+ |
PRKCI | down-regulates
phosphorylation
|
BAD |
0.324 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-172886 |
Ser118 |
GRELRRMsDEFVDSF |
Homo sapiens |
Glioblastoma Cell |
pmid |
sentence |
21419810 |
In-vitro kinase activity assay showed that pkc-_ directly phosphorylated bad at phospho specific residues, ser-112, ser-136 and ser-155 which in turn induced inactivation of bad and disruption of bad/bcl-xl dimer |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-172890 |
Ser75 |
EIRSRHSsYPAGTED |
Homo sapiens |
Glioblastoma Cell |
pmid |
sentence |
21419810 |
In-vitro kinase activity assay showed that pkc-_ directly phosphorylated bad at phospho specific residues, ser-112, ser-136 and ser-155 which in turn induced inactivation of bad and disruption of bad/bcl-xl dimer |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-172894 |
Ser99 |
PFRGRSRsAPPNLWA |
Homo sapiens |
Glioblastoma Cell |
pmid |
sentence |
21419810 |
In-vitro kinase activity assay showed that pkc-_ directly phosphorylated bad at phospho specific residues, ser-112, ser-136 and ser-155 which in turn induced inactivation of bad and disruption of bad/bcl-xl dimer |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
PRKCI | down-regulates activity
phosphorylation
|
FBXW7 |
0.27 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277250 |
Ser18 |
KRRRTGGsLRGNPSS |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
28850619 |
Here, we report that Fbw7α, the only Fbw7 isoform detected in eggs, is phosphorylated by PKC (protein kinase C) at a key residue (S18) in a manner coincident with Fbw7α inactivation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKCI | down-regulates activity
phosphorylation
|
MAPT (isoform 2) |
0.269 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275446 |
Ser324 |
RHLSNVSsTGSIDMV |
in vitro |
|
pmid |
sentence |
10090741 |
We have studied the relationship between the phosphorylation oftau by several kinases (MARK, PKA, MAPK, GSK3) and its assembly into PHFs. By contrast, MARK and PKA phosphorylate several sites within the repeats (notably theKXGS motifs including Ser262, Ser324, and Ser356, plus Ser320); in addition PKA phosphorylates somesites in the flanking domains, notably Ser214. This type of phosphorylation strongly reduces tau’s affinityfor microtubules, and at the same time inhibits tau’s assembly into PHFs. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
PRKCI | up-regulates activity
phosphorylation
|
VIM |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277623 |
Ser34 |
SRSYVTTsTRTYSLG |
Homo sapiens |
Prostate Cancer Cell Line |
pmid |
sentence |
33525953 |
Results suggest that aPKCs target multiple activation sites (Ser33/39/56) on Vimentin and therefore is essential for VIF dynamics regulation during the metastasis of prostate cancer cells. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKCI | up-regulates quantity by stabilization
phosphorylation
|
PARD6A |
0.86 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276432 |
Ser345 |
RGDGSGFsL |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
23249950 |
APKC associates and phosphorylates Par6 on S345. aPKC expression stabilizes Par6 protein levels. We show that the aPKC, PKCι, interacts with TGF-β receptors through Par6 and that these proteins localize to the leading edge of migrating cells. Furthermore, Par6 phosphorylation on serine 345 by TGF-β receptors is enhanced in the presence of aPKC. aPKC kinase activity, as well as an association with Par6, were found to be important for Par6 phosphorylation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKCI | up-regulates activity
phosphorylation
|
LLGL2 |
0.709 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263180 |
Ser653 |
LKKSLRQsFRRMRRS |
Canis lupus familiaris |
MDCK Cell |
pmid |
sentence |
12725730 |
This finding indicates that both mLgl-2 and mLgl-1 are phosphorylated in vivo in an aPKC lambda activity-dependent manner. |
|
Publications: |
1 |
Organism: |
Canis Lupus Familiaris |
+ |
PRKCI | up-regulates activity
phosphorylation
|
LLGL1 |
0.651 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263179 |
Ser659 |
RVKSLKKsLRQSFRR |
Canis lupus familiaris |
|
pmid |
sentence |
12725730 |
This finding indicates that both mLgl-2 and mLgl-1 are phosphorylated in vivo in an aPKC lambda activity-dependent manner. |
|
Publications: |
1 |
Organism: |
Canis Lupus Familiaris |
+ |
