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Actin, cytoplasmic 2 (Gamma-actin) [Cleaved into: Actin, cytoplasmic 2, N-terminally processed]

 ACTG_HUMAN              Reviewed;         375 AA.
P63261; A8K7C2; P02571; P14104; P99022; Q5U032; Q96E67;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
25-OCT-2017, entry version 161.
RecName: Full=Actin, cytoplasmic 2;
AltName: Full=Gamma-actin;
Contains:
RecName: Full=Actin, cytoplasmic 2, N-terminally processed;
Name=ACTG1; Synonyms=ACTG;
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=3737401; DOI=10.1093/nar/14.13.5275;
Erba H.P., Gunning P., Kedes L.;
"Nucleotide sequence of the human gamma cytoskeletal actin mRNA:
anomalous evolution of vertebrate non-muscle actin genes.";
Nucleic Acids Res. 14:5275-5294(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2837653; DOI=10.1128/MCB.8.4.1775;
Erba H.P., Eddy R., Shows T., Kedes L., Gunning P.;
"Structure, chromosome location, and expression of the human gamma-
actin gene: differential evolution, location, and expression of the
cytoskeletal beta- and gamma-actin genes.";
Mol. Cell. Biol. 8:1775-1789(1988).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=B-cell, Eye, Lung, Ovary, Placenta, Skin, and Uterus;
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).
[6]
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).
[7]
PROTEIN SEQUENCE OF 2-18; 29-37; 40-50; 85-113; 148-177; 184-191;
197-206; 239-254; 292-312 AND 316-326, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT GLU-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (JUN-2005) to UniProtKB.
[8]
PROTEIN SEQUENCE OF 2-116; 119-210; 216-254 AND 291-372, CLEAVAGE OF
INITIATOR METHIONINE, ACETYLATION AT GLU-2, METHYLATION AT HIS-73, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.,
Dozynkiewicz M., Norman J.C.;
Submitted (JUN-2009) to UniProtKB.
[9]
PROTEIN SEQUENCE OF 29-39; 85-113; 239-254 AND 292-312, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Afjehi-Sadat L.;
Submitted (MAR-2007) to UniProtKB.
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 144-375.
PubMed=3472224; DOI=10.1073/pnas.84.9.2575;
Chou C.C., Davis R.C., Fuller M.L., Slovin J.P., Wong A., Wright J.,
Kania S., Shaked R., Gatti R.A., Salser W.A.;
"Gamma-actin: unusual mRNA 3'-untranslated sequence conservation and
amino acid substitutions that may be cancer related.";
Proc. Natl. Acad. Sci. U.S.A. 84:2575-2579(1987).
[11]
CROSS-LINK 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).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT GLU-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).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND GLU-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).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND GLU-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).
[15]
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).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT GLU-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).
[17]
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).
[18]
VARIANTS DFNA20 ILE-89; MET-118; LEU-264 AND ALA-332.
PubMed=13680526; DOI=10.1086/379286;
Zhu M., Yang T., Wei S., DeWan A.T., Morell R.J., Elfenbein J.L.,
Fisher R.A., Leal S.M., Smith R.J.H., Friderici K.H.;
"Mutations in the gamma-actin gene (ACTG1) are associated with
dominant progressive deafness (DFNA20/26).";
Am. J. Hum. Genet. 73:1082-1091(2003).
[19]
VARIANT DFNA20 ILE-278.
PubMed=14684684; DOI=10.1136/jmg.40.12.879;
van Wijk E., Krieger E., Kemperman M.H., De Leenheer E.M.R.,
Huygen P.L.M., Cremers C.W.R.J., Cremers F.P.M., Kremer H.;
"A mutation in the gamma actin 1 (ACTG1) gene causes autosomal
dominant hearing loss (DFNA20/26).";
J. Med. Genet. 40:879-884(2003).
[20]
VARIANT DFNA20 ALA-370, AND CHARACTERIZATION OF VARIANT DFNA20
ALA-370.
PubMed=16773128; DOI=10.1038/sj.ejhg.5201670;
Rendtorff N.D., Zhu M., Fagerheim T., Antal T.L., Jones M.,
Teslovich T.M., Gillanders E.M., Barmada M., Teig E., Trent J.M.,
Friderici K.H., Stephan D.A., Tranebjaerg L.;
"A novel missense mutation in ACTG1 causes dominant deafness in a
Norwegian DFNA20/26 family, but ACTG1 mutations are not frequent among
families with hereditary hearing impairment.";
Eur. J. Hum. Genet. 14:1097-1105(2006).
[21]
VARIANT DFNA20 VAL-122.
PubMed=18804074; DOI=10.1016/S1673-8527(08)60075-2;
Liu P., Li H., Ren X., Mao H., Zhu Q., Zhu Z., Yang R., Yuan W.,
Liu J., Wang Q., Liu M.;
"Novel ACTG1 mutation causing autosomal dominant non-syndromic hearing
impairment in a Chinese family.";
J. Genet. Genomics 35:553-558(2008).
[22]
VARIANTS DFNA20 ASN-118 AND LYS-241.
PubMed=19477959; DOI=10.1093/hmg/ddp249;
Morin M., Bryan K.E., Mayo-Merino F., Goodyear R., Mencia A.,
Modamio-Hoybjor S., del Castillo I., Cabalka J.M., Richardson G.,
Moreno F., Rubenstein P.A., Moreno-Pelayo M.A.;
"In vivo and in vitro effects of two novel gamma-actin (ACTG1)
mutations that cause DFNA20/26 hearing impairment.";
Hum. Mol. Genet. 18:3075-3089(2009).
[23]
VARIANTS BRWS2 ILE-120; VAL-135; PHE-155; LYS-203; TRP-254 AND
TRP-256.
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: Actins are highly conserved proteins that are involved
in various types of cell motility and are ubiquitously expressed
in all eukaryotic cells.
-!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
structural filament (F-actin) in the form of a two-stranded helix.
Each actin can bind to 4 others.
-!- INTERACTION:
Self; NbExp=8; IntAct=EBI-351292, EBI-351292;
P60709:ACTB; NbExp=12; IntAct=EBI-351292, EBI-353944;
P40123:CAP2; NbExp=11; IntAct=EBI-351292, EBI-1051165;
O60826:CCDC22; NbExp=3; IntAct=EBI-351292, EBI-3943153;
P23528:CFL1; NbExp=8; IntAct=EBI-351292, EBI-352733;
Q549N0:CFL2; NbExp=5; IntAct=EBI-351292, EBI-10201319;
Q9Y281:CFL2; NbExp=8; IntAct=EBI-351292, EBI-351218;
P60981:DSTN; NbExp=7; IntAct=EBI-351292, EBI-745191;
Q08426:EHHADH; NbExp=3; IntAct=EBI-351292, EBI-2339219;
P40692:MLH1; NbExp=7; IntAct=EBI-351292, EBI-744248;
Q1KLZ0:PS1TP5BP1; NbExp=3; IntAct=EBI-351292, EBI-9978131;
Q96HA8:WDYHV1; NbExp=5; IntAct=EBI-351292, EBI-741158;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
-!- PTM: The methylhistidine determined by Bienvenut et al is assumed
to be the tele-methylhistidine isomer by similarity to the mouse
ortholog.
-!- 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 (By similarity). {ECO:0000250}.
-!- PTM: Monomethylation at Lys-84 (K84me1) regulates actin-myosin
interaction and actomyosin-dependent processes. Demethylation by
ALKBH4 is required for maintaining actomyosin dynamics supporting
normal cleavage furrow ingression during cytokinesis and cell
migration. {ECO:0000269|PubMed:23673617}.
-!- 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: Deafness, autosomal dominant, 20 (DFNA20) [MIM:604717]: A
form of non-syndromic sensorineural hearing loss. Sensorineural
deafness results from damage to the neural receptors of the inner
ear, the nerve pathways to the brain, or the area of the brain
that receives sound information. {ECO:0000269|PubMed:13680526,
ECO:0000269|PubMed:14684684, ECO:0000269|PubMed:16773128,
ECO:0000269|PubMed:18804074, ECO:0000269|PubMed:19477959}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Baraitser-Winter syndrome 2 (BRWS2) [MIM:614583]: 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.
-!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Mendelian genes actin, gamma 1 (ACTG1);
Note=Leiden Open Variation Database (LOVD);
URL="http://www.lovd.nl/ACTG1";
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EMBL; X04098; CAA27723.1; -; mRNA.
EMBL; M19283; AAA51579.1; -; Genomic_DNA.
EMBL; AK291937; BAF84626.1; -; mRNA.
EMBL; BT019856; AAV38659.1; -; mRNA.
EMBL; BC000292; AAH00292.1; -; mRNA.
EMBL; BC001920; AAH01920.1; -; mRNA.
EMBL; BC007442; AAH07442.1; -; mRNA.
EMBL; BC009848; AAH09848.1; -; mRNA.
EMBL; BC010999; AAH10999.1; -; mRNA.
EMBL; BC012050; AAH12050.1; -; mRNA.
EMBL; BC015005; AAH15005.1; -; mRNA.
EMBL; BC015695; AAH15695.1; -; mRNA.
EMBL; BC015779; AAH15779.1; -; mRNA.
EMBL; BC018774; AAH18774.1; -; mRNA.
EMBL; BC053572; AAH53572.1; -; mRNA.
EMBL; M16247; AAA51580.1; -; mRNA.
CCDS; CCDS11782.1; -.
PIR; A28098; ATHUG.
PIR; JC5818; JC5818.
RefSeq; NP_001186883.1; NM_001199954.1.
RefSeq; NP_001605.1; NM_001614.3.
UniGene; Hs.514581; -.
UniGene; Hs.713764; -.
PDB; 5JLH; EM; 3.90 A; A/B/C/D/E=2-375.
PDBsum; 5JLH; -.
ProteinModelPortal; P63261; -.
SMR; P63261; -.
BioGrid; 106586; 143.
CORUM; P63261; -.
IntAct; P63261; 77.
MINT; MINT-4998686; -.
STRING; 9606.ENSP00000331514; -.
iPTMnet; P63261; -.
PhosphoSitePlus; P63261; -.
SwissPalm; P63261; -.
BioMuta; ACTG1; -.
DMDM; 54036678; -.
DOSAC-COBS-2DPAGE; P63261; -.
OGP; P63261; -.
REPRODUCTION-2DPAGE; P63261; -.
SWISS-2DPAGE; P63261; -.
EPD; P63261; -.
MaxQB; P63261; -.
PaxDb; P63261; -.
PeptideAtlas; P63261; -.
PRIDE; P63261; -.
TopDownProteomics; P63261; -.
DNASU; 71; -.
Ensembl; ENST00000331925; ENSP00000331514; ENSG00000184009.
Ensembl; ENST00000573283; ENSP00000458435; ENSG00000184009.
Ensembl; ENST00000575087; ENSP00000459124; ENSG00000184009.
Ensembl; ENST00000575842; ENSP00000458162; ENSG00000184009.
Ensembl; ENST00000576544; ENSP00000461672; ENSG00000184009.
Ensembl; ENST00000615544; ENSP00000477968; ENSG00000184009.
GeneID; 71; -.
KEGG; hsa:71; -.
UCSC; uc002kak.3; human.
CTD; 71; -.
DisGeNET; 71; -.
EuPathDB; HostDB:ENSG00000184009.9; -.
GeneCards; ACTG1; -.
GeneReviews; ACTG1; -.
H-InvDB; HIX0001479; -.
H-InvDB; HIX0199868; -.
HGNC; HGNC:144; ACTG1.
HPA; HPA041264; -.
HPA; HPA041271; -.
MalaCards; ACTG1; -.
MIM; 102560; gene.
MIM; 604717; phenotype.
MIM; 614583; phenotype.
neXtProt; NX_P63261; -.
OpenTargets; ENSG00000184009; -.
Orphanet; 90635; Autosomal dominant non-syndromic sensorineural deafness type DFNA.
Orphanet; 2995; Baraitser-Winter syndrome.
PharmGKB; PA24468; -.
eggNOG; KOG0676; Eukaryota.
eggNOG; COG5277; LUCA.
GeneTree; ENSGT00760000118957; -.
HOVERGEN; HBG003771; -.
InParanoid; P63261; -.
KO; K05692; -.
OMA; ANGIHET; -.
OrthoDB; EOG091G08LD; -.
PhylomeDB; P63261; -.
TreeFam; TF354237; -.
Reactome; R-HSA-1445148; Translocation of 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-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-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-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.
SignaLink; P63261; -.
SIGNOR; P63261; -.
ChiTaRS; ACTG1; human.
GeneWiki; ACTG1; -.
GenomeRNAi; 71; -.
PMAP-CutDB; P63261; -.
PRO; PR:P63261; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000184009; -.
CleanEx; HS_ACTB; -.
CleanEx; HS_ACTG1; -.
ExpressionAtlas; P63261; baseline and differential.
Genevisible; P63261; HS.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; ISS:AgBase.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0097433; C:dense body; ISS:AgBase.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0031941; C:filamentous actin; IEA:Ensembl.
GO; GO:0005925; C:focal adhesion; ISS:AgBase.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0030016; C:myofibril; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:AgBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005200; F:structural constituent of cytoskeleton; IC:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0034329; P:cell junction assembly; TAS:Reactome.
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:0006928; P:movement of cell or subcellular component; TAS:UniProtKB.
GO; GO:0070527; P:platelet aggregation; IMP:UniProtKB.
GO; GO:0001895; P:retina homeostasis; IEP:UniProtKB.
