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Dual specificity tyrosine-phosphorylation-regulated kinase 1A (EC 2.7.12.1) (Dual specificity YAK1-related kinase) (MP86) (Protein kinase minibrain homolog) (MNBH)

 DYR1A_MOUSE             Reviewed;         763 AA.
Q61214;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 167.
RecName: Full=Dual specificity tyrosine-phosphorylation-regulated kinase 1A;
EC=2.7.12.1 {ECO:0000269|PubMed:20167603};
AltName: Full=Dual specificity YAK1-related kinase;
AltName: Full=MP86;
AltName: Full=Protein kinase minibrain homolog;
Short=MNBH;
Name=Dyrk1a; Synonyms=Dyrk;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=Swiss Webster / NIH; TISSUE=Embryo;
PubMed=8975710; DOI=10.1006/geno.1996.0636;
Song W.J., Sternberg L.R., Kasten-Sportes C., van Keuren M.L.,
Chung S.H., Slack A.C., Miller D.E., Glover T.W., Chiang P.W., Lou L.,
Kurnit D.W.;
"Isolation of human and murine homologues of the Drosophila minibrain
gene: human homologue maps to 21q22.2 in the Down syndrome 'critical
region'.";
Genomics 38:331-339(1996).
[2]
SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=9070862; DOI=10.1006/bbrc.1997.6154;
Song W.J., Chung S.H., Kurnit D.M.;
"The murine Dyrk protein maps to chromosome 16, localizes to the
nucleus, and can form multimers.";
Biochem. Biophys. Res. Commun. 231:640-644(1997).
[3]
INTERACTION WITH RAD54L2.
PubMed=15199138; DOI=10.1128/MCB.24.13.5821-5834.2004;
Sitz J.H., Tigges M., Baumgaertel K., Khaspekov L.G., Lutz B.;
"Dyrk1A potentiates steroid hormone-induced transcription via the
chromatin remodeling factor Arip4.";
Mol. Cell. Biol. 24:5821-5834(2004).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-145, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538; SER-748 AND
SER-758, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
FUNCTION, INTERACTION WITH SIRT1, AND CATALYTIC ACTIVITY.
PubMed=20167603; DOI=10.1074/jbc.M110.102574;
Guo X., Williams J.G., Schug T.T., Li X.;
"DYRK1A and DYRK3 promote cell survival through phosphorylation and
activation of SIRT1.";
J. Biol. Chem. 285:13223-13232(2010).
[7]
FUNCTION, AND INTERACTION WITH CRY2.
PubMed=20123978; DOI=10.1128/MCB.01047-09;
Kurabayashi N., Hirota T., Sakai M., Sanada K., Fukada Y.;
"DYRK1A and glycogen synthase kinase 3beta, a dual-kinase mechanism
directing proteasomal degradation of CRY2 for circadian timekeeping.";
Mol. Cell. Biol. 30:1757-1768(2010).
[8]
TISSUE SPECIFICITY.
PubMed=22998443; DOI=10.1021/jm301034u;
Tahtouh T., Elkins J.M., Filippakopoulos P., Soundararajan M.,
Burgy G., Durieu E., Cochet C., Schmid R.S., Lo D.C., Delhommel F.,
Oberholzer A.E., Pearl L.H., Carreaux F., Bazureau J.P., Knapp S.,
Meijer L.;
"Selectivity, cocrystal structures, and neuroprotective properties of
leucettines, a family of protein kinase inhibitors derived from the
marine sponge alkaloid leucettamine B.";
J. Med. Chem. 55:9312-9330(2012).
-!- 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 (PubMed:20167603).
{ECO:0000250|UniProtKB:Q9NR20, ECO:0000269|PubMed:20123978,
ECO:0000269|PubMed:20167603}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:20167603}.
-!- ENZYME REGULATION: Inhibited by RANBP9.
{ECO:0000250|UniProtKB:Q13627}.
-!- SUBUNIT: Interacts with RANBP9 (By similarity). Interacts with
RAD54L2/ARIP4 (PubMed:15199138). Interacts with WDR68 (By
similarity). Interacts with CRY2 (PubMed:20123978). Interacts with
SIRT1 (PubMed:20167603). {ECO:0000250|UniProtKB:Q13627,
ECO:0000269|PubMed:15199138, ECO:0000269|PubMed:20123978,
ECO:0000269|PubMed:20167603, ECO:0000269|PubMed:9070862}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-80344, EBI-80344;
P53805-2:RCAN1 (xeno); NbExp=5; IntAct=EBI-80344, EBI-1541912;
Q9JHG6:Rcan1; NbExp=2; IntAct=EBI-80344, EBI-644061;
Q923E4:Sirt1; NbExp=4; IntAct=EBI-80344, EBI-1802585;
-!- SUBCELLULAR LOCATION: Nucleus speckle
{ECO:0000269|PubMed:9070862}.
-!- TISSUE SPECIFICITY: Detected in brain (at protein level).
Expressed in a variety of embryonic and adult tissues. Expressed
abundantly in neurons of the brain, spinal cord, and retina in
developing embryos. {ECO:0000269|PubMed:22998443,
ECO:0000269|PubMed:8975710}.
-!- DOMAIN: The polyhistidine repeats act as targeting signals to
nuclear speckles. {ECO:0000250|UniProtKB:Q13627}.
-!- PTM: Autophosphorylated on numerous tyrosine residues. Can also
autophosphorylate on serine and threonine residues (in vitro) (By
similarity). {ECO:0000250|UniProtKB:Q13627}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. MNB/DYRK subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U58497; AAC52994.1; -; mRNA.
CCDS; CCDS28350.1; -.
RefSeq; NP_001106860.1; NM_001113389.1.
RefSeq; NP_031916.1; NM_007890.2.
RefSeq; XP_011244396.1; XM_011246094.2.
RefSeq; XP_011244397.1; XM_011246095.2.
UniGene; Mm.310973; -.
ProteinModelPortal; Q61214; -.
SMR; Q61214; -.
BioGrid; 199347; 3.
ELM; Q61214; -.
IntAct; Q61214; 4.
MINT; MINT-1205474; -.
STRING; 10090.ENSMUSP00000023614; -.
BindingDB; Q61214; -.
ChEMBL; CHEMBL4750; -.
iPTMnet; Q61214; -.
PhosphoSitePlus; Q61214; -.
EPD; Q61214; -.
MaxQB; Q61214; -.
PaxDb; Q61214; -.
PRIDE; Q61214; -.
Ensembl; ENSMUST00000023614; ENSMUSP00000023614; ENSMUSG00000022897.
Ensembl; ENSMUST00000119878; ENSMUSP00000113660; ENSMUSG00000022897.
GeneID; 13548; -.
KEGG; mmu:13548; -.
UCSC; uc008abg.2; mouse.
CTD; 1859; -.
MGI; MGI:1330299; Dyrk1a.
eggNOG; KOG0667; Eukaryota.
eggNOG; ENOG410XPET; LUCA.
GeneTree; ENSGT00760000119032; -.
HOGENOM; HOG000220863; -.
HOVERGEN; HBG051425; -.
InParanoid; Q61214; -.
KO; K08825; -.
OMA; RQGIDRE; -.
OrthoDB; EOG091G03J7; -.
PhylomeDB; Q61214; -.
TreeFam; TF314624; -.
BRENDA; 2.7.12.1; 3474.
Reactome; R-MMU-1538133; G0 and Early G1.
PRO; PR:Q61214; -.
Proteomes; UP000000589; Chromosome 16.
Bgee; ENSMUSG00000022897; -.
ExpressionAtlas; Q61214; baseline and differential.
Genevisible; Q61214; MM.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:MGI.
GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; ISO:MGI.
GO; GO:0043621; F:protein self-association; IPI:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0048156; F:tau protein binding; IPI:BHF-UCL.
