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Actin, alpha skeletal muscle (Alpha-actin-1)

 ACTS_HUMAN              Reviewed;         377 AA.
P68133; P02568; P99020; Q5T8M9;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
27-SEP-2017, entry version 148.
RecName: Full=Actin, alpha skeletal muscle;
AltName: Full=Alpha-actin-1;
Flags: Precursor;
Name=ACTA1; Synonyms=ACTA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Skeletal muscle;
PubMed=6190133; DOI=10.1093/nar/11.11.3503;
Hanauer A., Levin M., Heilig R., Daegelen D., Kahn A., Mandel J.-L.;
"Isolation and characterization of cDNA clones for human skeletal
muscle alpha actin.";
Nucleic Acids Res. 11:3503-3516(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2907503; DOI=10.1016/0888-7543(88)90123-1;
Taylor A., Erba H.P., Muscat G.E.O., Kedes L.;
"Nucleotide sequence and expression of the human skeletal alpha-actin
gene: evolution of functional regulatory domains.";
Genomics 3:323-336(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS NEM3 TYR-42; PRO-96;
SER-117; VAL-134; ASP-184; CYS-185; HIS-258; VAL-261; LEU-265;
LYS-282; GLY-288 AND PHE-372, AND VARIANTS MPCETM ARG-17 AND LEU-165.
PubMed=10508519; DOI=10.1038/13837;
Nowak K.J., Wattanasirichaigoon D., Goebel H.H., Wilce M., Pelin K.,
Donner K., Jacob R.L., Hubner C., Oexle K., Anderson J.R.,
Verity C.M., North K.N.;
"Mutations in the skeletal muscle alpha-actin gene in patients with
actin myopathy and nemaline myopathy.";
Nat. Genet. 23:208-212(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"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 GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skeletal muscle;
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).
[8]
INTERACTION WITH TTID.
PubMed=10958653; DOI=10.1093/hmg/9.14.2141;
Hauser M.A., Horrigan S.K., Salmikangas P., Torian U.M., Viles K.D.,
Dancel R., Tim R.W., Taivainen A., Bartoloni L., Gilchrist J.M.,
Stajich J.M., Gaskell P.C., Gilbert J.R., Vance J.M.,
Pericak-Vance M.A., Carpen O., Westbrook C.A., Speer M.C.;
"Myotilin is mutated in limb girdle muscular dystrophy 1A.";
Hum. Mol. Genet. 9:2141-2147(2000).
[9]
INTERACTION WITH USP25.
PubMed=16501887; DOI=10.1007/s00018-005-5533-1;
Bosch-Comas A., Lindsten K., Gonzalez-Duarte R., Masucci M.G.,
Marfany G.;
"The ubiquitin-specific protease USP25 interacts with three sarcomeric
proteins.";
Cell. Mol. Life Sci. 63:723-734(2006).
[10]
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).
[11]
MALONYLATION AT LYS-63.
PubMed=21908771; DOI=10.1074/mcp.M111.012658;
Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,
He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,
Dai J., Verdin E., Ye Y., Zhao Y.;
"The first identification of lysine malonylation substrates and its
regulatory enzyme.";
Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
[12]
METHYLATION AT LYS-86, 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).
[13]
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).
[14]
VARIANTS NEM3 SER-117; MET-138; GLY-185; CYS-270 AND LEU-359.
PubMed=11333380; DOI=10.1086/320605;
Ilkovski B., Cooper S.T., Nowak K., Ryan M.M., Yang N., Schnell C.,
Durling H.J., Roddick L.G., Wilkinson I., Kornberg A.J., Collins K.J.,
Wallace G., Gunning P., Hardeman E.C., Laing N.G., North K.N.;
"Nemaline myopathy caused by mutations in the muscle alpha-skeletal-
actin gene.";
Am. J. Hum. Genet. 68:1333-1343(2001).
[15]
REVIEW ON VARIANTS.
PubMed=12921789; DOI=10.1016/S0960-8966(03)00101-9;
Sparrow J.C., Nowak K.J., Durling H.J., Beggs A.H.,
Wallgren-Pettersson C., Romero N., Nonaka I., Laing N.G.;
"Muscle disease caused by mutations in the skeletal muscle alpha-actin
gene (ACTA1).";
Neuromuscul. Disord. 13:519-531(2003).
