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Actin, cytoplasmic 1 (Beta-actin) [Cleaved into: Actin, cytoplasmic 1, N-terminally processed]

 ACTB_HUMAN              Reviewed;         375 AA.
P60709; P02570; P70514; P99021; Q11211; Q64316; Q75MN2; Q96B34;
Q96HG5;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-APR-1988, sequence version 1.
07-NOV-2018, entry version 176.
RecName: Full=Actin, cytoplasmic 1;
AltName: Full=Beta-actin;
Contains:
RecName: Full=Actin, cytoplasmic 1, N-terminally processed;
Name=ACTB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6322116; DOI=10.1093/nar/12.3.1687;
Ponte P., Ng S.Y., Engel J., Gunning P., Kedes L.;
"Evolutionary conservation in the untranslated regions of actin mRNAs:
DNA sequence of a human beta-actin cDNA.";
Nucleic Acids Res. 12:1687-1696(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2994062; DOI=10.1073/pnas.82.18.6133;
Nakajima-Iijima S., Hamada H., Reddy P., Kakunaga T.;
"Molecular structure of the human cytoplasmic beta-actin gene:
interspecies homology of sequences in the introns.";
Proc. Natl. Acad. Sci. U.S.A. 82:6133-6137(1985).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1734024; DOI=10.1083/jcb.116.4.933;
Ohmori H., Toyama S., Toyama S.;
"Direct proof that the primary site of action of cytochalasin on cell
motility processes is actin.";
J. Cell Biol. 116:933-941(1992).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Eye, Kidney, Muscle, Pancreas, Placenta, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 2-28.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[8]
PROTEIN SEQUENCE OF 2-18; 29-37; 40-50; 85-95; 148-177; 184-191;
197-206; 292-312 AND 316-326, CLEAVAGE OF INITIATOR METHIONINE,
ACETYLATION AT ASP-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (JUN-2005) to UniProtKB.
[9]
PROTEIN SEQUENCE OF 19-62; 85-113; 184-191; 197-206; 216-254; 291-312;
316-326 AND 360-372, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 252-375.
PubMed=6842590; DOI=10.1016/0022-2836(83)90117-1;
Hanukoglu I., Tanese N., Fuchs E.;
"Complementary DNA sequence of a human cytoplasmic actin. Interspecies
divergence of 3' non-coding regions.";
J. Mol. Biol. 163:673-678(1983).
[11]
SUBCELLULAR LOCATION, AND INTERACTION WITH DHX9.
PubMed=11687588; DOI=10.1074/jbc.M109393200;
Zhang S., Buder K., Burkhardt C., Schlott B., Goerlach M., Grosse F.;
"Nuclear DNA helicase II/RNA helicase A binds to filamentous actin.";
J. Biol. Chem. 277:843-853(2002).
[12]
IDENTIFICATION IN A COMPLEX WITH RAN; XPO6 AND PFN1, AND INTERACTION
WITH XPO6.
PubMed=14592989; DOI=10.1093/emboj/cdg565;
Stueven T., Hartmann E., Goerlich D.;
"Exportin 6: a novel nuclear export receptor that is specific for
profilin.actin complexes.";
EMBO J. 22:5928-5940(2003).
[13]
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Lymphoblast;
PubMed=14654843; DOI=10.1038/nature02166;
Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A.,
Mann M.;
"Proteomic characterization of the human centrosome by protein
correlation profiling.";
Nature 426:570-574(2003).
[14]
INTERACTION WITH EMD.
PubMed=15328537; DOI=10.1371/journal.pbio.0020231;
Holaska J.M., Kowalski A.K., Wilson K.L.;
"Emerin caps the pointed end of actin filaments: evidence for an actin
cortical network at the nuclear inner membrane.";
PLoS Biol. 2:1354-1362(2004).
[15]
ISGYLATION.
PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
"Proteomic identification of proteins conjugated to ISG15 in mouse and
human cells.";
Biochem. Biophys. Res. Commun. 336:496-506(2005).
[16]
INTERACTION WITH GCSAM.
PubMed=17823310; DOI=10.1182/blood-2007-04-087775;
Lu X., Chen J., Malumbres R., Cubedo Gil E., Helfman D.M.,
Lossos I.S.;
"HGAL, a lymphoma prognostic biomarker, interacts with the
cytoskeleton and mediates the effects of IL-6 on cell migration.";
Blood 110:4268-4277(2007).
