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Myosin-7 (Myosin heavy chain 7) (Myosin heavy chain slow isoform) (MyHC-slow) (Myosin heavy chain, cardiac muscle beta isoform) (MyHC-beta)

 MYH7_HUMAN              Reviewed;        1935 AA.
P12883; A2TDB6; B6D424; Q14836; Q14837; Q14904; Q16579; Q2M1Y6;
Q92679; Q9H1D5; Q9UDA2; Q9UMM8;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
06-DEC-2005, sequence version 5.
25-OCT-2017, entry version 212.
RecName: Full=Myosin-7;
AltName: Full=Myosin heavy chain 7;
AltName: Full=Myosin heavy chain slow isoform;
Short=MyHC-slow;
AltName: Full=Myosin heavy chain, cardiac muscle beta isoform;
Short=MyHC-beta;
Name=MYH7; Synonyms=MYHCB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT SER-1124.
PubMed=2249844; DOI=10.1016/0888-7543(90)90272-V;
Jaenicke T., Diederich K.W., Haas W., Schleich J., Lichter P.,
Pfordt M., Bach A., Vosberg H.P.;
"The complete sequence of the human beta-myosin heavy chain gene and a
comparative analysis of its product.";
Genomics 8:194-206(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-107.
PubMed=2362820; DOI=10.1093/nar/18.12.3647;
Liew C.-C., Sole M.J., Yamauchi-Takihara K., Kellam B., Anderson D.H.,
Lin L., Liew J.;
"Complete sequence and organization of the human cardiac beta-myosin
heavy chain gene.";
Nucleic Acids Res. 18:3647-3651(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10996847;
DOI=10.1002/1097-4644(20001215)79:4<566::AID-JCB50>3.3.CO;2-5;
Wendel B., Reinhard R., Wachtendorf U., Zacharzowsky U.B.,
Osterziel K.J., Schulte H.D., Haase H., Hoehe M.R., Morano I.;
"The human beta-myosin heavy chain gene: sequence diversity and
functional characteristics of the protein.";
J. Cell. Biochem. 79:566-575(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
Smaniotto G., Melacini P.;
"Diverse clinicopathologic profiles and determinants of progressive
heart failure in hypertrophic cardiomyopathy.";
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
[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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-176, AND VARIANT GLU-107.
PubMed=2726733; DOI=10.1073/pnas.86.10.3504;
Yamauchi-Takihara K., Sole M.J., Liew J., Ing D., Liew C.-C.;
"Characterization of human cardiac myosin heavy chain genes.";
Proc. Natl. Acad. Sci. U.S.A. 86:3504-3508(1989).
[9]
ERRATUM.
Yamauchi-Takihara K., Sole M.J., Liew J., Ing D., Liew C.-C.;
Proc. Natl. Acad. Sci. U.S.A. 86:7416-7417(1989).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 370-434, TISSUE SPECIFICITY, AND VARIANT
GLN-403.
TISSUE=Skeletal muscle;
PubMed=8514894; DOI=10.1172/JCI116530;
Cuda G., Fananapazir L., Zhu W.S., Sellers J.R., Epstein N.D.;
"Skeletal muscle expression and abnormal function of beta-myosin in
hypertrophic cardiomyopathy.";
J. Clin. Invest. 91:2861-2865(1993).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 653-720.
PubMed=2522082; DOI=10.1007/BF00278991;
Diederich K.W., Eisele I., Ried T., Jaenicke T., Lichter P.,
Vosberg H.P.;
"Isolation and characterization of the complete human beta-myosin
heavy chain gene.";
Hum. Genet. 81:214-220(1989).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 684-721; 975-1111 AND 1853-1935.
PubMed=3021460; DOI=10.1111/j.1432-1033.1986.tb09989.x;
Lichter P., Umeda P.K., Levin J.E., Vosberg H.P.;
"Partial characterization of the human beta-myosin heavy-chain gene
which is expressed in heart and skeletal muscle.";
Eur. J. Biochem. 160:419-426(1986).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 785-1935.
TISSUE=Skeletal muscle;
PubMed=1691980; DOI=10.1111/j.1432-1033.1990.tb15459.x;
Bober E., Buchberger-Seidl A., Braun T., Singh S., Goedde H.W.,
Arnold H.H.;
"Identification of three developmentally controlled isoforms of human
myosin heavy chains.";
Eur. J. Biochem. 189:55-65(1990).
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 1310-1935.
PubMed=2421254; DOI=10.1093/nar/14.7.2951;
Saez L., Leinwand L.A.;
"Characterization of diverse forms of myosin heavy chain expressed in
adult human skeletal muscle.";
Nucleic Acids Res. 14:2951-2969(1986).
[15]
SEQUENCE REVISION.
Leinwand L.A.;
Submitted (MAR-1988) to the EMBL/GenBank/DDBJ databases.
[16]
NUCLEOTIDE SEQUENCE [MRNA] OF 1393-1935.
PubMed=3032769; DOI=10.1007/BF00283049;
Jandreski M.A., Liew C.-C.;
"Construction of a human ventricular cDNA library and characterization
of a beta myosin heavy chain cDNA clone.";
Hum. Genet. 76:47-53(1987).
[17]
NUCLEOTIDE SEQUENCE [MRNA] OF 1412-1935.
PubMed=2969919; DOI=10.1172/JCI113627;
Kurabayashi M., Tsuchimochi H., Komuro I., Takaku F., Yazaki Y.;
"Molecular cloning and characterization of human cardiac alpha- and
beta-form myosin heavy chain complementary DNA clones. Regulation of
expression during development and pressure overload in human atrium.";
J. Clin. Invest. 82:524-531(1988).
[18]
NUCLEOTIDE SEQUENCE [MRNA] OF 1854-1935.
PubMed=3037493; DOI=10.1093/nar/15.13.5443;
Saez L.J., Gianola K.M., McNally E.M., Feghali R., Eddy R.,
Shows T.B., Leinwand L.A.;
"Human cardiac myosin heavy chain genes and their linkage in the
genome.";
Nucleic Acids Res. 15:5443-5459(1987).
[19]
REVIEW ON VARIANTS.
PubMed=8533830; DOI=10.1002/ajmg.1320580314;
Arai S., Matsuoka R., Hirayama K., Sukurai H., Tamura M., Ozawa T.,
Kimura M., Imamura S., Furutani Y., Joh-o K., Kawana M., Takao A.,
Hosoda S., Momma K.;
"Missense mutation of the beta-cardiac myosin heavy-chain gene in
hypertrophic cardiomyopathy.";
Am. J. Med. Genet. 58:267-276(1995).
[20]
INVOLVEMENT IN CMH1, AND VARIANTS CMH1 HIS-243; ASP-497 AND GLY-906.
PubMed=16267253; DOI=10.1161/CIRCULATIONAHA.105.547448;
Arad M., Penas-Lado M., Monserrat L., Maron B.J., Sherrid M., Ho C.Y.,
Barr S., Karim A., Olson T.M., Kamisago M., Seidman J.G.,
Seidman C.E.;
"Gene mutations in apical hypertrophic cardiomyopathy.";
Circulation 112:2805-2811(2005).
[21]
INVOLVEMENT IN MSMA, AND VARIANT MSMA PRO-1793.
PubMed=16684601; DOI=10.1016/j.nmd.2006.03.011;
Dye D.E., Azzarelli B., Goebel H.H., Laing N.G.;
"Novel slow-skeletal myosin (MYH7) mutation in the original myosin
storage myopathy kindred.";
Neuromuscul. Disord. 16:357-360(2006).
[22]
INVOLVEMENT IN CMD1S, AND VARIANTS CMD1S ASP-239 DEL; HIS-243;
CYS-1359 AND THR-1776.
PubMed=18506004; DOI=10.1161/CIRCULATIONAHA.107.746164;
Klaassen S., Probst S., Oechslin E., Gerull B., Krings G., Schuler P.,
Greutmann M., Huerlimann D., Yegitbasi M., Pons L., Gramlich M.,
Drenckhahn J.D., Heuser A., Berger F., Jenni R., Thierfelder L.;
"Mutations in sarcomere protein genes in left ventricular
noncompaction.";
Circulation 117:2893-2901(2008).
[23]
INVOLVEMENT IN CMH1, AND VARIANT CMH1 SER-453.
PubMed=18175163; DOI=10.1007/s00246-007-9177-9;
Frazier A., Judge D.P., Schulman S.P., Johnson N., Holmes K.W.,
Murphy A.M.;
"Familial hypertrophic cardiomyopathy associated with cardiac beta-
myosin heavy chain and troponin I mutations.";
Pediatr. Cardiol. 29:846-850(2008).
[24]
INTERACTION WITH LRRC39.
PubMed=20847312; DOI=10.1161/CIRCRESAHA.110.222372;
Will R.D., Eden M., Just S., Hansen A., Eder A., Frank D., Kuhn C.,
Seeger T.S., Oehl U., Wiemann S., Korn B., Koegl M., Rottbauer W.,
Eschenhagen T., Katus H.A., Frey N.;
"Myomasp/LRRC39, a heart- and muscle-specific protein, is a novel
component of the sarcomeric M-band and is involved in stretch
sensing.";
Circ. Res. 107:1253-1264(2010).
[25]
INTERACTION WITH ECM29.
PubMed=20682791; DOI=10.1074/jbc.M110.154120;
Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S.,
Hughes R.E., Rechsteiner M.;
"A protein interaction network for Ecm29 links the 26 S proteasome to
molecular motors and endosomal components.";
J. Biol. Chem. 285:31616-31633(2010).
[26]
INVOLVEMENT IN CMD1S, AND VARIANTS CMD1S ASP-283; ASN-350; PRO-390;
GLU-1220 DEL; ASN-1459; LYS-1573 AND LYS-1918.
PubMed=21127202; DOI=10.1161/CIRCGENETICS.110.957985;
Postma A.V., van Engelen K., van de Meerakker J., Rahman T.,
Probst S., Baars M.J., Bauer U., Pickardt T., Sperling S.R.,
Berger F., Moorman A.F., Mulder B.J., Thierfelder L., Keavney B.,
Goodship J., Klaassen S.;
"Mutations in the sarcomere gene MYH7 in Ebstein anomaly.";
Circ. Cardiovasc. Genet. 4:43-50(2011).
[27]
INVOLVEMENT IN MSMB, AND VARIANT MSMB TRP-1820.
PubMed=25666907; DOI=10.1016/j.nmd.2015.01.007;
Yueceyar N., Ayhan O., Karasoy H., Tolun A.;
"Homozygous MYH7 R1820W mutation results in recessive myosin storage
myopathy: scapuloperoneal and respiratory weakness with dilated
cardiomyopathy.";
Neuromuscul. Disord. 25:340-344(2015).
[28]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 838-963, AND X-RAY
CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 838-963 OF VARIANT CMH1 LYS-924.
PubMed=17095604; DOI=10.1073/pnas.0606741103;
Blankenfeldt W., Thoma N.H., Wray J.S., Gautel M., Schlichting I.;
"Crystal structures of human cardiac beta-myosin II S2-Delta provide
insight into the functional role of the S2 subfragment.";
Proc. Natl. Acad. Sci. U.S.A. 103:17713-17717(2006).
[29]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1-787 IN COMPLEX WITH AN
INHIBITOR, AND FUNCTION.
PubMed=26246073; DOI=10.1038/ncomms8974;
Winkelmann D.A., Forgacs E., Miller M.T., Stock A.M.;
"Structural basis for drug-induced allosteric changes to human beta-
cardiac myosin motor activity.";
Nat. Commun. 6:7974-7974(2015).
[30]
X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) OF 1173-1238; 1361-1425;
1551-1609 AND 1777-1855, COILED COIL, AND DOMAIN.
PubMed=26150528; DOI=10.1073/pnas.1505813112;
Taylor K.C., Buvoli M., Korkmaz E.N., Buvoli A., Zheng Y.,
Heinze N.T., Cui Q., Leinwand L.A., Rayment I.;
"Skip residues modulate the structural properties of the myosin rod
and guide thick filament assembly.";
Proc. Natl. Acad. Sci. U.S.A. 112:E3806-E3815(2015).
[31]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1468-1692, AND COILED COIL.
PubMed=26573747; DOI=10.1002/prot.24964;
Korkmaz E.N., Taylor K.C., Andreas M.P., Ajay G., Heinze N.T., Cui Q.,
Rayment I.;
"A composite approach towards a complete model of the myosin rod.";
Proteins 84:172-189(2016).
[32]
VARIANT CMH1 GLN-403.
PubMed=1975517; DOI=10.1016/0092-8674(90)90274-I;
Geisterfer-Lowrance A.A.T., Kass S., Tanigawa G., Vosberg H.-P.,
McKenna W., Seidman C.E., Seidman J.G.;
"A molecular basis for familial hypertrophic cardiomyopathy: a beta
cardiac myosin heavy chain gene missense mutation.";
Cell 62:999-1006(1990).
[33]
VARIANT CMH1 ASN-615.
PubMed=1417858; DOI=10.1016/0006-291X(92)92396-F;
Nishi H., Kimura A., Harada H., Toshima H., Sasazuki T.;
"Novel missense mutation in cardiac beta myosin heavy chain gene found
in a Japanese patient with hypertrophic cardiomyopathy.";
Biochem. Biophys. Res. Commun. 188:379-387(1992).
[34]
VARIANTS CMH1 GLN-403 AND VAL-908.
PubMed=1638703; DOI=10.1161/01.CIR.86.2.345;
Epstein N.D., Cohn G.M., Cyran F., Fananapazir L.;
"Differences in clinical expression of hypertrophic cardiomyopathy
associated with two distinct mutations in the beta-myosin heavy chain
gene. A 908Leu-->Val mutation and a 403Arg-->Gln mutation.";
Circulation 86:345-352(1992).
[35]
VARIANTS CMH1 GLN-249; GLN-403; CYS-453 AND MET-606.
PubMed=1552912; DOI=10.1056/NEJM199204233261703;
Watkins H., Rosenzweig A., Hwang D.S., Levi T., McKenna W.,
Seidmann C.E., Seidmann J.G.;
"Characteristics and prognostic implications of myosin missense
mutations in familial hypertrophic cardiomyopathy.";
N. Engl. J. Med. 326:1108-1114(1992).
[36]
VARIANTS CMH1 GLN-403; CYS-453; ARG-584 AND MET-606.
PubMed=8250038;
Watkins H., Thierfelder L., Anan R., Jarcho J., Matsumori A.,
McKenna W., Seidman J.G., Seidman C.E.;
"Independent origin of identical beta cardiac myosin heavy-chain
mutations in hypertrophic cardiomyopathy.";
Am. J. Hum. Genet. 53:1180-1185(1993).
[37]
VARIANT CMH1 GLY-778.
PubMed=8343162; DOI=10.1006/bbrc.1993.1891;
Harada H., Kimura A., Nishi H., Sasazuki T., Toshima H.;
"A missense mutation of cardiac beta-myosin heavy chain gene linked to
familial hypertrophic cardiomyopathy in affected Japanese families.";
Biochem. Biophys. Res. Commun. 194:791-798(1993).
[38]
VARIANT CMH1 VAL-908.
PubMed=8435239; DOI=10.1136/hrt.69.2.136;
Al-Mahdawi S., Chamberlain S., Cleland J., Nihoyannopoulos P.,
Gilligan D., French J., Choudhury L., Williamson R., Oakley C.;
"Identification of a mutation in the beta cardiac myosin heavy chain
gene in a family with hypertrophic cardiomyopathy.";
Br. Heart J. 69:136-141(1993).
[39]
VARIANT CMH1 TRP-403.
PubMed=8268932; DOI=10.1093/hmg/2.10.1731;
Moolman J.C., Brink P.A., Corfield V.A.;
"Identification of a new missense mutation at Arg403, a CpG mutation
hotspot, in exon 13 of the beta-myosin heavy chain gene in
hypertrophic cardiomyopathy.";
Hum. Mol. Genet. 2:1731-1732(1993).
[40]
VARIANTS CMH1 LEU-403 AND TRP-403.
PubMed=8254035; DOI=10.1172/JCI116900;
Dausse E., Komajda M., Fetler L., Dubourg O., Dufour C., Carrier L.,
Wisnewsky C., Bercovici J., Hengstenberg C., Al-Mahdawi S.;
"Familial hypertrophic cardiomyopathy. Microsatellite haplotyping and
identification of a hot spot for mutations in the beta-myosin heavy
chain gene.";
J. Clin. Invest. 92:2807-2813(1993).
[41]
VARIANTS CMH1 GLU-256 AND ARG-741.
PubMed=8483915; DOI=10.1073/pnas.90.9.3993;
Fananapazir L., Dalakas M.C., Cyran F., Cohn G., Epstein N.D.;
"Missense mutations in the beta-myosin heavy-chain gene cause central
core disease in hypertrophic cardiomyopathy.";
Proc. Natl. Acad. Sci. U.S.A. 90:3993-3997(1993).
[42]
VARIANT CMH1 GLN-719.
PubMed=7848441; DOI=10.1093/hmg/3.6.1025;
Consevage M.W., Salada G.C., Baylen B.G., Ladda R.L., Rogan P.K.;
"A new missense mutation, Arg719Gln, in the beta-cardiac heavy chain
myosin gene of patients with familial hypertrophic cardiomyopathy.";
Hum. Mol. Genet. 3:1025-1026(1994).
[43]
VARIANT CMH1 TRP-719.
PubMed=7874131;
Greve G., Bachinski L., Friedman D.L., Czernuzewicz G., Anan R.,
Towbin J.A., Seidman C.E., Roberts R.;
"Isolation of a de novo mutant myocardial beta MHC protein in a
pedigree with hypertrophic cardiomyopathy.";
Hum. Mol. Genet. 3:2073-2075(1994).
[44]
VARIANTS CMH1 CYS-513; ARG-716 AND TRP-719.
PubMed=8282798; DOI=10.1172/JCI116957;
Anan R., Greve G., Thierfelder L., Watkins H., McKenna W., Solomon S.,
Vecchio C., Shono H., Nakao S., Tanaka H., Mares A. Jr., Towbin J.A.,
Spirito P., Roberts R., Seidman J.G., Seidman C.E.;
"Prognostic implications of novel beta cardiac myosin heavy chain gene
mutations that cause familial hypertrophic cardiomyopathy.";
J. Clin. Invest. 93:280-285(1994).
[45]
VARIANT CMH1 THR-797.
PubMed=7581410; DOI=10.1002/humu.1380060219;
Moolman J.C., Brink P.A., Corfield V.A.;
"Identification of a novel Ala797Thr mutation in exon 21 of the beta-
myosin heavy chain gene in hypertrophic cardiomyopathy.";
Hum. Mutat. 6:197-198(1995).
[46]
VARIANTS CMH1 ILE-124; CYS-162; LYS-187; LYS-222; LEU-244; HIS-663;
ASN-782 AND HIS-870.
PubMed=7731997; DOI=10.1073/pnas.92.9.3864;
Rayment I., Holden H.M., Sellers J.R., Fananapazir L., Epstein N.D.;
"Structural interpretation of the mutations in the beta-cardiac myosin
that have been implicated in familial hypertrophic cardiomyopathy.";
Proc. Natl. Acad. Sci. U.S.A. 92:3864-3868(1995).
[47]
VARIANT CMH1 CYS-453.
PubMed=8655135; DOI=10.1007/BF02281865;
Ko Y.-L., Chen J.-J., Tang T.-K., Cheng J.-J., Lin S.-Y., Liou Y.-C.,
Kuan P., Wu C.-W., Lien W.-P., Liew C.-C.;
"Malignant familial hypertrophic cardiomyopathy in a family with a
453Arg-->Cys mutation in the beta-myosin heavy chain gene: coexistence
of sudden death and end-stage heart failure.";
Hum. Genet. 97:585-590(1996).
[48]
VARIANT CMH1 ASN-383.
PubMed=8899546; DOI=10.1006/jmcc.1996.0180;
Kuang S.-Q., Yu J.-D., Lu L., He L.-M., Gong L.-S., Chen S.-J.,
Chen Z.;
"Identification of a novel missense mutation in the cardiac beta-
myosin heavy chain gene in a Chinese patient with sporadic
hypertrophic cardiomyopathy.";
J. Mol. Cell. Cardiol. 28:1879-1883(1996).
[49]
VARIANTS CMH1 GLN-249 AND GLU-450.
PubMed=10065021;
Arbustini E., Fasani R., Morbini P., Diegoli M., Grasso M.,
Dal Bello B., Marangoni E., Banfi P., Banchieri N., Bellini O.,
Comi G., Narula J., Campana C., Gavazzi A., Danesino C., Vigano M.;
"Coexistence of mitochondrial DNA and beta myosin heavy chain
mutations in hypertrophic cardiomyopathy with late congestive heart
failure.";
Heart 80:548-558(1998).
[50]
ERRATUM.
Arbustini E., Fasani R., Morbini P., Diegoli M., Grasso M.,
Dal Bello B., Marangoni E., Banfi P., Banchieri N., Bellini O.,
Comi G., Narula J., Campana C., Gavazzi A., Danesino C., Vigano M.;
Heart 81:330-330(1999).
[51]
VARIANTS CMH1 THR-349 AND TRP-719.
PubMed=9544842; DOI=10.1007/s004390050695;
Jeschke B., Uhl K., Weist B., Schroder D., Meitinger T., Dohlemann C.,
Vosberg H.-P.;
"A high risk phenotype of hypertrophic cardiomyopathy associated with
a compound genotype of two mutated beta-myosin heavy chain genes.";
Hum. Genet. 102:299-304(1998).
[52]
VARIANTS CMH1 THR-263; TRP-719; CYS-723 AND GLU-930 DEL.
PubMed=9829907;
DOI=10.1002/(SICI)1098-1004(1998)12:6<385::AID-HUMU4>3.0.CO;2-E;
Tesson F., Richard P., Charron P., Mathieu B., Cruaud C., Carrier L.,
Dubourg O., Lautie N., Desnos M., Millaire A., Isnard R., Hagege A.A.,
Bouhour J.-B., Bennaceur M., Hainque B., Guicheney P., Schwartz K.,
Komajda M.;
"Genotype-phenotype analysis in four families with mutations in beta-
myosin heavy chain gene responsible for familial hypertrophic
cardiomyopathy.";
Hum. Mutat. 12:385-392(1998).
[53]
VARIANTS CMH1 SER-696 AND TRP-719.
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).
[54]
VARIANTS CMH1 TRP-403; LYS-499; GLN-719 AND THR-797.
PubMed=10521296; DOI=10.1086/302623;
Moolman-Smook J.C., De Lange W.J., Bruwer E.C.D., Brink P.A.,
Corfield V.A.;
"The origins of hypertrophic cardiomyopathy-causing mutations in two
South African subpopulations: a unique profile of both independent and
founder events.";
Am. J. Hum. Genet. 65:1308-1320(1999).
[55]
VARIANT CMH1 CYS-694.
PubMed=10563488; DOI=10.1034/j.1399-0004.1999.560313.x;
Andersen P.S., Havndrup O., Bundgaard H., Larsen L.A., Vuust J.,
Kjeldsen K., Christiansen M.;
"Adult-onset familial hypertrophic cardiomyopathy caused by a novel
mutation, R694C, in the MYH7 gene.";
Clin. Genet. 56:244-246(1999).
[56]
VARIANT CMH1 THR-190.
PubMed=10329202; DOI=10.1006/jmcc.1998.0911;
Bundgaard H., Havndrup O., Andersen P.S., Larsen L.A., Brandt N.J.,
Vuust J., Kjeldsen K., Christiansen M.;
"Familial hypertrophic cardiomyopathy associated with a novel missense
mutation affecting the ATP-binding region of the cardiac beta-myosin
heavy chain.";
J. Mol. Cell. Cardiol. 31:745-750(1999).
[57]
VARIANT CMH1 LEU-712.
PubMed=10679957;
DOI=10.1002/(SICI)1098-1004(200003)15:3<298::AID-HUMU22>3.0.CO;2-7;
Sakthivel S., Joseph P.K., Tharakan J.M., Vosberg H.-P.,
Rajamanickam C.;
"A novel missense mutation (R712L) adjacent to the 'active thiol'
region of the cardiac beta-myosin heavy chain gene causing
hypertrophic cardiomyopathy in an Indian family.";
Hum. Mutat. 15:298-299(2000).
[58]
VARIANTS CMH1 CYS-869 AND CYS-870.
PubMed=10862102;
DOI=10.1002/1098-1004(200006)15:6<584::AID-HUMU25>3.0.CO;2-R;
Anan R., Shono H., Tei C.;
"Novel cardiac beta-myosin heavy chain gene missense mutations (R869C
and R870C) that cause familial hypertrophic cardiomyopathy.";
Hum. Mutat. 15:584-584(2000).
[59]
VARIANT CMH1 GLY-723.
PubMed=11113006; DOI=10.1006/jmcc.2000.1260;
Enjuto M., Francino A., Navarro-Lopez F., Viles D., Pare J.-C.,
Ballesta A.M.;
"Malignant hypertrophic cardiomyopathy caused by the Arg723Gly
mutation in beta-myosin heavy chain gene.";
J. Mol. Cell. Cardiol. 32:2307-2313(2000).
[60]
VARIANTS CMD1S PRO-532 AND LEU-764.
PubMed=11106718; DOI=10.1056/NEJM200012073432304;
Kamisago M., Sharma S.D., DePalma S.R., Solomon S., Sharma P.,
McDonough B., Smoot L., Mullen M.P., Woolf P.K., Wigle E.D.,
Seidman J.G., Seidman C.E.;
"Mutations in sarcomere protein genes as a cause of dilated
cardiomyopathy.";
N. Engl. J. Med. 343:1688-1696(2000).
[61]
VARIANT CMH1 VAL-390.
PubMed=11214007; DOI=10.1080/140174300750064477;
Havndrup O., Bundgaard H., Andersen P.S., Larsen L.A., Vuust J.,
Kjeldsen K., Christiansen M.;
"A novel missense mutation, Leu390Val, in the cardiac beta-myosin
heavy chain associated with pronounced septal hypertrophy in two
families with hypertrophic cardiomyopathy.";
Scand. Cardiovasc. J. 34:558-563(2000).
[62]
VARIANT CMH1 ASP-743.
PubMed=11733062; DOI=10.1016/S0092-8674(01)00586-4;
Davis J.S., Hassanzadeh S., Winitsky S., Lin H., Satorius C.,
Vemuri R., Aletras A.H., Wen H., Epstein N.D.;
"The overall pattern of cardiac contraction depends on a spatial
gradient of myosin regulatory light chain phosphorylation.";
Cell 107:631-641(2001).
[63]
VARIANT CMH1 VAL-728.
PubMed=11424919; DOI=10.1136/jmg.38.6.385;
Blair E., Price S.J., Baty C.J., Oestman-Smith I., Watkins H.;
"Mutations in cis can confound genotype-phenotype correlations in
hypertrophic cardiomyopathy.";
J. Med. Genet. 38:385-388(2001).
[64]
VARIANTS CMH1 GLN-249; MET-406; CYS-453; MET-606; HIS-663 AND LYS-877.
PubMed=11133230; DOI=10.1006/jmcc.2000.1287;
Greber-Platzer S., Marx M., Fleischmann C., Suppan C., Dobner M.,
Wimmer M.;
"Beta-myosin heavy chain gene mutations and hypertrophic
cardiomyopathy in Austrian children.";
J. Mol. Cell. Cardiol. 33:141-148(2001).
[65]
VARIANTS CMD1S THR-223 AND LEU-642.
PubMed=12379228; DOI=10.1016/S0006-291X(02)02374-4;
Daehmlow S., Erdmann J., Knueppel T., Gille C., Froemmel C.,
Hummel M., Hetzer R., Regitz-Zagrosek V.;
"Novel mutations in sarcomeric protein genes in dilated
cardiomyopathy.";
Biochem. Biophys. Res. Commun. 298:116-120(2002).
[66]
VARIANTS CMH1 HIS-663; TRP-719; ARG-768 AND GLY-906.
PubMed=12081993; DOI=10.1161/01.CIR.0000019070.70491.6D;
Ho C.Y., Sweitzer N.K., McDonough B., Maron B.J., Casey S.A.,
Seidman J.G., Seidman C.E., Solomon S.D.;
"Assessment of diastolic function with Doppler tissue imaging to
predict genotype in preclinical hypertrophic cardiomyopathy.";
Circulation 105:2992-2997(2002).
[67]
VARIANTS CMH1 THR-1379 AND GLY-1776, AND VARIANT CYS-1491.
