| + |
CDK5/CDK5R1 | up-regulates activity 
phosphorylation
|
VRK3 |
0.365 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275545 |
Ser108 |
RPPTPKSsPQKTRKS |
|
|
| pmid |
sentence |
| 27346674 |
Vaccinia-related kinase 3 (VRK3), a member of the VRK family, is widely expressed in human tissues and increases VHR phosphatase activity through a direct binding|Here we report that oxidative stress-induced cyclin-dependent kinase 5 (CDK5) activation stimulates neuroprotective signaling via phosphorylation of vaccinia-related kinase 3 (VRK3) at Ser 108. The binding of vaccinia H1-related (VHR) phosphatase to phosphorylated VRK3 increased its affinity for phospho-ERK and subsequently downregulated ERK activation| |
|
| Publications: |
1 |
| + |
CDK5/CDK5R1 | up-regulates activity
phosphorylation
|
SUDS3 |
0.285 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262739 |
Ser228 |
RTLNKLKsPKRPASP |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15489224 |
Cdk5/p35 phosphorylates mSds3 and regulates mSds3-mediated repression of transcription. the dimerization of the phosphorylation-deficient mutant of mSds3 (S228A) was not greatly enhanced by p35 when compared with wild type (Fig. 5D). This finding suggests that the phosphorylation of mSds3 by active Cdk5 increases the homodimerization potential of mSds3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK5/CDK5R1 | down-regulates 
phosphorylation
|
MAPT |
0.695 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251587 |
Ser235 |
SPQDSPPsKASPAQD |
Homo sapiens |
|
| pmid |
sentence |
| 21215781 |
Cdk5 regulates app (amyloid precursor protein) processing and tau hyperphosphorylationtau phosphorylation at t231, s235 and s262 also contributes to the dissociation of tau from microtubules |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251599 |
Ser519 |
SGYSSPGsPGTPGSR |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12226093 |
Phosphopeptide mapping revealed enhanced phosphorylation of ser(202)/thr(205) residues by p25-cdk5 considering the fact that phosphorylation of ser(202)/thr(205) antagonizes the tau-mediated nucleation of tubulin, p25-cdk5 may play a pivotal role in neuronal cell death in alzheimer's disease. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251600 |
Thr522 |
SSPGSPGtPGSRSRT |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12226093 |
Phosphopeptide mapping revealed enhanced phosphorylation of ser(202)/thr(205) residues by p25-cdk5 considering the fact that phosphorylation of ser(202)/thr(205) antagonizes the tau-mediated nucleation of tubulin, p25-cdk5 may play a pivotal role in neuronal cell death in alzheimer's disease. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251601 |
Thr548 |
KKVAVVRtPPKSPSS |
Homo sapiens |
|
| pmid |
sentence |
| 21215781 |
However, other kinases, such as cdk5, p38 and pka, also phosphorylate tau at t231tau phosphorylation at t231, s235 and s262 also contributes to the dissociation of tau from microtubules |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| Pathways: | Alzheimer |
| + |
CDK5/CDK5R1 |
phosphorylation
|
DCX |
0.415 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250654 |
Ser28 |
SRMNGLPsPTHSAHC |
in vitro |
|
| pmid |
sentence |
| 14741103 |
In order to determine the sites of phosphorylation by Cdk5, serine or threonine in the nine potential sites were substituted with alanine by site-directed mutagenesis to create mutant Dcx proteins. These were analyzed by co-transfection of 293T cells with cdk5/p35. All-sites-A mutant Dcx showed no slower migrating species on Western analysis, indicating that removal of all nine possible sites is sufficient to block the phosphorylation by Cdk5/p35 (Figure 3D). However, each single mutant Dcx retains the slower migrating species similar to the wild-type Dcx, suggesting that any single mutation is not sufficient to block phosphorylation by Cdk5/p35. | Therefore, S28 residue may be a substrate in vitro, but our best efforts failed to detect phosphorylation of S28 in vivo. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250655 |
Ser287 |
ATAGPKAsPTPQKTS |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 14741103 |
In order to determine the sites of phosphorylation by Cdk5, serine or threonine in the nine potential sites were substituted with alanine by site-directed mutagenesis to create mutant Dcx proteins. hese were analyzed by co-transfection of 293T cells with cdk5/p35. All-sites-A mutant Dcx showed no slower migrating species on Western analysis, indicating that removal of all nine possible sites is sufficient to block the phosphorylation by Cdk5/p35. However, each single mutant Dcx retains the slower migrating species similar to the wild-type Dcx, suggesting that any single mutation is not sufficient to block phosphorylation by Cdk5/p35. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250658 |
Ser306 |
GPMRRSKsPADSGND |
Homo sapiens |
|
| pmid |
sentence |
| 14741103 |
