ID TNNI3_HUMAN Reviewed; 210 AA. AC P19429; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 220. DE RecName: Full=Troponin I, cardiac muscle; DE AltName: Full=Cardiac troponin I; GN Name=TNNI3; Synonyms=TNNC1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Heart muscle; RX PubMed=2226790; DOI=10.1016/0014-5793(90)81234-f; RA Vallins W.J., Brand N.J., Dabhade N., Butler-Browne G., Yacoub M.H., RA Barton P.J.R.; RT "Molecular cloning of human cardiac troponin I using polymerase chain RT reaction."; RL FEBS Lett. 270:57-61(1990). RN [2] RP SEQUENCE REVISION TO 85, AND NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8406024; DOI=10.1016/0378-1119(93)90308-p; RA Armour K.L., Harris W.J., Tempest P.R.; RT "Cloning and expression in Escherichia coli of the cDNA encoding human RT cardiac troponin I."; RL Gene 131:287-292(1993). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1934363; DOI=10.1161/01.res.69.5.1409; RA Hunkeler N.M., Kullman J., Murphy A.M.; RT "Troponin I isoform expression in human heart."; RL Circ. Res. 69:1409-1414(1991). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8661099; DOI=10.1006/geno.1996.0317; RA Bhavsar P.K., Brand N.J., Yacoub M.H., Barton P.J.R.; RT "Isolation and characterization of the human cardiac troponin I gene RT (TNNI3)."; RL Genomics 35:11-23(1996). RN [5] RP PROTEIN SEQUENCE OF 11-36, ACETYLATION AT ALA-2, AND PHOSPHORYLATION AT RP SER-23 AND SER-24. RX PubMed=2226863; DOI=10.1016/0014-5793(90)81046-q; RA Mittmann K., Jaquet K., Heilmeyer L.M.G. Jr.; RT "A common motif of two adjacent phosphoserines in bovine, rabbit and human RT cardiac troponin I."; RL FEBS Lett. 273:41-45(1990). RN [6] RP PHOSPHORYLATION AT SER-23 AND SER-24. RX PubMed=9346285; DOI=10.1111/j.1432-1033.1997.00329.x; RA Keane N.E., Quirk P.G., Gao Y., Patchell V.B., Perry S.V., Levine B.A.; RT "The ordered phosphorylation of cardiac troponin I by the cAMP-dependent RT protein kinase -- structural consequences and functional implications."; RL Eur. J. Biochem. 248:329-337(1997). RN [7] RP PHOSPHORYLATION AT SER-150 BY PAK3. RX PubMed=12242269; DOI=10.1161/01.res.0000035246.27856.53; RA Buscemi N., Foster D.B., Neverova I., Van Eyk J.E.; RT "p21-activated kinase increases the calcium sensitivity of rat triton- RT skinned cardiac muscle fiber bundles via a mechanism potentially involving RT novel phosphorylation of troponin I."; RL Circ. Res. 91:509-516(2002). RN [8] RP PHOSPHORYLATION AT SER-23 AND SER-24. RX PubMed=15514163; DOI=10.1161/01.res.0000149299.34793.3c; RA Haworth R.S., Cuello F., Herron T.J., Franzen G., Kentish J.C., Gautel M., RA Avkiran M.; RT "Protein kinase D is a novel mediator of cardiac troponin I phosphorylation RT and regulates myofilament function."; RL Circ. Res. 95:1091-1099(2004). RN [9] RP INTERACTION WITH TRIM63. RX PubMed=15601779; DOI=10.1073/pnas.0404341102; RA Kedar V., McDonough H., Arya R., Li H.