PubMed=11861413; DOI=10.1161/hh0302.104532;
Blair E., Redwood C., de Jesus Oliveira M., Moolman-Smook J.C.,
Brink P., Corfield V.A., Oestman-Smith I., Watkins H.;
"Mutations of the light meromyosin domain of the beta-myosin heavy
chain rod in hypertrophic cardiomyopathy.";
Circ. Res. 90:263-269(2002).
[68]
VARIANTS CMH1 GLN-249; THR-349; GLN-403; ARG-595; MET-606; GLN-719;
TRP-719; GLU-927 DEL AND LYS-1555.
PubMed=11968089; DOI=10.1002/humu.10074;
Waldmueller S., Freund P., Mauch S., Toder R., Vosberg H.-P.;
"Low-density DNA microarrays are versatile tools to screen for known
mutations in hypertrophic cardiomyopathy.";
Hum. Mutat. 19:560-569(2002).
[69]
VARIANT MSMA TRP-1845.
PubMed=14520662; DOI=10.1002/ana.10693;
Tajsharghi H., Thornell L.-E., Lindberg C., Lindvall B.,
Henriksson K.-G., Oldfors A.;
"Myosin storage myopathy associated with a heterozygous missense
mutation in MYH7.";
Ann. Neurol. 54:494-500(2003).
[70]
VARIANTS CMH1 CYS-453; MET-517 AND GLU-734.
PubMed=12951062; DOI=10.1016/j.bbrc.2003.08.014;
Nanni L., Pieroni M., Chimenti C., Simionati B., Zimbello R.,
Maseri A., Frustaci A., Lanfranchi G.;
"Hypertrophic cardiomyopathy: two homozygous cases with 'typical'
hypertrophic cardiomyopathy and three new mutations in cases with
progression to dilated cardiomyopathy.";
Biochem. Biophys. Res. Commun. 309:391-398(2003).
[71]
VARIANTS CMH1 THR-190; MET-320; VAL-390; VAL-601; MET-606; CYS-694;
GLU-778 AND GLN-846.
PubMed=12566107; DOI=10.1016/S0008-6363(02)00711-3;
Havndrup O., Bundgaard H., Andersen P.S., Larsen L.A., Vuust J.,
Kjeldsen K., Christiansen M.;
"Outcome of clinical versus genetic family screening in hypertrophic
cardiomyopathy with focus on cardiac beta-myosin gene mutations.";
Cardiovasc. Res. 57:347-357(2003).
[72]
VARIANTS CMH1 MET-39; ASN-188; HIS-204; SER-232; GLN-249; THR-263;
THR-355; LEU-403; GLN-403; TRP-403; VAL-428; THR-443; CYS-453;
SER-479; LYS-483; MET-606; ILE-659; SER-663; HIS-663; CYS-671;
ARG-716; GLN-719; TRP-719; CYS-723; GLU-733; ARG-741; ARG-768;
GLU-778; HIS-787; THR-852; GLY-869; GLU-883 DEL; GLU-930 DEL;
ARG-1135; GLN-1218; MET-1377; THR-1379; TRP-1382 AND THR-1777, AND
VARIANT MET-1692.
PubMed=12707239; DOI=10.1161/01.CIR.0000066323.15244.54;
Richard P., Charron P., Carrier L., Ledeuil C., Cheav T.,
Pichereau C., Benaiche A., Isnard R., Dubourg O., Burban M.,
Gueffet J.-P., Millaire A., Desnos M., Schwartz K., Hainque B.,
Komajda M.;
"Hypertrophic cardiomyopathy: distribution of disease genes, spectrum
of mutations, and implications for a molecular diagnosis strategy.";
Circulation 107:2227-2232(2003).
[73]
ERRATUM.
Richard P., Charron P., Carrier L., Ledeuil C., Cheav T.,
Pichereau C., Benaiche A., Isnard R., Dubourg O., Burban M.,
Gueffet J.-P., Millaire A., Desnos M., Schwartz K., Hainque B.,
Komajda M.;
Circulation 109:3258-3258(2004).
[74]
VARIANTS CMH1 TRP-143; TRP-403; ILE-411; SER-584; HIS-694; TRP-719;
THR-736; PHE-796; ILE-824; HIS-870; PHE-905; GLN-924 AND ASN-928.
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).
[75]
VARIANTS CMH1 GLY-143; ILE-148; GLN-207; LEU-211; GLU-351; GLN-403;
SER-479; ALA-500; ARG-571; HIS-663; CYS-671; THR-736; GLY-763;
ASN-782; LEU-822; GLU-882 AND VAL-908.
PubMed=12820698; DOI=10.1089/109065703321560895;
Mohiddin S.A., Begley D.A., McLam E., Cardoso J.-P., Winkler J.B.,
Sellers J.R., Fananapazir L.;
"Utility of genetic screening in hypertrophic cardiomyopathy:
prevalence and significance of novel and double (homozygous and
heterozygous) beta-myosin mutations.";
Genet. Test. 7:21-27(2003).
[76]
VARIANTS CMH1 THR-196; LEU-211; GLN-249; GLN-403; LEU-404; ILE-411;
CYS-453; ARG-716; CYS-870; VAL-908 AND LYS-930.
PubMed=12975413; DOI=10.1136/heart.89.10.1179;
Woo A., Rakowski H., Liew J.C., Zhao M.-S., Liew C.-C., Parker T.G.,
Zeller M., Wigle E.D., Sole M.J.;
"Mutations of the beta myosin heavy chain gene in hypertrophic
cardiomyopathy: critical functional sites determine prognosis.";
Heart 89:1179-1185(2003).
[77]
VARIANTS CMH1 VAL-774 AND ASN-782.
PubMed=12590187;
Moric E., Mazurek U., Polonska J., Domal-Kwiatkowska D., Smolik S.,
Kozakiewicz K., Tendera M., Wilczok T.;
"Three novel mutations in exon 21 encoding beta-cardiac myosin heavy
chain.";
J. Appl. Genet. 44:103-109(2003).
[78]
VARIANTS CMH1 GLU-430 AND LYS-924.
PubMed=12818575; DOI=10.1016/S0022-2828(03)00146-9;
Moerner S., Richard P., Kazzam E., Hellman U., Hainque B.,
Schwartz K., Waldenstroem A.;
"Identification of the genotypes causing hypertrophic cardiomyopathy
in northern Sweden.";
J. Mol. Cell. Cardiol. 35:841-849(2003).
[79]
LACK OF ASSOCIATION OF VARIANT MET-1692 WITH HYPERTROPHIC
CARDIOMYOPATHY.
Richard P.;
Unpublished observations (OCT-2004).
[80]
VARIANTS MPD1 PRO-1500; LYS-1617 DEL; PRO-1663; PRO-1706 AND LYS-1729
DEL.
PubMed=15322983; DOI=10.1086/424760;
Meredith C., Herrmann R., Parry C., Liyanage K., Dye D.E.,
Durling H.J., Duff R.M., Beckman K., de Visser M.,
van der Graaff M.M., Hedera P., Fink J.K., Petty E.M., Lamont P.,
Fabian V., Bridges L., Voit T., Mastaglia F.L., Laing N.G.;
"Mutations in the slow skeletal muscle fiber myosin heavy chain gene
(MYH7) cause Laing early-onset distal myopathy (MPD1).";
Am. J. Hum. Genet. 75:703-708(2004).
[81]
VARIANTS CMH1 HIS-115; GLN-143; MET-263; CYS-312; THR-349; VAL-385;
GLN-403; MET-404; VAL-407; VAL-428; MET-440; CYS-453; THR-511;
ARG-515; CYS-663; HIS-663; CYS-694; ARG-716; GLN-719; ARG-741;
VAL-778; THR-797; LYS-847 DEL; CYS-858; HIS-869; GLY-894; VAL-908;
LYS-921; LYS-924; LYS-931; HIS-953; SER-1057; LYS-1356; MET-1377;
TRP-1420; ASN-1459; SER-1513; LYS-1768; MET-1854 AND MET-1929, AND
VARIANTS CYS-1491 AND ASN-1919.
PubMed=15358028; DOI=10.1016/j.jacc.2004.04.039;
Van Driest S.L., Jaeger M.A., Ommen S.R., Will M.L., Gersh B.J.,
Tajik A.J., Ackerman M.J.;
"Comprehensive analysis of the beta-myosin heavy chain gene in 389
unrelated patients with hypertrophic cardiomyopathy.";
J. Am. Coll. Cardiol. 44:602-610(2004).
[82]
VARIANT MSMA LEU-1901.
PubMed=15136674; DOI=10.1212/01.WNL.0000123255.92062.37;
Bohlega S., Abu-Amero S.N., Wakil S.M., Carroll P., Al-Amr R.,
Lach B., Al-Sayed Y., Cupler E.J., Meyer B.F.;
"Mutation of the slow myosin heavy chain rod domain underlies hyaline
body myopathy.";
Neurology 62:1518-1521(2004).
[83]
VARIANTS CMH1 VAL-26; GLN-143; ARG-425; THR-450; PHE-511; GLN-615;
CYS-663; HIS-663; PRO-734; ARG-741; THR-822; GLU-823; HIS-858; LYS-924
AND LYS-930.
PubMed=15563892; DOI=10.1016/j.cccn.2004.09.016;
Song L., Zou Y., Wang J., Wang Z., Zhen Y., Lou K., Zhang Q., Wang X.,
Wang H., Li J., Hui R.;
"Mutations profile in Chinese patients with hypertrophic
cardiomyopathy.";
Clin. Chim. Acta 351:209-216(2005).
[84]
VARIANTS CMD1S THR-201; ASN-412; VAL-550; ASN-1019; SER-1193; LYS-1426
AND CYS-1634, AND VARIANT CYS-1491.
PubMed=15769782; DOI=10.1093/eurheartj/ehi193;
Villard E., Duboscq-Bidot L., Charron P., Benaiche A., Conraads V.,
Sylvius N., Komajda M.;
"Mutation screening in dilated cardiomyopathy: prominent role of the
beta myosin heavy chain gene.";
Eur. Heart J. 26:794-803(2005).
[85]
VARIANTS CMH1 LYS-1327; TRP-1712 AND LYS-1753, AND VARIANTS CYS-1475
AND CYS-1491.
PubMed=15483641; DOI=10.1038/sj.ejhg.5201310;
Hougs L., Havndrup O., Bundgaard H., Koeber L., Vuust J., Larsen L.A.,
Christiansen M., Andersen P.S.;
"One third of Danish hypertrophic cardiomyopathy patients with MYH7
mutations have mutations in MYH7 rod region.";
Eur. J. Hum. Genet. 13:161-165(2005).
[86]
VARIANTS CMH1 VAL-227; GLY-328; GLU-351; GLN-403; TRP-403; ILE-411;
THR-435; CYS-453; HIS-453; MET-606; CYS-663; GLN-719; TRP-719;
HIS-787; GLY-894; VAL-908 AND LYS-927, AND VARIANT CYS-1519.
PubMed=15858117; DOI=10.1136/jcp.2004.021642;
Yu B., Sawyer N.A., Caramins M., Yuan Z.G., Saunderson R.B.,
Pamphlett R., Richmond D.R., Jeremy R.W., Trent R.J.;
"Denaturing high performance liquid chromatography: high throughput
mutation screening in familial hypertrophic cardiomyopathy and SNP
genotyping in motor neurone disease.";
J. Clin. Pathol. 58:479-485(2005).
[87]
VARIANTS CMH1 ASN-146; LEU-186; MET-606; HIS-663; ALA-698; GLN-719;
CYS-723; THR-736; GLU-742 AND ASP-1057.
PubMed=16199542; DOI=10.1136/jmg.2005.033886;
Ingles J., Doolan A., Chiu C., Seidman J., Seidman C., Semsarian C.;
"Compound and double mutations in patients with hypertrophic
cardiomyopathy: implications for genetic testing and counselling.";
J. Med. Genet. 42:E59-E59(2005).
[88]
VARIANTS CMH1 LEU-211; TRP-403; CYS-453; CYS-501; ARG-576; THR-736;
TRP-741; GLY-901; ASN-928; LYS-1356 AND THR-1454.
PubMed=15856146; DOI=10.1007/s00109-005-0635-7;
Perrot A., Schmidt-Traub H., Hoffmann B., Prager M., Bit-Avragim N.,
Rudenko R.I., Usupbaeva D.A., Kabaeva Z., Imanov B., Mirrakhimov M.M.,
Dietz R., Wycisk A., Tendera M., Gessner R., Osterziel K.J.;
"Prevalence of cardiac beta-myosin heavy chain gene mutations in
patients with hypertrophic cardiomyopathy.";
J. Mol. Med. 83:468-477(2005).
[89]
VARIANT CMH1 HIS-870.
PubMed=16650083; DOI=10.1111/j.1399-0004.2006.00599.x;
Tanjore R.R., Sikindlapuram A.D., Calambur N., Thakkar B.,
Kerkar P.G., Nallari P.;
"Genotype-phenotype correlation of R870H mutation in hypertrophic
cardiomyopathy.";
Clin. Genet. 69:434-436(2006).
[90]
VARIANTS CMH1 VAL-515 AND CYS-858.
PubMed=16938236; DOI=10.1157/13091891;
Mora R., Merino J.L., Peinado R., Olias F., Garcia-Guereta L.,
del Cerro M.J., Tarin M.N., Molano J.;
"Hypertrophic cardiomyopathy: infrequent mutation of the cardiac beta-
myosin heavy-chain gene.";
Rev. Esp. Cardiol. 59:846-849(2006).
[91]
VARIANT CMH1 LYS-1883.
PubMed=17372140; DOI=10.1212/01.wnl.0000257131.13438.2c;
Tajsharghi H., Oldfors A., Macleod D.P., Swash M.;
"Homozygous mutation in MYH7 in myosin storage myopathy and
cardiomyopathy.";
Neurology 68:962-962(2007).
[92]
VARIANT MPD1 MET-441.
PubMed=17548557; DOI=10.1212/01.wnl.0000264430.55233.72;
Darin N., Tajsharghi H., Oestman-Smith I., Gilljam T., Oldfors A.;
"New skeletal myopathy and cardiomyopathy associated with a missense
mutation in MYH7.";
Neurology 68:2041-2042(2007).
[93]
VARIANT MSMA TRP-1845, AND VARIANT SPMM TRP-1845.
