| + |
PRKCQ | down-regulates activity 
phosphorylation
|
IRS1 |
0.549 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260906 |
Ser1101 |
GCRRRHSsETFSSTP |
Mus musculus |
|
| pmid |
sentence |
| 15364919 |
Protein kinase C Theta inhibits insulin signaling by phosphorylating IRS1 at Ser(1101). |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PRKCQ | up-regulates activity 
phosphorylation
|
ARHGEF6 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272169 |
Ser225 |
KSSERPLsPKAVKGF |
|
|
| pmid |
sentence |
| 25694429 |
Recently, we have reported that the active form of Rac 1 GTPase binds to the glycogen phosphorylase muscle isoform (PYGM) and modulates its enzymatic activity leading to T cell proliferation.|More specifically, αPIX, a known guanine nucleotide exchange factor for the small GTPases of the Rho family, preferentially Rac 1, mediates PYGM activation in Kit 225 T cells stimulated with IL-2. Using directed mutagenesis, phosphorylation of αPIX Rho-GEF serines 225 and 488 is required for activation of the Rac 1/PYGM pathway. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272168 |
Ser488 |
LSASPRMsGFIYQGK |
|
|
| pmid |
sentence |
| 25694429 |
Recently, we have reported that the active form of Rac 1 GTPase binds to the glycogen phosphorylase muscle isoform (PYGM) and modulates its enzymatic activity leading to T cell proliferation.|More specifically, αPIX, a known guanine nucleotide exchange factor for the small GTPases of the Rho family, preferentially Rac 1, mediates PYGM activation in Kit 225 T cells stimulated with IL-2. Using directed mutagenesis, phosphorylation of αPIX Rho-GEF serines 225 and 488 is required for activation of the Rac 1/PYGM pathway. |
|
| Publications: |
2 |
| + |
PRKCQ | up-regulates activity
phosphorylation
|
PTPN7 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276045 |
Ser246 |
QYQEERRsVKHILFS |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 16479000 |
PKC θ is required for HePTP translocation to the immune synapse. PKC θ phosphorylates HePTP at S225 in primary T cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCQ | up-regulates activity
phosphorylation
|
STK39 |
0.458 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276006 |
Ser309 |
MMKKYGKsFRKLLSL |
in vitro |
|
| pmid |
sentence |
| 14988727 |
Recombinant SPAK was phosphorylated on Ser-311 in its kinase domain by PKCtheta, but not by PKCalpha. This synergistic activity, as well as the receptor-induced SPAK activation, required the PKCtheta-interacting region of SPAK, and Ser-311 mutation greatly reduced these activities of SPAK. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276007 |
Ser323 |
LCLQKDPsKRPTAAE |
in vitro |
|
| pmid |
sentence |
| 14988727 |
Recombinant SPAK was phosphorylated on Ser-311 in its kinase domain by PKCtheta, but not by PKCalpha. This synergistic activity, as well as the receptor-induced SPAK activation, required the PKCtheta-interacting region of SPAK, and Ser-311 mutation greatly reduced these activities of SPAK. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PRKCQ | up-regulates activity
phosphorylation
|
WIPF1 |
0.328 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249181 |
Ser488 |
RNESRSGsNRRERGA |
in vitro |
|
| pmid |
sentence |
| 12504004 |
TCR engagement also causes PKCtheta-dependent phosphorylation of WIP, causing the disengagement of WASP from the WIP-WASP complex, thereby releasing it from WIP inhibition. These results suggest that the ZAP-70-CrkL-WIP pathway and PKCtheta link TCR to WASP activation. | These results suggest that phosphorylation at S488 disrupts WIP binding to WASP. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKCQ | up-regulates activity
phosphorylation
|
ICAM3 |
0.339 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248979 |
Ser518 |
REHQRSGsYHVREES |
Homo sapiens |
JURKAT Cell |
| pmid |
sentence |
| 9268366 |
Ser489 was a phosphorylation site in vitro for recombinant protein kinase Ctheta. Finally, treatment of Jurkat cells with chelerythrine chloride, a protein kinase C inhibitor, prevented ICAM-3-triggered spreading. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCQ | up-regulates activity
phosphorylation
|
CARD11 |
0.768 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249193 |
Ser644 |
NLMFRKFsLERPFRP |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 21157432 |
NF-kappaB activation is triggered by PKCteta-dependent phosphorylation of Carma1 after TCR/CD28 co-stimulation. PKCteta-phosphorylated Carma1 was suggested to function as a molecular scaffold that recruits preassembled Bcl10-Malt1 complexes to the membrane|we demonstrate that PP2A removes PKCteta-dependent phosphorylation of Ser645 in Carma1, and show that maintenance of this phosphorylation is correlated with increased T-cell activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCQ | up-regulates activity
phosphorylation
|
TBK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272472 |
Ser716 |
HILERFGsLTMDGGL |
Homo sapiens |
|
| pmid |
sentence |
| 31792381 |
TBKBP1 recruits TBK1 to protein kinase C-theta (PKCθ) through a scaffold protein, CARD10. This enables PKCθ to phosphorylate TBK1 at Ser 716, a crucial step for TBK1 activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCQ | up-regulates activity
phosphorylation
|
GRM5 |
0.294 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249283 |
Ser840 |
VRSAFTTsTVVRMHV |
in vitro |
|
| pmid |
sentence |
| 15894802 |
