DYRK2_CHICK
ID DYRK2_CHICK Reviewed; 526 AA.
AC Q5ZIU3;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Dual specificity tyrosine-phosphorylation-regulated kinase 2;
DE EC=2.7.12.1 {ECO:0000250|UniProtKB:Q92630};
GN Name=DYRK2 {ECO:0000250|UniProtKB:Q92630}; ORFNames=RCJMB04_23i19;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1] {ECO:0000312|EMBL:CAG32350.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB {ECO:0000312|EMBL:CAG32350.1};
RC TISSUE=Bursa of Fabricius {ECO:0000312|EMBL:CAG32350.1};
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in the control of
CC mitotic transition and the regulation of cellular growth and/or
CC development. {ECO:0000250}.
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:0000250|UniProtKB:Q92630};
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:0000250|UniProtKB:Q92630};
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:0000250|UniProtKB:Q92630};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q92630};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q92630};
CC -!- ACTIVITY REGULATION: Autophosphorylates on tyrosine residues.
CC {ECO:0000250|UniProtKB:Q92630}.
CC -!- SUBUNIT: Interacts with MDM2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92630}. Nucleus
CC {ECO:0000250|UniProtKB:Q92630}.
CC -!- PTM: Phosphorylated on serine/threonine residues. Phosphorylation on
CC Thr-31 and Ser-367 by ATM in response to genotoxic stress disrupts MDM2
CC binding and prevents MDM2-mediated ubiquitination and subsequent
CC proteasome degradation, thus promoting p53/TP53-mediated apoptosis (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitination in nucleus by MDM2 in normal conditions leads to
CC proteasome degradation. {ECO:0000250}.
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; AJ720691; CAG32350.1; -; mRNA.
DR RefSeq; NP_001026651.1; NM_001031480.1.
DR RefSeq; XP_015137471.1; XM_015281985.1.
DR RefSeq; XP_015137476.1; XM_015281990.1.
DR AlphaFoldDB; Q5ZIU3; -.
DR SMR; Q5ZIU3; -.
DR STRING; 9031.ENSGALP00000016084; -.
DR PaxDb; Q5ZIU3; -.
DR Ensembl; ENSGALT00000016103; ENSGALP00000016084; ENSGALG00000009901.
DR GeneID; 427864; -.
DR KEGG; gga:427864; -.
DR CTD; 8445; -.
DR VEuPathDB; HostDB:geneid_427864; -.
DR eggNOG; KOG0667; Eukaryota.
DR GeneTree; ENSGT00940000158113; -.
DR HOGENOM; CLU_000288_5_13_1; -.
DR InParanoid; Q5ZIU3; -.
DR OrthoDB; 870358at2759; -.
DR PhylomeDB; Q5ZIU3; -.
DR TreeFam; TF314624; -.
DR Reactome; R-GGA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR PRO; PR:Q5ZIU3; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000009901; Expressed in skeletal muscle tissue and 12 other tissues.
DR ExpressionAtlas; Q5ZIU3; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
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:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR Gene3D; 3.30.10.30; -; 1.
DR InterPro; IPR042521; DYRK.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
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 Apoptosis; ATP-binding; Cytoplasm; Kinase; Magnesium; Manganese;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase;
KW Ubl conjugation.
FT CHAIN 1..526
FT /note="Dual specificity tyrosine-phosphorylation-regulated
FT kinase 2"
FT /id="PRO_0000291266"
FT DOMAIN 147..460
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 30..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 114..116
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 30..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 273
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 153..161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 226..229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 31
FT /note="Phosphothreonine; by ATM"
FT /evidence="ECO:0000250"
FT MOD_RES 307
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 367
FT /note="Phosphoserine; by ATM"
FT /evidence="ECO:0000250"
SQ SEQUENCE 526 AA; 59437 MW; E294B808874225A2 CRC64;
MNEHLHVGSH GQIQVQQLFE DNSNKRTVLT TQPNGLTTLG KSGLPVVQDR QSESAHRRQG
SSSSLKSTDG TGKVKASVMT PEQAMKQYMQ KLTTFEHNEI FGYTEIYFLG PNAKKRQGVI
GGPNNCGYDD DQGSYIQVPH DHIAYRYEVL KVIGKGSFGQ VVKAYDHKMH QHVALKMVRN
EKRFHRQAAE EIRILEHLRK QDKDNNMNVI HMLENFTFRS HICMTFELLS MNLYELIKKN
KFQGFSLPLV RKFAHSILQC LDALHKNRII HCDLKPENIL LKQQGRSGIK VIDFGSSCYE
HQRVYTYIQS RFYRAPEVIL GARYGMPIDM WSLGCILAEL LTGYPLLPGE DEGDQLACMI
ELLGMPSPKL LDSSKRAKNF VSSKGYPRYC TITTLSDGSI ILNGGRSRRG KLRGPPESRE
WGNALKGCDD PLFLDFLKQC LEWDPAIRMT PSQALRHPWL RRRLPKPPTG EKASAKRITE
STGAITSISK LPPTSSSASK LRTNLAQMTD ANGNIQQRTV LPKLVS
