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Protein

Myosin-binding protein C, cardiac-type

Gene

MYBPC3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi208Zinc1 Publication1
Metal bindingi210Zinc1 Publication1
Metal bindingi223Zinc1 Publication1
Metal bindingi225Zinc1 Publication1

GO - Molecular functioni

  • ATPase activator activity Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • myosin binding Source: BHF-UCL
  • myosin heavy chain binding Source: BHF-UCL
  • structural constituent of muscle Source: BHF-UCL
  • titin binding Source: BHF-UCL

GO - Biological processi

  • cardiac muscle contraction Source: BHF-UCL
  • cell adhesion Source: UniProtKB-KW
  • heart morphogenesis Source: BHF-UCL
  • muscle filament sliding Source: Reactome
  • positive regulation of ATPase activity Source: BHF-UCL
  • regulation of muscle filament sliding Source: BHF-UCL
  • regulation of striated muscle contraction Source: BHF-UCL
  • ventricular cardiac muscle tissue morphogenesis Source: HGNC
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Actin-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000134571-MONOMER.
ReactomeiR-HSA-390522. Striated Muscle Contraction.
SIGNORiQ14896.

Names & Taxonomyi

Protein namesi
Recommended name:
Myosin-binding protein C, cardiac-type
Short name:
Cardiac MyBP-C
Alternative name(s):
C-protein, cardiac muscle isoform
Gene namesi
Name:MYBPC3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:7551. MYBPC3.

Subcellular locationi

GO - Cellular componenti

  • A band Source: BHF-UCL
  • cytosol Source: Reactome
  • C zone Source: BHF-UCL
  • sarcomere Source: BHF-UCL
  • striated muscle myosin thick filament Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Thick filament

