl; ENST00000646664.1; ENSP00000494750.1; ENSG00000075624.18. DR Ensembl; ENST00000674681.1; ENSP00000502821.1; ENSG00000075624.18. DR Ensembl; ENST00000675515.1; ENSP00000501862.1; ENSG00000075624.18. DR Ensembl; ENST00000899420.1; ENSP00000569479.1; ENSG00000075624.18. DR Ensembl; ENST00000899421.1; ENSP00000569480.1; ENSG00000075624.18. DR Ensembl; ENST00000899425.1; ENSP00000569484.1; ENSG00000075624.18. DR Ensembl; ENST00000899429.1; ENSP00000569488.1; ENSG00000075624.18. DR Ensembl; ENST00000919306.1; ENSP00000589365.1; ENSG00000075624.18. DR Ensembl; ENST00000950579.1; ENSP00000620638.1; ENSG00000075624.18. DR GeneID; 60; -. DR KEGG; hsa:60; -. DR MANE-Select; ENST00000646664.1; ENSP00000494750.1; NM_001101.5; NP_001092.1. DR AGR; HGNC:132; -. DR CIViC; 60; 1 evidence item across 1 molecular profile. DR ClinPGx; PA24457; -. DR CTD; 60; -. DR DisGeNET; 60; -. DR GeneCards; ACTB; -. DR GeneReviews; ACTB; -. DR HGNC; HGNC:132; ACTB. DR HPA; ENSG00000075624; Low tissue specificity. DR MalaCards; ACTB; -. DR MIM; 102630; gene. DR MIM; 243310; phenotype. DR MIM; 604919; phenotype. DR MIM; 607371; phenotype. DR MIM; 620470; phenotype. DR MIM; 620475; phenotype. DR OpenTargets; ENSG00000075624; -. DR Orphanet; 674653; Actinomyopathy-associated syndromic thrombocytopenia. DR Orphanet; 2995; Baraitser-Winter cerebrofrontofacial syndrome. DR Orphanet; 64755; Becker nevus syndrome. DR Orphanet; 79107; Developmental malformations-deafness-dystonia syndrome. DR Orphanet; 673556; Pseudomyogenic hemangioendothelioma. DR VEuPathDB; HostDB:ENSG00000075624; -. DR eggNOG; KOG0676; Eukaryota. DR GeneTree; ENSGT00950000182960; -. DR HOGENOM; CLU_027965_0_2_1; -. DR InParanoid; P60709; -. DR OMA; CAKPDSQ; -. DR OrthoDB; 9816605at2759; -. DR PAN-GO; P60709; 11 GO annotations based on evolutionary models. DR PhylomeDB; P60709; -. DR PathwayCommons; P60709; -. DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane. DR Reactome; R-HSA-190873; Gap junction degradation. DR Reactome; R-HSA-196025; Formation of annular gap junctions. DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation. DR Reactome; R-HSA-3214847; HATs acetylate histones. DR Reactome; R-HSA-389957; Prefoldin mediated transfer of substrate to CCT/TriC. DR Reactome; R-HSA-390450; Folding of actin by CCT/TriC. DR Reactome; R-HSA-3928662; EPHB-mediated forward signaling. DR Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells. DR Reactome; R-HSA-418990; Adherens junctions interactions. DR Reactome; R-HSA-437239; Recycling pathway of L1. DR Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway. DR Reactome; R-HSA-445095; Interaction between L1 and Ankyrins. DR Reactome; R-HSA-446353; Cell-extracellular matrix interactions. DR Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression. DR Reactome; R-HSA-5626467; RHO GTPases activate IQGAPs. DR Reactome; R-HSA-5663213; RHO GTPases Activate WASPs and WAVEs. DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins. DR Reactome; R-HSA-5674135; MAP2K and MAPK activation. DR Reactome; R-HSA-5689603; UCH proteinases. DR Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER. DR Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants. DR Reactome; R-HSA-6802948; Signaling by high-kinase activity BRAF mutants. DR Reactome; R-HSA-6802952; Signaling by BRAF and RAF1 fusions. DR Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF. DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis. DR Reactome; R-HSA-9035034; RHOF