Thus, we showed that it is phosphorylation of Ser-839, not Thr-840, that is absolutely required for the unique Ca2+ oscillations produced by mGluR5 activation. The Thr-840 residue is important only in that it is permissive for the PKC-dependent phosphorylation of Ser-839. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249290 |
Thr841 |
RSAFTTStVVRMHVG |
in vitro |
|
| pmid |
sentence |
| 15894802 |
Thus, we showed that it is phosphorylation of Ser-839, not Thr-840, that is absolutely required for the unique Ca2+ oscillations produced by mGluR5 activation. The Thr-840 residue is important only in that it is permissive for the PKC-dependent phosphorylation of Ser-839. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PRKCQ | down-regulates activity
phosphorylation
|
CARD11 |
0.768 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276298 |
Ser893 |
SPRLSRAsFLFGQLL |
in vitro |
|
| pmid |
sentence |
| 35230873 |
PKCθ-catalyzed CARD11 Ser893 phosphorylation impairs CBM complex formation |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKCQ | up-regulates
phosphorylation
|
RAPGEF2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-181186 |
Ser960 |
KKRVRRSsFLNAKKL |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 18796635 |
After t-cell activation, the direct phosphorylation of rapgef2 at ser960 by pkc- theta regulates rap1 activation as well as lfa-1 adhesiveness to icam-1. Pkc- theta and its effector rapgef2 are critical factors in tcr signaling to rap1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCQ | up-regulates
phosphorylation
|
RASGRP3 |
0.333 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-130490 |
Thr133 |
YDWMRRVtQRKKVSK |
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 15545601 |
Activation of rasgrp3 by phosphorylation of thr-133 is required for b cell receptor-mediated ras activation. our data suggest that pkc, after being activated by diacylglycerol, phosphorylates rasgrp3, thereby contributing to its full activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCQ | up-regulates activity
phosphorylation
|
FOSL1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260878 |
Thr217 |
LEPEALHtPTLMTTP |
Homo sapiens |
|
| pmid |
sentence |
| 27816489 |
PKCθ-induced phosphorylations, in part at T217 and T227 residues, strongly and specifically increased Fra-1 transcriptional activity through the stimulation of Fra-1 transactivation domain, without affecting JUN factors. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260879 |
Thr227 |
LEPEALHtPTLMTTP |
Homo sapiens |
|
| pmid |
sentence |
| 27816489 |
PKCθ-induced phosphorylations, in part at T217 and T227 residues, strongly and specifically increased Fra-1 transcriptional activity through the stimulation of Fra-1 transactivation domain, without affecting JUN factors. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCQ | up-regulates activity
phosphorylation
|
PRKCQ |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249298 |
Thr219 |
SAINSREtMFHKERF |
Homo sapiens |
|
| pmid |
sentence |
| 16252004 |
Critical role of novel Thr-219 autophosphorylation for the cellular function of PKCtheta in T lymphocytes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCQ | down-regulates activity
phosphorylation
|
HABP4 |
0.306 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249250 |
Thr354 |
RKPANDItSQLEINF |
Homo sapiens |
|
| pmid |
sentence |
| 14699138 |
We found a strong phosphorylation of Ki-1/57 by PKCalphabeta, PKCdelta, PKClambda/zeta, and especially by PKCsigma, however not by PKCmi. These data show that Ki-1/57 can serve in principal as a substrate for a wide variety of different PKC isoforms but also that its phosphorylation is strongest with PKCsigma. | This suggests that the two threonine residues present in this fragment (Thr354 and Thr375) might be the main target residues for phosphorylation by PKC in vitro. | Ki-1/57 Exits the Nucleus upon PMA Activation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249256 |
Thr375 |
GRGARGGtRGGRGRI |
Homo sapiens |
|
| pmid |
sentence |
| 14699138 |
We found a strong phosphorylation of Ki-1/57 by PKCalphabeta, PKCdelta, PKClambda/zeta, and especially by PKCsigma, however not by PKCmi. These data show that Ki-1/57 can serve in principal as a substrate for a wide variety of different PKC isoforms but also that its phosphorylation is strongest with PKCsigma. | This suggests that the two threonine residues present in this fragment (Thr354 and Thr375) might be the main target residues for phosphorylation by PKC in vitro. | Ki-1/57 Exits the Nucleus upon PMA Activation |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCQ | down-regulates activity
phosphorylation
|
NOS3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251636 |
Thr495 |
TGITRKKtFKEVANA |
Homo sapiens |
Vascular Endothelium |
| pmid |
sentence |
| 24379783 |
The phosphorylation of both S617 and S635 have also been shown to promote increased eNOS-derived NO release (Michell et al., 2002). The phosphorylaiton of S617 can be induced by PKA or Akt activity, and may serve to sensitize eNOS to calmodulin binding and modulate the phosphorylation of other eNOS sites |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAP4K3 | up-regulates
phosphorylation
|
PRKCQ |
0.388 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176744 |
Thr538 |
LGDAKTNtFCGTPDY |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 21983831 |
We report that the kinase glk (map4k3) directly activated pkc-? During tcr signaling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCQ |
phosphorylation
|
MSN |
0.463 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249013 |
Thr558 |
LGRDKYKtLRQIRQG |
Homo sapiens |
Acute Myeloid Leukemia Cell |
| pmid |
sentence |
| 9856983 |
By using mass spectroscopy and direct microsequencing of CNBr fragments of phospho-moesin, the phosphorylation site was identified as KYKT*LRQIR (where * indicates the phosphorylation site) (Thr558), which is conserved in the ERM family | Thus, PKC-theta is identified as a major kinase within cells with specificity for moesin and with activation under non-classical PKC conditions. It appears likely that this activity corresponds to a specific intracellular pathway controlling the function of moesin as well as other ERM proteins. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LCK |
phosphorylation
|
PRKCQ |
0.543 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-74574 |
Tyr90 |
SETTVELySLAERCR |
Homo sapiens |
|
| pmid |
sentence |
| 10652356 |
Tyrosine 90 (tyr-90) in the regulatory domain of pkctheta was identified as the major phosphorylation site by lck. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PDPK1 | up-regulates
phosphorylation
|
PRKCQ |
0.547 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134869 |
|
|
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 15802604 |
We demonstrate that 3-phosphoinositide-dependent kinase 1 (pdk1) has an essential role in this pathway by regulating the activation of pkc and through signal-dependent recruiting of both pkc and card11 to lipid rafts. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCQ | up-regulates
phosphorylation
|
HSF1 |
0.355 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-200576 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23352416 |
At the same time, ea causes pkc?-Mediated phosphorylation and activation of the transcription factor heat shock factor 1, an inducer of glucose dependence. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CARD10 | up-regulates activity
relocalization
|
PRKCQ |
0.411 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272471 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31792381 |
TBKBP1 recruits TBK1 to protein kinase C-theta (PKCθ) through a scaffold protein, CARD10. This enables PKCθ to phosphorylate TBK1 at Ser 716, a crucial step for TBK1 activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCQ | form complex 
binding
|
PKCtheta/Nfix |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-238019 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 20178747 |
In the case of the MCK promoter, Nfix forms a complex with PKC theta that binds, phosphorylates, and activates MEF2A. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PRKCQ | up-regulates activity
phosphorylation
|
MGluR |
0.294 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270273 |
|
|
in vitro |
|
| pmid |
sentence |
| 15894802 |
Thus, we showed that it is phosphorylation of Ser-839, not Thr-840, that is absolutely required for the unique Ca2+ oscillations produced by mGluR5 activation. The Thr-840 residue is important only in that it is permissive for the PKC-dependent phosphorylation of Ser-839. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKCQ | up-regulates activity
phosphorylation
|
CBL |
0.361 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274144 |
|
|
Mus musculus |
T-lymphocyte |
| pmid |
sentence |
| 26284074 |
PKC-θ-mediated phosphorylation of serine and tyrosine residues of c-Cbl prevents its inhibitory effect. Phosphorylation of c-Cbl by PKC-θ inhibits the recruitment of Sh2-containing proteins and subsequent association of cbl E3 ubiquitin ligase with its target proteins |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PRKCQ | up-regulates quantity by expression 
transcriptional regulation
|
ITGB1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241525 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 26431586 |
It is known that the teta isoform of the PKC family promotes the fusion of myoblasts and regulates the expression of caveolin-3 and beta1D integrin [15]. Of note, it has also been demonstrated that PKCepsilon expression increases during insulin-induced myogenic differentiation of the C2C12 cells. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
VAV1 | up-regulates
|
PRKCQ |
0.601 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-75827 |
|
|
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 10725744 |
Vav synergizes with protein kinase c theta to mediate il-4 gene expression in response to cd28 costimulation in t cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FYN | up-regulates
phosphorylation
|
PRKCQ |
0.351 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-68798 |
|
|
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 10383400 |
Further indications of direct interaction are that p59fyn potentiates ?PKC Catalytic activity and that ?PKC Is a substrate for tyrosine phosphorylation by p59fyn. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
1,2-diacyl-sn-glycerol | up-regulates activity
binding
|
PRKCQ |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-242596 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14967450 |
The molecular requirements for diacylglycerol (dag) and calcium (ca2+) to promote pkc membrane translocation, the hallmark of pkc activation, have been clarified. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PRKCQ
- 
- 