[1]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT CMH4 GLN-819. TISSUE=Heart; PubMed=7744002 [NCBI, ExPASy, EBI, Israel, Japan] 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-541 AND GLN-819. PubMed=9048664 [NCBI, ExPASy, EBI, Israel, Japan] 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-450; GLN-494 AND GLN-501. DOI=10.1056/NEJM199804303381802; PubMed=9562578 [NCBI, ExPASy, EBI, Israel, Japan] 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-521; VAL-832; GLU-997 AND CYS-1047. NIEHS SNPs program; Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [MRNA] OF 639-693. DOI=10.1038/ng1295-438; PubMed=7493026 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[6]	STRUCTURE BY NMR OF 640-769, AND CHARACTERIZATION OF VARIANTS HIS-653 AND LYS-754. DOI=10.1016/S0022-2836(03)00425-X; PubMed=12787675 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[7]	STRUCTURE BY NMR OF 357-450. DOI=10.1023/B:JNMR.0000032510.03606.63; PubMed=15213454 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[8]	VARIANT CMH4 LYS-754. PubMed=9541104 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[9]	VARIANT CMH4 HIS-653. PubMed=9541115 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[10]	VARIANT MET-895. DOI=10.1086/302623; PubMed=10521296 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[11]	VARIANT CMH4 GLN-494, AND VARIANT GLN-326. DOI=10.1016/S0735-1097(01)01386-9; PubMed=11499718 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[12]	VARIANTS CMH4 TRP-282; ARG-506; ARG-565 AND ILE-1114. DOI=10.1016/S0735-1097(01)01387-0; PubMed=11499719 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[13]	VARIANT CMH4 THR-947, AND VARIANTS GLY-236 AND GLN-326. DOI=10.1016/S0006-291X(02)02374-4; PubMed=12379228 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[14]	VARIANTS CMH4 ALA-59 AND GLN-1001, AND VARIANT GLN-326. DOI=10.1161/hc0402.102990; PubMed=11815426 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[15]	VARIANTS CMH4 LYS-258; HIS-809; GLN-819 AND HIS-872. DOI=10.1016/j.bbrc.2003.08.014; PubMed=12951062 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[16]	VARIANTS CMH4 PRO-257; LYS-258; GLU-278; ALA-279; PRO-352; TRP-501; LYS-503 DEL; GLN-541; ARG-810; VAL-832; THR-1193 AND THR-1254, AND VARIANTS GLN-326 AND MET-895. DOI=10.1161/01.CIR.0000066323.15244.54; PubMed=12707239 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[17]	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).
[18]	VARIANTS CMH4 LYS-258; TRP-282; ARG-506; TRP-522; ARG-565; PRO-667; VAL-832 AND ILE-1114, AND VARIANTS GLY-236 AND GLN-326. DOI=10.1034/j.1399-0004.2003.00151.x; PubMed=12974739 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[19]	VARIANTS CMH4 SER-161; LYS-258; ASN-604; THR-832; TRP-833 AND THR-1130. DOI=10.1016/S0195-668X(03)00466-4; PubMed=14563344 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[20]	VARIANT CMH4 GLN-819. DOI=10.1016/S0735-1097(02)02957-1; PubMed=12628722 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[21]	VARIANTS CMH4 SER-237; HIS-667 AND THR-832, AND VARIANTS GLN-326 AND MET-895. DOI=10.1016/S0022-2828(03)00146-9; PubMed=12818575 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[22]	VARIANTS CMH4 ASN-228; LYS-258; LYS-812 DEL AND THR-832. DOI=10.1038/sj.ejhg.5201190; PubMed=15114369 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[23]	VARIANTS CMH4 ARG-5; LEU-219; ILE-256; LYS-258; HIS-457; ARG-489; GLN-494; TRP-501; GLN-541; VAL-603; ASN-604; LEU-607; CYS-732; ASN-769; ARG-791; HIS-809; LYS-810 DEL; THR-832; GLU-997; ARG-997; ILE-1112 AND THR-1130, AND VARIANTS MET-158; GLY-236; GLN-326; TRP-382; SER-415; ARG-506; MET-544 AND MET-895. DOI=10.1016/j.jacc.2004.07.045; PubMed=15519027 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[24]	VARIANT GLY-236. DOI=10.1016/j.jacc.2004.08.058; PubMed=15582318 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[25]	VARIANTS CMH4 LYS-258; ARG-263; SER-416; HIS-668 AND ASP-758. DOI=10.1016/j.cccn.2004.09.016; PubMed=15563892 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[26]	VARIANTS CMH4 HIS-273; TRP-501 AND GLN-541, AND VARIANT GLN-326. DOI=10.1136/jmg.2005.033886; PubMed=16199542 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[27]	VARIANTS CMH4 GLU-278; ARG-489; GLY-494; GLN-501; TRP-501; ASN-604; SER-1027 AND ARG-1247, AND VARIANTS MET-158; GLY-236; GLN-326; MET-895 AND TRP-1001. DOI=10.1056/NEJMoa075463; PubMed=18403758 [NCBI, ExPASy, EBI, Israel, Japan] 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).

