Relation Results

Identifier	Residue	Sequence	Organism
SIGNOR-278250	Ser10	NVRVSNGsPSLERMD	Homo sapiens
pmid	sentence
24806449	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

Identifier	Residue	Sequence	Organism
SIGNOR-279327	Ser1048	NRTHSLKsPRYLPEE	Homo sapiens
pmid	sentence
25368549	DYRK1A enhances the surface expression of GluN1 and GluN2A receptors.\|Mechanistically, the DYRK1A-dependent phosphorylation of GluN2A at Ser 1048 hinders the internalization of GluN1/GluN2A, causing an increase of surface GluN1/GluN2A in heterologous systems, as well as in primary cortical neurons.

Publications:

1

Organism:

Homo Sapiens

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

Identifier	Residue	Sequence	Organism
SIGNOR-279704	Ser159	NNTSTDGsLPSTPPP	Homo sapiens
pmid	sentence
32587776	Furthermore, DYRK1A likely directly bound and phosphorylated Mcl-1, thereby enhancing Mcl-1 protein stability and contributing to the development of acquired resistance to Bcl-2 inhibitors.\|DYRK1A upregulates Mcl-1 expression in NSCLC cells.\|We demonstrated that DYRK1A suppression by siRNA or harmine decreased the phosphorylation of Mcl-1 at Ser159/Thr163.

Identifier	Residue	Sequence	Organism
SIGNOR-279703	Thr163	TDGSLPStPPPAEEE	Homo sapiens
pmid	sentence
32587776	Furthermore, DYRK1A likely directly bound and phosphorylated Mcl-1, thereby enhancing Mcl-1 protein stability and contributing to the development of acquired resistance to Bcl-2 inhibitors.\|DYRK1A upregulates Mcl-1 expression in NSCLC cells.\|We demonstrated that DYRK1A suppression by siRNA or harmine decreased the phosphorylation of Mcl-1 at Ser159/Thr163.

Publications:

2

Organism:

Homo Sapiens

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
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

Identifier	Residue	Sequence	Organism
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

Identifier	Residue	Sequence	Organism
SIGNOR-277565	Ser251	NKVIPAKsPPPPTHS	in vitro
pmid	sentence
34109727	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
34109727	DYRK1A phosphorylates MEF2D and decreases its transcriptional activity

Publications:

2

Organism:

In Vitro, Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-277108	Ser258	NTNFRGVsLNLTRKF	Homo sapiens
pmid	sentence
33380426	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

Identifier	Residue	Sequence	Organism
SIGNOR-278279	Ser261	ARSSRPAsPCNKRKY	Homo sapiens
pmid	sentence
28235034	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
SIGNOR-278278	Ser278	NGRQPPYsPHHSPTP	Homo sapiens
pmid	sentence
28235034	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
SIGNOR-278277	Ser403	WAKPKPLsPTSYMSP	Homo sapiens
pmid	sentence
28235034	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
SIGNOR-278276	Ser409	LSPTSYMsPTLPALD	Homo sapiens
pmid	sentence
28235034	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

Identifier	Residue	Sequence	Organism
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
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
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
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
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
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

Identifier	Residue	Sequence	Organism
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.

Publications:

7

Organism:

Homo Sapiens

Tissue:

Brain

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262846	Ser28	FEKLDRAsPDLWPEQ	Homo sapiens	T-98G Cell
pmid	sentence
21498570	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

Identifier	Residue	Sequence	Organism
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.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-279520	Ser312	TESITATsPASMVGG	Homo sapiens
pmid	sentence
31723029	DYRK1A interacts with IRS-1 and phosphorylates IRS-1 at Ser-312 and Ser-616.\|We found that DYRK1A overexpression up-regulated IRS-1 expression by slowing the turnover of IRS-1 protein.

Identifier	Residue	Sequence	Organism
SIGNOR-279521	Ser616	DDGYMPMsPGVAPVP	Homo sapiens
pmid	sentence
31723029	DYRK1A interacts with IRS-1 and phosphorylates IRS-1 at Ser-312 and Ser-616.\|We found that DYRK1A overexpression up-regulated IRS-1 expression by slowing the turnover of IRS-1 protein.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
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

Identifier	Residue	Sequence	Organism
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
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

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

Identifier	Residue	Sequence	Organism
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

Identifier	Residue	Sequence	Organism
SIGNOR-183674	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

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	Organism
SIGNOR-252905		Homo sapiens
pmid	sentence
19188143	Additionally, ck1, dyrk1a, and cdk2 also phosphorylate foxos at various sites to inhibit foxos activity

