+ |
CDK5 | up-regulates activity
phosphorylation
|
VRK3 |
0.365 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275544 |
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 | up-regulates activity
phosphorylation
|
ERBB3 |
0.346 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250663 |
Ser1123 |
RSRSRSRsPRPRGDS |
Rattus norvegicus |
Cerebral Cortical Neuron |
pmid |
sentence |
12824184 |
We demonstrated that Cdk5 phosphorylated Ser-1176 in the neuregulin receptor ErbB2 and phosphorylated Thr-871 and Ser-1120 in the ErbB3 receptor. We identified the Ser-1120 sequence RSRSPR in ErbB3 as a novel phosphorylation consensus sequence of Cdk5. Finally, we found that Cdk5 activity is involved in neuregulin-induced Akt activity and neuregulin-mediated neuronal survival. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250664 |
Thr873 |
LLYSEAKtPIKWMAL |
Rattus norvegicus |
Cerebral Cortical Neuron |
pmid |
sentence |
12824184 |
We demonstrated that Cdk5 phosphorylated Ser-1176 in the neuregulin receptor ErbB2 and phosphorylated Thr-871 and Ser-1120 in the ErbB3 receptor. We identified the Ser-1120 sequence RSRSPR in ErbB3 as a novel phosphorylation consensus sequence of Cdk5. Finally, we found that Cdk5 activity is involved in neuregulin-induced Akt activity and neuregulin-mediated neuronal survival. |
|
Publications: |
2 |
Organism: |
Rattus Norvegicus |
+ |
CDK5 | down-regulates
phosphorylation
|
NOS3 |
0.38 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-164080 |
Ser114 |
RKLQGRPsPGPPAPE |
Homo sapiens |
Neuron |
pmid |
sentence |
20213743 |
Together, our data suggest that cdk5 can phosphorylate enos at the ser-113 site and down-regulate enos-derived no levels. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 | up-regulates
phosphorylation
|
HTT |
0.46 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-156836 |
Ser1179 |
LTNPPSLsPIRRKGK |
Homo sapiens |
Neuron |
pmid |
sentence |
17611284 |
Huntingtin is an antiapoptotic proteinwe show here that huntingtin is phosphorylated by the cyclin-dependent kinase 5 (cdk5) at serines 1181 and 1201. Phosphorylation can be induced by dna damage in vitro and in vivo. The state of huntingtin phosphorylation is a crucial regulator of neuronal cell death. Absence of phosphorylation of huntingtin at serines 1181 and 1201 confers toxic properties to wild-type huntingtin in a p53-dependent manner in striatal neurons and accelerates neuronal death induced by dna damage. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-156840 |
Ser1199 |
EQASVPLsPKKGSEA |
Homo sapiens |
Neuron |
pmid |
sentence |
17611284 |
Huntingtin is an antiapoptotic proteinwe show here that huntingtin is phosphorylated by the cyclin-dependent kinase 5 (cdk5) at serines 1181 and 1201. Phosphorylation can be induced by dna damage in vitro and in vivo. The state of huntingtin phosphorylation is a crucial regulator of neuronal cell death. Absence of phosphorylation of huntingtin at serines 1181 and 1201 confers toxic properties to wild-type huntingtin in a p53-dependent manner in striatal neurons and accelerates neuronal death induced by dna damage. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CDK5 | up-regulates activity
phosphorylation
|
GRIN2A |
0.541 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250666 |
Ser1232 |
SGHFTMRsPFKCDAC |
Rattus norvegicus |
Neuron |
pmid |
sentence |
11675505 |
Here, we demonstrate that cyclin dependent kinase-5 (Cdk5) associates with and phosphorylates NR2A subunits at Ser-1232 in vitro and in intact cells. Moreover, we show that roscovitine, a selective Cdk5 inhibitor, blocks both long-term potentiation induction and NMDA-evoked currents in rat CA1 hippocampal neurons. These results suggest that Cdk5 plays a key role in synaptic transmission and plasticity through its up-regulation of NMDARs. |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |
+ |
CDK5 | down-regulates
phosphorylation
|
CAMKK2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-198111 |
Ser129 |
ICPSLPYsPVSSPQS |
Homo sapiens |
|
pmid |
sentence |
22778263 |
Cdk5 and gsk3 phosphorylate ser-129, ser-133, and ser-137. Mutation of ser-129, ser-133, and ser-137 increases autonomous activity with little change in ca2 /cam-dependent activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-198115 |
Ser133 |
LPYSPVSsPQSSPRL |
Homo sapiens |
|
pmid |
sentence |
22778263 |
Cdk5 and gsk3 phosphorylate ser-129, ser-133, and ser-137. Mutation of ser-129, ser-133, and ser-137 increases autonomous activity with little change in ca2 /cam-dependent activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-197945 |
Ser137 |
PVSSPQSsPRLPRRP |
Homo sapiens |
|
pmid |
sentence |
22778263 |
Cdk5 and gsk3 phosphorylate ser-129, ser-133, and ser-137. Mutation of ser-129, ser-133, and ser-137 increases autonomous activity with little change in ca2 /cam-dependent activity. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
CDK5 | down-regulates
phosphorylation
|
PMAIP1 |
0.365 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-170357 |
Ser13 |
ARKNAQPsPARAPAE |
Homo sapiens |
Leukemia Cell |
pmid |
sentence |
21145489 |
We show that noxa is phosphorylated on a serine residue (s(13)) in the presence of glucose. Phosphorylation promotes its cytosolic sequestration and suppresses its apoptotic function. We identify cdk5 as the noxa kinase |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 | down-regulates
phosphorylation
|
PRKN |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-153445 |
Ser131 |
HTDSRKDsPPAGSPA |
Homo sapiens |
|
pmid |
sentence |
17327227 |
Phosphorylation by cdk5 decreased the auto-ubiquitylation of parkin both in vitro and in vivo. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Brain |
+ |
CDK5 | down-regulates activity
phosphorylation
|
PLD2 |
0.377 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276168 |
Ser134 |
ARFAVAYsPARDAGN |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
18625302 |
In this study, we suggest that the phosphorylation and activation of PLD2 by cyclin-dependent kinase 5 (Cdk5) is critical for EGF-dependent insulin secretion. We determined that the phosphorylation site of PLD2 was located at Ser(134). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 | up-regulates
phosphorylation
|
LMTK2 |
0.512 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-195329 |
Ser1450 |
LQTSKYFsPPPPARS |
Homo sapiens |
Neuron |
pmid |
sentence |
22220831 |
Here, we demonstrate that lmtk2 is phosphorylated on serine-1418 (lmtk2ser ) by cdk5/p35 and present evidence that this regulates its ability to phosphorylate pp1cthr __ |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Brain |
+ |
CDK5 | up-regulates
phosphorylation
|
TP53 |
0.722 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-156414 |
Ser15 |
PSVEPPLsQETFSDL |
Homo sapiens |
Neuron |
pmid |
sentence |
17591690 |
Here, we demonstrate for the first time that cdk5 interacts with p53 and increases its stability through posttranslational regulation, leading to accumulation of p53, particularly in the nucleus. We show that cdk5 phosphorylates p53 on ser15, ser33 and ser46 in vitro, |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-156418 |