-H., Rockman H.A., Patterson C.; RT "Muscle-specific RING finger 1 is a bona fide ubiquitin ligase that RT degrades cardiac troponin I."; RL Proc. Natl. Acad. Sci. U.S.A. 101:18135-18140(2004). RN [10] RP INTERACTION WITH STK4/MST1, AND PHOSPHORYLATION AT THR-31; THR-51; THR-129 RP AND THR-143. RX PubMed=18986304; DOI=10.1042/bj20081340; RA You B., Yan G., Zhang Z., Yan L., Li J., Ge Q., Jin J.P., Sun J.; RT "Phosphorylation of cardiac troponin I by mammalian sterile 20-like kinase RT 1."; RL Biochem. J. 418:93-101(2009). RN [11] RP PHOSPHORYLATION AT SER-5; SER-6; SER-23; SER-24; TYR-26; SER-42; SER-44; RP THR-51; SER-77; THR-78; THR-143; SER-166; THR-181 AND SER-199. RX PubMed=22972900; DOI=10.1161/circulationaha.112.096388; RA Zhang P., Kirk J.A., Ji W., dos Remedios C.G., Kass D.A., Van Eyk J.E., RA Murphy A.M.; RT "Multiple reaction monitoring to identify site-specific troponin I RT phosphorylated residues in the failing human heart."; RL Circulation 126:1828-1837(2012). RN [12] RP STRUCTURE BY NMR OF 148-164. RX PubMed=10387074; DOI=10.1021/bi9901679; RA Li M.X., Spyracopoulos L., Sykes B.D.; RT "Binding of cardiac troponin-I147-163 induces a structural opening in human RT cardiac troponin-C."; RL Biochemistry 38:8289-8298(1999). RN [13] RP STRUCTURE BY NMR OF 149-165 IN COMPLEX WITH CARDIAC TROPONIN C. RX PubMed=12060657; DOI=10.1074/jbc.m203896200; RA Wang X., Li M.X., Sykes B.D.; RT "Structure of the regulatory N-domain of human cardiac troponin C in RT complex with human cardiac troponin I147-163 and bepridil."; RL J. Biol. Chem. 277:31124-31133(2002). RN [14] RP VARIANTS CMH7 GLY-145 AND GLN-206. RX PubMed=9241277; DOI=10.1038/ng0897-379; RA Kimura A., Harada H., Park J.-E., Nishi H., Satoh M., Takahashi M., RA Hiroi S., Sasaoka T., Ohbuchi N., Nakamura T., Koyanagi T., Hwang T.-H., RA Choo J., Chung K.-S., Hasegawa A., Nagai R., Okazaki O., Nakamura H., RA Matsuzaki M., Sakamoto T., Toshima H., Koga Y., Imaizumi T., Sasazuki T.; RT "Mutations in the cardiac troponin I gene associated with hypertrophic RT cardiomyopathy."; RL Nat. Genet. 16:379-382(1997). RN [15] RP VARIANT CMH7 ASN-196, AND VARIANT SER-82. RX PubMed=11815426; DOI=10.1161/hc0402.102990; RA Niimura H., Patton K.K., McKenna W.J., Soults J., Maron B.J., Seidman J.G., RA Seidman C.E.; RT "Sarcomere protein gene mutations in hypertrophic cardiomyopathy of the RT elderly."; RL Circulation 105:446-451(2002). RN [16] RP VARIANTS RCM1 GLN-144; TRP-145; THR-171; GLU-178; HIS-190 AND HIS-192. RX PubMed=12531876; DOI=10.1172/jci16336; RA Mogensen J., Kubo T., Duque M., Uribe W., Shaw A., Murphy R., Gimeno J.R., RA Elliott P., McKenna W.J.; RT "Idiopathic restrictive cardiomyopathy is part of the clinical expression RT of cardiac troponin I mutations."; RL J. Clin. Invest. 111:209-216(2003). RN [17] RP VARIANTS CMH7 GLN-141; VAL-157; PRO-162; LYS-177 DEL; GLN-186 AND ASN-196. RX PubMed=12707239; DOI=10.1161/01.cir.0000066323.15244.54; RA Richard P., Charron P., Carrier L., Ledeuil C., Cheav T., Pichereau C., RA Benaiche A., Isnard R., Dubourg O., Burban M., Gueffet J.