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Tropomyosin alpha-1 chain (Alpha-tropomyosin) (Tropomyosin-1)

 TPM1_HUMAN              Reviewed;         284 AA.
P09493; B7Z5T7; D9YZV2; D9YZV3; D9YZV8; P09494; P10469; Q6DV89;
Q6DV90; Q7Z6L8; Q86W64; Q96IK2; Q9UCI1; Q9UCI2; Q9UCY9; Q9Y427;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 2.
25-OCT-2017, entry version 193.
RecName: Full=Tropomyosin alpha-1 chain;
AltName: Full=Alpha-tropomyosin;
AltName: Full=Tropomyosin-1;
Name=TPM1; Synonyms=C15orf13, TMSA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
PROTEIN SEQUENCE (ISOFORM 1), AND ACETYLATION AT MET-1.
PubMed=3548719; DOI=10.1016/0006-291X(87)91486-0;
Mische S.M., Manjula B.N., Fischetti V.A.;
"Relation of streptococcal M protein with human and rabbit
tropomyosin: the complete amino acid sequence of human cardiac alpha
tropomyosin, a highly conserved contractile protein.";
Biochem. Biophys. Res. Commun. 142:813-818(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Fibroblast;
PubMed=3336357; DOI=10.1128/MCB.8.1.160;
Lin C.-S., Leavitt J.;
"Cloning and characterization of a cDNA encoding transformation-
sensitive tropomyosin isoform 3 from tumorigenic human fibroblasts.";
Mol. Cell. Biol. 8:160-168(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
PubMed=3336363; DOI=10.1128/MCB.8.1.433;
McLeod A.R., Gooding C.;
"Human hTM alpha gene: expression in muscle and nonmuscle tissue.";
Mol. Cell. Biol. 8:433-440(1988).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 6), AND TISSUE SPECIFICITY.
TISSUE=Heart;
PubMed=15249230; DOI=10.1016/j.bbrc.2004.06.084;
Denz C.R., Narshi A., Zajdel R.W., Dube D.K.;
"Expression of a novel cardiac-specific tropomyosin isoform in
humans.";
Biochem. Biophys. Res. Commun. 320:1291-1297(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Tongue;
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 MRNA] (ISOFORM 7).
TISSUE=Uterus;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[9]
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.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
TISSUE=Brain, Hippocampus, and Placenta;
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).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 58-284 (ISOFORM 2).
TISSUE=Liver;
PubMed=3138425; DOI=10.1007/BF02100079;
Colote S., Widada J.S., Ferraz C., Bonhomme F., Marti J.,
Liautard J.-P.;
"Evolution of tropomyosin functional domains: differential splicing
and genomic constraints.";
J. Mol. Evol. 27:228-235(1988).
[12]
PROTEIN SEQUENCE OF 134-149 AND 153-167.
TISSUE=Colon;
PubMed=8450225;
Das K.M., Dasgupta A., Mandal A., Geng X.;
"Autoimmunity to cytoskeletal protein tropomyosin. A clue to the
pathogenetic mechanism for ulcerative colitis.";
J. Immunol. 150:2487-2493(1993).
[13]
MASS SPECTROMETRY.
TISSUE=Mammary cancer;
PubMed=11840567;
DOI=10.1002/1615-9861(200202)2:2<212::AID-PROT212>3.0.CO;2-H;
Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A.,
Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J.,
Zvelebil M.J.;
"Cluster analysis of an extensive human breast cancer cell line
protein expression map database.";
Proteomics 2:212-223(2002).
[14]
PHOSPHORYLATION AT SER-283, AND MUTAGENESIS OF SER-283.
PubMed=17895359; DOI=10.1242/jcs.003251;
Houle F., Poirier A., Dumaresq J., Huot J.;
"DAP kinase mediates the phosphorylation of tropomyosin-1 downstream
of the ERK pathway, which regulates the formation of stress fibers in
response to oxidative stress.";
J. Cell Sci. 120:3666-3677(2007).
[15]
TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
Ahamed M.E.;
Submitted (APR-2007) to UniProtKB.
