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Myosin-binding protein C, cardiac-type (Cardiac MyBP-C) (C-protein, cardiac muscle isoform)

 MYPC3_HUMAN             Reviewed;        1274 AA.
Q14896; A5PL00; Q16410; Q6R2F7; Q9UE27; Q9UM53;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
28-NOV-2012, sequence version 4.
25-OCT-2017, entry version 182.
RecName: Full=Myosin-binding protein C, cardiac-type;
Short=Cardiac MyBP-C;
AltName: Full=C-protein, cardiac muscle isoform;
Name=MYBPC3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT CMH4 GLN-820.
TISSUE=Heart;
PubMed=7744002;
Gautel M., Zuffardi O., Freiburg A., Labeit S.;
"Phosphorylation switches specific for the cardiac isoform of myosin
binding protein-C: a modulator of cardiac contraction?";
EMBO J. 14:1952-1960(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CMH4 GLN-542 AND
GLN-820.
PubMed=9048664;
Carrier L., Bonne G., Bahrend E., Yu B., Richard P., Niel F.,
Hainque B., Cruaud C., Gary F., Labeit S., Bouhour J.-B., Dubourg O.,
Desnos M., Hagege A.A., Trent R.J., Komajda M., Fiszman M.,
Schwartz K.;
"Organization and sequence of human cardiac myosin binding protein C
gene (MYBPC3) and identification of mutations predicted to produce
truncated proteins in familial hypertrophic cardiomyopathy.";
Circ. Res. 80:427-434(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CMH4 GLN-451; GLN-495
AND GLN-502.
PubMed=9562578; DOI=10.1056/NEJM199804303381802;
Niimura H., Bachinski L.L., Sangwatanaroj S., Watkins H.,
Chudley A.E., McKenna W., Kristinsson A., Roberts R., Sole M.,
Maron B.J., Seidman J.G., Seidman C.E.;
"Mutations in the gene for cardiac myosin-binding protein C and late-
onset familial hypertrophic cardiomyopathy.";
N. Engl. J. Med. 338:1248-1257(1998).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-158; ILE-189;
GLY-236; GLN-281; TRP-382; VAL-383; THR-522; VAL-833; GLU-998 AND
CYS-1048.
NIEHS SNPs program;
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Rieder M.J., Bertucci C., Stanaway I.B., Johnson E.J., Swanson J.E.,
Siegel D.L., da Ponte S.H., Igartua C., Patterson K., Nickerson D.A.;
Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[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 [MRNA] OF 640-694.
PubMed=7493026; DOI=10.1038/ng1295-438;
Bonne G., Carrier L., Bercovici J., Cruaud C., Richard P., Hainque B.,
Gautel M., Labeit S., James M., Beckmann J., Weissenbach J.,
Vosberg H.-P., Fiszman M., Komajda M., Schwartz K.;
"Cardiac myosin binding protein-C gene splice acceptor site mutation
is associated with familial hypertrophic cardiomyopathy.";
Nat. Genet. 11:438-440(1995).
[9]
STRUCTURE BY NMR OF 641-770, AND CHARACTERIZATION OF VARIANTS HIS-654
AND LYS-755.
PubMed=12787675; DOI=10.1016/S0022-2836(03)00425-X;
Idowu S.M., Gautel M., Perkins S.J., Pfuhl M.;
"Structure, stability and dynamics of the central domain of cardiac
myosin binding protein C (MyBP-C): implications for multidomain
assembly and causes for cardiomyopathy.";
J. Mol. Biol. 329:745-761(2003).
[10]
STRUCTURE BY NMR OF 358-450, AND DISULFIDE BOND.
PubMed=15213454; DOI=10.1023/B:JNMR.0000032510.03606.63;
Ababou A., Zhou L., Gautel M., Pfuhl M.;
"Sequence specific assignment of domain C1 of the N-terminal myosin-
binding site of human cardiac myosin binding protein C (MyBP-C).";
J. Biomol. NMR 29:431-432(2004).
[11]
X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 151-258.
PubMed=18560154; DOI=10.1107/S0907444908008792;
Fisher S.J., Helliwell J.R., Khurshid S., Govada L., Redwood C.,
Squire J.M., Chayen N.E.;
"An investigation into the protonation states of the C1 domain of
cardiac myosin-binding protein C.";
Acta Crystallogr. D 64:658-664(2008).
[12]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 151-258.
PubMed=18374358; DOI=10.1016/j.jmb.2008.02.044;
Govada L., Carpenter L., da Fonseca P.C., Helliwell J.R.,
Rizkallah P., Flashman E., Chayen N.E., Redwood C., Squire J.M.;
"Crystal structure of the C1 domain of cardiac myosin binding protein-
C: implications for hypertrophic cardiomyopathy.";
J. Mol. Biol. 378:387-397(2008).
[13]
STRUCTURE BY NMR OF 151-260, AND ZINC-BINDING SITE.
PubMed=18926831; DOI=10.1016/j.jmb.2008.09.065;
Ababou A., Rostkova E., Mistry S., Le Masurier C., Gautel M.,
Pfuhl M.;
"Myosin binding protein C positioned to play a key role in regulation
of muscle contraction: structure and interactions of domain C1.";
J. Mol. Biol. 384:615-630(2008).
[14]
VARIANT CMH4 LYS-755.
PubMed=9541104; DOI=10.1136/jmg.35.3.205;
Yu B., French J.A., Carrier L., Jeremy R.W., McTaggart D.R.,
Nicholson M.R., Hambly B., Semsarian C., Richmond D.R., Schwartz K.,
Trent R.J.;
"Molecular pathology of familial hypertrophic cardiomyopathy caused by
mutations in the cardiac myosin binding protein C gene.";
J. Med. Genet. 35:205-210(1998).
[15]
VARIANT CMH4 HIS-654.
PubMed=9541115; DOI=10.1136/jmg.35.3.253;
Moolman-Smook J.C., Mayosi B., Brink P., Corfield V.A.;
"Identification of a new missense mutation in MyBP-C associated with
hypertrophic cardiomyopathy.";
J. Med. Genet. 35:253-254(1998).
[16]
VARIANT MET-896.
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).
[17]
VARIANT CMH4 GLN-495, AND VARIANT GLN-326.
PubMed=11499718; DOI=10.1016/S0735-1097(01)01386-9;
Maron B.J., Niimura H., Casey S.A., Soper M.K., Wright G.B.,
Seidman J.G., Seidman C.E.;
"Development of left ventricular hypertrophy in adults in hypertrophic
cardiomyopathy caused by cardiac myosin-binding protein C gene
mutations.";
J. Am. Coll. Cardiol. 38:315-321(2001).
[18]
VARIANTS CMH4 TRP-282; ARG-507; ARG-566 AND ILE-1115.
