DYRK3_DROME
ID DYRK3_DROME Reviewed; 828 AA.
AC P83102; A4V144; Q2PDL5; Q5LJP2; Q8MT39; Q9Y1N4;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2003, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Putative dual specificity tyrosine-phosphorylation-regulated kinase 3 homolog;
DE EC=2.7.12.1;
GN Name=Dyrk3; ORFNames=CG40478;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-290.
RA Wallrath L.L., Cryderman D.E., Morris E.J., Pavlova M., Biessmann H.,
RA Levis R.W., Elgin S.C.R.;
RT "Telomere swapping alters chromosomal properties.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, 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 -!- 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 -!- 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;
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 -!- PTM: Autophosphorylated on tyrosine residues. {ECO:0000250}.
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=AAD39356.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014135; ABC65837.1; -; Genomic_DNA.
DR EMBL; AE014135; ABC65839.1; -; Genomic_DNA.
DR EMBL; AE014135; ABC65840.1; -; Genomic_DNA.
DR EMBL; AE014135; ABC65841.1; -; Genomic_DNA.
DR EMBL; AY118401; AAM48430.1; -; mRNA.
DR EMBL; AF103941; AAD39356.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_001033810.1; NM_001038721.2.
DR RefSeq; NP_001033812.1; NM_001038723.2.
DR RefSeq; NP_001033814.1; NM_001038725.2.
DR AlphaFoldDB; P83102; -.
DR SMR; P83102; -.
DR ELM; P83102; -.
DR STRING; 7227.FBpp0099820; -.
DR iPTMnet; P83102; -.
DR PaxDb; P83102; -.
DR PRIDE; P83102; -.
DR DNASU; 3885567; -.
DR EnsemblMetazoa; FBtr0100402; FBpp0099816; FBgn0027101.
DR EnsemblMetazoa; FBtr0100404; FBpp0099818; FBgn0027101.
DR EnsemblMetazoa; FBtr0100406; FBpp0099820; FBgn0027101.
DR GeneID; 3885567; -.
DR KEGG; dme:Dmel_CG40478; -.
DR UCSC; CG40478-RA; d. melanogaster.
DR CTD; 8444; -.
DR FlyBase; FBgn0027101; Dyrk3.
DR VEuPathDB; VectorBase:FBgn0027101; -.
DR eggNOG; KOG0667; Eukaryota.
DR GeneTree; ENSGT00940000166363; -.
DR HOGENOM; CLU_000288_5_4_1; -.
DR InParanoid; P83102; -.
DR OMA; MILYMNK; -.
DR OrthoDB; 870358at2759; -.
DR PhylomeDB; P83102; -.
DR Reactome; R-DME-6804756; Regulation of TP53 Activity through Phosphorylation.
DR BioGRID-ORCS; 3885567; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 3885567; -.
DR PRO; PR:P83102; -.
DR Proteomes; UP000000803; Chromosome 4.
DR Bgee; FBgn0027101; Expressed in saliva-secreting gland and 27 other tissues.
DR Genevisible; P83102; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
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:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
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; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..828
FT /note="Putative dual specificity tyrosine-phosphorylation-
FT regulated kinase 3 homolog"
FT /id="PRO_0000085939"
FT DOMAIN 276..589
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 402
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 282..290
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 305
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 616
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 828 AA; 92740 MW; 9A4AFB31AE52F3E1 CRC64;
MVGSQEKKNN HIELSETPAT DKNNLNTTHL ENTQLSKALS PPTSLPQIQI QMINQNLTHT
GIAQNNTEKA NRHQYRDSGL QYLTRCFEPL AMLNDSKEDF PTQPSNNIAN YPGDIQILPI
FDCCEISESI QAISLPNVTS PSKTKDVPGL FLRTISENSK SKSEPECESL ISVKESSVME
NHTFLFHEQI IMSGQQKCEL HEKPKVLVVS PQQVMILYMN KLTPYERTEI LTYPQIYFIG
ANAKKRPGVY GPNNSEYDNE QGAYIHVPHD HVAYRYEMLK IIGKGSFGQV IKAYDHKTHE
HVALKIVRNE KRFHRQAQEE IRILHHLRRH DKYNTMNIIH MFDYFTFRNH TCITFELLSI
NLYELIKKNG FKGFSLQLVR KFAHSLLQCL DALYKNDIIH CDMKPENVLL KQQGRSGIKV
IDFGSSCFEN QRIYTYIQSR FYRAPEVILG GKYGRAIDMW SLGCILAELL SGHALFPGEN
ESDQLACIIE VLGMPNKNIL ASSKRSKSFF SPKGYPRYCT VRTMSDGMVV LIGGQSRRGK
QRGPPCSKSL SKALDGCKDP LFLNFIRGCL EWDADKRLTP SEALKHPWLR RRLPRPPSSS
SGCGGVSGLC SSRNESPVTG QNRNFAAETT ASSTSATSIS LTIKRENSHS SLRLHHGAVP
ETDFKLIKSV PEGSSTATKE PMMNSDILPE SFRQTTVVSP SKHSADSGGM SCLSAVDVGP
SRYYPYMNNN ENNRLFSSSL NSSANSLSHL EQATKLDALG EYSASTTPNL LSKNTGYSFN
SGSINIDVAQ ESLVNIASNY ALDKSIDIIG KSNVSLHTNK LKVQSKDM
