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Protein Page:
TNNI3 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
TNNI3 Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity. Binds to actin and tropomyosin. Interacts with TRIM63. Interacts with STK4/MST1. Belongs to the troponin I family. Note: This description may include information from UniProtKB.
Protein type: Motor protein; Actin binding protein; Motility/polarity/chemotaxis
Cellular Component: sarcomere; troponin complex; cytosol
Molecular Function: troponin T binding; protein domain specific binding; troponin C binding; protein binding; metal ion binding; calcium channel inhibitor activity; actin binding; protein kinase binding; calcium-dependent protein binding
Biological Process: cellular calcium ion homeostasis; regulation of smooth muscle contraction; heart contraction; heart development; regulation of systemic arterial blood pressure by ischemic conditions; ventricular cardiac muscle morphogenesis; vasculogenesis; negative regulation of ATPase activity; muscle filament sliding; cardiac muscle contraction
Reference #:  P19429 (UniProtKB)
Alt. Names/Synonyms: Cardiac troponin I; CMD1FF; CMD2A; CMH7; cTnI; familial hypertrophic cardiomyopathy 7; MGC116817; RCM1; TNNC1; TNNI3; troponin I type 3 (cardiac); Troponin I, cardiac muscle
Gene Symbols: TNNI3
Molecular weight: 24,008 Da
Basal Isoelectric point: 9.87  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

TNNI3

Protein Structure Not Found.


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Sites Implicated In
cytoskeletal reorganization: S23‑p, S24‑p, S150‑p
signaling pathway regulation: S150‑p
activity, inhibited: S23‑p, S24‑p, S42‑p, S44‑p, T143‑p, S199‑p
molecular association, regulation: S23‑p, S24‑p, T31‑p, S39‑p, S42‑p, S44‑p, T51‑p, T129‑p, T143‑p, S166‑p
protein conformation: T31‑p, T51‑p, T129‑p, T143‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 2 S5-p ___MADGssDAAREP
0 2 S6-p __MADGssDAAREPR
42 15 S23-p PAPIRRRssNyRAyA
38 20 S24-p APIRRRssNyRAyAt
0 9 Y26-p IRRRssNyRAyAtEP
0 4 Y29-p RssNyRAyAtEPHAK
1 0 T31-p sNyRAyAtEPHAKKK
0 1 K36 yAtEPHAKKKskIsA
1 0 S39-p EPHAKKKskIsAsRK
0 2 K40-m3 PHAKKKskIsAsRKL
19 2 S42-p AKKKskIsAsRKLQL
19 2 S44-p KKskIsAsRKLQLKt
0 1 K50 AsRKLQLKtLLLQIA
1 1 T51-p sRKLQLKtLLLQIAK
0 1 K58 tLLLQIAKQELEREA
0 3 K72-ac AEERRGEkGRALstR
2 2 S77-p GEkGRALstRCQPLE
0 2 T78-p EkGRALstRCQPLEL
0 2 K106 QLHARVDKVDEERyD
0 21 Y112-p DKVDEERyDIEAKVT
0 2 K117 ERyDIEAKVTKNITE
0 1 K120 DIEAKVTKNITEIAD
1 0 T129-p ITEIADLtQKIFDLR
0 2 K131 EIADLtQKIFDLRGK
0 55 F133 ADLtQKIFDLRGKFK
23 3 T143-p RGKFKRPtLRRVRIs
7 1 S150-p tLRRVRIsADAMMQA
1 0 S150 tLRRVRISADAMMQA
0 1 K164 ALLGARAKEsLDLRA
1 2 S166-p LGARAKEsLDLRAHL
0 1 K174 LDLRAHLKQVkkEDt
0 1 K177-ac RAHLKQVkkEDtEKE
0 1 K178-ac AHLKQVkkEDtEKEN
0 1 T181-p KQVkkEDtEKENREV
0 1 K183 VkkEDtEKENREVGD
0 1 K193 REVGDWRKNIDALsG
0 1 K193 REVGDWRKNIDALsG
0 3 S199-p RKNIDALsGMEGRKK
4004 : Phospho-Troponin I (Cardiac) (Ser23/24) Antibody
4004 : Phospho-Troponin I (Cardiac) (Ser23/24) Antibody
  mouse