PubMed=11499719; DOI=10.1016/S0735-1097(01)01387-0;
Erdmann J., Raible J., Maki-Abadi J., Hummel M., Hammann J.,
Wollnik B., Frantz E., Fleck E., Hetzer R., Regitz-Zagrosek V.;
"Spectrum of clinical phenotypes and gene variants in cardiac myosin-
binding protein C mutation carriers with hypertrophic
cardiomyopathy.";
J. Am. Coll. Cardiol. 38:322-330(2001).
[19]
VARIANT CMH4 THR-948, AND VARIANTS GLY-236 AND GLN-326.
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).
[20]
VARIANTS CMH4 ALA-59 AND GLN-1002, AND VARIANT GLN-326.
PubMed=11815426; DOI=10.1161/hc0402.102990;
Niimura H., Patton K.K., McKenna W.J., Soults J., Maron B.J.,
Seidman J.G., Seidman C.E.;
"Sarcomere protein gene mutations in hypertrophic cardiomyopathy of
the elderly.";
Circulation 105:446-451(2002).
[21]
VARIANTS LEU-147; GLY-236; GLN-326; MET-896 AND HIS-1138.
PubMed=12110947; DOI=10.1007/s00109-002-0323-9;
Jaeaeskelaeinen P., Kuusisto J., Miettinen R., Kaerkkaeinen P.,
Kaerkkaeinen S., Heikkinen S., Peltola P., Pihlajamaeki J.,
Vauhkonen I., Laakso M.;
"Mutations in the cardiac myosin-binding protein C gene are the
predominant cause of familial hypertrophic cardiomyopathy in eastern
Finland.";
J. Mol. Med. 80:412-422(2002).
[22]
VARIANTS CMH4 LYS-258; HIS-810; GLN-820 AND HIS-873.
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).
[23]
VARIANTS CMH4 PRO-257; LYS-258; GLU-278; ALA-279; PRO-352; TRP-502;
LYS-504 DEL; GLN-542; ARG-811; VAL-833; THR-1194 AND THR-1255, AND
VARIANTS GLN-326 AND MET-896.
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).
[24]
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).
[25]
VARIANTS CMH4 LYS-258; TRP-282; ARG-507; TRP-523; ARG-566; PRO-668;
VAL-833 AND ILE-1115, AND VARIANTS GLY-236 AND GLN-326.
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).
[26]
VARIANTS CMH4 SER-161; LYS-258; ASN-605; THR-833; TRP-834 AND
THR-1131.
PubMed=14563344; DOI=10.1016/S0195-668X(03)00466-4;
Alders M., Jongbloed R., Deelen W., van den Wijngaard A.,
Doevendans P., Ten Cate F., Regitz-Zagrosek V., Vosberg H.-P.,
van Langen I., Wilde A., Dooijes D., Mannens M.;
"The 2373insG mutation in the MYBPC3 gene is a founder mutation, which
accounts for nearly one-fourth of the HCM cases in the Netherlands.";
Eur. Heart J. 24:1848-1853(2003).
[27]
VARIANT CMH4 GLN-820.
PubMed=12628722; DOI=10.1016/S0735-1097(02)02957-1;
Konno T., Shimizu M., Ino H., Matsuyama T., Yamaguchi M., Terai H.,
Hayashi K., Mabuchi T., Kiyama M., Sakata K., Hayashi T., Inoue M.,
Kaneda T., Mabuchi H.;
"A novel missense mutation in the myosin binding protein-C gene is
responsible for hypertrophic cardiomyopathy with left ventricular
dysfunction and dilation in elderly patients.";
J. Am. Coll. Cardiol. 41:781-786(2003).
[28]
VARIANTS CMH4 SER-237; HIS-668 AND THR-833, AND VARIANTS GLN-326 AND
MET-896.
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).
[29]
VARIANTS CMH4 ASN-228; LYS-258; LYS-813 DEL AND THR-833.
PubMed=15114369; DOI=10.1038/sj.ejhg.5201190;
Andersen P.S., Havndrup O., Bundgaard H., Larsen L.A., Vuust J.,
Pedersen A.K., Kjeldsen K., Christiansen M.;
"Genetic and phenotypic characterization of mutations in myosin-
binding protein C (MYBPC3) in 81 families with familial hypertrophic
cardiomyopathy: total or partial haploinsufficiency.";
Eur. J. Hum. Genet. 12:673-677(2004).
[30]
VARIANTS CMH4 ARG-5; LEU-219; ILE-256; LYS-258; HIS-458; ARG-490;
GLN-495; TRP-502; GLN-542; VAL-604; ASN-605; LEU-608; CYS-733;
ASN-770; ARG-792; HIS-810; LYS-811 DEL; THR-833; GLU-998; ARG-998;
ILE-1113 AND THR-1131, AND VARIANTS MET-158; GLY-236; GLN-326;
TRP-382; SER-416; ARG-507; MET-545 AND MET-896.
PubMed=15519027; DOI=10.1016/j.jacc.2004.07.045;
Van Driest S.L., Vasile V.C., Ommen S.R., Will M.L., Tajik A.J.,
Gersh B.J., Ackerman M.J.;
"Myosin binding protein C mutations and compound heterozygosity in
hypertrophic cardiomyopathy.";
J. Am. Coll. Cardiol. 44:1903-1910(2004).
[31]
VARIANT GLY-236.
PubMed=15582318; DOI=10.1016/j.jacc.2004.08.058;
Hayashi T., Arimura T., Itoh-Satoh M., Ueda K., Hohda S., Inagaki N.,
Takahashi M., Hori H., Yasunami M., Nishi H., Koga Y., Nakamura H.,
Matsuzaki M., Choi B.Y., Bae S.W., You C.W., Han K.H., Park J.E.,
Knoell R., Hoshijima M., Chien K.R., Kimura A.;
"Tcap gene mutations in hypertrophic cardiomyopathy and dilated
cardiomyopathy.";
J. Am. Coll. Cardiol. 44:2192-2201(2004).
[32]
VARIANTS CMH4 LYS-258; ARG-263; SER-417; HIS-669 AND ASP-759.
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).
[33]
VARIANT GLY-236, AND VARIANTS CMH4 ASP-342; VAL-627 AND MET-771.
PubMed=16004897; DOI=10.1016/j.ijcard.2004.05.060;
Garcia-Castro M., Reguero J.R., Alvarez V., Batalla A., Soto M.I.,
Albaladejo V., Coto E.;
"Hypertrophic cardiomyopathy linked to homozygosity for a new mutation
in the myosin-binding protein C gene (A627V) suggests a dosage
effect.";
Int. J. Cardiol. 102:501-507(2005).
[34]
VARIANTS CMH4 HIS-273; TRP-502 AND GLN-542, AND VARIANT GLN-326.
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).
[35]
VARIANTS CMH4 LYS-258; CYS-272; VAL-336; GLN-495; GLN-502; SER-957 AND
ILE-958.
