STY13_ARATH
ID STY13_ARATH Reviewed; 411 AA.
AC Q9ZQ31; Q94AI0;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Serine/threonine-protein kinase STY13 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000269|PubMed:16429265};
DE AltName: Full=AtSTYPK {ECO:0000303|PubMed:17291444};
DE AltName: Full=Serine/threonine/tyrosine-protein kinase 13 {ECO:0000303|PubMed:16429265};
GN Name=STY13 {ECO:0000303|PubMed:16429265};
GN OrderedLocusNames=At2g24360 {ECO:0000312|Araport:AT2G24360};
GN ORFNames=T28I24.9 {ECO:0000312|EMBL:AEC07566.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY,
RP AUTOPHOSPHORYLATION, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16429265; DOI=10.1007/s11103-005-4109-7;
RA Rudrabhatla P., Reddy M.M., Rajasekharan R.;
RT "Genome-wide analysis and experimentation of plant
RT serine/threonine/tyrosine-specific protein kinases.";
RL Plant Mol. Biol. 60:293-319(2006).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF SER-165; SER-181; SER-215; SER-259; SER-265;
RP SER-269; SER-315 AND SER-360.
RX PubMed=17291444; DOI=10.1016/j.abb.2007.01.003;
RA Reddy M.M., Rajasekharan R.;
RT "Serine/threonine/tyrosine protein kinase from Arabidopsis thaliana is
RT dependent on serine residues for its activity.";
RL Arch. Biochem. Biophys. 460:122-128(2007).
CC -!- FUNCTION: Serine/threonine protein kinase that phosphorylates proteins
CC on serine, threonine and tyrosine residues.
CC {ECO:0000269|PubMed:16429265}.
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=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:16429265};
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=2.7.11.1; Evidence={ECO:0000269|PubMed:16429265};
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:16429265}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AC006403; AAD18109.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC07566.1; -; Genomic_DNA.
DR EMBL; AY046026; AAK76700.1; -; mRNA.
DR EMBL; AY133876; AAM91810.1; -; mRNA.
DR PIR; G84635; G84635.
DR RefSeq; NP_565568.1; NM_127998.3.
DR AlphaFoldDB; Q9ZQ31; -.
DR SMR; Q9ZQ31; -.
DR STRING; 3702.AT2G24360.1; -.
DR iPTMnet; Q9ZQ31; -.
DR PaxDb; Q9ZQ31; -.
DR PRIDE; Q9ZQ31; -.
DR ProteomicsDB; 228276; -.
DR DNASU; 816972; -.
DR EnsemblPlants; AT2G24360.1; AT2G24360.1; AT2G24360.
DR GeneID; 816972; -.
DR Gramene; AT2G24360.1; AT2G24360.1; AT2G24360.
DR KEGG; ath:AT2G24360; -.
DR Araport; AT2G24360; -.
DR TAIR; locus:2061092; AT2G24360.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_000288_7_35_1; -.
DR InParanoid; Q9ZQ31; -.
DR OMA; NIVAHHV; -.
DR OrthoDB; 565206at2759; -.
DR PhylomeDB; Q9ZQ31; -.
DR PRO; PR:Q9ZQ31; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZQ31; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:TAIR.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; ISS:TAIR.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
DR GO; GO:0045995; P:regulation of embryonic development; IGI:TAIR.
DR GO; GO:0010344; P:seed oilbody biogenesis; IMP:TAIR.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
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 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..411
FT /note="Serine/threonine-protein kinase STY13"
FT /id="PRO_0000442917"
FT DOMAIN 130..392
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 256
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 136..144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 288
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22558"
FT MUTAGEN 165
FT /note="S->A: No effect on kinase activity."
FT /evidence="ECO:0000269|PubMed:17291444"
FT MUTAGEN 181
FT /note="S->A: No effect on kinase activity."
FT /evidence="ECO:0000269|PubMed:17291444"
FT MUTAGEN 215
FT /note="S->A: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:17291444"
FT MUTAGEN 259
FT /note="S->A: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:17291444"
FT MUTAGEN 265
FT /note="S->A: Slightly increases kinase activity."
FT /evidence="ECO:0000269|PubMed:17291444"
FT MUTAGEN 269
FT /note="S->A: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:17291444"
FT MUTAGEN 315
FT /note="S->A: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:17291444"
FT MUTAGEN 360
FT /note="S->A: No effect on kinase activity."
FT /evidence="ECO:0000269|PubMed:17291444"
SQ SEQUENCE 411 AA; 46002 MW; 3B7001CFBB411BAA CRC64;
MLEGAKFNVL AVGNHHNNDN NYYAFTQEFY QKLNEGSNMS MESMQTSNAG GSVSMSVDNS
SVGSSDALIG HPGLKPVRHY SLSVGQSVFR PGRVTHALND DALAQALMDT RYPTEGLTNY
DEWTIDLRKL NMGPAFAQGA FGKLYKGTYN GEDVAIKILE RPENSPEKAQ FMEQQFQQEV
SMLANLKHPN IVRFIGACRK PMVWCIVTEY AKGGSVRQFL TRRQNRAVPL KLAVKQALDV
ARGMAYVHGR NFIHRDLKSD NLLISADKSI KIADFGVARI EVQTEGMTPE TGTYRWMAPE
MIQHRAYNQK VDVYSFGIVL WELITGLLPF QNMTAVQAAF AVVNRGVRPT VPNDCLPVLS
DIMTRCWDAN PEVRPCFVEV VKLLEAAETE IMTTARKARF RCCLSQPMTI D