Ser20 |
PLSQETFsDLWKLLP |
Homo sapiens |
Neuron |
pmid |
sentence |
17591690 |
Here, we demonstrate for the first time that cdk5 interacts with p53 and increases its stability through posttranslational regulation, leading to accumulation of p53, particularly in the nucleus. We show that cdk5 phosphorylates p53 on ser15, ser33 and ser46 in vitro, |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-156422 |
Ser33 |
LPENNVLsPLPSQAM |
Homo sapiens |
|
pmid |
sentence |
17591690 |
We show that cdk5 phosphorylates p53 on ser15, ser33 and ser46 cdk5-stabilized p53 protein is transcriptionally active |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-156426 |
Ser46 |
AMDDLMLsPDDIEQW |
Homo sapiens |
Neuron |
pmid |
sentence |
17591690 |
We show that cdk5 phosphorylates p53 on ser15, ser33 and ser46 cdk5-stabilized p53 protein is transcriptionally active |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
+ |
CDK5 | up-regulates
phosphorylation
|
DNMT1 |
0.367 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-173685 |
Ser154 |
AKPEPSPsPRITRKS |
Homo sapiens |
|
pmid |
sentence |
21565170 |
We report that cyclin-dependent kinases (cdks) 1, 2 and 5 can phosphorylate ser154 of human dnmt1 in vitro. Further evidence of phosphorylation of endogenous dnmt1 at position 154 by cdks is also found in 293 cells treated with roscovitine, a specific inhibitor of cdk1, 2 and 5 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | up-regulates activity
phosphorylation
|
CDK5 |
0.303 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275966 |
Ser159 |
GIPVRCYsAEVVTLW |
in vitro |
|
pmid |
sentence |
10500146 |
We also show that casein kinase I, but not casein kinase II, can phosphorylate and activate cdk5 in vitro. Ser(159) in cdk5 is homologous to the regulatory Thr(160) in cdk2. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
CSNK1D | up-regulates activity
phosphorylation
|
CDK5 |
0.535 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250798 |
Ser159 |
GIPVRCYsAEVVTLW |
in vitro |
|
pmid |
sentence |
10500146 |
We also show that casein kinase I, but not casein kinase II, can phosphorylate and activate cdk5 in vitro. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
CDK5 | down-regulates activity
phosphorylation
|
TPPP |
0.414 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262931 |
Ser160 |
GVTKAISsPTVSRLT |
in vitro |
|
pmid |
sentence |
17693641 |
Here we show that TPPP induces tubulin self-assembly into intact frequently bundled microtubules, and that the phosphorylation of specific sites distinctly affects the function of TPPP. The phosphorylation sites Thr(14), Ser(18), Ser(160) for Cdk5; Ser(18), Ser(160) for ERK2, and Ser(32) for PKA were identified by mass spectrometry. The phosphorylation by ERK2 or Cdk5 resulted in the loss of microtubule-assembling activity of TPPP. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262932 |
Ser18 |
ANRTPPKsPGDPSKD |
in vitro |
|
pmid |
sentence |
17693641 |
Here we show that TPPP induces tubulin self-assembly into intact frequently bundled microtubules, and that the phosphorylation of specific sites distinctly affects the function of TPPP. The phosphorylation sites Thr(14), Ser(18), Ser(160) for Cdk5; Ser(18), Ser(160) for ERK2, and Ser(32) for PKA were identified by mass spectrometry. The phosphorylation by ERK2 or Cdk5 resulted in the loss of microtubule-assembling activity of TPPP. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262933 |
Thr14 |
PAKAANRtPPKSPGD |
in vitro |
|
pmid |
sentence |
17693641 |
Here we show that TPPP induces tubulin self-assembly into intact frequently bundled microtubules, and that the phosphorylation of specific sites distinctly affects the function of TPPP. The phosphorylation sites Thr(14), Ser(18), Ser(160) for Cdk5; Ser(18), Ser(160) for ERK2, and Ser(32) for PKA were identified by mass spectrometry. The phosphorylation by ERK2 or Cdk5 resulted in the loss of microtubule-assembling activity of TPPP. |
|
Publications: |
3 |
Organism: |
In Vitro |
+ |
CDK5 | up-regulates activity
phosphorylation
|
NDEL1 |
0.764 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250675 |
Ser198 |
TRKSAPSsPTLDCEK |
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. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250676 |
Ser231 |
GTENTFPsPKAIPNG |
Mus musculus |
|
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. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250677 |
Ser242 |
IPNGFGTsPLTPSAR |
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: |
3 |
Organism: |
Mus Musculus |
+ |
CDK5 | down-regulates activity
phosphorylation
|
NR3C1 |
0.459 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-154401 |
Ser203 |
DLEFSSGsPGKETNE |
Homo sapiens |
|
pmid |
sentence |
17440046 |
Cdk5 phosphorylated gr at multiple serines, including ser203 and ser211 of its n-terminal domain, and suppressed the transcriptional activity of this receptor on glucocorticoid-responsive promoters by attenuating attraction of transcriptional cofactors to dna.| the effect of CDK5 on GR-induced transcriptional activity is specific to gene promoter, and possibly, to tissue |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-154405 |
Ser211 |
PGKETNEsPWRSDLL |
Homo sapiens |
|
pmid |
sentence |
17440046 |
Cdk5 phosphorylated gr at multiple serines, including ser203 and ser211 of its n-terminal domain, and suppressed the transcriptional activity of this receptor on glucocorticoid-responsive promoters by attenuating attraction of transcriptional cofactors to dna.| the effect of CDK5 on GR-induced transcriptional activity is specific to gene promoter, and possibly, to tissue |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CDK5 | down-regulates
phosphorylation
|
MAPT |
0.754 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-171018 |
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-92603 |
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-92607 |
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-171022 |
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 |
+ |
CDK5 |
phosphorylation
|
AMPH |
0.537 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250648 |
Ser272 |
EEPSPLPsPTASPNH |
in vitro |
|
pmid |
sentence |
11113134 |
Amphiphysin is phosphorylated by cdk5 in a region including serines 272, 276, and 285. Amphiphysin 1 is also phosphorylated by the cdc2/cyclin B kinase complex in the same region and undergoes mitotic phosphorylation in dividing cells. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250649 |
Ser276 |
PLPSPTAsPNHTLAP |
in vitro |
|
pmid |
sentence |
11113134 |
Amphiphysin is phosphorylated by cdk5 in a region including serines 272, 276, and 285. Amphiphysin 1 is also phosphorylated by the cdc2/cyclin B kinase complex in the same region and undergoes mitotic phosphorylation in dividing cells. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250650 |
Ser285 |
NHTLAPAsPAPARPR |
in vitro |
|