Pathology & Biotechi

Involvement in diseasei

Cardiomyopathy, familial hypertrophic 4 (CMH4)24 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:115197
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0293905G → R in CMH4. 1 PublicationCorresponds to variant rs201278114dbSNPEnsembl.1
Natural variantiVAR_02939159T → A in CMH4. 1 PublicationCorresponds to variant rs121909375dbSNPEnsembl.1
Natural variantiVAR_029392161P → S in CMH4. 1 Publication1
Natural variantiVAR_029393219V → L in CMH4. 1 PublicationCorresponds to variant rs397516068dbSNPEnsembl.1
Natural variantiVAR_029394228D → N in CMH4. 1 PublicationCorresponds to variant rs369300885dbSNPEnsembl.1
Natural variantiVAR_029395237Y → S in CMH4. 1 PublicationCorresponds to variant rs397516070dbSNPEnsembl.1
Natural variantiVAR_029396256V → I in CMH4. 1 Publication1
Natural variantiVAR_019889257H → P in CMH4. 1 Publication1
Natural variantiVAR_019890258E → K in CMH4. 8 PublicationsCorresponds to variant rs397516074dbSNPEnsembl.1
Natural variantiVAR_042740263G → R in CMH4. 1 PublicationCorresponds to variant rs373730381dbSNPEnsembl.1
Natural variantiVAR_070449272R → C in CMH4. 1 PublicationCorresponds to variant rs397516075dbSNPEnsembl.1
Natural variantiVAR_042741273R → H in CMH4. 1 PublicationCorresponds to variant rs376461745dbSNPEnsembl.1
Natural variantiVAR_019891278G → E in CMH4. 2 PublicationsCorresponds to variant rs147315081dbSNPEnsembl.1
Natural variantiVAR_019892279G → A in CMH4. 1 PublicationCorresponds to variant rs375774648dbSNPEnsembl.1
Natural variantiVAR_029397282R → W in CMH4. 2 PublicationsCorresponds to variant rs727504234dbSNPEnsembl.1
Natural variantiVAR_074539334E → 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. 2 PublicationsCorresponds to variant rs573916965dbSNPEnsembl.1
Natural variantiVAR_070450336I → V in CMH4. 1 Publication1
Natural variantiVAR_074540342V → D in CMH4. 1 PublicationCorresponds to variant rs730880709dbSNPEnsembl.1
Natural variantiVAR_019894352L → P in CMH4. 1 Publication1
Natural variantiVAR_042742417A → S in CMH4. 1 Publication1
Natural variantiVAR_027879451E → Q in CMH4. 1 Publication1
Natural variantiVAR_029399458R → H in CMH4. 1 PublicationCorresponds to variant rs374255707dbSNPEnsembl.1
Natural variantiVAR_029400490G → R in CMH4, CMD1MM and LVNC10. 4 PublicationsCorresponds to variant rs200625851dbSNPEnsembl.1
Natural variantiVAR_070451490G → V in CMH4. 1 PublicationCorresponds to variant rs397514752dbSNPEnsembl.1
Natural variantiVAR_045929495R → G in CMH4. 1 PublicationCorresponds to variant rs397515905dbSNPEnsembl.1
Natural variantiVAR_027880495R → Q in CMH4. 4 PublicationsCorresponds to variant rs200411226dbSNPEnsembl.1
Natural variantiVAR_027881502R → Q in CMH4. 3 PublicationsCorresponds to variant rs397515907dbSNPEnsembl.1
Natural variantiVAR_019895502R → W in CMH4. 4 PublicationsCorresponds to variant rs375882485dbSNPEnsembl.1
Natural variantiVAR_019896504Missing in CMH4. 1 Publication1
Natural variantiVAR_029401507G → R in CMH4. 3 PublicationsCorresponds to variant rs35736435dbSNPEnsembl.1
Natural variantiVAR_029402523G → W in CMH4. 1 Publication1
Natural variantiVAR_003917542E → Q in CMH4. 4 PublicationsCorresponds to variant rs121909374dbSNPEnsembl.1
Natural variantiVAR_029404566C → R in CMH4. 2 PublicationsCorresponds to variant rs730880695dbSNPEnsembl.1
Natural variantiVAR_029405604D → V in CMH4. 1 Publication1
Natural variantiVAR_029406605D → N in CMH4; unknown pathological significance. 3 PublicationsCorresponds to variant rs376736293dbSNPEnsembl.1
Natural variantiVAR_029407608P → L in CMH4. 1 Publication1
Natural variantiVAR_074541627A → V in CMH4. 1 Publication1
Natural variantiVAR_003918654R → H in CMH4; as well folded and stable as the wild-type. 2 PublicationsCorresponds to variant rs1800565dbSNPEnsembl.1
Natural variantiVAR_029408668R → H in CMH4. 1 PublicationCorresponds to variant rs727503191dbSNPEnsembl.1
Natural variantiVAR_029409668R → P in CMH4. 1 Publication1