In order to determine the sites of phosphorylation by Cdk5, serine or threonine in the nine potential sites were substituted with alanine by site-directed mutagenesis to create mutant Dcx proteins. hese were analyzed by co-transfection of 293T cells with cdk5/p35. All-sites-A mutant Dcx showed no slower migrating species on Western analysis, indicating that removal of all nine possible sites is sufficient to block the phosphorylation by Cdk5/p35. However, each single mutant Dcx retains the slower migrating species similar to the wild-type Dcx, suggesting that any single mutation is not sufficient to block phosphorylation by Cdk5/p35. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250667 |
Ser332 |
STPKSKQsPISTPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14741103 |
In order to determine the sites of phosphorylation by Cdk5, serine or threonine in the nine potential sites were substituted with alanine by site-directed mutagenesis to create mutant Dcx proteins. hese were analyzed by co-transfection of 293T cells with cdk5/p35. All-sites-A mutant Dcx showed no slower migrating species on Western analysis, indicating that removal of all nine possible sites is sufficient to block the phosphorylation by Cdk5/p35. However, each single mutant Dcx retains the slower migrating species similar to the wild-type Dcx, suggesting that any single mutation is not sufficient to block phosphorylation by Cdk5/p35. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250673 |
Ser339 |
SPISTPTsPGSLRKH |
Homo sapiens |
|
| pmid |
sentence |
| 14741103 |
In order to determine the sites of phosphorylation by Cdk5, serine or threonine in the nine potential sites were substituted with alanine by site-directed mutagenesis to create mutant Dcx proteins. hese were analyzed by co-transfection of 293T cells with cdk5/p35. All-sites-A mutant Dcx showed no slower migrating species on Western analysis, indicating that removal of all nine possible sites is sufficient to block the phosphorylation by Cdk5/p35. However, each single mutant Dcx retains the slower migrating species similar to the wild-type Dcx, suggesting that any single mutation is not sufficient to block phosphorylation by Cdk5/p35. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250656 |
Thr289 |
AGPKASPtPQKTSAK |
Homo sapiens |
|
| pmid |
sentence |
| 14741103 |
In order to determine the sites of phosphorylation by Cdk5, serine or threonine in the nine potential sites were substituted with alanine by site-directed mutagenesis to create mutant Dcx proteins. hese were analyzed by co-transfection of 293T cells with cdk5/p35. All-sites-A mutant Dcx showed no slower migrating species on Western analysis, indicating that removal of all nine possible sites is sufficient to block the phosphorylation by Cdk5/p35. However, each single mutant Dcx retains the slower migrating species similar to the wild-type Dcx, suggesting that any single mutation is not sufficient to block phosphorylation by Cdk5/p35. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250659 |
Thr326 |
TSSSQLStPKSKQSP |
Homo sapiens |
|
| pmid |
sentence |
| 14741103 |
In order to determine the sites of phosphorylation by Cdk5, serine or threonine in the nine potential sites were substituted with alanine by site-directed mutagenesis to create mutant Dcx proteins. hese were analyzed by co-transfection of 293T cells with cdk5/p35. All-sites-A mutant Dcx showed no slower migrating species on Western analysis, indicating that removal of all nine possible sites is sufficient to block the phosphorylation by Cdk5/p35. However, each single mutant Dcx retains the slower migrating species similar to the wild-type Dcx, suggesting that any single mutation is not sufficient to block phosphorylation by Cdk5/p35. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250660 |
Thr336 |
SKQSPIStPTSPGSL |
Homo sapiens |
|
| pmid |
sentence |
| 14741103 |
In order to determine the sites of phosphorylation by Cdk5, serine or threonine in the nine potential sites were substituted with alanine by site-directed mutagenesis to create mutant Dcx proteins. hese were analyzed by co-transfection of 293T cells with cdk5/p35. All-sites-A mutant Dcx showed no slower migrating species on Western analysis, indicating that removal of all nine possible sites is sufficient to block the phosphorylation by Cdk5/p35. However, each single mutant Dcx retains the slower migrating species similar to the wild-type Dcx, suggesting that any single mutation is not sufficient to block phosphorylation by Cdk5/p35. |
|
| Publications: |
8 |
Organism: |
In Vitro, Homo Sapiens |
| + |
CDK5/CDK5R1 | up-regulates activity
phosphorylation
|
DCX |
0.415 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250657 |
Ser297 |
PQKTSAKsPGPMRRS |
Homo sapiens |
|
| pmid |
sentence |
| 14741103 |
We identified that Ser297 is the major phosphorylation site by Cdk5. Phosphorylation of this site occurs in human. | Mutation of Ser297 blocks the effect of Dcx on migration in a fashion similar to pharmacological inhibition of Cdk5 activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK5/CDK5R1 | up-regulates activity
phosphorylation
|
TP53 |
0.57 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250674 |
Ser315 |
LPNNTSSsPQPKKKP |
Rattus norvegicus |
PC-12 Cell |
| pmid |
sentence |
| 12064478 |
