Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Troponin I, cardiac muscle  

UniProtKB / Swiss-Prot ID :  TNNI3_MOUSE

Gene Name (Synonyms) : 
Tnni3  

Species :  Mus musculus (Mouse). 

Subcellular Localization :   

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

Protein Sequence MADESSDAAGEPQPAPAPVRRRSSANYRAYATEPHAKKKSKISASRKLQLKTLMLQIAKQEMEREAEERR...
Predicted Secondary Structure CCCCCCCCCCCCCCCCHHHHHHHHHHHHHHHHHHHHHHCCCCCHHHHHHHHHHHHHHHHHHHHHHHHHHH...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
23PhosphoserineVRRRSSANY
HHHHHHHHH
31.80Phosphositeplus
Link
23Phosphoserine (PKA_group;PKC_group;PKC_group;RSK_group;PKA_alpha)VRRRSSANY
HHHHHHHHH
31.80PhosphoELM
Link
23Phosphoserine; by PKA and PKD/PRKD1.VRRRSSANY
HHHHHHHHH
31.80UniProtKB
Link
24PhosphoserineRRRSSANYR
HHHHHHHHH
20.79Phosphositeplus
Link
24Phosphoserine (PKA_group;PKC_group;PKC_group;RSK_group;PKA_alpha)RRRSSANYR
HHHHHHHHH
20.79PhosphoELM
Link
24Phosphoserine; by PKA and PKD/PRKD1.RRRSSANYR
HHHHHHHHH
20.79UniProtKB
Link
27PhosphotyrosineSSANYRAYA
HHHHHHHHH
9.06Phosphositeplus
Link
43PhosphoserineKSKISASRK
CCCCCHHHH
24.75Phosphositeplus
Link-
43Phosphoserine (PKC_alpha)KSKISASRK
CCCCCHHHH
24.75PhosphoELM
Link-
43Phosphoserine; by PKC/PRKCE.KSKISASRK
CCCCCHHHH
24.75UniProtKB
Link-
45PhosphoserineKISASRKLQ
CCCHHHHHH
24.13Phosphositeplus
Link-
45Phosphoserine (PKC_alpha)KISASRKLQ
CCCHHHHHH
24.13PhosphoELM
Link-
45Phosphoserine; by PKC/PRKCE.KISASRKLQ
CCCHHHHHH
24.13UniProtKB
Link-
144PhosphothreonineFKRPTLRRV
EECCCCHHC
36.61Phosphositeplus
Link-
144Phosphothreonine (PKC_alpha)FKRPTLRRV
EECCCCHHC
36.61PhosphoELM
Link-
151PhosphoserineRVRISADAM
HCCHHHHHH
14.99Phosphositeplus
Link-
167PhosphoserineRAKESLDLR
HHHHCCCHH
26.86Phosphositeplus
Link-
200PhosphoserineIDALSGMEG
HHHHCCCHH
37.50Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Partial replacement of cardiac troponin I with a non-phosphorylatablemutant at serines 43/45 attenuates the contractile dysfunctionassociated with PKCepsilon phosphorylation.";
Scruggs S.B., Walker L.A., Lyu T., Geenen D.L., Solaro R.J.,Buttrick P.M., Goldspink P.H.;
J. Mol. Cell. Cardiol. 40:465-473(2006).
Cited for: PHOSPHORYLATION AT SER-43 AND SER-45.
"Phosphorylation-dependent conformational transition of the cardiacspecific N-extension of troponin I in cardiac troponin.";
Howarth J.W., Meller J., Solaro R.J., Trewhella J., Rosevear P.R.;
J. Mol. Biol. 373:706-722(2007).
Cited for: STRUCTURE BY NMR OF 1-32, AND PHOSPHORYLATION AT SER-23 AND SER-24.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures