Relation Results

Summary

Name DYRK1A
Full Name Dual specificity tyrosine-phosphorylation-regulated kinase 1A
Synonyms Dual specificity YAK1-related kinase, HP86, Protein kinase minibrain homolog, MNBH, hMNB | DYRK, MNB, MNBH
Primary ID Q13627
Links - -
Type protein
Relations 56
Function Dual-specificity kinase which possesses both serine/threonine and tyrosine kinase activities. May play a role in a signaling pathway regulating nuclea ...
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Type: Score: Layout: SPV 
0.3360.4250.5740.3960.4180.2370.4370.4020.6730.5160.5160.5840.3640.3150.4360.20.2690.4220.5730.4020.510.550.3080.4030.4150.7250.5230.3090.3190.403DYRK1ACDKN1BTP53RCAN1SRSF1MEF2DPPM1BNFATC1AMPHLIN52FOXO1FOXOCCNL2FOXO3PLK2MAPTGYS1DNM1SNCACCND1SF3B1SIRT1SPRY2NOTCHSRSF2DCAF7GLI1FOXO6FOXO4NOTCH1

Modifications Tables

Relations

Regulator
Mechanism
target
score
+ up-regulates activity img/direct-activation.png phosphorylation CDKN1B 0.336
Identifier Residue Sequence Organism Cell Line
SIGNOR-278250 Ser10 NVRVSNGsPSLERMD Homo sapiens
pmid sentence
DYRK1A phosphorylates p27 Kip1 at Ser10 in primary neurons and in vivo.|Thus, our results identify DYRK1A as the predominant kinase that phosphorylates and stabilizes p27Kip1 during neuronal differentiation.
Publications: 1 Organism: Homo Sapiens
+ up-regulates img/direct-activation.png phosphorylation TP53 0.425
Identifier Residue Sequence Organism Cell Line
SIGNOR-167407 Ser15 PSVEPPLsQETFSDL Homo sapiens Neuron
pmid sentence
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
+ up-regulates img/direct-activation.png phosphorylation RCAN1 0.574
Identifier Residue Sequence Organism Cell Line
SIGNOR-139958 Ser167 FLISPPAsPPVGWKQ Homo sapiens T-lymphocyte
pmid sentence
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
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
+ img/unknown.png phosphorylation SRSF1 0.396
Identifier Residue Sequence Organism Cell Line
SIGNOR-179615 Ser238 SRGSPRYsPRHSRSR Homo sapiens
pmid sentence
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
+ down-regulates activity img/direct_inhibition.png phosphorylation MEF2D 0.418
Identifier Residue Sequence Organism Cell Line
SIGNOR-277565 Ser251 NKVIPAKsPPPPTHS in vitro
pmid sentence
Here, we uncovered that dual-specificity tyrosine phosphorylation regulated kinase 1A (DYRK1A), a kinase critical in Down's syndrome pathogenesis, directly bound to and phosphorylated MEF2D at Ser251 in vitro. Phosphorylation of MEF2D by DYRK1A significantly increased MEF2D protein level but attenuated its transcriptional activity, which resulted in decreased transcriptions of MEF2D target genes.
Identifier Residue Sequence Organism Cell Line
SIGNOR-277901 Ser251 NKVIPAKsPPPPTHS Homo sapiens HEK-293 Cell
pmid sentence
DYRK1A phosphorylates MEF2D and decreases its transcriptional activity
Publications: 2 Organism: In Vitro, Homo Sapiens
+ down-regulates activity img/direct_inhibition.png dephosphorylation DYRK1A 0.237
Identifier Residue Sequence Organism Cell Line
SIGNOR-277108 Ser258 NTNFRGVsLNLTRKF Homo sapiens
pmid sentence
In conclusion, our study demonstrates that DYRK1A autophosphorylates Ser258, the dephosphorylation target of PPM1B, and PPM1B negatively regulates DYRK1A activity.|We found that PPM1B dephosphorylates DYRK1A at Ser258, contributing to the inhibition of DYRK1A activity.
