ACTB_MOUSE
ID ACTB_MOUSE Reviewed; 375 AA.
AC P60710; P02570; P70514; P99021; Q11211; Q3TI89; Q3TVP6; Q64316; Q6ZWM3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 181.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3754329; DOI=10.1093/nar/14.6.2829;
RA Tokunaga K., Taniguchi H., Yoda K., Shimizu M., Sakiyama S.;
RT "Nucleotide sequence of a full-length cDNA for mouse cytoskeletal beta-
RT actin mRNA.";
RL Nucleic Acids Res. 14:2829-2829(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, C57BL/6J, and NOD;
RC TISSUE=Bone marrow, Mammary gland, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PROTEIN SEQUENCE OF 2-375, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ASP-2, AND METHYLATION AT HIS-73.
RC TISSUE=Thymus;
RX PubMed=213279; DOI=10.1111/j.1432-1033.1978.tb12624.x;
RA Vandekerckhove J., Weber K.;
RT "Actin amino-acid sequences. Comparison of actins from calf thymus, bovine
RT brain, and SV40-transformed mouse 3T3 cells with rabbit skeletal muscle
RT actin.";
RL Eur. J. Biochem. 90:451-462(1978).
RN [4]
RP PROTEIN SEQUENCE OF 19-39; 51-61; 85-113; 148-177; 184-191; 197-206;
RP 216-254; 257-284; 291-326 AND 360-372, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 27-375.
RX PubMed=3084797; DOI=10.1007/bf02100994;
RA Alonso S., Minty A., Bourlet Y., Buckingham M.;
RT "Comparison of three actin-coding sequences in the mouse; evolutionary
RT relationships between the actin genes of warm-blooded vertebrates.";
RL J. Mol. Evol. 23:11-22(1986).
RN [6]
RP ACETYLATION.
RC TISSUE=Muscle;
RA Vilbois F.;
RL Submitted (OCT-1998) to UniProtKB.
RN [7]
RP INTERACTION WITH CPNE1 AND CPNE4.
RX PubMed=12522145; DOI=10.1074/jbc.m212632200;
RA Tomsig J.L., Snyder S.L., Creutz C.E.;
RT "Identification of targets for calcium signaling through the copine family
RT of proteins. Characterization of a coiled-coil copine-binding motif.";
RL J. Biol. Chem. 278:10048-10054(2003).
RN [8]
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 [9]
RP INTERACTION WITH TBC1D21.
RX PubMed=21128978; DOI=10.1111/j.1365-2605.2010.01126.x;
RA Lin Y.H., Lin Y.M., Kuo Y.C., Wang Y.Y., Kuo P.L.;
RT "Identification and characterization of a novel Rab GTPase-activating
RT protein in spermatids.";
RL Int. J. Androl. 34:E358-E367(2011).
RN [10]
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 [11]
RP OXIDATION AT MET-44 AND MET-47, AND DEOXIDATION AT MET-44 AND MET-47.
RX PubMed=23911929; DOI=10.1016/j.molcel.2013.06.019;
RA Lee B.C., Peterfi Z., Hoffmann F.W., Moore R.E., Kaya A., Avanesov A.,
RA Tarrago L., Zhou Y., Weerapana E., Fomenko D.E., Hoffmann P.R.,
RA Gladyshev V.N.;
RT "MsrB1 and MICALs regulate actin assembly and macrophage function via
RT reversible stereoselective methionine oxidation.";
RL Mol. Cell 51:397-404(2013).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23558171; DOI=10.1126/science.1235038;
RA Baarlink C., Wang H., Grosse R.;
RT "Nuclear actin network assembly by formins regulates the SRF coactivator
RT MAL.";
RL Science 340:864-867(2013).
RN [13]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=25759381; DOI=10.1074/jbc.m114.627166;
RA Plessner M., Melak M., Chinchilla P., Baarlink C., Grosse R.;
RT "Nuclear F-actin formation and reorganization upon cell spreading.";
RL J. Biol. Chem. 290:11209-11216(2015).
RN [14]
RP TISSUE SPECIFICITY.
RX PubMed=30659401; DOI=10.1007/s10735-019-09813-3;
RA Sharma S., Hanukoglu I.;
RT "Mapping the sites of localization of epithelial sodium channel (ENaC) and
RT CFTR in segments of the mammalian epididymis.";
RL J. Mol. Histol. 50:141-154(2019).
RN [15]
RP METHYLATION AT HIS-73.
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 [16]
RP TISSUE SPECIFICITY.
RX PubMed=31605441; DOI=10.1111/febs.15088;
RA Kumaran G.K., Hanukoglu I.;
RT "Identification and classification of epithelial cells in nephron segments
RT by actin cytoskeleton patterns.";
RL FEBS J. 287:1176-1194(2020).