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-213 (ISOFORMS 10; 3; 4 AND
8), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[19]
FUNCTION, CHARACTERIZATION OF VARIANTS CMH3 ASN-175 AND GLY-180, AND
SUBUNIT.
PubMed=23170982; DOI=10.1021/bi301323n;
Janco M., Kalyva A., Scellini B., Piroddi N., Tesi C., Poggesi C.,
Geeves M.A.;
"alpha-Tropomyosin with a D175N or E180G mutation in only one chain
differs from tropomyosin with mutations in both chains.";
Biochemistry 51:9880-9890(2012).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174, PHOSPHORYLATION
[LARGE SCALE ANALYSIS] AT SER-31 (ISOFORM 2), PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-51 (ISOFORM 5), AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
INTERACTION WITH LMOD2.
PubMed=26873245; DOI=10.1016/j.bbapap.2016.02.009;
Colpan M., Tolkatchev D., Grover S., Helms G.L., Cort J.R., Moroz N.,
Kostyukova A.S.;
"Localization of the binding interface between leiomodin-2 and alpha-
tropomyosin.";
Biochim. Biophys. Acta 1864:523-530(2016).
[22]
VARIANTS CMH3 ASN-175 AND GLY-180.
PubMed=8205619; DOI=10.1016/0092-8674(94)90054-X;
Thierfelder L., Watkins H., Macrae C., Lamas R., McKenna W.J.,
Vosberg H.-P., Seidman J.G., Seidman C.E.;
"Alpha-tropomyosin and cardiac troponin T mutations cause familial
hypertrophic cardiomyopathy: a disease of the sarcomere.";
Cell 77:701-712(1994).
[23]
VARIANTS CMH3 VAL-63 AND ASN-175.
PubMed=8523464; DOI=10.1016/0022-2828(95)90026-8;
Nakajima-Taniguchi C., Matsui H., Nagata S., Kishimoto T.,
Yamauchi-Takihara K.;
"Novel missense mutation in alpha-tropomyosin gene found in Japanese
patients with hypertrophic cardiomyopathy.";
J. Mol. Cell. Cardiol. 27:2053-2058(1995).
[24]
VARIANT CMH3 ASN-175.
PubMed=7898523; DOI=10.1056/NEJM199504203321603;
Watkins H., McKenna W.J., Thierfelder L., Suk H.J., Anan R.,
O'Donoghue A., Spirito P., Matsumori A., Moravec C.S., Seidman J.G.,
Seidman C.E.;
"Mutations in the genes for cardiac troponin T and alpha-tropomyosin
in hypertrophic cardiomyopathy.";
N. Engl. J. Med. 332:1058-1064(1995).
[25]
VARIANT CMH3 ASN-175.
PubMed=9822100; DOI=10.1016/S0735-1097(98)00448-3;
Jaeaeskelaeinen P., Soranta M., Miettinen R., Saarinen L.,
Pihlajamaeki J., Silvennoinen K., Tikanoja T., Laakso M., Kuusisto J.;
"The cardiac beta-myosin heavy chain gene is not the predominant gene
for hypertrophic cardiomyopathy in the Finnish population.";
J. Am. Coll. Cardiol. 32:1709-1716(1998).
[26]
VARIANTS CMD1Y LYS-40 AND LYS-54.
PubMed=11273725; DOI=10.1006/jmcc.2000.1339;
Olson T.M., Kishimoto N.Y., Whitby F.G., Michels V.V.;
"Mutations that alter the surface charge of alpha-tropomyosin are
associated with dilated cardiomyopathy.";
J. Mol. Cell. Cardiol. 33:723-732(2001).
[27]
VARIANT CMH3 VAL-180.
PubMed=12974739; DOI=10.1034/j.1399-0004.2003.00151.x;
Erdmann J., Daehmlow S., Wischke S., Senyuva M., Werner U., Raible J.,
Tanis N., Dyachenko S., Hummel M., Hetzer R., Regitz-Zagrosek V.;
"Mutation spectrum in a large cohort of unrelated consecutive patients
with hypertrophic cardiomyopathy.";
Clin. Genet. 64:339-349(2003).
