TNNC2
Troponin C type 2 (fast) |
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![](../I/m/PBB_Protein_TNNI2_image.jpg) PDB rendering based on 1a2x. |
Available structures |
PDB |
Ortholog search: PDBe, RCSB |
List of PDB id codes |
1a2x, 1avs, 1blq, 1ncx, 1ncy, 1ncz, 1npq, 1skt, 1smg, 1tcf, 1tn4, 1tnp, 1tnq, 1tnw, 1tnx, 1top, 1trf, 1ytz, 1yv0, 1zac, 2tn4, 4tnc, 5tnc
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Identifiers |
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Symbol | TNNC2 |
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External IDs | OMIM: 191039 MGI: 98780 HomoloGene: 55727 GeneCards: TNNC2 Gene |
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RNA expression pattern |
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More reference expression data |
Orthologs |
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Species | Human | Mouse | |
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Entrez | 7125 | 21925 | |
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Ensembl | ENSG00000101470 | ENSMUSG00000017300 | |
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UniProt | P02585 | P20801 | |
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RefSeq (mRNA) | NM_003279 | NM_009394 | |
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RefSeq (protein) | NP_003270 | NP_033420 | |
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Location (UCSC) | Chr 20: 44.45 – 44.46 Mb | Chr 2: 164.78 – 164.78 Mb | |
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PubMed search | | | |
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Troponin C, skeletal muscle is a protein that in humans is encoded by the TNNC2 gene.[1][2]
Troponin (Tn), a key protein complex in the regulation of striated muscle contraction, is composed of 3 subunits. The Tn-I subunit inhibits actomyosin ATPase, the Tn-T subunit binds tropomyosin and Tn-C, while the Tn-C subunit binds calcium and overcomes the inhibitory action of the troponin complex on actin filaments. The protein encoded by this gene is the Tn-C subunit.[2]
References
Further reading
- Romero-Herrera AE, Castillo O, Lehmann H (1977). "Human skeletal muscle proteins. The primary structure of troponin C.". J. Mol. Evol. 8 (3): 251–70. doi:10.1007/bf01730999. PMID 978749.
- 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.
- 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. doi:10.1016/0022-2836(88)90145-3. PMID 3166492.
- Prentice H, Kloner RA, Prigozy T et al. (1995). "Tissue restricted gene expression assayed by direct DNA injection into cardiac and skeletal muscle.". J. Mol. Cell. Cardiol. 26 (10): 1393–401. doi:10.1006/jmcc.1994.1157. PMID 7869399.
- Tiso N, Rampoldi L, Pallavicini A et al. (1997). "Fine mapping of five human skeletal muscle genes: alpha-tropomyosin, beta-tropomyosin, troponin-I slow-twitch, troponin-I fast-twitch, and troponin-C fast.". Biochem. Biophys. Res. Commun. 230 (2): 347–50. doi:10.1006/bbrc.1996.5958. PMID 9016781.
- Townsend PJ, Yacoub MH, Barton PJ (1998). "Assignment of the human fast skeletal muscle troponin C gene (TNNC2) between D20S721 and GCT10F11 on chromosome 20 by somatic cell hybrid analysis.". Ann. Hum. Genet. 61 (Pt 5): 457–9. doi:10.1046/j.1469-1809.1997.6150457.x. PMID 9459007.
- 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. doi:10.1073/pnas.95.9.4847. PMC 20176. PMID 9560191.
- Deloukas P, Matthews LH, Ashurst J et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20.". Nature 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052.
- 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.
- Gerhard DS, Wagner L, Feingold EA et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
PDB gallery |
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| | 1a2x: COMPLEX OF TROPONIN C WITH A 47 RESIDUE (1-47) FRAGMENT OF TROPONIN I |
| 1avs: X-RAY CRYSTALLOGRAPHIC STUDY OF CALCIUM-SATURATED N-TERMINAL DOMAIN OF TROPONIN C |
| 1blq: STRUCTURE AND INTERACTION SITE OF THE REGULATORY DOMAIN OF TROPONIN-C WHEN COMPLEXED WITH THE 96-148 REGION OF TROPONIN-I, NMR, 29 STRUCTURES |
| 1ncy: TROPONIN-C, COMPLEX WITH MANGANESE |
| 1npq: structure of a rhodamine-labeled N-domain Troponin C mutant (Ca2+ saturated) in complex with skeletal Troponin I 115-131 |
| 1skt: SOLUTION STRUCTURE OF APO N-DOMAIN OF TROPONIN C, NMR, 40 STRUCTURES |
| 1smg: CALCIUM-BOUND E41A MUTANT OF THE N-DOMAIN OF CHICKEN TROPONIN C, NMR, 40 STRUCTURES |
| 1tcf: CRYSTAL STRUCTURE OF CALCIUM-SATURATED RABBIT SKELETAL TROPONIN C |
| 1tnp: STRUCTURES OF THE APO AND CALCIUM TROPONIN-C REGULATORY DOMAINS: THE MUSCLE CONTRACTION SWITCH |
| 1tnq: STRUCTURES OF THE APO AND CALCIUM TROPONIN-C REGULATORY DOMAINS: THE MUSCLE CONTRACTION SWITCH |
| 1tnw: NMR SOLUTION STRUCTURE OF CALCIUM SATURATED SKELETAL MUSCLE TROPONIN C |
| 1tnx: NMR SOLUTION STRUCTURE OF CALCIUM SATURATED SKELETAL MUSCLE TROPONIN C |
| 1top: STRUCTURE OF CHICKEN SKELETAL MUSCLE TROPONIN-C AT 1.78 ANGSTROMS RESOLUTION |
| 1trf: SOLUTION STRUCTURE OF THE TR1C FRAGMENT OF SKELETAL MUSCLE TROPONIN-C |
| 1ytz: Crystal structure of skeletal muscle troponin in the Ca2+-activated state |
| 1yv0: Crystal structure of skeletal muscle troponin in the Ca2+-free state |
| 1zac: N-DOMAIN OF TROPONIN C FROM CHICKEN SKELETAL MUSCLE, NMR, MINIMIZED AVERAGE STRUCTURE |
| 4tnc: REFINED STRUCTURE OF CHICKEN SKELETAL MUSCLE TROPONIN C IN THE TWO-CALCIUM STATE AT 2-ANGSTROMS RESOLUTION |
| 5tnc: REFINED CRYSTAL STRUCTURE OF TROPONIN C FROM TURKEY SKELETAL MUSCLE AT 2.0 ANGSTROMS RESOLUTION |
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| Nonhuman | |
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| See also: cytoskeletal defects Index of cells |
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| Description |
- Structure
- Organelles
- peroxisome
- cytoskeleton
- centrosome
- epithelia
- cilia
- mitochondria
- Membranes
- Membrane transport
- ion channels
- vesicular transport
- solute carrier
- ABC transporters
- ATPase
- oxidoreduction-driven
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| Disease |
- Structural
- peroxisome
- cytoskeleton
- cilia
- mitochondria
- nucleus
- scleroprotein
- Membrane
- channelopathy
- solute carrier
- ATPase
- ABC transporters
- other
- extracellular ligands
- cell surface receptors
- intracellular signalling
- Vesicular transport
- Pore-forming toxins
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