Natural variantiVAR_042743669L → H in CMH4. 1 Publication1
Natural variantiVAR_029410733R → C in CMH4. 1 PublicationCorresponds to variant rs397515956dbSNPEnsembl.1
Natural variantiVAR_003919755N → K in CMH4; destabilizes the structure of Ig-like C2-type domain 5. 2 Publications1
Natural variantiVAR_042744759E → D in CMH4. 1 Publication1
Natural variantiVAR_029411770D → N in CMH4. 1 PublicationCorresponds to variant rs36211723dbSNPEnsembl.1
Natural variantiVAR_074542771V → M in CMH4. 1 PublicationCorresponds to variant rs371488302dbSNPEnsembl.1
Natural variantiVAR_029412792W → R in CMH4. 1 PublicationCorresponds to variant rs187830361dbSNPEnsembl.1
Natural variantiVAR_029413810R → H in CMH4. 2 PublicationsCorresponds to variant rs375675796dbSNPEnsembl.1
Natural variantiVAR_019897811K → R in CMH4. 1 Publication1
Natural variantiVAR_029414811Missing in CMH4. 1 Publication1
Natural variantiVAR_029415813Missing in CMH4. 1 Publication1
Natural variantiVAR_074543814Missing in CMH4; no effect on protein abundance; no effect on endopeptidase activity. 1 Publication1
Natural variantiVAR_029416820R → Q in CMH4. 4 PublicationsCorresponds to variant rs2856655dbSNPEnsembl.1
Natural variantiVAR_029417833A → T in CMH4 and CMD1MM. 5 PublicationsCorresponds to variant rs199865688dbSNPEnsembl.1
Natural variantiVAR_019898833A → V in CMH4. 3 PublicationsCorresponds to variant rs3729952dbSNPEnsembl.1
Natural variantiVAR_029418834R → T in CMH4. 1
Natural variantiVAR_029419834R → W in CMH4; unknown pathological significance. 1 PublicationCorresponds to variant rs752007810dbSNPEnsembl.1
Natural variantiVAR_029420873P → H in CMH4. 1 PublicationCorresponds to variant rs371401403dbSNPEnsembl.1
Natural variantiVAR_029421948N → T in CMH4. 1 PublicationCorresponds to variant rs121909376dbSNPEnsembl.1
Natural variantiVAR_070453957T → S in CMH4. 1 PublicationCorresponds to variant rs193922380dbSNPEnsembl.1
Natural variantiVAR_070454958T → I in CMH4. 1 PublicationCorresponds to variant rs376504548dbSNPEnsembl.1
Natural variantiVAR_020574998Q → E in CMH4; no effect on protein abundance; no effect on endopeptidase activity. 3 PublicationsCorresponds to variant rs11570112dbSNPEnsembl.1
Natural variantiVAR_029422998Q → R in CMH4. 1 PublicationCorresponds to variant rs727503177dbSNPEnsembl.1
Natural variantiVAR_0294231002R → Q in CMH4. 1 PublicationCorresponds to variant rs727504235dbSNPEnsembl.1
Natural variantiVAR_0294251003P → Q in CMH4. 1
Natural variantiVAR_0459301028T → S in CMH4. 1 PublicationCorresponds to variant rs397516002dbSNPEnsembl.1
Natural variantiVAR_0745441046T → M in CMH4; no effect on protein abundance; no effect on endopeptidase activity. 1 PublicationCorresponds to variant rs371061770dbSNPEnsembl.1
Natural variantiVAR_0294261113F → I in CMH4. 1 Publication1
Natural variantiVAR_0294271115V → I in CMH4. 2 PublicationsCorresponds to variant rs531189495dbSNPEnsembl.1
Natural variantiVAR_0294281131I → T in CMH4; unknown pathological significance. 2 PublicationsCorresponds to variant rs370890951dbSNPEnsembl.1
Natural variantiVAR_0294291155Missing in CMH4. 1
Natural variantiVAR_0199001194A → T in CMH4. 1 PublicationCorresponds to variant rs397516026dbSNPEnsembl.1
Natural variantiVAR_0459311248G → R in CMH4. 1 PublicationCorresponds to variant rs202147520dbSNPEnsembl.1
Natural variantiVAR_0199011255A → T in CMH4. 1 PublicationCorresponds to variant rs727503167dbSNPEnsembl.1
Cardiomyopathy, dilated 1MM (CMD1MM)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.
See also OMIM:615396
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_029400490G → R in CMH4, CMD1MM and LVNC10. 4 PublicationsCorresponds to variant rs200625851dbSNPEnsembl.1
Natural variantiVAR_029417833A → T in CMH4 and CMD1MM. 5 PublicationsCorresponds to variant rs199865688dbSNPEnsembl.1
Natural variantiVAR_0704551264C → F in CMD1MM. 1 PublicationCorresponds to variant rs397514751dbSNPEnsembl.1

