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Protein

Troponin C, skeletal muscle

Gene

TNNC2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi28 – 39121Add
BLAST
Calcium bindingi64 – 75122Add
BLAST
Calcium bindingi104 – 115123Add
BLAST
Calcium bindingi140 – 151124Add
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro

GO - Biological processi

  1. muscle filament sliding Source: Reactome
  2. regulation of muscle contraction Source: ProtInc
  3. skeletal muscle contraction Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_16969. Striated Muscle Contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Troponin C, skeletal muscle
Gene namesi
Name:TNNC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:11944. TNNC2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. troponin complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36633.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 160159Troponin C, skeletal musclePRO_0000073703Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP02585.
PRIDEiP02585.

PTM databases

PhosphoSiteiP02585.

Expressioni

Gene expression databases

BgeeiP02585.
CleanExiHS_TNNC2.
ExpressionAtlasiP02585. baseline.
GenevestigatoriP02585.

Organism-specific databases

HPAiHPA043174.

Interactioni

Protein-protein interaction databases

BioGridi112980. 2 interactions.
STRINGi9606.ENSP00000361636.

Structurei

3D structure databases

ProteinModelPortaliP02585.
SMRiP02585. Positions 3-160.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini15 – 5036EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini51 – 8636EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini91 – 12636EF-hand 3PROSITE-ProRule annotationAdd
BLAST
Domaini127 – 16034EF-hand 4PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the troponin C family.Curated
Contains 4 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5126.
GeneTreeiENSGT00760000118901.
HOGENOMiHOG000233018.
HOVERGENiHBG012180.
InParanoidiP02585.
KOiK12042.
OMAiMTDAQQE.
OrthoDBiEOG76X61W.
PhylomeDBiP02585.
TreeFamiTF318191.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 4 hits.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 4 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02585-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDQQAEARS YLSEEMIAEF KAAFDMFDAD GGGDISVKEL GTVMRMLGQT
60 70 80 90 100
PTKEELDAII EEVDEDGSGT IDFEEFLVMM VRQMKEDAKG KSEEELAECF
110 120 130 140 150
RIFDRNADGY IDPEELAEIF RASGEHVTDE EIESLMKDGD KNNDGRIDFD
160
EFLKMMEGVQ
Length:160
Mass (Da):18,122
Last modified:January 23, 2007 - v2
Checksum:iEA93729732A0F916
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 32TD → DT AA sequence (PubMed:978749).Curated
Sequence conflicti114 – 1141E → G in AAA91854 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07898 mRNA. Translation: CAA30737.1.
M33772, M33771 Genomic DNA. Translation: AAA61197.1.
M22307 mRNA. Translation: AAA91854.1.
AK291323 mRNA. Translation: BAF84012.1.
CR541864 mRNA. Translation: CAG46662.1.
CR541884 mRNA. Translation: CAG46682.1.
CH471077 Genomic DNA. Translation: EAW75803.1.
AL050348 Genomic DNA. No translation available.
BC005323 mRNA. Translation: AAH05323.1.
CCDSiCCDS13375.1.
PIRiA36574. TPHUCS.
RefSeqiNP_003270.1. NM_003279.2.
UniGeneiHs.182421.

Genome annotation databases

EnsembliENST00000372555; ENSP00000361636; ENSG00000101470.
GeneIDi7125.
KEGGihsa:7125.
UCSCiuc002xpr.3. human.

Polymorphism databases

DMDMi136043.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07898 mRNA. Translation: CAA30737.1.
M33772, M33771 Genomic DNA. Translation: AAA61197.1.
M22307 mRNA. Translation: AAA91854.1.
AK291323 mRNA. Translation: BAF84012.1.
CR541864 mRNA. Translation: CAG46662.1.
CR541884 mRNA. Translation: CAG46682.1.
CH471077 Genomic DNA. Translation: EAW75803.1.
AL050348 Genomic DNA. No translation available.
BC005323 mRNA. Translation: AAH05323.1.
CCDSiCCDS13375.1.
PIRiA36574. TPHUCS.
RefSeqiNP_003270.1. NM_003279.2.
UniGeneiHs.182421.

3D structure databases

ProteinModelPortaliP02585.
SMRiP02585. Positions 3-160.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112980. 2 interactions.
STRINGi9606.ENSP00000361636.

Chemistry

DrugBankiDB01023. Felodipine.

PTM databases

PhosphoSiteiP02585.

Polymorphism databases

DMDMi136043.

Proteomic databases

PaxDbiP02585.
PRIDEiP02585.

Protocols and materials databases

DNASUi7125.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000372555; ENSP00000361636; ENSG00000101470.
GeneIDi7125.
KEGGihsa:7125.
UCSCiuc002xpr.3. human.

Organism-specific databases

CTDi7125.
GeneCardsiGC20M044451.
HGNCiHGNC:11944. TNNC2.
HPAiHPA043174.
MIMi191039. gene.
neXtProtiNX_P02585.
PharmGKBiPA36633.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5126.
GeneTreeiENSGT00760000118901.
HOGENOMiHOG000233018.
HOVERGENiHBG012180.
InParanoidiP02585.
KOiK12042.
OMAiMTDAQQE.
OrthoDBiEOG76X61W.
PhylomeDBiP02585.
TreeFamiTF318191.

Enzyme and pathway databases

ReactomeiREACT_16969. Striated Muscle Contraction.

Miscellaneous databases

ChiTaRSiTNNC2. human.
GeneWikiiTNNC2.
GenomeRNAii7125.
NextBioi27883.
PROiP02585.
SOURCEiSearch...

Gene expression databases

BgeeiP02585.
CleanExiHS_TNNC2.
ExpressionAtlasiP02585. baseline.
GenevestigatoriP02585.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 4 hits.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 4 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Differential expression of slow and fast skeletal muscle troponin C. Slow skeletal muscle troponin C is expressed in human fibroblasts."
    Gahlmann R., Wade R., Gunning R., Kedes L.
    J. Mol. Biol. 201:379-391(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning, structural analysis, and expression of the human fast twitch skeletal muscle troponin C gene."
    Gahlmann R., Kedes L.
    J. Biol. Chem. 265:12520-12528(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Wu Q.L.
    Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Muscle.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Tongue.
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  9. "Human skeletal muscle proteins. The primary structure of troponin C."
    Romero-Herrera A.E., Castillo O., Lehmann H.
    J. Mol. Evol. 8:251-270(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-160, ACETYLATION AT THR-2.
    Tissue: Skeletal muscle.

Entry informationi

Entry nameiTNNC2_HUMAN
AccessioniPrimary (citable) accession number: P02585
Secondary accession number(s): Q6FH92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Skeletal muscle troponin C binds four calcium ions.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.