PubMed=18957093; DOI=10.1186/1471-2350-9-95;
Ehlermann P., Weichenhan D., Zehelein J., Steen H., Pribe R.,
Zeller R., Lehrke S., Zugck C., Ivandic B.T., Katus H.A.;
"Adverse events in families with hypertrophic or dilated
cardiomyopathy and mutations in the MYBPC3 gene.";
BMC Med. Genet. 9:95-95(2008).
[36]
VARIANTS CMH4 LYS-334; LYS-814 DEL; GLU-998 AND MET-1046,
CHARACTERIZATION OF VARIANTS CMH4 LYS-334; LYS-814 DEL; GLU-998 AND
MET-1046, VARIANT GLY-236, AND UBIQUITINATION.
PubMed=18929575; DOI=10.1016/j.jmb.2008.09.070;
Bahrudin U., Morisaki H., Morisaki T., Ninomiya H., Higaki K.,
Nanba E., Igawa O., Takashima S., Mizuta E., Miake J., Yamamoto Y.,
Shirayoshi Y., Kitakaze M., Carrier L., Hisatome I.;
"Ubiquitin-proteasome system impairment caused by a missense cardiac
myosin-binding protein C mutation and associated with cardiac
dysfunction in hypertrophic cardiomyopathy.";
J. Mol. Biol. 384:896-907(2008).
[37]
VARIANTS CMH4 GLU-278; ARG-490; GLY-495; GLN-502; TRP-502; ASN-605;
SER-1028 AND ARG-1248, AND VARIANTS MET-158; GLY-236; GLN-326; MET-896
AND TRP-1002.
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).
[38]
VARIANTS CMD1MM ARG-490; THR-833 AND PHE-1264.
PubMed=20215591; DOI=10.1161/CIRCGENETICS.109.912345;
Hershberger R.E., Norton N., Morales A., Li D., Siegfried J.D.,
Gonzalez-Quintana J.;
"Coding sequence rare variants identified in MYBPC3, MYH6, TPM1,
TNNC1, and TNNI3 from 312 patients with familial or idiopathic dilated
cardiomyopathy.";
Circ. Cardiovasc. Genet. 3:155-161(2010).
[39]
VARIANTS LVNC10 ARG-490 AND LEU-873.
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).
[40]
VARIANT CMH4 VAL-490.
PubMed=23840593; DOI=10.1371/journal.pone.0067087;
Wang Y., Wang Z., Yang Q., Zou Y., Zhang H., Yan C., Feng X., Chen Y.,
Zhang Y., Wang J., Zhou X., Ahmad F., Hui R., Song L.;
"Autosomal recessive transmission of MYBPC3 mutation results in
malignant phenotype of hypertrophic cardiomyopathy.";
PLoS ONE 8:E67087-E67087(2013).
[41]
INVOLVEMENT IN RCM, AND VARIANT LYS-334.
PubMed=26163040; DOI=10.1161/JAHA.115.001879;
Wu W., Lu C.X., Wang Y.N., Liu F., Chen W., Liu Y.T., Han Y.C.,
Cao J., Zhang S.Y., Zhang X.;
"Novel phenotype-genotype correlations of restrictive cardiomyopathy
with myosin-binding protein C (MYBPC3) gene mutations tested by next-
generation sequencing.";
J. Am. Heart. Assoc. 4:0-0(2015).
-!- FUNCTION: Thick filament-associated protein located in the
crossbridge region of vertebrate striated muscle a bands. In vitro
it binds MHC, F-actin and native thin filaments, and modifies the
activity of actin-activated myosin ATPase. It may modulate muscle
contraction or may play a more structural role.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-704176, EBI-704176;
Q5VU43-11:PDE4DIP; NbExp=5; IntAct=EBI-704176, EBI-10769071;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q14896-1; Sequence=Displayed;
Name=2;
IsoId=Q14896-2; Sequence=VSP_047141;
-!- PTM: Substrate for phosphorylation by PKA and PKC. Reversible
phosphorylation appears to modulate contraction (By similarity).
{ECO:0000250}.
-!- PTM: Polyubiquitinated. {ECO:0000269|PubMed:18929575}.
-!- DISEASE: Cardiomyopathy, familial hypertrophic 4 (CMH4)
[MIM:115197]: 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:11499718, ECO:0000269|PubMed:11499719,
ECO:0000269|PubMed:11815426, ECO:0000269|PubMed:12379228,
ECO:0000269|PubMed:12628722, ECO:0000269|PubMed:12707239,
ECO:0000269|PubMed:12818575, ECO:0000269|PubMed:12951062,
ECO:0000269|PubMed:12974739, ECO:0000269|PubMed:14563344,
ECO:0000269|PubMed:15114369, ECO:0000269|PubMed:15519027,
ECO:0000269|PubMed:15563892, ECO:0000269|PubMed:16004897,
ECO:0000269|PubMed:16199542, ECO:0000269|PubMed:18403758,
ECO:0000269|PubMed:18929575, ECO:0000269|PubMed:18957093,
ECO:0000269|PubMed:23840593, ECO:0000269|PubMed:7744002,
ECO:0000269|PubMed:9048664, ECO:0000269|PubMed:9541104,
ECO:0000269|PubMed:9541115, ECO:0000269|PubMed:9562578}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Cardiomyopathy, dilated 1MM (CMD1MM) [MIM:615396]: 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:20215591}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Note=MYBPC3 mutations may be involved in restrictive
cardiomyopathy (RCM), a rare non-ischemic myocardial disease. RCM
is characterized by restrictive ventricular-filling physiology in
the presence of normal or reduced diastolic and/or systolic
volumes (of 1 or both ventricles), biatrial enlargement, and
normal ventricular wall thickness. {ECO:0000269|PubMed:26163040}.
-!- DISEASE: Left ventricular non-compaction 10 (LVNC10) [MIM:615396]:
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 immunoglobulin superfamily. MyBP
family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/mybpc3/";
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EMBL; X84075; CAA58882.1; -; mRNA.
EMBL; Y10129; CAA71216.1; -; Genomic_DNA.
EMBL; U91629; AAC04620.1; -; Genomic_DNA.
EMBL; AY518390; AAR89909.1; -; Genomic_DNA.
EMBL; GU324918; ADL14489.1; -; Genomic_DNA.
EMBL; AC090582; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC136543; AAI36544.1; -; mRNA.
EMBL; BC136546; AAI36547.1; -; mRNA.
EMBL; BC142685; AAI42686.1; -; mRNA.
EMBL; BC151211; AAI51212.1; -; mRNA.
EMBL; S80778; AAB35662.1; -; mRNA.
CCDS; CCDS53621.1; -. [Q14896-1]
PIR; S55050; S55050.