PubMed=17336526; DOI=10.1016/j.nmd.2007.01.010;
Pegoraro E., Gavassini B.F., Borsato C., Melacini P., Vianello A.,
Stramare R., Cenacchi G., Angelini C.;
"MYH7 gene mutation in myosin storage myopathy and scapulo-peroneal
myopathy.";
Neuromuscul. Disord. 17:321-329(2007).
[94]
VARIANTS CMH1 ASN-146; MET-606; HIS-663; GLN-719; MET-763; CYS-787;
VAL-908; LYS-924 AND MET-1414.
PubMed=18403758; DOI=10.1056/NEJMoa075463;
Morita H., Rehm H.L., Menesses A., McDonough B., Roberts A.E.,
Kucherlapati R., Towbin J.A., Seidman J.G., Seidman C.E.;
"Shared genetic causes of cardiac hypertrophy in children and
adults.";
N. Engl. J. Med. 358:1899-1908(2008).
[95]
VARIANTS CMD1S 1101-GLY--LEU-1104 DEL; ALA-1044; GLU-1263 AND
VAL-1297.
PubMed=21846512; DOI=10.1016/j.ejmg.2011.07.005;
Millat G., Bouvagnet P., Chevalier P., Sebbag L., Dulac A.,
Dauphin C., Jouk P.S., Delrue M.A., Thambo J.B., Le Metayer P.,
Seronde M.F., Faivre L., Eicher J.C., Rousson R.;
"Clinical and mutational spectrum in a cohort of 105 unrelated
patients with dilated cardiomyopathy.";
Eur. J. Med. Genet. 54:E570-E575(2011).
[96]
VARIANT CMH1 LYS-1752.
PubMed=25182012; DOI=10.1007/s00246-014-1002-7;
Lee D.D., Veith R.L., Dimmock D.P., Samyn M.M.;
"Hypertrophic cardiomyopathy: a new mutation illustrates the need for
family-centered care.";
Pediatr. Cardiol. 35:1474-1477(2014).
-!- FUNCTION: Myosins are actin-based motor molecules with ATPase
activity essential for muscle contraction. Forms regular bipolar
thick filaments that, together with actin thin filaments,
constitute the fundamental contractile unit of skeletal and
cardiac muscle. {ECO:0000305|PubMed:26150528,
ECO:0000305|PubMed:26246073}.
-!- SUBUNIT: Muscle myosin is a hexameric protein that consists of 2
heavy chain subunits (MHC), 2 alkali light chain subunits (MLC)
and 2 regulatory light chain subunits (MLC-2). Interacts with
ECM29 (PubMed:20682791). Interacts (via C-terminus) with LRRC39
(PubMed:20847312). {ECO:0000269|PubMed:20682791,
ECO:0000269|PubMed:20847312}.
-!- INTERACTION:
Q9BQD3:KXD1; NbExp=3; IntAct=EBI-519141, EBI-739657;
-!- SUBCELLULAR LOCATION: Cytoplasm, myofibril
{ECO:0000250|UniProtKB:P02564}. Cytoplasm, myofibril, sarcomere
{ECO:0000250|UniProtKB:P02564}. Note=Thick filaments of the
myofibrils. {ECO:0000250|UniProtKB:P02564}.
-!- TISSUE SPECIFICITY: Both wild type and variant Gln-403 are
detected in skeletal muscle (at protein level).
{ECO:0000269|PubMed:8514894}.
-!- DOMAIN: The rodlike tail sequence is highly repetitive, showing
cycles of a 28-residue repeat pattern composed of 4 heptapeptides,
characteristic for alpha-helical coiled coils (PubMed:26150528,
PubMed:26573747). Four skip residues (Skip1: Thr-1188, Skip2: Glu-
1385, Skip3: Glu-1582 and Skip4: Gly-1807) introduce
discontinuities in the coiled-coil heptad repeats. The first three
skip residues are structurally comparable and induce a unique
local relaxation of the coiled-coil superhelical pitch and the
fourth skip residue lies within a highly flexible molecular hinge
that is necessary for myosin incorporation in the bare zone of
sarcomeres (PubMed:26150528). {ECO:0000269|PubMed:26150528,
ECO:0000269|PubMed:26573747}.
-!- DOMAIN: Limited proteolysis of myosin heavy chain produces 1 light
meromyosin (LMM) and 1 heavy meromyosin (HMM). HMM can be further
cleaved into 2 globular subfragments (S1) and 1 rod-shaped
subfragment (S2). {ECO:0000305}.
-!- DISEASE: Cardiomyopathy, familial hypertrophic 1 (CMH1)
[MIM:192600]: 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:10065021, ECO:0000269|PubMed:10329202,
ECO:0000269|PubMed:10521296, ECO:0000269|PubMed:10563488,
ECO:0000269|PubMed:10679957, ECO:0000269|PubMed:10862102,
ECO:0000269|PubMed:11113006, ECO:0000269|PubMed:11133230,
ECO:0000269|PubMed:11214007, ECO:0000269|PubMed:11424919,
ECO:0000269|PubMed:11733062, ECO:0000269|PubMed:11861413,
ECO:0000269|PubMed:11968089, ECO:0000269|PubMed:12081993,
ECO:0000269|PubMed:12566107, ECO:0000269|PubMed:12590187,
ECO:0000269|PubMed:12707239, ECO:0000269|PubMed:12818575,
ECO:0000269|PubMed:12820698, ECO:0000269|PubMed:12951062,
ECO:0000269|PubMed:12974739, ECO:0000269|PubMed:12975413,
ECO:0000269|PubMed:1417858, ECO:0000269|PubMed:15358028,
ECO:0000269|PubMed:15483641, ECO:0000269|PubMed:1552912,
ECO:0000269|PubMed:15563892, ECO:0000269|PubMed:15856146,
ECO:0000269|PubMed:15858117, ECO:0000269|PubMed:16199542,
ECO:0000269|PubMed:16267253, ECO:0000269|PubMed:1638703,
ECO:0000269|PubMed:16650083, ECO:0000269|PubMed:16938236,
ECO:0000269|PubMed:17095604, ECO:0000269|PubMed:17372140,
ECO:0000269|PubMed:18175163, ECO:0000269|PubMed:18403758,
ECO:0000269|PubMed:1975517, ECO:0000269|PubMed:25182012,
ECO:0000269|PubMed:7581410, ECO:0000269|PubMed:7731997,
ECO:0000269|PubMed:7848441, ECO:0000269|PubMed:7874131,
ECO:0000269|PubMed:8250038, ECO:0000269|PubMed:8254035,
ECO:0000269|PubMed:8268932, ECO:0000269|PubMed:8282798,
ECO:0000269|PubMed:8343162, ECO:0000269|PubMed:8435239,
ECO:0000269|PubMed:8483915, ECO:0000269|PubMed:8655135,
ECO:0000269|PubMed:8899546, ECO:0000269|PubMed:9544842,
ECO:0000269|PubMed:9822100, ECO:0000269|PubMed:9829907}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Myopathy, myosin storage, autosomal dominant (MSMA)
[MIM:608358]: A rare congenital myopathy characterized by
subsarcolemmal hyalinized bodies in type 1 muscle fibers.
{ECO:0000269|PubMed:14520662, ECO:0000269|PubMed:15136674,
ECO:0000269|PubMed:16684601, ECO:0000269|PubMed:17336526}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Scapuloperoneal myopathy MYH7-related (SPMM)
[MIM:181430]: Progressive muscular atrophia beginning in the lower
legs and affecting the shoulder region earlier and more severely
than distal arm. {ECO:0000269|PubMed:17336526}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- DISEASE: Cardiomyopathy, dilated 1S (CMD1S) [MIM:613426]: 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:11106718, ECO:0000269|PubMed:12379228,
ECO:0000269|PubMed:15769782, ECO:0000269|PubMed:18506004,
ECO:0000269|PubMed:21127202, ECO:0000269|PubMed:21846512}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Myopathy, distal, 1 (MPD1) [MIM:160500]: A muscular
disorder characterized by early-onset selective weakness of the
great toe and ankle dorsiflexors, followed by weakness of the
finger extensors. Mild proximal weakness occasionally develops
years later after the onset of the disease.
{ECO:0000269|PubMed:15322983, ECO:0000269|PubMed:17548557}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Myopathy, myosin storage, autosomal recessive (MSMB)
[MIM:255160]: An autosomal recessive form of myosin storage
myopathy, a muscle disease characterized by subsarcolemmal
accumulation of hyalinized bodies in type 1 muscle fibers. MSMB
clinical features include muscle weakness, type II respiratory
failure and cardiac failure, due to hypertrophic cardiomyopathy.
{ECO:0000269|PubMed:25666907}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: The cardiac alpha isoform is a 'fast' ATPase
myosin, while the beta isoform is a 'slow' ATPase.
-!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
superfamily. Myosin family. {ECO:0000305}.
-!- CAUTION: Represents a conventional myosin. This protein should not
be confused with the unconventional myosin-7 (MYO7).
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M57965; AAA51837.1; -; Genomic_DNA.
EMBL; M58018; AAA62830.1; -; mRNA.
EMBL; X52889; CAA37068.1; -; Genomic_DNA.
EMBL; AJ238393; CAC20413.1; -; Genomic_DNA.
EMBL; EU747717; ACH92815.1; -; mRNA.
EMBL; EF179180; ABN05283.1; -; Genomic_DNA.
EMBL; CH471078; EAW66152.1; -; Genomic_DNA.
EMBL; BC112171; AAI12172.1; -; mRNA.
EMBL; BC112173; AAI12174.1; -; mRNA.
EMBL; M25135; AAA60384.1; -; Genomic_DNA.
EMBL; M25133; AAA60384.1; JOINED; Genomic_DNA.
EMBL; M25134; AAA60384.1; JOINED; Genomic_DNA.
EMBL; M27636; AAA79019.1; -; Genomic_DNA.
EMBL; X04627; CAA28300.1; -; Genomic_DNA.
EMBL; X04628; CAA28300.1; JOINED; Genomic_DNA.
EMBL; X04629; CAA28300.1; JOINED; Genomic_DNA.
EMBL; X04630; CAA28300.1; JOINED; Genomic_DNA.
EMBL; X04631; CAA28300.1; JOINED; Genomic_DNA.
EMBL; X04632; CAA28300.1; JOINED; Genomic_DNA.
EMBL; X04633; CAA28300.1; JOINED; Genomic_DNA.
EMBL; X51591; CAA35940.1; -; mRNA.
EMBL; X03741; CAA27381.1; ALT_SEQ; mRNA.
EMBL; X06976; CAA30039.1; -; mRNA.
EMBL; M17712; AAA36343.1; -; mRNA.
EMBL; M21665; AAA36345.1; -; mRNA.
EMBL; X05631; CAA29119.1; -; mRNA.
CCDS; CCDS9601.1; -.
PIR; A37102; A37102.
RefSeq; NP_000248.2; NM_000257.3.
RefSeq; XP_016876829.1; XM_017021340.1.
UniGene; Hs.719946; -.
PDB; 1IK2; Model; -; A=1-841.
PDB; 2FXM; X-ray; 2.70 A; A/B=838-963.
PDB; 2FXO; X-ray; 2.50 A; A/B/C/D=838-963.
PDB; 3DTP; EM; 20.00 A; A=842-961, B=842-963.
PDB; 4DB1; X-ray; 2.60 A; A/B=2-783.
PDB; 4P7H; X-ray; 3.20 A; A/B=1-787.
PDB; 4PA0; X-ray; 2.25 A; A/B=1-787.
PDB; 4XA1; X-ray; 3.20 A; A/B/C/D=1173-1238.
PDB; 4XA3; X-ray; 2.55 A; A/B=1361-1425.
PDB; 4XA4; X-ray; 2.33 A; A/B=1551-1609.
PDB; 4XA6; X-ray; 3.42 A; A/B/C/D=1777-1855.
PDB; 5CHX; X-ray; 2.30 A; A/B=1590-1657.
PDB; 5CJ0; X-ray; 2.30 A; A/B=1631-1692.
PDB; 5CJ1; X-ray; 2.10 A; A/B/C/D/E/F/G/H=1526-1571.
PDB; 5CJ4; X-ray; 3.10 A; A/B/C/D=1562-1622.
PDB; 5TBY; EM; 20.00 A; A/B=1-1935.
PDB; 5WJ7; X-ray; 2.50 A; A/B=1733-1797.
PDB; 5WJB; X-ray; 2.90 A; A/B/C/D=1733-1797.
PDB; 5WLQ; X-ray; 3.10 A; A=1677-1755.
PDB; 5WLZ; X-ray; 3.50 A; A/B/C/D=1677-1758.
PDB; 5WME; X-ray; 2.30 A; A/B/C/D=1730-1786.
PDBsum; 1IK2; -.
PDBsum; 2FXM; -.
PDBsum; 2FXO; -.
PDBsum; 3DTP; -.
PDBsum; 4DB1; -.
PDBsum; 4P7H; -.
PDBsum; 4PA0; -.
PDBsum; 4XA1; -.
PDBsum; 4XA3; -.
PDBsum; 4XA4; -.
PDBsum; 4XA6; -.
PDBsum; 5CHX; -.
PDBsum; 5CJ0; -.
PDBsum; 5CJ1; -.
PDBsum; 5CJ4; -.
PDBsum; 5TBY; -.
PDBsum; 5WJ7; -.
PDBsum; 5WJB; -.
PDBsum; 5WLQ; -.
PDBsum; 5WLZ; -.
PDBsum; 5WME; -.
ProteinModelPortal; P12883; -.
SMR; P12883; -.
BioGrid; 110710; 41.
IntAct; P12883; 24.
MINT; MINT-1512407; -.
STRING; 9606.ENSP00000347507; -.
ChEMBL; CHEMBL3831286; -.
iPTMnet; P12883; -.
PhosphoSitePlus; P12883; -.
BioMuta; MYH7; -.
DMDM; 83304912; -.
UCD-2DPAGE; P12883; -.
EPD; P12883; -.
MaxQB; P12883; -.
PaxDb; P12883; -.
PeptideAtlas; P12883; -.
PRIDE; P12883; -.
Ensembl; ENST00000355349; ENSP00000347507; ENSG00000092054.
GeneID; 4625; -.
KEGG; hsa:4625; -.
UCSC; uc001wjx.4; human.
CTD; 4625; -.
DisGeNET; 4625; -.
EuPathDB; HostDB:ENSG00000092054.12; -.