[17]
IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS
SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
Johnsen A.H., Christiansen J., Nielsen F.C.;
"Molecular composition of IMP1 ribonucleoprotein granules.";
Mol. Cell. Proteomics 6:798-811(2007).
[18]
IDENTIFICATION IN THE BAF COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=18765789; DOI=10.1101/gad.471408;
Lange M., Kaynak B., Forster U.B., Toenjes M., Fischer J.J., Grimm C.,
Schlesinger J., Just S., Dunkel I., Krueger T., Mebus S., Lehrach H.,
Lurz R., Gobom J., Rottbauer W., Abdelilah-Seyfried S., Sperling S.;
"Regulation of muscle development by DPF3, a novel histone acetylation
and methylation reader of the BAF chromatin remodeling complex.";
Genes Dev. 22:2370-2384(2008).
[19]
CROSS-LINK BETWEEN LYS-50 AND GLU-270 BY V.CHOLERAE TOXIN RTXA
(MICROBIAL INFECTION).
PubMed=19015515; DOI=10.1073/pnas.0808082105;
Kudryashov D.S., Durer Z.A., Ytterberg A.J., Sawaya M.R., Pashkov I.,
Prochazkova K., Yeates T.O., Loo R.R., Loo J.A., Satchell K.J.,
Reisler E.;
"Connecting actin monomers by iso-peptide bond is a toxicity mechanism
of the Vibrio cholerae MARTX toxin.";
Proc. Natl. Acad. Sci. U.S.A. 105:18537-18542(2008).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT ASP-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[21]
RETRACTED PAPER.
PubMed=19377461; DOI=10.1038/nature07954;
Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G.,
Kitagawa H., Kato S.;
"GlcNAcylation of a histone methyltransferase in retinoic-acid-induced
granulopoiesis.";
Nature 459:455-459(2009).
[22]
INTERACTION WITH FAM107A.
PubMed=21969592; DOI=10.1073/pnas.1103318108;
Schmidt M.V., Schuelke J.P., Liebl C., Stiess M., Avrabos C., Bock J.,
Wochnik G.M., Davies H.A., Zimmermann N., Scharf S.H., Truembach D.,
Wurst W., Zieglgaensberger W., Turck C., Holsboer F., Stewart M.G.,
Bradke F., Eder M., Mueller M.B., Rein T.;
"Tumor suppressor down-regulated in renal cell carcinoma 1 (DRR1) is a
stress-induced actin bundling factor that modulates synaptic efficacy
and cognition.";
Proc. Natl. Acad. Sci. U.S.A. 108:17213-17218(2011).
[23]
ACETYLATION [LARGE SCALE ANALYSIS] AT ASP-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[24]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND ASP-2, CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[25]
RETRACTION NOTICE OF PUBMED:19377461.
PubMed=24336203; DOI=10.1038/nature12896;
Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G.,
Kitagawa H., Kato S.;
"Retraction: GlcNAcylation of a histone methyltransferase in retinoic-
acid-induced granulopoiesis.";
Nature 505:574-574(2014).
[26]
INTERACTION WITH ERBB2.
PubMed=21555369; DOI=10.1158/0008-5472.CAN-10-3504;
Li L.Y., Chen H., Hsieh Y.H., Wang Y.N., Chu H.J., Chen Y.H.,
Chen H.Y., Chien P.J., Ma H.T., Tsai H.C., Lai C.C., Sher Y.P.,
Lien H.C., Tsai C.H., Hung M.C.;
"Nuclear ErbB2 enhances translation and cell growth by activating
transcription of ribosomal RNA genes.";
Cancer Res. 71:4269-4279(2011).
[27]
METHYLATION AT LYS-84, AND DEMETHYLATION BY ALKBH4.
PubMed=23673617; DOI=10.1038/ncomms2863;
Li M.M., Nilsen A., Shi Y., Fusser M., Ding Y.H., Fu Y., Liu B.,
Niu Y., Wu Y.S., Huang C.M., Olofsson M., Jin K.X., Lv Y., Xu X.Z.,
He C., Dong M.Q., Rendtlew Danielsen J.M., Klungland A., Yang Y.G.;
"ALKBH4-dependent demethylation of actin regulates actomyosin
dynamics.";
Nat. Commun. 4:1832-1832(2013).