Comments

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.
PTM: Substrate for phosphorylation by PKA and PKC. Reversible phosphorylation appears to modulate contraction (By similarity).
DISEASE: Defects in MYBPC3 are the cause of cardiomyopathy familial hypertrophic type 4 (CMH4) [MIM:115197]. Familial hypertrophic cardiomyopathy is 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.
SIMILARITY: Belongs to the immunoglobulin superfamily. MyBP family.
SIMILARITY: Contains 3 fibronectin type-III domains.
SIMILARITY: Contains 7 Ig-like C2-type (immunoglobulin-like) domains.
WEB RESOURCE: Name=Familial hypertrophic cardiomyopathy mutation database; URL="http://www.angis.org.au/Databases/Heart/heartbreak.html";.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=MYBPC3";.
WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/mybpc3/";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X84075; CAA58882.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Y10129; CAA71216.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U91629; AAC04620.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY518390; AAR89909.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S80778; AAB35662.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00798035; -.

S55050; S55050.

3D structure databases

PDB

1GXE; NMR; -; A=640-769.	[ExPASy / RCSB / EBI]
1PD6; NMR; -; A=358-450.	[ExPASy / RCSB / EBI]
2AVG; NMR; -; A=151-260.	[ExPASy / RCSB / EBI]
2K1M; NMR; -; A=2-96.	[ExPASy / RCSB / EBI]
2V6H; X-ray; 1.55 A; A=151-258.	[ExPASy / RCSB / EBI]
3CX2; X-ray; 1.30 A; A=151-258.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1GXE; -.
1PD6; -.
2AVG; -.
2K1M; -.
2V6H; -.
3CX2; -.

ModBase

Q14896.

Protein-protein interaction databases

IntAct

Q14896; 1.

PTM databases

PhosphoSite

Q14896; -.

Organism-specific databases

GC11M047309; -.

HGNC:7551; MYBPC3.

115197; phenotype. [NCBI / EBI]
600958; gene. [NCBI / EBI]

Orphanet

155; Cardiomyopathy, hypertrophic, primary or idiopathic.

PharmGKB

PA31351; -.

Gene expression databases

Q14896; -.

Q14896; -.

HS_MYBPC3; -.

ENSG00000134571; Homo sapiens.

Ontologies

GO:0014705;	Cellular component: C zone (non-traceable author statement from UniProtKB).
GO:0005863;	Cellular component: striated muscle thick filament (inferred from direct assay from UniProtKB).
GO:0003779;	Molecular function: actin binding (inferred from electronic annotation from UniProtKB-KW).
GO:0001671;	Molecular function: ATPase activator activity (inferred from sequence or structural similarity from UniProtKB).
GO:0032036;	Molecular function: myosin heavy chain binding (inferred from physical interaction from UniProtKB).
GO:0008307;	Molecular function: structural constituent of muscle (inferred from mutant phenotype from UniProtKB).
GO:0031432;	Molecular function: titin binding (non-traceable author statement from UniProtKB).
GO:0060048;	Biological process: cardiac muscle contraction (inferred from sequence or structural similarity from UniProtKB).
GO:0007155;	Biological process: cell adhesion (inferred from electronic annotation from UniProtKB-KW).
GO:0032781;	Biological process: positive regulation of ATPase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0032971;	Biological process: regulation of muscle filament sliding (inferred from sequence or structural similarity from UniProtKB).
GO:0006942;	Biological process: regulation of striated muscle contraction (inferred from sequence or structural similarity from UniProtKB).
GO:0055010;	Biological process: ventricular cardiac muscle morphogenesis (inferred from mutant phenotype from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR008957; Fibronectin_typ-III-like_fold.
IPR003961; FN_III.
IPR013151; Ig.
IPR007110; Ig-like.
IPR013783; Ig-like_fold.
IPR013098; Ig_I-set.
IPR003599; Ig_sub.
IPR003598; Ig_sub2.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.40.30; FN_III-like; 2.
G3DSA:2.60.40.10; Ig-like_fold; 8.