GTPase cycle. DR Reactome; R-HSA-9649948; Signaling downstream of RAS mutants. DR Reactome; R-HSA-9656223; Signaling by RAF1 mutants. DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea. DR Reactome; R-HSA-9662361; Sensory processing of sound by outer hair cells of the cochlea. DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis. DR Reactome; R-HSA-9764561; Regulation of CDH1 Function. DR Reactome; R-HSA-9824585; Regulation of MITF-M-dependent genes involved in pigmentation. DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production. DR Reactome; R-HSA-9845323; Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs). DR Reactome; R-HSA-9913351; Formation of the dystrophin-glycoprotein complex (DGC). DR Reactome; R-HSA-9932451; SWI/SNF chromatin remodelers. DR Reactome; R-HSA-9933937; Formation of the canonical BAF (cBAF) complex. DR Reactome; R-HSA-9933939; Formation of the polybromo-BAF (pBAF) complex. DR Reactome; R-HSA-9933946; Formation of the embryonic stem cell BAF (esBAF) complex. DR Reactome; R-HSA-9933947; Formation of the non-canonical BAF (ncBAF) complex. DR Reactome; R-HSA-9934037; Formation of neuronal progenitor and neuronal BAF (npBAF and nBAF). DR Reactome; R-HSA-9938024; Somatic hypermutation of immunoglobulin genes. DR Reactome; R-HSA-9953170; GBP-mediated host defense. DR Reactome; R-HSA-9958825; Activation of STAT3 by cadherin engagement. DR SignaLink; P60709; -. DR SIGNOR; P60709; -. DR Agora; ENSG00000075624; -. DR BioGRID-ORCS; 60; 541 hits in 1170 CRISPR screens. DR CD-CODE; 232F8A39; P-body. DR CD-CODE; 91857CE7; Nucleolus. DR CD-CODE; DEE660B4; Stress granule. DR CD-CODE; F85A2E29; IMP1 RNP granule. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. DR ChiTaRS; ACTB; human. DR EvolutionaryTrace; P60709; -. DR GeneWiki; Beta-actin; -. DR GenomeRNAi; 60; -. DR Pharos; P60709; Tbio. DR PRO; PR:P60709; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; P60709; protein. DR Bgee; ENSG00000075624; Expressed in saphenous vein and 212 other cell types or tissues. DR ExpressionAtlas; P60709; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB. DR GO; GO:0005884; C:actin filament; IBA:GO_Central. DR GO; GO:0005912; C:adherens junction; IDA:ARUK-UCL. DR GO; GO:0043296; C:apical junction complex; IDA:ARUK-UCL. DR GO; GO:0030424; C:axon; IBA:GO_Central. DR GO; GO:0140092; C:bBAF complex; NAS:ComplexPortal. DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB. DR GO; GO:0035060; C:brahma complex; NAS:ComplexPortal. DR GO; GO:0005911; C:cell-cell junction; IMP:ARUK-UCL. DR GO; GO:0000785; C:chromatin; HDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL. DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL. DR GO; GO:0005856; C:cytoskeleton; IDA:ARUK-UCL. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0097433; C:dense body; ISS:AgBase. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; HDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0000930; C:gamma-tubulin complex; NAS:ComplexPortal. DR GO; GO:0140288; C:GBAF complex; NAS:ComplexPortal. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. DR GO; GO:0000776; C:kinetochore; NAS:ComplexPortal. DR GO; GO:0030027; C:lamellipodium; IDA:ARUK-UCL. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0071565; C:nBAF complex; NAS:ComplexPortal. DR GO; GO:0071564; C:npBAF complex; NAS:ComplexPortal. DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB. DR GO; GO:0016363; C:nuclear matrix; NAS:ComplexPortal. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0000786; C:nucleosome; IDA:ComplexPortal. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS:AgBase. DR GO; GO:0098871; C:postsynaptic actin cytoskeleton; IDA:SynGO. DR GO; GO:0098793; C:presynapse; TAS:ARUK-UCL. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB. DR GO; GO:0016586; C:RSC-type complex; NAS:ComplexPortal. DR GO; GO:0016514; C:SWI/SNF complex; NAS:ComplexPortal. DR GO; GO:0045202; C:synapse; IBA:GO_Central. DR GO; GO:0070160; C:tight junction; IDA:ARUK-UCL. DR GO; GO:0031982; C:vesicle; HDA:UniProtKB. DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0019894; F:kinesin binding; IPI:UniProtKB. DR GO; GO:0050998; F:nitric-oxide synthase binding; IPI:BHF-UCL. DR GO; GO:0030235; F:nitric-oxide synthase regulator activity; IDA:BHF-UCL. DR GO; GO:0019901; F:protein kinase binding; IPI:ARUK-UCL. DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:UniProtKB. DR GO; GO:0098973; F:structural constituent of postsynaptic actin cytoskeleton; IDA:SynGO. DR GO; GO:0030957; F:Tat protein binding; IPI:BHF-UCL. DR GO; GO:0048156; F:tau protein binding; NAS:ARUK-UCL. DR GO; GO:0141108; F:transporter regulator activity; IGI:ARUK-UCL. DR GO; GO:0034333; P:adherens junction assembly; IMP:ARUK-UCL. DR GO; GO:0045176; P:apical protein localization; IMP:ARUK-UCL. DR GO; GO:0007409; P:axonogenesis; IBA:GO_Central. DR GO; GO:0048870; P:cell motility; IMP:UniProtKB. DR GO; GO:0072749; P:cellular response to cytochalasin B; IMP:UniProtKB. DR GO; GO:0006338; P:chromatin remodeling; HDA:GO_Central. DR GO; GO:0007010; P:cytoskeleton organization; ISS:ARUK-UCL. DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:ARUK-UCL. DR GO; GO:0035633; P:maintenance of blood-brain barrier; NAS:ARUK-UCL. DR GO; GO:0007020; P:microtubule nucleation; NAS:ComplexPortal. DR GO; GO:0001738; P:morphogenesis of a polarized epithelium; IMP:ARUK-UCL. DR GO; GO:0045596; P:negative regulation of cell differentiation; NAS:ComplexPortal. DR GO; GO:0070527; P:platelet aggregation; HMP:UniProtKB. DR GO; GO:0045597; P:positive regulation of cell differentiation; NAS:ComplexPortal. DR GO; GO:0008284; P:positive regulation of cell population proliferation; NAS:ComplexPortal. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; NAS:ComplexPortal. DR GO; GO:2000781; P:positive regulation of double-strand break repair; NAS:ComplexPortal. DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IDA:ComplexPortal. DR GO; GO:0045663; P:positive regulation of myoblast differentiation; NAS:ComplexPortal. DR GO; GO:0051623; P:positive regulation of norepinephrine uptake; TAS:ARUK-UCL. DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; NAS:ComplexPortal. DR GO; GO:0045582; P:positive regulation of T cell differentiation; NAS:ComplexPortal. DR GO; GO:0071896; P:protein localization to adherens junction; IMP:ARUK-UCL. DR GO; GO:0042981; P:regulation of apoptotic process; NAS:ComplexPortal. DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal. DR GO; GO:2000779; P:regulation of double-strand break repair; NAS:ComplexPortal. DR GO; GO:0070316; P:regulation of G0 to G1 transition; NAS:ComplexPortal. DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; NAS:ComplexPortal. DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; NAS:ComplexPortal. DR GO; GO:0051621; P:regulation of norepinephrine uptake; IGI:ARUK-UCL. DR GO; GO:2000819; P:regulation of nucleotide-excision repair; NAS:ComplexPortal. DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; IMP:ARUK-UCL. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; NAS:ComplexPortal. DR GO; GO:0150111; P:regulation of transepithelial transport; IMP:ARUK-UCL. DR GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB. DR CDD; cd10224; ASKHA_NBD_actin; 1. DR DisProt; DP03957; -. DR FunFam; 3.30.420.40:FF:000218; actin, alpha sarcomeric/skeletal-like; 1. DR FunFam; 3.30.420.40:FF:000291; Actin, alpha skeletal muscle; 1. DR FunFam; 3.90.640.10:FF:000047; Actin, alpha skeletal muscle; 1. DR FunFam; 3.30.420.40:FF:000058; Putative actin-related protein 5; 1. DR Gene3D; 3.30.420.40; -; 2. DR Gene3D; 3.90.640.10; Actin, Chain A, domain 4; 1. DR InterPro; IPR004000; Actin. DR InterPro; IPR020902; Actin/actin-like_CS. DR InterPro; IPR004001; Actin_CS. DR InterPro; IPR043129; ATPase_NBD. DR PANTHER; PTHR11937; ACTIN; 1. DR Pfam; PF00022; Actin; 1. DR PRINTS; PR00190; ACTIN. DR SMART; SM00268; ACTIN; 1. DR SUPFAM; SSF53067; Actin-like ATPase domain; 2. DR PROSITE; PS00406; ACTINS_1; 1. DR PROSITE; PS00432; ACTINS_2; 1. DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Deafness; KW Direct protein sequencing; Disease variant; Dystonia; Hydrolase; KW Intellectual disability; Isopeptide bond; Methylation; Nucleotide-binding; KW Nucleus; Oxidation; Proteomics identification; Reference proteome; KW Ubl conjugation. FT CHAIN 1..375 FT /note="Actin, cytoplasmic 1" FT /id="PRO_0000367073" FT INIT_MET 1 FT /note="Removed; alternate" FT /evidence="ECO:0000269|PubMed:12665801, FT ECO:0000269|PubMed:36173861, ECO:0000269|Ref.8, FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712" FT CHAIN 2..375 FT /note="Actin, cytoplasmic 1, N-terminally processed" FT /evidence="ECO:0000305|PubMed:29581253" FT /id="PRO_0000000771" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|PubMed:36173861, FT ECO:0007744|PubMed:22814378" FT MOD_RES 2 FT /note="N-acetylaspartate; in Actin, cytoplasmic 1, N- FT terminally processed" FT /evidence="ECO:0000269|PubMed:29581253, FT ECO:0000269|PubMed:30028079, ECO:0000269|Ref.8, FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712" FT MOD_RES 44 FT /note="Methionine (R)-sulfoxide" FT /evidence="ECO:0000269|PubMed:29343822" FT MOD_RES 47 FT /note="Methionine (R)-sulfoxide" FT /evidence="ECO:0000269|PubMed:29343822" FT MOD_RES 73 FT /note="Tele-methylhistidine" FT /evidence="ECO:0000269|PubMed:30526847, FT ECO:0000269|PubMed:30626964, ECO:0000269|PubMed:30785395, FT ECO:0000269|PubMed:31388018, ECO:0000269|PubMed:32503840" FT MOD_RES 84 FT /note="N6-methyllysine" FT /evidence="ECO:0000269|PubMed:23673617" FT CROSSLNK 50 FT /note="(Microbial infection) Isoglutamyl lysine isopeptide FT (Lys-Glu) (interchain with E-270); by Vibrio toxins RtxA FT and VgrG1" FT /evidence="ECO:0000305|PubMed:19015515" FT CROSSLNK 270 FT /note="(Microbial infection) Isoglutamyl lysine isopeptide FT (Glu-Lys) (interchain with K-50); by Vibrio toxins RtxA and FT VgrG1" FT /evidence="ECO:0000305|PubMed:19015515" FT VARIANT 12 FT /note="N -> D (in BRWS1; dbSNP:rs281875331)" FT /evidence="ECO:0000269|PubMed:22366783" FT /id="VAR_067810" FT VARIANT 65 FT /note="L -> V (in BRWS1; dbSNP:rs281875332)" FT /evidence="ECO:0000269|PubMed:22366783" FT /id="VAR_067811" FT VARIANT 70 FT /note="P -> A (in BRWS1; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:30733661" FT /id="VAR_088861" FT VARIANT 111 FT /note="N -> D (in CSMH; uncertain significance; somatic FT variant)" FT /evidence="ECO:0000269|PubMed:32170967" FT /id="VAR_088862" FT VARIANT 137 FT /note="Q -> H (in CSMH; uncertain significance; somatic FT variant)" FT /evidence="ECO:0000269|PubMed:32170967" FT /id="VAR_088863" FT VARIANT 146 FT /note="G -> A (in CSMH; somatic variant)" FT /evidence="ECO:0000269|PubMed:32170967" FT /id="VAR_088864" FT VARIANT 146 FT /note="G -> D (in CSMH; somatic variant)" FT /evidence="ECO:0000269|PubMed:32170967" FT /id="VAR_088865" FT VARIANT 146 FT /note="G -> S (in CSMH; somatic variant)" FT /evidence="ECO:0000269|PubMed:32170967" FT /id="VAR_088866" FT VARIANT 146 FT /note="G -> V (in CSMH; somatic variant)" FT /evidence="ECO:0000269|PubMed:32170967" FT /id="VAR_088867" FT VARIANT 147 FT /note="R -> C (in BNS and CSMH; also found in isolated FT non-syndromic Becker nevi; somatic variant)" FT /evidence="ECO:0000269|PubMed:28347698, FT ECO:0000269|PubMed:32170967" FT /id="VAR_088868" FT VARIANT 147 FT /note="R -> S (in CSMH; also found in isolated FT non-syndromic Becker nevi; somatic variant)" FT /evidence="ECO:0000269|PubMed:28347698, FT ECO:0000269|PubMed:32170967" FT /id="VAR_088869" FT VARIANT 171 FT /note="L -> F (in THC8; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:30733661" FT /id="VAR_088870" FT VARIANT 183 FT /note="R -> W (in DDS1; likely pathogenic; results in FT reduced actin polymerization rate and increased FT depolymerization; results in higher ATP hydrolysis compared FT to the wild type; does not affect thermal stability; FT modifies cell response to latrunculin A; FT dbSNP:rs104894003)" FT /evidence="ECO:0000269|PubMed:16685646, FT ECO:0000269|PubMed:25255767, ECO:0000269|PubMed:28487785, FT ECO:0000269|PubMed:29788902, ECO:0000269|PubMed:35005077" FT /id="VAR_030026" FT VARIANT 196 FT /note="R -> C (in BRWS1; dbSNP:rs281875333)" FT /evidence="ECO:0000269|PubMed:22366783" FT /id="VAR_067812" FT VARIANT 196 FT /note="R -> H (in BRWS1; dbSNP:rs281875334)" FT /evidence="ECO:0000269|PubMed:22366783" FT /id="VAR_067813" FT VARIANT 243 FT /note="P -> L (in dbSNP:rs11546899)" FT /id="VAR_048185" FT VARIANT 313 FT /note="M -> R (in THC8; uncertain significance)" FT /evidence="ECO:0000269|PubMed:30315159" FT /id="VAR_088871" FT VARIANT 338..341 FT /note="Missing (in THC8; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:30315159" FT /id="VAR_088872" FT VARIANT 364 FT /note="E -> K (in THC8; uncertain significance; results in FT reduced actin polymerization rate without affecting FT depolymerization; has no effect on ATP hydrolysis rate; FT does not affect thermal stability)" FT /evidence="ECO:0000269|PubMed:10411937, FT ECO:0000269|PubMed:25255767" FT /id="VAR_088873" FT MUTAGEN 69 FT /note="Y->A: Decreased interaction with SETD3." FT /evidence="ECO:0000269|PubMed:30785395" FT MUTAGEN 71 FT /note="I->A: Decreased interaction with SETD3." FT /evidence="ECO:0000269|PubMed:30785395" FT MUTAGEN 71 FT /note="I->A: Impaired methylation by SETD3." FT /evidence="ECO:0000269|PubMed:30626964" FT MUTAGEN 73 FT /note="H->A: Abolished methylation by SETD3." FT /evidence="ECO:0000269|PubMed:30785395" FT MUTAGEN 73 FT /note="H->K: Weak methylation by a A-256 or V-256 SETD3 FT mutant. High methylation by a F-256 and A-274 SETD3 FT mutant." FT /evidence="ECO:0000269|PubMed:31388018, FT ECO:0000269|PubMed:32503840" FT MUTAGEN 74 FT /note="G->A: Impaired methylation by SETD3." FT /evidence="ECO:0000269|PubMed:30626964" FT MUTAGEN 79 FT /note="W->E: Does not affect methylation by