RefSeq; NP_000247.2; NM_000256.3. [Q14896-1]
UniGene; Hs.524906; -.
PDB; 1GXE; NMR; -; A=641-770.
PDB; 1PD6; NMR; -; A=358-451.
PDB; 2AVG; NMR; -; A=151-260.
PDB; 2K1M; NMR; -; A=2-96.
PDB; 2MQ0; NMR; -; A=453-543.
PDB; 2MQ3; NMR; -; A=453-543.
PDB; 2V6H; X-ray; 1.55 A; A=151-258.
PDB; 3CX2; X-ray; 1.30 A; A=151-258.
PDB; 5K6P; NMR; -; A=319-451.
PDBsum; 1GXE; -.
PDBsum; 1PD6; -.
PDBsum; 2AVG; -.
PDBsum; 2K1M; -.
PDBsum; 2MQ0; -.
PDBsum; 2MQ3; -.
PDBsum; 2V6H; -.
PDBsum; 3CX2; -.
PDBsum; 5K6P; -.
ProteinModelPortal; Q14896; -.
SMR; Q14896; -.
BioGrid; 110692; 10.
IntAct; Q14896; 14.
MINT; MINT-6174801; -.
STRING; 9606.ENSP00000442795; -.
iPTMnet; Q14896; -.
PhosphoSitePlus; Q14896; -.
BioMuta; MYBPC3; -.
DMDM; 425906074; -.
UCD-2DPAGE; Q14896; -.
PaxDb; Q14896; -.
PeptideAtlas; Q14896; -.
PRIDE; Q14896; -.
Ensembl; ENST00000545968; ENSP00000442795; ENSG00000134571. [Q14896-1]
GeneID; 4607; -.
KEGG; hsa:4607; -.
UCSC; uc058bdz.1; human. [Q14896-1]
CTD; 4607; -.
DisGeNET; 4607; -.
EuPathDB; HostDB:ENSG00000134571.10; -.
GeneCards; MYBPC3; -.
GeneReviews; MYBPC3; -.
HGNC; HGNC:7551; MYBPC3.
HPA; HPA040147; -.
HPA; HPA043898; -.
MalaCards; MYBPC3; -.
MIM; 115197; phenotype.
MIM; 600958; gene.
MIM; 615396; phenotype.
neXtProt; NX_Q14896; -.
OpenTargets; ENSG00000134571; -.
Orphanet; 154; Familial isolated dilated cardiomyopathy.
Orphanet; 155; Familial isolated hypertrophic cardiomyopathy.
Orphanet; 54260; Left ventricular noncompaction.
PharmGKB; PA31351; -.
eggNOG; ENOG410IFCI; Eukaryota.
eggNOG; ENOG4110AYI; LUCA.
GeneTree; ENSGT00860000133685; -.
HOGENOM; HOG000220906; -.
HOVERGEN; HBG052560; -.
InParanoid; Q14896; -.
KO; K12568; -.
OMA; RVFSHNM; -.
TreeFam; TF351819; -.
Reactome; R-HSA-390522; Striated Muscle Contraction.
SIGNOR; Q14896; -.
ChiTaRS; MYBPC3; human.
EvolutionaryTrace; Q14896; -.
GeneWiki; Myosin_binding_protein_C,_cardiac; -.
GenomeRNAi; 4607; -.
PRO; PR:Q14896; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000134571; -.
CleanEx; HS_MYBPC3; -.
ExpressionAtlas; Q14896; baseline and differential.
Genevisible; Q14896; HS.
GO; GO:0031672; C:A band; IDA:BHF-UCL.
GO; GO:0014705; C:C zone; NAS:BHF-UCL.
GO; GO:0097512; C:cardiac myofibril; IDA:CAFA.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0031430; C:M band; IBA:GO_Central.
GO; GO:0030017; C:sarcomere; IDA:BHF-UCL.
GO; GO:0005863; C:striated muscle myosin thick filament; IDA:BHF-UCL.
GO; GO:0030018; C:Z disc; IBA:GO_Central.
GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
GO; GO:0001671; F:ATPase activator activity; ISS:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0051371; F:muscle alpha-actinin binding; IBA:GO_Central.
GO; GO:0017022; F:myosin binding; IDA:BHF-UCL.
GO; GO:0032036; F:myosin heavy chain binding; IPI:BHF-UCL.
GO; GO:0008307; F:structural constituent of muscle; IMP:BHF-UCL.
GO; GO:0097493; F:structural molecule activity conferring elasticity; IBA:GO_Central.
GO; GO:0031432; F:titin binding; NAS:BHF-UCL.
GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
GO; GO:0060048; P:cardiac muscle contraction; ISS:BHF-UCL.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0003007; P:heart morphogenesis; IMP:BHF-UCL.
GO; GO:0030049; P:muscle filament sliding; TAS:Reactome.
GO; GO:0032781; P:positive regulation of ATPase activity; ISS:BHF-UCL.
GO; GO:0032971; P:regulation of muscle filament sliding; ISS:BHF-UCL.
GO; GO:0006942; P:regulation of striated muscle contraction; ISS:BHF-UCL.
GO; GO:0045214; P:sarcomere organization; IBA:GO_Central.
GO; GO:0006941; P:striated muscle contraction; IBA:GO_Central.
GO; GO:0071688; P:striated muscle myosin thick filament assembly; IBA:GO_Central.
GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IMP:HGNC.
CDD; cd00063; FN3; 3.
Gene3D; 2.60.40.10; -; 11.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
Pfam; PF00041; fn3; 3.
Pfam; PF07679; I-set; 8.
SMART; SM00060; FN3; 3.
SMART; SM00409; IG; 8.
SMART; SM00408; IGc2; 6.
SUPFAM; SSF48726; SSF48726; 8.
SUPFAM; SSF49265; SSF49265; 2.
PROSITE; PS50853; FN3; 3.
PROSITE; PS50835; IG_LIKE; 6.
1: Evidence at protein level;
3D-structure; Acetylation; Actin-binding; Alternative splicing;
Cardiomyopathy; Cell adhesion; Complete proteome; Disease mutation;
Disulfide bond; Immunoglobulin domain; Metal-binding; Methylation;
Muscle protein; Phosphoprotein; Polymorphism; Reference proteome;
Repeat; Thick filament; Ubl conjugation; Zinc.
CHAIN 1 1274 Myosin-binding protein C, cardiac-type.
/FTId=PRO_0000072693.
DOMAIN 153 256 Ig-like C2-type 1.
DOMAIN 362 452 Ig-like C2-type 2.
DOMAIN 453 543 Ig-like C2-type 3.
DOMAIN 544 633 Ig-like C2-type 4.
DOMAIN 645 771 Ig-like C2-type 5.
DOMAIN 774 870 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 872 967 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 971 1065 Ig-like C2-type 6.
