Search Results
Overview
| Uniprot ID | P63316 |
|---|---|
| Protein Name | Troponin C, slow skeletal and cardiac muscles |
| Gene Name | TNNC1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 92 | MKDDSKGKSEEELSD |
Function
Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments
Protein Sequence
10
MDDIYKAAVE
20
QLTEEQKNEF
30
KAAFDIFVLG
40
AEDGCISTKE
50
LGKVMRMLGQ
60
NPTPEELQEM
70
IDEVDEDGSG
80
TVDFDEFLVM
90
MVRCMKDDSK
100
GKSEEELSDL
110
FRMFDKNADG
120
YIDLDELKIM
130
LQATGETITE
140
DDIEELMKDG
150
DKNNDGRIDY
160
DEFLEFMKGV
E
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:1990584 | cardiac Troponin complex |
| Molecular Function | GO:0042803 | protein homodimerization activity |
| Molecular Function | GO:0031013 | troponin I binding |
| Molecular Function | GO:0031014 | troponin T binding |
| Biological Process | GO:0086003 | cardiac muscle cell contraction |
| Biological Process | GO:0060048 | cardiac muscle contraction |
| Biological Process | GO:0002086 | diaphragm contraction |
| Biological Process | GO:0030049 | muscle filament sliding |
| Biological Process | GO:0032780 | negative regulation of ATP-dependent activity |
| Biological Process | GO:0006937 | regulation of muscle contraction |
| Biological Process | GO:0032972 | regulation of muscle filament sliding speed |
| Biological Process | GO:0010038 | response to metal ion |
| Biological Process | GO:0003009 | skeletal muscle contraction |
| Biological Process | GO:0055010 | ventricular cardiac muscle tissue morphogenesis |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0030017 | sarcomere |
| Cellular Component | GO:0005861 | troponin complex |
| Molecular Function | GO:0051015 | actin filament binding |
| Molecular Function | GO:0005509 | calcium ion binding |
| Molecular Function | GO:0048306 | calcium-dependent protein binding |
Reference
[1] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.