[28]
VARIANTS LVNC9 LYS-192 AND GLU-248.
PubMed=21551322; DOI=10.1161/CIRCGENETICS.110.959270;
Probst S., Oechslin E., Schuler P., Greutmann M., Boye P., Knirsch W.,
Berger F., Thierfelder L., Jenni R., Klaassen S.;
"Sarcomere gene mutations in isolated left ventricular noncompaction
cardiomyopathy do not predict clinical phenotype.";
Circ. Cardiovasc. Genet. 4:367-374(2011).
-!- FUNCTION: Binds to actin filaments in muscle and non-muscle cells
(PubMed:23170982). Plays a central role, in association with the
troponin complex, in the calcium dependent regulation of
vertebrate striated muscle contraction (PubMed:23170982). Smooth
muscle contraction is regulated by interaction with caldesmon. In
non-muscle cells is implicated in stabilizing cytoskeleton actin
filaments.
-!- SUBUNIT: Homodimer (PubMed:23170982). Heterodimer of an alpha
(TPM1, TPM3 or TPM4) and a beta (TPM2) chain (By similarity).
Interacts with HRG (via the HRR domain); the interaction
contributes to the antiangiogenic properties of the
histidine/proline-rich region (HRR) of HRG (By similarity).
Interacts (via N-terminus) with LMOD2 (via N-terminus) and TMOD1
(via N-terminus) (PubMed:26873245). {ECO:0000250,
ECO:0000250|UniProtKB:P04268, ECO:0000250|UniProtKB:P04692,
ECO:0000269|PubMed:23170982, ECO:0000269|PubMed:26873245}.
-!- INTERACTION:
Q9UL45:BLOC1S6; NbExp=4; IntAct=EBI-12123928, EBI-465781;
Q8TAB5:C1orf216; NbExp=3; IntAct=EBI-351158, EBI-747505;
Q8TC20:CAGE1; NbExp=3; IntAct=EBI-351158, EBI-10196469;
Q8TC20-4:CAGE1; NbExp=4; IntAct=EBI-12123928, EBI-11522698;
Q08379:GOLGA2; NbExp=3; IntAct=EBI-10196387, EBI-618309;
V9HW56:HEL-S-108; NbExp=3; IntAct=EBI-10196387, EBI-10330141;
O14879:IFIT3; NbExp=4; IntAct=EBI-12123928, EBI-745127;
Q9BQD3:KXD1; NbExp=6; IntAct=EBI-12123928, EBI-739657;
Q9Y6D9:MAD1L1; NbExp=5; IntAct=EBI-12123928, EBI-742610;
Q8N0S2:SYCE1; NbExp=4; IntAct=EBI-12123928, EBI-6872807;
P0C1Z6:TFPT; NbExp=3; IntAct=EBI-12123928, EBI-1245626;
P0C1Z6-2:TFPT; NbExp=3; IntAct=EBI-10196387, EBI-10178002;
P13805:TNNT1; NbExp=4; IntAct=EBI-351158, EBI-726527;
P13805-3:TNNT1; NbExp=4; IntAct=EBI-12123928, EBI-12151635;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:P04692}. Note=Associates with F-actin
stress fibers. {ECO:0000250|UniProtKB:P04692}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=10;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=Skeletal muscle, TPM1alpha;
IsoId=P09493-1; Sequence=Displayed;
Name=2; Synonyms=Smooth muscle;
IsoId=P09493-2; Sequence=VSP_006576, VSP_006578, VSP_006579;
Note=Incomplete sequence. Contains a phosphoserine at position
31. {ECO:0000244|PubMed:24275569};
Name=3; Synonyms=Fibroblast, TM3;
IsoId=P09493-3; Sequence=VSP_006577, VSP_006579;
Note=Contains a N6-acetyllysine at position 213.
{ECO:0000244|PubMed:19608861};
Name=4;
IsoId=P09493-4; Sequence=VSP_006577;
Note=Contains a N6-acetyllysine at position 213.