DOMAIN 1068 1163 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1181 1274 Ig-like C2-type 7.
COMPBIAS 102 152 Pro-rich.
METAL 208 208 Zinc. {ECO:0000269|PubMed:18926831}.
METAL 210 210 Zinc. {ECO:0000269|PubMed:18926831}.
METAL 223 223 Zinc. {ECO:0000269|PubMed:18926831}.
METAL 225 225 Zinc. {ECO:0000269|PubMed:18926831}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:O70468}.
MOD_RES 47 47 Phosphoserine.
{ECO:0000250|UniProtKB:O70468}.
MOD_RES 275 275 Phosphoserine; by PKA and PKC.
{ECO:0000250|UniProtKB:O70468}.
MOD_RES 284 284 Phosphoserine; by PKA and PKC.
{ECO:0000250|UniProtKB:O70468}.
MOD_RES 304 304 Phosphoserine; by PKA and PKC.
{ECO:0000250|UniProtKB:O70468}.
MOD_RES 311 311 Phosphoserine.
{ECO:0000250|UniProtKB:O70468}.
MOD_RES 427 427 Phosphoserine.
{ECO:0000250|UniProtKB:O70468}.
MOD_RES 550 550 Phosphoserine.
{ECO:0000250|UniProtKB:O70468}.
MOD_RES 607 607 Phosphothreonine.
{ECO:0000250|UniProtKB:P56741}.
MOD_RES 1241 1241 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:O70468}.
DISULFID 436 443 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 408 409 SK -> R (in isoform 2). {ECO:0000305}.
/FTId=VSP_047141.
VARIANT 5 5 G -> R (in CMH4; dbSNP:rs201278114).
{ECO:0000269|PubMed:15519027}.
/FTId=VAR_029390.
VARIANT 59 59 T -> A (in CMH4; dbSNP:rs121909375).
{ECO:0000269|PubMed:11815426}.
/FTId=VAR_029391.
VARIANT 147 147 P -> L (in dbSNP:rs730880615).
{ECO:0000269|PubMed:12110947}.
/FTId=VAR_074538.
VARIANT 158 158 V -> M (in dbSNP:rs3729986).
{ECO:0000269|PubMed:15519027,
ECO:0000269|PubMed:18403758,
ECO:0000269|Ref.4}.
/FTId=VAR_020085.
VARIANT 161 161 P -> S (in CMH4).
{ECO:0000269|PubMed:14563344}.
/FTId=VAR_029392.
VARIANT 189 189 V -> I (in dbSNP:rs11570052).
{ECO:0000269|Ref.4}.
/FTId=VAR_020568.
VARIANT 219 219 V -> L (in CMH4; dbSNP:rs397516068).
{ECO:0000269|PubMed:15519027}.
/FTId=VAR_029393.
VARIANT 228 228 D -> N (in CMH4; dbSNP:rs369300885).
{ECO:0000269|PubMed:15114369}.
/FTId=VAR_029394.
VARIANT 236 236 S -> G (in dbSNP:rs3729989).
{ECO:0000269|PubMed:12110947,
ECO:0000269|PubMed:12379228,
ECO:0000269|PubMed:12974739,
ECO:0000269|PubMed:15519027,
ECO:0000269|PubMed:15582318,
ECO:0000269|PubMed:16004897,
ECO:0000269|PubMed:18403758,
ECO:0000269|PubMed:18929575,
ECO:0000269|Ref.4}.
/FTId=VAR_020086.
VARIANT 237 237 Y -> S (in CMH4; dbSNP:rs397516070).
{ECO:0000269|PubMed:12818575}.
/FTId=VAR_029395.
VARIANT 256 256 V -> I (in CMH4).
{ECO:0000269|PubMed:15519027}.
/FTId=VAR_029396.
VARIANT 257 257 H -> P (in CMH4).
{ECO:0000269|PubMed:12707239}.
/FTId=VAR_019889.
VARIANT 258 258 E -> K (in CMH4; dbSNP:rs397516074).
{ECO:0000269|PubMed:12707239,
ECO:0000269|PubMed:12951062,
ECO:0000269|PubMed:12974739,
ECO:0000269|PubMed:14563344,
ECO:0000269|PubMed:15114369,
ECO:0000269|PubMed:15519027,
ECO:0000269|PubMed:15563892,
ECO:0000269|PubMed:18957093}.
/FTId=VAR_019890.
VARIANT 263 263 G -> R (in CMH4; dbSNP:rs373730381).
{ECO:0000269|PubMed:15563892}.
/FTId=VAR_042740.
VARIANT 272 272 R -> C (in CMH4; dbSNP:rs397516075).
{ECO:0000269|PubMed:18957093}.
/FTId=VAR_070449.
VARIANT 273 273 R -> H (in CMH4; dbSNP:rs376461745).
{ECO:0000269|PubMed:16199542}.
/FTId=VAR_042741.
VARIANT 278 278 G -> E (in CMH4; dbSNP:rs147315081).
{ECO:0000269|PubMed:12707239,
ECO:0000269|PubMed:18403758}.
/FTId=VAR_019891.
VARIANT 279 279 G -> A (in CMH4; dbSNP:rs375774648).
{ECO:0000269|PubMed:12707239}.
/FTId=VAR_019892.
VARIANT 281 281 R -> Q (in dbSNP:rs11570060).
{ECO:0000269|Ref.4}.
/FTId=VAR_020569.
VARIANT 282 282 R -> W (in CMH4; dbSNP:rs727504234).
{ECO:0000269|PubMed:11499719,
ECO:0000269|PubMed:12974739}.
/FTId=VAR_029397.
VARIANT 326 326 R -> Q (in dbSNP:rs34580776).
{ECO:0000269|PubMed:11499718,
ECO:0000269|PubMed:11815426,
ECO:0000269|PubMed:12110947,
ECO:0000269|PubMed:12379228,
ECO:0000269|PubMed:12707239,
ECO:0000269|PubMed:12818575,
ECO:0000269|PubMed:12974739,
ECO:0000269|PubMed:15519027,
ECO:0000269|PubMed:16199542,
ECO:0000269|PubMed:18403758}.
/FTId=VAR_019893.
VARIANT 334 334 E -> K (in CMH4; also found in a patient
with RCM; decreases protein abundance;
increases polyubiquitination level;
accelerates the degradation process; no
effect on phosphorylation; decreases
endopeptidase activity; increases
apoptotic process; dbSNP:rs573916965).
{ECO:0000269|PubMed:18929575,
ECO:0000269|PubMed:26163040}.
/FTId=VAR_074539.
VARIANT 336 336 I -> V (in CMH4).
{ECO:0000269|PubMed:18957093}.
/FTId=VAR_070450.
VARIANT 342 342 V -> D (in CMH4; dbSNP:rs730880709).
{ECO:0000269|PubMed:16004897}.