the present study it is shown that in apoptotic PC12 cells the levels of p53 and Cdk5 increase concomitantly. Further, Cdk5/p25 effectively phosphorylates recombinant p53 in vitro. Transient transfection of Cdk5/p25 into cells results in an increase in p53 levels, as well as the expression of the p53-responsive genes p21 and Bax. Furthermore, evidence is provided that increased Cdk5 activity increases p53 transcriptional activity significantly, suggesting that p53 is modulated in situ by Cdk5. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
CDK5/CDK5R1 | down-regulates activity
phosphorylation
|
MAPT |
0.695 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251598 |
Ser516 |
GDRSGYSsPGSPGTP |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251588 |
Ser519 |
SGYSSPGsPGTPGSR |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251589 |
Ser531 |
GSRSRTPsLPTPPTR |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251590 |
Ser552 |
VVRTPPKsPSSAKSR |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251591 |
Ser713 |
GAEIVYKsPVVSGDT |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251592 |
Ser721 |
PVVSGDTsPRHLSNV |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251597 |
Thr498 |
KTPPAPKtPPSSGEP |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251593 |
Thr522 |
SSPGSPGtPGSRSRT |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251594 |
Thr529 |
TPGSRSRtPSLPTPP |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251595 |
Thr534 |
SRTPSLPtPPTREPK |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251596 |
Thr548 |
KKVAVVRtPPKSPSS |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Publications: |
11 |
Organism: |
Homo Sapiens |
| Pathways: | Alzheimer |
| + |
CDK5/CDK5R1 | up-regulates activity
phosphorylation
|
NDEL1 |
0.623 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250678 |
Thr219 |
ASLSLPAtPVGKGTE |
Mus musculus |
Brain |
| pmid |
sentence |
| 12796778 |
Three specific phosphorylation sites (Ser198, Thr219 and Ser231) and two weak phosphorylation sites (Ser242 and Thr245) for CDK5/p35 are located in this region of NUDEL | Each single or double mutant compromised,and the triple mutant completely eliminated, interaction with 14-3-3ε. | 14-3-3ε sustains NUDEL phosphorylation and protects it from phosphatase.e dynein motor function. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
CDK5/CDK5R1 | up-regulates activity
phosphorylation
|
BACE1 |
0.384 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276934 |
Thr252 |
YTGSLWYtPIRREWY |
Rattus norvegicus |
PC-12 Cell |
| pmid |
sentence |
| 26317805 |
First, we show that BACE1 is phosphorylated by the p25/Cdk5 complex at Thr252 and that this phosphorylation increases BACE1 activity. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
CDK5/CDK5R1 | down-regulates activity
phosphorylation
|
MAP2K1 |
0.478 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250653 |
Thr286 |
VEGDAAEtPPRPRTP |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 11684694 |
Phosphorylation of MEK1 by cdk5/p35 down-regulates the mitogen-activated protein kinase pathway. | suggesting that Thr286 in MEK1 is a site of cdk5/p35 phosphorylation that inhibits MEK1 activity. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
CDK5R1 | form complex 
binding
|
CDK5/CDK5R1 |
0.942 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250682 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11331872 |
Induced p35 forms a complex with Cdk5 and activates its kinase activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Alzheimer |
| + |
CAPN1 | up-regulates activity
cleavage
|
CDK5/CDK5R1 |
0.559 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251581 |
|
|
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 25969760 |
Calpains also modulate the activity of CDK5. Physiologically, CDK 5 is activated by p35 and its cleaved product p25. The latter has a longer half life than p35 and therefore it is a more potent activator of CDK5. The cleavage of p35 to p25 is mediated by calpain |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Alzheimer |
| + |
CAPN2 | up-regulates activity
cleavage
|
CDK5/CDK5R1 |
0.551 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251608 |
|
|
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 25969760 |
Calpains also modulate the activity of CDK5. Physiologically, CDK 5 is activated by p35 and its cleaved product p25. The latter has a longer half life than p35 and therefore it is a more potent activator of CDK5. The cleavage of p35 to p25 is mediated by calpain |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK5 | form complex
binding
|
CDK5/CDK5R1 |
0.942 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250683 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11331872 |
Induced p35 forms a complex with Cdk5 and activates its kinase activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAPN3 | up-regulates activity
cleavage
|
CDK5/CDK5R1 |
0.33 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251602 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25969760 |
Calpains also modulate the activity of CDK5. Physiologically, CDK 5 is activated by p35 and its cleaved product p25. The latter has a longer half life than p35 and therefore it is a more potent activator of CDK5. The cleavage of p35 to p25 is mediated by calpain |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CDK5/CDK5R1
CPX-2201