[16]
VARIANTS NEM3 VAL-134 AND ARG-271.
PubMed=11166164; DOI=10.1016/S0960-8966(00)00167-X;
Jungbluth H., Sewry C.A., Brown S.C., Nowak K.J., Laing N.G.,
Wallgren-Pettersson C., Pelin K., Manzur A.Y., Mercuri E.,
Dubowitz V., Muntoni F.;
"Mild phenotype of nemaline myopathy with sleep hypoventilation due to
a mutation in the skeletal muscle alpha-actin (ACTA1) gene.";
Neuromuscul. Disord. 11:35-40(2001).
[17]
VARIANTS NEM3 LEU-37; LEU-40; TYR-42; ARG-43; ASN-66; LEU-75; ARG-75;
LEU-77; ALA-79; LYS-85; ALA-136; ASP-148; GLY-181; ASP-184; GLY-185;
SER-199; GLY-226; VAL-229; ILE-229; ARG-248; ASP-253; CYS-270;
HIS-281; LYS-282; GLY-288 AND GLN-375.
PubMed=15236405; DOI=10.1002/ana.20157;
Agrawal P.B., Strickland C.D., Midgett C., Morales A., Newburger D.E.,
Poulos M.A., Tomczak K.K., Ryan M.M., Iannaccone S.T., Crawford T.O.,
Laing N.G., Beggs A.H.;
"Heterogeneity of nemaline myopathy cases with skeletal muscle alpha-
actin gene mutations.";
Ann. Neurol. 56:86-96(2004).
[18]
VARIANTS CFTD PRO-223; VAL-294 AND SER-334.
PubMed=15468086; DOI=10.1002/ana.20260;
Laing N.G., Clarke N.F., Dye D.E., Liyanage K., Walker K.R.,
Kobayashi Y., Shimakawa S., Hagiwara T., Ouvrier R., Sparrow J.C.,
Nishino I., North K.N., Nonaka I.;
"Actin mutations are one cause of congenital fibre type
disproportion.";
Ann. Neurol. 56:689-694(2004).
[19]
VARIANTS NEM3 ILE-68; LYS-74; SER-117; MET-138; LEU-165; MET-165;
GLY-185; CYS-270 AND LEU-359.
PubMed=15198992; DOI=10.1093/hmg/ddh185;
Ilkovski B., Nowak K.J., Domazetovska A., Maxwell A.L., Clement S.,
Davies K.E., Laing N.G., North K.N., Cooper S.T.;
"Evidence for a dominant-negative effect in ACTA1 nemaline myopathy
caused by abnormal folding, aggregation and altered polymerization of
mutant actin isoforms.";
Hum. Mol. Genet. 13:1727-1743(2004).
[20]
VARIANTS NEM3 TYR-3 AND ALA-336.
PubMed=15520409; DOI=10.1136/jmg.2004.020271;
Kaindl A.M., Rueschendorf F., Krause S., Goebel H.-H., Koehler K.,
Becker C., Pongratz D., Mueller-Hoecker J., Nuernberg P.,
Stoltenburg-Didinger G., Lochmueller H., Huebner A.;
"Missense mutations of ACTA1 cause dominant congenital myopathy with
cores.";
J. Med. Genet. 41:842-848(2004).
[21]
VARIANTS NEM3 ASP-270 AND GLU-375.
PubMed=15336687; DOI=10.1016/j.nmd.2004.05.016;
Ohlsson M., Tajsharghi H., Darin N., Kyllerman M., Oldfors A.;
"Follow-up of nemaline myopathy in two patients with novel mutations
in the skeletal muscle alpha-actin gene (ACTA1).";
Neuromuscul. Disord. 14:471-475(2004).
[22]
VARIANT NEM3 MET-165.
PubMed=16427282; DOI=10.1016/j.nmd.2005.11.004;
Hutchinson D.O., Charlton A., Laing N.G., Ilkovski B., North K.N.;
"Autosomal dominant nemaline myopathy with intranuclear rods due to
mutation of the skeletal muscle ACTA1 gene: clinical and pathological
variability within a kindred.";
Neuromuscul. Disord. 16:113-121(2006).
