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_HUMAN

Gene Name (Synonyms) : 
TNNI3, TNNC1  

Species :  Homo sapiens (Human). 

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 MADGSSDAAREPRPAPAPIRRRSSNYRAYATEPHAKKKSKISASRKLQLKTLLLQIAKQELEREAEERRG...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCHHHHCCCCCHHHHHHHHHHHHHHHHHHHHHHHHHHHH...
Protein Variant
LocationDescription
2A -> V (in CMD2A). VAR_043989
36K -> Q (in CMD1FF). VAR_063548
79R -> C (in dbSNP:rs3729712). VAR_029453
82P -> S (in CMH7). VAR_016078
116A -> G (in CMD1FF). VAR_067264
141R -> Q (in CMH7). VAR_019872
144L -> Q (in RCM1). VAR_016079
145R -> G (in CMH7). VAR_007603
145R -> W (in RCM1; dbSNP:rs28934871). VAR_016080
157A -> V (in CMH7). VAR_019873
162R -> P (in CMH7). VAR_019874
162R -> Q (in CMH7). VAR_042745
166S -> F (in CMH7). VAR_029454
171A -> T (in RCM1). VAR_016081
177Missing (in CMH7). VAR_019875
178K -> E (in RCM1; dbSNP:rs28934870). VAR_016082
185N -> K (in CMD1FF). VAR_063549
186R -> Q (in CMH7). VAR_019876
190D -> H (in CMH7 and RCM1). VAR_016083
192R -> H (in RCM1). VAR_016084
196D -> N (in CMH7). VAR_016085
204R -> H (in CMH7). VAR_042746
206K -> Q (in CMH7). VAR_007604
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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
Protein Variant
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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
2N-acetylalanine.---MADGSS
---CCCCCC
29.85UniProtKB
Link-
23PhosphoserineIRRRSSNYR
CCCCCCCCC
22.56HPRD
Link-
23PhosphoserineIRRRSSNYR
CCCCCCCCC
22.56Phosphositeplus
Link-
23Phosphoserine (PKA_group)IRRRSSNYR
CCCCCCCCC
22.56PhosphoELM
Link-
23Phosphoserine (PRKCA)IRRRSSNYR
CCCCCCCCC
22.56HPRD
Link-
23Phosphoserine; by PKA and PKD/PRKD1.IRRRSSNYR
CCCCCCCCC
22.56UniProtKB
Link-
24PhosphoserineRRRSSNYRA
CCCCCCCCC
35.75HPRD
Link-
24PhosphoserineRRRSSNYRA
CCCCCCCCC
35.75Phosphositeplus
Link-
24Phosphoserine (PKA_group)RRRSSNYRA
CCCCCCCCC
35.75PhosphoELM
Link-
24Phosphoserine (PRKCA)RRRSSNYRA
CCCCCCCCC
35.75HPRD
Link-
24Phosphoserine; by PKA and PKD/PRKD1.RRRSSNYRA
CCCCCCCCC
35.75UniProtKB
Link-
31PhosphothreonineRAYATEPHA
CCCCCCCHH
37.06Phosphositeplus
Link-
31Phosphothreonine; by STK4/MST1.RAYATEPHA
CCCCCCCHH
37.06UniProtKB
Link-
39PhosphoserineAKKKSKISA
HHHCCCCCH
44.06HPRD
Link
39PhosphoserineAKKKSKISA
HHHCCCCCH
44.06Phosphositeplus
Link
42PhosphoserineKSKISASRK
CCCCCHHHH
24.75Phosphositeplus
Link
42Phosphoserine (PRKCA)KSKISASRK
CCCCCHHHH
24.75HPRD
Link
44PhosphoserineKISASRKLQ
CCCHHHHHH
24.13Phosphositeplus
Link
44Phosphoserine (PKC_epsilon)KISASRKLQ
CCCHHHHHH
24.13PhosphoELM
Link
44Phosphoserine (PRKCA)KISASRKLQ
CCCHHHHHH
24.13HPRD
Link
51PhosphothreonineLQLKTLLLQ
HHHHHHHHH
31.09Phosphositeplus
Link
51Phosphothreonine; by STK4/MST1.LQLKTLLLQ
HHHHHHHHH
31.09UniProtKB
Link
77PhosphoserineGRALSTRCQ
HHHHHHCCC
16.90Phosphositeplus
Link
77Phosphoserine (PRKCA)GRALSTRCQ
HHHHHHCCC
16.90HPRD
Link
78PhosphothreonineRALSTRCQP
HHHHHCCCC
35.99Phosphositeplus
Link
129PhosphothreonineIADLTQKIF
HHHHHHHHH
28.50Phosphositeplus
Link
129Phosphothreonine; by STK4/MST1.IADLTQKIF
HHHHHHHHH
28.50UniProtKB
Link
143PhosphothreonineFKRPTLRRV
EECCCCCEE
36.61PhosphoELM
Link
143PhosphothreonineFKRPTLRRV
EECCCCCEE
36.61Phosphositeplus