{ECO:0000244|PubMed:19608861};
Name=5;
IsoId=P09493-5; Sequence=VSP_017498, VSP_017499;
Note=Contains a phosphoserine at position 51.
{ECO:0000244|PubMed:24275569};
Name=6; Synonyms=10, TPM1kappa;
IsoId=P09493-6; Sequence=VSP_036064;
Name=7;
IsoId=P09493-7; Sequence=VSP_036064, VSP_006579;
Note=No experimental confirmation available.;
Name=8;
IsoId=P09493-8; Sequence=VSP_047297, VSP_047298, VSP_047299,
VSP_047300, VSP_006579;
Note=Gene prediction based on EST data. Contains a
N6-acetyllysine at position 213. {ECO:0000244|PubMed:19608861};
Name=9;
IsoId=P09493-9; Sequence=VSP_006579;
Note=Gene prediction based on EST data.;
Name=10;
IsoId=P09493-10; Sequence=VSP_047299, VSP_047300, VSP_047301;
Note=No experimental confirmation available. Contains a
N6-acetyllysine at position 213. {ECO:0000244|PubMed:19608861};
-!- TISSUE SPECIFICITY: Detected in primary breast cancer tissues but
undetectable in normal breast tissues in Sudanese patients.
Isoform 1 is expressed in adult and fetal skeletal muscle and
cardiac tissues, with higher expression levels in the cardiac
tissues. Isoform 10 is expressed in adult and fetal cardiac
tissues, but not in skeletal muscle. {ECO:0000269|PubMed:15249230,
ECO:0000269|Ref.15}.
-!- DOMAIN: The molecule is in a coiled coil structure that is formed
by 2 polypeptide chains. The sequence exhibits a prominent seven-
residues periodicity.
-!- PTM: Phosphorylated at Ser-283 by DAPK1 in response to oxidative
stress and this phosphorylation enhances stress fiber formation in
endothelial cells. {ECO:0000269|PubMed:17895359}.
-!- MASS SPECTROMETRY: Mass=32875.93; Method=MALDI; Range=1-284
(P09493-3); Evidence={ECO:0000269|PubMed:11840567};
-!- DISEASE: Cardiomyopathy, familial hypertrophic 3 (CMH3)
[MIM:115196]: A hereditary heart disorder characterized by
ventricular hypertrophy, which is usually asymmetric and often
involves the interventricular septum. The symptoms include
dyspnea, syncope, collapse, palpitations, and chest pain. They can
be readily provoked by exercise. The disorder has inter- and
intrafamilial variability ranging from benign to malignant forms
with high risk of cardiac failure and sudden cardiac death.
{ECO:0000269|PubMed:12974739, ECO:0000269|PubMed:23170982,
ECO:0000269|PubMed:7898523, ECO:0000269|PubMed:8205619,
ECO:0000269|PubMed:8523464, ECO:0000269|PubMed:9822100}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Cardiomyopathy, dilated 1Y (CMD1Y) [MIM:611878]: A
disorder characterized by ventricular dilation and impaired
systolic function, resulting in congestive heart failure and
arrhythmia. Patients are at risk of premature death.
{ECO:0000269|PubMed:11273725}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Left ventricular non-compaction 9 (LVNC9) [MIM:611878]: A
disease due to an arrest of myocardial morphogenesis. It is
characterized by a hypertrophic left ventricle with deep
trabeculations and with poor systolic function, with or without
associated left ventricular dilation. In some cases, it is
associated with other congenital heart anomalies.
{ECO:0000269|PubMed:21551322}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}.
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EMBL; M19267; AAA36771.1; -; mRNA.
EMBL; M19713; AAA61225.1; -; mRNA.
EMBL; M19714; AAA61226.1; -; mRNA.
EMBL; M19715; AAA61227.1; -; mRNA.
EMBL; AY640414; AAT68294.1; -; mRNA.
EMBL; AY640415; AAT68295.1; -; mRNA.
EMBL; AK299387; BAH13023.1; -; mRNA.
EMBL; AL050179; CAB43309.2; -; mRNA.