/FTId=VAR_074540.
VARIANT 352 352 L -> P (in CMH4).
{ECO:0000269|PubMed:12707239}.
/FTId=VAR_019894.
VARIANT 382 382 R -> W (in dbSNP:rs11570076).
{ECO:0000269|PubMed:15519027,
ECO:0000269|Ref.4}.
/FTId=VAR_020570.
VARIANT 383 383 L -> V (in dbSNP:rs11570077).
{ECO:0000269|Ref.4}.
/FTId=VAR_020571.
VARIANT 416 416 G -> S (in dbSNP:rs371513491).
{ECO:0000269|PubMed:15519027}.
/FTId=VAR_029398.
VARIANT 417 417 A -> S (in CMH4).
{ECO:0000269|PubMed:15563892}.
/FTId=VAR_042742.
VARIANT 451 451 E -> Q (in CMH4).
{ECO:0000269|PubMed:9562578}.
/FTId=VAR_027879.
VARIANT 458 458 R -> H (in CMH4; dbSNP:rs374255707).
{ECO:0000269|PubMed:15519027}.
/FTId=VAR_029399.
VARIANT 490 490 G -> R (in CMH4, CMD1MM and LVNC10;
dbSNP:rs200625851).
{ECO:0000269|PubMed:15519027,
ECO:0000269|PubMed:18403758,
ECO:0000269|PubMed:20215591,
ECO:0000269|PubMed:21551322}.
/FTId=VAR_029400.
VARIANT 490 490 G -> V (in CMH4; dbSNP:rs397514752).
{ECO:0000269|PubMed:23840593}.
/FTId=VAR_070451.
VARIANT 495 495 R -> G (in CMH4; dbSNP:rs397515905).
{ECO:0000269|PubMed:18403758}.
/FTId=VAR_045929.
VARIANT 495 495 R -> Q (in CMH4; dbSNP:rs200411226).
{ECO:0000269|PubMed:11499718,
ECO:0000269|PubMed:15519027,
ECO:0000269|PubMed:18957093,
ECO:0000269|PubMed:9562578}.
/FTId=VAR_027880.
VARIANT 502 502 R -> Q (in CMH4; dbSNP:rs397515907).
{ECO:0000269|PubMed:18403758,
ECO:0000269|PubMed:18957093,
ECO:0000269|PubMed:9562578}.
/FTId=VAR_027881.
VARIANT 502 502 R -> W (in CMH4; dbSNP:rs375882485).
{ECO:0000269|PubMed:12707239,
ECO:0000269|PubMed:15519027,
ECO:0000269|PubMed:16199542,
ECO:0000269|PubMed:18403758}.
/FTId=VAR_019895.
VARIANT 504 504 Missing (in CMH4).
{ECO:0000269|PubMed:12707239}.
/FTId=VAR_019896.
VARIANT 507 507 G -> R (in CMH4; dbSNP:rs35736435).
{ECO:0000269|PubMed:11499719,
ECO:0000269|PubMed:12974739,
ECO:0000269|PubMed:15519027}.
/FTId=VAR_029401.
VARIANT 522 522 A -> T (in dbSNP:rs11570082).
{ECO:0000269|Ref.4}.
/FTId=VAR_020573.
VARIANT 523 523 G -> W (in CMH4).
{ECO:0000269|PubMed:12974739}.
/FTId=VAR_029402.
VARIANT 542 542 E -> Q (in CMH4; dbSNP:rs121909374).
{ECO:0000269|PubMed:12707239,
ECO:0000269|PubMed:15519027,
ECO:0000269|PubMed:16199542,
ECO:0000269|PubMed:9048664}.
/FTId=VAR_003917.
VARIANT 545 545 L -> M (in dbSNP:rs377163678).
{ECO:0000269|PubMed:15519027}.
/FTId=VAR_029403.
VARIANT 566 566 C -> R (in CMH4; dbSNP:rs730880695).
{ECO:0000269|PubMed:11499719,
ECO:0000269|PubMed:12974739}.
/FTId=VAR_029404.
VARIANT 604 604 D -> V (in CMH4).
{ECO:0000269|PubMed:15519027}.
/FTId=VAR_029405.
VARIANT 605 605 D -> N (in CMH4; unknown pathological
significance; dbSNP:rs376736293).
{ECO:0000269|PubMed:14563344,
ECO:0000269|PubMed:15519027,
ECO:0000269|PubMed:18403758}.
/FTId=VAR_029406.
VARIANT 608 608 P -> L (in CMH4).
{ECO:0000269|PubMed:15519027}.
/FTId=VAR_029407.
VARIANT 627 627 A -> V (in CMH4).
{ECO:0000269|PubMed:16004897}.
/FTId=VAR_074541.
VARIANT 654 654 R -> H (in CMH4; as well folded and
stable as the wild-type;
dbSNP:rs1800565).
{ECO:0000269|PubMed:12787675,
ECO:0000269|PubMed:9541115}.
/FTId=VAR_003918.
VARIANT 668 668 R -> H (in CMH4; dbSNP:rs727503191).
{ECO:0000269|PubMed:12818575}.
/FTId=VAR_029408.
VARIANT 668 668 R -> P (in CMH4).
{ECO:0000269|PubMed:12974739}.
/FTId=VAR_029409.
VARIANT 669 669 L -> H (in CMH4).
{ECO:0000269|PubMed:15563892}.
/FTId=VAR_042743.
VARIANT 733 733 R -> C (in CMH4; dbSNP:rs397515956).
{ECO:0000269|PubMed:15519027}.
/FTId=VAR_029410.
VARIANT 755 755 N -> K (in CMH4; destabilizes the
structure of Ig-like C2-type domain 5).
{ECO:0000269|PubMed:12787675,
ECO:0000269|PubMed:9541104}.
/FTId=VAR_003919.
VARIANT 759 759 E -> D (in CMH4).
{ECO:0000269|PubMed:15563892}.
/FTId=VAR_042744.
VARIANT 770 770 D -> N (in CMH4; dbSNP:rs36211723).
{ECO:0000269|PubMed:15519027}.
/FTId=VAR_029411.
VARIANT 771 771 V -> M (in CMH4; dbSNP:rs371488302).
{ECO:0000269|PubMed:16004897}.
/FTId=VAR_074542.
VARIANT 792 792 W -> R (in CMH4; dbSNP:rs187830361).
{ECO:0000269|PubMed:15519027}.
/FTId=VAR_029412.
VARIANT 810 810 R -> H (in CMH4; dbSNP:rs375675796).
{ECO:0000269|PubMed:12951062,
ECO:0000269|PubMed:15519027}.
/FTId=VAR_029413.
VARIANT 811 811 K -> R (in CMH4).
{ECO:0000269|PubMed:12707239}.
/FTId=VAR_019897.
VARIANT 811 811 Missing (in CMH4).