pmid |
sentence |
11113134 |
Amphiphysin is phosphorylated by cdk5 in a region including serines 272, 276, and 285. Amphiphysin 1 is also phosphorylated by the cdc2/cyclin B kinase complex in the same region and undergoes mitotic phosphorylation in dividing cells. |
|
Publications: |
3 |
Organism: |
In Vitro |
+ |
CDK5 | up-regulates
phosphorylation
|
AGAP2 |
0.265 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-178660 |
Ser279 |
KSKTLDNsDLHPGPP |
Homo sapiens |
Neuron, Glioblastoma Cell |
pmid |
sentence |
18487454 |
Here, we demonstrate that cyclin dependent kinase 5 (cdk5), a protein known to function mainly in postmitotic neurons, directly phosphorylates pike-a at ser-279 in its gtpase domain in glioblastoma cells. This phosphorylation event stimulates pike-a gtpase activity and the activity of its downstream effector akt. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 | down-regulates quantity by destabilization
phosphorylation
|
BAG3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277502 |
Ser291 |
STPLHSPsPIRVHTV |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
31955914 |
CDK5-mediated phosphorylation on S297 promotes BAG3 degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 | up-regulates activity
phosphorylation
|
TRIM59 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272929 |
Ser308 |
LIPKMKIsPKRMSCS |
|
|
pmid |
sentence |
31488827 |
Here, we identify TRIM59 as a substrate of CDK5. EGFR-activated CDK5 directly binds to and phosphorylates TRIM59, a ubiquitin ligase at serine 308, which recruits PIN1 for cis-trans isomerization of TRIM59, leading to TRIM59 binding to importin α5 and nuclear translocation. |
|
Publications: |
1 |
+ |
CDK5 |
phosphorylation
|
CABLES1 |
0.73 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-112418 |
Ser313 |
RCRTLSGsPRPKNFK |
Chlorocebus aethiops |
|
pmid |
sentence |
11733001 |
P70ik3-1 is phosphorylated by either cyclin A/cdk3 or cyclin E/cdk3 reconstituted in COS7 cells. Accordingly, we can conclude that in COS7 cells, Ser274 in p70ik3-1 is phosphorylated by endogenous kinases other than cdk5 (Fig. 4), at least one of which is cdk3 as shown in this work. Currently, however, the question of how ik3-1 function is modified by its cdk3-mediated phosphorylation of Ser274 remains to be adressed. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
CDK5 | down-regulates quantity
phosphorylation
|
PHACTR3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273607 |
Ser318 |
QGRESKGsPKKRLDV |
Rattus norvegicus |
Neuron |
pmid |
sentence |
21487013 |
We show that scapinin is phosphorylated at a highly conserved site in the central region of the protein (Ser-277) by Cdk5 in vitro. Expression of a scapinin phospho-mimetic mutant (S277D) restored normal axon elongation without affecting actin binding. Instead, phosphorylated scapinin was sequestered in the cytoplasm of neurons and away from the axon. |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |
+ |
CDK5 | down-regulates activity
phosphorylation
|
DRD2 |
0.393 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-259401 |
Ser321 |
GLHSTPDsPAKPEKN |
Homo sapiens |
|
pmid |
sentence |
24391960 |
These results indicate that Cdk5-mediated phosphorylation of S321 inhibits DRD2 function, providing a novel regulatory mechanism for dopamine signaling. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Dopaminergic Synapse |
+ |
CDK5 | down-regulates activity
phosphorylation
|
HTR6 |
0.382 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264407 |
Ser350 |
ERQASLAsPSLRTSH |
Mus musculus |
NG-108-15 Cell |
pmid |
sentence |
32047117 |
Cdk5 phosphorylates the 5-HT6R on serine 350 (Ser350)|This suggests that the 5-HT6R is unable to interact with GPRIN1 when it is phosphorylated by Cdk5. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
CDK5 | down-regulates
phosphorylation
|
STMN1 |
0.386 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-166682 |
Ser38 |
SVPEFPLsPPKKKDL |
Homo sapiens |
|
pmid |
sentence |
20630875 |
Involved in the regulation of the microtubule (mt) filament system by destabilizing microtubules. Prevents assembly and promotes disassembly of microtubules. The kinases involved in phosphorylating stmn ser-16 and ser-63 include camp-dependent protein kinase (pka) and pak1, whereas stmn ser-25 and ser-38 have been shown to be targets for proline-directed serine/threonine kinases such as cyclin-dependent kinases, erk1/2, and members of the p38 mapk subfamily. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 | up-regulates
phosphorylation
|
HTRA2 |
0.468 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-174598 |
Ser400 |
IHKVILGsPAHRAGL |
Homo sapiens |
|
pmid |
sentence |
21701498 |
Here we report that cyclin-dependent kinase-5 (cdk5), a kinase implicated in the pathogenesis of several neurodegenerative diseases, is responsible for phosphorylating htra2 at s400.We have shown previously that phosphomimetic mutants of htra2 at s400 result in increased proteolytic activity and contribute to enhanced resistance to mitochondrial stress |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 | down-regulates activity
phosphorylation
|
MEF2A |
0.521 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-100574 |
Ser408 |
SIKSEPIsPPRDRMT |
Homo sapiens |
Cerebral Cortical Neuron |
pmid |
sentence |
12691662 |
Cdk5-mediated inhibition of the protective effects of transcription factor mef2 in neurotoxicity-induced apoptosis.We have identified the prosurvival transcription factor mef2 as a direct nuclear target of cdk5. Cdk5 phosphorylates mef2 at a distinct serine in its transactivation domain to inhibit mef2 activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 | up-regulates
phosphorylation
|
TLN1 |
0.471 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-185210 |
Ser425 |
TMLEDSVsPKKSTVL |
Homo sapiens |
|
pmid |
sentence |
19363486 |
Cdk5 phosphorylated talin head at ser 425, inhibiting its binding to smurf1, thus preventing talin head ubiquitylation and degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 | up-regulates quantity by stabilization
phosphorylation
|
TPX2 |
0.277 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265100 |
Ser486 |
LPITVPKsPAFALKN |
Homo sapiens |
|
pmid |
sentence |
31272499 |
CDK5-mediated phosphorylation and stabilization of TPX2 promotes hepatocellular tumorigenesis |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Hepatobiliary Carcinoma Cell |
+ |
CDK5 | down-regulates quantity by destabilization
phosphorylation
|
AMFR |
0.25 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277356 |
Ser516 |
SIRPALNsPVERPSS |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
28528366 |
We found that GP78 expression is decreased in MPTP-based cellular and animal PD models, and CDK5 directly phosphorylated GP78 at Ser516, which promoted the ubiquitination and degradation of GP78. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 | down-regulates activity
phosphorylation
|
MAPT |
0.754 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249327 |
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-249317 |
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-249318 |
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-249319 |
Ser552 |
VVRTPPKsPSSAKSR |
Homo sapiens |
|
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-249320 |
Ser713 |
GAEIVYKsPVVSGDT |
Homo sapiens |
|
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-249321 |
Ser721 |
PVVSGDTsPRHLSNV |
Homo sapiens |
|
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-249326 |
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-249322 |
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-249323 |
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-249324 |
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-249325 |
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 |
+ |
CDK5 | up-regulates activity
phosphorylation
|
DPYSL3 |
0.588 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-145963 |
Ser518 |
KGGTPAGsARGSPTR |
Homo sapiens |
|
pmid |
sentence |
16611631 |
Together, these results suggest that crmp4 is able to increase neurite formation and elongation in neurons, although not as potently as crmp2, and that this process is regulated by ser522/ser518/thr514/thr509 phosphorylation in both cases. We demonstrate that cdk5 primes crmp2 and crmp4 for subsequent phosphorylation by gsk3, whereas dyrk2, phosphorylates and primes only crmp4 in vitro |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-145967 |
Thr509 |
PVFDLTTtPKGGTPA |
Homo sapiens |
|
pmid |
sentence |
16611631 |
Together, these results suggest that crmp4 is able to increase neurite formation and elongation in neurons, although not as potently as crmp2, and that this process is regulated by ser522/ser518/thr514/thr509 phosphorylation in both cases. We demonstrate that cdk5 primes crmp2 and crmp4 for subsequent phosphorylation by gsk3, whereas dyrk2, phosphorylates and primes only crmp4 in vitro |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-145971 |
Thr514 |
TTTPKGGtPAGSARG |
Homo sapiens |
|
pmid |
sentence |
16611631 |
Together, these results suggest that crmp4 is able to increase neurite formation and elongation in neurons, although not as potently as crmp2, and that this process is regulated by ser522/ser518/thr514/thr509 phosphorylation in both cases. We demonstrate that cdk5 primes crmp2 and crmp4 for subsequent phosphorylation by gsk3, whereas dyrk2, phosphorylates and primes only crmp4 in vitro |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
CDK5 | down-regulates activity
phosphorylation
|
DPYSL2 |
0.642 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264838 |
Ser522 |
PASSAKTsPAKQQAP |
Homo sapiens |
Neuron |
pmid |
sentence |
25040932 |
Cdk5 and DYRK2 phosphorylate CRMP2 and CRMP4, respectively, priming these proteins at S522 before their subsequent phosphorylation by GSK-3b at T509, T516 and S518|e CRMP2 phosphorylation by GSK-3b disrupts its interaction with tubulin (Yamashita & Goshima, 2012), leading to growth inhibition |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 | up-regulates
phosphorylation
|
CRMP1 |
0.608 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-159314 |
Ser522 |
PAPSAKSsPSKHQPP |
Homo sapiens |
Neuron |
pmid |
sentence |
18003833 |
These findings suggest that sema3a-induced spine development is regulated by phosphorylation of crmp1 by cdk5. Introduction of crmp1-wt, but not crmp1-t509a/s522a, a crmp1 mutant that cannot be phosphorylated by cdk5, rescued the defect in sema3a responsiveness. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-145912 |
Thr509 |
PVYEVPAtPKYATPA |
Homo sapiens |
Neuron |
pmid |
sentence |
16611631 |
In summary, phosphorylation of thr509 of human crmp1 appears to be regulated by two mechanisms; direct phosphorylation by cdk5, or by priming of ser522 by cdk5 followed by sequential phosphorylation of ser518, thr514, and thr509 by gsk3. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-159318 |
Thr509 |
PVYEVPAtPKYATPA |
Homo sapiens |
Neuron |
pmid |
sentence |
18003833 |
These findings suggest that sema3a-induced spine development is regulated by phosphorylation of crmp1 by cdk5. Introduction of crmp1-wt, but not crmp1-t509a/s522a, a crmp1 mutant that cannot be phosphorylated by cdk5, rescued the defect in sema3a responsiveness. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
CDK5 | up-regulates
phosphorylation
|
SYN1 |
0.581 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-78883 |
Ser551 |
PAARPPAsPSPQRQA |
Homo sapiens |
|
pmid |
sentence |
10880969 |
Synapsin i (syni), a major sv phosphoprotein involved in the regulation of sv trafficking and neurotransmitter release, is one of the presynaptic substrates of cdk5, which phosphorylates it in its c-terminal region at ser(549) (site 6) and ser(551) (site 7). Phosphorylation of syni by cdk5 is physiologically regulated and enhances its binding to f-actin. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-78887 |
Ser553 |
ARPPASPsPQRQAGP |
Homo sapiens |
|
pmid |
sentence |
10880969 |
Synapsin i (syni), a major sv phosphoprotein involved in the regulation of sv trafficking and neurotransmitter release, is one of the presynaptic substrates of cdk5, which phosphorylates it in its c-terminal region at ser(549) (site 6) and ser(551) (site 7). Phosphorylation of syni by cdk5 is physiologically regulated and enhances its binding to f-actin. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CDK5 | up-regulates activity
phosphorylation
|
DLC1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276443 |
Ser557 |
LEEFDVFsPKQDLVP |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
25452387 |
The CDK5 kinase phosphorylates four serines in DLC1 located N-terminal to the Rho-GAP domain. When not phosphorylated, this N-terminal region functions as an autoinhibitory domain that places DLC1 in a closed, inactive conformation by efficiently binding to the Rho-GAP domain. CDK5 phosphorylation reduces this binding and orchestrates the coordinate activation DLC1, including its localization to focal adhesions, its Rho-GAP activity, and its ability to bind tensin and talin. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276444 |
Ser642 |
DSFGSLPsPKELSSF |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
25452387 |
The CDK5 kinase phosphorylates four serines in DLC1 located N-terminal to the Rho-GAP domain. When not phosphorylated, this N-terminal region functions as an autoinhibitory domain that places DLC1 in a closed, inactive conformation by efficiently binding to the Rho-GAP domain. CDK5 phosphorylation reduces this binding and orchestrates the coordinate activation DLC1, including its localization to focal adhesions, its Rho-GAP activity, and its ability to bind tensin and talin. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276445 |
Ser859 |
RRENSSDsPKELKRR |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
25452387 |