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 (By similarity). 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 (By similarity). 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:23558171, PubMed:25759381).
CC {ECO:0000250|UniProtKB:P60709, ECO:0000269|PubMed:23558171,
CC ECO:0000269|PubMed:25759381}.
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:25759381). Each actin can bind to 4 others (By similarity).
CC Identified in a IGF2BP1-dependent mRNP granule complex containing
CC untranslated mRNAs (By similarity). Component of the BAF complex, which
CC includes at least actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2,
CC SMARCA4/BRG1, MARCB1/BAF47, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57,
CC SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more of
CC SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C (By similarity). In
CC muscle cells, the BAF complex also contains DPF3 (By similarity). Found
CC in a complex with XPO6, Ran, ACTB and PFN1 (By similarity). Component
CC of a complex composed at least of ACTB, AP2M1, AP2A1, AP2A2, MEGF10 and
CC VIM (By similarity). Interacts with XPO6 and EMD (By similarity).
CC Interacts with ERBB2 (By similarity). Interacts with GCSAM (By
CC similarity). Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA
CC domain) (PubMed:12522145). Interacts with TBC1D21 (PubMed:21128978).
CC Interacts with DHX9 (via C-terminus); this interaction is direct and
CC mediates the attachment to nuclear ribonucleoprotein complexes (By
CC similarity). Interacts with FAM107A (PubMed:21969592).
CC {ECO:0000250|UniProtKB:P60709, ECO:0000269|PubMed:12522145,
CC ECO:0000269|PubMed:21128978, ECO:0000269|PubMed:21969592,
CC ECO:0000269|PubMed:25759381}.
CC -!- INTERACTION:
CC P60710; P97792: Cxadr; NbExp=6; IntAct=EBI-353957, EBI-7429264;
CC P60710; Q923J1: Trpm7; NbExp=2; IntAct=EBI-353957, EBI-8010314;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus
CC {ECO:0000269|PubMed:23558171, ECO:0000269|PubMed:25759381}.
CC Note=Localized in cytoplasmic mRNP granules containing untranslated
CC mRNAs. {ECO:0000250|UniProtKB:P60709}.
CC -!- TISSUE SPECIFICITY: Expressed in the epididymis (at protein level)
CC (PubMed:30659401). Expressed in the kidney (at protein level)
CC (PubMed:31605441). {ECO:0000269|PubMed:30659401,
CC ECO:0000269|PubMed:31605441}.
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 (PubMed:23911929). MICAL1 and MICAL2 produce the (R)-
CC S-oxide form. The (R)-S-oxide form is reverted by MSRB1 and MSRB2,
CC which promote actin repolymerization (PubMed:23911929).
CC {ECO:0000269|PubMed:23911929}.
CC -!- PTM: Monomethylation at Lys-84 (K84me1) regulates actin-myosin
CC interaction and actomyosin-dependent processes. Demethylation by ALKBH4
CC is required for maintaining actomyosin dynamics supporting normal
CC cleavage furrow ingression during cytokinesis and cell migration.
CC {ECO:0000250|UniProtKB:P60709}.
CC -!- PTM: Methylated at His-73 by SETD3 (PubMed:30626964). Methylation at
CC His-73 is required for smooth muscle contraction of the laboring uterus
CC during delivery (PubMed:30626964). {ECO:0000269|PubMed:30626964}.
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. In contrast,
CC filament nucleation by the Arp2/3 complex is not affected.
CC {ECO:0000250|UniProtKB:P60709}.
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}.
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DR EMBL; X03672; CAA27307.1; -; mRNA.
DR EMBL; AK088691; BAC40507.1; -; mRNA.
DR EMBL; AK145191; BAE26283.1; -; mRNA.
DR EMBL; AK145196; BAE26288.1; -; mRNA.
DR EMBL; AK145308; BAE26359.1; -; mRNA.
DR EMBL; AK150711; BAE29789.1; -; mRNA.
DR EMBL; AK150879; BAE29928.1; -; mRNA.
DR EMBL; AK151010; BAE30031.1; -; mRNA.
DR EMBL; AK151136; BAE30144.1; -; mRNA.
DR EMBL; AK151145; BAE30152.1; -; mRNA.
DR EMBL; AK151159; BAE30164.1; -; mRNA.
DR EMBL; AK151166; BAE30169.1; -; mRNA.
DR EMBL; AK151190; BAE30187.1; -; mRNA.
DR EMBL; AK151202; BAE30199.1; -; mRNA.
DR EMBL; AK151226; BAE30218.1; -; mRNA.
DR EMBL; AK151277; BAE30264.1; -; mRNA.
DR EMBL; AK151350; BAE30326.1; -; mRNA.
DR EMBL; AK151398; BAE30366.1; -; mRNA.
DR EMBL; AK151995; BAE30859.1; -; mRNA.
DR EMBL; AK151999; BAE30863.1; -; mRNA.
DR EMBL; AK152615; BAE31359.1; -; mRNA.
DR EMBL; AK152651; BAE31388.1; -; mRNA.
DR EMBL; AK152844; BAE31537.1; -; mRNA.
DR EMBL; AK159759; BAE35350.1; -; mRNA.
DR EMBL; AK159834; BAE35412.1; -; mRNA.
DR EMBL; AK160029; BAE35572.1; -; mRNA.
DR EMBL; AK166349; BAE38723.1; -; mRNA.
DR EMBL; AK166498; BAE38810.1; -; mRNA.
DR EMBL; AK167117; BAE39265.1; -; mRNA.
DR EMBL; AK167960; BAE39957.1; -; mRNA.
DR EMBL; X03765; CAA27396.1; -; mRNA.
DR EMBL; M12481; AAA37144.1; -; mRNA.
DR CCDS; CCDS19833.1; -.
DR PIR; A39104; ATMSB.
DR RefSeq; NP_031419.1; NM_007393.5.
DR AlphaFoldDB; P60710; -.
DR SMR; P60710; -.
DR BioGRID; 197944; 365.
DR ComplexPortal; CPX-1232; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1233; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1234; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1235; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1236; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1237; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1238; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1239; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1240; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1241; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1242; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1243; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1244; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1245; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1246; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1247; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1248; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A variant.
DR ComplexPortal; CPX-1250; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B variant.
DR ComplexPortal; CPX-1251; Embryonic stem cell-specific SWI/SNF ATP-dependent chromatin remodeling complex.
DR ComplexPortal; CPX-1252; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1253; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1254; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1255; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1256; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1257; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1258; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1259; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1261; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1262; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1263; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1264; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-4202; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA2 variant.
DR ComplexPortal; CPX-4204; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA2 variant.
DR ComplexPortal; CPX-4221; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA4 variant.
DR ComplexPortal; CPX-4222; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA4 variant.
DR ComplexPortal; CPX-4227; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA2 variant.
DR ComplexPortal; CPX-4228; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA2 variant.
DR ComplexPortal; CPX-4229; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA4 variant.
DR ComplexPortal; CPX-4230; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA4 variant.
DR ComplexPortal; CPX-990; NuA4 histone acetyltransferase complex.
DR CORUM; P60710; -.
DR DIP; DIP-31574N; -.
DR IntAct; P60710; 225.
DR MINT; P60710; -.
DR STRING; 10090.ENSMUSP00000098066; -.
DR CarbonylDB; P60710; -.
DR iPTMnet; P60710; -.
DR PhosphoSitePlus; P60710; -.
DR SwissPalm; P60710; -.
DR COMPLUYEAST-2DPAGE; P60710; -.
DR REPRODUCTION-2DPAGE; P60710; -.
DR SWISS-2DPAGE; P99041; -.
DR UCD-2DPAGE; P60710; -.
DR CPTAC; non-CPTAC-3542; -.
DR EPD; P60710; -.
DR jPOST; P60710; -.
DR MaxQB; P60710; -.
DR PaxDb; P60710; -.
DR PeptideAtlas; P60710; -.
DR PRIDE; P60710; -.
DR ProteomicsDB; 285751; -.
DR TopDownProteomics; P60710; -.
DR Antibodypedia; 3623; 2015 antibodies from 57 providers.
DR DNASU; 11461; -.
DR Ensembl; ENSMUST00000100497; ENSMUSP00000098066; ENSMUSG00000029580.
DR GeneID; 11461; -.
DR KEGG; mmu:11461; -.
DR UCSC; uc009ajk.1; mouse.
DR CTD; 60; -.
DR MGI; MGI:87904; Actb.
DR VEuPathDB; HostDB:ENSMUSG00000029580; -.
DR eggNOG; KOG0676; Eukaryota.
DR GeneTree; ENSGT00950000182960; -.
DR InParanoid; P60710; -.
DR OMA; FHTTAER; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; P60710; -.
DR TreeFam; TF354237; -.
DR Reactome; R-MMU-190873; Gap junction degradation.
DR Reactome; R-MMU-196025; Formation of annular gap junctions.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
DR Reactome; R-MMU-418990; Adherens junctions interactions.
DR Reactome; R-MMU-437239; Recycling pathway of L1.
DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-MMU-445095; Interaction between L1 and Ankyrins.
DR Reactome; R-MMU-446353; Cell-extracellular matrix interactions.
DR Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-MMU-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-MMU-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-5674135; MAP2K and MAPK activation.
DR Reactome; R-MMU-5689603; UCH proteinases.
DR Reactome; R-MMU-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-MMU-9035034; RHOF GTPase cycle.
