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Actin, aortic smooth muscle (Alpha-actin-2) (Cell growth-inhibiting gene 46 protein)

 ACTA_HUMAN              Reviewed;         377 AA.
P62736; B2R8A4; P03996; P04108; Q6FI19;
23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 1.
25-OCT-2017, entry version 143.
RecName: Full=Actin, aortic smooth muscle;
AltName: Full=Alpha-actin-2;
AltName: Full=Cell growth-inhibiting gene 46 protein;
Flags: Precursor;
Name=ACTA2; Synonyms=ACTSA, ACTVS; ORFNames=GIG46;
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=2701935; DOI=10.1093/nar/17.4.1767;
Kamada S., Kakunaga T.;
"The nucleotide sequence of a human smooth muscle alpha-actin (aortic
type) cDNA.";
Nucleic Acids Res. 17:1767-1767(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2295650;
Reddy S., Ozgur K., Lu M., Chang W., Mohan S.R., Kumar C.C.,
Ruley H.E.;
"Structure of the human smooth muscle alpha-actin gene. Analysis of a
cDNA and 5' upstream region.";
J. Biol. Chem. 265:1683-1687(1990).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kim J.W.;
"Identification of a human cell growth inhibiting gene.";
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skeletal muscle;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=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).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-330.
PubMed=6330528; DOI=10.1128/MCB.4.6.1073;
Ueyama H., Hamada H., Battula N., Kakunaga T.;
"Structure of a human smooth muscle actin gene (aortic type) with a
unique intron site.";
Mol. Cell. Biol. 4:1073-1078(1984).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 331-377.
PubMed=2612915; DOI=10.1016/0378-1119(89)90520-9;
Kamada S., Nakano Y., Kakunaga T.;
"Structure of 3'-downstream segment of the human smooth muscle
(aortic-type) alpha-actin-encoding gene and isolation of the specific
DNA probe.";
Gene 84:455-462(1989).
[11]
INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x;
Leong W.F., Chow V.T.;
"Transcriptomic and proteomic analyses of rhabdomyosarcoma cells
reveal differential cellular gene expression in response to
enterovirus 71 infection.";
Cell. Microbiol. 8:565-580(2006).
[12]
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).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT GLU-3, CLEAVAGE OF PROPEPTIDE
[LARGE SCALE ANALYSIS] AFTER CYS-2, 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]
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]
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).
[16]
VARIANTS AAT6 THR-117; GLN-118; HIS-135; CYS-149; ALA-154; CYS-258;
HIS-258; GLY-292 AND ASN-353.
PubMed=17994018; DOI=10.1038/ng.2007.6;
Guo D.-C., Pannu H., Tran-Fadulu V., Papke C.L., Yu R.K., Avidan N.,
Bourgeois S., Estrera A.L., Safi H.J., Sparks E., Amor D., Ades L.,
McConnell V., Willoughby C.E., Abuelo D., Willing M., Lewis R.A.,
Kim D.H., Scherer S., Tung P.P., Ahn C., Buja L.M., Raman C.S.,
Shete S.S., Milewicz D.M.;
"Mutations in smooth muscle alpha-actin (ACTA2) lead to thoracic
aortic aneurysms and dissections.";
Nat. Genet. 39:1488-1493(2007).
[17]
VARIANTS AAT6 HIS-39; THR-117; GLN-118; CYS-149; ALA-154; GLN-185;
GLN-212; HIS-258; CYS-258; ASN-326 AND ASN-353.
PubMed=19409525; DOI=10.1016/j.ajhg.2009.04.007;
Guo D.-C., Papke C.L., Tran-Fadulu V., Regalado E.S., Avidan N.,
Johnson R.J., Kim D.H., Pannu H., Willing M.C., Sparks E.,
Pyeritz R.E., Singh M.N., Dalman R.L., Grotta J.C., Marian A.J.,
Boerwinkle E.A., Frazier L.Q., LeMaire S.A., Coselli J.S.,
Estrera A.L., Safi H.J., Veeraraghavan S., Muzny D.M., Wheeler D.A.,
Willerson J.T., Yu R.K., Shete S.S., Scherer S.E., Raman C.S.,
Buja L.M., Milewicz D.M.;
"Mutations in smooth muscle alpha-actin (ACTA2) cause coronary artery
disease, stroke, and Moyamoya disease, along with thoracic aortic
disease.";
Am. J. Hum. Genet. 84:617-627(2009).
[18]
VARIANTS AAT6 CYS-145; CYS-149 AND GLN-212, AND PREDISPOSITION TO A
VARIETY OF VASCULAR DISEASES.