[28]
ACETYLATION [LARGE SCALE ANALYSIS] AT ASP-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[29]
CROSS-LINK BY V.CHOLERAE TOXIN RTXA (MICROBIAL INFECTION).
PubMed=26228148; DOI=10.1126/science.aab4090;
Heisler D.B., Kudryashova E., Grinevich D.O., Suarez C.,
Winkelman J.D., Birukov K.G., Kotha S.R., Parinandi N.L.,
Vavylonis D., Kovar D.R., Kudryashov D.S.;
"ACD toxin-produced actin oligomers poison formin-controlled actin
polymerization.";
Science 349:535-539(2015).
[30]
INTERACTION WITH FAM107A.
PubMed=28604741; DOI=10.1038/onc.2017.181;
Mu P., Akashi T., Lu F., Kishida S., Kadomatsu K.;
"A novel nuclear complex of DRR1, F-actin and COMMD1 involved in NF-
kappaB degradation and cell growth suppression in neuroblastoma.";
Oncogene 36:5745-5756(2017).
[31]
ACETYLATION AT ASP-2.
PubMed=30028079; DOI=10.1111/febs.14605;
Wiame E., Tahay G., Tyteca D., Vertommen D., Stroobant V.,
Bommer G.T., Van Schaftingen E.;
"NAT6 acetylates the N-terminus of different forms of actin.";
FEBS J. 285:3299-3316(2018).
[32]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=29925947; DOI=10.1038/s41586-018-0237-5;
Schrank B.R., Aparicio T., Li Y., Chang W., Chait B.T.,
Gundersen G.G., Gottesman M.E., Gautier J.;
"Nuclear ARP2/3 drives DNA break clustering for homology-directed
repair.";
Nature 559:61-66(2018).
[33]
FUNCTION, AND ACETYLATION AT ASP-2.
PubMed=29581253; DOI=10.1073/pnas.1718336115;
Drazic A., Aksnes H., Marie M., Boczkowska M., Varland S.,
Timmerman E., Foyn H., Glomnes N., Rebowski G., Impens F., Gevaert K.,
Dominguez R., Arnesen T.;
"NAA80 is actin's N-terminal acetyltransferase and regulates
cytoskeleton assembly and cell motility.";
Proc. Natl. Acad. Sci. U.S.A. 115:4399-4404(2018).
[34]
VARIANT DJO TRP-183, AND CHARACTERIZATION OF VARIANT DJO TRP-183.
PubMed=16685646; DOI=10.1086/504271;
Procaccio V., Salazar G., Ono S., Styers M.L., Gearing M., Davila A.,
Jimenez R., Juncos J., Gutekunst C.-A., Meroni G., Fontanella B.,
Sontag E., Sontag J.-M., Faundez V., Wainer B.H.;
"A mutation of beta -actin that alters depolymerization dynamics is
associated with autosomal dominant developmental malformations,
deafness, and dystonia.";
Am. J. Hum. Genet. 78:947-960(2006).
[35]
VARIANTS BRWS1 ASP-12; VAL-65; CYS-196 AND HIS-196.
PubMed=22366783; DOI=10.1038/ng.1091;
Riviere J.B., van Bon B.W., Hoischen A., Kholmanskikh S.S.,
O'Roak B.J., Gilissen C., Gijsen S., Sullivan C.T., Christian S.L.,
Abdul-Rahman O.A., Atkin J.F., Chassaing N., Drouin-Garraud V.,
Fry A.E., Fryns J.P., Gripp K.W., Kempers M., Kleefstra T.,
Mancini G.M., Nowaczyk M.J., van Ravenswaaij-Arts C.M., Roscioli T.,
Marble M., Rosenfeld J.A., Siu V.M., de Vries B.B., Shendure J.,
Verloes A., Veltman J.A., Brunner H.G., Ross M.E., Pilz D.T.,
Dobyns W.B.;
"De novo mutations in the actin genes ACTB and ACTG1 cause Baraitser-
Winter syndrome.";
Nat. Genet. 44:440-444(2012).