GeneCards; MYH7; -.
GeneReviews; MYH7; -.
H-InvDB; HIX0172409; -.
HGNC; HGNC:7577; MYH7.
HPA; CAB015384; -.
HPA; HPA001239; -.
HPA; HPA001349; -.
MalaCards; MYH7; -.
MIM; 160500; phenotype.
MIM; 160760; gene.
MIM; 181430; phenotype.
MIM; 192600; phenotype.
MIM; 255160; phenotype.
MIM; 608358; phenotype.
MIM; 613426; phenotype.
neXtProt; NX_P12883; -.
OpenTargets; ENSG00000092054; -.
Orphanet; 324604; Classic multiminicore myopathy.
Orphanet; 1880; Ebstein malformation.
Orphanet; 154; Familial isolated dilated cardiomyopathy.
Orphanet; 155; Familial isolated hypertrophic cardiomyopathy.
Orphanet; 53698; Hyaline body myopathy.
Orphanet; 59135; Laing early-onset distal myopathy.
Orphanet; 54260; Left ventricular noncompaction.
PharmGKB; PA31374; -.
eggNOG; KOG0161; Eukaryota.
eggNOG; COG5022; LUCA.
GeneTree; ENSGT00760000118919; -.
HOVERGEN; HBG004704; -.
InParanoid; P12883; -.
KO; K17751; -.
OMA; VYPDFKM; -.
OrthoDB; EOG091G07UM; -.
PhylomeDB; P12883; -.
TreeFam; TF314375; -.
Reactome; R-HSA-1445148; Translocation of GLUT4 to the plasma membrane.
SIGNOR; P12883; -.
ChiTaRS; MYH7; human.
EvolutionaryTrace; P12883; -.
GeneWiki; MYH7; -.
GenomeRNAi; 4625; -.
PRO; PR:P12883; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000092054; -.
Genevisible; P12883; HS.
GO; GO:0005859; C:muscle myosin complex; TAS:UniProtKB.
GO; GO:0030016; C:myofibril; ISS:UniProtKB.
GO; GO:0016459; C:myosin complex; TAS:HGNC.
GO; GO:0032982; C:myosin filament; IDA:BHF-UCL.
GO; GO:0030017; C:sarcomere; ISS:UniProtKB.
GO; GO:0001725; C:stress fiber; IEA:Ensembl.
GO; GO:0030018; C:Z disc; IEA:Ensembl.
GO; GO:0051015; F:actin filament binding; IEA:InterPro.
GO; GO:0030898; F:actin-dependent ATPase activity; IMP:HGNC.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; IDA:HGNC.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0000146; F:microfilament motor activity; IDA:BHF-UCL.
GO; GO:0007512; P:adult heart development; IMP:HGNC.
GO; GO:0046034; P:ATP metabolic process; IDA:BHF-UCL.
GO; GO:0060048; P:cardiac muscle contraction; IMP:BHF-UCL.
GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; IEA:Ensembl.
GO; GO:0006936; P:muscle contraction; IDA:HGNC.
GO; GO:0030049; P:muscle filament sliding; IMP:HGNC.
GO; GO:0002027; P:regulation of heart rate; IDA:HGNC.
GO; GO:0031449; P:regulation of slow-twitch skeletal muscle fiber contraction; IMP:BHF-UCL.
GO; GO:0002026; P:regulation of the force of heart contraction; IDA:BHF-UCL.
GO; GO:0014728; P:regulation of the force of skeletal muscle contraction; IMP:BHF-UCL.
GO; GO:0003009; P:skeletal muscle contraction; IMP:BHF-UCL.
GO; GO:0006941; P:striated muscle contraction; IDA:BHF-UCL.
GO; GO:0014883; P:transition between fast and slow fiber; IEA:Ensembl.
GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IMP:HGNC.
Gene3D; 2.30.30.360; -; 1.
InterPro; IPR000048; IQ_motif_EF-hand-BS.
InterPro; IPR001609; Myosin_head_motor_dom.
InterPro; IPR004009; Myosin_N.
InterPro; IPR008989; Myosin_S1_N.
InterPro; IPR002928; Myosin_tail.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00063; Myosin_head; 1.
Pfam; PF02736; Myosin_N; 1.
Pfam; PF01576; Myosin_tail_1; 1.
PRINTS; PR00193; MYOSINHEAVY.
SMART; SM00015; IQ; 1.
SMART; SM00242; MYSc; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50096; IQ; 1.
PROSITE; PS51456; MYOSIN_MOTOR; 1.
1: Evidence at protein level;
3D-structure; Actin-binding; ATP-binding; Calmodulin-binding;
Cardiomyopathy; Coiled coil; Complete proteome; Cytoplasm;
Disease mutation; Methylation; Motor protein; Muscle protein; Myosin;
Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
Thick filament.
CHAIN 1 1935 Myosin-7.
/FTId=PRO_0000123407.
DOMAIN 85 778 Myosin motor.
DOMAIN 781 810 IQ. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
NP_BIND 178 185 ATP.
REGION 655 677 Actin-binding.
REGION 757 771 Actin-binding.
COILED 839 1935 {ECO:0000255,
ECO:0000269|PubMed:26150528,
ECO:0000269|PubMed:26573747}.
MOD_RES 129 129 N6,N6,N6-trimethyllysine. {ECO:0000255}.
MOD_RES 378 378 Phosphothreonine.
{ECO:0000250|UniProtKB:P02563}.
MOD_RES 1137 1137 Phosphoserine.
{ECO:0000250|UniProtKB:P02563}.
MOD_RES 1269 1269 Phosphoserine.
{ECO:0000250|UniProtKB:Q02566}.
MOD_RES 1282 1282 Phosphothreonine.
{ECO:0000250|UniProtKB:P02563}.
MOD_RES 1308 1308 Phosphotyrosine.
{ECO:0000250|UniProtKB:P02563}.
MOD_RES 1309 1309 Phosphothreonine.
{ECO:0000250|UniProtKB:P02563}.
MOD_RES 1510 1510 Phosphoserine.
{ECO:0000250|UniProtKB:P02564}.
MOD_RES 1513 1513 Phosphothreonine.
{ECO:0000250|UniProtKB:P02563}.
VARIANT 3 3 D -> A (in dbSNP:rs3729993).
/FTId=VAR_029430.
VARIANT 26 26 A -> V (in CMH1; dbSNP:rs186964570).
{ECO:0000269|PubMed:15563892}.
/FTId=VAR_004566.
VARIANT 39 39 V -> M (in CMH1; dbSNP:rs376160714).
{ECO:0000269|PubMed:12707239}.
/FTId=VAR_019845.
VARIANT 59 59 V -> I (in CMH1; dbSNP:rs771132107).
/FTId=VAR_004567.
VARIANT 107 107 D -> E (in dbSNP:rs2754166).
{ECO:0000269|PubMed:2362820,
ECO:0000269|PubMed:2726733}.
/FTId=VAR_017745.
VARIANT 115 115 Y -> H (in CMH1; dbSNP:rs397516183).
{ECO:0000269|PubMed:15358028}.
/FTId=VAR_042762.
VARIANT 124 124 T -> I (in CMH1).
{ECO:0000269|PubMed:7731997}.
/FTId=VAR_020797.
VARIANT 143 143 R -> G (in CMH1; dbSNP:rs727503278).
{ECO:0000269|PubMed:12820698}.
/FTId=VAR_042763.
VARIANT 143 143 R -> Q (in CMH1; dbSNP:rs397516209).
{ECO:0000269|PubMed:15358028,
ECO:0000269|PubMed:15563892}.
/FTId=VAR_004568.
VARIANT 143 143 R -> W (in CMH1; dbSNP:rs727503278).
{ECO:0000269|PubMed:12974739}.
/FTId=VAR_029431.
VARIANT 146 146 K -> N (in CMH1; dbSNP:rs397516212).
{ECO:0000269|PubMed:16199542,
ECO:0000269|PubMed:18403758}.
/FTId=VAR_042764.
VARIANT 148 148 S -> I (in CMH1; dbSNP:rs772691929).
{ECO:0000269|PubMed:12820698}.
/FTId=VAR_042765.
VARIANT 162 162 Y -> C (in CMH1).
{ECO:0000269|PubMed:7731997}.
/FTId=VAR_020798.
VARIANT 186 186 V -> L (in CMH1; dbSNP:rs786205906).
{ECO:0000269|PubMed:16199542}.
/FTId=VAR_042766.
VARIANT 187 187 N -> K (in CMH1).
{ECO:0000269|PubMed:7731997}.
/FTId=VAR_020799.
VARIANT 188 188 T -> N (in CMH1; dbSNP:rs730880844).
{ECO:0000269|PubMed:12707239}.
/FTId=VAR_019846.
VARIANT 190 190 R -> T (in CMH1).
{ECO:0000269|PubMed:10329202,
ECO:0000269|PubMed:12566107}.
/FTId=VAR_020800.
VARIANT 196 196 A -> T (in CMH1).
{ECO:0000269|PubMed:12975413}.
/FTId=VAR_042767.
VARIANT 201 201 I -> T (in CMD1S; dbSNP:rs397516258).
{ECO:0000269|PubMed:15769782}.
/FTId=VAR_042768.
VARIANT 204 204 R -> H (in CMH1; dbSNP:rs397516260).
{ECO:0000269|PubMed:12707239}.
/FTId=VAR_019847.
VARIANT 207 207 K -> Q (in CMH1; dbSNP:rs727504273).
{ECO:0000269|PubMed:12820698}.
/FTId=VAR_042769.
VARIANT 211 211 P -> L (in CMH1; dbSNP:rs727503277).
{ECO:0000269|PubMed:12820698,
ECO:0000269|PubMed:12975413,
ECO:0000269|PubMed:15856146}.
/FTId=VAR_042770.
VARIANT 222 222 Q -> K (in CMH1).
{ECO:0000269|PubMed:7731997}.
/FTId=VAR_020801.
VARIANT 223 223 A -> T (in CMD1S; dbSNP:rs121913645).
{ECO:0000269|PubMed:12379228}.
/FTId=VAR_017746.
VARIANT 227 227 L -> V (in CMH1).
{ECO:0000269|PubMed:15858117}.
/FTId=VAR_042771.
VARIANT 232 232 N -> S (in CMH1).
{ECO:0000269|PubMed:12707239}.
/FTId=VAR_019848.
VARIANT 239 239 Missing (in CMD1S).
{ECO:0000269|PubMed:18506004}.
/FTId=VAR_073875.
VARIANT 243 243 R -> H (in CMH1 and CMD1S;
dbSNP:rs267606910).
{ECO:0000269|PubMed:16267253,
ECO:0000269|PubMed:18506004}.
/FTId=VAR_073876.
VARIANT 244 244 F -> L (in CMH1; dbSNP:rs730880849).
{ECO:0000269|PubMed:7731997}.
/FTId=VAR_020802.
VARIANT 249 249 R -> Q (in CMH1; dbSNP:rs3218713).
{ECO:0000269|PubMed:10065021,
ECO:0000269|PubMed:11133230,
ECO:0000269|PubMed:11968089,
ECO:0000269|PubMed:12707239,
ECO:0000269|PubMed:12975413,
ECO:0000269|PubMed:1552912}.
/FTId=VAR_004569.
VARIANT 256 256 G -> E (in CMH1; dbSNP:rs121913633).
{ECO:0000269|PubMed:8483915}.
/FTId=VAR_004570.
VARIANT 263 263 I -> M (in CMH1; dbSNP:rs730880855).
{ECO:0000269|PubMed:15358028}.
/FTId=VAR_042772.
VARIANT 263 263 I -> T (in CMH1; dbSNP:rs397516269).
{ECO:0000269|PubMed:12707239,
ECO:0000269|PubMed:9829907}.
/FTId=VAR_004571.
VARIANT 283 283 Y -> D (in CMD1S; dbSNP:rs397515482).
{ECO:0000269|PubMed:21127202}.
/FTId=VAR_073877.
VARIANT 312 312 F -> C (in CMH1).
{ECO:0000269|PubMed:15358028}.
/FTId=VAR_042773.
VARIANT 320 320 V -> M (in CMH1; dbSNP:rs376897125).
{ECO:0000269|PubMed:12566107}.
/FTId=VAR_020803.
VARIANT 328 328 E -> G (in CMH1).
{ECO:0000269|PubMed:15858117}.
/FTId=VAR_042774.
VARIANT 349 349 M -> T (in CMH1; dbSNP:rs121913640).
{ECO:0000269|PubMed:11968089,
ECO:0000269|PubMed:15358028,
ECO:0000269|PubMed:9544842}.
/FTId=VAR_004572.
VARIANT 350 350 Y -> N (in CMD1S).
{ECO:0000269|PubMed:21127202}.
/FTId=VAR_073878.
VARIANT 351 351 K -> E (in CMH1; dbSNP:rs730880864).
{ECO:0000269|PubMed:12820698,
ECO:0000269|PubMed:15858117}.
/FTId=VAR_042775.
VARIANT 355 355 A -> T (in CMH1; dbSNP:rs397516088).
{ECO:0000269|PubMed:12707239}.
/FTId=VAR_019849.
VARIANT 383 383 K -> N (in CMH1).
{ECO:0000269|PubMed:8899546}.
/FTId=VAR_042776.
VARIANT 385 385 A -> V (in CMH1).
{ECO:0000269|PubMed:15358028}.
/FTId=VAR_042777.
VARIANT 390 390 L -> P (in CMD1S).
{ECO:0000269|PubMed:21127202}.
/FTId=VAR_073879.
VARIANT 390 390 L -> V (in CMH1).
{ECO:0000269|PubMed:11214007,
ECO:0000269|PubMed:12566107}.
/FTId=VAR_020804.
VARIANT 403 403 R -> L (in CMH1; dbSNP:rs121913624).
{ECO:0000269|PubMed:12707239,
ECO:0000269|PubMed:8254035}.
/FTId=VAR_004573.
VARIANT 403 403 R -> Q (in CMH1; dbSNP:rs121913624).
{ECO:0000269|PubMed:11968089,
ECO:0000269|PubMed:12707239,
ECO:0000269|PubMed:12820698,
ECO:0000269|PubMed:12975413,
ECO:0000269|PubMed:15358028,
ECO:0000269|PubMed:1552912,
ECO:0000269|PubMed:15858117,
ECO:0000269|PubMed:1638703,
ECO:0000269|PubMed:1975517,
ECO:0000269|PubMed:8250038,
ECO:0000269|PubMed:8514894}.
