DYRK2_DROME
ID DYRK2_DROME Reviewed; 722 AA.
AC Q9V3D5; A4V0P7; Q8T0L9;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Dual specificity tyrosine-phosphorylation-regulated kinase 2;
DE EC=2.7.12.1 {ECO:0000269|PubMed:12786602};
DE AltName: Full=Protein smell impaired at 35A;
DE AltName: Full=dDyrk2;
GN Name=Dyrk2 {ECO:0000312|FlyBase:FBgn0016930};
GN Synonyms=smi35A {ECO:0000312|FlyBase:FBgn0016930};
GN ORFNames=CG4551 {ECO:0000312|FlyBase:FBgn0016930};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|EMBL:AAQ22557.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, COFACTOR, ACTIVITY REGULATION,
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, PHOSPHORYLATION AT TYR-356 AND
RP TYR-358, AND MUTAGENESIS OF TYR-356 AND TYR-358.
RC STRAIN=Oregon-R {ECO:0000269|PubMed:12786602};
RC TISSUE=Embryo {ECO:0000269|PubMed:12786602};
RX PubMed=12786602; DOI=10.1042/bj20030500;
RA Lochhead P.A., Sibbet G., Kinstrie R., Cleghon T., Rylatt M.,
RA Morrison D.K., Cleghon V.;
RT "dDYRK2: a novel dual-specificity tyrosine-phosphorylation-regulated kinase
RT in Drosophila.";
RL Biochem. J. 374:381-391(2003).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10471707};
RX PubMed=10471707; DOI=10.1093/genetics/153.1.179;
RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T.,
RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A.,
RA Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R.,
RA Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K.,
RA Celniker S.E., Rubin G.M.;
RT "An exploration of the sequence of a 2.9-Mb region of the genome of
RT Drosophila melanogaster: the Adh region.";
RL Genetics 153:179-219(1999).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000305}; TISSUE=Embryo {ECO:0000305};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D.E., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 381-722.
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: In vitro; can phosphorylate exogenous substrates on Ser and
CC Thr residues. May have a physiological role in development being
CC involved in cellular growth and differentiation.
CC {ECO:0000269|PubMed:12786602}.
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:0000269|PubMed:12786602};
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:0000269|PubMed:12786602};
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:0000269|PubMed:12786602};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12786602};
CC -!- ACTIVITY REGULATION: Autophosphorylates on Tyr-356 and Tyr-358.
CC {ECO:0000269|PubMed:12786602}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12786602}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed and active during embryogenesis
CC and pupation and at lower levels in larva and adult.
CC {ECO:0000269|PubMed:12786602}.
CC -!- PTM: Phosphorylated on serine/threonine residues.
CC {ECO:0000269|PubMed:12786602, ECO:0000269|PubMed:18327897}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MNB/DYRK subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL39328.1; Type=Miscellaneous discrepancy; Note=Deletion within an exon that does not correspond to an intron.; Evidence={ECO:0000305};
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DR EMBL; AF168467; AAD47290.1; -; mRNA.
DR EMBL; AE014134; AAF53380.1; -; Genomic_DNA.
DR EMBL; AE014134; AAS64705.1; -; Genomic_DNA.
DR EMBL; AE014134; AAS64706.1; -; Genomic_DNA.
DR EMBL; AE014134; ABC65900.1; -; Genomic_DNA.
DR EMBL; AE014134; ABC65901.1; -; Genomic_DNA.
DR EMBL; BT010088; AAQ22557.1; -; mRNA.
DR EMBL; AY069183; AAL39328.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001033906.1; NM_001038817.1.
DR RefSeq; NP_001033907.1; NM_001038818.1.
DR RefSeq; NP_523564.1; NM_078840.5.
DR RefSeq; NP_995710.1; NM_205988.3.
DR RefSeq; NP_995711.1; NM_205989.3.
DR AlphaFoldDB; Q9V3D5; -.
DR SMR; Q9V3D5; -.
DR BioGRID; 60857; 3.
DR IntAct; Q9V3D5; 14.
DR STRING; 7227.FBpp0088344; -.
DR iPTMnet; Q9V3D5; -.
DR PaxDb; Q9V3D5; -.
DR DNASU; 34831; -.
DR EnsemblMetazoa; FBtr0089288; FBpp0088344; FBgn0016930.
DR EnsemblMetazoa; FBtr0089289; FBpp0089218; FBgn0016930.
DR EnsemblMetazoa; FBtr0089290; FBpp0089219; FBgn0016930.
DR EnsemblMetazoa; FBtr0100447; FBpp0099869; FBgn0016930.
DR EnsemblMetazoa; FBtr0100448; FBpp0099870; FBgn0016930.
DR GeneID; 34831; -.
DR KEGG; dme:Dmel_CG4551; -.
DR CTD; 8445; -.
DR FlyBase; FBgn0016930; Dyrk2.
DR VEuPathDB; VectorBase:FBgn0016930; -.
DR eggNOG; KOG0667; Eukaryota.
DR GeneTree; ENSGT00940000159401; -.
DR HOGENOM; CLU_000288_5_13_1; -.
DR InParanoid; Q9V3D5; -.
DR OMA; SSCYNFA; -.
DR OrthoDB; 870358at2759; -.
DR PhylomeDB; Q9V3D5; -.
DR SignaLink; Q9V3D5; -.
DR BioGRID-ORCS; 34831; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Dyrk2; fly.
DR GenomeRNAi; 34831; -.
DR PRO; PR:Q9V3D5; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0016930; Expressed in brain and 48 other tissues.
DR ExpressionAtlas; Q9V3D5; baseline and differential.
DR Genevisible; Q9V3D5; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0042048; P:olfactory behavior; IMP:FlyBase.
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:0030177; P:positive regulation of Wnt signaling pathway; IMP:FlyBase.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IMP:FlyBase.
DR GO; GO:0007608; P:sensory perception of smell; IMP:FlyBase.
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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Magnesium; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Tyrosine-protein kinase.
FT CHAIN 1..722
FT /note="Dual specificity tyrosine-phosphorylation-regulated
FT kinase 2"
FT /id="PRO_0000085937"
FT DOMAIN 198..494
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000305"
FT REGION 54..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 324
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q92630,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 204..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92630,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92630,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 356
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:12786602"
FT MOD_RES 358
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:12786602"
FT MUTAGEN 356
FT /note="Y->D,F: Blocks tyrosine phosphorylation."
FT /evidence="ECO:0000269|PubMed:12786602"
FT MUTAGEN 358
FT /note="Y->D,F: Blocks tyrosine phosphorylation."
FT /evidence="ECO:0000269|PubMed:12786602"
SQ SEQUENCE 722 AA; 79609 MW; E431C03DDFE81F4E CRC64;
MLDRCEMPIQ LDNEKLRRDV RLSGSRLDLP QLCNGSRRLD GHNNHVAANE NTVTTTSLNG
NGNGNGNSNS NNNNNIGSPV SSSTTNSSNG GNERGSSTKS NSSSGSGSSG NSASSTGSGE
LKCNTPMTPS ELVKKFRNYL TDLEFEELKV YKEVWYFGQH ASKNYNKPAP TANTTNLGYD
DDNGNYKIIE HDHIAFRYEI LEVIGKGSFG QVIRALDHKT NTHVAIKIIR NKKRFLNQAV
VELNILDELR EKDADGSHNV IHMLDYTYFR KHLCITFELM SLNLYELIKK NNYNGFSMSL
IRRFCNSIVK CLRLLYKENI IHCDLKPENI LLKQRGSSSI KVIDFGSSCY VDRKIYTYIQ
SRFYRSPEVI LGLQYGTAID MWSLGCILAE LYTGFPLFPG ENEVEQLACI MEVLGLPPKV
LISVARRRRL FFDSRDAPRC ITNTKGRKRS PGSKSLAHIL HCQDRYFIDF LQRCLEWDPA
ERMTPDEAAH HEFLQPSASS RHRSCRMSSS SSSSGLNSVS QKSSCYSFSE ISPGTNGPVV
ASITSTTAVH NAAIATTTKS RQQPPSQSHG HAQSNGHLPD IKLSASDKYN SMQKVAVRSK
ITSSVSDLES VQQYSLHRIY GGVGSGSTHH VSSAATRKHL PGTGSGIVGA MSSKYGSSTL
AHNHHNVTHH NASTATIATT THHHHHHGGQ QQQQSSSGAS TMAMSHSQST GDVSDRAIFG
RA