-!- FUNCTION: Actin is a highly conserved protein that polymerizes to
produce filaments that form cross-linked networks in the cytoplasm
of cells (PubMed:29581253). Actin exists in both monomeric (G-
actin) and polymeric (F-actin) forms, both forms playing key
functions, such as cell motility and contraction
(PubMed:29581253). In addition to their role in the cytoplasmic
cytoskeleton, G- and F-actin also localize in the nucleus, and
regulate gene transcription and motility and repair of damaged DNA
(PubMed:29925947). {ECO:0000269|PubMed:29581253,
ECO:0000269|PubMed:29925947}.
-!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
structural filament (F-actin) in the form of a two-stranded helix
(PubMed:28604741, PubMed:16685646). Each actin can bind to 4
others (PubMed:28604741, PubMed:16685646). Identified in a
IGF2BP1-dependent mRNP granule complex containing untranslated
mRNAs (PubMed:17289661). Component of the BAF complex, which
includes at least actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2,
SMARCA4/BRG1, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57
SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more
of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C
(PubMed:18765789). In muscle cells, the BAF complex also contains
DPF3 (PubMed:18765789). Found in a complex with XPO6, Ran, ACTB
and PFN1 (PubMed:14592989). Interacts with XPO6 and EMD
(PubMed:15328537). Interacts with ERBB2 (PubMed:21555369).
Interacts with GCSAM (PubMed:17823310). Interacts with TBC1D21 (By
similarity). Interacts with CPNE1 (via VWFA domain) and CPNE4 (via
VWFA domain) (By similarity). Interacts with DHX9 (via C-
terminus); this interaction is direct and mediates the attachment
to nuclear ribonucleoprotein complexes (PubMed:11687588).
Interacts with FAM107A (PubMed:21969592, PubMed:28604741).
{ECO:0000250|UniProtKB:P60710, ECO:0000269|PubMed:11687588,
ECO:0000269|PubMed:14592989, ECO:0000269|PubMed:15328537,
ECO:0000269|PubMed:16685646, ECO:0000269|PubMed:17289661,
ECO:0000269|PubMed:17823310, ECO:0000269|PubMed:18765789,
ECO:0000269|PubMed:21555369, ECO:0000269|PubMed:21969592,
ECO:0000269|PubMed:28604741}.
-!- INTERACTION:
Self; NbExp=12; IntAct=EBI-353944, EBI-353944;
P63261:ACTG1; NbExp=12; IntAct=EBI-353944, EBI-351292;
P08413:Camk2b (xeno); NbExp=4; IntAct=EBI-353944, EBI-916155;
P40123:CAP2; NbExp=4; IntAct=EBI-353944, EBI-1051165;
P23528:CFL1; NbExp=6; IntAct=EBI-353944, EBI-352733;
Q549N0:CFL2; NbExp=3; IntAct=EBI-353944, EBI-10201319;
Q9Y281:CFL2; NbExp=8; IntAct=EBI-353944, EBI-351218;
P60981:DSTN; NbExp=6; IntAct=EBI-353944, EBI-745191;
P50402:EMD; NbExp=2; IntAct=EBI-353944, EBI-489887;
P04626:ERBB2; NbExp=10; IntAct=EBI-353944, EBI-641062;
Q8TCJ0-2:FBXO25; NbExp=3; IntAct=EBI-353944, EBI-6264551;
P11142:HSPA8; NbExp=2; IntAct=EBI-353944, EBI-351896;
Q8K4J6:Mkl1 (xeno); NbExp=3; IntAct=EBI-353944, EBI-8291665;
O14950:MYL12B; NbExp=3; IntAct=EBI-353944, EBI-1642165;
P14598:NCF1; NbExp=3; IntAct=EBI-353944, EBI-395044;
P29474:NOS3; NbExp=3; IntAct=EBI-353944, EBI-1391623;
Q92636:NSMAF; NbExp=2; IntAct=EBI-353944, EBI-2947053;
P07737:PFN1; NbExp=2; IntAct=EBI-353944, EBI-713780;
P37802:TAGLN2; NbExp=3; IntAct=EBI-353944, EBI-1056740;
Q9BSI4:TINF2; NbExp=2; IntAct=EBI-353944, EBI-717399;
Q96HA8:WDYHV1; NbExp=3; IntAct=EBI-353944, EBI-741158;
P63104:YWHAZ; NbExp=3; IntAct=EBI-353944, EBI-347088;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:11687588, ECO:0000269|PubMed:17289661}.
