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Protein

Troponin I, slow skeletal muscle

Gene

TNNI1

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

Functioni

Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi106 – 11712By similarityAdd
BLAST

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. muscle filament sliding Source: Reactome
  2. regulation of striated muscle contraction Source: UniProtKB
  3. ventricular cardiac muscle tissue morphogenesis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_16969. Striated Muscle Contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Troponin I, slow skeletal muscle
Alternative name(s):
Troponin I, slow-twitch isoform
Gene namesi
Name:TNNI1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:11945. TNNI1.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36634.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 187186Troponin I, slow skeletal musclePRO_0000186139Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylprolineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP19237.
PRIDEiP19237.

PTM databases

PhosphoSiteiP19237.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

BgeeiP19237.
ExpressionAtlasiP19237. baseline and differential.
GenevestigatoriP19237.

Organism-specific databases

HPAiCAB009349.
HPA028190.

Interactioni

Subunit structurei

Binds to actin and tropomyosin.

Protein-protein interaction databases

BioGridi112989. 9 interactions.
IntActiP19237. 2 interactions.
MINTiMINT-1467470.

Structurei

3D structure databases

ProteinModelPortaliP19237.
SMRiP19237. Positions 5-183.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 4847Involved in binding TNCAdd
BLAST
Regioni97 – 11822Involved in binding TNC and actinAdd
BLAST

Sequence similaritiesi

Belongs to the troponin I family.Curated

Phylogenomic databases

eggNOGiNOG328514.
GeneTreeiENSGT00390000002746.
HOVERGENiHBG052737.
InParanoidiP19237.
KOiK10371.
OMAiVQRKSKI.
OrthoDBiEOG71G9WD.
PhylomeDBiP19237.
TreeFamiTF313374.

Family and domain databases

InterProiIPR001978. Troponin.
[Graphical view]
PfamiPF00992. Troponin. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P19237-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPEVERKPKI TASRKLLLKS LMLAKAKECW EQEHEEREAE KVRYLAERIP
60 70 80 90 100
TLQTRGLSLS ALQDLCRELH AKVEVVDEER YDIEAKCLHN TREIKDLKLK
110 120 130 140 150
VMDLRGKFKR PPLRRVRVSA DAMLRALLGS KHKVSMDLRA NLKSVKKEDT
160 170 180
EKERPVEVGD WRKNVEAMSG MEGRKKMFDA AKSPTSQ
Length:187
Mass (Da):21,692
Last modified:January 23, 2007 - v3
Checksum:i7A8363CC7559B962
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 52VE → FQ in AC096677 (PubMed:16710414).Curated
Sequence conflicti30 – 301W → R in CAG29297 (Ref. 4) Curated
Sequence conflicti103 – 1031D → A in CAD91135 (PubMed:17974005).Curated
Sequence conflicti131 – 1311K → R in CAC44240 (Ref. 3) Curated
Sequence conflicti143 – 1431K → T in CAG46793 (Ref. 4) Curated
Sequence conflicti182 – 1832KS → NA in AAA61228 (PubMed:2365354).Curated
Sequence conflicti182 – 1832KS → NA in CAG46827 (Ref. 4) Curated
Sequence conflicti182 – 1832KS → NA in CAG46793 (Ref. 4) Curated
Sequence conflicti182 – 1832KS → NA in CAG29297 (Ref. 4) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti67 – 671R → W.
Corresponds to variant rs2296695 [ dbSNP | Ensembl ].
VAR_052403

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04760 mRNA. Translation: AAA61228.1.
L21910
, L21906, L21908, L21909 Genomic DNA. Translation: AAC14461.1.
AJ315823 mRNA. Translation: CAC44240.1.
CR450301 mRNA. Translation: CAG29297.1.
CR541996 mRNA. Translation: CAG46793.1.
CR542030 mRNA. Translation: CAG46827.1.
AL831820 mRNA. Translation: CAD38534.1.
AL831975 mRNA. Translation: CAH56221.1.
BX510903 mRNA. Translation: CAD91135.1.
AK223588 mRNA. Translation: BAD97308.1.
AK311896 mRNA. Translation: BAG34837.1.
AC096677 Genomic DNA. No translation available.
BC012600 mRNA. Translation: AAH12600.1.
BC012601 mRNA. Translation: AAH12601.1.
CCDSiCCDS1411.1.
PIRiA53740. TPHUIW.
RefSeqiNP_003272.3. NM_003281.3.
UniGeneiHs.320890.

