| + |
DYRK1A | up-regulates 
phosphorylation
|
TP53 |
0.02 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167407 |
Ser15 |
PSVEPPLsQETFSDL |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 20696760 |
Dyrk1a phosphorylates p53 and inhibits proliferation of embryonic neuronal cells. we found that dyrk1a phosphorylates p53 at ser-15 in vitro and in immortalized rat embryonic hippocampal progenitor h19-7 cells. In addition, dyrk1a-induced p53 phosphorylation at ser-15 led to a robust induction of p53 target genes |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DYRK1A | up-regulates
phosphorylation
|
RCAN1 |
0.46 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-139958 |
Ser167 |
FLISPPAsPPVGWKQ |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 16126726 |
We show that rcan1 self-associates and forms multimers, and that this process is promoted by the dyrk1a-mediated phosphorylation of rcan1 at the thr(192) residue. these results suggest that the phosphorylation of rcan1 by dyrk1a stimulates the formation of insoluble aggregates upon aging. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-102290 |
Ser167 |
FLISPPAsPPVGWKQ |
Homo sapiens |
|
| pmid |
sentence |
| 12809556 |
In the present study, dyrk1a is shown to directly interact with and phosphorylate rcan1 at ser112 and thr192 residues. Dyrk1a-mediated phosphorylation of rcan1 at ser112 primes the protein for the gsk3_-mediated phosphorylation of ser108. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
DYRK1A |
phosphorylation
|
SRSF1 |
0.56 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179615 |
Ser238 |
SRGSPRYsPRHSRSR |
Homo sapiens |
|
| pmid |
sentence |
| 18658135 |
Here, we demonstrate that dyrk1a, a kinase encoded by a gene in the ds critical region, phosphorylates alternative splicing factor (asf) at ser-227, ser-234, and ser-238, driving it into nuclear speckles and preventing it from facilitating tau exon 10 inclusion. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
DYRK1A | down-regulates 
phosphorylation
|
AMPH |
0.27 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-126839 |
Ser262 |
LRIAKTPsPPEEPSP |
Homo sapiens |
|
| pmid |
sentence |
| 15262992 |
Recent studies show that phosphorylation of amphiphysin1 prd by cdk5 inhibited the association of amphiphysin1 with ap-2 in synaptic vesicle endocytosis (7, 8) similar to that by mapk (present report). Cdk5 appears to phosphorylate amphiphysin1 at serines 261, 272, 276, and 285 and threonine 310, located in the prd |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-126843 |
Ser272 |
EEPSPLPsPTASPNH |
Homo sapiens |
|
| pmid |
sentence |
| 15262992 |
Recent studies show that phosphorylation of amphiphysin1 prd by cdk5 inhibited the association of amphiphysin1 with ap-2 in synaptic vesicle endocytosis (7, 8) similar to that by mapk (present report). Cdk5 appears to phosphorylate amphiphysin1 at serines 261, 272, 276, and 285 and threonine 310, located in the prd |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-126847 |
Ser276 |
PLPSPTAsPNHTLAP |
Homo sapiens |
|
| pmid |
sentence |
| 15262992 |
Recent studies show that phosphorylation of amphiphysin1 prd by cdk5 inhibited the association of amphiphysin1 with ap-2 in synaptic vesicle endocytosis (7, 8) similar to that by mapk (present report). Cdk5 appears to phosphorylate amphiphysin1 at serines 261, 272, 276, and 285 and threonine 310, located in the prd |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-126851 |
Ser285 |
NHTLAPAsPAPARPR |
Homo sapiens |
|
| pmid |
sentence |
| 15262992 |
Recent studies show that phosphorylation of amphiphysin1 prd by cdk5 inhibited the association of amphiphysin1 with ap-2 in synaptic vesicle endocytosis (7, 8) similar to that by mapk (present report). Cdk5 appears to phosphorylate amphiphysin1 at serines 261, 272, 276, and 285 and threonine 310, located in the prd |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-146902 |
Ser293 |
PAPARPRsPSQTRKG |
Homo sapiens |
|
| pmid |
sentence |
| 16733250 |
Here we report that amphiphysin i (amph i) is also a mnb/dyrk1a substrate. This kinase phosphorylated native amph i in rodent brains and recombinant human amph i expressed in escherichia coli. Serine 293 (ser-293) was identified as the major site, whereas serine 295 and threonine 310 were found as minor kinase sitesamph i phosphorylated by mnb/dyrk1a decreased endophilin binding in vitro. From these results we conclude that amph i at ser-293 is phosphorylated by mnb/dyrk1a and that the phosphorylation has physiological significance in controlling the interaction of amphiphysin with endocytic accessory proteins. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-146906 |
Ser295 |
PARPRSPsQTRKGPP |
Homo sapiens |
|
| pmid |
sentence |
| 16733250 |
Here we report that amphiphysin i (amph i) is also a mnb/dyrk1a substrate. This kinase phosphorylated native amph i in rodent brains and recombinant human amph i expressed in escherichia coli. Serine 293 (ser-293) was identified as the major site, whereas serine 295 and threonine 310 were found as minor kinase sitesamph i phosphorylated by mnb/dyrk1a decreased endophilin binding in vitro. From these results we conclude that amph i at ser-293 is phosphorylated by mnb/dyrk1a and that the phosphorylation has physiological significance in controlling the interaction of amphiphysin with endocytic accessory proteins. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-146910 |
Thr310 |
VPPLPKVtPTKELQQ |
Homo sapiens |
|
| pmid |
sentence |
| 16733250 |
Here we report that amphiphysin i (amph i) is also a mnb/dyrk1a substrate. This kinase phosphorylated native amph i in rodent brains and recombinant human amph i expressed in escherichia coli. Serine 293 (ser-293) was identified as the major site, whereas serine 295 and threonine 310 were found as minor kinase sitesamph i phosphorylated by mnb/dyrk1a decreased endophilin binding in vitro. From these results we conclude that amph i at ser-293 is phosphorylated by mnb/dyrk1a and that the phosphorylation has physiological significance in controlling the interaction of amphiphysin with endocytic accessory proteins. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-126855 |
Thr310 |
VPPLPKVtPTKELQQ |
Homo sapiens |
|
| pmid |
sentence |
| 15262992 |
Recent studies show that phosphorylation of amphiphysin1 prd by cdk5 inhibited the association of amphiphysin1 with ap-2 in synaptic vesicle endocytosis (7, 8) similar to that by mapk (present report). Cdk5 appears to phosphorylate amphiphysin1 at serines 261, 272, 276, and 285 and threonine 310, located in the prd |
|
| Publications: |
8 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
DYRK1A | down-regulates activity
phosphorylation
|
FOXO |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252909 |
Ser329 |
STISGRLsPIMTEQD |
Homo sapiens |
|
| pmid |
sentence |
| 11311120 |
The kinase dyrk1a phosphorylates the transcription factor fkhr at ser329 in vitro, a novel in vivo phosphorylation siteser(329) phosphorylation also decreases the ability of fkhr to stimulate gene transactivation and reduces the proportion of fkhr present in the nucleus |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252906 |
Ser330 |
RLSPIMAsTELDEVQ |
Homo sapiens |
|
| pmid |
sentence |
| 19188143 |
Additionally, ck1, dyrk1a, and cdk2 also phosphorylate foxos at various sites to inhibit foxos activity phosphorylation of foxos by akt, ikk, erk, ck1, cdk2, and dyrk1a universally leads to foxo's inhibition. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Skeletal Muscle |
| + |
DYRK1A | down-regulates activity
phosphorylation
|
FOXO1 |
0.11 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-106829 |
Ser329 |
STISGRLsPIMTEQD |
Homo sapiens |
|
| pmid |
sentence |
| 11311120 |
The kinase dyrk1a phosphorylates the transcription factor fkhr at ser329 in vitro, a novel in vivo phosphorylation siteser(329) phosphorylation also decreases the ability of fkhr to stimulate gene transactivation and reduces the proportion of fkhr present in the nucleus |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Skeletal Muscle |
| + |
DYRK1A |
phosphorylation
|
CCNL2 |