Link
143Phosphothreonine (PRKCA)FKRPTLRRV
EECCCCCEE
36.61HPRD
Link
143Phosphothreonine; by STK4/MST1.FKRPTLRRV
EECCCCCEE
36.61UniProtKB
Link
150PhosphoserineRVRISADAM
EECCCHHHH
14.99Phosphositeplus
Link
150Phosphoserine (PAK3)RVRISADAM
EECCCHHHH
14.99PhosphoELM
Link
150Phosphoserine; by PAK3.RVRISADAM
EECCCHHHH
14.99UniProtKB
Link
166PhosphoserineRAKESLDLR
HHHHCCCHH
26.86HPRD
Link-
166PhosphoserineRAKESLDLR
HHHHCCCHH
26.86PhosphoELM
Link-
166PhosphoserineRAKESLDLR
HHHHCCCHH
26.86Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
ACTS_HUMANin vitroHPRD:11769HPRD12383268
PKD2_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:11769HPRD12525172
PAPP1_HUMANin vitroHPRD:11769HPRD12626203
TNNT1_HUMANin vitroHPRD:11769HPRD11904166
TNNC1_HUMANin vitroHPRD:11769HPRD15134451
15049709
11904166
9346285
12939162
12122471
12060657
16302972
TNNI3_HUMANin vitroHPRD:11769HPRD12060657
TNNT2_HUMANin vitroHPRD:11769HPRD12840750
9219516
9560191
RCAN3_HUMANin vitro
yeast 2-hybrid
HPRD:11769HPRD16516408
TNNC1_HUMANENSP00000341838STRING
MYPC3_HUMANENSP00000341838STRING
TNNT1_HUMANENSP00000341838STRING
TNI3K_HUMANENSP00000341838STRING
GATA4_HUMANENSP00000341838STRING
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Disease Reference
Kegg disease
OMIM disease
613690Cardiomyopathy, familial hypertrophic 7 (CMH7)
115210Cardiomyopathy, familial restrictive 1 (RCM1)
611880Cardiomyopathy, dilated 2A (CMD2A)
613286Cardiomyopathy, dilated 1FF (CMD1FF)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"A common motif of two adjacent phosphoserines in bovine, rabbit andhuman cardiac troponin I.";
Mittmann K., Jaquet K., Heilmeyer L.M.G. Jr.;
FEBS Lett. 273:41-45(1990).
Cited for: PROTEIN SEQUENCE OF 11-36, ACETYLATION AT ALA-2, AND PHOSPHORYLATIONAT SER-23 AND SER-24.
Phosphorylation
ReferencePubMed
"Phosphorylation of cardiac troponin I by mammalian sterile 20-likekinase 1.";
You B., Yan G., Zhang Z., Yan L., Li J., Ge Q., Jin J.P., Sun J.;
Biochem. J. 418:93-101(2009).
Cited for: INTERACTION WITH STK4/MST1, AND PHOSPHORYLATION AT THR-31; THR-51;THR-129 AND THR-143.
"A common motif of two adjacent phosphoserines in bovine, rabbit andhuman cardiac troponin I.";
Mittmann K., Jaquet K., Heilmeyer L.M.G. Jr.;
FEBS Lett. 273:41-45(1990).
Cited for: PROTEIN SEQUENCE OF 11-36, ACETYLATION AT ALA-2, AND PHOSPHORYLATIONAT SER-23 AND SER-24.
"The ordered phosphorylation of cardiac troponin I by the cAMP-dependent protein kinase -- structural consequences and functionalimplications.";
Keane N.E., Quirk P.G., Gao Y., Patchell V.B., Perry S.V.,Levine B.A.;
Eur. J. Biochem. 248:329-337(1997).
Cited for: PHOSPHORYLATION AT SER-23 AND SER-24.
"p21-activated kinase increases the calcium sensitivity of rat triton-skinned cardiac muscle fiber bundles via a mechanism potentiallyinvolving novel phosphorylation of troponin I.";
Buscemi N., Foster D.B., Neverova I., Van Eyk J.E.;
Circ. Res. 91:509-516(2002).
Cited for: PHOSPHORYLATION AT SER-150 BY PAK3.
"Protein kinase D is a novel mediator of cardiac troponin Iphosphorylation and regulates myofilament function.";
Haworth R.S., Cuello F., Herron T.J., Franzen G., Kentish J.C.,Gautel M., Avkiran M.;
Circ. Res. 95:1091-1099(2004).
Cited for: 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