GO; GO:0045214; P:sarcomere organization; IEA:Ensembl.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
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;
Isopeptide bond; Mental retardation; Methylation;
Non-syndromic deafness; Nucleotide-binding; Oxidation; Polymorphism;
Reference proteome.
CHAIN 1 375 Actin, cytoplasmic 2.
/FTId=PRO_0000367100.
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.7, ECO:0000269|Ref.8}.
CHAIN 2 375 Actin, cytoplasmic 2, N-terminally
processed.
/FTId=PRO_0000000831.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
MOD_RES 2 2 N-acetylglutamate; in Actin, cytoplasmic
2, N-terminally processed; partial.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712,
ECO:0000269|Ref.7, ECO:0000269|Ref.8}.
MOD_RES 44 44 Methionine (R)-sulfoxide. {ECO:0000250}.
MOD_RES 47 47 Methionine (R)-sulfoxide. {ECO:0000250}.
MOD_RES 73 73 Tele-methylhistidine.
{ECO:0000269|Ref.8}.
MOD_RES 84 84 N6-methyllysine.
{ECO:0000269|PubMed:23673617}.
CROSSLNK 50 50 Isoglutamyl lysine isopeptide (Lys-Glu)
(interchain with E-270); by Vibrio toxins
RtxA and VgrG1.
{ECO:0000250|UniProtKB:P60709}.
CROSSLNK 270 270 Isoglutamyl lysine isopeptide (Glu-Lys)
(interchain with K-50); by Vibrio toxins
RtxA and VgrG1.
{ECO:0000250|UniProtKB:P60709}.
VARIANT 89 89 T -> I (in DFNA20; dbSNP:rs28999111).
{ECO:0000269|PubMed:13680526}.
/FTId=VAR_032434.
VARIANT 118 118 K -> M (in DFNA20; dbSNP:rs104894544).
{ECO:0000269|PubMed:13680526}.
/FTId=VAR_032435.
VARIANT 118 118 K -> N (in DFNA20; dbSNP:rs267606630).
{ECO:0000269|PubMed:19477959}.
/FTId=VAR_067824.
VARIANT 120 120 T -> I (in BRWS2; dbSNP:rs281875325).
{ECO:0000269|PubMed:22366783}.
/FTId=VAR_067814.
VARIANT 122 122 I -> V (in DFNA20; dbSNP:rs281875330).
{ECO:0000269|PubMed:18804074}.
/FTId=VAR_067825.
VARIANT 135 135 A -> V (in BRWS2; dbSNP:rs11549190).
{ECO:0000269|PubMed:22366783}.
/FTId=VAR_067815.
VARIANT 155 155 S -> F (in BRWS2; dbSNP:rs281875326).
{ECO:0000269|PubMed:22366783}.
/FTId=VAR_067816.
VARIANT 160 160 T -> I (in dbSNP:rs11549206).
/FTId=VAR_048186.
VARIANT 203 203 T -> K (in BRWS2; dbSNP:rs281875327).
{ECO:0000269|PubMed:22366783}.
/FTId=VAR_067817.
VARIANT 241 241 E -> K (in DFNA20; dbSNP:rs267606631).
{ECO:0000269|PubMed:19477959}.
/FTId=VAR_067826.
VARIANT 254 254 R -> W (in BRWS2; dbSNP:rs281875328).
{ECO:0000269|PubMed:22366783}.
/FTId=VAR_067818.
VARIANT 256 256 R -> W (in BRWS2; dbSNP:rs281875329).
{ECO:0000269|PubMed:22366783}.
/FTId=VAR_067819.
VARIANT 264 264 P -> L (in DFNA20; dbSNP:rs104894546).
{ECO:0000269|PubMed:13680526}.
/FTId=VAR_032436.
VARIANT 278 278 T -> I (in DFNA20; dbSNP:rs28999112).
{ECO:0000269|PubMed:14684684}.
/FTId=VAR_032437.
VARIANT 332 332 P -> A (in DFNA20; dbSNP:rs104894545).
{ECO:0000269|PubMed:13680526}.
/FTId=VAR_032438.
VARIANT 370 370 V -> A (in DFNA20; restricts cell growth
at elevated temperature or under
hyperosmolar stress as measured in growth
assays with yeast expressing the
mutation; dbSNP:rs104894547).
{ECO:0000269|PubMed:16773128}.
/FTId=VAR_032439.
CONFLICT 316 316 E -> K (in Ref. 10; AAA51580).
{ECO:0000305}.
CONFLICT 344 344 S -> F (in Ref. 10; AAA51580).
{ECO:0000305}.
SEQUENCE 375 AA; 41793 MW; 54D08F986964EFD5 CRC64;
MEEEIAALVI 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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