EMBL; GU324929; ADL14500.1; -; Genomic_DNA.
EMBL; GU324930; ADL14501.1; -; Genomic_DNA.
EMBL; GU324933; ADL14504.1; -; Genomic_DNA.
EMBL; GU324935; ADL14506.1; -; Genomic_DNA.
EMBL; AC079328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471082; EAW77619.1; -; Genomic_DNA.
EMBL; CH471082; EAW77622.1; -; Genomic_DNA.
EMBL; CH471082; EAW77623.1; -; Genomic_DNA.
EMBL; CH471082; EAW77627.1; -; Genomic_DNA.
EMBL; CH471082; EAW77628.1; -; Genomic_DNA.
EMBL; BC007433; AAH07433.1; -; mRNA.
EMBL; BC050473; AAH50473.1; -; mRNA.
EMBL; BC053545; AAH53545.1; -; mRNA.
EMBL; X12369; CAA30930.1; -; mRNA.
CCDS; CCDS10181.1; -. [P09493-10]
CCDS; CCDS32262.1; -. [P09493-7]
CCDS; CCDS32263.1; -. [P09493-3]
CCDS; CCDS32264.1; -. [P09493-5]
CCDS; CCDS45273.1; -. [P09493-1]
CCDS; CCDS58368.1; -. [P09493-8]
CCDS; CCDS58369.1; -. [P09493-9]
PIR; A27674; A27674.
PIR; A27678; A25825.
PIR; S05585; S05585.
RefSeq; NP_000357.3; NM_000366.5. [P09493-10]
RefSeq; NP_001018004.1; NM_001018004.1. [P09493-9]
RefSeq; NP_001018005.1; NM_001018005.1. [P09493-1]
RefSeq; NP_001018006.1; NM_001018006.1. [P09493-3]
RefSeq; NP_001018007.1; NM_001018007.1. [P09493-7]
RefSeq; NP_001018008.1; NM_001018008.1. [P09493-5]
RefSeq; NP_001018020.1; NM_001018020.1. [P09493-8]
RefSeq; NP_001288173.1; NM_001301244.1. [P09493-6]
RefSeq; NP_001317273.1; NM_001330344.1.
RefSeq; NP_001317275.1; NM_001330346.1.
RefSeq; NP_001317280.1; NM_001330351.1.
UniGene; Hs.133892; -.
UniGene; Hs.602995; -.
PDB; 3MUD; X-ray; 2.20 A; C/D=1-40.
PDB; 5KHT; X-ray; 1.50 A; A/B/C/D=1-52.
PDBsum; 3MUD; -.
PDBsum; 5KHT; -.
ProteinModelPortal; P09493; -.
SMR; P09493; -.
BioGrid; 113021; 128.
IntAct; P09493; 38.
MINT; MINT-1458755; -.
iPTMnet; P09493; -.
PhosphoSitePlus; P09493; -.
SwissPalm; P09493; -.
BioMuta; TPM1; -.
DMDM; 136092; -.
UCD-2DPAGE; P09493; -.
EPD; P09493; -.
MaxQB; P09493; -.
PeptideAtlas; P09493; -.
PRIDE; P09493; -.
DNASU; 7168; -.
Ensembl; ENST00000267996; ENSP00000267996; ENSG00000140416. [P09493-7]
Ensembl; ENST00000288398; ENSP00000288398; ENSG00000140416. [P09493-10]
Ensembl; ENST00000334895; ENSP00000334624; ENSG00000140416. [P09493-5]
Ensembl; ENST00000358278; ENSP00000351022; ENSG00000140416. [P09493-3]
Ensembl; ENST00000403994; ENSP00000385107; ENSG00000140416. [P09493-1]
Ensembl; ENST00000559397; ENSP00000452879; ENSG00000140416. [P09493-8]
Ensembl; ENST00000559556; ENSP00000453941; ENSG00000140416. [P09493-9]
GeneID; 7168; -.
KEGG; hsa:7168; -.
UCSC; uc002alg.4; human. [P09493-1]
CTD; 7168; -.
