TNNT1
| Troponin T type 1 (skeletal, slow) | |||||||||||||
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| Identifiers | |||||||||||||
| Symbols | TNNT1 ; ANM; NEM5; STNT; TNT; TNTS | ||||||||||||
| External IDs | OMIM: 191041 MGI: 1333868 HomoloGene: 20704 GeneCards: TNNT1 Gene | ||||||||||||
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| RNA expression pattern | |||||||||||||
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| Orthologs | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | 7138 | 21955 | |||||||||||
| Ensembl | ENSG00000105048 | ENSMUSG00000064179 | |||||||||||
| UniProt | P13805 | O88346 | |||||||||||
| RefSeq (mRNA) | NM_001126132 | NM_001277903 | |||||||||||
| RefSeq (protein) | NP_001119604 | NP_001264832 | |||||||||||
| Location (UCSC) | Chr 19: 55.64 – 55.66 Mb | Chr 7: 4.5 – 4.52 Mb | |||||||||||
| PubMed search | |||||||||||||
Troponin T, slow skeletal muscle is a protein that in humans is encoded by the TNNT1 gene.[1][2]
Interactions
TNNT1 has been shown to interact with PRKG1.[3]
References
- ↑ Samson F, de Jong PJ, Trask BJ, Koza-Taylor P, Speer MC, Potter T, Roses AD, Gilbert JR (Sep 1992). "Assignment of the human slow skeletal troponin T gene to 19q13.4 using somatic cell hybrids and fluorescence in situ hybridization analysis". Genomics 13 (4): 1374–5. doi:10.1016/0888-7543(92)90077-6. PMID 1505979.
- ↑ "Entrez Gene: TNNT1 troponin T type 1 (skeletal, slow)".
- ↑ Yuasa, K; Michibata H; Omori K; Yanaka N (Dec 1999). "A novel interaction of cGMP-dependent protein kinase I with troponin T". J. Biol. Chem. (UNITED STATES) 274 (52): 37429–34. doi:10.1074/jbc.274.52.37429. ISSN 0021-9258. PMID 10601315.
External links
Further reading
- Nadal-Ginard B, Mahdavi V (1990). "Molecular basis of cardiac performance. Plasticity of the myocardium generated through protein isoform switches". J. Clin. Invest. 84 (6): 1693–700. doi:10.1172/JCI114351. PMC 304044. PMID 2687327.
- Wu AH, Ford L (1999). "Release of cardiac troponin in acute coronary syndromes: ischemia or necrosis?". Clin. Chim. Acta 284 (2): 161–74. doi:10.1016/S0009-8981(99)00078-9. PMID 10451243.
- Novelli G, Gennarelli M, Zelano G et al. (1993). "Polymerase chain reaction in the detection of mRNA transcripts from the slow skeletal troponin T (TNNT1) gene in myotonic dystrophy and normal muscle". Cell Biochem. Funct. 10 (4): 251–6. doi:10.1002/cbf.290100407. PMID 1473264.
- Gahlmann R, Troutt AB, Wade RP et al. (1987). "Alternative splicing generates variants in important functional domains of human slow skeletal troponin T". J. Biol. Chem. 262 (33): 16122–6. PMID 2824479.
- Heeley DH, Golosinska K, Smillie LB (1987). "The effects of troponin T fragments T1 and T2 on the binding of nonpolymerizable tropomyosin to F-actin in the presence and absence of troponin I and troponin C". J. Biol. Chem. 262 (21): 9971–8. PMID 3611073.
- Pearlstone JR, Smillie LB (1983). "Effects of troponin-I plus-C on the binding of troponin-T and its fragments to alpha-tropomyosin. Ca2+ sensitivity and cooperativity". J. Biol. Chem. 258 (4): 2534–42. PMID 6822572.
- Samson F, Mesnard L, Mihovilovic M et al. (1994). "A new human slow skeletal troponin T (TnTs) mRNA isoform derived from alternative splicing of a single gene". Biochem. Biophys. Res. Commun. 199 (2): 841–7. doi:10.1006/bbrc.1994.1305. PMID 8135831.
- Novelli G, Gennarelli M, Sangiuolo F et al. (1993). "Isolation and cloning by a polymerase chain reaction of a genomic DNA fragment of the human slow skeletal troponin (TNNT1) gene". Cell Biochem. Funct. 11 (3): 187–91. doi:10.1002/cbf.290110306. PMID 8403232.
- 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.
- 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. doi:10.1073/pnas.95.3.957. PMC 18637. PMID 9448267.
- Jha PK, Sarkar S (1998). "A recombinant monocysteine mutant (Ser to Cys-155) of fast skeletal troponin T: identification by cross-linking of a domain involved in a physiologically relevant interaction with troponins C and I". Biochemistry 37 (35): 12253–60. doi:10.1021/bi980025z. PMID 9724539.
- Barton PJ, Cullen ME, Townsend PJ et al. (1999). "Close physical linkage of human troponin genes: organization, sequence, and expression of the locus encoding cardiac troponin I and slow skeletal troponin T". Genomics 57 (1): 102–9. doi:10.1006/geno.1998.5702. PMID 10191089.
- Mukherjea P, Tong L, Seidman JG et al. (1999). "Altered regulatory function of two familial hypertrophic cardiomyopathy troponin T mutants". Biochemistry 38 (40): 13296–301. doi:10.1021/bi9906120. PMID 10529204.
- Yuasa K, Michibata H, Omori K, Yanaka N (2000). "A novel interaction of cGMP-dependent protein kinase I with troponin T". J. Biol. Chem. 274 (52): 37429–34. doi:10.1074/jbc.274.52.37429. PMID 10601315.
- Johnston JJ, Kelley RI, Crawford TO et al. (2000). "A Novel Nemaline Myopathy in the Amish Caused by a Mutation in Troponin T1". Am. J. Hum. Genet. 67 (4): 814–21. doi:10.1086/303089. PMC 1287886. PMID 10952871.
- 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. doi:10.1016/S0014-5793(02)02340-2. PMID 11904166.
- Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
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