Pfam

PF00041; fn3; 3.
PF07679; I-set; 7.
PF00047; ig; 1.
Pfam graphical view of domain structure.

SMART

SM00060; FN3; 3.
SM00409; IG; 7.
SM00408; IGc2; 1.
SMART graphical view of domain structure.

PROSITE

PS50853; FN3; 3.
PS50835; IG_LIKE; 6.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

Q14896; -.

Genome annotation databases

Ensembl

ENSG00000134571; Homo sapiens. [Contig view]

Phylogenomic databases

HOGENOM

Q14896; -.

HOVERGEN

Q14896; -.

Other

SOURCE

MYBPC3; Homo sapiens.

ProtoNet

Q14896.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Actin-binding; Cardiomyopathy; Cell adhesion; Disease mutation; Immunoglobulin domain; Muscle protein; Phosphoprotein; Polymorphism; Repeat; Thick filament.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 1273`	`1273`	`Myosin-binding protein C, cardiac-type.`	`PRO_0000072693`
`DOMAIN`	`153 256`	`104`	`Ig-like C2-type 1.`
`DOMAIN`	`362 451`	`90`	`Ig-like C2-type 2.`
`DOMAIN`	`452 542`	`91`	`Ig-like C2-type 3.`
`DOMAIN`	`543 632`	`90`	`Ig-like C2-type 4.`
`DOMAIN`	`644 770`	`127`	`Ig-like C2-type 5.`
`DOMAIN`	`771 863`	`93`	`Fibronectin type-III 1.`
`DOMAIN`	`868 961`	`94`	`Fibronectin type-III 2.`
`DOMAIN`	`970 1064`	`95`	`Ig-like C2-type 6.`
`DOMAIN`	`1065 1157`	`93`	`Fibronectin type-III 3.`
`DOMAIN`	`1180 1273`	`94`	`Ig-like C2-type 7.`
`COMPBIAS`	`102 152`	`51`	`Pro-rich.`
`MOD_RES`	`275 275`		`Phosphoserine; by PKA and PKC (By similarity).`
`MOD_RES`	`284 284`		`Phosphoserine; by PKA and PKC (By similarity).`
`MOD_RES`	`304 304`		`Phosphoserine; by PKA and PKC (By similarity).`
`VARIANT`	`5 5`	`1`	`G -> R (in CMH4).`	`VAR_029390`
`VARIANT`	`59 59`	`1`	`T -> A (in CMH4).`	`VAR_029391`
`VARIANT`	`158 158`	`1`	`V -> M (in dbSNP:rs3729986 [NCBI]).`	`VAR_020085`
`VARIANT`	`161 161`	`1`	`P -> S (in CMH4).`	`VAR_029392`
`VARIANT`	`189 189`	`1`	`V -> I (in dbSNP:rs11570052 [NCBI]).`	`VAR_020568`
`VARIANT`	`219 219`	`1`	`V -> L (in CMH4).`	`VAR_029393`
`VARIANT`	`228 228`	`1`	`D -> N (in CMH4).`	`VAR_029394`
`VARIANT`	`236 236`	`1`	`S -> G (in dbSNP:rs3729989 [NCBI]).`	`VAR_020086`
`VARIANT`	`237 237`	`1`	`Y -> S (in CMH4).`	`VAR_029395`
`VARIANT`	`256 256`	`1`	`V -> I (in CMH4).`	`VAR_029396`
`VARIANT`	`257 257`	`1`	`H -> P (in CMH4).`	`VAR_019889`
`VARIANT`	`258 258`	`1`	`E -> K (in CMH4).`	`VAR_019890`
`VARIANT`	`263 263`	`1`	`G -> R (in CMH4).`	`VAR_042740`
`VARIANT`	`273 273`	`1`	`R -> H (in CMH4).`	`VAR_042741`