[23]
VARIANT NEM3 GLU-338.
PubMed=16945537; DOI=10.1016/j.nmd.2006.07.005;
D'Amico A., Graziano C., Pacileo G., Petrini S., Nowak K.J.,
Boldrini R., Jacques A., Feng J.-J., Porfirio B., Sewry C.A.,
Santorelli F.M., Limongelli G., Bertini E., Laing N., Marston S.B.;
"Fatal hypertrophic cardiomyopathy and nemaline myopathy associated
with ACTA1 K336E mutation.";
Neuromuscul. Disord. 16:548-552(2006).
[24]
CHARACTERIZATION OF VARIANT CFTD VAL-294.
PubMed=17387733; DOI=10.1002/ana.21112;
Clarke N.F., Ilkovski B., Cooper S., Valova V.A., Robinson P.J.,
Nonaka I., Feng J.-J., Marston S., North K.;
"The pathogenesis of ACTA1-related congenital fiber type
disproportion.";
Ann. Neurol. 61:552-561(2007).
[25]
CHARACTERIZATION OF VARIANT NEM3 MET-165.
PubMed=17705262; DOI=10.1002/ana.21200;
Domazetovska A., Ilkovski B., Kumar V., Valova V.A., Vandebrouck A.,
Hutchinson D.O., Robinson P.J., Cooper S.T., Sparrow J.C., Peckham M.,
North K.N.;
"Intranuclear rod myopathy: molecular pathogenesis and mechanisms of
weakness.";
Ann. Neurol. 62:597-608(2007).
[26]
VARIANT NEM3 ASN-328, AND CHARACTERIZATION OF VARIANT NEM3 ASN-328.
PubMed=22442437; DOI=10.1212/WNL.0b013e31824e8ebe;
Jain R.K., Jayawant S., Squier W., Muntoni F., Sewry C.A., Manzur A.,
Quinlivan R., Lillis S., Jungbluth H., Sparrow J.C., Ravenscroft G.,
Nowak K.J., Memo M., Marston S.B., Laing N.G.;
"Nemaline myopathy with stiffness and hypertonia associated with an
ACTA1 mutation.";
Neurology 78:1100-1103(2012).
[27]
VARIANT NEM3 CYS-358.
PubMed=23650303; DOI=10.1542/peds.2012-1139;
Gatayama R., Ueno K., Nakamura H., Yanagi S., Ueda H., Yamagishi H.,
Yasui S.;
"Nemaline myopathy with dilated cardiomyopathy in childhood.";
Pediatrics 131:E1986-E1990(2013).
[28]
INVOLVEMENT IN SHPM, VARIANT SHPM ASP-197, CHARACTERIZATION OF VARIANT
SHPM ASP-197, AND CHARACTERIZATION OF VARIANT NEM3 GLY-288.
PubMed=25938801; DOI=10.1001/jamaneurol.2015.37;
Zukosky K., Meilleur K., Traynor B.J., Dastgir J., Medne L.,
Devoto M., Collins J., Rooney J., Zou Y., Yang M.L., Gibbs J.R.,
Meier M., Stetefeld J., Finkel R.S., Schessl J., Elman L., Felice K.,
Ferguson T.A., Ceyhan-Birsoy O., Beggs A.H., Tennekoon G.,
Johnson J.O., Boennemann C.G.;
"Association of a Novel ACTA1 Mutation With a Dominant Progressive
Scapuloperoneal Myopathy in an Extended Family.";
JAMA Neurol. 72:689-698(2015).
-!- 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. Identified in a complex composed
of ACTA1, COBL, GSN AND TMSB4X (By similarity). Interacts with
TTID. Interacts (via its C-terminus) with USP25; the interaction
occurs for all USP25 isoforms but is strongest for isoform USP25m
in muscle differentiating cells. {ECO:0000250,
ECO:0000269|PubMed:10958653, ECO:0000269|PubMed:16501887}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
-!- 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: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-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: Nemaline myopathy 3 (NEM3) [MIM:161800]: A form of
nemaline myopathy. Nemaline myopathies are muscular disorders
characterized by muscle weakness of varying severity and onset,
and abnormal thread-like or rod-shaped structures in muscle fibers
on histologic examination. {ECO:0000269|PubMed:10508519,
ECO:0000269|PubMed:11166164, ECO:0000269|PubMed:11333380,
ECO:0000269|PubMed:15198992, ECO:0000269|PubMed:15236405,
ECO:0000269|PubMed:15336687, ECO:0000269|PubMed:15520409,
ECO:0000269|PubMed:16427282, ECO:0000269|PubMed:16945537,
ECO:0000269|PubMed:17705262, ECO:0000269|PubMed:22442437,
ECO:0000269|PubMed:23650303, ECO:0000269|PubMed:25938801}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Myopathy, actin, congenital, with excess of thin
myofilaments (MPCETM) [MIM:161800]: A congenital muscular disorder
characterized at histological level by areas of sarcoplasm devoid
of normal myofibrils and mitochondria, and replaced with dense
masses of thin filaments. Central cores, rods, ragged red fibers,
and necrosis are absent. {ECO:0000269|PubMed:10508519}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Myopathy, congenital, with fiber-type disproportion
(CFTD) [MIM:255310]: A genetically heterogeneous disorder in which
there is relative hypotrophy of type 1 muscle fibers compared to
type 2 fibers on skeletal muscle biopsy. However, these findings
are not specific and can be found in many different myopathic and
neuropathic conditions. {ECO:0000269|PubMed:15468086,
ECO:0000269|PubMed:17387733}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Myopathy, scapulohumeroperoneal (SHPM) [MIM:616852]: An
autosomal dominant muscular disorder characterized by progressive
muscle weakness with initial scapulo-humeral-peroneal and distal
distribution. Over time, muscle weakness progresses to proximal
muscle groups. Clinical characteristics include scapular winging,
mild lower facial weakness, foot drop due to foot eversion and
dorsiflexion weakness, and selective muscle atrophy. Age at onset
and disease progression are variable.
{ECO:0000269|PubMed:25938801}. 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; J00068; AAB59376.1; -; mRNA.
EMBL; M20543; AAA60296.1; -; Genomic_DNA.
EMBL; AF182035; AAF02694.1; -; Genomic_DNA.
EMBL; CR536516; CAG38754.1; -; mRNA.
EMBL; CR541796; CAG46595.1; -; mRNA.
EMBL; AL160004; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471098; EAW69898.1; -; Genomic_DNA.
EMBL; BC012597; AAH12597.1; -; mRNA.
CCDS; CCDS1578.1; -.
PIR; A31251; ATHU.
RefSeq; NP_001091.1; NM_001100.3.
UniGene; Hs.1288; -.
ProteinModelPortal; P68133; -.
SMR; P68133; -.
BioGrid; 106573; 138.
IntAct; P68133; 19.
MINT; MINT-135471; -.
STRING; 9606.ENSP00000355645; -.
DrugBank; DB04151; 4-Methyl-Histidine.
DrugBank; DB04629; Aplyronine A.
DrugBank; DB03850; Jaspisamide A.
DrugBank; DB03616; Kabiramide C.
DrugBank; DB02621; Latrunculin A.
DrugBank; DB08080; LATRUNCULIN B.
DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DrugBank; DB04774; Reidispongiolide A.
DrugBank; DB04775; Reidispongiolide C.
DrugBank; DB04783; Sphinxolide B.
DrugBank; DB02772; Sucrose.
DrugBank; DB03903; Tmr.
DrugBank; DB03021; Ulapualide A.
iPTMnet; P68133; -.
PhosphoSitePlus; P68133; -.
SwissPalm; P68133; -.
BioMuta; ACTA1; -.
DMDM; 61218043; -.
EPD; P68133; -.
MaxQB; P68133; -.
PaxDb; P68133; -.
PeptideAtlas; P68133; -.
PRIDE; P68133; -.
DNASU; 58; -.
Ensembl; ENST00000366684; ENSP00000355645; ENSG00000143632.
GeneID; 58; -.
KEGG; hsa:58; -.
UCSC; uc001htm.4; human.
CTD; 58; -.
DisGeNET; 58; -.
EuPathDB; HostDB:ENSG00000143632.14; -.
GeneCards; ACTA1; -.
GeneReviews; ACTA1; -.
HGNC; HGNC:129; ACTA1.
HPA; CAB000045; -.
HPA; HPA041264; -.
HPA; HPA041271; -.
MalaCards; ACTA1; -.
MIM; 102610; gene.
MIM; 161800; phenotype.
MIM; 255310; phenotype.
MIM; 616852; phenotype.
neXtProt; NX_P68133; -.
OpenTargets; ENSG00000143632; -.
Orphanet; 171439; Childhood-onset nemaline myopathy.
Orphanet; 2020; Congenital fiber-type disproportion myopathy.
Orphanet; 98904; Congenital myopathy with excess of thin filaments.
Orphanet; 171433; Intermediate nemaline myopathy.
Orphanet; 171430; Severe congenital nemaline myopathy.
Orphanet; 171436; Typical nemaline myopathy.
PharmGKB; PA24455; -.
eggNOG; KOG0676; Eukaryota.
eggNOG; COG5277; LUCA.
GeneTree; ENSGT00760000118957; -.
HOGENOM; HOG000233340; -.
HOVERGEN; HBG003771; -.
InParanoid; P68133; -.
KO; K10354; -.
OMA; GRTTGEC; -.
OrthoDB; EOG091G08LD; -.
PhylomeDB; P68133; -.
TreeFam; TF354237; -.
Reactome; R-HSA-390522; Striated Muscle Contraction.
SignaLink; P68133; -.
SIGNOR; P68133; -.
ChiTaRS; ACTA1; human.
EvolutionaryTrace; P68133; -.
GeneWiki; Actin,_alpha_1; -.
GenomeRNAi; 58; -.
PRO; PR:P68133; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000143632; -.
CleanEx; HS_ACTA1; -.
ExpressionAtlas; P68133; baseline and differential.
Genevisible; P68133; HS.
GO; GO:0015629; C:actin cytoskeleton; IMP:UniProtKB.
GO; GO:0005884; C:actin filament; IDA:UniProtKB.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0044297; C:cell body; ISS:AgBase.
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:0030017; C:sarcomere; IDA:UniProtKB.
GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
GO; GO:0005865; C:striated muscle thin filament; IDA:UniProtKB.
GO; GO:0043531; F:ADP binding; TAS:UniProtKB.
GO; GO:0005524; F:ATP binding; TAS:UniProtKB.
GO; GO:0017022; F:myosin binding; TAS:UniProtKB.
GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:UniProtKB.
GO; GO:0016049; P:cell growth; IEA:Ensembl.
GO; GO:0090131; P:mesenchyme migration; ISS:AgBase.
GO; GO:0006936; P:muscle contraction; TAS:UniProtKB.
GO; GO:0030049; P:muscle filament sliding; TAS:Reactome.
GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase.
GO; GO:0009991; P:response to extracellular stimulus; IEA:Ensembl.
GO; GO:0010226; P:response to lithium ion; IEA:Ensembl.
GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
GO; GO:0048545; P:response to steroid hormone; IEA:Ensembl.
GO; GO:0043503; P:skeletal muscle fiber adaptation; IEA:Ensembl.
GO; GO:0048741; P:skeletal muscle fiber development; ISS:UniProtKB.
GO; GO:0030240; P:skeletal muscle thin filament assembly; IMP: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;
Acetylation; ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton;
Disease mutation; Isopeptide bond; Methylation; Muscle protein;
Nemaline myopathy; Nucleotide-binding; Oxidation; Reference proteome.
PROPEP 1 2 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000000844.
CHAIN 3 377 Actin, alpha skeletal muscle.
/FTId=PRO_0000000845.
MOD_RES 3 3 N-acetylaspartate.
{ECO:0000250|UniProtKB:P68135}.
MOD_RES 46 46 Methionine (R)-sulfoxide. {ECO:0000250}.
MOD_RES 49 49 Methionine (R)-sulfoxide. {ECO:0000250}.
MOD_RES 63 63 N6-malonyllysine.
{ECO:0000269|PubMed:21908771}.
MOD_RES 86 86 N6-methyllysine.
{ECO:0000269|PubMed:23673617}.