PubMed=19639654; DOI=10.1002/humu.21081;
Morisaki H., Akutsu K., Ogino H., Kondo N., Yamanaka I., Tsutsumi Y.,
Yoshimuta T., Okajima T., Matsuda H., Minatoya K., Sasaki H.,
Tanaka H., Ishibashi-Ueda H., Morisaki T.;
"Mutation of ACTA2 gene as an important cause of familial and
nonfamilial nonsyndromatic thoracic aortic aneurysm and/or dissection
(TAAD).";
Hum. Mutat. 30:1406-1411(2009).
[19]
VARIANT MSMDYS HIS-179.
PubMed=20734336; DOI=10.1002/ajmg.a.33657;
Milewicz D.M., Ostergaard J.R., Ala-Kokko L.M., Khan N., Grange D.K.,
Mendoza-Londono R., Bradley T.J., Olney A.H., Ades L., Maher J.F.,
Guo D., Buja L.M., Kim D., Hyland J.C., Regalado E.S.;
"De novo ACTA2 mutation causes a novel syndrome of multisystemic
smooth muscle dysfunction.";
Am. J. Med. Genet. A 152:2437-2443(2010).
[20]
VARIANT MYMY5 HIS-179.
PubMed=20970362; DOI=10.1016/j.ejpn.2010.09.002;
Roder C., Peters V., Kasuya H., Nishizawa T., Wakita S., Berg D.,
Schulte C., Khan N., Tatagiba M., Krischek B.;
"Analysis of ACTA2 in European Moyamoya disease patients.";
Eur. J. Paediatr. Neurol. 15:117-122(2011).
-!- 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.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
-!- INDUCTION: Up-regulated in response to enterovirus 71 (EV71)
infection. {ECO:0000269|PubMed:16548883}.
-!- PTM: Oxidation of Met-46 and Met-49 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-86 (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:0000250|UniProtKB:P68032}.
-!- 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-52 of one monomer and
Glu-272 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: Note=ACTA2 mutations predispose patients to a variety of
diffuse and diverse vascular diseases, premature onset coronary
artery disease (CAD), premature ischemic strokes and Moyamoya
disease. {ECO:0000269|PubMed:19409525}.
-!- DISEASE: Aortic aneurysm, familial thoracic 6 (AAT6) [MIM:611788]:
A disease characterized by permanent dilation of the thoracic
aorta usually due to degenerative changes in the aortic wall. It
is primarily associated with a characteristic histologic
appearance known as 'medial necrosis' or 'Erdheim cystic medial
necrosis' in which there is degeneration and fragmentation of
elastic fibers, loss of smooth muscle cells, and an accumulation
of basophilic ground substance. {ECO:0000269|PubMed:17994018,
ECO:0000269|PubMed:19409525, ECO:0000269|PubMed:19639654}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Moyamoya disease 5 (MYMY5) [MIM:614042]: A progressive
cerebral angiopathy characterized by bilateral intracranial
carotid artery stenosis and telangiectatic vessels in the region
of the basal ganglia. The abnormal vessels resemble a 'puff of
smoke' (moyamoya) on cerebral angiogram. Affected individuals can
develop transient ischemic attacks and/or cerebral infarction, and
rupture of the collateral vessels can cause intracranial
hemorrhage. Hemiplegia of sudden onset and epileptic seizures
constitute the prevailing presentation in childhood, while
subarachnoid bleeding occurs more frequently in adults.
{ECO:0000269|PubMed:20970362}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Multisystemic smooth muscle dysfunction syndrome (MSMDYS)
[MIM:613834]: A syndrome characterized by dysfunction of smooth
muscle cells throughout the body, leading to aortic and
cerebrovascular disease, fixed dilated pupils, hypotonic bladder,
malrotation, and hypoperistalsis of the gut and pulmonary
hypertension. {ECO:0000269|PubMed:20734336}. 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}.
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EMBL; X13839; CAA32064.1; -; mRNA.
EMBL; J05192; AAA51577.1; -; mRNA.
EMBL; AY692464; AAW29811.1; -; mRNA.
EMBL; CR536518; CAG38756.1; -; mRNA.
EMBL; AK313294; BAG36101.1; -; mRNA.
EMBL; AL157394; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471066; EAW50153.1; -; Genomic_DNA.
EMBL; BC017554; AAH17554.1; -; mRNA.
EMBL; BC093052; AAH93052.1; -; mRNA.
EMBL; K01741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; K01742; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; K01743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M33216; AAA60560.1; -; Genomic_DNA.
CCDS; CCDS7392.1; -.