GO; GO:0007623; P:circadian rhythm; IMP:UniProtKB.
GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IDA:BHF-UCL.
GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IMP:MGI.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:BHF-UCL.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
GO; GO:0090312; P:positive regulation of protein deacetylation; IDA:BHF-UCL.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IEA:Ensembl.
InterPro; IPR028318; DYRK1A/MNB.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR24058:SF28; PTHR24058:SF28; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Kinase; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
Transferase; Tyrosine-protein kinase.
CHAIN 1 763 Dual specificity tyrosine-
phosphorylation-regulated kinase 1A.
/FTId=PRO_0000085932.
DOMAIN 159 479 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 165 173 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 238 241 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 117 134 Bipartite nuclear localization signal.
{ECO:0000255}.
COMPBIAS 509 515 Poly-Ser.
COMPBIAS 599 602 Poly-His.
COMPBIAS 607 619 Poly-His.
COMPBIAS 656 672 Ser/Thr-rich.
COMPBIAS 664 671 Poly-Ser.
ACT_SITE 287 287 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 188 188 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 14 14 Phosphoserine.
{ECO:0000250|UniProtKB:Q13627}.
MOD_RES 111 111 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:Q13627}.
MOD_RES 140 140 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:Q13627}.
MOD_RES 145 145 Phosphotyrosine.
{ECO:0000244|PubMed:18034455}.
MOD_RES 159 159 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:Q13627}.
MOD_RES 177 177 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:Q13627}.
MOD_RES 219 219 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:Q63470}.
MOD_RES 310 310 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:Q13627}.
MOD_RES 319 319 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:Q13627}.
MOD_RES 321 321 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:Q13627}.
MOD_RES 402 402 Phosphothreonine; by autocatalysis.
{ECO:0000250|UniProtKB:Q13627}.
MOD_RES 449 449 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:Q13627}.
MOD_RES 529 529 Phosphoserine.
{ECO:0000250|UniProtKB:Q13627}.
MOD_RES 538 538 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 748 748 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 758 758 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
SEQUENCE 763 AA; 85494 MW; E117DDD6C5E8C74F CRC64;
MHTGGETSAC KPSSVRLAPS FSFHAAGLQM AAQMPHSHQY SDRRQPSISD QQVSALPYSD
QIQQPLTNQV MPDIVMLQRR MPQTFRDPAT APLRKLSVDL IKTYKHINEV YYAKKKRRHQ
QGQGDDSSHK KERKVYNDGY DDDNYDYIVK NGEKWMDRYE IDSLIGKGSF GQVVKAYDRV
EQEWVAIKII KNKKAFLNQA QIEVRLLELM NKHDTEMKYY IVHLKRHFMF RNHLCLVFEM
LSYNLYDLLR NTNFRGVSLN LTRKFAQQMC TALLFLATPE LSIIHCDLKP ENILLCNPKR
SAIKIVDFGS SCQLGQRIYQ YIQSRFYRSP EVLLGMPYDL AIDMWSLGCI LVEMHTGEPL
FSGANEVDQM NKIVEVLGIP PAHILDQAPK ARKFFEKLPD GTWSLKKTKD GKREYKPPGT
RKLHNILGVE TGGPGGRRAG ESGHTVADYL KFKDLILRML DYDPKTRIQP YYALQHSFFK
KTADEGTNTS NSVSTSPAME QSQSSGTTSS TSSSSGGSSG TSNSGRARSD PTHQHRHSGG
HFAAAVQAMD CETHSPQVRQ QFPAPLGWSG TEAPTQVTVE THPVQETTFH VAPQQNALHH
HHGNSSHHHH HHHHHHHHHG QQALGNRTRP RVYNSPTNSS STQDSMEVGH SHHSMTSLSS
STTSSSTSSS STGNQGNQAY QNRPVAANTL DFGQNGAMDV NLTVYSNPRQ ETGIAGHPTY
QFSANTGPAH YMTEGHLAMR QGADREESPM TGVCVQQSPV ASS


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