DisGeNET; 7168; -.
EuPathDB; HostDB:ENSG00000140416.19; -.
GeneCards; TPM1; -.
GeneReviews; TPM1; -.
HGNC; HGNC:12010; TPM1.
HPA; CAB017698; -.
HPA; HPA000261; -.
HPA; HPA047089; -.
HPA; HPA053624; -.
MalaCards; TPM1; -.
MIM; 115196; phenotype.
MIM; 191010; gene.
MIM; 611878; phenotype.
neXtProt; NX_P09493; -.
OpenTargets; ENSG00000140416; -.
Orphanet; 154; Familial isolated dilated cardiomyopathy.
Orphanet; 155; Familial isolated hypertrophic cardiomyopathy.
Orphanet; 54260; Left ventricular noncompaction.
PharmGKB; PA36690; -.
GeneTree; ENSGT00550000074494; -.
HOGENOM; HOG000231521; -.
HOVERGEN; HBG107404; -.
InParanoid; P09493; -.
KO; K10373; -.
PhylomeDB; P09493; -.
TreeFam; TF351519; -.
Reactome; R-HSA-390522; Striated Muscle Contraction.
Reactome; R-HSA-445355; Smooth Muscle Contraction.
ChiTaRS; TPM1; human.
GeneWiki; TPM1; -.
GenomeRNAi; 7168; -.
PRO; PR:P09493; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000140416; -.
ExpressionAtlas; P09493; baseline and differential.
Genevisible; P09493; HS.
GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
GO; GO:0005884; C:actin filament; IBA:GO_Central.
GO; GO:0032059; C:bleb; IMP:BHF-UCL.
GO; GO:0005856; C:cytoskeleton; TAS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0031941; C:filamentous actin; IEA:Ensembl.
GO; GO:0005862; C:muscle thin filament tropomyosin; TAS:ProtInc.
GO; GO:0032587; C:ruffle membrane; IDA:BHF-UCL.
GO; GO:0030017; C:sarcomere; TAS:BHF-UCL.
GO; GO:0001725; C:stress fiber; IDA:BHF-UCL.
GO; GO:0003779; F:actin binding; TAS:BHF-UCL.
GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
GO; GO:0008092; F:cytoskeletal protein binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:BHF-UCL.
GO; GO:0008307; F:structural constituent of muscle; TAS:ProtInc.
GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
GO; GO:0060048; P:cardiac muscle contraction; IMP:BHF-UCL.
GO; GO:0034614; P:cellular response to reactive oxygen species; IEP:BHF-UCL.
GO; GO:0007010; P:cytoskeleton organization; TAS:BHF-UCL.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0006928; P:movement of cell or subcellular component; TAS:UniProtKB.
GO; GO:0006936; P:muscle contraction; TAS:Reactome.
GO; GO:0030049; P:muscle filament sliding; ISS:BHF-UCL.
GO; GO:0030336; P:negative regulation of cell migration; ISS:BHF-UCL.
GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; IMP:BHF-UCL.
GO; GO:1904706; P:negative regulation of vascular smooth muscle cell proliferation; IMP:BHF-UCL.
GO; GO:0032781; P:positive regulation of ATPase activity; ISS:BHF-UCL.
GO; GO:0045785; P:positive regulation of cell adhesion; ISS:BHF-UCL.
GO; GO:0003065; P:positive regulation of heart rate by epinephrine; ISS:BHF-UCL.
GO; GO:0051496; P:positive regulation of stress fiber assembly; ISS:BHF-UCL.
GO; GO:0008360; P:regulation of cell shape; IMP:BHF-UCL.
GO; GO:0008016; P:regulation of heart contraction; TAS:ProtInc.
GO; GO:0006937; P:regulation of muscle contraction; TAS:ProtInc.
GO; GO:0031529; P:ruffle organization; ISS:BHF-UCL.
GO; GO:0045214; P:sarcomere organization; IMP:BHF-UCL.
GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IMP:BHF-UCL.
GO; GO:0042060; P:wound healing; ISS:BHF-UCL.