The CDK5 kinase phosphorylates four serines in DLC1 located N-terminal to the Rho-GAP domain. When not phosphorylated, this N-terminal region functions as an autoinhibitory domain that places DLC1 in a closed, inactive conformation by efficiently binding to the Rho-GAP domain. CDK5 phosphorylation reduces this binding and orchestrates the coordinate activation DLC1, including its localization to focal adhesions, its Rho-GAP activity, and its ability to bind tensin and talin. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276446 |
Ser946 |
SVSPCPSsPKQIHLD |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
25452387 |
The CDK5 kinase phosphorylates four serines in DLC1 located N-terminal to the Rho-GAP domain. When not phosphorylated, this N-terminal region functions as an autoinhibitory domain that places DLC1 in a closed, inactive conformation by efficiently binding to the Rho-GAP domain. CDK5 phosphorylation reduces this binding and orchestrates the coordinate activation DLC1, including its localization to focal adhesions, its Rho-GAP activity, and its ability to bind tensin and talin. |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
+ |
CDK5 | down-regulates
phosphorylation
|
PIP5K1C |
0.371 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-134455 |
Ser650 |
DERSWVYsPLHYSAQ |
Homo sapiens |
|
pmid |
sentence |
15738269 |
The interaction of talin with phosphatidylinositol(4) phosphate 5 kinase type i gamma (pipki gamma) regulates pi(4,5)p2 synthesis at synapses and at focal adhesions. Here, we show that phosphorylation of serine 650 (s650) within the talin-binding sequence of human pipki gamma blocks this interaction. At synapses, s650 is phosphorylated by p35/cdk5 and mitogen-activated protein kinase at rest, and dephosphorylated by calcineurin upon stimulation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 |
phosphorylation
|
PPP1R1A |
0.381 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249194 |
Ser67 |
LKSTLAMsPRQRKKM |
Rattus norvegicus |
|
pmid |
sentence |
11278334 |
In vitro and in vivo studies indicated that phospho-Ser-67 inhibitor-1 was dephosphorylated by protein phosphatases-2A and -2B. | However, inhibitor-1 phosphorylated at Ser-67 was a less efficient substrate for cAMP-dependent protein kinase. These results demonstrate regulation of a Cdk5-dependent phosphorylation site in inhibitor-1 and suggest a role for this site in modulating the amplitude of signal transduction events that involve cAMP-dependent protein kinase activation. |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |
+ |
CDK5 |
phosphorylation
|
STMN3 |
0.329 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264893 |
Ser68 |
PSDLSPEsPMLSSPP |
in vitro |
|
pmid |
sentence |
22577147 |
Altogether, these results indicate that CDK5 phosphorylates similarly serines 68 and 73, whereas ERK2 targets mostly serine 68 and GSK-3beta mostly serine 60.|This observation may support the hypothesis of a specific localization of stathmin 3 depending on its phosphorylation by GSK-3beta |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264894 |
Ser73 |
PESPMLSsPPKKKDT |
in vitro |
|
pmid |
sentence |
22577147 |
Altogether, these results indicate that CDK5 phosphorylates similarly serines 68 and 73, whereas ERK2 targets mostly serine 68 and GSK-3beta mostly serine 60.|This observation may support the hypothesis of a specific localization of stathmin 3 depending on its phosphorylation by GSK-3beta |
|
Publications: |
2 |
Organism: |
In Vitro |
+ |
CDK5 | up-regulates
phosphorylation
|
STAT3 |
0.413 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-124325 |
Ser727 |
NTIDLPMsPRTLDSL |
Homo sapiens |
Neuron |
pmid |
sentence |
15096606 |
We report here that the cdk5/p35 complex associates with stat3 and phosphorylates stat3 on the ser-727 residue in vitro and in vivo. Ser phosphorylation of stat3 and transcription of stat3 target genes, such as c-fos and junb, in a cdk5-dependent manner. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Muscle, Myotube, Brain |
+ |
CDK5 | up-regulates
phosphorylation
|
PTK2 |
0.311 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-86223 |
Ser732 |
SSEGFYPsPQHMVQT |
Homo sapiens |
Neuron |
pmid |
sentence |
12941275 |
Here, we show that fak phosphorylation by cdk5 at s732 is important for microtubule organization, nuclear movement, and neuronal migration. In cultured neurons, s732-phosphorylated fak is enriched along a centrosome-associated microtubule fork that abuts the nucleus. Overexpression of the nonphosphorylatable mutant fak s732a results in disorganization of the microtubule fork and impairment of nuclear movement in vitro, and neuronal positioning defects in vivo. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 | up-regulates
phosphorylation
|
SRC |
0.398 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-71950 |
Ser75 |
NSSDTVTsPQRAGPL |
Homo sapiens |
Neuron |
pmid |
sentence |
10544291 |
These results present compelling evidence that cdk5/p35 kinase is responsible for the novel phosphorylation of c-src at ser75 in neuronal cells, raising the intriguing possibility that c-src acts as an effector of cdk5/p35 kinase during neuronal development. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 | up-regulates activity
phosphorylation
|
DNM1 |
0.531 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250661 |
Ser774 |
SVPAGRRsPTSSPTP |
in vitro |
|
pmid |
sentence |
12855954 |
Here, we show that cyclin-dependent kinase 5 (Cdk5) phosphorylates dynamin I on Ser 774 and Ser 778 in vitro, which are identical to its endogenous phosphorylation sites in vivo. Cdk5 antagonists and expression of dominant-negative Cdk5 block phosphorylation of dynamin I, but not of amphiphysin or AP180, in nerve terminals and inhibit SVE. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250662 |
Ser778 |
GRRSPTSsPTPQRRA |
in vitro |
|
pmid |
sentence |
12855954 |
Here, we show that cyclin-dependent kinase 5 (Cdk5) phosphorylates dynamin I on Ser 774 and Ser 778 in vitro, which are identical to its endogenous phosphorylation sites in vivo. Cdk5 antagonists and expression of dominant-negative Cdk5 block phosphorylation of dynamin I, but not of amphiphysin or AP180, in nerve terminals and inhibit SVE. |
|
Publications: |
2 |
Organism: |
In Vitro |
+ |
CDK5 | down-regulates activity
phosphorylation
|
PARP1 |
0.261 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276357 |
Ser782 |
YSLLRGGsDDSSKDP |
in vitro |
|
pmid |
sentence |
21922195 |
These results would suggest that the phosphorylation of PARP-1 via Cdk5's kinase activity is necessary for its persistence at damage sites.Based on these results and the recruitment data, we hypothesize that the phosphorylation of the PARP-1 protein by Cdk5 on one or more of the serines 782, 785, and 786 results in an attenuation of its ribosylating activity facilitating its persistence at the sites of DNA damage. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276358 |
Ser785 |
LRGGSDDsSKDPIDV |
in vitro |
|
pmid |
sentence |
21922195 |
