TNNI1_HUMAN
ID TNNI1_HUMAN Reviewed; 187 AA.
AC P19237; A6NEH3; A8MSJ0; Q659A5; Q6FGS7; Q6FGW1; Q6ICU2; Q86T57; Q96DT9;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Troponin I, slow skeletal muscle;
DE AltName: Full=Troponin I, slow-twitch isoform;
GN Name=TNNI1;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Skeletal muscle;
RX PubMed=2365354; DOI=10.1016/0888-7543(90)90168-t;
RA Wade R., Eddy R., Shows T.B., Kedes L.;
RT "cDNA sequence, tissue-specific expression, and chromosomal mapping of the
RT human slow-twitch skeletal muscle isoform of troponin I.";
RL Genomics 7:346-357(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC TISSUE=Blood;
RX PubMed=8144655; DOI=10.1016/s0021-9258(17)34109-1;
RA Corin S.J., Juhasz O., Zhu L., Conley P., Kedes L., Wade R.;
RT "Structure and expression of the human slow twitch skeletal muscle troponin
RT I gene.";
RL J. Biol. Chem. 269:10651-10659(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
RA Frigimelica E., Ievolella C., Lanfranchi G.;
RT "Full length sequencing of some human and murine muscular transcripts
RT (Telethon Italy project B41).";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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.
CC -!- INTERACTION:
CC P19237; X5D778: ANKRD11; NbExp=3; IntAct=EBI-746692, EBI-17183751;
CC P19237; Q9H6L4: ARMC7; NbExp=3; IntAct=EBI-746692, EBI-742909;
CC P19237; Q2NKX9: C2orf68; NbExp=3; IntAct=EBI-746692, EBI-11603468;
CC P19237; Q9NPB3: CABP2; NbExp=3; IntAct=EBI-746692, EBI-12011224;
CC P19237; Q9NP86: CABP5; NbExp=3; IntAct=EBI-746692, EBI-10311131;
CC P19237; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-746692, EBI-10171570;
CC P19237; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-746692, EBI-10961624;
CC P19237; Q96GN5: CDCA7L; NbExp=3; IntAct=EBI-746692, EBI-5278764;
CC P19237; Q96LK0: CEP19; NbExp=3; IntAct=EBI-746692, EBI-741885;
CC P19237; O15182: CETN3; NbExp=3; IntAct=EBI-746692, EBI-712959;
CC P19237; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-746692, EBI-11962928;
CC P19237; Q8TEB1: DCAF11; NbExp=3; IntAct=EBI-746692, EBI-2213388;
CC P19237; Q96JC9: EAF1; NbExp=3; IntAct=EBI-746692, EBI-769261;
CC P19237; Q5VUJ9-2: EFCAB2; NbExp=3; IntAct=EBI-746692, EBI-13317131;
CC P19237; Q8N9N8: EIF1AD; NbExp=3; IntAct=EBI-746692, EBI-750700;
CC P19237; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-746692, EBI-744099;
CC P19237; P62508-3: ESRRG; NbExp=3; IntAct=EBI-746692, EBI-12001340;
CC P19237; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-746692, EBI-14069005;
CC P19237; Q969R5: L3MBTL2; NbExp=3; IntAct=EBI-746692, EBI-739909;
CC P19237; O95983-2: MBD3; NbExp=3; IntAct=EBI-746692, EBI-11978579;
CC P19237; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-746692, EBI-348259;
CC P19237; Q99750: MDFI; NbExp=3; IntAct=EBI-746692, EBI-724076;
CC P19237; P55081: MFAP1; NbExp=3; IntAct=EBI-746692, EBI-1048159;
CC P19237; Q8NEH6: MNS1; NbExp=3; IntAct=EBI-746692, EBI-743811;
CC P19237; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-746692, EBI-11522433;