InterPro; IPR000533; Tropomyosin.
Pfam; PF00261; Tropomyosin; 1.
PRINTS; PR00194; TROPOMYOSIN.
PROSITE; PS00326; TROPOMYOSIN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Actin-binding; Alternative splicing;
Cardiomyopathy; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Direct protein sequencing; Disease mutation;
Muscle protein; Phosphoprotein; Reference proteome.
CHAIN 1 284 Tropomyosin alpha-1 chain.
/FTId=PRO_0000205620.
COILED 1 284 {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000269|PubMed:3548719}.
MOD_RES 45 45 Phosphoserine.
{ECO:0000250|UniProtKB:P04692}.
MOD_RES 53 53 Phosphothreonine.
{ECO:0000250|UniProtKB:P07951}.
MOD_RES 61 61 Phosphoserine.
{ECO:0000250|UniProtKB:P58774}.
MOD_RES 79 79 Phosphothreonine.
{ECO:0000250|UniProtKB:P07951}.
MOD_RES 87 87 Phosphoserine.
{ECO:0000250|UniProtKB:P06753}.
MOD_RES 108 108 Phosphothreonine.
{ECO:0000250|UniProtKB:P07951}.
MOD_RES 174 174 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 186 186 Phosphoserine.
{ECO:0000250|UniProtKB:P58771}.
MOD_RES 206 206 Phosphoserine.
{ECO:0000250|UniProtKB:P58771}.
MOD_RES 215 215 Phosphoserine.
{ECO:0000250|UniProtKB:P58775}.
MOD_RES 252 252 Phosphoserine.
{ECO:0000250|UniProtKB:P58771}.
MOD_RES 261 261 Phosphotyrosine.
{ECO:0000250|UniProtKB:P04692}.
MOD_RES 271 271 Phosphoserine.
{ECO:0000250|UniProtKB:P58771}.
MOD_RES 282 282 Phosphothreonine.
{ECO:0000250|UniProtKB:P07951}.
MOD_RES 283 283 Phosphoserine; by DAPK1.
{ECO:0000269|PubMed:17895359}.
VAR_SEQ 1 80 MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLED
ELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATD
-> MCRLRIFLRTASSEHLHERKLRET (in isoform
2). {ECO:0000303|PubMed:3138425}.
/FTId=VSP_006576.
VAR_SEQ 1 80 MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLED
ELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATD
-> MAGSSSLEAVRRKIRSLQEQADAAEERAGTLQRELDHE
RKLRET (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_017498.
VAR_SEQ 41 80 DELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATD
-> EDIAAKEKLLRVSEDERDRVLEELHKAEDSLLAAEEAA
AK (in isoform 6 and isoform 7).
{ECO:0000303|PubMed:15249230,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_036064.
VAR_SEQ 41 53 DELVSLQKKLKGT -> EDIAAKEKLLRVS (in
isoform 8). {ECO:0000305}.
/FTId=VSP_047297.
VAR_SEQ 57 80 LDKYSEALKDAQEKLELAEKKATD -> RDRVLEELHKAED
SLLAAEEAAAK (in isoform 8).
{ECO:0000305}.
/FTId=VSP_047298.
VAR_SEQ 189 212 KCAELEEELKTVTNNLKSLEAQAE -> QVRQLEEQLRIMD
SDLESINAAED (in isoform 2).
{ECO:0000303|PubMed:3138425}.
/FTId=VSP_006578.
VAR_SEQ 189 212 KCAELEEELKTVTNNLKSLEAQAE -> QVRQLEEQLRIMD
QTLKALMAAED (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:3336357,
ECO:0000303|PubMed:3336363}.
/FTId=VSP_006577.
VAR_SEQ 189 192 KCAE -> QVRQ (in isoform 8 and isoform
10). {ECO:0000305}.
/FTId=VSP_047299.
VAR_SEQ 196 212 ELKTVTNNLKSLEAQAE -> QLRIMDQTLKALMAAED
(in isoform 8 and isoform 10).
{ECO:0000305}.
/FTId=VSP_047300.
