Troponin C, skeletal muscle

Protein-coding gene in the species Homo sapiens
TNNC2
Identifiers
AliasesTNNC2, troponin C2, fast skeletal type, CFAP85, FAP85
External IDsOMIM: 191039; MGI: 98780; HomoloGene: 55727; GeneCards: TNNC2; OMA:TNNC2 - orthologs
Gene location (Human)
Chromosome 20 (human)
Chr.Chromosome 20 (human)[1]
Chromosome 20 (human)
Genomic location for TNNC2
Genomic location for TNNC2
Band20q13.12Start45,823,214 bp[1]
End45,833,745 bp[1]
Gene location (Mouse)
Chromosome 2 (mouse)
Chr.Chromosome 2 (mouse)[2]
Chromosome 2 (mouse)
Genomic location for TNNC2
Genomic location for TNNC2
Band2|2 H3Start164,619,081 bp[2]
End164,621,887 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • Skeletal muscle tissue of rectus abdominis

  • muscle of thigh

  • gastrocnemius muscle

  • thoracic diaphragm

  • quadriceps femoris muscle

  • vastus lateralis muscle

  • Skeletal muscle tissue of biceps brachii

  • body of tongue

  • triceps brachii muscle

  • deltoid muscle
Top expressed in
  • intercostal muscle

  • soleus muscle

  • medial head of gastrocnemius muscle

  • masseter muscle

  • tibialis anterior muscle

  • body of femur

  • thoracic diaphragm

  • skeletal muscle tissue

  • muscle of thigh

  • ankle
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • actin binding
  • protein binding
  • metal ion binding
  • calcium-dependent protein binding
  • actin filament binding
  • calcium ion binding
Cellular component
  • cytosol
  • troponin complex
Biological process
  • regulation of muscle contraction
  • skeletal muscle contraction
  • muscle filament sliding
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

7125

21925

Ensembl

ENSG00000101470

ENSMUSG00000017300

UniProt

P02585

P20801

RefSeq (mRNA)

NM_003279

NM_009394

RefSeq (protein)

NP_003270

NP_033420

Location (UCSC)Chr 20: 45.82 – 45.83 MbChr 2: 164.62 – 164.62 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Troponin C, skeletal muscle is a protein that in humans is encoded by the TNNC2 gene.[5][6]

Troponin (Tn), is a key protein complex in the regulation of striated muscle contraction, composed of three subunits. The TnI subunit inhibits actomyosin ATPase, the TnT subunit binds tropomyosin and TnC, while the TnC subunit binds calcium and overcomes the inhibitory action of the troponin complex on actin thin filaments. The protein encoded by the TNNC2 gene is the TnC subunit.[6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000101470 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000017300 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Gahlmann R, Kedes L (Aug 1990). "Cloning, structural analysis, and expression of the human fast twitch skeletal muscle troponin C gene". J Biol Chem. 265 (21): 12520–8. doi:10.1016/S0021-9258(19)38376-0. PMID 2373703.
  6. ^ a b "Entrez Gene: TNNC2 troponin C type 2 (fast)".

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. S2CID 12057790.
  • 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. doi:10.1016/S0021-9258(18)98721-1. 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. S2CID 1450195.
  • 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. Bibcode:2001Natur.414..865D. 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. Bibcode:2002PNAS...9916899M. 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.
  • v
  • t
  • e
  • 1a2x: COMPLEX OF TROPONIN C WITH A 47 RESIDUE (1-47) FRAGMENT OF TROPONIN I
    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
    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
    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
  • 1ncx: TROPONIN C
    1ncx: TROPONIN C
  • 1ncy: TROPONIN-C, COMPLEX WITH MANGANESE
    1ncy: TROPONIN-C, COMPLEX WITH MANGANESE
  • 1ncz: TROPONIN C
    1ncz: TROPONIN C
  • 1npq: structure of a rhodamine-labeled N-domain Troponin C mutant (Ca2+ saturated) in complex with skeletal Troponin I 115-131
    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
    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
    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
    1tcf: CRYSTAL STRUCTURE OF CALCIUM-SATURATED RABBIT SKELETAL TROPONIN C
  • 1tn4: FOUR CALCIUM TNC
    1tn4: FOUR CALCIUM TNC
  • 1tnp: STRUCTURES OF THE APO AND CALCIUM TROPONIN-C REGULATORY DOMAINS: THE MUSCLE CONTRACTION SWITCH
    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
    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
    1tnw: NMR SOLUTION STRUCTURE OF CALCIUM SATURATED SKELETAL MUSCLE TROPONIN C
  • 1tnx: 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
    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
    1trf: SOLUTION STRUCTURE OF THE TR1C FRAGMENT OF SKELETAL MUSCLE TROPONIN-C
  • 1ytz: Crystal structure of skeletal muscle troponin in the Ca2+-activated state
    1ytz: Crystal structure of skeletal muscle troponin in the Ca2+-activated state
  • 1yv0: Crystal structure of skeletal muscle troponin in the Ca2+-free 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
    1zac: N-DOMAIN OF TROPONIN C FROM CHICKEN SKELETAL MUSCLE, NMR, MINIMIZED AVERAGE STRUCTURE
  • 2tn4: FOUR CALCIUM TNC
    2tn4: FOUR CALCIUM TNC
  • 4tnc: REFINED STRUCTURE OF CHICKEN SKELETAL MUSCLE TROPONIN C IN THE TWO-CALCIUM STATE AT 2-ANGSTROMS RESOLUTION
    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
    5tnc: REFINED CRYSTAL STRUCTURE OF TROPONIN C FROM TURKEY SKELETAL MUSCLE AT 2.0 ANGSTROMS RESOLUTION
  • v
  • t
  • e
Human
Microfilaments
and ABPs
Myofilament
Actins
Myosins
Other
Other
Intermediate
filaments
Type 1/2
(Keratin,
Cytokeratin)
Epithelial keratins
(soft alpha-keratins)
Hair keratins
(hard alpha-keratins)
Ungrouped alpha
Not alpha
Type 3
Type 4
Type 5
Microtubules
and MAPs
Tubulins
MAPs
Kinesins
Dyneins
Microtubule organising proteins
Microtubule severing proteins
Other
Catenins
Membrane
Other
Nonhuman
See also: cytoskeletal defects


Stub icon

This article on a gene on human chromosome 20 is a stub. You can help Wikipedia by expanding it.

  • v
  • t
  • e