-P., Millaire A., RA Desnos M., Schwartz K., Hainque B., Komajda M.; RT "Hypertrophic cardiomyopathy: distribution of disease genes, spectrum of RT mutations, and implications for a molecular diagnosis strategy."; RL Circulation 107:2227-2232(2003). RN [18] RP ERRATUM OF PUBMED:12707239. RA Richard P., Charron P., Carrier L., Ledeuil C., Cheav T., Pichereau C., RA Benaiche A., Isnard R., Dubourg O., Burban M., Gueffet J.-P., Millaire A., RA Desnos M., Schwartz K., Hainque B., Komajda M.; RL Circulation 109:3258-3258(2004). RN [19] RP VARIANT CMH7 PHE-166. RX PubMed=12974739; DOI=10.1034/j.1399-0004.2003.00151.x; RA Erdmann J., Daehmlow S., Wischke S., Senyuva M., Werner U., Raible J., RA Tanis N., Dyachenko S., Hummel M., Hetzer R., Regitz-Zagrosek V.; RT "Mutation spectrum in a large cohort of unrelated consecutive patients with RT hypertrophic cardiomyopathy."; RL Clin. Genet. 64:339-349(2003). RN [20] RP VARIANT CMD2A VAL-2. RX PubMed=15070570; DOI=10.1016/s0140-6736(04)15468-8; RA Murphy R.T., Mogensen J., Shaw A., Kubo T., Hughes S., McKenna W.J.; RT "Novel mutation in cardiac troponin I in recessive idiopathic dilated RT cardiomyopathy."; RL Lancet 363:371-372(2004). RN [21] RP VARIANTS CMH7 PRO-162; GLN-162 AND HIS-204. RX PubMed=16199542; DOI=10.1136/jmg.2005.033886; RA Ingles J., Doolan A., Chiu C., Seidman J., Seidman C., Semsarian C.; RT "Compound and double mutations in patients with hypertrophic RT cardiomyopathy: implications for genetic testing and counselling."; RL J. Med. Genet. 42:E59-E59(2005). RN [22] RP VARIANTS CMD1FF GLN-36 AND LYS-185. RX PubMed=19590045; DOI=10.1161/circresaha.109.196055; RA Carballo S., Robinson P., Otway R., Fatkin D., Jongbloed J.D., de Jonge N., RA Blair E., van Tintelen J.P., Redwood C., Watkins H.; RT "Identification and functional characterization of cardiac troponin I as a RT novel disease gene in autosomal dominant dilated cardiomyopathy."; RL Circ. Res. 105:375-382(2009). RN [23] RP VARIANT CMD1FF GLY-116. RX PubMed=21846512; DOI=10.1016/j.ejmg.2011.07.005; RA Millat G., Bouvagnet P., Chevalier P., Sebbag L., Dulac A., Dauphin C., RA Jouk P.S., Delrue M.A., Thambo J.B., Le Metayer P., Seronde M.F., RA Faivre L., Eicher J.C., Rousson R.; RT "Clinical and mutational spectrum in a cohort of 105 unrelated patients RT with dilated cardiomyopathy."; RL Eur. J. Med. Genet. 54:E570-E575(2011). CC -!- FUNCTION: Troponin I is the inhibitory subunit of troponin, the thin CC filament regulatory complex which confers calcium-sensitivity to CC striated muscle actomyosin ATPase activity. CC -!- SUBUNIT: Binds to actin and tropomyosin. Interacts with TRIM63. CC Interacts with STK4/MST1. {ECO:0000269|PubMed:12060657, CC ECO:0000269|PubMed:15601779, ECO:0000269|PubMed:18986304}. CC -!