Genome annotation databases

EnsembliENST00000336092; ENSP00000337022; ENSG00000159173.
ENST00000361379; ENSP00000354488; ENSG00000159173.
ENST00000367312; ENSP00000356281; ENSG00000159173.
GeneIDi7135.
KEGGihsa:7135.
UCSCiuc001gwp.3. human.

Polymorphism databases

DMDMi1351298.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04760 mRNA. Translation: AAA61228.1.
L21910
, L21906, L21908, L21909 Genomic DNA. Translation: AAC14461.1.
AJ315823 mRNA. Translation: CAC44240.1.
CR450301 mRNA. Translation: CAG29297.1.
CR541996 mRNA. Translation: CAG46793.1.
CR542030 mRNA. Translation: CAG46827.1.
AL831820 mRNA. Translation: CAD38534.1.
AL831975 mRNA. Translation: CAH56221.1.
BX510903 mRNA. Translation: CAD91135.1.
AK223588 mRNA. Translation: BAD97308.1.
AK311896 mRNA. Translation: BAG34837.1.
AC096677 Genomic DNA. No translation available.
BC012600 mRNA. Translation: AAH12600.1.
BC012601 mRNA. Translation: AAH12601.1.
CCDSiCCDS1411.1.
PIRiA53740. TPHUIW.
RefSeqiNP_003272.3. NM_003281.3.
UniGeneiHs.320890.

3D structure databases

ProteinModelPortaliP19237.
SMRiP19237. Positions 5-183.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112989. 9 interactions.
IntActiP19237. 2 interactions.
MINTiMINT-1467470.

PTM databases

PhosphoSiteiP19237.

Polymorphism databases

DMDMi1351298.

Proteomic databases

PaxDbiP19237.
PRIDEiP19237.

Protocols and materials databases

DNASUi7135.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000336092; ENSP00000337022; ENSG00000159173.
ENST00000361379; ENSP00000354488; ENSG00000159173.
ENST00000367312; ENSP00000356281; ENSG00000159173.
GeneIDi7135.
KEGGihsa:7135.
UCSCiuc001gwp.3. human.

Organism-specific databases

CTDi7135.
GeneCardsiGC01M201372.
HGNCiHGNC:11945. TNNI1.
HPAiCAB009349.
HPA028190.
MIMi191042. gene.
neXtProtiNX_P19237.
PharmGKBiPA36634.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG328514.
GeneTreeiENSGT00390000002746.
HOVERGENiHBG052737.
InParanoidiP19237.
KOiK10371.
OMAiVQRKSKI.
OrthoDBiEOG71G9WD.
PhylomeDBiP19237.
TreeFamiTF313374.

Enzyme and pathway databases

ReactomeiREACT_16969. Striated Muscle Contraction.

Miscellaneous databases

ChiTaRSiTNNI1. human.
GeneWikiiTNNI1.
GenomeRNAii7135.
NextBioi27917.
PROiP19237.
SOURCEiSearch...

Gene expression databases

BgeeiP19237.
ExpressionAtlasiP19237. baseline and differential.
GenevestigatoriP19237.

Family and domain databases

InterProiIPR001978. Troponin.
[Graphical view]
PfamiPF00992. Troponin. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA sequence, tissue-specific expression, and chromosomal mapping of the human slow-twitch skeletal muscle isoform of troponin I."
    Wade R., Eddy R., Shows T.B., Kedes L.
    Genomics 7:346-357(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Skeletal muscle.
  2. "Structure and expression of the human slow twitch skeletal muscle troponin I gene."
    Corin S.J., Juhasz O., Zhu L., Conley P., Kedes L., Wade R.
    J. Biol. Chem. 269:10651-10659(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
    Tissue: Blood.
  3. "Full length sequencing of some human and murine muscular transcripts (Telethon Italy project B41)."
    Frigimelica E., Ievolella C., Lanfranchi G.
    Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Skeletal muscle.
  4. "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 (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Skeletal muscle.
  6. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  7. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  8. "The DNA sequence and biological annotation of human chromosome 1."
    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.
    Nature 441:315-321(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Skeletal muscle.

Entry informationi

Entry nameiTNNI1_HUMAN
AccessioniPrimary (citable) accession number: P19237
Secondary accession number(s): A6NEH3
, A8MSJ0, Q659A5, Q6FGS7, Q6FGW1, Q6ICU2, Q86T57, Q96DT9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 128 of the entry and version 3 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.