 
S5-p ___MADEssDAAGEP
S6-p __MADEssDAAGEPQ
S23-p PAPVRRRssANyRAY
S24-p APVRRRssANyRAYA
Y27-p RRRssANyRAYATEP
Y30 ssANyRAYATEPHAk
T32 ANyRAYATEPHAkKK
K37-ub YATEPHAkKKSKIsA
S40 EPHAkKKSKIsAsRK
K41 PHAkKKSKIsAsRKL
S43-p AkKKSKIsAsRKLQL
S45-p KKSKIsAsRKLQLkT
K51-ub AsRKLQLkTLMLQIA
T52 sRKLQLkTLMLQIAk
K59-ub TLMLQIAkQEMEREA
K73 AEERRGEKGRVLRTR
R78 GEKGRVLRTRCQPLE
T79 EKGRVLRTRCQPLEL
K107-ub QLHARVDkVDEERYD
Y113 DkVDEERYDVEAkVT
K118-ub ERYDVEAkVTkNITE
K121-ub DVEAkVTkNITEIAD
T130 ITEIADLTQkIyDLR
K132-ub EIADLTQkIyDLRGK
Y134-p ADLTQkIyDLRGKFK
T144-p RGKFKRPtLRRVRIs
S151-p tLRRVRIsADAMMQA
S151 tLRRVRISADAMMQA
K165-ub ALLGTRAkEsLDLRA
S167-p LGTRAkEsLDLRAHL
K175-ub LDLRAHLkQVKKEDI
K178 RAHLkQVKKEDIEkE
K179 AHLkQVKKEDIEkEN
I182 kQVKKEDIEkENREV
K184-ub VKKEDIEkENREVGD
K194-ub REVGDWRkNIDALsG
K194-ac REVGDWRkNIDALsG
S200-p RkNIDALsGMEGRKK
  rat

 
S5 ___MADESSDAAGEP
S6 __MADESSDAAGEPQ
S23-p PAPVRRRssANYRAY
S24-p APVRRRssANYRAYA
Y27 RRRssANYRAYATEP
Y30 ssANYRAYATEPHAK
T32 ANYRAYATEPHAKKK
K37 YATEPHAKKKSKIsA
S40 EPHAKKKSKIsAsRK
K41 PHAKKKSKIsAsRKL
S43-p AKKKSKIsAsRKLQL
S45-p KKSKIsAsRKLQLKT
K51 AsRKLQLKTLMLQIA
T52 sRKLQLKTLMLQIAK
K59 TLMLQIAKQEMEREA
K73 AEERRGEKGRVLsTR
S78-p GEKGRVLsTRCQPLV
T79 EKGRVLsTRCQPLVL
K107 QLHARVDKVDEERYD
Y113 DKVDEERYDVEAKVT
K118 ERYDVEAKVTKNITE
K121 DVEAKVTKNITEIAD
T130 ITEIADLTQKIyDLR
K132 EIADLTQKIyDLRGK
Y134-p ADLTQKIyDLRGKFK
T144-p RGKFKRPtLRRVRIs
S151-p tLRRVRIsADAMMQA
S151-gl tLRRVRIsADAMMQA
K165 ALLGTRAKESLDLRA
S167 LGTRAKESLDLRAHL
K175 LDLRAHLKQVKKEDI
K178 RAHLKQVKKEDIEKE
K179 AHLKQVKKEDIEKEN
I182 KQVKKEDIEKENREV
K184 VKKEDIEKENREVGD
K194 REVGDWRKNIDALSG
K194 REVGDWRKNIDALSG
S200 RKNIDALSGMEGRKK
4004 : Phospho-Troponin I (Cardiac) (Ser23/24) Antibody
4004 : Phospho-Troponin I (Cardiac) (Ser23/24) Antibody
  rabbit

