ACTB_HUMAN
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 03-AUG-2022, entry version 200.
DE RecName: Full=Actin, cytoplasmic 1;
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 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 [23]
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 [24]
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 [25]
RP RETRACTION NOTICE OF PUBMED:22814378.
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.;
RT "Retraction: GlcNAcylation of a histone methyltransferase in retinoic-acid-
RT induced granulopoiesis.";
RL Nature 505:574-574(2014).
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 X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 66-88 IN COMPLEX WITH SETD3,
RP METHYLATION AT HIS-73, AND MUTAGENESIS OF TYR-69; ILE-71; HIS-73; ASP-80;
RP 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 [37]
RP X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 67-75 IN COMPLEX WITH SETD3,
RP METHYLATION AT HIS-73, AND 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 [38] {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 (1.75 ANGSTROMS) OF 66-80 IN COMPLEX WITH SETD3,
RP METHYLATION AT HIS-73, AND 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 [39] {ECO:0007744|PDB:6WK1, ECO:0007744|PDB:6WK2}
RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 66-88 IN COMPLEX WITH SETD3, AND
RP 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 [40] {ECO:0007744|PDB:6V62, ECO:0007744|PDB:6V63}
RP X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 66-88 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 [41]
RP VARIANT DJO TRP-183, AND CHARACTERIZATION OF VARIANT DJO 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 [42]
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).
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:29581253). Actin exists in both monomeric (G-actin) and
CC polymeric (F-actin) forms, both forms playing key functions, such as
CC cell motility and contraction (PubMed:29581253). In addition to their
CC role in the cytoplasmic cytoskeleton, G- and F-actin also localize in
CC the nucleus, and regulate gene transcription and motility and repair of
CC damaged DNA (PubMed:29925947). {ECO:0000269|PubMed:29581253,
CC ECO:0000269|PubMed:29925947}.
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:28604741, PubMed:16685646). Each actin can bind to 4 others
CC (PubMed:28604741, PubMed:16685646). 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 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). {ECO:0000250|UniProtKB:P60710,
CC ECO:0000269|PubMed:11687588, ECO:0000269|PubMed:14592989,
CC ECO:0000269|PubMed:15328537, ECO:0000269|PubMed:16685646,
CC ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:17823310,
CC ECO:0000269|PubMed:18765789, ECO:0000269|PubMed:21555369,
CC ECO:0000269|PubMed:21969592, ECO:0000269|PubMed:28604741}.
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; P40123: CAP2; NbExp=5; IntAct=EBI-353944, EBI-1051165;
CC P60709; Q16543: CDC37; NbExp=3; IntAct=EBI-353944, EBI-295634;
CC P60709; P23528: CFL1; NbExp=9; IntAct=EBI-353944, EBI-352733;
CC P60709; Q549N0: CFL2; NbExp=3; IntAct=EBI-353944, EBI-10201319;
CC P60709; Q9Y281: CFL2; NbExp=10; IntAct=EBI-353944, EBI-351218;
CC P60709; P13569: CFTR; NbExp=5; IntAct=EBI-353944, EBI-349854;
CC P60709; P60981: DSTN; NbExp=9; 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=10; 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=2; 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; 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-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, juvenile-onset (DJO) [MIM:607371]: A form of
CC dystonia with juvenile onset. Dystonia is defined by the presence of
CC sustained involuntary muscle contraction, often leading to abnormal
CC postures. Patients with juvenile-onset dystonia manifest progressive,
CC generalized, dopa-unresponsive dystonia, developmental malformations
CC and sensory hearing loss. {ECO:0000269|PubMed:16685646}. 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}. 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="http://atlasgeneticsoncology.org/Genes/ACTBID42959ch7p22.html";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/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://web.expasy.org/spotlight/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
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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_001101.3.
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 PDBsum; 3BYH; -.
DR PDBsum; 3D2U; -.
DR PDBsum; 3J82; -.
DR PDBsum; 3LUE; -.
DR PDBsum; 6ANU; -.
DR PDBsum; 6ICT; -.
DR PDBsum; 6ICV; -.
DR PDBsum; 6LTJ; -.
DR PDBsum; 6MBJ; -.
DR PDBsum; 6MBK; -.
DR PDBsum; 6MBL; -.
DR PDBsum; 6NBW; -.
DR PDBsum; 6OX0; -.
DR PDBsum; 6OX1; -.
DR PDBsum; 6OX2; -.
DR PDBsum; 6OX3; -.
DR PDBsum; 6OX4; -.
DR PDBsum; 6OX5; -.
DR PDBsum; 6V62; -.
DR PDBsum; 6V63; -.
DR PDBsum; 6WK1; -.
DR PDBsum; 6WK2; -.
DR PDBsum; 7AS4; -.
DR PDBsum; 7P1H; -.
DR AlphaFoldDB; P60709; -.
DR SASBDB; P60709; -.
DR SMR; P60709; -.
DR BioGRID; 106575; 915.
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-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 IntAct; P60709; 339.
DR MINT; P60709; -.
DR STRING; 9606.ENSP00000349960; -.
DR ChEMBL; CHEMBL2062353; -.
DR DrugBank; DB12695; Phenethyl Isothiocyanate.
DR DrugBank; DB04216; Quercetin.
DR CarbonylDB; P60709; -.
DR GlyGen; P60709; 6 sites, 2 O-linked glycans (6 sites).
DR iPTMnet; P60709; -.
DR MetOSite; P60709; -.
DR PhosphoSitePlus; P60709; -.
DR SwissPalm; P60709; -.
DR BioMuta; ACTB; -.
DR DMDM; 46397333; -.
DR DOSAC-COBS-2DPAGE; P60709; -.
DR REPRODUCTION-2DPAGE; P60709; -.
DR SWISS-2DPAGE; P60709; -.
DR UCD-2DPAGE; P60709; -.
DR EPD; P60709; -.
DR jPOST; P60709; -.
DR MassIVE; P60709; -.
DR PaxDb; P60709; -.
DR PeptideAtlas; P60709; -.
DR PRIDE; P60709; -.
DR ProteomicsDB; 57224; -.
DR TopDownProteomics; P60709; -.
DR ABCD; P60709; 4 sequenced antibodies.
DR Antibodypedia; 3623; 2015 antibodies from 57 providers.
DR DNASU; 60; -.
DR Ensembl; ENST00000493945.6; ENSP00000494269.1; ENSG00000075624.17.
DR Ensembl; ENST00000642480.2; ENSP00000495995.2; ENSG00000075624.17.
DR Ensembl; ENST00000646664.1; ENSP00000494750.1; ENSG00000075624.17.
DR Ensembl; ENST00000674681.1; ENSP00000502821.1; ENSG00000075624.17.
DR Ensembl; ENST00000675515.1; ENSP00000501862.1; ENSG00000075624.17.
DR GeneID; 60; -.
DR KEGG; hsa:60; -.
DR MANE-Select; ENST00000646664.1; ENSP00000494750.1; NM_001101.5; NP_001092.1.
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; 607371; phenotype.
DR neXtProt; NX_P60709; -.
DR OpenTargets; ENSG00000075624; -.
DR Orphanet; 2995; Baraitser-Winter cerebrofrontofacial syndrome.
DR Orphanet; 64755; Becker nevus syndrome.
DR Orphanet; 79107; Developmental malformations-deafness-dystonia syndrome.
DR PharmGKB; PA24457; -.
DR VEuPathDB; HostDB:ENSG00000075624; -.
DR eggNOG; KOG0676; Eukaryota.
DR GeneTree; ENSGT00950000182960; -.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; P60709; -.
DR OMA; AGIHENT; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; P60709; -.
DR TreeFam; TF354237; -.
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-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; P60709; -.
DR SIGNOR; P60709; -.
DR BioGRID-ORCS; 60; 527 hits in 1088 CRISPR screens.
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 210 other tissues.
DR ExpressionAtlas; P60709; baseline and differential.
DR Genevisible; P60709; HS.
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; IC:ComplexPortal.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0035060; C:brahma complex; IC:ComplexPortal.
DR GO; GO:0044305; C:calyx of Held; IEA:Ensembl.
DR GO; GO:0005911; C:cell-cell junction; IMP:ARUK-UCL.
DR GO; GO:0000785; C:chromatin; HDA:UniProtKB.
DR GO; GO:0030863; C:cortical cytoskeleton; IEA:Ensembl.
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:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0140288; C:GBAF complex; IC:ComplexPortal.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0000776; C:kinetochore; IC: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; IC:ComplexPortal.
DR GO; GO:0071564; C:npBAF complex; IC:ComplexPortal.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IC: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; IC:ComplexPortal.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0016514; C:SWI/SNF complex; IC: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:0005524; F:ATP binding; IEA:UniProtKB-KW.
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: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: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:0007163; P:establishment or maintenance of cell polarity; IMP:ARUK-UCL.
DR GO; GO:0016573; P:histone acetylation; IC:ComplexPortal.
DR GO; GO:0043968; P:histone H2A acetylation; IDA:ComplexPortal.
DR GO; GO:0043967; P:histone H4 acetylation; IDA:ComplexPortal.
DR GO; GO:0035633; P:maintenance of blood-brain barrier; NAS:ARUK-UCL.
DR GO; GO:0001738; P:morphogenesis of a polarized epithelium; IMP:ARUK-UCL.
DR GO; GO:0045596; P:negative regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:0032091; P:negative regulation of protein binding; ISS:ARUK-UCL.
DR GO; GO:0070527; P:platelet aggregation; HMP:UniProtKB.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IC:ComplexPortal.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IC: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; IC: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; IC:ComplexPortal.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; IC:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; IDA:SynGO.
DR GO; GO:0071896; P:protein localization to adherens junction; IMP:ARUK-UCL.
DR GO; GO:0042981; P:regulation of apoptotic process; IC:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; ISS:ARUK-UCL.
DR GO; GO:2000779; P:regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:0070316; P:regulation of G0 to G1 transition; IC:ComplexPortal.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IC:ComplexPortal.
DR GO; GO:0051621; P:regulation of norepinephrine uptake; IGI:ARUK-UCL.
DR GO; GO:2000819; P:regulation of nucleotide-excision repair; IC: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; IC:ComplexPortal.
DR GO; GO:0150111; P:regulation of transepithelial transport; IMP:ARUK-UCL.
DR GO; GO:0022898; P:regulation of transmembrane transporter activity; IGI:ARUK-UCL.
DR GO; GO:0001895; P:retina homeostasis; HEP:UniProtKB.
DR GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IEA:Ensembl.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR004001; Actin_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; 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;
KW Intellectual disability; Isopeptide bond; Methylation; Nucleotide-binding;
KW Nucleus; Oxidation; Reference proteome; 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, 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: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 183
FT /note="R -> W (in DJO; modifies cell response to
FT latrunculin A; dbSNP:rs104894003)"
FT /evidence="ECO:0000269|PubMed:16685646"
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 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 STRAND 8..12
FT /evidence="ECO:0007829|PDB:6NBW"
FT STRAND 14..21
FT /evidence="ECO:0007829|PDB:6NBW"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:6NBW"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:6NBW"
FT HELIX 55..60
FT /evidence="ECO:0007829|PDB:6NBW"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:6NBW"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:6MBK"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:6OX3"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:6NBW"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:6NBW"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:6NBW"
FT HELIX 113..125
FT /evidence="ECO:0007829|PDB:6NBW"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:6NBW"
FT HELIX 137..144
FT /evidence="ECO:0007829|PDB:6NBW"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:6NBW"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:6NBW"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:6NBW"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:6NBW"
FT HELIX 182..194
FT /evidence="ECO:0007829|PDB:6NBW"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:6NBW"
FT HELIX 203..216
FT /evidence="ECO:0007829|PDB:6NBW"
FT HELIX 223..232
FT /evidence="ECO:0007829|PDB:6NBW"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:6NBW"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:6NBW"
FT HELIX 253..259
FT /evidence="ECO:0007829|PDB:6NBW"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:6NBW"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:6NBW"
FT HELIX 274..283
FT /evidence="ECO:0007829|PDB:6NBW"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:6NBW"
FT HELIX 290..295
FT /evidence="ECO:0007829|PDB:6NBW"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:6NBW"
FT HELIX 302..305
FT /evidence="ECO:0007829|PDB:6NBW"
FT HELIX 309..320
FT /evidence="ECO:0007829|PDB:6NBW"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:6NBW"
FT HELIX 338..346
FT /evidence="ECO:0007829|PDB:6NBW"
FT HELIX 352..355
FT /evidence="ECO:0007829|PDB:6NBW"
FT HELIX 359..365
FT /evidence="ECO:0007829|PDB:6NBW"
FT HELIX 369..373
FT /evidence="ECO:0007829|PDB:6NBW"
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