These results would suggest that the phosphorylation of PARP-1 via Cdk5's kinase activity is necessary for its persistence at damage sites.Based on these results and the recruitment data, we hypothesize that the phosphorylation of the PARP-1 protein by Cdk5 on one or more of the serines 782, 785, and 786 results in an attenuation of its ribosylating activity facilitating its persistence at the sites of DNA damage. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276359 |
Ser786 |
RGGSDDSsKDPIDVN |
in vitro |
|
pmid |
sentence |
21922195 |
These results would suggest that the phosphorylation of PARP-1 via Cdk5's kinase activity is necessary for its persistence at damage sites.Based on these results and the recruitment data, we hypothesize that the phosphorylation of the PARP-1 protein by Cdk5 on one or more of the serines 782, 785, and 786 results in an attenuation of its ribosylating activity facilitating its persistence at the sites of DNA damage. |
|
Publications: |
3 |
Organism: |
In Vitro |
+ |
CDK5 | up-regulates
phosphorylation
|
ATM |
0.427 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-183454 |
Ser794 |
LSNCTKKsPNKIASG |
Homo sapiens |
Neuron |
pmid |
sentence |
19151707 |
Here we show that cdk5 (cyclin-dependent kinase 5), activated by dna damage, directly phosphorylates atm at ser 794 in post-mitotic neurons. Phosphorylation at ser 794 precedes, and is required for, atm autophosphorylation at ser 1981, and activates atm kinase activity |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 | down-regulates
phosphorylation
|
CDK5R1 |
0.942 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-177963 |
Ser8 |
MGTVLSLsPSYRKAT |
Homo sapiens |
|
pmid |
sentence |
18326489 |
When overexpressed with cdk5, a large fraction of the double mutant p35(s8a/t138a) co-sedimented with microtubules (fig. 5b), further supporting the idea that the phosphorylation at these two residues by cdk5 is inhibitory to the microtubule association. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-177967 |
Thr138 |
PAVTSAGtPKRVIVQ |
Homo sapiens |
|
pmid |
sentence |
18326489 |
P35 phosphorylation by cdk5 interferes with the microtubule-binding and polymerizing activities of p35. Using a mutational approach, we found that only phosphorylation at thr-138, one of the two residues primarily phosphorylated in vivo, inhibits the polymerizing activity |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CDK5 | down-regulates
phosphorylation
|
RB1 |
0.342 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-134468 |
Ser811 |
IYISPLKsPYKISEG |
Homo sapiens |
|
pmid |
sentence |
15741232 |
Phosphorylation was observed 6 hours after p25 induction and was abolished in the presence of a cdk5 inhibitor, roscovitine, which does not inhibit the usual rb cyclin-d kinases cdk4 and cdk6. Furthermore, analyses of levels and subcellular localization of cdk-related cyclins did not reveal any change following cdk5 activation, arguing for a direct effect of cdk5 activity on rb protein. Rb phosphorylation was visualized using phosphorylation-dependent antibodies (p-rbser795 and p-rbser807/811). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 | up-regulates
phosphorylation
|
AR |
0.381 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-175696 |
Ser83 |
QQQQQETsPRQQQQQ |
Homo sapiens |
Prostate Gland Cancer Cell |
pmid |
sentence |
21799006 |
Cdk5 enables phosphorylation of ar at ser-81 site through direct biochemical interaction and, therefore, results in the stabilization of ar proteins |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 | down-regulates
phosphorylation
|
EPRS1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-187383 |
Ser886 |
LSQSSDSsPTRNSEP |
Homo sapiens |
|
pmid |
sentence |
19647514 |
Ser(886) phosphorylation is required for the interaction of nsap1, which blocks eprs binding to target mrnas. The same phosphorylation event induces subsequent binding of ribosomal protein l13a and gapdh and restores mrna binding. Ifn-_ activates cdk5 to phosphorylate ser(886) in the linker domain of glutamyl-prolyl trna synthetase (eprs), the initial event in assembly of the gait complex. Cdk5/p35 also induces, albeit indirectly via a distinct kinase, phosphorylation of ser(999), the second essential event in gait pathway activation |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-171138 |
Ser886 |
LSQSSDSsPTRNSEP |
Homo sapiens |
Macrophage |
pmid |
sentence |
21220307 |
Ser(886) phosphorylation is required for the interaction of nsap1, which blocks eprs binding to target mrnas. The same phosphorylation event induces subsequent binding of ribosomal protein l13a and gapdh and restores mrna binding. Ifn-_ activates cdk5 to phosphorylate ser(886) in the linker domain of glutamyl-prolyl trna synthetase (eprs), the initial event in assembly of the gait complex. Cdk5/p35 also induces, albeit indirectly via a distinct kinase, phosphorylation of ser(999), the second essential event in gait pathway activation |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CDK5 |
phosphorylation
|
NES |
0.564 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250669 |
Thr1299 |
GETLPDStPLGFYLR |
Mus musculus |
|
pmid |
sentence |
12832492 |
We identify nestin as a novel in vivo target for cdk5 and p35 kinase, a critical signaling determinant in development. Two cdk5-specific phosphorylation sites on nestin, Thr-1495 and Thr-316, were established, the latter of which was used as a marker for cdk5-specific phosphorylation in vivo. | Cdk5 activity is necessary for differentiation and the concomitant nestin reorganization in C2C12 myoblasts. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250670 |
Thr315 |
AENSRLQtPGGGSKT |
Mus musculus |
C2C12 Cell |
pmid |
sentence |
12832492 |
We identify nestin as a novel in vivo target for cdk5 and p35 kinase, a critical signaling determinant in development. Two cdk5-specific phosphorylation sites on nestin, Thr-1495 and Thr-316, were established, the latter of which was used as a marker for cdk5-specific phosphorylation in vivo. | Cdk5 activity is necessary for differentiation and the concomitant nestin reorganization in C2C12 myoblasts. |
|
Publications: |
2 |
Organism: |
Mus Musculus |
+ |
CDK5 | down-regulates activity
phosphorylation
|
MAPK10 |
0.351 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250668 |
Thr131 |
ISLLNVFtPQKTLEE |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
11823425 |
Here, we show that cdk5 directly phosphorylates c-Jun N-terminal kinase 3 (JNK3) on Thr131 and inhibits its kinase activity, leading to reduced c-Jun phosphorylation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 | up-regulates
phosphorylation
|
NFAT5 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-170886 |
Thr135 |
TVQQHPStPKRHTVL |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
21209322 |
High nacl-induced activation of cdk5 increases phosphorylation of the osmoprotective transcription factor tonebp/orebp at threonine 135, which contributes to its rapid nuclear localization. n hek293 cells, mass spectrometry shows phosphorylation of tonebp/orebp-s120, -s134, -t135, and -s155. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 | down-regulates
phosphorylation
|
PIK3C3 |