{ECO:0000269|PubMed:15519027}.
/FTId=VAR_029414.
VARIANT 813 813 Missing (in CMH4).
{ECO:0000269|PubMed:15114369}.
/FTId=VAR_029415.
VARIANT 814 814 Missing (in CMH4; no effect on protein
abundance; no effect on endopeptidase
activity). {ECO:0000269|PubMed:18929575}.
/FTId=VAR_074543.
VARIANT 820 820 R -> Q (in CMH4; dbSNP:rs2856655).
{ECO:0000269|PubMed:12628722,
ECO:0000269|PubMed:12951062,
ECO:0000269|PubMed:7744002,
ECO:0000269|PubMed:9048664}.
/FTId=VAR_029416.
VARIANT 833 833 A -> T (in CMH4 and CMD1MM;
dbSNP:rs199865688).
{ECO:0000269|PubMed:12818575,
ECO:0000269|PubMed:14563344,
ECO:0000269|PubMed:15114369,
ECO:0000269|PubMed:15519027,
ECO:0000269|PubMed:20215591}.
/FTId=VAR_029417.
VARIANT 833 833 A -> V (in CMH4; dbSNP:rs3729952).
{ECO:0000269|PubMed:12707239,
ECO:0000269|PubMed:12974739,
ECO:0000269|Ref.4}.
/FTId=VAR_019898.
VARIANT 834 834 R -> T (in CMH4).
/FTId=VAR_029418.
VARIANT 834 834 R -> W (in CMH4; unknown pathological
significance; dbSNP:rs752007810).
{ECO:0000269|PubMed:14563344}.
/FTId=VAR_029419.
VARIANT 873 873 P -> H (in CMH4; dbSNP:rs371401403).
{ECO:0000269|PubMed:12951062}.
/FTId=VAR_029420.
VARIANT 873 873 P -> L (in LVNC10; dbSNP:rs371401403).
{ECO:0000269|PubMed:21551322}.
/FTId=VAR_070452.
VARIANT 896 896 V -> M (may act as a phenotype modifier
in cardiomyopathy patients;
dbSNP:rs35078470).
{ECO:0000269|PubMed:10521296,
ECO:0000269|PubMed:12110947,
ECO:0000269|PubMed:12707239,
ECO:0000269|PubMed:12818575,
ECO:0000269|PubMed:15519027,
ECO:0000269|PubMed:18403758}.
/FTId=VAR_019899.
VARIANT 948 948 N -> T (in CMH4; dbSNP:rs121909376).
{ECO:0000269|PubMed:12379228}.
/FTId=VAR_029421.
VARIANT 957 957 T -> S (in CMH4; dbSNP:rs193922380).
{ECO:0000269|PubMed:18957093}.
/FTId=VAR_070453.
VARIANT 958 958 T -> I (in CMH4; dbSNP:rs376504548).
{ECO:0000269|PubMed:18957093}.
/FTId=VAR_070454.
VARIANT 998 998 Q -> E (in CMH4; no effect on protein
abundance; no effect on endopeptidase
activity; dbSNP:rs11570112).
{ECO:0000269|PubMed:15519027,
ECO:0000269|PubMed:18929575,
ECO:0000269|Ref.4}.
/FTId=VAR_020574.
VARIANT 998 998 Q -> R (in CMH4; dbSNP:rs727503177).
{ECO:0000269|PubMed:15519027}.
/FTId=VAR_029422.
VARIANT 1002 1002 R -> Q (in CMH4; dbSNP:rs727504235).
{ECO:0000269|PubMed:11815426}.
/FTId=VAR_029423.
VARIANT 1002 1002 R -> W (in dbSNP:rs3729799).
{ECO:0000269|PubMed:18403758}.
/FTId=VAR_029424.
VARIANT 1003 1003 P -> Q (in CMH4).
/FTId=VAR_029425.
VARIANT 1028 1028 T -> S (in CMH4; dbSNP:rs397516002).
{ECO:0000269|PubMed:18403758}.
/FTId=VAR_045930.
VARIANT 1046 1046 T -> M (in CMH4; no effect on protein
abundance; no effect on endopeptidase
activity; dbSNP:rs371061770).
{ECO:0000269|PubMed:18929575}.
/FTId=VAR_074544.
VARIANT 1048 1048 R -> C (in dbSNP:rs11570113).
{ECO:0000269|Ref.4}.
/FTId=VAR_020575.
VARIANT 1113 1113 F -> I (in CMH4).
{ECO:0000269|PubMed:15519027}.
/FTId=VAR_029426.
VARIANT 1115 1115 V -> I (in CMH4; dbSNP:rs531189495).
{ECO:0000269|PubMed:11499719,
ECO:0000269|PubMed:12974739}.
/FTId=VAR_029427.
VARIANT 1131 1131 I -> T (in CMH4; unknown pathological
significance; dbSNP:rs370890951).
{ECO:0000269|PubMed:14563344,
ECO:0000269|PubMed:15519027}.
/FTId=VAR_029428.
VARIANT 1138 1138 R -> H (in dbSNP:rs187705120).
{ECO:0000269|PubMed:12110947}.
/FTId=VAR_074545.
VARIANT 1155 1155 Missing (in CMH4).
/FTId=VAR_029429.
VARIANT 1194 1194 A -> T (in CMH4; dbSNP:rs397516026).
{ECO:0000269|PubMed:12707239}.
/FTId=VAR_019900.
VARIANT 1248 1248 G -> R (in CMH4; dbSNP:rs202147520).
{ECO:0000269|PubMed:18403758}.
/FTId=VAR_045931.
VARIANT 1255 1255 A -> T (in CMH4; dbSNP:rs727503167).
{ECO:0000269|PubMed:12707239}.
/FTId=VAR_019901.
VARIANT 1264 1264 C -> F (in CMD1MM; dbSNP:rs397514751).
{ECO:0000269|PubMed:20215591}.
/FTId=VAR_070455.
CONFLICT 248 248 D -> E (in Ref. 1 and 2). {ECO:0000305}.
CONFLICT 302 303 RD -> SS (in Ref. 4; AAR89909).
{ECO:0000305}.
CONFLICT 536 536 A -> R (in Ref. 1; CAA58882).
{ECO:0000305}.
STRAND 19 22 {ECO:0000244|PDB:2K1M}.
STRAND 27 32 {ECO:0000244|PDB:2K1M}.
STRAND 34 37 {ECO:0000244|PDB:2K1M}.
STRAND 41 43 {ECO:0000244|PDB:2K1M}.
STRAND 45 49 {ECO:0000244|PDB:2K1M}.
STRAND 56 60 {ECO:0000244|PDB:2K1M}.
STRAND 63 70 {ECO:0000244|PDB:2K1M}.
STRAND 77 83 {ECO:0000244|PDB:2K1M}.
STRAND 86 95 {ECO:0000244|PDB:2K1M}.
STRAND 156 159 {ECO:0000244|PDB:2AVG}.
STRAND 164 167 {ECO:0000244|PDB:3CX2}.
STRAND 172 179 {ECO:0000244|PDB:3CX2}.
STRAND 184 186 {ECO:0000244|PDB:2AVG}.
STRAND 188 193 {ECO:0000244|PDB:3CX2}.
TURN 194 196 {ECO:0000244|PDB:3CX2}.
HELIX 199 202 {ECO:0000244|PDB:3CX2}.
STRAND 207 214 {ECO:0000244|PDB:3CX2}.
TURN 215 218 {ECO:0000244|PDB:3CX2}.
STRAND 219 226 {ECO:0000244|PDB:3CX2}.
HELIX 231 233 {ECO:0000244|PDB:3CX2}.
STRAND 235 242 {ECO:0000244|PDB:3CX2}.
STRAND 247 257 {ECO:0000244|PDB:3CX2}.
HELIX 321 326 {ECO:0000244|PDB:5K6P}.
HELIX 330 332 {ECO:0000244|PDB:5K6P}.
HELIX 333 339 {ECO:0000244|PDB:5K6P}.
HELIX 345 355 {ECO:0000244|PDB:5K6P}.
STRAND 366 368 {ECO:0000244|PDB:1PD6}.
STRAND 371 376 {ECO:0000244|PDB:1PD6}.
STRAND 381 386 {ECO:0000244|PDB:1PD6}.
STRAND 388 392 {ECO:0000244|PDB:1PD6}.
STRAND 395 403 {ECO:0000244|PDB:1PD6}.
STRAND 407 415 {ECO:0000244|PDB:1PD6}.
STRAND 418 423 {ECO:0000244|PDB:1PD6}.
STRAND 427 430 {ECO:0000244|PDB:1PD6}.
STRAND 432 438 {ECO:0000244|PDB:1PD6}.
STRAND 441 443 {ECO:0000244|PDB:1PD6}.
STRAND 446 450 {ECO:0000244|PDB:1PD6}.
STRAND 456 458 {ECO:0000244|PDB:2MQ0}.
STRAND 465 467 {ECO:0000244|PDB:2MQ0}.
STRAND 471 474 {ECO:0000244|PDB:2MQ3}.
STRAND 475 479 {ECO:0000244|PDB:2MQ0}.
STRAND 486 488 {ECO:0000244|PDB:2MQ0}.
STRAND 499 506 {ECO:0000244|PDB:2MQ0}.
STRAND 509 517 {ECO:0000244|PDB:2MQ0}.
TURN 519 521 {ECO:0000244|PDB:2MQ3}.
STRAND 524 528 {ECO:0000244|PDB:2MQ0}.
STRAND 533 537 {ECO:0000244|PDB:2MQ0}.
STRAND 650 652 {ECO:0000244|PDB:1GXE}.
STRAND 658 665 {ECO:0000244|PDB:1GXE}.
STRAND 670 672 {ECO:0000244|PDB:1GXE}.
STRAND 675 677 {ECO:0000244|PDB:1GXE}.
STRAND 680 686 {ECO:0000244|PDB:1GXE}.
STRAND 722 724 {ECO:0000244|PDB:1GXE}.
STRAND 726 730 {ECO:0000244|PDB:1GXE}.
STRAND 733 737 {ECO:0000244|PDB:1GXE}.
TURN 743 745 {ECO:0000244|PDB:1GXE}.
STRAND 747 754 {ECO:0000244|PDB:1GXE}.
STRAND 759 768 {ECO:0000244|PDB:1GXE}.
SEQUENCE 1274 AA; 140762 MW; 4E5385C40085B796 CRC64;
MPEPGKKPVS AFSKKPRSVE VAAGSPAVFE AETERAGVKV RWQRGGSDIS ASNKYGLATE
GTRHTLTVRE VGPADQGSYA VIAGSSKVKF DLKVIEAEKA EPMLAPAPAP AEATGAPGEA
PAPAAELGES APSPKGSSSA ALNGPTPGAP DDPIGLFVMR PQDGEVTVGG SITFSARVAG
ASLLKPPVVK WFKGKWVDLS SKVGQHLQLH DSYDRASKVY LFELHITDAQ PAFTGSYRCE
VSTKDKFDCS NFNLTVHEAM GTGDLDLLSA FRRTSLAGGG RRISDSHEDT GILDFSSLLK
KRDSFRTPRD SKLEAPAEED VWEILRQAPP SEYERIAFQY GVTDLRGMLK RLKGMRRDEK
KSTAFQKKLE PAYQVSKGHK IRLTVELADH DAEVKWLKNG QEIQMSGSKY IFESIGAKRT
LTISQCSLAD DAAYQCVVGG EKCSTELFVK EPPVLITRPL EDQLVMVGQR VEFECEVSEE
GAQVKWLKDG VELTREETFK YRFKKDGQRH HLIINEAMLE DAGHYALCTS GGQALAELIV
QEKKLEVYQS IADLMVGAKD QAVFKCEVSD ENVRGVWLKN GKELVPDSRI KVSHIGRVHK
LTIDDVTPAD EADYSFVPEG FACNLSAKLH FMEVKIDFVP RQEPPKIHLD CPGRIPDTIV
VVAGNKLRLD VPISGDPAPT VIWQKAITQG NKAPARPAPD APEDTGDSDE WVFDKKLLCE
TEGRVRVETT KDRSIFTVEG AEKEDEGVYT VTVKNPVGED QVNLTVKVID VPDAPAAPKI
SNVGEDSCTV QWEPPAYDGG QPILGYILER KKKKSYRWMR LNFDLIQELS HEARRMIEGV
VYEMRVYAVN AIGMSRPSPA SQPFMPIGPP SEPTHLAVED VSDTTVSLKW RPPERVGAGG
LDGYSVEYCP EGCSEWVAAL QGLTEHTSIL VKDLPTGARL LFRVRAHNMA GPGAPVTTTE
PVTVQEILQR PRLQLPRHLR QTIQKKVGEP VNLLIPFQGK PRPQVTWTKE GQPLAGEEVS
IRNSPTDTIL FIRAARRVHS GTYQVTVRIE NMEDKATLVL QVVDKPSPPQ DLRVTDAWGL
NVALEWKPPQ DVGNTELWGY TVQKADKKTM EWFTVLEHYR RTHCVVPELI IGNGYYFRVF
SQNMVGFSDR AATTKEPVFI PRPGITYEPP NYKALDFSEA PSFTQPLVNR SVIAGYTAML
CCAVRGSPKP KISWFKNGLD LGEDARFRMF SKQGVLTLEI RKPCPFDGGI YVCRATNLQG
EARCECRLEV RVPQ


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