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.

Left ventricular non-compaction 10 (LVNC10)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:615396
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_029400490G → R in CMH4, CMD1MM and LVNC10. 4 PublicationsCorresponds to variant rs200625851dbSNPEnsembl.1
Natural variantiVAR_070452873P → L in LVNC10. 1 PublicationCorresponds to variant rs371401403dbSNPEnsembl.1

Keywords - Diseasei

Cardiomyopathy, Disease mutation

Organism-specific databases

DisGeNETi4607.
MalaCardsiMYBPC3.
MIMi115197. phenotype.
615396. phenotype.
OpenTargetsiENSG00000134571.
Orphaneti154. Familial isolated dilated cardiomyopathy.
155. Familial isolated hypertrophic cardiomyopathy.
54260. Left ventricular noncompaction.
PharmGKBiPA31351.

Polymorphism and mutation databases

BioMutaiMYBPC3.
DMDMi425906074.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000726931 – 1274Myosin-binding protein C, cardiac-typeAdd BLAST1274

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei47PhosphoserineBy similarity1
Modified residuei275Phosphoserine; by PKA and PKCBy similarity1
Modified residuei284Phosphoserine; by PKA and PKCBy similarity1
Modified residuei304Phosphoserine; by PKA and PKCBy similarity1
Modified residuei311PhosphoserineBy similarity1
Modified residuei427PhosphoserineBy similarity1
Disulfide bondi436 ↔ 443PROSITE-ProRule annotation
Modified residuei550PhosphoserineBy similarity1
Modified residuei607PhosphothreonineBy similarity1
Modified residuei1241Omega-N-methylarginineBy similarity1

Post-translational modificationi

Substrate for phosphorylation by PKA and PKC. Reversible phosphorylation appears to modulate contraction (By similarity).By similarity
Polyubiquitinated.1 Publication

Keywords - PTMi

Acetylation, Disulfide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ14896.
PeptideAtlasiQ14896.
PRIDEiQ14896.

2D gel databases

UCD-2DPAGEQ14896.

PTM databases

iPTMnetiQ14896.
PhosphoSitePlusiQ14896.

Expressioni

Gene expression databases

BgeeiENSG00000134571.
CleanExiHS_MYBPC3.
ExpressionAtlasiQ14896. baseline and differential.
GenevisibleiQ14896. HS.

Organism-specific databases

HPAiHPA040147.
HPA043898.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-704176,EBI-704176
PDE4DIPQ5VU43-115EBI-704176,EBI-10769071

GO - Molecular functioni

  • myosin binding Source: BHF-UCL
  • myosin heavy chain binding Source: BHF-UCL
  • titin binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi110692. 10 interactors.
IntActiQ14896. 13 interactors.
MINTiMINT-6174801.
STRINGi9606.ENSP00000442795.