- INTERACTION: CC P19429; Q5VU43-11: PDE4DIP; NbExp=4; IntAct=EBI-704146, EBI-10769071; CC P19429; O43933: PEX1; NbExp=3; IntAct=EBI-704146, EBI-988601; CC P19429; A6NK89: RASSF10; NbExp=3; IntAct=EBI-704146, EBI-6912267; CC P19429; Q9UKA8-1: RCAN3; NbExp=3; IntAct=EBI-704146, EBI-10762111; CC P19429; Q9UKA8-4: RCAN3; NbExp=2; IntAct=EBI-704146, EBI-10762136; CC P19429; P02585: TNNC2; NbExp=3; IntAct=EBI-704146, EBI-10249681; CC P19429; Q59H18: TNNI3K; NbExp=2; IntAct=EBI-704146, EBI-704142; CC P19429; Q59H18-2: TNNI3K; NbExp=2; IntAct=EBI-704146, EBI-10762055; CC P19429; O76024: WFS1; NbExp=3; IntAct=EBI-704146, EBI-720609; CC -!- PTM: Phosphorylated at Ser-42 and Ser-44 by PRKCE; phosphorylation CC increases myocardium contractile dysfunction (By similarity). CC Phosphorylated at Ser-23 and Ser-24 by PRKD1; phosphorylation reduces CC myofilament calcium sensitivity. Phosphorylated preferentially at Thr- CC 31. Phosphorylation by STK4/MST1 alters its binding affinity to TNNC1 CC (cardiac Tn-C) and TNNT2 (cardiac Tn-T). {ECO:0000250, CC ECO:0000269|PubMed:12242269, ECO:0000269|PubMed:15514163, CC ECO:0000269|PubMed:18986304, ECO:0000269|PubMed:2226863, CC ECO:0000269|PubMed:22972900, ECO:0000269|PubMed:9346285}. CC -!- DISEASE: Cardiomyopathy, familial hypertrophic, 7 (CMH7) [MIM:613690]: CC A hereditary heart disorder characterized by ventricular hypertrophy, CC which is usually asymmetric and often involves the interventricular CC septum. The symptoms include dyspnea, syncope, collapse, palpitations, CC and chest pain. They can be readily provoked by exercise. The disorder CC has inter- and intrafamilial variability ranging from benign to CC malignant forms with high risk of cardiac failure and sudden cardiac CC death. {ECO:0000269|PubMed:11815426, ECO:0000269|PubMed:12707239, CC ECO:0000269|PubMed:12974739, ECO:0000269|PubMed:16199542, CC ECO:0000269|PubMed:9241277}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Cardiomyopathy, familial restrictive 1 (RCM1) [MIM:115210]: A CC heart disorder characterized by impaired filling of the ventricles with CC reduced diastolic volume, in the presence of normal or near normal wall CC thickness and systolic function. {ECO:0000269|PubMed:12531876}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- DISEASE: Cardiomyopathy, dilated, 2A (CMD2A) [MIM:611880]: A disorder CC characterized by ventricular dilation and impaired systolic function, CC resulting in congestive heart failure and arrhythmia. Patients are at CC risk of premature death. {ECO:0000269|PubMed:19590045, CC ECO:0000269|PubMed:21846512}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Cardiomyopathy, dilated, 1FF (CMD1FF) [MIM:613286]: A disorder CC characterized by ventricular dilation and impaired systolic function, CC resulting in congestive heart failure and arrhythmia. Patients are at CC risk of premature death. {ECO:0000269|PubMed:19590045, CC ECO:0000269|PubMed:21846512}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the troponin I family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X54163; CAA38102.1; -; mRNA. DR EMBL; M64247; AAA16157.1; -; mRNA. DR EMBL; X90780; CAA62301.1; -; Genomic_DNA. DR CCDS; CCDS42628.1; -. DR PIR; A61229; TPHUIC. DR RefSeq; NP_000354.4; NM_000363.4. DR