P02585 (TNNC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Troponin C, skeletal muscle

Gene names

Name:

TNNC2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	160 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Miscellaneous	Skeletal muscle troponin C binds four calcium ions.
Sequence similarities	Belongs to the troponin C family. Contains 4 EF-hand domains.

Ontologies

Keywords
Domain	Repeat
Ligand	Calcium Metal-binding
Molecular function	Muscle protein
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	muscle filament sliding Traceable author statement. Source: Reactome regulation of muscle contraction Traceable author statement Ref.2. Source: ProtInc skeletal muscle contraction Inferred from direct assay PubMed 17194691. Source: UniProtKB
Cellular_component	cytosol Traceable author statement. Source: Reactome troponin complex Inferred from direct assay PubMed 17194691. Source: UniProtKB
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.6
	Chain	2 – 160	159	Troponin C, skeletal muscle		PRO_0000073703
Regions
	Domain	15 – 50	36	EF-hand 1
	Domain	51 – 86	36	EF-hand 2
	Domain	91 – 126	36	EF-hand 3
	Domain	127 – 160	34	EF-hand 4
	Calcium binding	28 – 39	12	1
	Calcium binding	64 – 75	12	2
	Calcium binding	104 – 115	12	3
	Calcium binding	140 – 151	12	4
Amino acid modifications
	Modified residue	2	1	N-acetylthreonine Ref.6
Experimental info
	Sequence conflict	2 – 3	2	TD → DT AA sequence Ref.6
	Sequence conflict	114	1	E → G in AAA91854. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P02585 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: EA93729732A0F916	FASTA	160	18,122
	10 20 30 40 50 60 MTDQQAEARS YLSEEMIAEF KAAFDMFDAD GGGDISVKEL GTVMRMLGQT PTKEELDAII 70 80 90 100 110 120 EEVDEDGSGT IDFEEFLVMM VRQMKEDAKG KSEEELAECF RIFDRNADGY IDPEELAEIF 130 140 150 160 RASGEHVTDE EIESLMKDGD KNNDGRIDFD EFLKMMEGVQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"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].
[5]	"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.
[6]	"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. Tissue: Skeletal muscle.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X07898 mRNA. Translation: CAA30737.1. M33772, M33771 Genomic DNA. Translation: AAA61197.1. M22307 mRNA. Translation: AAA91854.1. AL050348 Genomic DNA. No translation available. BC005323 mRNA. Translation: AAH05323.1.
IPI	IPI00219796.
PIR	TPHUCS. A36574.
RefSeq	NP_003270.1. NM_003279.2.
UniGene	Hs.182421.
3D structure databases
ProteinModelPortal	P02585.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000361636.
PTM databases
PhosphoSite	P02585.
Polymorphism databases
DMDM	136043.
Proteomic databases
PaxDb	P02585.
PRIDE	P02585.
Protocols and materials databases
DNASU	7125.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000372555; ENSP00000361636; ENSG00000101470.
GeneID	7125.
KEGG	hsa:7125.
UCSC	uc002xpr.3. human.
Organism-specific databases
CTD	7125.
GeneCards	GC20M044451.
HGNC	HGNC:11944. TNNC2.
HPA	HPA043174.
MIM	191039. gene.
neXtProt	NX_P02585.
PharmGKB	PA36633.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5126.
HOGENOM	HOG000233018.
HOVERGEN	HBG012180.
InParanoid	P02585.
KO	K12042.
OMA	MTDAQQE.
OrthoDB	EOG4Z0B6X.
PhylomeDB	P02585.
Enzyme and pathway databases
Reactome	REACT_17044. Muscle contraction.
Gene expression databases
ArrayExpress	P02585.
Bgee	P02585.
CleanEx	HS_TNNC2.
Genevestigator	P02585.
GermOnline	ENSG00000101470. Homo sapiens.
Family and domain databases
Gene3D	1.10.238.10. 2 hits.
InterPro	IPR011992. EF-hand-like_dom. IPR018247. EF_Hand_1_Ca_BS. IPR002048. EF_hand_dom. [Graphical view]
Pfam	PF13499. EF_hand_5. 1 hit. [Graphical view]
SMART	SM00054. EFh. 4 hits. [Graphical view]
PROSITE	PS00018. EF_HAND_1. 4 hits. PS50222. EF_HAND_2. 4 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	TNNC2. human.
GenomeRNAi	7125.
NextBio	27883.
SOURCE	Search...

Entry information

Entry name

TNNC2_HUMAN

Accession

Primary (citable) accession number: P02585

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 130 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.