/FTId=VAR_004574.
VARIANT 403 403 R -> W (in CMH1; dbSNP:rs3218714).
{ECO:0000269|PubMed:10521296,
ECO:0000269|PubMed:12707239,
ECO:0000269|PubMed:12974739,
ECO:0000269|PubMed:15856146,
ECO:0000269|PubMed:15858117,
ECO:0000269|PubMed:8254035,
ECO:0000269|PubMed:8268932}.
/FTId=VAR_004575.
VARIANT 404 404 V -> L (in CMH1).
{ECO:0000269|PubMed:12975413}.
/FTId=VAR_042778.
VARIANT 404 404 V -> M (in CMH1; dbSNP:rs730880867).
{ECO:0000269|PubMed:15358028}.
/FTId=VAR_042779.
VARIANT 406 406 V -> M (in CMH1).
{ECO:0000269|PubMed:11133230}.
/FTId=VAR_020805.
VARIANT 407 407 G -> V (in CMH1; dbSNP:rs397516095).
{ECO:0000269|PubMed:15358028}.
/FTId=VAR_042780.
VARIANT 411 411 V -> I (in CMH1; dbSNP:rs730880868).
{ECO:0000269|PubMed:12974739,
ECO:0000269|PubMed:12975413,
ECO:0000269|PubMed:15858117}.
/FTId=VAR_029432.
VARIANT 412 412 T -> N (in CMD1S).
{ECO:0000269|PubMed:15769782}.
/FTId=VAR_042781.
VARIANT 425 425 G -> R (in CMH1; dbSNP:rs397516097).
{ECO:0000269|PubMed:15563892}.
/FTId=VAR_042782.
VARIANT 428 428 A -> V (in CMH1; dbSNP:rs727503266).
{ECO:0000269|PubMed:12707239,
ECO:0000269|PubMed:15358028}.
/FTId=VAR_019850.
VARIANT 430 430 A -> E (in CMH1).
{ECO:0000269|PubMed:12818575}.
/FTId=VAR_029433.
VARIANT 435 435 M -> T (in CMH1).
{ECO:0000269|PubMed:15858117}.
/FTId=VAR_042783.
VARIANT 440 440 V -> M (in CMH1; dbSNP:rs397516098).
{ECO:0000269|PubMed:15358028}.
/FTId=VAR_042784.
VARIANT 441 441 T -> M (in MPD1; dbSNP:rs121913653).
{ECO:0000269|PubMed:17548557}.
/FTId=VAR_042785.
VARIANT 443 443 I -> T (in CMH1).
{ECO:0000269|PubMed:12707239}.
/FTId=VAR_019851.
VARIANT 450 450 K -> E (in CMH1).
{ECO:0000269|PubMed:10065021}.
/FTId=VAR_042786.
VARIANT 450 450 K -> T (in CMH1).
{ECO:0000269|PubMed:15563892}.
/FTId=VAR_042787.
VARIANT 453 453 R -> C (in CMH1; dbSNP:rs121913625).
{ECO:0000269|PubMed:11133230,
ECO:0000269|PubMed:12707239,
ECO:0000269|PubMed:12951062,
ECO:0000269|PubMed:12975413,
ECO:0000269|PubMed:15358028,
ECO:0000269|PubMed:1552912,
ECO:0000269|PubMed:15856146,
ECO:0000269|PubMed:15858117,
ECO:0000269|PubMed:8250038,
ECO:0000269|PubMed:8655135}.
/FTId=VAR_004576.
VARIANT 453 453 R -> H (in CMH1; dbSNP:rs397516101).
{ECO:0000269|PubMed:15858117}.
/FTId=VAR_042788.
VARIANT 453 453 R -> S (in CMH1; dbSNP:rs121913625).
{ECO:0000269|PubMed:18175163}.
/FTId=VAR_073880.
VARIANT 466 466 E -> Q (in dbSNP:rs4981473).
/FTId=VAR_029434.
VARIANT 479 479 N -> S (in CMH1; dbSNP:rs727504236).
{ECO:0000269|PubMed:12707239,
ECO:0000269|PubMed:12820698}.
/FTId=VAR_019852.
VARIANT 483 483 E -> K (in CMH1; dbSNP:rs121913651).
{ECO:0000269|PubMed:12707239}.
/FTId=VAR_019853.
VARIANT 497 497 E -> D (in CMH1; dbSNP:rs267606911).
{ECO:0000269|PubMed:16267253}.
/FTId=VAR_073881.
VARIANT 499 499 E -> K (in CMH1; dbSNP:rs3218715).
{ECO:0000269|PubMed:10521296}.
/FTId=VAR_020806.
VARIANT 500 500 E -> A (in CMH1; dbSNP:rs727504286).
{ECO:0000269|PubMed:12820698}.
/FTId=VAR_042789.
VARIANT 501 501 Y -> C (in CMH1).
{ECO:0000269|PubMed:15856146}.
/FTId=VAR_042790.
VARIANT 511 511 I -> F (in CMH1).
{ECO:0000269|PubMed:15563892}.
/FTId=VAR_042791.
VARIANT 511 511 I -> T (in CMH1; dbSNP:rs397516110).
{ECO:0000269|PubMed:15358028}.
/FTId=VAR_042792.
VARIANT 513 513 F -> C (in CMH1; dbSNP:rs121913636).
{ECO:0000269|PubMed:8282798}.
/FTId=VAR_004577.
VARIANT 515 515 M -> R (in CMH1).
{ECO:0000269|PubMed:15358028}.
/FTId=VAR_042793.
VARIANT 515 515 M -> V (in CMH1; infrequent).
{ECO:0000269|PubMed:16938236}.
/FTId=VAR_039562.
VARIANT 517 517 L -> M (in CMH1; dbSNP:rs727504237).
{ECO:0000269|PubMed:12951062}.
/FTId=VAR_029435.
VARIANT 532 532 S -> P (in CMD1S; dbSNP:rs121913642).
{ECO:0000269|PubMed:11106718}.
/FTId=VAR_017747.
VARIANT 550 550 A -> V (in CMD1S).
{ECO:0000269|PubMed:15769782}.
/FTId=VAR_042794.
VARIANT 571 571 G -> R (in CMH1; dbSNP:rs730880879).
{ECO:0000269|PubMed:12820698}.
/FTId=VAR_042795.
VARIANT 576 576 H -> R (in CMH1; dbSNP:rs727504238).
{ECO:0000269|PubMed:15856146}.
/FTId=VAR_042796.
VARIANT 584 584 G -> R (in CMH1; dbSNP:rs121913626).
{ECO:0000269|PubMed:8250038}.
/FTId=VAR_004578.
VARIANT 584 584 G -> S (in CMH1; dbSNP:rs121913626).
{ECO:0000269|PubMed:12974739}.
/FTId=VAR_029436.
VARIANT 587 587 D -> V (in CMH1).
/FTId=VAR_004579.
VARIANT 595 595 Q -> R (in CMH1).
{ECO:0000269|PubMed:11968089}.
/FTId=VAR_020807.
VARIANT 601 601 L -> V (in CMH1).
{ECO:0000269|PubMed:12566107}.
/FTId=VAR_020808.
VARIANT 602 602 N -> S (in CMH1; dbSNP:rs730880880).
/FTId=VAR_004580.
VARIANT 606 606 V -> M (in CMH1; in cis with V-728 gives
a more severe phenotype;
dbSNP:rs121913627).
{ECO:0000269|PubMed:11133230,
ECO:0000269|PubMed:11968089,
ECO:0000269|PubMed:12566107,
ECO:0000269|PubMed:12707239,
ECO:0000269|PubMed:1552912,
ECO:0000269|PubMed:15858117,
ECO:0000269|PubMed:16199542,
ECO:0000269|PubMed:18403758,
ECO:0000269|PubMed:8250038}.
/FTId=VAR_004581.
VARIANT 615 615 K -> N (in CMH1).
{ECO:0000269|PubMed:1417858}.
/FTId=VAR_004582.
VARIANT 615 615 K -> Q (in CMH1).
{ECO:0000269|PubMed:15563892}.
/FTId=VAR_042797.
VARIANT 642 642 S -> L (in CMD1S; dbSNP:rs121913646).
{ECO:0000269|PubMed:12379228}.
/FTId=VAR_017748.
VARIANT 659 659 M -> I (in CMH1).
{ECO:0000269|PubMed:12707239}.
/FTId=VAR_019854.
VARIANT 663 663 R -> C (in CMH1; dbSNP:rs397516127).
{ECO:0000269|PubMed:15358028,
ECO:0000269|PubMed:15563892,
ECO:0000269|PubMed:15858117}.
/FTId=VAR_042798.
VARIANT 663 663 R -> H (in CMH1; dbSNP:rs371898076).
{ECO:0000269|PubMed:11133230,
ECO:0000269|PubMed:12081993,
ECO:0000269|PubMed:12707239,
ECO:0000269|PubMed:12820698,
ECO:0000269|PubMed:15358028,
ECO:0000269|PubMed:15563892,
ECO:0000269|PubMed:16199542,
ECO:0000269|PubMed:18403758,
ECO:0000269|PubMed:7731997}.
/FTId=VAR_019855.
VARIANT 663 663 R -> S (in CMH1).
{ECO:0000269|PubMed:12707239}.
/FTId=VAR_019856.
VARIANT 671 671 R -> C (in CMH1; dbSNP:rs727503263).
{ECO:0000269|PubMed:12707239,
ECO:0000269|PubMed:12820698}.
/FTId=VAR_019857.
VARIANT 694 694 R -> C (in CMH1; dbSNP:rs727504240).
{ECO:0000269|PubMed:10563488,
ECO:0000269|PubMed:12566107,
ECO:0000269|PubMed:15358028}.
/FTId=VAR_020809.
VARIANT 694 694 R -> H (in CMH1).
{ECO:0000269|PubMed:12974739}.
/FTId=VAR_029437.
VARIANT 696 696 N -> S (in CMH1; dbSNP:rs730880732).
{ECO:0000269|PubMed:9822100}.
/FTId=VAR_020810.
VARIANT 698 698 V -> A (in CMH1; dbSNP:rs397516130).
{ECO:0000269|PubMed:16199542}.
/FTId=VAR_042799.
VARIANT 712 712 R -> L (in CMH1).
{ECO:0000269|PubMed:10679957}.
/FTId=VAR_020811.
VARIANT 716 716 G -> R (in CMH1; dbSNP:rs121913638).
{ECO:0000269|PubMed:12707239,
ECO:0000269|PubMed:12975413,
ECO:0000269|PubMed:15358028,
ECO:0000269|PubMed:8282798}.
/FTId=VAR_004583.
VARIANT 719 719 R -> Q (in CMH1; dbSNP:rs121913641).
{ECO:0000269|PubMed:10521296,
ECO:0000269|PubMed:11968089,
ECO:0000269|PubMed:12707239,
ECO:0000269|PubMed:15358028,
ECO:0000269|PubMed:15858117,
ECO:0000269|PubMed:16199542,
ECO:0000269|PubMed:18403758,
ECO:0000269|PubMed:7848441}.
/FTId=VAR_017749.
VARIANT 719 719 R -> W (in CMH1; dbSNP:rs121913637).
{ECO:0000269|PubMed:11968089,
ECO:0000269|PubMed:12081993,
ECO:0000269|PubMed:12707239,
ECO:0000269|PubMed:12974739,
ECO:0000269|PubMed:15858117,
ECO:0000269|PubMed:7874131,
ECO:0000269|PubMed:8282798,
ECO:0000269|PubMed:9544842,
ECO:0000269|PubMed:9822100,
ECO:0000269|PubMed:9829907}.
/FTId=VAR_004584.
VARIANT 723 723 R -> C (in CMH1; dbSNP:rs121913630).
{ECO:0000269|PubMed:12707239,
ECO:0000269|PubMed:16199542,
ECO:0000269|PubMed:9829907}.
/FTId=VAR_004585.
VARIANT 723 723 R -> G (in CMH1; malignant phenotype;
dbSNP:rs121913630).
{ECO:0000269|PubMed:11113006}.
/FTId=VAR_020812.
VARIANT 728 728 A -> V (in CMH1; in cis with M-606 gives
a more severe phenotype;
dbSNP:rs121913644).
{ECO:0000269|PubMed:11424919}.
/FTId=VAR_017750.
VARIANT 731 731 P -> L (in CMH1).
/FTId=VAR_004586.
VARIANT 733 733 G -> E (in CMH1; dbSNP:rs727504241).
{ECO:0000269|PubMed:12707239}.
/FTId=VAR_019858.
VARIANT 734 734 Q -> E (in CMH1).
{ECO:0000269|PubMed:12951062}.
/FTId=VAR_029438.
VARIANT 734 734 Q -> P (in CMH1; dbSNP:rs863225097).
{ECO:0000269|PubMed:15563892}.
/FTId=VAR_042800.
VARIANT 736 736 I -> M (in CMH1).
/FTId=VAR_004587.
VARIANT 736 736 I -> T (in CMH1; dbSNP:rs727503261).
{ECO:0000269|PubMed:12820698,
ECO:0000269|PubMed:12974739,
ECO:0000269|PubMed:15856146,
ECO:0000269|PubMed:16199542}.
/FTId=VAR_029439.
VARIANT 741 741 G -> R (in CMH1; dbSNP:rs121913632).
{ECO:0000269|PubMed:12707239,
ECO:0000269|PubMed:15358028,
ECO:0000269|PubMed:15563892,
ECO:0000269|PubMed:8483915}.
/FTId=VAR_004588.
VARIANT 741 741 G -> W (in CMH1; dbSNP:rs121913632).
{ECO:0000269|PubMed:15856146}.
/FTId=VAR_004589.
VARIANT 742 742 A -> E (in CMH1; dbSNP:rs786205907).
{ECO:0000269|PubMed:16199542}.
/FTId=VAR_042801.
VARIANT 743 743 E -> D (in CMH1; dbSNP:rs397516139).
{ECO:0000269|PubMed:11733062}.
/FTId=VAR_014199.
VARIANT 763 763 V -> G (in CMH1; dbSNP:rs730880735).
{ECO:0000269|PubMed:12820698}.
/FTId=VAR_042802.
VARIANT 763 763 V -> M (in CMH1; dbSNP:rs727504253).
{ECO:0000269|PubMed:18403758}.