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 3 3 D -> Y (in NEM3; some patients have core
lesions on muscle biopsy;
dbSNP:rs121909527).
{ECO:0000269|PubMed:15520409}.
/FTId=VAR_062424.
VARIANT 17 17 G -> R (in MPCETM; dbSNP:rs121909521).
{ECO:0000269|PubMed:10508519}.
/FTId=VAR_011680.
VARIANT 27 27 D -> N (in NEM3).
/FTId=VAR_062425.
VARIANT 37 37 V -> L (in NEM3).
{ECO:0000269|PubMed:15236405}.
/FTId=VAR_062426.
VARIANT 40 40 P -> L (in NEM3).
{ECO:0000269|PubMed:15236405}.
/FTId=VAR_062427.
VARIANT 42 42 H -> Y (in NEM3; severe).
{ECO:0000269|PubMed:10508519,
ECO:0000269|PubMed:15236405}.
/FTId=VAR_015579.
VARIANT 43 43 Q -> R (in NEM3).
{ECO:0000269|PubMed:15236405}.
/FTId=VAR_062428.
VARIANT 44 44 G -> V (in NEM3).
/FTId=VAR_062429.
VARIANT 45 45 V -> F (in NEM3; dbSNP:rs398123562).
/FTId=VAR_062430.
VARIANT 66 66 I -> N (in NEM3).
{ECO:0000269|PubMed:15236405}.
/FTId=VAR_062431.
VARIANT 68 68 T -> I (in NEM3).
{ECO:0000269|PubMed:15198992}.
/FTId=VAR_062432.
VARIANT 74 74 E -> K (in NEM3).
{ECO:0000269|PubMed:15198992}.
/FTId=VAR_062433.
VARIANT 75 75 H -> L (in NEM3).
{ECO:0000269|PubMed:15236405}.
/FTId=VAR_062434.
VARIANT 75 75 H -> R (in NEM3).
{ECO:0000269|PubMed:15236405}.
/FTId=VAR_062435.
VARIANT 77 77 I -> L (in NEM3).
{ECO:0000269|PubMed:15236405}.
/FTId=VAR_062436.
VARIANT 79 79 T -> A (in NEM3).
{ECO:0000269|PubMed:15236405}.
/FTId=VAR_062437.
VARIANT 85 85 E -> K (in NEM3).
{ECO:0000269|PubMed:15236405}.
/FTId=VAR_062438.
VARIANT 96 96 L -> P (in NEM3; autosomal recessive;
dbSNP:rs121909519).
{ECO:0000269|PubMed:10508519}.
/FTId=VAR_011681.
VARIANT 116 116 A -> T (in NEM3).
/FTId=VAR_062439.
VARIANT 117 117 N -> S (in NEM3; autosomal dominant;
dbSNP:rs121909520).
{ECO:0000269|PubMed:10508519,
ECO:0000269|PubMed:11333380,
ECO:0000269|PubMed:15198992}.
/FTId=VAR_011682.
VARIANT 117 117 N -> T (in NEM3).
/FTId=VAR_062440.
VARIANT 118 118 R -> H (in NEM3).
/FTId=VAR_062441.
VARIANT 134 134 M -> V (in NEM3; autosomal dominant).
{ECO:0000269|PubMed:10508519,
ECO:0000269|PubMed:11166164}.
/FTId=VAR_013470.
VARIANT 136 136 V -> A (in NEM3).
{ECO:0000269|PubMed:15236405}.
/FTId=VAR_062442.
VARIANT 138 138 I -> M (in NEM3; autosomal recessive;
dbSNP:rs121909526).
{ECO:0000269|PubMed:11333380,
ECO:0000269|PubMed:15198992}.
/FTId=VAR_011683.
VARIANT 140 140 A -> P (in NEM3).
/FTId=VAR_062443.
VARIANT 142 142 L -> P (in NEM3).
/FTId=VAR_062444.
VARIANT 148 148 G -> D (in NEM3).
{ECO:0000269|PubMed:15236405}.
/FTId=VAR_062445.
VARIANT 150 150 T -> N (in NEM3).
/FTId=VAR_062446.
VARIANT 156 156 D -> N (in NEM3).
/FTId=VAR_062447.