`VARIANT`	`278 278`	`1`	`G -> E (in CMH4).`	`VAR_019891`
`VARIANT`	`279 279`	`1`	`G -> A (in CMH4).`	`VAR_019892`
`VARIANT`	`281 281`	`1`	`R -> Q (in dbSNP:rs11570060 [NCBI]).`	`VAR_020569`
`VARIANT`	`282 282`	`1`	`R -> W (in CMH4).`	`VAR_029397`
`VARIANT`	`326 326`	`1`	`R -> Q (in dbSNP:rs34580776 [NCBI]).`	`VAR_019893`
`VARIANT`	`352 352`	`1`	`L -> P (in CMH4).`	`VAR_019894`
`VARIANT`	`382 382`	`1`	`R -> W (in dbSNP:rs11570076 [NCBI]).`	`VAR_020570`
`VARIANT`	`383 383`	`1`	`L -> V (in dbSNP:rs11570077 [NCBI]).`	`VAR_020571`
`VARIANT`	`415 415`	`1`	`G -> S.`	`VAR_029398`
`VARIANT`	`416 416`	`1`	`A -> S (in CMH4).`	`VAR_042742`
`VARIANT`	`450 450`	`1`	`E -> Q (in CMH4).`	`VAR_027879`
`VARIANT`	`457 457`	`1`	`R -> H (in CMH4).`	`VAR_029399`
`VARIANT`	`489 489`	`1`	`G -> R (in CMH4).`	`VAR_029400`
`VARIANT`	`494 494`	`1`	`R -> G (in CMH4).`	`VAR_045929`
`VARIANT`	`494 494`	`1`	`R -> Q (in CMH4).`	`VAR_027880`
`VARIANT`	`501 501`	`1`	`R -> Q (in CMH4).`	`VAR_027881`
`VARIANT`	`501 501`	`1`	`R -> W (in CMH4).`	`VAR_019895`
`VARIANT`	`503 503`	`1`	`Missing (in CMH4).`	`VAR_019896`
`VARIANT`	`506 506`	`1`	`G -> R (in CMH4).`	`VAR_029401`
`VARIANT`	`521 521`	`1`	`A -> T (in dbSNP:rs11570082 [NCBI]).`	`VAR_020573`
`VARIANT`	`522 522`	`1`	`G -> W (in CMH4).`	`VAR_029402`
`VARIANT`	`541 541`	`1`	`E -> Q (in CMH4).`	`VAR_003917`
`VARIANT`	`544 544`	`1`	`L -> M.`	`VAR_029403`
`VARIANT`	`565 565`	`1`	`C -> R (in CMH4).`	`VAR_029404`
`VARIANT`	`603 603`	`1`	`D -> V (in CMH4).`	`VAR_029405`
`VARIANT`	`604 604`	`1`	`D -> N (in CMH4; pathogenicity remains to be determined).`	`VAR_029406`
`VARIANT`	`607 607`	`1`	`P -> L (in CMH4).`	`VAR_029407`
`VARIANT`	`653 653`	`1`	`R -> H (in CMH4; as well folded and stable as the wild-type; dbSNP:rs1800565 [NCBI]).`	`VAR_003918`
`VARIANT`	`667 667`	`1`	`R -> H (in CMH4).`	`VAR_029408`
`VARIANT`	`667 667`	`1`	`R -> P (in CMH4).`	`VAR_029409`
`VARIANT`	`668 668`	`1`	`L -> H (in CMH4).`	`VAR_042743`
`VARIANT`	`732 732`	`1`	`R -> C (in CMH4).`	`VAR_029410`
`VARIANT`	`754 754`	`1`	`N -> K (in CMH4; destabilizes the structure of Ig-like C2-type domain 5).`	`VAR_003919`
`VARIANT`	`758 758`	`1`	`E -> D (in CMH4).`	`VAR_042744`
`VARIANT`	`769 769`	`1`	`D -> N (in CMH4).`	`VAR_029411`
`VARIANT`	`791 791`	`1`	`W -> R (in CMH4).`	`VAR_029412`
`VARIANT`	`809 809`	`1`	`R -> H (in CMH4).`	`VAR_029413`
`VARIANT`	`810 810`	`1`	`K -> R (in CMH4).`	`VAR_019897`
`VARIANT`	`810 810`	`1`	`Missing (in CMH4).`	`VAR_029414`
`VARIANT`	`812 812`	`1`	`Missing (in CMH4).`	`VAR_029415`
`VARIANT`	`819 819`	`1`	`R -> Q (in CMH4; dbSNP:rs2856655 [NCBI]).`	`VAR_029416`
`VARIANT`	`832 832`	`1`	`A -> T (in CMH4; pathogenicity is uncertain).`	`VAR_029417`
`VARIANT`	`832 832`	`1`	`A -> V (in CMH4; dbSNP:rs3729952 [NCBI]).`	`VAR_019898`
`VARIANT`	`833 833`	`1`	`R -> T (in CMH4).`	`VAR_029418`
`VARIANT`	`833 833`	`1`	`R -> W (in CMH4; pathogenicity is uncertain).`	`VAR_029419`
`VARIANT`	`872 872`	`1`	`P -> H (in CMH4).`	`VAR_029420`
`VARIANT`	`895 895`	`1`	`V -> M (may act as a phenotype modifier in cardiomyopathy patients; dbSNP:rs35078470 [NCBI]).`	`VAR_019899`
`VARIANT`	`947 947`	`1`	`N -> T (in CMH4).`	`VAR_029421`
`VARIANT`	`997 997`	`1`	`Q -> E (in CMH4; dbNP:11570112).`	`VAR_020574`
`VARIANT`	`997 997`	`1`	`Q -> R (in CMH4).`	`VAR_029422`
`VARIANT`	`1001 1001`	`1`	`R -> Q (in CMH4).`	`VAR_029423`
`VARIANT`	`1001 1001`	`1`	`R -> W (in dbSNP:rs3729799 [NCBI]).`	`VAR_029424`
`VARIANT`	`1002 1002`	`1`	`P -> Q (in CMH4).`	`VAR_029425`
`VARIANT`	`1027 1027`	`1`	`T -> S (in CMH4).`	`VAR_045930`
`VARIANT`	`1047 1047`	`1`	`R -> C (in dbSNP:rs11570113 [NCBI]).`	`VAR_020575`
`VARIANT`	`1112 1112`	`1`	`F -> I (in CMH4).`	`VAR_029426`
`VARIANT`	`1114 1114`	`1`	`V -> I (in CMH4).`	`VAR_029427`
`VARIANT`	`1130 1130`	`1`	`I -> T (in CMH4; pathogenicity is uncertain).`	`VAR_029428`
`VARIANT`	`1154 1154`	`1`	`Missing (in CMH4).`	`VAR_029429`
`VARIANT`	`1193 1193`	`1`	`A -> T (in CMH4).`	`VAR_019900`
`VARIANT`	`1247 1247`	`1`	`G -> R (in CMH4).`	`VAR_045931`
`VARIANT`	`1254 1254`	`1`	`A -> T (in CMH4).`	`VAR_019901`
`CONFLICT`	`248 248`		`D -> E (in Ref. 1 and 2).`
`CONFLICT`	`302 303`		`SS -> RD (in Ref. 1; CAA58882, 2; CAA71216 and 3; AAC04620).`
`CONFLICT`	`408 408`		`R -> SK (in Ref. 1; CAA58882, 2; CAA71216 and 3; AAC04620).`
`CONFLICT`	`535 535`		`A -> R (in Ref. 1; CAA58882).`
`STRAND`	`164 167`	`4`
`STRAND`	`172 179`	`8`
`STRAND`	`188 193`	`6`
`TURN`	`194 196`	`3`
`HELIX`	`199 202`	`4`
`STRAND`	`207 214`	`8`
`TURN`	`215 218`	`4`
`STRAND`	`219 226`	`8`
`HELIX`	`231 233`	`3`
`STRAND`	`235 242`	`8`
`STRAND`	`247 257`	`11`
`STRAND`	`649 651`	`3`
`STRAND`	`657 664`	`8`
`STRAND`	`669 671`	`3`
`STRAND`	`674 676`	`3`
`STRAND`	`679 685`	`7`
`STRAND`	`721 723`	`3`
`STRAND`	`725 729`	`5`
`STRAND`	`732 736`	`5`
`TURN`	`742 744`	`3`
`STRAND`	`746 753`	`8`
`STRAND`	`758 767`	`10`

