Troponin C type 1

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Troponin C type 1 (slow)
File:PBB Protein TNNC1 image.jpg
PDB rendering based on 1aj4.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols TNNC1 ; TNC; TNNC
External IDs Template:OMIM5 Template:MGI HomoloGene55728
RNA expression pattern
File:PBB GE TNNC1 209904 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Troponin C type 1 (slow), also known as TNNC1, is a human gene.[1]


References

  1. "Entrez Gene: TNNC1 troponin C type 1 (slow)".

Further reading

  • Gomes AV, Potter JD (2005). "Cellular and molecular aspects of familial hypertrophic cardiomyopathy caused by mutations in the cardiac troponin I gene". Mol. Cell. Biochem. 263 (1–2): 99–114. PMID 15524171.
  • Tomasselli AG, Hui JO, Adams L; et al. (1991). "Actin, troponin C, Alzheimer amyloid precursor protein and pro-interleukin 1 beta as substrates of the protease from human immunodeficiency virus". J. Biol. Chem. 266 (22): 14548–53. PMID 1907279.
  • Schreier T, Kedes L, Gahlmann R (1991). "Cloning, structural analysis, and expression of the human slow twitch skeletal muscle/cardiac troponin C gene". J. Biol. Chem. 265 (34): 21247–53. PMID 2250022.
  • Gahlmann R, Wade R, Gunning P, Kedes L (1988). "Differential expression of slow and fast skeletal muscle troponin C. Slow skeletal muscle troponin C is expressed in human fibroblasts". J. Mol. Biol. 201 (2): 379–91. PMID 3166492.
  • Roher A, Lieska N, Spitz W (1986). "The amino acid sequence of human cardiac troponin-C". Muscle Nerve. 9 (1): 73–7. doi:10.1002/mus.880090112. PMID 3951483.
  • Grand RJ, Levine BA, Perry SV (1982). "Proton-magnetic-resonance studies on the interaction of rabbit skeletal-muscle troponin I with troponin C and actin". Biochem. J. 203 (1): 61–8. PMID 7103951.
  • Thierfelder L, Watkins H, MacRae C; et al. (1994). "Alpha-tropomyosin and cardiac troponin T mutations cause familial hypertrophic cardiomyopathy: a disease of the sarcomere". Cell. 77 (5): 701–12. PMID 8205619.
  • Jha PK, Leavis PC, Sarkar S (1997). "Interaction of deletion mutants of troponins I and T: COOH-terminal truncation of troponin T abolishes troponin I binding and reduces Ca2+ sensitivity of the reconstituted regulatory system". Biochemistry. 35 (51): 16573–80. doi:10.1021/bi9622433. PMID 8987992.
  • Song WJ, Van Keuren ML, Drabkin HA; et al. (1997). "Assignment of the human slow twitch skeletal muscle/cardiac troponin C gene (TNNC1) to human chromosome 3p21.3-->3p14.3 using somatic cell hybrids". Cytogenet. Cell Genet. 75 (1): 36–7. PMID 8995486.
  • Takeda S, Kobayashi T, Taniguchi H; et al. (1997). "Structural and functional domains of the troponin complex revealed by limited digestion". Eur. J. Biochem. 246 (3): 611–7. PMID 9219516.
  • Spyracopoulos L, Li MX, Sia SK; et al. (1997). "Calcium-induced structural transition in the regulatory domain of human cardiac troponin C.". Biochemistry. 36 (40): 12138–46. doi:10.1021/bi971223d. PMID 9315850.
  • Keane NE, Quirk PG, Gao Y; et al. (1997). "The ordered phosphorylation of cardiac troponin I by the cAMP-dependent protein kinase--structural consequences and functional implications". Eur. J. Biochem. 248 (2): 329–37. PMID 9346285.
  • Stefancsik R, Jha PK, Sarkar S (1998). "Identification and mutagenesis of a highly conserved domain in troponin T responsible for troponin I binding: potential role for coiled coil interaction". Proc. Natl. Acad. Sci. U.S.A. 95 (3): 957–62. PMID 9448267.
  • Vassylyev DG, Takeda S, Wakatsuki S; et al. (1998). "Crystal structure of troponin C in complex with troponin I fragment at 2.3-A resolution". Proc. Natl. Acad. Sci. U.S.A. 95 (9): 4847–52. PMID 9560191.
  • Redwood C, Lohmann K, Bing W; et al. (2000). "Investigation of a truncated cardiac troponin T that causes familial hypertrophic cardiomyopathy: Ca(2+) regulatory properties of reconstituted thin filaments depend on the ratio of mutant to wild-type protein". Circ. Res. 86 (11): 1146–52. PMID 10850966.
  • Hoffmann B, Schmidt-Traub H, Perrot A; et al. (2001). "First mutation in cardiac troponin C, L29Q, in a patient with hypertrophic cardiomyopathy". Hum. Mutat. 17 (6): 524. doi:10.1002/humu.1143. PMID 11385718.
  • Schmidtmann A, Lohmann K, Jaquet K (2002). "The interaction of the bisphosphorylated N-terminal arm of cardiac troponin I-A 31P-NMR study". FEBS Lett. 513 (2–3): 289–93. PMID 11904166.
  • Lindhout DA, Li MX, Schieve D, Sykes BD (2002). "Effects of T142 phosphorylation and mutation R145G on the interaction of the inhibitory region of human cardiac troponin I with the C-domain of human cardiac troponin C.". Biochemistry. 41 (23): 7267–74. PMID 12044157.
  • Wang X, Li MX, Sykes BD (2002). "Structure of the regulatory N-domain of human cardiac troponin C in complex with human cardiac troponin I147-163 and bepridil". J. Biol. Chem. 277 (34): 31124–33. doi:10.1074/jbc.M203896200. PMID 12060657.
  • Li MX, Saude EJ, Wang X; et al. (2003). "Kinetic studies of calcium and cardiac troponin I peptide binding to human cardiac troponin C using NMR spectroscopy". Eur. Biophys. J. 31 (4): 245–56. doi:10.1007/s00249-002-0227-1. PMID 12122471.