DYR1A_XENLA
ID DYR1A_XENLA Reviewed; 750 AA.
AC Q2TAE3;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Dual specificity tyrosine-phosphorylation-regulated kinase 1A;
DE EC=2.7.12.1;
DE AltName: Full=Protein kinase minibrain homolog;
GN Name=dyrk1a {ECO:0000250|UniProtKB:Q13627};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000312|EMBL:AAI10969.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAI10969.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP INDUCTION.
RX PubMed=16720323; DOI=10.2741/1979;
RA Qu Y., Adler V., Chu T., Platica O., Michl J., Pestka S., Izotova L.,
RA Boutjdir M., Pincus M.R.;
RT "Two dual specificity kinases are preferentially induced by wild-type
RT rather than by oncogenic RAS-P21 in Xenopus oocytes.";
RL Front. Biosci. 11:2420-2427(2006).
CC -!- FUNCTION: May play a role in a signaling pathway regulating nuclear
CC functions of cell proliferation. Phosphorylates serine, threonine and
CC tyrosine residues in its sequence and in exogenous substrates (By
CC similarity). {ECO:0000250|UniProtKB:Q13627}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.12.1; Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}.
CC -!- INDUCTION: By insulin. {ECO:0000269|PubMed:16720323}.
CC -!- DOMAIN: The polyhistidine repeats act as targeting signals to nuclear
CC speckles. {ECO:0000250}.
CC -!- PTM: Autophosphorylated on tyrosine residues.
CC {ECO:0000250|UniProtKB:Q13627}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MNB/DYRK subfamily. {ECO:0000305}.
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DR EMBL; BC110968; AAI10969.1; -; mRNA.
DR RefSeq; NP_001156669.1; NM_001163197.1.
DR AlphaFoldDB; Q2TAE3; -.
DR SMR; Q2TAE3; -.
DR DNASU; 446302; -.
DR GeneID; 446302; -.
DR KEGG; xla:446302; -.
DR CTD; 446302; -.
DR Xenbase; XB-GENE-1017110; dyrk1a.S.
DR OrthoDB; 689446at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 446302; Expressed in muscle tissue and 19 other tissues.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR CDD; cd14226; PKc_DYRK1; 1.
DR InterPro; IPR028318; DYRK1A/B_MNB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR044131; PKc_DYR1A/1B.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24058:SF121; PTHR24058:SF121; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..750
FT /note="Dual specificity tyrosine-phosphorylation-regulated
FT kinase 1A"
FT /id="PRO_0000284707"
FT DOMAIN 151..471
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 56..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 109..126
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 56..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..612
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 279
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 157..165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 230..233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 750 AA; 84157 MW; 2A14AA063E7EBC0E CRC64;
MHTGGETSAC KPSSVRLAPS FSFHAAGLQM AGQMSHSHQQ YSDRHQQNLN DQQASALPYN
DQTPQPLPNQ RRMPQTFRDP ATAPLRKLSV DLIKTYKHIN EVYYAKKKRR HQQGQGDDSS
HKKERKVYND GYDDDNYDYI VKNGEKWMDR YEIDSLIGKG SFGQVVKAYD RVEQEWVAIK
IIKNKKAFLN QAQIEVRLLE LMNKHDTEMK YYIVHLKRHF MFRNHLCLVF EMLSYNLYDL
LRNTNFRGVS LNLTRKFAQQ MCTALLFLAT PELSIIHCDL KPENILLCNP KRSAIKIVDF
GSSCQLGQRI YQYIQSRFYR SPEVLLGTPY DLAIDMWSLG CILVEMHTGE PLFSGANEVD
QMSKIVEVLG IPPAHILDQA PKARKFFEKM PEGTWNLKKT KDGKKEYKPP GTRKLHNILG
VENGGPGGRR AGESGHTVAD YLKFKDVILR MLDYDAKTRI QPYYALQHSF FKKTADEGTN
TSNSVSTSPA MEQSQSSGTT SSTSSSSGGS SGTSNSGRAR SDPTHQHRHS GGHFTTAVAM
DCETHSPQVR QQFPPGWTVP EAPTQVTIET HPVQETTFHV PPSQKNVPHH HGNGSHHHHH
HHHHHHGQHI LSNRTRTRIY NSPSTSSSTQ DSMDIGNSHH SMTSLSSSTT SSSTSSSSTG
NQGNQAYQNR PVAANTLDFG QNGTLDVNLT VYSNPRQETG ITGHPDYQYS ANTGPGHYVT
EGQLTMRQGI DREDSPMTGV CVQQSPVASS