Publications: 1 Organism: Homo Sapiens
+ up-regulates activity img/direct-activation.png phosphorylation NFATC1 0.437
Identifier Residue Sequence Organism Cell Line
SIGNOR-278279 Ser261 ARSSRPAsPCNKRKY Homo sapiens
pmid sentence
DYRK1A phosphorylation of NFATc1 and alphaA at S261, S278, S403 and S409 interfered with NFATc1 ubiquitination and ubiquitin-proteasome degradation.|Here, we demonstrated that DYRK1A increased NFATc1 (NFATc1 and alphaA isoform) protein stability, in contrast to the decrease of NFATc2 protein stability by DYRK1A.
Identifier Residue Sequence Organism Cell Line
SIGNOR-278278 Ser278 NGRQPPYsPHHSPTP Homo sapiens
pmid sentence
DYRK1A phosphorylation of NFATc1 and alphaA at S261, S278, S403 and S409 interfered with NFATc1 ubiquitination and ubiquitin-proteasome degradation.|Here, we demonstrated that DYRK1A increased NFATc1 (NFATc1 and alphaA isoform) protein stability, in contrast to the decrease of NFATc2 protein stability by DYRK1A.
Identifier Residue Sequence Organism Cell Line
SIGNOR-278277 Ser403 WAKPKPLsPTSYMSP Homo sapiens
pmid sentence
DYRK1A phosphorylation of NFATc1 and alphaA at S261, S278, S403 and S409 interfered with NFATc1 ubiquitination and ubiquitin-proteasome degradation.|Here, we demonstrated that DYRK1A increased NFATc1 (NFATc1 and alphaA isoform) protein stability, in contrast to the decrease of NFATc2 protein stability by DYRK1A.
Identifier Residue Sequence Organism Cell Line
SIGNOR-278276 Ser409 LSPTSYMsPTLPALD Homo sapiens
pmid sentence
DYRK1A phosphorylation of NFATc1 and alphaA at S261, S278, S403 and S409 interfered with NFATc1 ubiquitination and ubiquitin-proteasome degradation.|Here, we demonstrated that DYRK1A increased NFATc1 (NFATc1 and alphaA isoform) protein stability, in contrast to the decrease of NFATc2 protein stability by DYRK1A.
Publications: 4 Organism: Homo Sapiens
+ down-regulates img/direct_inhibition.png phosphorylation AMPH 0.402
Identifier Residue Sequence Organism Cell Line
SIGNOR-126839 Ser262 LRIAKTPsPPEEPSP Homo sapiens
pmid sentence
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
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
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
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-146906 Ser295 PARPRSPsQTRKGPP Homo sapiens
pmid sentence
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
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
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: 7 Organism: Homo Sapiens
Tissue: Brain
+ up-regulates activity img/direct-activation.png phosphorylation LIN52 0.673
Identifier Residue Sequence Organism Cell Line
SIGNOR-262846 Ser28 FEKLDRAsPDLWPEQ Homo sapiens T-98G Cell
pmid sentence
Here we report that DYRK1A can specifically phosphorylate LIN52 on serine residue 28, and that this phosphorylation is required for DREAM assembly.
Publications: 1 Organism: Homo Sapiens
+ down-regulates activity img/direct_inhibition.png phosphorylation AMPH 0.402
Identifier Residue Sequence Organism Cell Line
SIGNOR-146902 Ser293 PAPARPRsPSQTRKG Homo sapiens
pmid sentence
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.