PDB; 1J1D; X-ray; 2.61 A; C/F=31-163. DR PDB; 1J1E; X-ray; 3.30 A; C/F=31-210. DR PDB; 1LXF; NMR; -; I=148-164. DR PDB; 1MXL; NMR; -; I=148-164. DR PDB; 1OZS; NMR; -; B=129-148. DR PDB; 2KGB; NMR; -; I=145-164. DR PDB; 2KRD; NMR; -; I=148-164. DR PDB; 2L1R; NMR; -; B=145-164. DR PDB; 2MZP; NMR; -; I=145-171. DR PDB; 2N7L; NMR; -; C=145-174. DR PDB; 4Y99; X-ray; 2.00 A; C=1-210. DR PDB; 5VLN; NMR; -; A=139-164. DR PDB; 5W88; NMR; -; A=133-164. DR PDB; 5WCL; NMR; -; A=139-164. DR PDB; 6KN7; EM; 6.60 A; U/b=41-210. DR PDB; 6KN8; EM; 4.80 A; U/b=41-166. DR PDB; 6MV3; NMR; -; A=139-164. DR PDB; 7JGI; NMR; -; A=139-164. DR PDB; 7SC2; X-ray; 1.81 A; A=139-164. DR PDB; 7SC3; X-ray; 2.23 A; A=139-164. DR PDB; 7SUP; NMR; -; A=147-180. DR PDB; 7SVC; NMR; -; A=147-180. DR PDB; 7SWG; NMR; -; A=147-180. DR PDB; 7SWI; NMR; -; A=147-180. DR PDB; 7SXC; NMR; -; A=147-180. DR PDB; 7SXD; NMR; -; A=147-180. DR PDB; 7UH9; NMR; -; A=139-164. DR PDB; 7UHA; NMR; -; A=139-164. DR PDB; 7UTI; EM; 4.80 A; V/a=1-210. DR PDB; 7UTL; EM; 6.60 A; V/c=1-210. DR PDB; 8DZV; X-ray; 1.20 A; C=40-52. DR PDBsum; 1J1D; -. DR PDBsum; 1J1E; -. DR PDBsum; 1LXF; -. DR PDBsum; 1MXL; -. DR PDBsum; 1OZS; -. DR PDBsum; 2KGB; -. DR PDBsum; 2KRD; -. DR PDBsum; 2L1R; -. DR PDBsum; 2MZP; -. DR PDBsum; 2N7L; -. DR PDBsum; 4Y99; -. DR PDBsum; 5VLN; -. DR PDBsum; 5W88; -. DR PDBsum; 5WCL; -. DR PDBsum; 6KN7; -. DR PDBsum; 6KN8; -. DR PDBsum; 6MV3; -. DR PDBsum; 7JGI; -. DR PDBsum; 7SC2; -. DR PDBsum; 7SC3; -. DR PDBsum; 7SUP; -. DR PDBsum; 7SVC; -. DR PDBsum; 7SWG; -. DR PDBsum; 7SWI; -. DR PDBsum; 7SXC; -. DR PDBsum; 7SXD; -. DR PDBsum; 7UH9; -. DR PDBsum; 7UHA; -. DR PDBsum; 7UTI; -. DR PDBsum; 7UTL; -. DR PDBsum; 8DZV; -. DR AlphaFoldDB; P19429; -. DR BMRB; P19429; -. DR EMDB; EMD-0728; -. DR EMDB; EMD-0729; -. DR SMR; P19429; -. DR BioGRID; 112991; 19. DR ComplexPortal; CPX-3280; Cardiac Troponin complex. DR DIP; DIP-34065N; -. DR IntAct; P19429; 23. DR MINT; P19429; -. DR STRING; 9606.ENSP00000341838; -. DR ChEMBL; CHEMBL2095202; -. DR DrugBank; DB04513; N-(6-Aminohexyl)-5-Chloro-1-Naphthalenesulfonamide. DR GlyGen; P19429; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P19429; -. DR PhosphoSitePlus; P19429; -. DR BioMuta; TNNI3; -. DR DMDM; 136213; -. DR MassIVE; P19429; -. DR PaxDb; 9606-ENSP00000341838; -. DR PeptideAtlas; P19429; -. DR ProteomicsDB; 53658; -. DR ABCD; P19429; 5 sequenced antibodies. DR Antibodypedia; 4354; 2810 antibodies from 52 providers. DR CPTC; P19429; 1 antibody. DR DNASU; 7137; -. DR Ensembl; ENST00000344887.10; ENSP00000341838.5; ENSG00000129991.13. DR GeneID; 7137; -. DR KEGG; hsa:7137; -. DR MANE-Select; ENST00000344887.10; ENSP00000341838.5; NM_000363.5; NP_000354.4. DR AGR; HGNC:11947; -. DR CTD; 7137; -. DR DisGeNET; 7137; -. DR GeneCards; TNNI3; -. DR GeneReviews; TNNI3; -. DR HGNC; HGNC:11947; TNNI3. DR HPA; ENSG00000129991; Tissue enriched (heart). DR MalaCards; TNNI3; -. DR MIM; 115210; phenotype. DR MIM; 191044; gene. DR MIM; 611880; phenotype. DR