Nucleus {ECO:0000269|PubMed:11687588,
ECO:0000269|PubMed:29925947}. Note=Localized in cytoplasmic mRNP
granules containing untranslated mRNAs.
{ECO:0000269|PubMed:17289661}.
-!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
-!- PTM: Oxidation of Met-44 and Met-47 by MICALs (MICAL1, MICAL2 or
MICAL3) to form methionine sulfoxide promotes actin filament
depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form.
The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promote
actin repolymerization. {ECO:0000250|UniProtKB:P60710}.
-!- PTM: Monomethylation at Lys-84 (K84me1) regulates actin-myosin
interaction and actomyosin-dependent processes (PubMed:23673617).
Demethylation by ALKBH4 is required for maintaining actomyosin
dynamics supporting normal cleavage furrow ingression during
cytokinesis and cell migration (PubMed:23673617).
{ECO:0000269|PubMed:23673617}.
-!- PTM: Actin, cytoplasmic 1, N-terminally processed: N-terminal
acetylation by NAA80 affects actin filament depolymerization and
elongation, including elongation driven by formins
(PubMed:29581253). In contrast, filament nucleation by the Arp2/3
complex is not affected (PubMed:29581253).
{ECO:0000269|PubMed:29581253}.
-!- PTM: (Microbial infection) Monomeric actin is cross-linked by
V.cholerae toxins RtxA and VgrG1 in case of infection: bacterial
toxins mediate the cross-link between Lys-50 of one monomer and
Glu-270 of another actin monomer, resulting in formation of highly
toxic actin oligomers that cause cell rounding (PubMed:19015515).
The toxin can be highly efficient at very low concentrations by
acting on formin homology family proteins: toxic actin oligomers
bind with high affinity to formins and adversely affect both
nucleation and elongation abilities of formins, causing their
potent inhibition in both profilin-dependent and independent
manners (PubMed:26228148). {ECO:0000305|PubMed:19015515,
ECO:0000305|PubMed:26228148}.
-!- DISEASE: Dystonia, juvenile-onset (DJO) [MIM:607371]: A form of
dystonia with juvenile onset. Dystonia is defined by the presence
of sustained involuntary muscle contraction, often leading to
abnormal postures. Patients with juvenile-onset dystonia manifest
progressive, generalized, dopa-unresponsive dystonia,
developmental malformations and sensory hearing loss.
{ECO:0000269|PubMed:16685646}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Baraitser-Winter syndrome 1 (BRWS1) [MIM:243310]: A rare
developmental disorder characterized by the combination of
congenital ptosis, high-arched eyebrows, hypertelorism, ocular
colobomata, and a brain malformation consisting of anterior-
predominant lissencephaly. Other typical features include
postnatal short stature and microcephaly, intellectual disability,
seizures, and hearing loss. {ECO:0000269|PubMed:22366783}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms,
alpha, beta and gamma have been identified. The alpha actins are
found in muscle tissues and are a major constituent of the
contractile apparatus. The beta and gamma actins coexist in most
cell types as components of the cytoskeleton and as mediators of
internal cell motility. {ECO:0000305}.
-!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
-!- CAUTION: Was originally thought to be part of the MLL5-L complex,
at least composed of KMT2E, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1,
ACTB and OGT (PubMed:19377461). However, the corresponding article
has been retracted (PubMed:24336203).
{ECO:0000269|PubMed:19377461, ECO:0000269|PubMed:24336203}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/ACTBID42959ch7p22.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/actb/";
-!- WEB RESOURCE: Name=Mendelian genes actin, beta (ACTB); Note=Leiden
Open Variation Database (LOVD);
URL="http://www.lovd.nl/ACTB";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X00351; CAA25099.1; -; mRNA.
EMBL; M10277; AAA51567.1; -; Genomic_DNA.
EMBL; X63432; CAA45026.1; -; mRNA.
EMBL; AY582799; AAS79319.1; -; Genomic_DNA.
EMBL; AC006483; AAP22343.1; -; Genomic_DNA.