CC P19237; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-746692, EBI-10232538;
CC P19237; Q92569: PIK3R3; NbExp=3; IntAct=EBI-746692, EBI-79893;
CC P19237; Q8ND90: PNMA1; NbExp=6; IntAct=EBI-746692, EBI-302345;
CC P19237; O15160: POLR1C; NbExp=3; IntAct=EBI-746692, EBI-1055079;
CC P19237; O43741: PRKAB2; NbExp=3; IntAct=EBI-746692, EBI-1053424;
CC P19237; P21673: SAT1; NbExp=3; IntAct=EBI-746692, EBI-711613;
CC P19237; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-746692, EBI-748391;
CC P19237; Q5MJ10: SPANXN2; NbExp=3; IntAct=EBI-746692, EBI-12023934;
CC P19237; P63316: TNNC1; NbExp=5; IntAct=EBI-746692, EBI-3906339;
CC P19237; P13805-3: TNNT1; NbExp=3; IntAct=EBI-746692, EBI-12151635;
CC P19237; P45379-11: TNNT2; NbExp=3; IntAct=EBI-746692, EBI-17559309;
CC P19237; P06753: TPM3; NbExp=3; IntAct=EBI-746692, EBI-355607;
CC P19237; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-746692, EBI-725997;
CC P19237; A0A024R8A9: USP20; NbExp=3; IntAct=EBI-746692, EBI-14096082;
CC P19237; P36508: ZNF76; NbExp=3; IntAct=EBI-746692, EBI-7254550;
CC -!- TISSUE SPECIFICITY: Highest levels observed in human skeletal muscle
CC (e.g. gastrocnemious muscle), differentiated cultures of primary human
CC muscle cells and rhabdomyosarcoma cells cultured in low serum medium.
CC Expressed in C2 muscle cell myoblasts and myotubes.
CC {ECO:0000269|PubMed:2365354, ECO:0000269|PubMed:8144655}.
CC -!- SIMILARITY: Belongs to the troponin I family. {ECO:0000305}.
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DR EMBL; J04760; AAA61228.1; -; mRNA.
DR EMBL; L21910; AAC14461.1; -; Genomic_DNA.
DR EMBL; L21906; AAC14461.1; JOINED; Genomic_DNA.
DR EMBL; L21908; AAC14461.1; JOINED; Genomic_DNA.
DR EMBL; L21909; AAC14461.1; JOINED; Genomic_DNA.
DR EMBL; AJ315823; CAC44240.1; -; mRNA.
DR EMBL; CR450301; CAG29297.1; -; mRNA.
DR EMBL; CR541996; CAG46793.1; -; mRNA.
DR EMBL; CR542030; CAG46827.1; -; mRNA.
DR EMBL; AL831820; CAD38534.1; -; mRNA.
DR EMBL; AL831975; CAH56221.1; -; mRNA.
DR EMBL; BX510903; CAD91135.1; -; mRNA.
DR EMBL; AK223588; BAD97308.1; -; mRNA.
DR EMBL; AK311896; BAG34837.1; -; mRNA.
DR EMBL; AC096677; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012600; AAH12600.1; -; mRNA.
DR EMBL; BC012601; AAH12601.1; -; mRNA.
DR CCDS; CCDS1411.1; -.
DR PIR; A53740; TPHUIW.
DR RefSeq; NP_003272.3; NM_003281.3.
DR AlphaFoldDB; P19237; -.
DR SMR; P19237; -.
DR BioGRID; 112989; 53.
DR IntAct; P19237; 42.
DR STRING; 9606.ENSP00000354488; -.
DR iPTMnet; P19237; -.
DR PhosphoSitePlus; P19237; -.
DR BioMuta; TNNI1; -.
DR DMDM; 1351298; -.
DR MassIVE; P19237; -.
DR PaxDb; P19237; -.
DR PeptideAtlas; P19237; -.
DR PRIDE; P19237; -.
DR ProteomicsDB; 53641; -.
DR Antibodypedia; 3993; 395 antibodies from 30 providers.
DR DNASU; 7135; -.
DR Ensembl; ENST00000336092.8; ENSP00000337022.4; ENSG00000159173.19.
DR Ensembl; ENST00000361379.9; ENSP00000354488.4; ENSG00000159173.19.
DR Ensembl; ENST00000367312.5; ENSP00000356281.1; ENSG00000159173.19.