PRKCI | up-regulates
phosphorylation
|
ECT2 |
0.488 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-170790 |
Thr359 |
YLYEKANtPELKKSV |
Homo sapiens |
Lung Cancer Cell |
pmid |
sentence |
21189248 |
Our data support a model in which pkc?-Mediated phosphorylation regulates ect2 binding to the oncogenic pkc?-Par6 complex thereby activating rac1 activity and driving transformed growth and invasion. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKCI | down-regulates activity
phosphorylation
|
NOS3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251635 |
Thr495 |
TGITRKKtFKEVANA |
Homo sapiens |
|
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 |
+ |
PRKCI | up-regulates
phosphorylation
|
EZR |
0.35 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-160855 |
Thr567 |
QGRDKYKtLRQIRQG |
Homo sapiens |
CACO-2 Cell |
pmid |
sentence |
18270268 |
Pkciota phosphorylated ezrin on t567 in vitro, and in sf9 cells that do not activate human ezrin. we conclude that, although other molecular mechanisms contribute to ezrin activation, apically localized phosphorylation by pkciota is essential for the activation and normal distribution of ezrin at the early stages of intestinal epithelial cell differentiation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SRC | up-regulates
phosphorylation
|
PRKCI |
0.512 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-111920 |
Tyr265 |
RVIGRGSyAKVLLVR |
Homo sapiens |
|
pmid |
sentence |
11713277 |
Nerve growth factor stimulates multisite tyrosine phosphorylation and activation of the atypical protein kinase c's via a src kinase pathway. tyrosine 256, 271, and 325 were identified as major sites phosphorylated by src in the catalytic domain. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-111924 |
Tyr280 |
LKKTDRIyAMKVVKK |
Homo sapiens |
|
pmid |
sentence |
11713277 |
Nerve growth factor stimulates multisite tyrosine phosphorylation and activation of the atypical protein kinase c's via a src kinase pathway. tyrosine 256, 271, and 325 were identified as major sites phosphorylated by src in the catalytic domain. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-111928 |
Tyr334 |
RLFFVIEyVNGGDLM |
Homo sapiens |
|
pmid |
sentence |
11713277 |
Nerve growth factor stimulates multisite tyrosine phosphorylation and activation of the atypical protein kinase c's via a src kinase pathway. tyrosine 256, 271, and 325 were identified as major sites phosphorylated by src in the catalytic domain. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
PRKCI | down-regulates
phosphorylation
|
NUMB |
0.761 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-156765 |
|
|
Homo sapiens |
|
pmid |
sentence |
17609107 |
Numb is regulated by phosphorylation since the protein is released from ccss and no longer binds integrins when phosphorylated by atypical protein kinase c (apkc). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
VCB-Cul2 | down-regulates quantity by destabilization
polyubiquitination
|
PRKCI |
0.367 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272591 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
11574546 |
The von Hippel-Lindau tumor-suppressor protein (pVHL) forms a protein complex (VCB-Cul2) with elongin C, elongin B, Cul-2, and Rbx1, which functions as a ubiquitin-protein ligase (E3). The alpha-subunits of the hypoxia-inducible factors have been identified as targets for the VCB-Cul2 ubiquitin ligase. we show that PKClambda can be ubiquitinated in vitro in a cell-free ubiquitination assay using purified recombinant components including VCB-Cul2. Given the known function of aPKC in the regulation of cell polarity and cell growth, PKClambda may be a target of pVHL in its function as a tumor suppressor.Degradation of the Ubiquitin-conjugated Active Form of PKCλ Is Blocked by a Proteasome Inhibitor in Vivo |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
1,2-diacyl-sn-glycerol | up-regulates activity
binding
|
PRKCI |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-242581 |
|
|
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 |
+ |
RAB2A | down-regulates activity
binding
|
PRKCI |
0.468 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261301 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
14570876 |
Rab2 Binds to the PKCι/λ Regulatory Domain and Inhibits PKCι/λ-dependent GAPDH Phosphorylation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |