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Troponin I, slow skeletal muscle (Troponin I, slow-twitch isoform)

 TNNI1_HUMAN             Reviewed;         187 AA.
P19237; A6NEH3; A8MSJ0; Q659A5; Q6FGS7; Q6FGW1; Q6ICU2; Q86T57;
Q96DT9;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
27-SEP-2017, entry version 147.
RecName: Full=Troponin I, slow skeletal muscle;
AltName: Full=Troponin I, slow-twitch isoform;
Name=TNNI1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Skeletal muscle;
PubMed=2365354; DOI=10.1016/0888-7543(90)90168-T;
Wade R., Eddy R., Shows T.B., Kedes L.;
"cDNA sequence, tissue-specific expression, and chromosomal mapping of
the human slow-twitch skeletal muscle isoform of troponin I.";
Genomics 7:346-357(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
TISSUE=Blood;
PubMed=8144655;
Corin S.J., Juhasz O., Zhu L., Conley P., Kedes L., Wade R.;
"Structure and expression of the human slow twitch skeletal muscle
troponin I gene.";
J. Biol. Chem. 269:10651-10659(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skeletal muscle;
Frigimelica E., Ievolella C., Lanfranchi G.;
"Full length sequencing of some human and murine muscular transcripts
(Telethon Italy project B41).";
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skeletal muscle;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skeletal muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: Troponin I is the inhibitory subunit of troponin, the
thin filament regulatory complex which confers calcium-sensitivity
to striated muscle actomyosin ATPase activity.
-!- SUBUNIT: Binds to actin and tropomyosin.
-!- INTERACTION:
Q99750:MDFI; NbExp=3; IntAct=EBI-746692, EBI-724076;
Q8ND90:PNMA1; NbExp=5; IntAct=EBI-746692, EBI-302345;
P63316:TNNC1; NbExp=3; IntAct=EBI-746692, EBI-3906339;
-!- TISSUE SPECIFICITY: Highest levels observed in human skeletal
muscle (e.g. gastrocnemious muscle), differentiated cultures of
primary human muscle cells and rhabdomyosarcoma cells cultured in
low serum medium. Expressed in C2 muscle cell myoblasts and
myotubes. {ECO:0000269|PubMed:2365354,
ECO:0000269|PubMed:8144655}.
-!- SIMILARITY: Belongs to the troponin I family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; J04760; AAA61228.1; -; mRNA.
EMBL; L21910; AAC14461.1; -; Genomic_DNA.
EMBL; L21906; AAC14461.1; JOINED; Genomic_DNA.
EMBL; L21908; AAC14461.1; JOINED; Genomic_DNA.
EMBL; L21909; AAC14461.1; JOINED; Genomic_DNA.
EMBL; AJ315823; CAC44240.1; -; mRNA.
EMBL; CR450301; CAG29297.1; -; mRNA.
EMBL; CR541996; CAG46793.1; -; mRNA.
EMBL; CR542030; CAG46827.1; -; mRNA.
EMBL; AL831820; CAD38534.1; -; mRNA.
EMBL; AL831975; CAH56221.1; -; mRNA.
EMBL; BX510903; CAD91135.1; -; mRNA.
EMBL; AK223588; BAD97308.1; -; mRNA.
EMBL; AK311896; BAG34837.1; -; mRNA.
EMBL; AC096677; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC012600; AAH12600.1; -; mRNA.
EMBL; BC012601; AAH12601.1; -; mRNA.
CCDS; CCDS1411.1; -.
PIR; A53740; TPHUIW.
RefSeq; NP_003272.3; NM_003281.3.
UniGene; Hs.320890; -.
ProteinModelPortal; P19237; -.
SMR; P19237; -.
BioGrid; 112989; 14.
IntAct; P19237; 5.
MINT; MINT-1467470; -.
STRING; 9606.ENSP00000337022; -.
iPTMnet; P19237; -.
PhosphoSitePlus; P19237; -.
BioMuta; TNNI1; -.
DMDM; 1351298; -.
PaxDb; P19237; -.
PeptideAtlas; P19237; -.
PRIDE; P19237; -.
DNASU; 7135; -.
Ensembl; ENST00000336092; ENSP00000337022; ENSG00000159173.
Ensembl; ENST00000361379; ENSP00000354488; ENSG00000159173.
Ensembl; ENST00000367312; ENSP00000356281; ENSG00000159173.
GeneID; 7135; -.
KEGG; hsa:7135; -.
UCSC; uc057oib.1; human.
CTD; 7135; -.
DisGeNET; 7135; -.
EuPathDB; HostDB:ENSG00000159173.18; -.
GeneCards; TNNI1; -.
HGNC; HGNC:11945; TNNI1.
HPA; HPA028190; -.
MIM; 191042; gene.
neXtProt; NX_P19237; -.
OpenTargets; ENSG00000159173; -.
PharmGKB; PA36634; -.
eggNOG; KOG3977; Eukaryota.
eggNOG; ENOG410Y9IX; LUCA.
GeneTree; ENSGT00390000002746; -.
HOVERGEN; HBG052737; -.
InParanoid; P19237; -.
KO; K10371; -.
PhylomeDB; P19237; -.
TreeFam; TF313374; -.
Reactome; R-HSA-390522; Striated Muscle Contraction.
ChiTaRS; TNNI1; human.
GeneWiki; TNNI1; -.
GenomeRNAi; 7135; -.
PRO; PR:P19237; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000159173; -.
ExpressionAtlas; P19237; baseline and differential.
Genevisible; P19237; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005861; C:troponin complex; IBA:GO_Central.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0060048; P:cardiac muscle contraction; IBA:GO_Central.
GO; GO:0030049; P:muscle filament sliding; TAS:Reactome.
GO; GO:0006942; P:regulation of striated muscle contraction; NAS:UniProtKB.
GO; GO:0003009; P:skeletal muscle contraction; IBA:GO_Central.
GO; GO:0014883; P:transition between fast and slow fiber; IEA:Ensembl.
GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IEA:Ensembl.
InterPro; IPR001978; Troponin.
Pfam; PF00992; Troponin; 1.
1: Evidence at protein level;
Acetylation; Actin-binding; Calcium; Complete proteome; Metal-binding;
Muscle protein; Phosphoprotein; Polymorphism; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P02645}.
CHAIN 2 187 Troponin I, slow skeletal muscle.
/FTId=PRO_0000186139.
CA_BIND 106 117 {ECO:0000250}.
REGION 2 48 Involved in binding TNC.
REGION 97 118 Involved in binding TNC and actin.
MOD_RES 2 2 N-acetylproline.
{ECO:0000250|UniProtKB:P02645}.
MOD_RES 58 58 Phosphoserine.
{ECO:0000250|UniProtKB:Q9WUZ5}.
VARIANT 67 67 R -> W (in dbSNP:rs2296695).
/FTId=VAR_052403.
CONFLICT 4 5 VE -> FQ (in Ref. 8; AC096677).
{ECO:0000305}.
CONFLICT 30 30 W -> R (in Ref. 4; CAG29297).
{ECO:0000305}.
CONFLICT 103 103 D -> A (in Ref. 5; CAD91135).
{ECO:0000305}.
CONFLICT 131 131 K -> R (in Ref. 3; CAC44240).
{ECO:0000305}.
CONFLICT 143 143 K -> T (in Ref. 4; CAG46793).
{ECO:0000305}.
CONFLICT 182 183 KS -> NA (in Ref. 1; AAA61228 and 4;
CAG46827/CAG46793/CAG29297).
{ECO:0000305}.
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


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