EMBL; BC001301; AAH01301.1; -; mRNA.
EMBL; BC002409; AAH02409.1; -; mRNA.
EMBL; BC004251; AAH04251.1; -; mRNA.
EMBL; BC008633; AAH08633.1; -; mRNA.
EMBL; BC012854; AAH12854.1; -; mRNA.
EMBL; BC013380; AAH13380.1; -; mRNA.
EMBL; BC014861; AAH14861.1; -; mRNA.
EMBL; BC016045; AAH16045.1; -; mRNA.
EMBL; V00478; CAA23745.1; -; mRNA.
CCDS; CCDS5341.1; -.
PIR; A25168; ATHUB.
RefSeq; NP_001092.1; NM_001101.3.
UniGene; Hs.520640; -.
PDB; 3BYH; EM; 12.00 A; A=2-375.
PDB; 3D2U; X-ray; 2.21 A; C/G=170-178.
PDB; 3J82; EM; 7.70 A; B/C/D=2-375.
PDB; 3LUE; EM; -; A/B/C/D/E/F/G/H/I/J=2-375.
PDB; 6ANU; EM; 7.00 A; A/B/C/D/E/F=1-375.
PDBsum; 3BYH; -.
PDBsum; 3D2U; -.
PDBsum; 3J82; -.
PDBsum; 3LUE; -.
PDBsum; 6ANU; -.
ProteinModelPortal; P60709; -.
SMR; P60709; -.
BioGrid; 106575; 318.
ComplexPortal; CPX-1164; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant.
ComplexPortal; CPX-1194; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant.
ComplexPortal; CPX-1195; Embryonic stem cell-specific SWI/SNF ATP-dependent chromatin remodeling complex.
ComplexPortal; CPX-1196; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B variant.
ComplexPortal; CPX-1199; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A variant.
ComplexPortal; CPX-1201; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
ComplexPortal; CPX-1202; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
ComplexPortal; CPX-1203; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
ComplexPortal; CPX-1204; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
ComplexPortal; CPX-1205; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
ComplexPortal; CPX-1206; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
ComplexPortal; CPX-1207; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant.
ComplexPortal; CPX-1209; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
ComplexPortal; CPX-1210; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant.
ComplexPortal; CPX-1211; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
ComplexPortal; CPX-1212; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
ComplexPortal; CPX-1213; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
ComplexPortal; CPX-1215; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
ComplexPortal; CPX-1216; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
ComplexPortal; CPX-1217; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
ComplexPortal; CPX-1218; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
ComplexPortal; CPX-1219; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
ComplexPortal; CPX-1220; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
ComplexPortal; CPX-1221; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
ComplexPortal; CPX-1222; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
ComplexPortal; CPX-1223; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
ComplexPortal; CPX-1224; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
ComplexPortal; CPX-1225; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant.
ComplexPortal; CPX-1226; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
ComplexPortal; CPX-1227; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant.
ComplexPortal; CPX-1228; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
ComplexPortal; CPX-978; NuA4 histone acetyltransferase complex.
CORUM; P60709; -.
DIP; DIP-29686N; -.
IntAct; P60709; 220.
MINT; P60709; -.
STRING; 9606.ENSP00000349960; -.
ChEMBL; CHEMBL2062353; -.
CarbonylDB; P60709; -.
iPTMnet; P60709; -.
PhosphoSitePlus; P60709; -.
SwissPalm; P60709; -.
BioMuta; ACTB; -.
DMDM; 46397333; -.
DOSAC-COBS-2DPAGE; P60709; -.
REPRODUCTION-2DPAGE; P60709; -.
SWISS-2DPAGE; P60709; -.
UCD-2DPAGE; P60709; -.
EPD; P60709; -.
PaxDb; P60709; -.
PeptideAtlas; P60709; -.
PRIDE; P60709; -.
ProteomicsDB; 57224; -.
TopDownProteomics; P60709; -.
DNASU; 60; -.
Ensembl; ENST00000331789; ENSP00000349960; ENSG00000075624.
Ensembl; ENST00000493945; ENSP00000494269; ENSG00000075624.
Ensembl; ENST00000646664; ENSP00000494750; ENSG00000075624.
GeneID; 60; -.