PIR; A35020; ATHUSM.
RefSeq; NP_001135417.1; NM_001141945.2.
RefSeq; NP_001307784.1; NM_001320855.1.
RefSeq; NP_001604.1; NM_001613.2.
UniGene; Hs.500483; -.
ProteinModelPortal; P62736; -.
SMR; P62736; -.
BioGrid; 106574; 166.
CORUM; P62736; -.
ELM; P62736; -.
IntAct; P62736; 25.
STRING; 9606.ENSP00000224784; -.
iPTMnet; P62736; -.
PhosphoSitePlus; P62736; -.
SwissPalm; P62736; -.
BioMuta; ACTA2; -.
DMDM; 51316972; -.
REPRODUCTION-2DPAGE; IPI00008603; -.
UCD-2DPAGE; P62736; -.
EPD; P62736; -.
MaxQB; P62736; -.
PaxDb; P62736; -.
PeptideAtlas; P62736; -.
PRIDE; P62736; -.
TopDownProteomics; P62736; -.
DNASU; 59; -.
Ensembl; ENST00000224784; ENSP00000224784; ENSG00000107796.
GeneID; 59; -.
KEGG; hsa:59; -.
UCSC; uc001kfp.4; human.
CTD; 59; -.
DisGeNET; 59; -.
EuPathDB; HostDB:ENSG00000107796.12; -.
GeneCards; ACTA2; -.
GeneReviews; ACTA2; -.
HGNC; HGNC:130; ACTA2.
HPA; CAB000002; -.
HPA; CAB013531; -.
HPA; HPA041264; -.
HPA; HPA041271; -.
MalaCards; ACTA2; -.
MIM; 102620; gene.
MIM; 611788; phenotype.
MIM; 613834; phenotype.
MIM; 614042; phenotype.
neXtProt; NX_P62736; -.
OpenTargets; ENSG00000107796; -.
Orphanet; 91387; Familial thoracic aortic aneurysm and aortic dissection.
Orphanet; 2573; Moyamoya disease.
Orphanet; 404463; Multisystemic smooth muscle dysfunction syndrome.
PharmGKB; PA24456; -.
eggNOG; KOG0676; Eukaryota.
eggNOG; COG5277; LUCA.
GeneTree; ENSGT00390000015439; -.
HOGENOM; HOG000233340; -.
HOVERGEN; HBG003771; -.
InParanoid; P62736; -.
KO; K12313; -.
OMA; AMCEEED; -.
OrthoDB; EOG091G08LD; -.
PhylomeDB; P62736; -.
TreeFam; TF354237; -.
Reactome; R-HSA-445355; Smooth Muscle Contraction.
SignaLink; P62736; -.
SIGNOR; P62736; -.
GeneWiki; ACTA2; -.
GenomeRNAi; 59; -.
PMAP-CutDB; P62736; -.
PRO; PR:P62736; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000107796; -.
CleanEx; HS_ACTA2; -.
ExpressionAtlas; P62736; baseline and differential.
Genevisible; P62736; HS.
GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
GO; GO:0044297; C:cell body; ISS:AgBase.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0030175; C:filopodium; ISS:AgBase.
GO; GO:0030027; C:lamellipodium; ISS:AgBase.
GO; GO:0043234; C:protein complex; IDA:MGI.
GO; GO:0030485; C:smooth muscle contractile fiber; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019901; F:protein kinase binding; ISS:ParkinsonsUK-UCL.
GO; GO:0072144; P:glomerular mesangial cell development; IEP:UniProtKB.
GO; GO:0090131; P:mesenchyme migration; ISS:AgBase.
GO; GO:0006936; P:muscle contraction; TAS:Reactome.
GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase.
GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
GO; GO:0009615; P:response to virus; IEP:UniProtKB.
GO; GO:0014829; P:vascular smooth muscle contraction; IEA:Ensembl.
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;
Acetylation; Aortic aneurysm; ATP-binding; Complete proteome;
Cytoplasm; Cytoskeleton; Disease mutation; Isopeptide bond;
Methylation; Muscle protein; Nucleotide-binding; Oxidation;
Polymorphism; Reference proteome.
PROPEP 1 2 Removed in mature form.
{ECO:0000244|PubMed:22223895}.
/FTId=PRO_0000000738.
CHAIN 3 377 Actin, aortic smooth muscle.
/FTId=PRO_0000000739.
MOD_RES 3 3 N-acetylglutamate.
{ECO:0000244|PubMed:22223895}.
MOD_RES 46 46 Methionine (R)-sulfoxide. {ECO:0000250}.