VARIANT 165 165 V -> L (in MPCETM; dbSNP:rs121909522).
{ECO:0000269|PubMed:10508519,
ECO:0000269|PubMed:15198992}.
/FTId=VAR_011684.
VARIANT 165 165 V -> M (in NEM3; results in sequestration
of sarcomeric and Z line proteins into
intranuclear aggregates; there is some
evidence of muscle regeneration
suggesting a compensatory effect;
dbSNP:rs121909522).
{ECO:0000269|PubMed:15198992,
ECO:0000269|PubMed:16427282,
ECO:0000269|PubMed:17705262}.
/FTId=VAR_062448.
VARIANT 172 172 A -> G (in NEM3).
/FTId=VAR_062449.
VARIANT 181 181 D -> G (in NEM3).
{ECO:0000269|PubMed:15236405}.
/FTId=VAR_062450.
VARIANT 181 181 D -> H (in NEM3).
/FTId=VAR_062451.
VARIANT 181 181 D -> N (in NEM3).
/FTId=VAR_062452.
VARIANT 184 184 G -> D (in NEM3; mild).
{ECO:0000269|PubMed:10508519,
ECO:0000269|PubMed:15236405}.
/FTId=VAR_015580.
VARIANT 185 185 R -> C (in NEM3; severe).
{ECO:0000269|PubMed:10508519}.
/FTId=VAR_015582.
VARIANT 185 185 R -> D (in NEM3; requires 2 nucleotide
substitutions).
/FTId=VAR_062453.
VARIANT 185 185 R -> G (in NEM3; autosomal dominant;
severe). {ECO:0000269|PubMed:11333380,
ECO:0000269|PubMed:15198992,
ECO:0000269|PubMed:15236405}.
/FTId=VAR_015581.
VARIANT 185 185 R -> S (in NEM3).
/FTId=VAR_062454.
VARIANT 197 197 E -> D (in SHPM; no effect on
cytoskeleton structure;
dbSNP:rs869312739).
{ECO:0000269|PubMed:25938801}.
/FTId=VAR_076426.
VARIANT 198 198 R -> L (in NEM3).
/FTId=VAR_062455.
VARIANT 199 199 G -> S (in NEM3).
{ECO:0000269|PubMed:15236405}.
/FTId=VAR_062456.
VARIANT 223 223 L -> P (in CFTD; dbSNP:rs121909530).
{ECO:0000269|PubMed:15468086}.
/FTId=VAR_032917.
VARIANT 226 226 E -> G (in NEM3).
{ECO:0000269|PubMed:15236405}.
/FTId=VAR_062457.
VARIANT 226 226 E -> Q (in NEM3).
/FTId=VAR_062458.
VARIANT 227 227 N -> V (in NEM3; requires 2 nucleotide
substitutions).
/FTId=VAR_062459.
VARIANT 229 229 M -> I (in NEM3).
{ECO:0000269|PubMed:15236405}.
/FTId=VAR_062460.
VARIANT 229 229 M -> T (in NEM3).
/FTId=VAR_062461.
VARIANT 229 229 M -> V (in NEM3; dbSNP:rs794727714).
{ECO:0000269|PubMed:15236405}.
/FTId=VAR_062462.
VARIANT 243 243 E -> K (in NEM3; dbSNP:rs367543051).
/FTId=VAR_062463.
VARIANT 248 248 Q -> K (in NEM3).
/FTId=VAR_062464.
VARIANT 248 248 Q -> R (in NEM3).
{ECO:0000269|PubMed:15236405}.
/FTId=VAR_062465.
VARIANT 253 253 G -> D (in NEM3).
{ECO:0000269|PubMed:15236405}.
/FTId=VAR_062466.
VARIANT 258 258 R -> H (in NEM3; severe).
{ECO:0000269|PubMed:10508519}.
/FTId=VAR_015583.
VARIANT 258 258 R -> L (in NEM3).
/FTId=VAR_062467.
VARIANT 261 261 E -> V (in NEM3; autosomal recessive;
dbSNP:rs121909523).
{ECO:0000269|PubMed:10508519}.
/FTId=VAR_011685.
VARIANT 265 265 Q -> L (in NEM3; severe).