MIM; 613286; phenotype. DR MIM; 613690; phenotype. DR neXtProt; NX_P19429; -. DR OpenTargets; ENSG00000129991; -. DR Orphanet; 154; Familial isolated dilated cardiomyopathy. DR Orphanet; 75249; Familial isolated restrictive cardiomyopathy. DR Orphanet; 155; NON RARE IN EUROPE: Familial isolated hypertrophic cardiomyopathy. DR PharmGKB; PA36636; -. DR VEuPathDB; HostDB:ENSG00000129991; -. DR eggNOG; KOG3977; Eukaryota. DR GeneTree; ENSGT01030000234588; -. DR InParanoid; P19429; -. DR OrthoDB; 2882372at2759; -. DR PhylomeDB; P19429; -. DR TreeFam; TF313374; -. DR PathwayCommons; P19429; -. DR Reactome; R-HSA-390522; Striated Muscle Contraction. DR Reactome; R-HSA-5578775; Ion homeostasis. DR SignaLink; P19429; -. DR SIGNOR; P19429; -. DR BioGRID-ORCS; 7137; 18 hits in 1156 CRISPR screens. DR ChiTaRS; TNNI3; human. DR EvolutionaryTrace; P19429; -. DR GeneWiki; TNNI3; -. DR GenomeRNAi; 7137; -. DR Pharos; P19429; Tbio. DR PRO; PR:P19429; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; P19429; Protein. DR Bgee; ENSG00000129991; Expressed in apex of heart and 101 other cell types or tissues. DR ExpressionAtlas; P19429; baseline and differential. DR GO; GO:0097512; C:cardiac myofibril; IMP:CAFA. DR GO; GO:1990584; C:cardiac Troponin complex; IMP:CAFA. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0030017; C:sarcomere; TAS:BHF-UCL. DR GO; GO:0005861; C:troponin complex; IDA:UniProtKB. DR GO; GO:0003779; F:actin binding; IDA:UniProtKB. DR GO; GO:0051015; F:actin filament binding; IPI:CAFA. DR GO; GO:0019855; F:calcium channel inhibitor activity; IPI:UniProtKB. DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB. DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB. DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB. DR GO; GO:0030172; F:troponin C binding; IPI:UniProtKB. DR GO; GO:0031014; F:troponin T binding; IPI:UniProtKB. DR GO; GO:0060048; P:cardiac muscle contraction; IMP:UniProtKB. DR GO; GO:0060047; P:heart contraction; IMP:UniProtKB. DR GO; GO:0007507; P:heart development; ISS:UniProtKB. DR GO; GO:0006874; P:intracellular calcium ion homeostasis; ISS:UniProtKB. DR GO; GO:0032780; P:negative regulation of ATP-dependent activity; IDA:UniProtKB. DR GO; GO:0010882; P:regulation of cardiac muscle contraction by calcium ion signaling; IMP:CAFA. DR GO; GO:0006940; P:regulation of smooth muscle contraction; IEA:Ensembl. DR GO; GO:0001980; P:regulation of systemic arterial blood pressure by ischemic conditions; ISS:UniProtKB. DR GO; GO:0003009; P:skeletal muscle contraction; IBA:GO_Central. DR GO; GO:0001570; P:vasculogenesis; ISS:UniProtKB. DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IMP:HGNC-UCL. DR DisProt; DP00166; -. DR Gene3D; 1.20.5.350; -; 1. DR Gene3D; 6.10.250.180; -; 1. DR InterPro; IPR001978; Troponin. DR InterPro; IPR021666; Troponin-I_N. DR InterPro; IPR038077; Troponin_sf. DR PANTHER; PTHR13738; TROPONIN I; 1. DR PANTHER; PTHR13738:SF2; TROPONIN I, CARDIAC MUSCLE; 1. DR Pfam; PF00992; Troponin; 1. DR