 
S4 ____ADESRDAAGEA
R5 ___ADESRDAAGEAR
S22-p PAPVRRRsSANYRAY
S23 APVRRRsSANYRAYA
Y26 RRRsSANYRAYATEP
Y29 sSANYRAYATEPHAK
T31 ANYRAYATEPHAKSK
K36 YATEPHAKSKKKISA
K39 EPHAKSKKKISASRK
K40 PHAKSKKKISASRKL
S42 AKSKKKISASRKLQL
S44 SKKKISASRKLQLKT
K50 ASRKLQLKTLMLQIA
T51 SRKLQLKTLMLQIAK
K58 TLMLQIAKQELEREA
K72 AEERRGEKGRALsTR
S77-p GEKGRALsTRCQPLE
T78 EKGRALsTRCQPLEL
K106 QLHARVDKVDEERYD
Y112 DKVDEERYDVEAKVT
K117 ERYDVEAKVTKNITE
K120 DVEAKVTKNITEIAD
T129 ITEIADLTQKIFDLR
K131 EIADLTQKIFDLRGK
F133 ADLTQKIFDLRGKFK
T143-p RGKFKRPtLRLRVRI
S151-p LRLRVRIsADAMMQA
S151 LRLRVRISADAMMQA
K165 ALLGTRAKETLDLRA
T167 LGTRAKETLDLRAHL
K175 LDLRAHLKQVKKEDT
K178 RAHLKQVKKEDTEKE
K179 AHLKQVKKEDTEKEN
T182 KQVKKEDTEKENREV
K184 VKKEDTEKENREVGD
K194 REVGDWRKNIDLLSG
K194 REVGDWRKNIDLLSG
S200 RKNIDLLSGMEGRKK
  dog

 
S5 ___MADESGDAAGCP
G6 __MADESGDAAGCPP
S23 PAPIRRQSSANYRAY
S24 APIRRQSSANYRAYA
Y27 RRQSSANYRAYATEP
Y30 SSANYRAYATEPHAK
T32 ANYRAYATEPHAKKK
K37 YATEPHAKKKSKISA
S40 EPHAKKKSKISASRK
K41 PHAKKKSKISASRKL
S43 AKKKSKISASRKLQL
S45 KKSKISASRKLQLKT
K51 ASRKLQLKTLMLQIA
T52 SRKLQLKTLMLQIAK
K59 TLMLQIAKQELEREA
K73 AEERRGEKGRALSTR
S78 GEKGRALSTRCQPLE
T79 EKGRALSTRCQPLEL
K107 QLHARVDKVDEERYD
Y113 DKVDEERYDVEAKVT
K118 ERYDVEAKVTKNITE
K121 DVEAKVTKNITEIAD
T130 ITEIADLTQKIFDLR
K132 EIADLTQKIFDLRGK
F134 ADLTQKIFDLRGKFK
T144 RGKFKRPTLRRVRIS
S151 TLRRVRISADAMMQA
S151 TLRRVRISADAMMQA
K165 ALLGTRAKEsLDLRA
S167-p LGTRAKEsLDLRAHL
K175 LDLRAHLKQVKKEDt
K178 RAHLKQVKKEDtEKE
K179 AHLKQVKKEDtEKEN
T182-p KQVKKEDtEKENREV
K184 VKKEDtEKENREVGD
K194 REVGDWRKNIDALsG
K194 REVGDWRKNIDALsG
S200-p RKNIDALsGMEGRKK
  cow

 
S5 ___MADRSGGSTAGD
G6 __MADRSGGSTAGDT
S24-p PPPVRRRssANYRAY
S25-p PPVRRRssANYRAYA
Y28 RRRssANYRAYATEP
Y31 ssANYRAYATEPHAK
T33 ANYRAYATEPHAKKK
K38 YATEPHAKKKSKIsA
S41 EPHAKKKSKIsAsRK
K42 PHAKKKSKIsAsRKL
S44-p AKKKSKIsAsRKLQL
S46-p KKSKIsAsRKLQLKT
K52 AsRKLQLKTLMLQIA
T53 sRKLQLKTLMLQIAK
K60 TLMLQIAKQELEREA
K74 AEERRGEKGRALsTR
S79-p GEKGRALsTRCQPLE
T80 EKGRALsTRCQPLEL
K108 QLHARVDKVDEERYD
Y114 DKVDEERYDVEAKVT
K119 ERYDVEAKVTKNITE
K122 DVEAKVTKNITEIAD
N131 ITEIADLNQKIFDLR
K133 EIADLNQKIFDLRGK
F135 ADLNQKIFDLRGKFK
T145-p RGKFKRPtLRRVRIS
S152 tLRRVRISADAMMQA
S152 tLRRVRISADAMMQA
K166 ALLGARAKETLDLRA
T168 LGARAKETLDLRAHL
K176 LDLRAHLKQVKKEDT
K179 RAHLKQVKKEDTEKE
K180 AHLKQVKKEDTEKEN
T183 KQVKKEDTEKENREV
K185 VKKEDTEKENREVGD
K195 REVGDWRKNIDALSG
K195 REVGDWRKNIDALSG
S201 RKNIDALSGMEGRKK
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