{ECO:0000269|PubMed:10508519}.
/FTId=VAR_015584.
VARIANT 270 270 G -> C (in NEM3; autosomal dominant;
dbSNP:rs121909525).
{ECO:0000269|PubMed:11333380,
ECO:0000269|PubMed:15198992,
ECO:0000269|PubMed:15236405}.
/FTId=VAR_011686.
VARIANT 270 270 G -> D (in NEM3).
{ECO:0000269|PubMed:15336687}.
/FTId=VAR_062468.
VARIANT 270 270 G -> R (in NEM3).
/FTId=VAR_062469.
VARIANT 271 271 M -> R (in NEM3; autosomal dominant).
{ECO:0000269|PubMed:11166164}.
/FTId=VAR_013471.
VARIANT 274 274 A -> E (in NEM3).
/FTId=VAR_062470.
VARIANT 281 281 Y -> H (in NEM3).
{ECO:0000269|PubMed:15236405}.
/FTId=VAR_062471.
VARIANT 282 282 N -> K (in NEM3; severe).
{ECO:0000269|PubMed:10508519,
ECO:0000269|PubMed:15236405}.
/FTId=VAR_015585.
VARIANT 285 285 M -> K (in NEM3).
/FTId=VAR_062472.
VARIANT 288 288 D -> G (in NEM3; severe; formation of
rod-like structure).
{ECO:0000269|PubMed:10508519,
ECO:0000269|PubMed:15236405,
ECO:0000269|PubMed:25938801}.
/FTId=VAR_015586.
VARIANT 294 294 D -> V (in CFTD; results in decreased
motility due to abnormal interactions
between actin and tropomyosin with
tropomyosin stabilized in the 'off'
position; the mutant protein incorporates
into actin filaments and does not result
in increased actin aggregation or
disruption of the sarcomere;
dbSNP:rs121909529).
{ECO:0000269|PubMed:15468086,
ECO:0000269|PubMed:17387733}.
/FTId=VAR_032918.
VARIANT 328 328 K -> N (in NEM3; no effect on actin
structure; higher sensitivty to calcium;
dbSNP:rs398122936).
{ECO:0000269|PubMed:22442437}.
/FTId=VAR_076427.
VARIANT 334 334 P -> S (in CFTD; dbSNP:rs121909531).
{ECO:0000269|PubMed:15468086}.
/FTId=VAR_032919.
VARIANT 336 336 E -> A (in NEM3; dbSNP:rs121909528).
{ECO:0000269|PubMed:15520409}.
/FTId=VAR_062473.
VARIANT 338 338 K -> E (in NEM3).
{ECO:0000269|PubMed:16945537}.
/FTId=VAR_062474.
VARIANT 338 338 K -> I (in NEM3).
/FTId=VAR_062475.
VARIANT 350 350 S -> L (in NEM3).
/FTId=VAR_062476.
VARIANT 358 358 W -> C (in NEM3; found in a patient with
a rare combination of NEM3 and dilated
cardiomyopathy; dbSNP:rs587777354).
{ECO:0000269|PubMed:23650303}.
/FTId=VAR_076428.
VARIANT 359 359 I -> L (in NEM3; autosomal dominant;
severe; dbSNP:rs121909524).
{ECO:0000269|PubMed:11333380,
ECO:0000269|PubMed:15198992}.
/FTId=VAR_015587.
VARIANT 372 372 V -> F (in NEM3; severe).
{ECO:0000269|PubMed:10508519}.
/FTId=VAR_011687.
VARIANT 374 374 R -> S (in NEM3).
/FTId=VAR_062477.
VARIANT 375 375 K -> E (in NEM3).
{ECO:0000269|PubMed:15336687}.
/FTId=VAR_062478.
VARIANT 375 375 K -> Q (in NEM3).
{ECO:0000269|PubMed:15236405}.
/FTId=VAR_062479.
SEQUENCE 377 AA; 42051 MW; DF2A3A046346A179 CRC64;
MCDEDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA
QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP EEHPTLLTEA PLNPKANREK
MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDSGDG VTHNVPIYEG YALPHAIMRL
DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK
SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV
MSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIT
KQEYDEAGPS IVHRKCF


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