Publications: 1 Organism: Homo Sapiens
+ down-regulates activity img/direct_inhibition.png phosphorylation FOXO1 0.516
Identifier Residue Sequence Organism Cell Line
SIGNOR-106829 Ser329 STISGRLsPIMTEQD Homo sapiens
pmid sentence
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
+ down-regulates activity img/direct_inhibition.png phosphorylation FOXO 0.516
Identifier Residue Sequence Organism Cell Line
SIGNOR-252909 Ser329 STISGRLsPIMTEQD Homo sapiens
pmid sentence
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
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
+ img/unknown.png phosphorylation CCNL2 0.584
Identifier Residue Sequence Organism Cell Line
SIGNOR-251087 Ser330 LDGTSGFsPAPKLVE Chlorocebus aethiops COS-7 Cell
pmid sentence
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
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
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
+ down-regulates activity img/direct_inhibition.png phosphorylation FOXO3 0.364
Identifier Residue Sequence Organism Cell Line
SIGNOR-106833 Ser330 RLSPIMAsTELDEVQ Homo sapiens
pmid sentence
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
+ down-regulates img/direct_inhibition.png phosphorylation FOXO 0.516
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
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-252905 Homo sapiens
pmid sentence
Additionally, ck1, dyrk1a, and cdk2 also phosphorylate foxos at various sites to inhibit foxos activity
Publications: 2 Organism: Homo Sapiens
+ down-regulates img/direct_inhibition.png phosphorylation FOXO3 0.364
Identifier Residue Sequence Organism Cell Line
SIGNOR-183674 Ser330 RLSPIMAsTELDEVQ Homo sapiens
pmid sentence
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
+ up-regulates quantity by stabilization img/direct-activation.png phosphorylation PLK2 0.315
Identifier Residue Sequence Organism Cell Line
SIGNOR-277791 Ser358 VPDFHLSsPAKNFFK Homo sapiens HEK-293 Cell
pmid sentence
 In the present study, it was demonstrated that dual specificity tyrosine-phosphorylation-regulated kinase 1A (DYRK1A) interacts with and phosphorylates PLK2 at Ser358. DYRK1A-mediated phosphorylation of PLK2 increases its protein stability. 
Identifier Residue Sequence Organism Cell Line
SIGNOR-277805 Ser358 VPDFHLSsPAKNFFK Homo sapiens HEK-293 Cell
pmid sentence
 In the present study, it was demonstrated that dual specificity tyrosine-phosphorylation-regulated kinase 1A (DYRK1A) interacts with and phosphorylates PLK2 at Ser358. DYRK1A-mediated phosphorylation of PLK2 increases its protein stability. 
Publications: 2 Organism: Homo Sapiens
+ down-regulates img/direct_inhibition.png phosphorylation MAPT 0.436
Identifier Residue Sequence Organism Cell Line
SIGNOR-171030 Ser519 SGYSSPGsPGTPGSR Homo sapiens
pmid sentence
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
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
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
+ up-regulates activity img/direct-activation.png phosphorylation DYRK1A 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-251090 Ser529 SNSGRARsDPTHQHR Homo sapiens U2-OS Cell
pmid sentence
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
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
+ down-regulates activity img/direct_inhibition.png phosphorylation GYS1 0.269
Identifier Residue Sequence Organism Cell Line
SIGNOR-260632 Ser641 YRYPRPAsVPPSPSL Chlorocebus aethiops COS-7 Cell
pmid sentence
DYRK Family Protein Kinases Phosphorylate and Inactivate Glycogen Synthase. both protein kinases phosphorylate site 3a but no other sites that affect glycogen synthase activity.
Publications: 1 Organism: Chlorocebus Aethiops
+ down-regulates img/direct_inhibition.png phosphorylation DNM1 0.422
Identifier Residue Sequence Organism Cell Line
SIGNOR-127440 Ser795 VPPARPGsRGPAPGP Homo sapiens
pmid sentence
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
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
+ up-regulates img/direct-activation.png phosphorylation SNCA 0.573
Identifier Residue Sequence Organism Cell Line
SIGNOR-149393 Ser87 KTVEGAGsIAAATGF Homo sapiens Neuron
pmid sentence
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
+ down-regulates img/direct_inhibition.png phosphorylation CCND1 0.402
Identifier Residue Sequence Organism Cell Line
SIGNOR-202838 Thr286 EEVDLACtPTDVRDV Homo sapiens
pmid sentence
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
+ img/unknown.png phosphorylation SF3B1 0.51
Identifier Residue Sequence Organism Cell Line
SIGNOR-144975 Thr434 PARKLTAtPTPLGGM Homo sapiens HEK-293 Cell
pmid sentence
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
+ up-regulates activity img/direct-activation.png phosphorylation SIRT1 0.55
Identifier Residue Sequence Organism Cell Line
SIGNOR-278473 Thr530 YLSELPPtPLHVSED Homo sapiens
pmid sentence
DYRK1A and DYRK3 directly phosphorylate SIRT1 at Thr(522), promoting deacetylation of p53.|DYRK1A and DYRK3 promote cell survival through phosphorylation and activation of SIRT1.