Pfam; PF11636; Troponin-I_N; 1. DR SUPFAM; SSF90250; Troponin coil-coiled subunits; 1. DR Genevisible; P19429; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Actin-binding; Cardiomyopathy; KW Direct protein sequencing; Disease variant; Muscle protein; Phosphoprotein; KW Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:2226863" FT CHAIN 2..210 FT /note="Troponin I, cardiac muscle" FT /id="PRO_0000186151" FT REGION 1..43 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 32..79 FT /note="Involved in binding TNC" FT REGION 129..149 FT /note="Involved in binding TNC and actin" FT SITE 80 FT /note="Involved in TNI-TNT interactions" FT SITE 97 FT /note="Involved in TNI-TNT interactions" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|PubMed:2226863" FT MOD_RES 5 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:22972900" FT MOD_RES 6 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:22972900" FT MOD_RES 23 FT /note="Phosphoserine; by PKA and PKD/PRKD1" FT /evidence="ECO:0000269|PubMed:15514163, FT ECO:0000269|PubMed:2226863, ECO:0000269|PubMed:22972900, FT ECO:0000269|PubMed:9346285" FT MOD_RES 24 FT /note="Phosphoserine; by PKA and PKD/PRKD1" FT /evidence="ECO:0000269|PubMed:15514163, FT ECO:0000269|PubMed:2226863, ECO:0000269|PubMed:22972900, FT ECO:0000269|PubMed:9346285" FT MOD_RES 26 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:22972900" FT MOD_RES 31 FT /note="Phosphothreonine; by STK4/MST1" FT /evidence="ECO:0000269|PubMed:18986304" FT MOD_RES 42 FT /note="Phosphoserine; by PKC/PRKCE" FT /evidence="ECO:0000250|UniProtKB:P48787" FT MOD_RES 44 FT /note="Phosphoserine; by PKC/PRKCE" FT /evidence="ECO:0000250|UniProtKB:P48787" FT MOD_RES 51 FT /note="Phosphothreonine; by STK4/MST1" FT /evidence="ECO:0000269|PubMed:18986304, FT ECO:0000269|PubMed:22972900" FT MOD_RES 77 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:22972900" FT MOD_RES 78 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:22972900" FT MOD_RES 129 FT /note="Phosphothreonine; by STK4/MST1" FT /evidence="ECO:0000269|PubMed:18986304" FT MOD_RES 143 FT /note="Phosphothreonine; by STK4/MST1" FT /evidence="ECO:0000269|PubMed:18986304, FT ECO:0000269|PubMed:22972900" FT MOD_RES 150 FT /note="Phosphoserine; by PAK3" FT /evidence="ECO:0000269|PubMed:12242269" FT MOD_RES 166 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:22972900" FT MOD_RES 181 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:22972900" FT MOD_RES 199 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:22972900" FT VARIANT 2 FT /note="A -> V (in CMD2A; dbSNP:rs397516359)" FT /evidence="ECO:0000269|PubMed:15070570" FT /id="VAR_043989" FT VARIANT 36 FT /note="K -> Q (in CMD1FF; dbSNP:rs267607130)" FT /evidence="ECO:0000269|PubMed:19590045" FT /id="VAR_063548" FT VARIANT 79 FT /note="R -> C (in dbSNP:rs3729712)" FT /id="VAR_029453" FT VARIANT 82 FT /note="P -> S (risk factor for CMH7; dbSNP:rs77615401)" FT /evidence="ECO:0000269|PubMed:11815426" FT /id="VAR_016078" FT VARIANT 116 