KSG9_ARATH
ID KSG9_ARATH Reviewed; 407 AA.
AC Q39012;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Shaggy-related protein kinase iota;
DE EC=2.7.11.1 {ECO:0000269|PubMed:23496207};
DE AltName: Full=ASK-iota;
DE AltName: Full=GSK3/shaggy-related protein kinase 1;
DE Short=AtGSK1;
DE AltName: Full=Protein BIN2-like 2;
DE AltName: Full=Shaggy-related protein kinase 2-3;
DE Short=AtSK2-3;
DE AltName: Full=Shaggy-related protein kinase 22 {ECO:0000303|PubMed:28575660};
DE Short=AtSK22 {ECO:0000303|PubMed:28575660};
GN Name=ASK9; Synonyms=BIL2, GSK1, SK2-3, SK22 {ECO:0000303|PubMed:28575660};
GN OrderedLocusNames=At1g06390 {ECO:0000312|Araport:AT1G06390};
GN ORFNames=T2D23.9 {ECO:0000312|EMBL:AAF82167.1};
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 [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Root;
RA Dornelas M.C., Schwebel-Dugue N., Thomas M., Lecharny A., Kreis M.;
RT "Three new cDNAs related to SGG/GSK-3 (SHAGGY/glycogen synthase kinase-3)
RT from Arabidopsis thaliana.";
RL (er) Plant Gene Register PGR97-008(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Piao H.L., Jang H.J., Pih K.T., Lim J.H., Kang S.G., Jin J.B., Hwang I.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 [5]
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH BSK6, AND MUTAGENESIS OF
RP LYS-99.
RX PubMed=23496207; DOI=10.1111/tpj.12175;
RA Sreeramulu S., Mostizky Y., Sunitha S., Shani E., Nahum H., Salomon D.,
RA Hayun L.B., Gruetter C., Rauh D., Ori N., Sessa G.;
RT "BSKs are partially redundant positive regulators of brassinosteroid
RT signaling in Arabidopsis.";
RL Plant J. 74:905-919(2013).
RN [7]
RP INTERACTION WITH KIB1.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=28575660; DOI=10.1016/j.molcel.2017.05.012;
RA Zhu J.-Y., Li Y., Cao D.-M., Yang H., Oh E., Bi Y., Zhu S., Wang Z.-Y.;
RT "The F-box protein KIB1 mediates brassinosteroid-induced inactivation and
RT degradation of GSK3-like kinases in Arabidopsis.";
RL Mol. Cell 66:648-657(2017).
CC -!- FUNCTION: Phosphorylates BSK1, BSK3, BSK5, BSK6, BSK8 AND BSK11 in
CC vitro (PubMed:23496207). May mediate extracellular signals to regulate
CC transcription in differentiating cells (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:23496207}.
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:23496207};
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:23496207};
CC -!- SUBUNIT: Binds to KIB1 (PubMed:28575660). Interacts with BSK6
CC (PubMed:23496207). {ECO:0000269|PubMed:23496207,
CC ECO:0000269|PubMed:28575660}.
CC -!- PTM: Autophosphorylated mainly on threonine and serine residues.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. GSK-3 subfamily. {ECO:0000305}.
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DR EMBL; X99696; CAA68027.1; -; mRNA.
DR EMBL; AF019927; AAB71545.1; -; mRNA.
DR EMBL; AC068143; AAF82167.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27980.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27981.1; -; Genomic_DNA.
DR EMBL; AY035048; AAK59553.1; -; mRNA.
DR EMBL; AY051053; AAK93730.1; -; mRNA.
DR PIR; S77922; S77922.
DR RefSeq; NP_172127.1; NM_100519.3.
DR RefSeq; NP_973771.1; NM_202042.3.
DR AlphaFoldDB; Q39012; -.
DR SMR; Q39012; -.
DR BioGRID; 22391; 14.
DR IntAct; Q39012; 5.
DR STRING; 3702.AT1G06390.1; -.
DR iPTMnet; Q39012; -.
DR PaxDb; Q39012; -.
DR PRIDE; Q39012; -.
DR ProteomicsDB; 250710; -.
DR EnsemblPlants; AT1G06390.1; AT1G06390.1; AT1G06390.
DR EnsemblPlants; AT1G06390.2; AT1G06390.2; AT1G06390.
DR GeneID; 837150; -.
DR Gramene; AT1G06390.1; AT1G06390.1; AT1G06390.
DR Gramene; AT1G06390.2; AT1G06390.2; AT1G06390.
DR KEGG; ath:AT1G06390; -.
DR Araport; AT1G06390; -.
DR TAIR; locus:2202255; AT1G06390.
DR eggNOG; KOG0658; Eukaryota.
DR HOGENOM; CLU_000288_181_20_1; -.
DR InParanoid; Q39012; -.
DR OMA; LMRPMDH; -.
DR OrthoDB; 990896at2759; -.
DR PhylomeDB; Q39012; -.
DR BRENDA; 2.7.11.26; 399.
DR PRO; PR:Q39012; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q39012; baseline and differential.
DR Genevisible; Q39012; AT.
DR GO; GO:0005737; C:cytoplasm; 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; HDA:TAIR.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IPI:TAIR.
DR GO; GO:0042538; P:hyperosmotic salinity response; IMP:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; HDA:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
DR GO; GO:0032880; P:regulation of protein localization; IDA:TAIR.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd14137; STKc_GSK3; 1.
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 InterPro; IPR039192; STKc_GSK3.
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 Acetylation; ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P43288"
FT CHAIN 2..407
FT /note="Shaggy-related protein kinase iota"
FT /id="PRO_0000086224"
FT DOMAIN 70..354
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 195
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 76..84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P43288"
FT MOD_RES 230
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q39011"
FT MUTAGEN 99
FT /note="K->R: Abolishes kinase activity."
FT /evidence="ECO:0000269|PubMed:23496207"
SQ SEQUENCE 407 AA; 46024 MW; 96BC4C53754A764C CRC64;
MASLPLGPQP HALAPPLQLH DGDALKRRPE LDSDKEMSAA VIEGNDAVTG HIISTTIGGK
NGEPKQTISY MAERVVGTGS FGIVFQAKCL ETGESVAIKK VLQDRRYKNR ELQLMRPMDH
PNVISLKHCF FSTTSRDELF LNLVMEYVPE TLYRVLRHYT SSNQRMPIFY VKLYTYQIFR
GLAYIHTVPG VCHRDVKPQN LLVDPLTHQV KLCDFGSAKV LVKGEPNISY ICSRYYRAPE
LIFGATEYTA SIDIWSAGCV LAELLLGQPL FPGENSVDQL VEIIKVLGTP TREEIRCMNP
NYTDFRFPQI KAHPWHKVFH KRMPPEAIDL ASRLLQYSPS LRCTALEACA HPFFNELREP
NARLPNGRPL PPLFNFKQEL GGASMELINR LIPEHVRRQM STGLQNS
