DYRK2_DICDI
ID DYRK2_DICDI Reviewed; 915 AA.
AC Q54BC9;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Probable serine/threonine-protein kinase dyrk2;
DE EC=2.7.12.1;
DE AltName: Full=Dual specificity tyrosine-phosphorylation-regulated kinase 2;
GN Name=dyrk2; ORFNames=DDB_G0293750;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 -!- 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; AAFI02000219; EAL60552.1; -; Genomic_DNA.
DR RefSeq; XP_628965.1; XM_628963.1.
DR AlphaFoldDB; Q54BC9; -.
DR SMR; Q54BC9; -.
DR STRING; 44689.DDB0230102; -.
DR PaxDb; Q54BC9; -.
DR PRIDE; Q54BC9; -.
DR EnsemblProtists; EAL60552; EAL60552; DDB_G0293750.
DR GeneID; 8629393; -.
DR KEGG; ddi:DDB_G0293750; -.
DR dictyBase; DDB_G0293750; dyrk2.
DR eggNOG; KOG0667; Eukaryota.
DR HOGENOM; CLU_318182_0_0_1; -.
DR InParanoid; Q54BC9; -.
DR OMA; TMAEQSE; -.
DR Reactome; R-DDI-6804756; Regulation of TP53 Activity through Phosphorylation.
DR PRO; PR:Q54BC9; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; ISS:dictyBase.
DR GO; GO:0005856; C:cytoskeleton; 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:RHEA.
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; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..915
FT /note="Probable serine/threonine-protein kinase dyrk2"
FT /id="PRO_0000362010"
FT DOMAIN 605..902
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 51..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 731
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 611..619
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 634
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 915 AA; 98276 MW; A7BFF787F80278D6 CRC64;
MTSLHKQIIE SHNNDITKLK SSMSTRAAAR RSVCLSSMSY TLGADDVTPI TSNTTPSNNN
NNNNTTTTIT TTTTTPTISP LKQSTTGSII PKSILVTKSG SKEEPIVSSS KSSSNSSSIN
NNFNNLYSAS TFSSSTKKVH ERPSINPGFR KPREALLSGN SDSGIIKKPS SSSTSSSSSS
SSTTSNIKAP IQISHSSNSG SSSSGGNNNN SDDNSGSSTI KHTAASLSKM KLSPSHTISD
SPRSSTMKSR SVSISNGSLF SPTNTSVNNS NNNTSSNIKT PTKSSISENL DQNTPPPPSS
SSTTKTPTAT TTTTTTTTSS SSSTSTNTTP SKSSVDDVFA RLANVSKPAI KSRSLSVSAS
LARVEQSPPT KDKGDKESSS SSSSSSSSFS SKFTKILRSS SKTPTPTSSN TTVQPSTTSL
SASKISSRKD TKSLSSFSTT TTTTTLKSSS SSSSSSSSSS KSNIASSSSS SSNNLTNLLT
QSQSISSTST STTTTPTSTS PTLASSMSVL SSPTSTTTTS TSTTSTTTTP TKSSCTIITP
SIALKLYIND LTSAEQSEIL DYPQIYFTGN TNKKTKFNSQ LPNNGYDNDI GEYKVVERDH
IAYRFEIVSI LGQGSFCQVV KGYDYKTGEM VALKILRNQK RFHNQALTEI KILEYLKTND
PNSTASIVHL NNYFYFRNHL ILTFELLSMN LYDFLKVNHF QGYNLNLVRR FGAQILTSLR
FLSKRNIIHA DLKPENILLK SPTKSGIKLI DFGSSCFENE QIFTYIQSRF YRSPEVILGT
KYDKSIDIWS LGCILVEIFT GVPLFPGSDE PEQLACIMEV LGAPPKSVID NSTRKDIFFE
DDGTPKPVKN STTGELYTIG TKSFKDSIRS GDEDFDNFIL DCLKWEPSQR ITAEQGLKHD
WIIKVIAPTA PSTPS