FT /note="A -> G (in CMD1FF; dbSNP:rs777177571)" FT /evidence="ECO:0000269|PubMed:21846512" FT /id="VAR_067264" FT VARIANT 141 FT /note="R -> Q (in CMH7; dbSNP:rs397516347)" FT /evidence="ECO:0000269|PubMed:12707239" FT /id="VAR_019872" FT VARIANT 144 FT /note="L -> Q (in RCM1; dbSNP:rs121917760)" FT /evidence="ECO:0000269|PubMed:12531876" FT /id="VAR_016079" FT VARIANT 145 FT /note="R -> G (in CMH7; dbSNP:rs104894724)" FT /evidence="ECO:0000269|PubMed:9241277" FT /id="VAR_007603" FT VARIANT 145 FT /note="R -> W (in RCM1; dbSNP:rs104894724)" FT /evidence="ECO:0000269|PubMed:12531876" FT /id="VAR_016080" FT VARIANT 157 FT /note="A -> V (in CMH7; dbSNP:rs397516353)" FT /evidence="ECO:0000269|PubMed:12707239" FT /id="VAR_019873" FT VARIANT 162 FT /note="R -> P (in CMH7; dbSNP:rs397516354)" FT /evidence="ECO:0000269|PubMed:12707239, FT ECO:0000269|PubMed:16199542" FT /id="VAR_019874" FT VARIANT 162 FT /note="R -> Q (in CMH7; dbSNP:rs397516354)" FT /evidence="ECO:0000269|PubMed:16199542" FT /id="VAR_042745" FT VARIANT 166 FT /note="S -> F (in CMH7; dbSNP:rs727504242)" FT /evidence="ECO:0000269|PubMed:12974739" FT /id="VAR_029454" FT VARIANT 171 FT /note="A -> T (in RCM1; dbSNP:rs121917761)" FT /evidence="ECO:0000269|PubMed:12531876" FT /id="VAR_016081" FT VARIANT 177 FT /note="Missing (in CMH7)" FT /evidence="ECO:0000269|PubMed:12707239" FT /id="VAR_019875" FT VARIANT 178 FT /note="K -> E (in RCM1; dbSNP:rs104894730)" FT /evidence="ECO:0000269|PubMed:12531876" FT /id="VAR_016082" FT VARIANT 185 FT /note="N -> K (in CMD1FF; dbSNP:rs267607129)" FT /evidence="ECO:0000269|PubMed:19590045" FT /id="VAR_063549" FT VARIANT 186 FT /note="R -> Q (in CMH7; dbSNP:rs397516357)" FT /evidence="ECO:0000269|PubMed:12707239" FT /id="VAR_019876" FT VARIANT 190 FT /note="D -> H (in CMH7 and RCM1)" FT /evidence="ECO:0000269|PubMed:12531876" FT /id="VAR_016083" FT VARIANT 192 FT /note="R -> H (in RCM1; dbSNP:rs104894729)" FT /evidence="ECO:0000269|PubMed:12531876" FT /id="VAR_016084" FT VARIANT 196 FT /note="D -> N (in CMH7; dbSNP:rs104894727)" FT /evidence="ECO:0000269|PubMed:11815426, FT ECO:0000269|PubMed:12707239" FT /id="VAR_016085" FT VARIANT 204 FT /note="R -> H (in CMH7; dbSNP:rs727504275)" FT /evidence="ECO:0000269|PubMed:16199542" FT /id="VAR_042746" FT VARIANT 206 FT /note="K -> Q (in CMH7; dbSNP:rs104894725)" FT /evidence="ECO:0000269|PubMed:9241277" FT /id="VAR_007604" FT HELIX 43..50 FT /evidence="ECO:0007829|PDB:8DZV" FT HELIX 85..87 FT /evidence="ECO:0007829|PDB:1J1E" FT HELIX 90..136 FT /evidence="ECO:0007829|PDB:4Y99" FT HELIX 140..159 FT /evidence="ECO:0007829|PDB:7SC2" FT HELIX 160..162 FT /evidence="ECO:0007829|PDB:4Y99" FT HELIX 163..188 FT /evidence="ECO:0007829|PDB:1J1E" SQ SEQUENCE 210 AA; 24008 MW; 20A804F8C24AE1B0 CRC64; MADGSSDAAR EPRPAPAPIR RRSSNYRAYA TEPHAKKKSK ISASRKLQLK TLLLQIAKQE LEREAEERRG EKGRALSTRC QPLELAGLGF AELQDLCRQL HARVDKVDEE RYDIEAKVTK NITEIADLTQ KIFDLRGKFK RPTLRRVRIS ADAMMQALLG ARAKESLDLR AHLKQVKKED TEKENREVGD WRKNIDALSG MEGRKKKFES //