/FTId=VAR_045926.
VARIANT 764 764 F -> L (in CMD1S; dbSNP:rs121913643).
{ECO:0000269|PubMed:11106718}.
/FTId=VAR_017751.
VARIANT 768 768 G -> R (in CMH1; dbSNP:rs727503260).
{ECO:0000269|PubMed:12081993,
ECO:0000269|PubMed:12707239}.
/FTId=VAR_019859.
VARIANT 774 774 E -> V (in CMH1).
{ECO:0000269|PubMed:12590187}.
/FTId=VAR_042803.
VARIANT 778 778 D -> E (in CMH1; dbSNP:rs2069544).
{ECO:0000269|PubMed:12566107,
ECO:0000269|PubMed:12707239}.
/FTId=VAR_019860.
VARIANT 778 778 D -> G (in CMH1; dbSNP:rs121913634).
{ECO:0000269|PubMed:8343162}.
/FTId=VAR_004590.
VARIANT 778 778 D -> V (in CMH1).
{ECO:0000269|PubMed:15358028}.
/FTId=VAR_042804.
VARIANT 782 782 S -> N (in CMH1).
{ECO:0000269|PubMed:12590187,
ECO:0000269|PubMed:12820698,
ECO:0000269|PubMed:7731997}.
/FTId=VAR_020813.
VARIANT 787 787 R -> C (in CMH1; dbSNP:rs145677314).
{ECO:0000269|PubMed:18403758}.
/FTId=VAR_045927.
VARIANT 787 787 R -> H (in CMH1; dbSNP:rs376754645).
{ECO:0000269|PubMed:12707239,
ECO:0000269|PubMed:15858117}.
/FTId=VAR_019861.
VARIANT 796 796 L -> F (in CMH1).
{ECO:0000269|PubMed:12974739}.
/FTId=VAR_029440.
VARIANT 797 797 A -> T (in CMH1; dbSNP:rs3218716).
{ECO:0000269|PubMed:10521296,
ECO:0000269|PubMed:15358028,
ECO:0000269|PubMed:7581410}.
/FTId=VAR_004591.
VARIANT 822 822 M -> L (in CMH1; dbSNP:rs730880742).
{ECO:0000269|PubMed:12820698}.
/FTId=VAR_042805.
VARIANT 822 822 M -> T (in CMH1).
{ECO:0000269|PubMed:15563892}.
/FTId=VAR_042806.
VARIANT 823 823 G -> E (in CMH1).
{ECO:0000269|PubMed:15563892}.
/FTId=VAR_042807.
VARIANT 824 824 V -> I (in CMH1).
{ECO:0000269|PubMed:12974739}.
/FTId=VAR_029441.
VARIANT 846 846 E -> Q (in CMH1; dbSNP:rs730880748).
{ECO:0000269|PubMed:12566107}.
/FTId=VAR_020814.
VARIANT 847 847 Missing (in CMH1).
{ECO:0000269|PubMed:15358028}.
/FTId=VAR_042808.
VARIANT 852 852 M -> T (in CMH1; dbSNP:rs397516157).
{ECO:0000269|PubMed:12707239}.
/FTId=VAR_019862.
VARIANT 858 858 R -> C (in CMH1; infrequent;
dbSNP:rs2754158).
{ECO:0000269|PubMed:15358028,
ECO:0000269|PubMed:16938236}.
/FTId=VAR_039563.
VARIANT 858 858 R -> H (in CMH1; dbSNP:rs2856897).
{ECO:0000269|PubMed:15563892}.
/FTId=VAR_042809.
VARIANT 869 869 R -> C (in CMH1; dbSNP:rs730880750).
{ECO:0000269|PubMed:10862102}.
/FTId=VAR_020815.
VARIANT 869 869 R -> G (in CMH1).
{ECO:0000269|PubMed:12707239}.
/FTId=VAR_019863.
VARIANT 869 869 R -> H (in CMH1; dbSNP:rs202141173).
{ECO:0000269|PubMed:15358028}.
/FTId=VAR_042810.
VARIANT 870 870 R -> C (in CMH1; dbSNP:rs36211715).
{ECO:0000269|PubMed:10862102,
ECO:0000269|PubMed:12975413}.
/FTId=VAR_020816.
VARIANT 870 870 R -> H (in CMH1; dbSNP:rs36211715).
{ECO:0000269|PubMed:12974739,
ECO:0000269|PubMed:16650083,
ECO:0000269|PubMed:7731997}.
/FTId=VAR_004592.
VARIANT 877 877 M -> K (in CMH1).
{ECO:0000269|PubMed:11133230}.
/FTId=VAR_020817.
VARIANT 882 882 Q -> E (in CMH1; dbSNP:rs397516160).
{ECO:0000269|PubMed:12820698}.
/FTId=VAR_042811.
VARIANT 883 883 Missing (in CMH1).
{ECO:0000269|PubMed:12707239}.
/FTId=VAR_019864.
VARIANT 894 894 E -> G (in CMH1; dbSNP:rs397516161).
{ECO:0000269|PubMed:15358028,
ECO:0000269|PubMed:15858117}.
/FTId=VAR_042812.
VARIANT 901 901 A -> G (in CMH1).
{ECO:0000269|PubMed:15856146}.
/FTId=VAR_042813.
VARIANT 905 905 C -> F (in CMH1).
{ECO:0000269|PubMed:12974739}.
/FTId=VAR_029442.
VARIANT 906 906 D -> G (in CMH1; dbSNP:rs267606908).
{ECO:0000269|PubMed:12081993,
ECO:0000269|PubMed:16267253}.
/FTId=VAR_042814.
VARIANT 908 908 L -> V (in CMH1; dbSNP:rs121913631).
{ECO:0000269|PubMed:12820698,
ECO:0000269|PubMed:12975413,
ECO:0000269|PubMed:15358028,
ECO:0000269|PubMed:15858117,
ECO:0000269|PubMed:1638703,
ECO:0000269|PubMed:18403758,
ECO:0000269|PubMed:8435239}.
/FTId=VAR_004593.
VARIANT 921 921 E -> K (in CMH1; dbSNP:rs730880759).
{ECO:0000269|PubMed:15358028}.
/FTId=VAR_042815.
VARIANT 924 924 E -> K (in CMH1; dbSNP:rs121913628).
{ECO:0000269|PubMed:12818575,
ECO:0000269|PubMed:15358028,
ECO:0000269|PubMed:15563892,
ECO:0000269|PubMed:18403758}.
/FTId=VAR_004594.
VARIANT 924 924 E -> Q (in CMH1).
{ECO:0000269|PubMed:12974739}.
/FTId=VAR_029443.
VARIANT 927 927 E -> K (in CMH1; dbSNP:rs397516170).
{ECO:0000269|PubMed:15858117}.
/FTId=VAR_042816.
VARIANT 927 927 Missing (in CMH1).
{ECO:0000269|PubMed:11968089}.
/FTId=VAR_020818.
VARIANT 928 928 D -> N (in CMH1; dbSNP:rs727503252).
{ECO:0000269|PubMed:12974739,
ECO:0000269|PubMed:15856146}.
/FTId=VAR_029444.
VARIANT 930 930 E -> K (in CMH1; dbSNP:rs397516171).
{ECO:0000269|PubMed:12975413,
ECO:0000269|PubMed:15563892}.
/FTId=VAR_004595.
VARIANT 930 930 Missing (in CMH1).
{ECO:0000269|PubMed:12707239,
ECO:0000269|PubMed:9829907}.
/FTId=VAR_004596.
VARIANT 931 931 E -> K (in CMH1).
{ECO:0000269|PubMed:15358028}.
/FTId=VAR_042817.
VARIANT 935 935 E -> K (in CMH1; dbSNP:rs121913639).
/FTId=VAR_004597.
VARIANT 949 949 E -> K (in CMH1; dbSNP:rs121913629).
/FTId=VAR_004598.
VARIANT 953 953 D -> H (in CMH1).
{ECO:0000269|PubMed:15358028}.
/FTId=VAR_042818.
VARIANT 1019 1019 T -> N (in CMD1S; dbSNP:rs755392435).
{ECO:0000269|PubMed:15769782}.
/FTId=VAR_042819.
VARIANT 1044 1044 V -> A (in CMD1S).
{ECO:0000269|PubMed:21846512}.
/FTId=VAR_067260.
VARIANT 1057 1057 G -> D (in CMH1).
{ECO:0000269|PubMed:16199542}.
/FTId=VAR_042820.
VARIANT 1057 1057 G -> S (in CMH1; dbSNP:rs397516179).
{ECO:0000269|PubMed:15358028}.
/FTId=VAR_042821.
VARIANT 1101 1104 Missing (in CMD1S).
{ECO:0000269|PubMed:21846512}.
/FTId=VAR_067261.
VARIANT 1124 1124 A -> S (in dbSNP:rs1041961).
{ECO:0000269|PubMed:2249844}.
/FTId=VAR_017753.
VARIANT 1135 1135 L -> R (in CMH1).
{ECO:0000269|PubMed:12707239}.
/FTId=VAR_019865.
VARIANT 1193 1193 R -> S (in CMD1S).
{ECO:0000269|PubMed:15769782}.
/FTId=VAR_042822.
VARIANT 1218 1218 E -> Q (in CMH1).
{ECO:0000269|PubMed:12707239}.
/FTId=VAR_019866.
VARIANT 1220 1220 Missing (in CMD1S).
{ECO:0000269|PubMed:21127202}.
/FTId=VAR_073882.
VARIANT 1263 1263 A -> E (in CMD1S; dbSNP:rs758889483).
{ECO:0000269|PubMed:21846512}.
/FTId=VAR_067262.
VARIANT 1297 1297 L -> V (in CMD1S).
{ECO:0000269|PubMed:21846512}.
/FTId=VAR_067263.
VARIANT 1327 1327 N -> K (in CMH1; dbSNP:rs141764279).
{ECO:0000269|PubMed:15483641}.
/FTId=VAR_042823.
VARIANT 1356 1356 E -> K (in CMH1; dbSNP:rs727503246).
{ECO:0000269|PubMed:15358028,
ECO:0000269|PubMed:15856146}.
/FTId=VAR_042824.
VARIANT 1359 1359 R -> C (in CMD1S; dbSNP:rs45451303).
{ECO:0000269|PubMed:18506004}.
/FTId=VAR_073883.
VARIANT 1377 1377 T -> M (in CMH1; dbSNP:rs397516201).
{ECO:0000269|PubMed:12707239,
ECO:0000269|PubMed:15358028}.
/FTId=VAR_019867.
VARIANT 1379 1379 A -> T (in CMH1; dbSNP:rs397516202).
{ECO:0000269|PubMed:11861413,
ECO:0000269|PubMed:12707239}.
/FTId=VAR_019868.
VARIANT 1382 1382 R -> W (in CMH1; dbSNP:rs730880910).
{ECO:0000269|PubMed:12707239}.
/FTId=VAR_019869.
VARIANT 1414 1414 L -> M (in CMH1; dbSNP:rs201895208).
{ECO:0000269|PubMed:18403758}.
/FTId=VAR_045928.
VARIANT 1420 1420 R -> W (in CMH1; dbSNP:rs145213771).
{ECO:0000269|PubMed:15358028}.
/FTId=VAR_042825.
VARIANT 1426 1426 E -> K (in CMD1S; dbSNP:rs397516208).
{ECO:0000269|PubMed:15769782}.
/FTId=VAR_042826.
VARIANT 1454 1454 A -> T (in CMH1).
{ECO:0000269|PubMed:15856146}.
/FTId=VAR_042827.
VARIANT 1459 1459 K -> N (in CMH1 and CMD1S;
dbSNP:rs201307101).
{ECO:0000269|PubMed:15358028,
ECO:0000269|PubMed:21127202}.
/FTId=VAR_042828.
VARIANT 1475 1475 R -> C (in dbSNP:rs139646545).
{ECO:0000269|PubMed:15483641}.
/FTId=VAR_042829.
VARIANT 1491 1491 S -> C (in dbSNP:rs3729823).
{ECO:0000269|PubMed:11861413,
ECO:0000269|PubMed:15358028,
ECO:0000269|PubMed:15483641,
ECO:0000269|PubMed:15769782}.
/FTId=VAR_020819.
VARIANT 1500 1500 R -> P (in MPD1; dbSNP:rs121913647).
{ECO:0000269|PubMed:15322983}.
/FTId=VAR_022369.
VARIANT 1513 1513 T -> S (in CMH1; dbSNP:rs397516222).
{ECO:0000269|PubMed:15358028}.
/FTId=VAR_042830.
VARIANT 1519 1519 S -> C. {ECO:0000269|PubMed:15858117}.
/FTId=VAR_042831.
VARIANT 1555 1555 E -> K (in CMH1).
{ECO:0000269|PubMed:11968089}.
/FTId=VAR_020820.
VARIANT 1573 1573 E -> K (in CMD1S; dbSNP:rs750987717).
{ECO:0000269|PubMed:21127202}.
/FTId=VAR_073884.
VARIANT 1617 1617 Missing (in MPD1).
{ECO:0000269|PubMed:15322983}.
/FTId=VAR_042832.
VARIANT 1634 1634 R -> C (in CMD1S; dbSNP:rs397516232).
{ECO:0000269|PubMed:15769782}.
/FTId=VAR_042833.
VARIANT 1663 1663 A -> P (in MPD1; dbSNP:rs797044601).
{ECO:0000269|PubMed:15322983}.
/FTId=VAR_022370.
VARIANT 1692 1692 V -> M (probable polymorphism; has been
originally reported as a hypertrophic
cardiomyopathy mutation).
{ECO:0000269|PubMed:12707239}.
/FTId=VAR_019870.
VARIANT 1706 1706 L -> P (in MPD1; dbSNP:rs797044602).
{ECO:0000269|PubMed:15322983}.
/FTId=VAR_022371.
VARIANT 1712 1712 R -> W (in CMH1; dbSNP:rs121913650).
{ECO:0000269|PubMed:15483641}.
/FTId=VAR_042834.
VARIANT 1729 1729 Missing (in MPD1).
{ECO:0000269|PubMed:15322983}.
/FTId=VAR_042835.
VARIANT 1752 1752 E -> K (in CMH1; associated with
phenotype variability;
dbSNP:rs730880916).
{ECO:0000269|PubMed:25182012}.
/FTId=VAR_072816.