0.365 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-165772 |
Thr159 |
DGSEPTKtPGRTSST |
Homo sapiens |
Neuron |
pmid |
sentence |
20513426 |
Thr159 phosphorylation negatively regulates the ptdins3 kinase activity of vps34 and autophagy cdk5/p25, a neuronal cdk shown to play a role in alzheimer's disease, can also phosphorylate thr159 of vps34. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 | down-regulates activity
phosphorylation
|
PAK1 |
0.519 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249328 |
Thr212 |
VIEPLPVtPTRDVAT |
Chlorocebus aethiops |
COS Cell |
pmid |
sentence |
11604394 |
Our previous work revealed that the neuronal p35/Cdk5 kinase associates with Pak1 in a RacGTP-dependent manner, causing hyperphosphorylation and down-regulation of Pak1 kinase activity. We have now demonstrated direct phosphorylation of Pak1 on threonine 212 by the p35/Cdk5 kinase. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
CDK5 | up-regulates activity
phosphorylation
|
APEX1 |
0.387 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276337 |
Thr233 |
NKKNAGFtPQERQGF |
Homo sapiens |
|
pmid |
sentence |
21727086 |
Apurinic/apyrimidinic endonuclease-1 (APE1) is a multifunctional DNA repair/gene regulatory protein in mammalian cells, and was recently reported to be phosphorylated at Thr233 by CDK5. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 | up-regulates activity
phosphorylation
|
EZR |
0.477 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250665 |
Thr235 |
YEKDDKLtPKIGFPW |
Homo sapiens |
SAOS-2 Cell |
pmid |
sentence |
12769842 |
Increased ezrin expression and activation by CDK5 coincident with acquisition of the senescent phenotype. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 | down-regulates quantity by destabilization
phosphorylation
|
HTR1A |
0.274 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264406 |
Thr314 |
LPSEAGPtPCAPASF |
Chlorocebus aethiops |
COS Cell |
pmid |
sentence |
30712943 |
Cyclin-dependent kinase 5 promotes proteasomal degradation of the 5-HT 1A receptor via phosphorylation|5-HT1AR was phosphorylated by the Cdk5-p35 complex at Thr314 in the third cytoplasmic loop. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
CDK5 | down-regulates activity
phosphorylation
|
PPP1CA |
0.403 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-151803 |
Thr320 |
NPGGRPItPPRNSAK |
Homo sapiens |
|
pmid |
sentence |
17202132 |
We observed that phosphorylation of protein phosphatase 1 (PP1) on Thr320 is reduced in brain extracts from Egr-1-/- mice, indicating that a kinase downstream of Egr-1 phosphorylates PP1. In HEK 293 cells co-transfected with PP1 and Cdk5, Cdk5 phosphorylates PP1. In vitro, Cdk5 purified from bovine brain phosphorylates bacterially expressed recombinant PP1 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-92269 |
Thr320 |
NPGGRPItPPRNSAK |
Homo sapiens |
|
pmid |
sentence |
12202491 |
Pp1 isoforms contain an arg-pro-ile/val-thr-pro-pro-arg sequence near the c terminus, a known site of phosphorylation by cdc/cdk kinases, and phosphorylation attenuates phosphatase activity. Increasing doses of cdk2 resulted in increased phosphorylation of the thr-320 site. Phosphorylation of this site in pp1 corresponded to decreased pp1 activity. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Pathways: | Dopaminergic Synapse |
+ |
CDK5 | up-regulates
phosphorylation
|
PSEN1 |
0.526 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-89145 |
Thr354 |
HLGPHRStPESRAAV |
Homo sapiens |
|
pmid |
sentence |
12056836 |
Cyclin-dependent kinase-5/p35 phosphorylates presenilin 1 to regulate carboxy-terminal fragment stabilityhere we demonstrate that cyclin dependent kinase-5/p35 (cdk5/p35) phosphorylates ps1 on threonine(354) within c-ps1 both in vitro and in vivo. Threonine(354) phosphorylation functions to selectively stabilize c-ps1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 | down-regulates quantity by destabilization
phosphorylation
|
PEBP1 |
0.344 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276672 |
Thr42 |
DELGKVLtPTQVKNR |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
25104559 |
Here, we demonstrate that RKIP is a substrate of cyclin-dependent kinase 5 (CDK5) in neurons and that the phosphorylation of RKIP at T42 causes the release of Raf-1. Moreover, T42 phosphorylation promotes the exposure and recognition of the target motif "KLYEQ" in the C-terminus of RKIP by chaperone Hsc70 and the subsequent degradation of RKIP via chaperone-mediated autophagy (CMA). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 | up-regulates activity
phosphorylation
|
CORO1A |
0.293 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-245187 |
Thr424 |
AAPEASGtPSSDAVS |
Homo sapiens |
MEL-JUSO Cell |
pmid |
sentence |
26823173 |
We here show that phosphorylation of coronin 1 on Thr(418/424) by cyclin-dependent kinase (CDK) 5 activity was responsible for coronin 1-G_s association and the modulation of cAMP production. Together these results show an essential role for CDK5 activity in promoting the coronin 1-dependent cAMP/PKA pathway. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 | up-regulates
phosphorylation
|
CLOCK |
0.335 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-203227 |
Thr451 |
AVSDPSStPTKIPTD |
Homo sapiens |
|
pmid |
sentence |
24235147 |
Cdk5 phosphorylates clock at the thr-451 and thr-461 residues in association with transcriptional activation of clock. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-203231 |
Thr461 |
KIPTDTStPPRQHLP |
Homo sapiens |
|
pmid |
sentence |
24235147 |
Cdk5 phosphorylates clock at the thr-451 and thr-461 residues in association with transcriptional activation of clock. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CDK5 | down-regulates activity
phosphorylation
|
KIF13B |
0.374 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262737 |
Thr506 |
SEGQVMLtPQKNTRT |
Cricetulus griseus |
CHO Cell |
pmid |
sentence |
27512725 |
Overexpression of Cdk5 or its activator p35 promoted and inhibition of Cdk5 activity prevented the KIF13B-TRPV1 association, indicating that Cdk5 promotes TRPV1 anterograde transport by mediating the motor-cargo association. Cdk5 phosphorylates KIF13B at Thr-506, a residue located in the FHA domain. T506A mutation reduced the motor-cargo interaction and the cell-permeable TAT-T506 peptide, targeting to the Thr-506, decreased TRPV1 surface localization, demonstrating the essential role of Thr-506 phosphorylation in TRPV1 transport. |
|
Publications: |
1 |
Organism: |
Cricetulus Griseus |
+ |
CDK5 | down-regulates
phosphorylation
|
STXBP2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-157528 |
Thr572 |
IGSSHILtPTRFLDD |
Homo sapiens |
Neuron |
pmid |
sentence |
17716669 |
It was shown that munc18 inhibition of neuronal syntaxin 1 can be overcome by cdk5 phosphorylation, indicating that structural change disrupts the syntaxin-munc18 interaction. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 | down-regulates activity
phosphorylation
|
PIK3C3 |
0.365 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-259811 |