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277791	Ser358	VPDFHLSsPAKNFFK	Homo sapiens	HEK-293 Cell
pmid	sentence
37387444	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
37387444	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

Identifier	Residue	Sequence	Organism
SIGNOR-278930	Ser408	GPLPRAPsISTVEPK	Homo sapiens
pmid	sentence
28735864	Here, we have used an in vitro kinase assay and phospho-peptide mass spectrometry analysis to identify site(s) of direct phosphorylation of GLI1 by DYRK1A and have determined that DYRK1A phosphorylates GLI1 at Ser408 within its nuclear localization sequence.\|The kinase DYRK1A (dual-specificity tyrosine phosphorylation regulated kinase 1a) has been shown to activate GLI1 via a phosphorylation event, leading to the translocation of GLI1 from the cytoplasm to the nucleus .

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
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
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
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

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

Identifier	Residue	Sequence	Organism
SIGNOR-279609	Ser62	S-->E	Homo sapiens
pmid	sentence
24901999	We also found that DYRK1A phosphorylated c-Myc on Ser62, priming phosphorylation on Thr58 by GSK3\u03b2 and subsequent degradation.\|c-Myc expression is down-regulated by DYRK1A.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-260632	Ser641	YRYPRPAsVPPSPSL	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
14593110	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

Identifier	Residue	Sequence	Organism
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
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

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

Identifier	Residue	Sequence	Organism
SIGNOR-279326	Thr125	PEVLRPEtPRPVDIG	Homo sapiens
pmid	sentence
19016842	Depletion of DYRK1A from human cells by short interfering RNA inhibits the basal phosphorylation of caspase 9 at an inhibitory site, Thr125. DYRK1A-dependent phosphorylation of Thr125 is also blocked by harmine, confirming the use of this beta-carboline alkaloid as a potent inhibitor of DYRK1A in cells.\|When co-expressed in cells, DYRK1A interacts with caspase 9, strongly induces Thr125 phosphorylation and inhibits caspase 9 auto-processing.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
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

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

Identifier	Residue	Sequence	Organism
SIGNOR-278473	Thr530	YLSELPPtPLHVSED	Homo sapiens
pmid	sentence
20167603	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

Identifier	Residue	Sequence	Organism
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

Identifier	Residue	Sequence	Organism
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
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

Identifier	Residue	Organism
SIGNOR-279366		Homo sapiens
pmid	sentence
22110360	Moreover, Dyrk1A appears to directly phosphorylate the C-terminal domain of ASK1.\|The current finding that Dyrk1A enhances the activities of ASK1 and JNK1, it could act as a pro-apoptotic player.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-260630		Chlorocebus aethiops	COS-7 Cell
pmid	sentence
14593110	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

Identifier	Residue	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

Identifier	Residue	Organism
SIGNOR-90809		Homo sapiens
pmid	sentence
12138125	Dyrk1 phosphorylates gli1 on more than one domain.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-279166		Homo sapiens
pmid	sentence
27049307	These results suggest that Dyrk1A enhances SRp55 promoted cTnT exon 5 inclusion.\|These results supported the finding that phosphorylation of SRp55 by Dyrk1A promotes cTnT exon 5 inclusion.Alternative splicing of cTnT exon 5 is regulated developmentally.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	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

Identifier	Residue	Organism
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

Identifier	Residue	Organism
SIGNOR-278307		Homo sapiens
pmid	sentence
21470964	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

Identifier	Residue	Organism
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

Identifier	Residue	Organism
SIGNOR-279032		Homo sapiens
pmid	sentence
22514676	The phosphorylation of MAP1A and MAP2 by Dyrk1A was further confirmed by immunoprecipitating these proteins from the soluble fraction obtained after phosphorylating MTs (XREF_FIG).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-183680		Homo sapiens
pmid	sentence
19188143	Additionally, ck1, dyrk1a, and cdk2 also phosphorylate foxos at various sites to inhibit foxos activity

Publications:

1

Organism:

Homo Sapiens

Name	DYRK1A View Modifications
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	67
Function	Dual-specificity kinase which possesses both serine/threonine and tyrosine kinase activities. May play a role in a signaling pathway regulating nuclear functions of cell proliferation. Modulates alternative splicing by phosphorylating the splice factor SRSF6 (By similarity). Exhibits a substrate preference for proline at position P+1 and arginine at position P-3. Has pro-survival function and negatively regulates the apoptotic process. Promotes cell survival upon genotoxic stress through phosphorylation of SIRT1. This in turn inhibits TP53 activity and apoptosis (By similarity).

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