MOD_RES 49 49 Methionine (R)-sulfoxide. {ECO:0000250}.
MOD_RES 75 75 Tele-methylhistidine.
{ECO:0000250|UniProtKB:P62739}.
MOD_RES 86 86 N6-methyllysine.
{ECO:0000250|UniProtKB:P68032}.
CROSSLNK 52 52 Isoglutamyl lysine isopeptide (Lys-Glu)
(interchain with E-272); by Vibrio toxins
RtxA and VgrG1.
{ECO:0000250|UniProtKB:P60709}.
CROSSLNK 272 272 Isoglutamyl lysine isopeptide (Glu-Lys)
(interchain with K-52); by Vibrio toxins
RtxA and VgrG1.
{ECO:0000250|UniProtKB:P60709}.
VARIANT 39 39 R -> H (in AAT6; dbSNP:rs794728021).
{ECO:0000269|PubMed:19409525}.
/FTId=VAR_062577.
VARIANT 117 117 N -> T (in AAT6).
{ECO:0000269|PubMed:17994018,
ECO:0000269|PubMed:19409525}.
/FTId=VAR_045915.
VARIANT 118 118 R -> Q (in AAT6; dbSNP:rs112602953).
{ECO:0000269|PubMed:17994018,
ECO:0000269|PubMed:19409525}.
/FTId=VAR_045916.
VARIANT 135 135 Y -> H (in AAT6; dbSNP:rs751300489).
{ECO:0000269|PubMed:17994018}.
/FTId=VAR_045917.
VARIANT 145 145 Y -> C (in AAT6).
{ECO:0000269|PubMed:19639654}.
/FTId=VAR_062578.
VARIANT 149 149 R -> C (in AAT6; dbSNP:rs121434526).
{ECO:0000269|PubMed:17994018,
ECO:0000269|PubMed:19409525,
ECO:0000269|PubMed:19639654}.
/FTId=VAR_045918.
VARIANT 154 154 V -> A (in AAT6).
{ECO:0000269|PubMed:17994018,
ECO:0000269|PubMed:19409525}.
/FTId=VAR_045919.
VARIANT 179 179 R -> H (in MYMY5 and MSMDYS; disease
phenotype include smooth muscle cells
dysfunction in organs throughout the body
with decreased contractile function in
the iris, bladder and gastrointestinal
tract; dbSNP:rs387906592).
{ECO:0000269|PubMed:20734336,
ECO:0000269|PubMed:20970362}.
/FTId=VAR_064516.
VARIANT 185 185 R -> Q (in AAT6).
{ECO:0000269|PubMed:19409525}.
/FTId=VAR_062579.
VARIANT 196 196 T -> S (in dbSNP:rs1803028).
/FTId=VAR_011944.
VARIANT 212 212 R -> Q (in AAT6; dbSNP:rs397516685).
{ECO:0000269|PubMed:19409525,
ECO:0000269|PubMed:19639654}.
/FTId=VAR_062580.
VARIANT 258 258 R -> C (in AAT6; dbSNP:rs121434528).
{ECO:0000269|PubMed:17994018,
ECO:0000269|PubMed:19409525}.
/FTId=VAR_045920.
VARIANT 258 258 R -> H (in AAT6; dbSNP:rs121434527).
{ECO:0000269|PubMed:17994018,
ECO:0000269|PubMed:19409525}.
/FTId=VAR_045921.
VARIANT 292 292 R -> G (in AAT6).
{ECO:0000269|PubMed:17994018}.
/FTId=VAR_045922.
VARIANT 320 320 T -> A (in dbSNP:rs1803027).
/FTId=VAR_011945.
VARIANT 326 326 T -> N (in AAT6; dbSNP:rs777832794).
{ECO:0000269|PubMed:19409525}.
/FTId=VAR_062581.
VARIANT 353 353 T -> N (in AAT6).
{ECO:0000269|PubMed:17994018,
ECO:0000269|PubMed:19409525}.
/FTId=VAR_045923.
VARIANT 373 373 H -> P (in dbSNP:rs1062398).
/FTId=VAR_011946.
CONFLICT 234 234 S -> W (in Ref. 2; AAA51577).
{ECO:0000305}.
SEQUENCE 377 AA; 42009 MW; 2D0543262DB35CA5 CRC64;
MCEEEDSTAL VCDNGSGLCK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA
QSKRGILTLK YPIEHGIITN WDDMEKIWHH SFYNELRVAP EEHPTLLTEA PLNPKANREK
MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDSGDG VTHNVPIYEG YALPHAIMRL
DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK
SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV
LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIS
KQEYDEAGPS IVHRKCF


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