DR BioGRID-ORCS; 11461; 29 hits in 76 CRISPR screens.
DR ChiTaRS; Actb; mouse.
DR PRO; PR:P60710; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P60710; protein.
DR Bgee; ENSMUSG00000029580; Expressed in late embryo and 263 other tissues.
DR ExpressionAtlas; P60710; baseline and differential.
DR Genevisible; P60710; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005912; C:adherens junction; ISO:MGI.
DR GO; GO:0043296; C:apical junction complex; ISO:MGI.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0140092; C:bBAF complex; IC:ComplexPortal.
DR GO; GO:0035060; C:brahma complex; IC:ComplexPortal.
DR GO; GO:0044305; C:calyx of Held; IDA:SynGO.
DR GO; GO:0005911; C:cell-cell junction; ISO:MGI.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IDA:ARUK-UCL.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0097433; C:dense body; ISS:AgBase.
DR GO; GO:0005925; C:focal adhesion; ISS:AgBase.
DR GO; GO:0140288; C:GBAF complex; IC:ComplexPortal.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; IC:ComplexPortal.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; 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; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; IC:ComplexPortal.
DR GO; GO:0000786; C:nucleosome; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:AgBase.
DR GO; GO:0002102; C:podosome; ISO:MGI.
DR GO; GO:0098871; C:postsynaptic actin cytoskeleton; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0016586; C:RSC-type complex; IC:ComplexPortal.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0001725; C:stress fiber; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019894; F:kinesin binding; ISO:MGI.
DR GO; GO:0050998; F:nitric-oxide synthase binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0098973; F:structural constituent of postsynaptic actin cytoskeleton; ISO:MGI.
DR GO; GO:0030957; F:Tat protein binding; ISO:MGI.
DR GO; GO:0034333; P:adherens junction assembly; ISO:MGI.
DR GO; GO:0045176; P:apical protein localization; ISO:MGI.
DR GO; GO:0007409; P:axonogenesis; ISO:MGI.
DR GO; GO:0048870; P:cell motility; ISO:MGI.
DR GO; GO:0072749; P:cellular response to cytochalasin B; ISO:MGI.
DR GO; GO:0071257; P:cellular response to electrical stimulus; ISO:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; ISO:MGI.
DR GO; GO:0016573; P:histone acetylation; IC:ComplexPortal.
DR GO; GO:0043968; P:histone H2A acetylation; ISO:MGI.
DR GO; GO:0043967; P:histone H4 acetylation; ISO:MGI.
DR GO; GO:0001738; P:morphogenesis of a polarized epithelium; ISO:MGI.
DR GO; GO:0045596; P:negative regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:1904030; P:negative regulation of cyclin-dependent protein kinase activity; IC:ARUK-UCL.
DR GO; GO:0032091; P:negative regulation of protein binding; IDA:ARUK-UCL.
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; ISO:MGI.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IC:ComplexPortal.
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; ISO:MGI.
DR GO; GO:0071896; P:protein localization to adherens junction; ISO:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; IC:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; ISO:MGI.
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; ISO:MGI.
DR GO; GO:2000819; P:regulation of nucleotide-excision repair; IC:ComplexPortal.
DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0150111; P:regulation of transepithelial transport; ISO:MGI.
DR GO; GO:0022898; P:regulation of transmembrane transporter activity; ISO:MGI.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IDA:SynGO.
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 Acetylation; ATP-binding; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Methylation; Nucleotide-binding; Nucleus;
KW Oxidation; Reference proteome; Ubl conjugation.
FT CHAIN 1..375
FT /note="Actin, cytoplasmic 1"
FT /id="PRO_0000367076"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|PubMed:213279"
FT CHAIN 2..375
FT /note="Actin, cytoplasmic 1, N-terminally processed"
FT /id="PRO_0000000775"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P60709"
FT MOD_RES 2
FT /note="N-acetylaspartate; in Actin, cytoplasmic 1, N-
FT terminally processed"
FT /evidence="ECO:0000269|PubMed:213279"
FT MOD_RES 44
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000269|PubMed:23911929"
FT MOD_RES 47
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000269|PubMed:23911929"
FT MOD_RES 73
FT /note="Tele-methylhistidine"
FT /evidence="ECO:0000269|PubMed:213279,
FT ECO:0000269|PubMed:30626964"
FT MOD_RES 84
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P60709"
FT CONFLICT 38
FT /note="P -> S (in Ref. 5; CAA27396/AAA37144)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="S -> F (in Ref. 2; BAE39957)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="D -> E (in Ref. 2; BAE35572)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="P -> T (in Ref. 2; BAE39957)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="G -> R (in Ref. 2; BAE39957)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="L -> V (in Ref. 2; BAE39957)"
FT /evidence="ECO:0000305"
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