VAR_SEQ 258 284 DELYAQKLKYKAISEELDHALNDMTSI -> EKVAHAKEEN
LSMHQMLDQTLLELNNM (in isoform 2, isoform
3, isoform 7, isoform 8 and isoform 9).
{ECO:0000303|PubMed:17974005,
ECO:0000303|PubMed:3138425,
ECO:0000303|PubMed:3336357,
ECO:0000303|PubMed:3336363}.
/FTId=VSP_006579.
VAR_SEQ 259 284 ELYAQKLKYKAISEELDHALNDMTSI -> QLYQQLEQNRR
LTNELKLALNED (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_017499.
VAR_SEQ 284 284 I -> M (in isoform 10). {ECO:0000305}.
/FTId=VSP_047301.
VARIANT 40 40 E -> K (in CMD1Y; dbSNP:rs104894501).
{ECO:0000269|PubMed:11273725}.
/FTId=VAR_043986.
VARIANT 54 54 E -> K (in CMD1Y; dbSNP:rs104894505).
{ECO:0000269|PubMed:11273725}.
/FTId=VAR_043987.
VARIANT 63 63 A -> V (in CMH3; dbSNP:rs199476306).
{ECO:0000269|PubMed:8523464}.
/FTId=VAR_013135.
VARIANT 175 175 D -> N (in CMH3; no change in
homodimerization; no change in homodimer
thermal stability; decreased actin
binding; recessive effect in the
homodimer; increased calcium-dependent
regulation of myosin binding to actin
filaments; dominant effect in the
homodimer; dbSNP:rs28934270).
{ECO:0000269|PubMed:23170982,
ECO:0000269|PubMed:7898523,
ECO:0000269|PubMed:8205619,
ECO:0000269|PubMed:8523464,
ECO:0000269|PubMed:9822100}.
/FTId=VAR_007601.
VARIANT 180 180 E -> G (in CMH3; no change in
homodimerization; decreased in hom odimer
thermal stability; decreased in actin
binding; increased calcium-dependent
regulation of myosin binding to actin
filaments; dominant effect in the
homodimer; dbSNP:rs28934269).
{ECO:0000269|PubMed:23170982,
ECO:0000269|PubMed:8205619}.
/FTId=VAR_007602.
VARIANT 180 180 E -> V (in CMH3; dbSNP:rs104894502).
{ECO:0000269|PubMed:12974739}.
/FTId=VAR_029452.
VARIANT 192 192 E -> K (in LVNC9; dbSNP:rs199476315).
{ECO:0000269|PubMed:21551322}.
/FTId=VAR_070121.
VARIANT 248 248 K -> E (in LVNC9; dbSNP:rs199476319).
{ECO:0000269|PubMed:21551322}.
/FTId=VAR_070122.
MUTAGEN 15 15 K->N: Impairs interaction with LMOD2 and
TMOD1. {ECO:0000269|PubMed:26873245}.
MUTAGEN 283 283 S->A: Loss of phosphorylation and
decreased formation of actin stress
fibers. {ECO:0000269|PubMed:17895359}.
MUTAGEN 283 283 S->E: Increased formation of actin stress
fibers. {ECO:0000269|PubMed:17895359}.
CONFLICT 109 109 A -> V (in Ref. 11; CAA30930).
{ECO:0000305}.
CONFLICT 203 203 N -> D (in Ref. 4; AAT68294/AAT68295).
{ECO:0000305}.
HELIX 1 28 {ECO:0000244|PDB:5KHT}.
SEQUENCE 284 AA; 32709 MW; F57139E2B0972F4D CRC64;
MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEDRSKQLE DELVSLQKKL KGTEDELDKY
SEALKDAQEK LELAEKKATD AEADVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA
DESERGMKVI ESRAQKDEEK MEIQEIQLKE AKHIAEDADR KYEEVARKLV IIESDLERAE
ERAELSEGKC AELEEELKTV TNNLKSLEAQ AEKYSQKEDR YEEEIKVLSD KLKEAETRAE
FAERSVTKLE KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI


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