0.50 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251087 |
Ser330 |
LDGTSGFsPAPKLVE |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 14623875 |
DYRK1A interacted with cyclin L2 in pull-down assays, and overexpression of DYRK1A stimulated phosphorylation of cyclin L2 in COS-7 cells. | Three phosphoserines were identified in the slower migrating bands (Fig. 9; Ser-330, Ser-338, and Ser-369). All of these serine residues are located N-terminal of proline residues, consistent with our previous classification of DYRK1A as a “proline-directed” kinase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251088 |
Ser338 |
PAPKLVEsPKEGKGS |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 14623875 |
DYRK1A interacted with cyclin L2 in pull-down assays, and overexpression of DYRK1A stimulated phosphorylation of cyclin L2 in COS-7 cells. | Three phosphoserines were identified in the slower migrating bands (Fig. 9; Ser-330, Ser-338, and Ser-369). All of these serine residues are located N-terminal of proline residues, consistent with our previous classification of DYRK1A as a “proline-directed” kinase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251089 |
Ser369 |
AKKAKADsPVNGLPK |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 14623875 |
DYRK1A interacted with cyclin L2 in pull-down assays, and overexpression of DYRK1A stimulated phosphorylation of cyclin L2 in COS-7 cells. | Three phosphoserines were identified in the slower migrating bands (Fig. 9; Ser-330, Ser-338, and Ser-369). All of these serine residues are located N-terminal of proline residues, consistent with our previous classification of DYRK1A as a “proline-directed” kinase. |
|
| Publications: |
3 |
Organism: |
Chlorocebus Aethiops |
| + |
DYRK1A | down-regulates
phosphorylation
|
FOXO |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252907 |
Ser330 |
RLSPIMAsTELDEVQ |
Homo sapiens |
Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell |
| pmid |
sentence |
| 19188143 |
Additionally, ck1, dyrk1a, and cdk2 also phosphorylate foxos at various sites to inhibit foxos activity phosphorylation of foxos by akt, ikk, erk, ck1, cdk2, and dyrk1a universally leads to foxo's inhibition. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252908 |
|
|
Homo sapiens |
Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell |
| pmid |
sentence |
| 19188143 |
Additionally, ck1, dyrk1a, and cdk2 also phosphorylate foxos at various sites to inhibit foxos activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252905 |
|
|
Homo sapiens |
Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell |
| pmid |
sentence |
| 19188143 |
Additionally, ck1, dyrk1a, and cdk2 also phosphorylate foxos at various sites to inhibit foxos activity |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
DYRK1A | down-regulates
phosphorylation
|
FOXO3 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183674 |
Ser330 |
RLSPIMAsTELDEVQ |
Homo sapiens |
Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell |
| pmid |
sentence |
| 19188143 |
Additionally, ck1, dyrk1a, and cdk2 also phosphorylate foxos at various sites to inhibit foxos activity phosphorylation of foxos by akt, ikk, erk, ck1, cdk2, and dyrk1a universally leads to foxo's inhibition. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DYRK1A | down-regulates activity
phosphorylation
|
FOXO3 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-106833 |
Ser330 |
RLSPIMAsTELDEVQ |
Homo sapiens |
|
| pmid |
sentence |
| 19188143 |
Additionally, ck1, dyrk1a, and cdk2 also phosphorylate foxos at various sites to inhibit foxos activity phosphorylation of foxos by akt, ikk, erk, ck1, cdk2, and dyrk1a universally leads to foxo's inhibition. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DYRK1A | down-regulates
phosphorylation
|
MAPT |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-171030 |
Ser519 |
SGYSSPGsPGTPGSR |
Homo sapiens |
|
| pmid |
sentence |
| 21215781 |
Dyrk1a phosphorylates tau at least at s202, t212 and s404, but t212 phosphorylation is known to initiate tau hyperphosphorylation by gsk3b (ryoo et al., 2007;woods et al., 2001) and has been demonstrated to have a role in alternative splicing of taumrna |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-171034 |
Ser721 |
PVVSGDTsPRHLSNV |
Homo sapiens |
|
| pmid |
sentence |
| 21215781 |
Dyrk1a phosphorylates tau at least at s202, t212 and s404, but t212 phosphorylation is known to initiate tau hyperphosphorylation by gsk3b (ryoo et al., 2007;woods et al., 2001) and has been demonstrated to have a role in alternative splicing of taumrna |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-171038 |
Thr529 |
TPGSRSRtPSLPTPP |
Homo sapiens |
|
| pmid |
sentence |
| 21215781 |
Dyrk1a phosphorylates tau at least at s202, t212 and s404, but t212 phosphorylation is known to initiate tau hyperphosphorylation by gsk3b (ryoo et al., 2007;woods et al., 2001) and has been demonstrated to have a role in alternative splicing of taumrna |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
DYRK1A | up-regulates activity
phosphorylation
|
DYRK1A |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251090 |
Ser529 |
SNSGRARsDPTHQHR |
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 17229891 |
In the present study, we show that DYRK1A autophosphorylates, via an intramolecular mechanism, on Ser-520, in the PEST domain of the protein. | Instead, we demonstrate that this phosphorylation allows the binding of 14-3-3beta, which in turn stimulates the catalytic activity of DYRK1A. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-111145 |
Tyr321 |
LGQRIYQyIQSRFYR |
Homo sapiens |
COS-7 Cell |
| pmid |
sentence |
| 11672423 |
Direct identification of phosphorylated residues by tandem ms confirmed that tyr-321, but not tyr-319, was phosphorylated. When expressed in cos-7 cells, dyrk1a was found to be fully phosphorylated on tyr-321. A catalytically inactive mutant of dyrk1a contained no detectable phosphotyrosine, indicating that tyr-321 is autophosphorylated by dyrk1a. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
DYRK1A | down-regulates
phosphorylation
|
DNM1 |
0.54 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-127440 |
Ser795 |
VPPARPGsRGPAPGP |
Homo sapiens |
|
| pmid |
sentence |
| 15287745 |
Mnb/dyrk1a was shown to phosphorylate dynamin 1 and alter its interactions with several sh3 domain-containing endocytic accessory proteins.Phosphorylation At s795 and s857 was confirmed in full-length dynamin 1, and s857 was subsequently determined to be the major mnb/dyrk1a phosphorylation site in vitro. Phosphorylation at s857 was demonstrated to be the basis for altering the binding of dynamin 1 to amphiphysin 1 and grb 2 by site-directed mutants mimicking phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-127444 |
Ser857 |
ASPSRPEsPRPPFDL |
Homo sapiens |
|
| pmid |
sentence |
| 15287745 |
Mnb/dyrk1a was shown to phosphorylate dynamin 1 and alter its interactions with several sh3 domain-containing endocytic accessory proteins.Phosphorylation At s795 and s857 was confirmed in full-length dynamin 1, and s857 was subsequently determined to be the major mnb/dyrk1a phosphorylation site in vitro. Phosphorylation at s857 was demonstrated to be the basis for altering the binding of dynamin 1 to amphiphysin 1 and grb 2 by site-directed mutants mimicking phosphorylation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
DYRK1A | up-regulates
phosphorylation
|
SNCA |
0.05 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149393 |
Ser87 |
KTVEGAGsIAAATGF |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 16959772 |
In vitro kinase assay of anti-dyrk1a immunocomplexes demonstrated that dyrk1a could phosphorylate alpha-synuclein at ser-87. Furthermore, aggregates formed by phosphorylated alpha-synuclein have a distinct morphology and are more neurotoxic compared with aggregates composed of unmodified wild type alpha-synuclein. These findings suggest alpha-synuclein inclusion formation regulated by dyrk1a, potentially affecting neuronal cell viability. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DYRK1A | down-regulates
phosphorylation
|
CCND1 |
0.05 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-202838 |
Thr286 |
EEVDLACtPTDVRDV |
Homo sapiens |
|
| pmid |
sentence |
| 24119401 |
Dyrk1a controls the rate of cycd1 degradation by directly phosphorylating cycd1 at thr 286 and thereby regulates the fraction of cycling cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DYRK1A |
phosphorylation
|
SF3B1 |
0.49 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-144975 |
Thr434 |
PARKLTAtPTPLGGM |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16512921 |
The present data show that the splicing factor sf3b1 is a substrate of the protein kinase dyrk1a and suggest that dyrk1a may be involved in the regulation of pre mrna-splicing. by mass spectrometry and mutational analysis of sf3b1, thr434 was identified as the major phosphorylation site for dyrk1a. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DYRK1A | down-regulates
phosphorylation
|
SPRY2 |
0.36 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179828 |
Thr75 |
KPAPRPStQHKHERL |
Homo sapiens |
|
| pmid |
sentence |
| 18678649 |
We identify dyrk1a as one of the protein kinases of sprouty2. We show that dyrk1a interacts with and regulates the phosphorylation status of sprouty2. Moreover, we identify thr75 on sprouty2 as a dyrk1a phosphorylation site in vitro and in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
DYRK1A | up-regulates
phosphorylation
|
DYRK1A |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-79760 |
Tyr319 |
CQLGQRIyQYIQSRF |
Homo sapiens |
|
| pmid |
sentence |
| 10910078 |
Mirk kinase is activated by autophosphorylation on tyrosine at the y271/y273 site |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-79764 |
Tyr321 |
LGQRIYQyIQSRFYR |
Homo sapiens |
|
| pmid |
sentence |
| 10910078 |
Mirk kinase is activated by autophosphorylation on tyrosine at the y271/y273 site |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
DYRK1A | down-regulates
phosphorylation
|
NOTCH1 |
0.06 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-185494 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19383720 |
Dyrk1a physically interacts with the nicd inducing its phosphorylation in the ankyrin domain, thereby attenuating notch . |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
DYRK1A | down-regulates
phosphorylation
|
FOXO6 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183680 |
|
|
Homo sapiens |
Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell |
| pmid |
sentence |
| 19188143 |
Additionally, ck1, dyrk1a, and cdk2 also phosphorylate foxos at various sites to inhibit foxos activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DYRK1A | down-regulates
phosphorylation
|
FOXO4 |
0.12 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183677 |
|
|
Homo sapiens |
Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell |
| pmid |
sentence |
| 19188143 |
Additionally, ck1, dyrk1a, and cdk2 also phosphorylate foxos at various sites to inhibit foxos activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DYRK1A | down-regulates
phosphorylation
|
FOXO1 |
0.11 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183670 |
|
|
Homo sapiens |
Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell |
| pmid |
sentence |
| 19188143 |
Additionally, ck1, dyrk1a, and cdk2 also phosphorylate foxos at various sites to inhibit foxos activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DYRK1A | down-regulates
phosphorylation
|
NOTCH |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254313 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19383720 |
Dyrk1a physically interacts with the nicd inducing its phosphorylation in the ankyrin domain, thereby attenuating notch . |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
DYRK1A | up-regulates
phosphorylation
|
GLI1 |
0.19 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-90809 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12138125 |
Dyrk1 phosphorylates gli1 on more than one domain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
DYRK1A
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