SETD3." FT /evidence="ECO:0000269|PubMed:30626964" FT MUTAGEN 80 FT /note="D->A: Decreased interaction with SETD3." FT /evidence="ECO:0000269|PubMed:30785395" FT MUTAGEN 81 FT /note="D->A: Decreased interaction with SETD3." FT /evidence="ECO:0000269|PubMed:30785395" FT MUTAGEN 82 FT /note="M->A: Decreased interaction with SETD3." FT /evidence="ECO:0000269|PubMed:30785395" FT CONFLICT 97 FT /note="A -> P (in Ref. 6; AAH16045)" FT /evidence="ECO:0000305" FT CONFLICT 116 FT /note="R -> L (in Ref. 6; AAH12854)" FT /evidence="ECO:0000305" FT TURN 3..5 FT /evidence="ECO:0007829|PDB:8DNH" FT STRAND 8..12 FT /evidence="ECO:0007829|PDB:9QEW" FT STRAND 14..22 FT /evidence="ECO:0007829|PDB:9QEW" FT STRAND 24..26 FT /evidence="ECO:0007829|PDB:9QEW" FT STRAND 28..32 FT /evidence="ECO:0007829|PDB:9QEW" FT STRAND 35..38 FT /evidence="ECO:0007829|PDB:9QEW" FT STRAND 40..42 FT /evidence="ECO:0007829|PDB:8OI8" FT STRAND 44..47 FT /evidence="ECO:0007829|PDB:8DNH" FT STRAND 51..54 FT /evidence="ECO:0007829|PDB:9B85" FT HELIX 56..60 FT /evidence="ECO:0007829|PDB:9QEW" FT HELIX 62..64 FT /evidence="ECO:0007829|PDB:9QEW" FT STRAND 68..70 FT /evidence="ECO:0007829|PDB:6MBK" FT STRAND 75..77 FT /evidence="ECO:0007829|PDB:9QEW" FT TURN 81..83 FT /evidence="ECO:0007829|PDB:6OX3" FT HELIX 88..94 FT /evidence="ECO:0007829|PDB:9QEW" FT HELIX 98..100 FT /evidence="ECO:0007829|PDB:9QEW" FT STRAND 103..107 FT /evidence="ECO:0007829|PDB:9QEW" FT HELIX 113..125 FT /evidence="ECO:0007829|PDB:9QEW" FT STRAND 130..136 FT /evidence="ECO:0007829|PDB:9QEW" FT HELIX 137..144 FT /evidence="ECO:0007829|PDB:9QEW" FT STRAND 148..155 FT /evidence="ECO:0007829|PDB:9QEW" FT STRAND 160..166 FT /evidence="ECO:0007829|PDB:9QEW" FT HELIX 172..174 FT /evidence="ECO:0007829|PDB:9QEW" FT STRAND 176..179 FT /evidence="ECO:0007829|PDB:9QEW" FT HELIX 182..192 FT /evidence="ECO:0007829|PDB:9QEW" FT HELIX 193..196 FT /evidence="ECO:0007829|PDB:9QEW" FT HELIX 203..216 FT /evidence="ECO:0007829|PDB:9QEW" FT HELIX 223..232 FT /evidence="ECO:0007829|PDB:9QEW" FT HELIX 234..236 FT /evidence="ECO:0007829|PDB:9CAE" FT STRAND 238..241 FT /evidence="ECO:0007829|PDB:9QEW" FT STRAND 243..245 FT /evidence="ECO:0007829|PDB:9QFO" FT STRAND 247..251 FT /evidence="ECO:0007829|PDB:9QEW" FT HELIX 253..259 FT /evidence="ECO:0007829|PDB:9QEW" FT TURN 260..262 FT /evidence="ECO:0007829|PDB:9QEW" FT HELIX 264..267 FT /evidence="ECO:0007829|PDB:9QEW" FT HELIX 274..283 FT /evidence="ECO:0007829|PDB:9QEW" FT HELIX 287..289 FT /evidence="ECO:0007829|PDB:9QEW" FT HELIX 290..294 FT /evidence="ECO:0007829|PDB:9QEW" FT STRAND 297..301 FT /evidence="ECO:0007829|PDB:9QEW" FT HELIX 302..304 FT /evidence="ECO:0007829|PDB:9QEW" FT STRAND 306..308 FT /evidence="ECO:0007829|PDB:8X19" FT HELIX 309..320 FT /evidence="ECO:0007829|PDB:9QEW" FT STRAND 323..325 FT /evidence="ECO:0007829|PDB:8QR1" FT HELIX 335..337 FT /evidence="ECO:0007829|PDB:9QEW" FT HELIX 338..346 FT /evidence="ECO:0007829|PDB:9QEW" FT HELIX 350..352 FT /evidence="ECO:0007829|PDB:9QEW" FT TURN 353..355 FT /evidence="ECO:0007829|PDB:9QEW" FT STRAND 356..358 FT /evidence="ECO:0007829|PDB:9QEW" FT HELIX 359..363 FT /evidence="ECO:0007829|PDB:9QEW" FT HELIX 367..369 FT /evidence="ECO:0007829|PDB:9QEW" FT HELIX 370..373 FT /evidence="ECO:0007829|PDB:9QEW" SQ SEQUENCE 375 AA; 41737 MW; 6AFD05CA94E360E2 CRC64; MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMATA ASSSSLEKSY ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ EYDESGPSIV HRKCF //