Structurei

Secondary structure

11274
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi19 – 22Combined sources4
Beta strandi27 – 32Combined sources6
Beta strandi34 – 37Combined sources4
Beta strandi41 – 43Combined sources3
Beta strandi45 – 49Combined sources5
Beta strandi56 – 60Combined sources5
Beta strandi63 – 70Combined sources8
Beta strandi77 – 83Combined sources7
Beta strandi86 – 95Combined sources10
Beta strandi156 – 159Combined sources4
Beta strandi164 – 167Combined sources4
Beta strandi172 – 179Combined sources8
Beta strandi184 – 186Combined sources3
Beta strandi188 – 193Combined sources6
Turni194 – 196Combined sources3
Helixi199 – 202Combined sources4
Beta strandi207 – 214Combined sources8
Turni215 – 218Combined sources4
Beta strandi219 – 226Combined sources8
Helixi231 – 233Combined sources3
Beta strandi235 – 242Combined sources8
Beta strandi247 – 257Combined sources11
Beta strandi366 – 368Combined sources3
Beta strandi371 – 376Combined sources6
Beta strandi381 – 386Combined sources6
Beta strandi388 – 392Combined sources5
Beta strandi395 – 403Combined sources9
Beta strandi407 – 415Combined sources9
Beta strandi418 – 423Combined sources6
Beta strandi427 – 430Combined sources4
Beta strandi432 – 438Combined sources7
Beta strandi441 – 443Combined sources3
Beta strandi446 – 450Combined sources5
Beta strandi456 – 458Combined sources3
Beta strandi465 – 467Combined sources3
Beta strandi471 – 474Combined sources4
Beta strandi475 – 479Combined sources5
Beta strandi486 – 488Combined sources3
Beta strandi499 – 506Combined sources8
Beta strandi509 – 517Combined sources9
Turni519 – 521Combined sources3
Beta strandi524 – 528Combined sources5
Beta strandi533 – 537Combined sources5
Beta strandi650 – 652Combined sources3
Beta strandi658 – 665Combined sources8
Beta strandi670 – 672Combined sources3
Beta strandi675 – 677Combined sources3
Beta strandi680 – 686Combined sources7
Beta strandi722 – 724Combined sources3
Beta strandi726 – 730Combined sources5
Beta strandi733 – 737Combined sources5
Turni743 – 745Combined sources3
Beta strandi747 – 754Combined sources8
Beta strandi759 – 768Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GXENMR-A641-770[»]
1PD6NMR-A358-451[»]
2AVGNMR-A151-260[»]
2K1MNMR-A2-96[»]
2MQ0NMR-A453-543[»]
2MQ3NMR-A453-543[»]
2V6HX-ray1.55A151-258[»]
3CX2X-ray1.30A151-258[»]
ProteinModelPortaliQ14896.
SMRiQ14896.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14896.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini153 – 256Ig-like C2-type 1Add BLAST104
Domaini362 – 452Ig-like C2-type 2Add BLAST91
Domaini453 – 543Ig-like C2-type 3Add BLAST91
Domaini544 – 633Ig-like C2-type 4Add BLAST90
Domaini645 – 771Ig-like C2-type 5Add BLAST127
Domaini774 – 870Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST97
Domaini872 – 967Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST96
Domaini971 – 1065Ig-like C2-type 6Add BLAST95
Domaini1068 – 1163Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST96
Domaini1181 – 1274Ig-like C2-type 7Add BLAST94

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi102 – 152Pro-richAdd BLAST51

Sequence similaritiesi

Belongs to the immunoglobulin superfamily. MyBP family.Curated
Contains 3 fibronectin type-III domains.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat

Phylogenomic databases

eggNOGiENOG410IFCI. Eukaryota.
ENOG4110AYI. LUCA.
GeneTreeiENSGT00860000133685.
HOGENOMiHOG000220906.
HOVERGENiHBG052560.
InParanoidiQ14896.
KOiK12568.
OMAiRVFSHNM.
TreeFamiTF351819.