Thr668 |
ENLDLKLtPYKVLAT |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
20513426 |
Phosphorylation of Vps34 on Thr159 inhibits its interaction with Beclin 1. two additional amino acids in Vps34, Thr159 and Thr668, were found to be phosphorylated only after co-transfection with Cdk5/p25 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 | up-regulates activity
phosphorylation
|
ADD1 |
0.258 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277487 |
Thr724 |
KKKKKFRtPSFLKKS |
Homo sapiens |
MDA-MB-231 Cell |
pmid |
sentence |
31548578 |
We found that Cdk5 directly phosphorylated the actin-binding protein adducin-1 (ADD1) at T724 in vitro and in intact cells. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 |
phosphorylation
|
PPP1R2 |
0.363 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250672 |
Thr73 |
MKIDEPStPYHSMMG |
in vitro |
|
pmid |
sentence |
11320080 |
Neuronal Cdc2-like protein kinase (Cdk5/p25) is associated with protein phosphatase 1 and phosphorylates inhibitor-2. | NCLK Phosphorylates Thr72 of I-2 |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
CDK5 |
phosphorylation
|
APP |
0.584 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250651 |
Thr743 |
VEVDAAVtPEERHLS |
Rattus norvegicus |
Neuron |
pmid |
sentence |
10936190 |
In vitro, active cyclin-dependent kinase 5 (Cdk5) phosphorylated the cytoplasmic domain of APP at Thr(668). Treatment of mature neurons with an antisense oligonucleotide to Cdk5 suppressed Cdk5 expression and significantly diminished the level of phosphorylated APP. The expression of APP was unaffected in antisense-treated neurons. These results indicate that in neurons APP is phosphorylated by Cdk5, and that this may play a role in its localization. |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |
+ |
CDK5 | up-regulates activity
phosphorylation
|
PPP1R1B |
0.769 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250671 |
Thr75 |
RPNPCAYtPPSLKAV |
Rattus norvegicus |
Brain |
pmid |
sentence |
10604473 |
We find that DARPP-32 is converted into an inhibitor of PKA when phosphorylated at threonine 75 by cyclin-dependent kinase 5 (Cdk5). Cdk5 phosphorylates DARPP-32 in vitro and in intact brain cells. Phospho-Thr 75 DARPP-32 inhibits PKA in vitro by a competitive mechanism. |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |
Pathways: | Dopaminergic Synapse |
+ |
PRKCD | down-regulates activity
phosphorylation
|
CDK5 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277386 |
Thr77 |
LHSDKKLtLVFEFCD |
Homo sapiens |
DU-145 Cell |
pmid |
sentence |
29511352 |
This generates a binding site for the C2 domain of PKCδ, which in turn phosphorylates CDK5 on T77. The resulting dissociation of the CDK5R1/CDK5 complex abolishes the activity of CDK5. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ABL1 | up-regulates activity
phosphorylation
|
CDK5 |
0.567 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-245288 |
Tyr15 |
EKIGEGTyGTVFKAK |
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
10896159 |
Phosphorylation of Cdk5 by c-Abl occurs on tyrosine 15 (Y15), which is stimulatory for p35/Cdk5 kinase activity. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
FYN | up-regulates activity
phosphorylation
|
CDK5 |
0.59 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251156 |
Tyr15 |
EKIGEGTyGTVFKAK |
Homo sapiens |
|
pmid |
sentence |
14757045 |
Constitutively active Fyn phosphorylated Tyr15 of Cdk5. Fyn Facilitates Kinase Activity of Cdk5 Via Tyr15 Phosphorylation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
seliciclib | down-regulates
chemical inhibition
|
CDK5 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-206574 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 | down-regulates
phosphorylation
|
LMTK2 |
0.512 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-102717 |
|
|
Homo sapiens |
|
pmid |
sentence |
12832520 |
Cprk displays catalytic activity in in vitro kinase assays and is itself phosphorylated by cdk5/p35. Cdk5/p35 inhibits cprk activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-102652 |
|
|
Homo sapiens |
|
pmid |
sentence |
12832520 |
Cprk displays catalytic activity in in vitro kinase assays and is itself phosphorylated by cdk5/p35. Cdk5/p35 inhibits cprk activity. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CDK5R1 | up-regulates
binding
|
CDK5 |
0.942 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-123387 |
|
|
Homo sapiens |
|
pmid |
sentence |
15013773 |
In brain, p35 or p25 exists with and activates cdk5 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Dinaciclib | down-regulates
chemical inhibition
|
CDK5 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-191328 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
4-(2,6-dichlorobenzamido)-N-(piperidin-4-yl)-pyrazole-3-carboxamide | down-regulates
chemical inhibition
|
CDK5 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-189993 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
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 |
+ |
alvocidib hydrochloride | down-regulates
chemical inhibition
|
CDK5 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-192467 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5R1 | up-regulates activity
binding
|
CDK5 |
0.942 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-268153 |
|
|
Homo sapiens |
Neuron |
pmid |
sentence |
10604467 |
Cyclin-dependent kinase 5 (Cdk5) is required for proper development of the mammalian central nervous system. To be activated, Cdk5 has to associate with its regulatory subunit, p35. We have found that p25, a truncated form of p35, accumulates in neurons in the brains of patients with Alzheimer's disease. This accumulation correlates with an increase in Cdk5 kinase activity. Unlike p35, p25 is not readily degraded, and binding of p25 to Cdk5 constitutively activates Cdk5, changes its cellular location and alters its substrate specificity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 | down-regulates activity
phosphorylation
|
PP1 |
0.484 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264649 |
|
|
Homo sapiens |
|
pmid |
sentence |
12202491 |
Pp1 isoforms contain an arg-pro-ile/val-thr-pro-pro-arg sequence near the c terminus, a known site of phosphorylation by cdc/cdk kinases, and phosphorylation attenuates phosphatase activity. Increasing doses of cdk2 resulted in increased phosphorylation of the thr-320 site. Phosphorylation of this site in pp1 corresponded to decreased pp1 activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
alvocidib | down-regulates
chemical inhibition
|
CDK5 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-192104 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
N-[6,6-dimethyl-5-[(1-methyl-4-piperidinyl)-oxomethyl]-1,4-dihydropyrrolo[3,4-c]pyrazol-3-yl]-3-methylbutanamide | down-regulates
chemical inhibition
|
CDK5 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-206133 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Publications: |
1 |
Organism: |
Homo Sapiens |