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Shaggy-related protein kinase iota (EC 2.7.11.1) (ASK-iota) (GSK3/shaggy-related protein kinase 1) (AtGSK1) (Protein BIN2-like 2) (Shaggy-related protein kinase 2-3) (AtSK2-3) (Shaggy-related protein kinase 22) (AtSK22)

 KSG9_ARATH              Reviewed;         407 AA.
Q39012;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
05-DEC-2018, entry version 155.
RecName: Full=Shaggy-related protein kinase iota;
EC=2.7.11.1 {ECO:0000269|PubMed:23496207};
AltName: Full=ASK-iota;
AltName: Full=GSK3/shaggy-related protein kinase 1;
Short=AtGSK1;
AltName: Full=Protein BIN2-like 2;
AltName: Full=Shaggy-related protein kinase 2-3;
Short=AtSK2-3;
AltName: Full=Shaggy-related protein kinase 22 {ECO:0000303|PubMed:28575660};
Short=AtSK22 {ECO:0000303|PubMed:28575660};
Name=ASK9;
Synonyms=BIL2, GSK1, SK2-3, SK22 {ECO:0000303|PubMed:28575660};
OrderedLocusNames=At1g06390 {ECO:0000312|Araport:AT1G06390};
ORFNames=T2D23.9 {ECO:0000312|EMBL:AAF82167.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia; TISSUE=Root;
Dornelas M.C., Schwebel-Dugue N., Thomas M., Lecharny A., Kreis M.;
"Three new cDNAs related to SGG/GSK-3 (SHAGGY/glycogen synthase
kinase-3) from Arabidopsis thaliana.";
(er) Plant Gene Register PGR97-008(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
Piao H.L., Jang H.J., Pih K.T., Lim J.H., Kang S.G., Jin J.B.,
Hwang I.;
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH BSK6, AND MUTAGENESIS
OF LYS-99.
PubMed=23496207; DOI=10.1111/tpj.12175;
Sreeramulu S., Mostizky Y., Sunitha S., Shani E., Nahum H.,
Salomon D., Hayun L.B., Gruetter C., Rauh D., Ori N., Sessa G.;
"BSKs are partially redundant positive regulators of brassinosteroid
signaling in Arabidopsis.";
Plant J. 74:905-919(2013).
[7]
INTERACTION WITH KIB1.
STRAIN=cv. Columbia, and cv. Wassilewskija;
PubMed=28575660; DOI=10.1016/j.molcel.2017.05.012;
Zhu J.-Y., Li Y., Cao D.-M., Yang H., Oh E., Bi Y., Zhu S.,
Wang Z.-Y.;
"The F-box protein KIB1 mediates brassinosteroid-induced inactivation
and degradation of GSK3-like kinases in Arabidopsis.";
Mol. Cell 66:648-657(2017).
-!- FUNCTION: Phosphorylates BSK1, BSK3, BSK5, BSK6, BSK8 AND BSK11 in
vitro (PubMed:23496207). May mediate extracellular signals to
regulate transcription in differentiating cells (By similarity).
{ECO:0000250, ECO:0000269|PubMed:23496207}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
EC=2.7.11.1; Evidence={ECO:0000269|PubMed:23496207};
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.1; Evidence={ECO:0000269|PubMed:23496207};
-!- SUBUNIT: Binds to KIB1 (PubMed:28575660). Interacts with BSK6
(PubMed:23496207). {ECO:0000269|PubMed:23496207,
ECO:0000269|PubMed:28575660}.
-!- PTM: Autophosphorylated mainly on threonine and serine residues.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. GSK-3 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X99696; CAA68027.1; -; mRNA.
EMBL; AF019927; AAB71545.1; -; mRNA.
EMBL; AC068143; AAF82167.1; -; Genomic_DNA.
EMBL; CP002684; AEE27980.1; -; Genomic_DNA.
EMBL; CP002684; AEE27981.1; -; Genomic_DNA.
EMBL; AY035048; AAK59553.1; -; mRNA.
EMBL; AY051053; AAK93730.1; -; mRNA.
PIR; S77922; S77922.
RefSeq; NP_172127.1; NM_100519.3.
RefSeq; NP_973771.1; NM_202042.3.
UniGene; At.133; -.
UniGene; At.24592; -.
ProteinModelPortal; Q39012; -.
SMR; Q39012; -.
BioGrid; 22391; 14.
IntAct; Q39012; 5.
STRING; 3702.AT1G06390.1; -.
iPTMnet; Q39012; -.
PaxDb; Q39012; -.
EnsemblPlants; AT1G06390.1; AT1G06390.1; AT1G06390.
EnsemblPlants; AT1G06390.2; AT1G06390.2; AT1G06390.
GeneID; 837150; -.
Gramene; AT1G06390.1; AT1G06390.1; AT1G06390.
Gramene; AT1G06390.2; AT1G06390.2; AT1G06390.
KEGG; ath:AT1G06390; -.
Araport; AT1G06390; -.
TAIR; locus:2202255; AT1G06390.
eggNOG; KOG0658; Eukaryota.
eggNOG; COG0515; LUCA.
HOGENOM; HOG000233017; -.
InParanoid; Q39012; -.
OMA; PEDRMKP; -.
OrthoDB; EOG09360BBG; -.
PhylomeDB; Q39012; -.
BRENDA; 2.7.11.26; 399.
Reactome; R-ATH-3371453; Regulation of HSF1-mediated heat shock response.
PRO; PR:Q39012; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q39012; baseline and differential.
Genevisible; Q39012; AT.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:TAIR.
GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IPI:TAIR.
GO; GO:0042538; P:hyperosmotic salinity response; IMP:TAIR.
GO; GO:0046777; P:protein autophosphorylation; IDA:TAIR.
GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
GO; GO:0032880; P:regulation of protein localization; IDA:TAIR.
CDD; cd14137; STKc_GSK3; 1.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR039192; STKc_GSK3.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Acetylation; ATP-binding; Complete proteome; Kinase;
Nucleotide-binding; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P43288}.
CHAIN 2 407 Shaggy-related protein kinase iota.
/FTId=PRO_0000086224.
DOMAIN 70 354 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 76 84 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 195 195 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 99 99 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P43288}.
MOD_RES 230 230 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q39011}.
MUTAGEN 99 99 K->R: Abolishes kinase activity.
{ECO:0000269|PubMed:23496207}.
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


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