VARIANT 1753 1753 E -> K (in CMH1; dbSNP:rs545585809).
{ECO:0000269|PubMed:15483641}.
/FTId=VAR_042836.
VARIANT 1768 1768 E -> K (in CMH1; dbSNP:rs397516241).
{ECO:0000269|PubMed:15358028}.
/FTId=VAR_042837.
VARIANT 1776 1776 S -> G (in CMH1; dbSNP:rs369437262).
{ECO:0000269|PubMed:11861413}.
/FTId=VAR_020821.
VARIANT 1776 1776 S -> T (in CMD1S).
{ECO:0000269|PubMed:18506004}.
/FTId=VAR_073885.
VARIANT 1777 1777 A -> T (in CMH1; dbSNP:rs200939753).
{ECO:0000269|PubMed:12707239}.
/FTId=VAR_019871.
VARIANT 1793 1793 L -> P (in MSMA; dbSNP:rs121913654).
{ECO:0000269|PubMed:16684601}.
/FTId=VAR_073886.
VARIANT 1820 1820 R -> W (in MSMB; dbSNP:rs145734640).
{ECO:0000269|PubMed:25666907}.
/FTId=VAR_073887.
VARIANT 1845 1845 R -> W (in MSMA and SPMM;
dbSNP:rs28933098).
{ECO:0000269|PubMed:14520662,
ECO:0000269|PubMed:17336526}.
/FTId=VAR_017754.
VARIANT 1854 1854 T -> M (in CMH1; dbSNP:rs372381770).
{ECO:0000269|PubMed:15358028}.
/FTId=VAR_042838.
VARIANT 1883 1883 E -> K (in CMH1; dbSNP:rs121913652).
{ECO:0000269|PubMed:17372140}.
/FTId=VAR_042839.
VARIANT 1901 1901 H -> L (in MSMA; dbSNP:rs121913649).
{ECO:0000269|PubMed:15136674}.
/FTId=VAR_042840.
VARIANT 1918 1918 N -> K (in CMD1S).
{ECO:0000269|PubMed:21127202}.
/FTId=VAR_073888.
VARIANT 1919 1919 K -> N. {ECO:0000269|PubMed:15358028}.
/FTId=VAR_042841.
VARIANT 1929 1929 T -> M (in CMH1; dbSNP:rs730880918).
{ECO:0000269|PubMed:15358028}.
/FTId=VAR_042842.
CONFLICT 88 88 E -> Q (in Ref. 8; AAA60384).
{ECO:0000305}.
CONFLICT 397 397 K -> G (in Ref. 10). {ECO:0000305}.
CONFLICT 672 674 CII -> LYH (in Ref. 2; CAA37068).
{ECO:0000305}.
CONFLICT 858 858 R -> A (in Ref. 2; CAA37068).
{ECO:0000305}.
CONFLICT 942 943 KL -> NV (in Ref. 2; CAA37068).
{ECO:0000305}.
CONFLICT 1077 1077 D -> E (in Ref. 13; CAA35940).
{ECO:0000305}.
CONFLICT 1159 1159 V -> C (in Ref. 2; CAA37068 and 3;
CAC20413). {ECO:0000305}.
CONFLICT 1207 1207 I -> M (in Ref. 4; ACH92815).
{ECO:0000305}.
CONFLICT 1313 1313 E -> G (in Ref. 14; CAA27381).
{ECO:0000305}.
CONFLICT 1356 1356 E -> R (in Ref. 14; CAA27381).
{ECO:0000305}.
CONFLICT 1359 1360 RV -> GD (in Ref. 14; CAA27381).
{ECO:0000305}.
CONFLICT 1575 1576 KL -> NV (in Ref. 17; AAA36345).
{ECO:0000305}.
CONFLICT 1576 1577 LA -> RQ (in Ref. 14; CAA27381).
{ECO:0000305}.
CONFLICT 1681 1681 Missing (in Ref. 2; CAA37068).
{ECO:0000305}.
CONFLICT 1703 1704 EQ -> DE (in Ref. 13; CAA35940).
{ECO:0000305}.
CONFLICT 1703 1704 EQ -> DR (in Ref. 2; CAA37068 and 16;
AAA36343). {ECO:0000305}.
CONFLICT 1866 1866 D -> A (in Ref. 18; CAA29119).
{ECO:0000305}.
HELIX 3 15 {ECO:0000244|PDB:4PA0}.
HELIX 20 26 {ECO:0000244|PDB:4PA0}.
TURN 33 35 {ECO:0000244|PDB:4PA0}.
STRAND 36 41 {ECO:0000244|PDB:4PA0}.
TURN 42 44 {ECO:0000244|PDB:4PA0}.
STRAND 45 55 {ECO:0000244|PDB:4PA0}.
STRAND 58 63 {ECO:0000244|PDB:4PA0}.
TURN 64 66 {ECO:0000244|PDB:4DB1}.
STRAND 68 72 {ECO:0000244|PDB:4PA0}.
HELIX 73 75 {ECO:0000244|PDB:4PA0}.
HELIX 82 84 {ECO:0000244|PDB:4PA0}.
HELIX 90 92 {ECO:0000244|PDB:4PA0}.
HELIX 98 110 {ECO:0000244|PDB:4PA0}.
STRAND 115 118 {ECO:0000244|PDB:4PA0}.
STRAND 121 125 {ECO:0000244|PDB:4PA0}.
HELIX 136 142 {ECO:0000244|PDB:4PA0}.
HELIX 147 149 {ECO:0000244|PDB:4PA0}.
HELIX 154 168 {ECO:0000244|PDB:4PA0}.
STRAND 172 179 {ECO:0000244|PDB:4PA0}.
HELIX 184 198 {ECO:0000244|PDB:4PA0}.
HELIX 216 231 {ECO:0000244|PDB:4PA0}.
STRAND 244 252 {ECO:0000244|PDB:4PA0}.
STRAND 256 266 {ECO:0000244|PDB:4PA0}.
HELIX 270 273 {ECO:0000244|PDB:4PA0}.
HELIX 284 289 {ECO:0000244|PDB:4PA0}.
HELIX 296 300 {ECO:0000244|PDB:4PA0}.
HELIX 307 309 {ECO:0000244|PDB:4PA0}.
HELIX 311 313 {ECO:0000244|PDB:4PA0}.
HELIX 325 338 {ECO:0000244|PDB:4PA0}.
HELIX 343 359 {ECO:0000244|PDB:4PA0}.
STRAND 364 366 {ECO:0000244|PDB:4PA0}.
STRAND 368 371 {ECO:0000244|PDB:4PA0}.
STRAND 373 376 {ECO:0000244|PDB:4PA0}.
HELIX 379 387 {ECO:0000244|PDB:4PA0}.
HELIX 392 400 {ECO:0000244|PDB:4PA0}.
HELIX 417 447 {ECO:0000244|PDB:4PA0}.
STRAND 455 463 {ECO:0000244|PDB:4PA0}.
STRAND 469 471 {ECO:0000244|PDB:4PA0}.
HELIX 473 503 {ECO:0000244|PDB:4PA0}.
HELIX 513 517 {ECO:0000244|PDB:4PA0}.
HELIX 518 525 {ECO:0000244|PDB:4PA0}.
HELIX 530 537 {ECO:0000244|PDB:4PA0}.
HELIX 545 556 {ECO:0000244|PDB:4PA0}.
TURN 557 559 {ECO:0000244|PDB:4PA0}.
STRAND 570 572 {ECO:0000244|PDB:4DB1}.
STRAND 577 581 {ECO:0000244|PDB:4PA0}.
STRAND 584 588 {ECO:0000244|PDB:4PA0}.
HELIX 593 598 {ECO:0000244|PDB:4PA0}.
HELIX 603 610 {ECO:0000244|PDB:4PA0}.
HELIX 615 620 {ECO:0000244|PDB:4PA0}.
HELIX 647 663 {ECO:0000244|PDB:4PA0}.
STRAND 665 673 {ECO:0000244|PDB:4PA0}.
HELIX 686 695 {ECO:0000244|PDB:4PA0}.
HELIX 698 706 {ECO:0000244|PDB:4PA0}.
STRAND 711 714 {ECO:0000244|PDB:4PA0}.
HELIX 715 722 {ECO:0000244|PDB:4PA0}.
HELIX 723 725 {ECO:0000244|PDB:4PA0}.
HELIX 727 729 {ECO:0000244|PDB:4PA0}.
STRAND 733 735 {ECO:0000244|PDB:4PA0}.
HELIX 738 747 {ECO:0000244|PDB:4PA0}.
STRAND 749 751 {ECO:0000244|PDB:4PA0}.
STRAND 755 758 {ECO:0000244|PDB:4PA0}.
STRAND 760 765 {ECO:0000244|PDB:4PA0}.
HELIX 767 787 {ECO:0000244|PDB:4PA0}.
HELIX 838 958 {ECO:0000244|PDB:2FXO}.
TURN 959 961 {ECO:0000244|PDB:2FXO}.
HELIX 1173 1258 {ECO:0000244|PDB:4XA1}.
HELIX 1259 1261 {ECO:0000244|PDB:4XA1}.
HELIX 1265 1272 {ECO:0000244|PDB:4XA1}.
HELIX 1361 1425 {ECO:0000244|PDB:4XA3}.
HELIX 1526 1570 {ECO:0000244|PDB:5CJ1}.
HELIX 1590 1655 {ECO:0000244|PDB:5CHX}.
HELIX 1777 1806 {ECO:0000244|PDB:4XA6}.
HELIX 1810 1841 {ECO:0000244|PDB:4XA6}.
TURN 1842 1846 {ECO:0000244|PDB:4XA6}.
HELIX 1847 1856 {ECO:0000244|PDB:4XA6}.
HELIX 1864 1869 {ECO:0000244|PDB:4XA6}.
SEQUENCE 1935 AA; 223097 MW; C58B22F914215718 CRC64;
MGDSEMAVFG AAAPYLRKSE KERLEAQTRP FDLKKDVFVP DDKQEFVKAK IVSREGGKVT
AETEYGKTVT VKEDQVMQQN PPKFDKIEDM AMLTFLHEPA VLYNLKDRYG SWMIYTYSGL
FCVTVNPYKW LPVYTPEVVA AYRGKKRSEA PPHIFSISDN AYQYMLTDRE NQSILITGES
GAGKTVNTKR VIQYFAVIAA IGDRSKKDQS PGKGTLEDQI IQANPALEAF GNAKTVRNDN
SSRFGKFIRI HFGATGKLAS ADIETYLLEK SRVIFQLKAE RDYHIFYQIL SNKKPELLDM
LLITNNPYDY AFISQGETTV ASIDDAEELM ATDNAFDVLG FTSEEKNSMY KLTGAIMHFG
NMKFKLKQRE EQAEPDGTEE ADKSAYLMGL NSADLLKGLC HPRVKVGNEY VTKGQNVQQV
IYATGALAKA VYERMFNWMV TRINATLETK QPRQYFIGVL DIAGFEIFDF NSFEQLCINF
TNEKLQQFFN HHMFVLEQEE YKKEGIEWTF IDFGMDLQAC IDLIEKPMGI MSILEEECMF
PKATDMTFKA KLFDNHLGKS ANFQKPRNIK GKPEAHFSLI HYAGIVDYNI IGWLQKNKDP
LNETVVGLYQ KSSLKLLSTL FANYAGADAP IEKGKGKAKK GSSFQTVSAL HRENLNKLMT
NLRSTHPHFV RCIIPNETKS PGVMDNPLVM HQLRCNGVLE GIRICRKGFP NRILYGDFRQ
RYRILNPAAI PEGQFIDSRK GAEKLLSSLD IDHNQYKFGH TKVFFKAGLL GLLEEMRDER
LSRIITRIQA QSRGVLARME YKKLLERRDS LLVIQWNIRA FMGVKNWPWM KLYFKIKPLL
KSAEREKEMA SMKEEFTRLK EALEKSEARR KELEEKMVSL LQEKNDLQLQ VQAEQDNLAD
AEERCDQLIK NKIQLEAKVK EMNERLEDEE EMNAELTAKK RKLEDECSEL KRDIDDLELT
LAKVEKEKHA TENKVKNLTE EMAGLDEIIA KLTKEKKALQ EAHQQALDDL QAEEDKVNTL
TKAKVKLEQQ VDDLEGSLEQ EKKVRMDLER AKRKLEGDLK LTQESIMDLE NDKQQLDERL
KKKDFELNAL NARIEDEQAL GSQLQKKLKE LQARIEELEE ELEAERTARA KVEKLRSDLS
RELEEISERL EEAGGATSVQ IEMNKKREAE FQKMRRDLEE ATLQHEATAA ALRKKHADSV
AELGEQIDNL QRVKQKLEKE KSEFKLELDD VTSNMEQIIK AKANLEKMCR TLEDQMNEHR
SKAEETQRSV NDLTSQRAKL QTENGELSRQ LDEKEALISQ LTRGKLTYTQ QLEDLKRQLE
EEVKAKNALA HALQSARHDC DLLREQYEEE TEAKAELQRV LSKANSEVAQ WRTKYETDAI
QRTEELEEAK KKLAQRLQEA EEAVEAVNAK CSSLEKTKHR LQNEIEDLMV DVERSNAAAA
ALDKKQRNFD KILAEWKQKY EESQSELESS QKEARSLSTE LFKLKNAYEE SLEHLETFKR
ENKNLQEEIS DLTEQLGSSG KTIHELEKVR KQLEAEKMEL QSALEEAEAS LEHEEGKILR
AQLEFNQIKA EIERKLAEKD EEMEQAKRNH LRVVDSLQTS LDAETRSRNE ALRVKKKMEG
DLNEMEIQLS HANRMAAEAQ KQVKSLQSLL KDTQIQLDDA VRANDDLKEN IAIVERRNNL
LQAELEELRA VVEQTERSRK LAEQELIETS ERVQLLHSQN TSLINQKKKM DADLSQLQTE
VEEAVQECRN AEEKAKKAIT DAAMMAEELK KEQDTSAHLE RMKKNMEQTI KDLQHRLDEA
EQIALKGGKK QLQKLEARVR ELENELEAEQ KRNAESVKGM RKSERRIKEL TYQTEEDRKN
LLRLQDLVDK LQLKVKAYKR QAEEAEEQAN TNLSKFRKVQ HELDEAEERA DIAESQVNKL
RAKSRDIGTK GLNEE


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