Family and domain databases

CDDicd00063. FN3. 3 hits.
Gene3Di2.60.40.10. 11 hits.
InterProiIPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]
PfamiPF00041. fn3. 3 hits.
PF07679. I-set. 8 hits.
[Graphical view]
SMARTiSM00060. FN3. 3 hits.
SM00409. IG. 8 hits.
SM00408. IGc2. 6 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 8 hits.
SSF49265. SSF49265. 2 hits.
PROSITEiPS50853. FN3. 3 hits.
PS50835. IG_LIKE. 6 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q14896-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPEPGKKPVS AFSKKPRSVE VAAGSPAVFE AETERAGVKV RWQRGGSDIS
60 70 80 90 100
ASNKYGLATE GTRHTLTVRE VGPADQGSYA VIAGSSKVKF DLKVIEAEKA
110 120 130 140 150
EPMLAPAPAP AEATGAPGEA PAPAAELGES APSPKGSSSA ALNGPTPGAP
160 170 180 190 200
DDPIGLFVMR PQDGEVTVGG SITFSARVAG ASLLKPPVVK WFKGKWVDLS
210 220 230 240 250
SKVGQHLQLH DSYDRASKVY LFELHITDAQ PAFTGSYRCE VSTKDKFDCS
260 270 280 290 300
NFNLTVHEAM GTGDLDLLSA FRRTSLAGGG RRISDSHEDT GILDFSSLLK
310 320 330 340 350
KRDSFRTPRD SKLEAPAEED VWEILRQAPP SEYERIAFQY GVTDLRGMLK
360 370 380 390 400
RLKGMRRDEK KSTAFQKKLE PAYQVSKGHK IRLTVELADH DAEVKWLKNG
410 420 430 440 450
QEIQMSGSKY IFESIGAKRT LTISQCSLAD DAAYQCVVGG EKCSTELFVK
460 470 480 490 500
EPPVLITRPL EDQLVMVGQR VEFECEVSEE GAQVKWLKDG VELTREETFK
510 520 530 540 550
YRFKKDGQRH HLIINEAMLE DAGHYALCTS GGQALAELIV QEKKLEVYQS
560 570 580 590 600
IADLMVGAKD QAVFKCEVSD ENVRGVWLKN GKELVPDSRI KVSHIGRVHK
610 620 630 640 650
LTIDDVTPAD EADYSFVPEG FACNLSAKLH FMEVKIDFVP RQEPPKIHLD
660 670 680 690 700
CPGRIPDTIV VVAGNKLRLD VPISGDPAPT VIWQKAITQG NKAPARPAPD
710 720 730 740 750
APEDTGDSDE WVFDKKLLCE TEGRVRVETT KDRSIFTVEG AEKEDEGVYT
760 770 780 790 800
VTVKNPVGED QVNLTVKVID VPDAPAAPKI SNVGEDSCTV QWEPPAYDGG
810 820 830 840 850
QPILGYILER KKKKSYRWMR LNFDLIQELS HEARRMIEGV VYEMRVYAVN
860 870 880 890 900
AIGMSRPSPA SQPFMPIGPP SEPTHLAVED VSDTTVSLKW RPPERVGAGG
910 920 930 940 950
LDGYSVEYCP EGCSEWVAAL QGLTEHTSIL VKDLPTGARL LFRVRAHNMA
960 970 980 990 1000
GPGAPVTTTE PVTVQEILQR PRLQLPRHLR QTIQKKVGEP VNLLIPFQGK
1010 1020 1030 1040 1050
PRPQVTWTKE GQPLAGEEVS IRNSPTDTIL FIRAARRVHS GTYQVTVRIE
1060 1070 1080 1090 1100
NMEDKATLVL QVVDKPSPPQ DLRVTDAWGL NVALEWKPPQ DVGNTELWGY
1110 1120 1130 1140 1150
TVQKADKKTM EWFTVLEHYR RTHCVVPELI IGNGYYFRVF SQNMVGFSDR
1160 1170 1180 1190 1200
AATTKEPVFI PRPGITYEPP NYKALDFSEA PSFTQPLVNR SVIAGYTAML
1210 1220 1230 1240 1250
CCAVRGSPKP KISWFKNGLD LGEDARFRMF SKQGVLTLEI RKPCPFDGGI
1260 1270
YVCRATNLQG EARCECRLEV RVPQ
Length:1,274
Mass (Da):140,762
Last modified:November 28, 2012 - v4
Checksum:i4E5385C40085B796
GO
Isoform 2 (identifier: Q14896-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     408-409: SK → R

Show »
Length:1,273
Mass (Da):140,703
Checksum:iA23FC20A513F4920
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti248D → E (PubMed:7744002).Curated1
Sequence conflicti248D → E (PubMed:9048664).Curated1
Sequence conflicti302 – 303RD → SS in AAR89909 (Ref. 4) Curated2
Sequence conflicti536A → R in CAA58882 (PubMed:7744002).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0293905G → R in CMH4. 1 PublicationCorresponds to variant rs201278114dbSNPEnsembl.1
Natural variantiVAR_02939159T → A in CMH4. 1 PublicationCorresponds to variant rs121909375dbSNPEnsembl.1
Natural variantiVAR_074538147P → L.1 PublicationCorresponds to variant rs730880615dbSNPEnsembl.1
Natural variantiVAR_020085158V → M.3 PublicationsCorresponds to variant rs3729986dbSNPEnsembl.1
Natural variantiVAR_029392161P → S in CMH4. 1 Publication1
Natural variantiVAR_020568189V → I.1 PublicationCorresponds to variant rs11570052dbSNPEnsembl.1
Natural variantiVAR_029393219V → L in CMH4. 1 PublicationCorresponds to variant rs397516068dbSNPEnsembl.1
Natural variantiVAR_029394228D → N in CMH4. 1 PublicationCorresponds to variant rs369300885dbSNPEnsembl.1
Natural variantiVAR_020086236S → G.9 PublicationsCorresponds to variant rs3729989dbSNPEnsembl.1
Natural variantiVAR_029395237Y → S in CMH4. 1 PublicationCorresponds to variant rs397516070dbSNPEnsembl.1
Natural variantiVAR_029396256V → I in CMH4. 1 Publication1
Natural variantiVAR_019889257H → P in CMH4. 1 Publication1
Natural variantiVAR_019890258E → K in CMH4. 8 PublicationsCorresponds to variant rs397516074dbSNPEnsembl.1
Natural variantiVAR_042740263G → R in CMH4. 1 PublicationCorresponds to variant rs373730381dbSNPEnsembl.1
Natural variantiVAR_070449272R → C in CMH4. 1 PublicationCorresponds to variant rs397516075dbSNPEnsembl.1
Natural variantiVAR_042741273R → H in CMH4. 1 PublicationCorresponds to variant rs376461745dbSNPEnsembl.1
Natural variantiVAR_019891278G → E in CMH4. 2 PublicationsCorresponds to variant rs147315081dbSNPEnsembl.1
Natural variantiVAR_019892279G → A in CMH4. 1 PublicationCorresponds to variant rs375774648dbSNPEnsembl.1
Natural variantiVAR_020569281R → Q.1 PublicationCorresponds to variant rs11570060dbSNPEnsembl.1
Natural variantiVAR_029397282R → W in CMH4. 2 PublicationsCorresponds to variant rs727504234dbSNPEnsembl.1
Natural variantiVAR_019893326R → Q.10 PublicationsCorresponds to variant rs34580776dbSNPEnsembl.1
Natural variantiVAR_074539334E → 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. 2 PublicationsCorresponds to variant rs573916965dbSNPEnsembl.1
Natural variantiVAR_070450336I → V in CMH4. 1 Publication1
Natural variantiVAR_074540342V → D in CMH4. 1 PublicationCorresponds to variant rs730880709dbSNPEnsembl.1
Natural variantiVAR_019894352L → P in CMH4. 1 Publication1
Natural variantiVAR_020570382R → W.2 PublicationsCorresponds to variant rs11570076dbSNPEnsembl.1
Natural variantiVAR_020571383L → V.1 PublicationCorresponds to variant rs11570077dbSNPEnsembl.1
Natural variantiVAR_029398416G → S.1 PublicationCorresponds to variant rs371513491dbSNPEnsembl.1
Natural variantiVAR_042742417A → S in CMH4. 1 Publication1
Natural variantiVAR_027879451E → Q in CMH4. 1 Publication1
Natural variantiVAR_029399458R → H in CMH4. 1 PublicationCorresponds to variant rs374255707dbSNPEnsembl.1
Natural variantiVAR_029400490G → R in CMH4, CMD1MM and LVNC10. 4 PublicationsCorresponds to variant rs200625851dbSNPEnsembl.1
Natural variantiVAR_070451490G → V in CMH4. 1 PublicationCorresponds to variant rs397514752dbSNPEnsembl.1
Natural variantiVAR_045929495R → G in CMH4. 1 PublicationCorresponds to variant rs397515905dbSNPEnsembl.1
Natural variantiVAR_027880495R → Q in CMH4. 4 PublicationsCorresponds to variant rs200411226dbSNPEnsembl.1
Natural variantiVAR_027881502R → Q in CMH4. 3 PublicationsCorresponds to variant rs397515907dbSNPEnsembl.1
Natural variantiVAR_019895502R → W in CMH4. 4 PublicationsCorresponds to variant rs375882485dbSNPEnsembl.1
Natural variantiVAR_019896504Missing in CMH4. 1 Publication1
Natural variantiVAR_029401507G → R in CMH4. 3 PublicationsCorresponds to variant rs35736435dbSNPEnsembl.1
Natural variantiVAR_020573522A → T.1 PublicationCorresponds to variant rs11570082dbSNPEnsembl.1
Natural variantiVAR_029402523G → W in CMH4. 1 Publication1
Natural variantiVAR_003917542E → Q in CMH4. 4 PublicationsCorresponds to variant rs121909374dbSNPEnsembl.1
Natural variantiVAR_029403545L → M.1 PublicationCorresponds to variant rs377163678dbSNPEnsembl.1
Natural variantiVAR_029404566C → R in CMH4. 2 PublicationsCorresponds to variant rs730880695dbSNPEnsembl.1
Natural variantiVAR_029405604D → V in CMH4. 1 Publication1
Natural variantiVAR_029406605D → N in CMH4; unknown pathological significance. 3 PublicationsCorresponds to variant rs376736293dbSNPEnsembl.1
Natural variantiVAR_029407608P → L in CMH4. 1 Publication1
Natural variantiVAR_074541627A → V in CMH4. 1 Publication1
Natural variantiVAR_003918654R → H in CMH4; as well folded and stable as the wild-type. 2 PublicationsCorresponds to variant rs1800565dbSNPEnsembl.1
Natural variantiVAR_029408668R → H in CMH4. 1 PublicationCorresponds to variant rs727503191dbSNPEnsembl.1
Natural variantiVAR_029409668R → P in CMH4. 1 Publication1
Natural variantiVAR_042743669L → H in CMH4. 1 Publication1
Natural variantiVAR_029410733R → C in CMH4. 1 PublicationCorresponds to variant rs397515956dbSNPEnsembl.1
Natural variantiVAR_003919755N → K in CMH4; destabilizes the structure of Ig-like C2-type domain 5. 2 Publications1
Natural variantiVAR_042744759E → D in CMH4. 1 Publication1
Natural variantiVAR_029411770D → N in CMH4. 1 PublicationCorresponds to variant rs36211723dbSNPEnsembl.1
Natural variantiVAR_074542771V → M in CMH4. 1 PublicationCorresponds to variant rs371488302dbSNPEnsembl.1
Natural variantiVAR_029412792W → R in CMH4. 1 PublicationCorresponds to variant rs187830361dbSNPEnsembl.1
Natural variantiVAR_029413810R → H in CMH4. 2 PublicationsCorresponds to variant rs375675796dbSNPEnsembl.1
Natural variantiVAR_019897811K → R in CMH4. 1 Publication1
Natural variantiVAR_029414811Missing in CMH4. 1 Publication1
Natural variantiVAR_029415813Missing in CMH4. 1 Publication1
Natural variantiVAR_074543814Missing in CMH4; no effect on protein abundance; no effect on endopeptidase activity. 1 Publication1
Natural variantiVAR_029416820R → Q in CMH4. 4 PublicationsCorresponds to variant rs2856655dbSNPEnsembl.1
Natural variantiVAR_029417833A → T in CMH4 and CMD1MM. 5 PublicationsCorresponds to variant rs199865688dbSNPEnsembl.1
Natural variantiVAR_019898833A → V in CMH4. 3 PublicationsCorresponds to variant rs3729952dbSNPEnsembl.1
Natural variantiVAR_029418834R → T in CMH4. 1
Natural variantiVAR_029419834R → W in CMH4; unknown pathological significance. 1 PublicationCorresponds to variant rs752007810dbSNPEnsembl.1
Natural variantiVAR_029420873P → H in CMH4. 1 PublicationCorresponds to variant rs371401403dbSNPEnsembl.1
Natural variantiVAR_070452873P → L in LVNC10. 1 PublicationCorresponds to variant rs371401403dbSNPEnsembl.1
Natural variantiVAR_019899896V → M May act as a phenotype modifier in cardiomyopathy patients. 6 Publications