Publications: 1 Organism: Homo Sapiens
+ down-regulates img/direct_inhibition.png phosphorylation SPRY2 0.308
Identifier Residue Sequence Organism Cell Line
SIGNOR-179828 Thr75 KPAPRPStQHKHERL Homo sapiens
pmid sentence
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
+ up-regulates img/direct-activation.png phosphorylation DYRK1A 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-79760 Tyr319 CQLGQRIyQYIQSRF Homo sapiens
pmid sentence
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
Mirk kinase is activated by autophosphorylation on tyrosine at the y271/y273 site
Publications: 2 Organism: Homo Sapiens
+ down-regulates img/direct_inhibition.png phosphorylation FOXO1 0.516
Identifier Residue Sequence Organism Cell Line
SIGNOR-183670 Homo sapiens Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell
pmid sentence
Additionally, ck1, dyrk1a, and cdk2 also phosphorylate foxos at various sites to inhibit foxos activity.
Publications: 1 Organism: Homo Sapiens
+ down-regulates img/direct_inhibition.png phosphorylation NOTCH 0.403
Identifier Residue Sequence Organism Cell Line
SIGNOR-254313 Homo sapiens
pmid sentence
Dyrk1a physically interacts with the nicd inducing its phosphorylation in the ankyrin domain, thereby attenuating notch .
Publications: 1 Organism: Homo Sapiens
Tissue: Brain
+ down-regulates activity img/direct_inhibition.png phosphorylation SRSF2 0.415
Identifier Residue Sequence Organism Cell Line
SIGNOR-278307 Homo sapiens
pmid sentence
Dyrk1A inhibits SC35\u2032s activity to promote tau exon 10 inclusion.|Dyrk1A interacts with and phosphorylates SC35 and inhibits its activity to promote tau exon 10 inclusion.
Publications: 1 Organism: Homo Sapiens
+ up-regulates activity img/direct-activation.png binding DYRK1A 0.725
Identifier Residue Sequence Organism Cell Line
SIGNOR-260630 Chlorocebus aethiops COS-7 Cell
pmid sentence
Two isoforms of DYRK, DYRK1A and DYRK1B, co-immunoprecipitate with HAN11 when coexpressed in COS cells indicating that the proteins interact in mammalian cells. HAN11 might target DYRKs to cytosolic locations for regulation of specific cellular functions.
Publications: 1 Organism: Chlorocebus Aethiops
+ up-regulates img/direct-activation.png phosphorylation GLI1 0.523
Identifier Residue Sequence Organism Cell Line
SIGNOR-90809 Homo sapiens
pmid sentence
Dyrk1 phosphorylates gli1 on more than one domain.
Publications: 1 Organism: Homo Sapiens
+ down-regulates img/direct_inhibition.png phosphorylation FOXO6 0.309
Identifier Residue Sequence Organism Cell Line
SIGNOR-183680 Homo sapiens
pmid sentence
Additionally, ck1, dyrk1a, and cdk2 also phosphorylate foxos at various sites to inhibit foxos activity
Publications: 1 Organism: Homo Sapiens
+ down-regulates img/direct_inhibition.png phosphorylation FOXO4 0.319
Identifier Residue Sequence Organism Cell Line
SIGNOR-183677 Homo sapiens Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell
pmid sentence
Additionally, ck1, dyrk1a, and cdk2 also phosphorylate foxos at various sites to inhibit foxos activity
Publications: 1 Organism: Homo Sapiens
+ down-regulates img/direct_inhibition.png phosphorylation NOTCH1 0.403
Identifier Residue Sequence Organism Cell Line
SIGNOR-185494 Homo sapiens
pmid sentence
Dyrk1a physically interacts with the nicd inducing its phosphorylation in the ankyrin domain, thereby attenuating notch .
Publications: 1 Organism: Homo Sapiens
Tissue: Brain
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