| + |
PAK3 | down-regulates 
phosphorylation
|
TNNI3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134593 |
Ser150 |
TLRRVRIsADAMMQA |
Homo sapiens |
|
| pmid |
sentence |
| 15769444 |
In vitro addition of pak3 to skinned rat cardiac fibres increased myofilament ca2+ sensitivity with no change in maximal ca2+-activated force [67]. These effects were associated with pak3-induced phosphorylation of myofilament proteins, including ctni which was phosphorylated at a novel site, ser149, located in the region forming a ca2+-sensitive interaction with the n-terminal regulatory domain of tnc. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| + |
PAK3 |
phosphorylation
|
TNNI3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-92990 |
Ser150 |
TLRRVRIsADAMMQA |
Homo sapiens |
|
| pmid |
sentence |
| 12242269 |
Importantly, cardiac troponin i was found to be phosphorylated at serine 149 of human cardiac troponin i, representing a novel phosphorylation site. These findings suggest a novel mechanism of modulating the calcium sensitivity of cardiac muscle contraction. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| + |
PRKCA | down-regulates activity
phosphorylation
|
TNNI3 |
0.349 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249069 |
Ser166 |
LGARAKEsLDLRAHL |
in vitro |
|
| pmid |
sentence |
| 11121119 |
In addition to the established phosphorylation sites (S22 and S23) we found that S38 and S165 were the other two main sites of phosphorylation. | Overphosphorylation of troponin I reduced its affinity for troponin C, as measured by isothermal titration microcalorimetry. Phosphorylation of S22/23A also decreased its affinity for troponin C indicating that phosphorylation of S38 and/or S165 impedes binding of troponin I to troponin C. Formation of a troponin I/troponin C complex prior to cAMP-dependent protein kinase treatment did not prevent overphosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249068 |
Ser39 |
EPHAKKKsKISASRK |
in vitro |
|
| pmid |
sentence |
| 11121119 |
In addition to the established phosphorylation sites (S22 and S23) we found that S38 and S165 were the other two main sites of phosphorylation. | Overphosphorylation of troponin I reduced its affinity for troponin C, as measured by isothermal titration microcalorimetry. Phosphorylation of S22/23A also decreased its affinity for troponin C indicating that phosphorylation of S38 and/or S165 impedes binding of troponin I to troponin C. Formation of a troponin I/troponin C complex prior to cAMP-dependent protein kinase treatment did not prevent overphosphorylation. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PPP2CA | down-regulates
dephosphorylation
|
TNNI3 |
0.387 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134597 |
Ser23 |
PAPIRRRsSNYRAYA |
Homo sapiens |
|
| pmid |
sentence |
| 15769444 |
The major phosphatase thought to dephosphorylate ctni and phospholamban is type 2a protein phosphatase (pp2a) [61]. Activation of pp2a and ensuing dephosphorylation of regulatory proteins is involved in the anti-adrenergic effects of adenosine and muscarinic receptor activation see also fig2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134601 |
Ser24 |
APIRRRSsNYRAYAT |
Homo sapiens |
|
| pmid |
sentence |
| 15769444 |
The major phosphatase thought to dephosphorylate ctni and phospholamban is type 2a protein phosphatase (pp2a) [61]. Activation of pp2a and ensuing dephosphorylation of regulatory proteins is involved in the anti-adrenergic effects of adenosine and muscarinic receptor activation see also fig2. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| + |
PRKCA | up-regulates activity 
phosphorylation
|
TNNI3 |
0.349 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249066 |
Ser23 |
PAPIRRRsSNYRAYA |
in vitro |
|
| pmid |
sentence |
| 11121119 |
In addition to the established phosphorylation sites (S22 and S23) we found that S38 and S165 were the other two main sites of phosphorylation. | Phosphorylation of S22/23A also decreased its affinity for troponin C indicating that phosphorylation of S38 and/or S165 impedes binding of troponin I to troponin C. Formation of a troponin I/troponin C complex prior to cAMP-dependent protein kinase treatment did not prevent overphosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249067 |
Ser24 |
APIRRRSsNYRAYAT |
in vitro |
|
| pmid |
sentence |
| 11121119 |
In addition to the established phosphorylation sites (S22 and S23) we found that S38 and S165 were the other two main sites of phosphorylation. | Phosphorylation of S22/23A also decreased its affinity for troponin C indicating that phosphorylation of S38 and/or S165 impedes binding of troponin I to troponin C. Formation of a troponin I/troponin C complex prior to cAMP-dependent protein kinase treatment did not prevent overphosphorylation. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PRKCD | up-regulates activity
phosphorylation
|
TNNI3 |
0.276 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178880 |
Ser23 |
PAPIRRRsSNYRAYA |
Homo sapiens |
|
| pmid |
sentence |
| 18550549 |
Src phosphorylates pkcdelta at tyr311 and tyr332 leading to enhanced pkcdelta autophosphorylation at thr505 (its activation loop) and pkcdelta-dependent ctni phosphorylation at both ser23/ser24 and thr144. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178884 |
Ser24 |
APIRRRSsNYRAYAT |
Homo sapiens |
|
| pmid |
sentence |
| 18550549 |
Src phosphorylates pkcdelta at tyr311 and tyr332 leading to enhanced pkcdelta autophosphorylation at thr505 (its activation loop) and pkcdelta-dependent ctni phosphorylation at both ser23/ser24 and thr144. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKACA | up-regulates activity
phosphorylation
|
TNNI3 |
0.398 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134605 |
Ser23 |
PAPIRRRsSNYRAYA |
Homo sapiens |
|
| pmid |
sentence |
| 15769444 |
Phosphorylation at ser 23/24 (e.g., by pka or pkg) results in reduction in myofilament ca2+ sensitivity and an increase in crossbridge cycling rate, leading to acceleration of relaxation and an increase in power output but a reduced economy of contraction. Conversely, phosphorylation at ser 43/45 (by pkc) is associated with reduced maximum ca2+-activated force and decreased crossbridge cycling rates, which are likely to reduce power output and delay relaxation, with an increased economy of contraction. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134609 |
Ser24 |
APIRRRSsNYRAYAT |
Homo sapiens |
|
| pmid |
sentence |
| 15769444 |
Phosphorylation at ser 23/24 (e.g., by pka or pkg) results in reduction in myofilament ca2+ sensitivity and an increase in crossbridge cycling rate, leading to acceleration of relaxation and an increase in power output but a reduced economy of contraction. Conversely, phosphorylation at ser 43/45 (by pkc) is associated with reduced maximum ca2+-activated force and decreased crossbridge cycling rates, which are likely to reduce power output and delay relaxation, with an increased economy of contraction. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKG1 | up-regulates activity
phosphorylation
|
TNNI3 |
0.366 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134640 |
Ser23 |
PAPIRRRsSNYRAYA |
Homo sapiens |
|
| pmid |
sentence |
| 15769444 |
Phosphorylation at ser 23/24 (e.g., by pka or pkg) results in reduction in myofilament ca2+ sensitivity and an increase in crossbridge cycling rate, leading to acceleration of relaxation and an increase in power output but a reduced economy of contraction. Conversely, phosphorylation at ser 43/45 (by pkc) is associated with reduced maximum ca2+-activated force and decreased crossbridge cycling rates, which are likely to reduce power output and delay relaxation, with an increased economy of contraction. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134644 |
Ser24 |
APIRRRSsNYRAYAT |
Homo sapiens |
|
| pmid |
sentence |
| 15769444 |
Phosphorylation at ser 23/24 (e.g., by pka or pkg) results in reduction in myofilament ca2+ sensitivity and an increase in crossbridge cycling rate, leading to acceleration of relaxation and an increase in power output but a reduced economy of contraction. Conversely, phosphorylation at ser 43/45 (by pkc) is associated with reduced maximum ca2+-activated force and decreased crossbridge cycling rates, which are likely to reduce power output and delay relaxation, with an increased economy of contraction. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCB | down-regulates
phosphorylation
|
TNNI3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134624 |
Ser42 |
AKKKSKIsASRKLQL |
Homo sapiens |
|
| pmid |
sentence |
| 15769444 |
Phosphorylation at ser 23/24 (e.g., by pka or pkg) results in reduction in myofilament ca2+ sensitivity and an increase in crossbridge cycling rate, leading to acceleration of relaxation and an increase in power output but a reduced economy of contraction. Conversely, phosphorylation at ser 43/45 (by pkc) is associated with reduced maximum ca2+-activated force and decreased crossbridge cycling rates, which are likely to reduce power output and delay relaxation, with an increased economy of contraction. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134628 |
Ser44 |
KKSKISAsRKLQLKT |
Homo sapiens |
|
| pmid |
sentence |
| 15769444 |
Phosphorylation at ser 23/24 (e.g., by pka or pkg) results in reduction in myofilament ca2+ sensitivity and an increase in crossbridge cycling rate, leading to acceleration of relaxation and an increase in power output but a reduced economy of contraction. Conversely, phosphorylation at ser 43/45 (by pkc) is associated with reduced maximum ca2+-activated force and decreased crossbridge cycling rates, which are likely to reduce power output and delay relaxation, with an increased economy of contraction. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149957 |
Thr143 |
RGKFKRPtLRRVRIS |
Homo sapiens |
|
| pmid |
sentence |
| 17010989 |
Pkc-betaii sensitizes cardiac myofilaments to ca2+ by phosphorylating troponin i on threonine-144. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PRKCG | down-regulates