Sequence information

Length: 1273 AA [This is the length of the unprocessed precursor]

Molecular weight: 140606 Da [This is the MW of the unprocessed precursor]

CRC64: 77744F1FC63F5F7A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPEPGKKPVS AFSKKPRSVE VAAGSPAVFE AETERAGVKV RWQRGGSDIS ASNKYGLATE 

        70         80         90        100        110        120 
GTRHTLTVRE VGPADQGSYA VIAGSSKVKF DLKVIEAEKA EPMLAPAPAP AEATGAPGEA 

       130        140        150        160        170        180 
PAPAAELGES APSPKGSSSA ALNGPTPGAP DDPIGLFVMR PQDGEVTVGG SITFSARVAG 

       190        200        210        220        230        240 
ASLLKPPVVK WFKGKWVDLS SKVGQHLQLH DSYDRASKVY LFELHITDAQ PAFTGSYRCE 

       250        260        270        280        290        300 
VSTKDKFDCS NFNLTVHEAM GTGDLDLLSA FRRTSLAGGG RRISDSHEDT GILDFSSLLK 

       310        320        330        340        350        360 
KSSSFRTPRD SKLEAPAEED VWEILRQAPP SEYERIAFQY GVTDLRGMLK RLKGMRRDEK 

       370        380        390        400        410        420 
KSTAFQKKLE PAYQVSKGHK IRLTVELADH DAEVKWLKNG QEIQMSGRYI FESIGAKRTL 

       430        440        450        460        470        480 
TISQCSLADD AAYQCVVGGE KCSTELFVKE PPVLITRPLE DQLVMVGQRV EFECEVSEEG 

       490        500        510        520        530        540 
AQVKWLKDGV ELTREETFKY RFKKDGQRHH LIINEAMLED AGHYALCTSG GQALAELIVQ 

       550        560        570        580        590        600 
EKKLEVYQSI ADLMVGAKDQ AVFKCEVSDE NVRGVWLKNG KELVPDSRIK VSHIGRVHKL 

       610        620        630        640        650        660 
TIDDVTPADE ADYSFVPEGF ACNLSAKLHF MEVKIDFVPR QEPPKIHLDC PGRIPDTIVV 

       670        680        690        700        710        720 
VAGNKLRLDV PISGDPAPTV IWQKAITQGN KAPARPAPDA PEDTGDSDEW VFDKKLLCET 

       730        740        750        760        770        780 
EGRVRVETTK DRSIFTVEGA EKEDEGVYTV TVKNPVGEDQ VNLTVKVIDV PDAPAAPKIS 

       790        800        810        820        830        840 
NVGEDSCTVQ WEPPAYDGGQ PILGYILERK KKKSYRWMRL NFDLIQELSH EARRMIEGVV 

       850        860        870        880        890        900 
YEMRVYAVNA IGMSRPSPAS QPFMPIGPPS EPTHLAVEDV SDTTVSLKWR PPERVGAGGL 

       910        920        930        940        950        960 
DGYSVEYCPE GCSEWVAALQ GLTEHTSILV KDLPTGARLL FRVRAHNMAG PGAPVTTTEP 

       970        980        990       1000       1010       1020 
VTVQEILQRP RLQLPRHLRQ TIQKKVGEPV NLLIPFQGKP RPQVTWTKEG QPLAGEEVSI 

      1030       1040       1050       1060       1070       1080 
RNSPTDTILF IRAARRVHSG TYQVTVRIEN MEDKATLVLQ VVDKPSPPQD LRVTDAWGLN 

      1090       1100       1110       1120       1130       1140 
VALEWKPPQD VGNTELWGYT VQKADKKTME WFTVLEHYRR THCVVPELII GNGYYFRVFS 

      1150       1160       1170       1180       1190       1200 
QNMVGFSDRA ATTKEPVFIP RPGITYEPPN YKALDFSEAP SFTQPLVNRS VIAGYTAMLC 

      1210       1220       1230       1240       1250       1260 
CAVRGSPKPK ISWFKNGLDL GEDARFRMFS KQGVLTLEIR KPCPFDGGIY VCRATNLQGE 

      1270 
ARCECRLEVR VPQ

Q14896 in FASTA format

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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools