| Tag | Content |
|---|
| CPLM ID | CPLM-009064 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Myosin-binding protein C, cardiac-type |
Protein Synonyms/Alias | Cardiac MyBP-C; C-protein, cardiac muscle isoform |
Gene Name | Mybpc3 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 6 | **MPEPGKRPVSAFT | acetylation | [1] |
|
Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | 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. |
Sequence Annotation | DOMAIN 8 95 Ig-like C2-type 1.
DOMAIN 157 259 Ig-like C2-type 2.
DOMAIN 361 452 Ig-like C2-type 3.
DOMAIN 452 546 Ig-like C2-type 4.
DOMAIN 645 765 Ig-like C2-type 5.
DOMAIN 772 864 Fibronectin type-III 1.
DOMAIN 869 962 Fibronectin type-III 2.
DOMAIN 971 1059 Ig-like C2-type 6.
DOMAIN 1066 1158 Fibronectin type-III 3.
DOMAIN 1181 1269 Ig-like C2-type 7.
METAL 212 212 Zinc (By similarity).
METAL 214 214 Zinc (By similarity).
METAL 227 227 Zinc (By similarity).
METAL 229 229 Zinc (By similarity).
MOD_RES 1 1 N-acetylmethionine (By similarity).
MOD_RES 279 279 Phosphoserine; by PKA and PKC (By
MOD_RES 287 287 Phosphothreonine; by PKA and PKC (By
MOD_RES 288 288 Phosphoserine (By similarity).
MOD_RES 307 307 Phosphoserine; by PKA (By similarity).
DISULFID 436 443 Potential. |
Keyword | Acetylation; Actin-binding; Cell adhesion; Complete proteome; Disulfide bond; Immunoglobulin domain; Metal-binding; Muscle protein; Phosphoprotein; Reference proteome; Repeat; Thick filament; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1274 AA |
Protein Sequence | MPEPGKRPVS AFTKKPRSVE VTAGSAAVFE AETERSGLKV QWQRDGSDIA ANDKYGLAAE 60
GKRHTLTVRD VGPDDQGSYA VIAGSSKVKF DLKVTEPAPP EKAESAVAPT SMEAPETPKE 120
VPALATQLEG NVSSPEGSVS VTQDGSVAGS QGAPDDPIGL FLMRPQDGEV TVGGSIVFSA 180
RVAGASLLKP PVVKWFKGKW VDLSSKVGQH LQLHDSYDRA SKVYLFELHI TDAQATSAGG 240
YRCEVSTKDK FDSCNFNLTV HEAIGSGDLD LRSAFRRTSL AGTGRRTSDS HEDAGTLDFS 300
SLLKKSSFRR DSKLEAPAEE DVWEILRQAP PSEYERIAFQ HGVTDLRGML KRLKGMKHDE 360
KKSTAFQKKL EPAYQVNKGH KIRLTVELAD PDAEVKWLKN GQEIQMSGRY IFESIGAKRT 420
LTISQCSLAD DAAYQCVVGG EKCSTELFVK EPPVLITRSL EDQLVMVGQR VEFECEVSEE 480
GAQVKWLKDG VELTREETFK YRFKKDGRKH HLIINEATLE DAGHYAVRTS GGQALAELIV 540
QEKKLEVYQS IADLAVGAKD QAVFKCEVSD ENVRGVWLKN GKELVPDNRI KVSHIGRVHK 600
LTIDDVTPAD EADYSFVPEG FACNLSAKLH FMEVKIDFVP RQEPPKIHLD CPGSTPDTIV 660
VVAGNKLRLD VPISGDPAPT VIWQKTITQG KKASAGPPPG APEDAGADEE WVFDKKLLCE 720
TEGRVRVETT KDRSVFTVEG AEKEDEGVYT VTVKNPVGED QVNLTVKVID VPDAPAAPKI 780
SNVGEDSCIV QWEPPAYDGG QPVLGYILER KKKKSYRWMR LNFDLLRELS HEARRMIEGV 840
AYEMRVYAVN AVGMSRPSPA SQPFMPIGPP GEPTHLTVED VSDTTVSLKW RPPERVGAGG 900
LDGYSVEYCQ EGCSEWVTAL QGLTERTSLL VKDLPTGARL LFRVRAHNVA GPGGPIITKE 960
PVTVQEILQR PRLQLPRHLR QTIQKKVGEP VNLLIPFQGK PRPQVTWTKE GQPLAGEEVS 1020
IRNSPTDTIL FIRAAHRTHS GTYQVTVRIE NMEDKATLVL QIVDKPSPPL DIRVVETWGF 1080
SVALEWKPPQ DDGNTEIWGY TVQKADKKTM EWFTVLEHYR QTHCVVSELI IGNGYYFRVF 1140
SHNMVGSSDR AAATKEPIFI PRPGITYEPP KYKALDFSEA PSFTQPLTNR SIIAGYNAIL 1200
CCAVRGSPKP KISWFKNGLD LGEDARFRMF CKQGVLTLEI RKPCPYDGGV YVCRATNLQG 1260
EAQCECRLEV RVPQ 1274 |
Gene Ontology | GO:0031672; C:A band; IEA:Compara. GO:0005863; C:striated muscle myosin thick filament; IDA:BHF-UCL. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0008307; F:structural constituent of muscle; IEA:Compara. GO:0060048; P:cardiac muscle contraction; IEP:BHF-UCL. GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. GO:0031034; P:myosin filament assembly; IEA:Compara. GO:0002027; P:regulation of heart rate; IEA:Compara. GO:0006942; P:regulation of striated muscle contraction; IEP:BHF-UCL. GO:0045214; P:sarcomere organization; IEA:Compara. GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IEA:Compara. |
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Pfam | |
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PROSITE | |
PRINTS | |