KEGG; hsa:60; -.
CTD; 60; -.
DisGeNET; 60; -.
EuPathDB; HostDB:ENSG00000075624.13; -.
GeneCards; ACTB; -.
HGNC; HGNC:132; ACTB.
HPA; CAB002621; -.
HPA; HPA041264; -.
HPA; HPA041271; -.
MalaCards; ACTB; -.
MIM; 102630; gene.
MIM; 243310; phenotype.
MIM; 607371; phenotype.
neXtProt; NX_P60709; -.
OpenTargets; ENSG00000075624; -.
Orphanet; 2995; Baraitser-Winter cerebrofrontofacial syndrome.
Orphanet; 64755; Becker nevus syndrome.
Orphanet; 79107; Developmental malformations-deafness-dystonia syndrome.
PharmGKB; PA24457; -.
eggNOG; KOG0676; Eukaryota.
eggNOG; COG5277; LUCA.
GeneTree; ENSGT00760000118957; -.
HOVERGEN; HBG003771; -.
InParanoid; P60709; -.
KO; K05692; -.
OMA; YKCDLDI; -.
OrthoDB; EOG091G08LD; -.
PhylomeDB; P60709; -.
TreeFam; TF354237; -.
Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
Reactome; R-HSA-190873; Gap junction degradation.
Reactome; R-HSA-196025; Formation of annular gap junctions.
Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-HSA-3214847; HATs acetylate histones.
Reactome; R-HSA-389957; Prefoldin mediated transfer of substrate to CCT/TriC.
Reactome; R-HSA-390450; Folding of actin by CCT/TriC.
Reactome; R-HSA-3928662; EPHB-mediated forward signaling.
Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
Reactome; R-HSA-418990; Adherens junctions interactions.
Reactome; R-HSA-437239; Recycling pathway of L1.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-445095; Interaction between L1 and Ankyrins.
Reactome; R-HSA-446353; Cell-extracellular matrix interactions.
Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
Reactome; R-HSA-5626467; RHO GTPases activate IQGAPs.
Reactome; R-HSA-5663213; RHO GTPases Activate WASPs and WAVEs.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-5674135; MAP2K and MAPK activation.
Reactome; R-HSA-5689603; UCH proteinases.
Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants.
Reactome; R-HSA-6802948; Signaling by high-kinase activity BRAF mutants.
Reactome; R-HSA-6802949; Signaling by RAS mutants.
Reactome; R-HSA-6802952; Signaling by BRAF and RAF fusions.
Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
SignaLink; P60709; -.
ChiTaRS; ACTB; human.
EvolutionaryTrace; P60709; -.
GeneWiki; Beta-actin; -.
GenomeRNAi; 60; -.
PRO; PR:P60709; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000075624; Expressed in 230 organ(s), highest expression level in popliteal artery.
CleanEx; HS_ACTB; -.
ExpressionAtlas; P60709; baseline and differential.
Genevisible; P60709; HS.
GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL.
GO; GO:0005856; C:cytoskeleton; IDA:ARUK-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0097433; C:dense body; ISS:AgBase.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; HDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:AgBase.
GO; GO:0098871; C:postsynaptic actin cytoskeleton; IDA:SynGO.
GO; GO:0098793; C:presynapse; TAS:ARUK-UCL.
GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0031982; C:vesicle; HDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0019894; F:kinesin binding; IPI:UniProtKB.
GO; GO:0050998; F:nitric-oxide synthase binding; IPI:BHF-UCL.
GO; GO:0019901; F:protein kinase binding; IPI:ARUK-UCL.
GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:UniProtKB.
GO; GO:0098973; F:structural constituent of postsynaptic actin cytoskeleton; IDA:SynGO.
GO; GO:0030957; F:Tat protein binding; IPI:BHF-UCL.
GO; GO:0043044; P:ATP-dependent chromatin remodeling; HDA:UniProtKB.
GO; GO:0034329; P:cell junction assembly; TAS:Reactome.
GO; GO:0048870; P:cell motility; IMP:UniProtKB.
GO; GO:0072749; P:cellular response to cytochalasin B; IMP:UniProtKB.
GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0032091; P:negative regulation of protein binding; ISS:ARUK-UCL.