DR GeneID; 7135; -.
DR KEGG; hsa:7135; -.
DR MANE-Select; ENST00000361379.9; ENSP00000354488.4; NM_003281.4; NP_003272.3.
DR UCSC; uc057oib.1; human.
DR CTD; 7135; -.
DR DisGeNET; 7135; -.
DR GeneCards; TNNI1; -.
DR HGNC; HGNC:11945; TNNI1.
DR HPA; ENSG00000159173; Group enriched (skeletal muscle, tongue).
DR MIM; 191042; gene.
DR neXtProt; NX_P19237; -.
DR OpenTargets; ENSG00000159173; -.
DR PharmGKB; PA36634; -.
DR VEuPathDB; HostDB:ENSG00000159173; -.
DR eggNOG; KOG3977; Eukaryota.
DR GeneTree; ENSGT01030000234588; -.
DR InParanoid; P19237; -.
DR OMA; CIHNTRE; -.
DR OrthoDB; 1566919at2759; -.
DR PhylomeDB; P19237; -.
DR TreeFam; TF313374; -.
DR PathwayCommons; P19237; -.
DR Reactome; R-HSA-390522; Striated Muscle Contraction.
DR SignaLink; P19237; -.
DR BioGRID-ORCS; 7135; 8 hits in 1063 CRISPR screens.
DR ChiTaRS; TNNI1; human.
DR GeneWiki; TNNI1; -.
DR GenomeRNAi; 7135; -.
DR Pharos; P19237; Tbio.
DR PRO; PR:P19237; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P19237; protein.
DR Bgee; ENSG00000159173; Expressed in skeletal muscle tissue of rectus abdominis and 123 other tissues.
DR ExpressionAtlas; P19237; baseline and differential.
DR Genevisible; P19237; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005861; C:troponin complex; IEA:InterPro.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0060048; P:cardiac muscle contraction; IBA:GO_Central.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0006942; P:regulation of striated muscle contraction; NAS:UniProtKB.
DR GO; GO:0003009; P:skeletal muscle contraction; IBA:GO_Central.
DR GO; GO:0014883; P:transition between fast and slow fiber; IEA:Ensembl.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IEA:Ensembl.
DR Gene3D; 1.20.5.350; -; 1.
DR InterPro; IPR001978; Troponin.
DR InterPro; IPR038077; Troponin_sf.
DR Pfam; PF00992; Troponin; 1.
DR SUPFAM; SSF90250; SSF90250; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Muscle protein; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02645"
FT CHAIN 2..187
FT /note="Troponin I, slow skeletal muscle"
FT /id="PRO_0000186139"
FT REGION 2..48
FT /note="Involved in binding TNC"
FT REGION 97..118
FT /note="Involved in binding TNC and actin"
FT MOD_RES 2
FT /note="N-acetylproline"
FT /evidence="ECO:0000250|UniProtKB:P02645"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUZ5"
FT VARIANT 67
FT /note="R -> W (in dbSNP:rs2296695)"
FT /id="VAR_052403"
FT CONFLICT 4..5
FT /note="VE -> FQ (in Ref. 8; AC096677)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="W -> R (in Ref. 4; CAG29297)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="D -> A (in Ref. 5; CAD91135)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="K -> R (in Ref. 3; CAC44240)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="K -> T (in Ref. 4; CAG46793)"
FT /evidence="ECO:0000305"
FT CONFLICT 182..183
FT /note="KS -> NA (in Ref. 1; AAA61228 and 4; CAG46827/
FT CAG46793/CAG29297)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 187 AA; 21692 MW; 7A8363CC7559B962 CRC64;
MPEVERKPKI TASRKLLLKS LMLAKAKECW EQEHEEREAE KVRYLAERIP TLQTRGLSLS
ALQDLCRELH AKVEVVDEER YDIEAKCLHN TREIKDLKLK VMDLRGKFKR PPLRRVRVSA
DAMLRALLGS KHKVSMDLRA NLKSVKKEDT EKERPVEVGD WRKNVEAMSG MEGRKKMFDA
AKSPTSQ