phosphorylation
|
TNNI3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134632 |
Ser42 |
AKKKSKIsASRKLQL |
Homo sapiens |
|
| pmid |
sentence |
| 15769444 |
Phosphorylation at ser 23/24 (e.g., by pka or pkg) results in reduction in myofilament ca2+ sensitivity and an increase in crossbridge cycling rate, leading to acceleration of relaxation and an increase in power output but a reduced economy of contraction. Conversely, phosphorylation at ser 43/45 (by pkc) is associated with reduced maximum ca2+-activated force and decreased crossbridge cycling rates, which are likely to reduce power output and delay relaxation, with an increased economy of contraction. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134636 |
Ser44 |
KKSKISAsRKLQLKT |
Homo sapiens |
|
| pmid |
sentence |
| 15769444 |
Phosphorylation at ser 23/24 (e.g., by pka or pkg) results in reduction in myofilament ca2+ sensitivity and an increase in crossbridge cycling rate, leading to acceleration of relaxation and an increase in power output but a reduced economy of contraction. Conversely, phosphorylation at ser 43/45 (by pkc) is associated with reduced maximum ca2+-activated force and decreased crossbridge cycling rates, which are likely to reduce power output and delay relaxation, with an increased economy of contraction. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| + |
PRKCA | down-regulates
phosphorylation
|
TNNI3 |
0.349 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134613 |
Ser42 |
AKKKSKIsASRKLQL |
Homo sapiens |
|
| pmid |
sentence |
| 15769444 |
Phosphorylation at ser 23/24 (e.g., by pka or pkg) results in reduction in myofilament ca2+ sensitivity and an increase in crossbridge cycling rate, leading to acceleration of relaxation and an increase in power output but a reduced economy of contraction. Conversely, phosphorylation at ser 43/45 (by pkc) is associated with reduced maximum ca2+-activated force and decreased crossbridge cycling rates, which are likely to reduce power output and delay relaxation, with an increased economy of contraction. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134617 |
Ser44 |
KKSKISAsRKLQLKT |
Homo sapiens |
|
| pmid |
sentence |
| 15769444 |
Phosphorylation at ser 23/24 (e.g., by pka or pkg) results in reduction in myofilament ca2+ sensitivity and an increase in crossbridge cycling rate, leading to acceleration of relaxation and an increase in power output but a reduced economy of contraction. Conversely, phosphorylation at ser 43/45 (by pkc) is associated with reduced maximum ca2+-activated force and decreased crossbridge cycling rates, which are likely to reduce power output and delay relaxation, with an increased economy of contraction. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| + |
PRKCA |
phosphorylation
|
TNNI3 |
0.349 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248890 |
Ser77 |
GEKGRALsTRCQPLE |
in vitro |
|
| pmid |
sentence |
| 2584239 |
We have now determined that PKC phosphorylated serine 43 (and/or serine 45), serine 78, and threonine 144 in the free Tn-I subunit |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
STK4 |
phosphorylation
|
TNNI3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182049 |
Thr129 |
ITEIADLtQKIFDLR |
Homo sapiens |
|
| pmid |
sentence |
| 18986304 |
Ms analysis indicated that mst1 phosphorylates ctni at thr(31), thr(51), thr(129) and thr(143). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182053 |
Thr143 |
RGKFKRPtLRRVRIS |
Homo sapiens |
|
| pmid |
sentence |
| 18986304 |
Ms analysis indicated that mst1 phosphorylates ctni at thr(31), thr(51), thr(129) and thr(143). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182057 |
Thr31 |
SNYRAYAtEPHAKKK |
Homo sapiens |
|
| pmid |
sentence |
| 18986304 |
Ms analysis indicated that mst1 phosphorylates ctni at thr(31), thr(51), thr(129) and thr(143). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182061 |
Thr51 |
SRKLQLKtLLLQIAK |
Homo sapiens |
|
| pmid |
sentence |
| 18986304 |
Ms analysis indicated that mst1 phosphorylates ctni at thr(31), thr(51), thr(129) and thr(143). |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney |
| + |
PRKCD | down-regulates
phosphorylation
|
TNNI3 |
0.276 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-204666 |
Thr143 |
RGKFKRPtLRRVRIS |
Homo sapiens |
|
| pmid |
sentence |
| 24585778 |
Length-dependent activation is modulated by cardiac troponin i bisphosphorylation at ser23 and ser24 but not by thr143 phosphorylation. Thr143 is a known target of protein kinase c (pkc) whose activity is increased in cardiac disease |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178888 |
Thr143 |
RGKFKRPtLRRVRIS |
Homo sapiens |
|
| pmid |
sentence |
| 18550549 |
Src phosphorylates pkcdelta at tyr311 and tyr332 leading to enhanced pkcdelta autophosphorylation at thr505 (its activation loop) and pkcdelta-dependent ctni phosphorylation at both ser23/ser24 and thr144. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
3.0
TNNI3
- 
- 