GO; GO:0070527; P:platelet aggregation; HMP:UniProtKB.
GO; GO:0045815; P:positive regulation of gene expression, epigenetic; TAS:Reactome.
GO; GO:0051623; P:positive regulation of norepinephrine uptake; TAS:ARUK-UCL.
GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; IDA:SynGO.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; ISS:ARUK-UCL.
GO; GO:0051621; P:regulation of norepinephrine uptake; IGI:ARUK-UCL.
GO; GO:1903076; P:regulation of protein localization to plasma membrane; IMP:ARUK-UCL.
GO; GO:0022898; P:regulation of transmembrane transporter activity; IGI:ARUK-UCL.
GO; GO:0001895; P:retina homeostasis; HEP:UniProtKB.
GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
InterPro; IPR004000; Actin.
InterPro; IPR020902; Actin/actin-like_CS.
InterPro; IPR004001; Actin_CS.
PANTHER; PTHR11937; PTHR11937; 1.
Pfam; PF00022; Actin; 1.
PRINTS; PR00190; ACTIN.
SMART; SM00268; ACTIN; 1.
PROSITE; PS00406; ACTINS_1; 1.
PROSITE; PS00432; ACTINS_2; 1.
PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Complete proteome; Cytoplasm;
Cytoskeleton; Deafness; Direct protein sequencing; Disease mutation;
Dystonia; Isopeptide bond; Mental retardation; Methylation;
Nucleotide-binding; Nucleus; Oxidation; Polymorphism;
Reference proteome; Ubl conjugation.
CHAIN 1 375 Actin, cytoplasmic 1.
/FTId=PRO_0000367073.
INIT_MET 1 1 Removed; alternate.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:12665801,
ECO:0000269|Ref.8}.
CHAIN 2 375 Actin, cytoplasmic 1, N-terminally
processed. {ECO:0000305|PubMed:29581253}.
/FTId=PRO_0000000771.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 2 2 N-acetylaspartate; in Actin, cytoplasmic
1, N-terminally processed.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:29581253,
ECO:0000269|PubMed:30028079,
ECO:0000269|Ref.8}.
MOD_RES 44 44 Methionine (R)-sulfoxide.
{ECO:0000250|UniProtKB:P60710}.
MOD_RES 47 47 Methionine (R)-sulfoxide.
{ECO:0000250|UniProtKB:P60710}.
MOD_RES 73 73 Tele-methylhistidine.
{ECO:0000250|UniProtKB:P60710}.
MOD_RES 84 84 N6-methyllysine.
{ECO:0000269|PubMed:23673617}.
CROSSLNK 50 50 (Microbial infection) Isoglutamyl lysine
isopeptide (Lys-Glu) (interchain with E-
270); by Vibrio toxins RtxA and VgrG1.
{ECO:0000305|PubMed:19015515}.
CROSSLNK 270 270 (Microbial infection) Isoglutamyl lysine
isopeptide (Glu-Lys) (interchain with K-
50); by Vibrio toxins RtxA and VgrG1.
{ECO:0000305|PubMed:19015515}.
VARIANT 12 12 N -> D (in BRWS1; dbSNP:rs281875331).
{ECO:0000269|PubMed:22366783}.
/FTId=VAR_067810.
VARIANT 65 65 L -> V (in BRWS1; dbSNP:rs281875332).
{ECO:0000269|PubMed:22366783}.
/FTId=VAR_067811.
VARIANT 183 183 R -> W (in DJO; modifies cell response to
latrunculin A; dbSNP:rs104894003).
{ECO:0000269|PubMed:16685646}.
/FTId=VAR_030026.
VARIANT 196 196 R -> C (in BRWS1; dbSNP:rs281875333).
{ECO:0000269|PubMed:22366783}.
/FTId=VAR_067812.
VARIANT 196 196 R -> H (in BRWS1; dbSNP:rs281875334).
{ECO:0000269|PubMed:22366783}.
/FTId=VAR_067813.
VARIANT 243 243 P -> L (in dbSNP:rs11546899).
/FTId=VAR_048185.
CONFLICT 97 97 A -> P (in Ref. 6; AAH16045).
{ECO:0000305}.
CONFLICT 116 116 R -> L (in Ref. 6; AAH12854).
{ECO:0000305}.
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


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