KSG6_ARATH
ID KSG6_ARATH Reviewed; 412 AA.
AC Q39010; O80862; Q541C5; Q8LAX6;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Shaggy-related protein kinase zeta;
DE EC=2.7.11.1;
DE AltName: Full=ASK-zeta;
DE AltName: Full=Shaggy-related protein kinase 2-2;
DE Short=AtSK2-2;
DE AltName: Full=Shaggy-related protein kinase 23 {ECO:0000303|PubMed:28575660};
DE Short=AtSK23 {ECO:0000303|PubMed:28575660};
GN Name=ASK6; Synonyms=SK2-2, SK23 {ECO:0000303|PubMed:28575660};
GN OrderedLocusNames=At2g30980 {ECO:0000312|Araport:AT2G30980};
GN ORFNames=F7F1.19 {ECO:0000312|EMBL:AAC20732.1};
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=Leaf;
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=9611268; DOI=10.1016/s0378-1119(98)00147-4;
RA Dornelas M.C., Lejeune B., Dron M., Kreis M.;
RT "The Arabidopsis SHAGGY-related protein kinase (ASK) gene family:
RT structure, organization and evolution.";
RL Gene 212:249-257(1998).
RN [3]
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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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: May mediate extracellular signals to regulate transcription
CC in differentiating cells. {ECO:0000250}.
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 -!- 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;
CC -!- SUBUNIT: Binds to KIB1 (PubMed:28575660). Interacts with beet curly top
CC virus AL4/C4 and tomato golden mosaic virus AL4/AC4.
CC {ECO:0000269|PubMed:28575660}.
CC -!- INTERACTION:
CC Q39010; Q8GY45: At1g35210; NbExp=4; IntAct=EBI-1238323, EBI-4436537;
CC Q39010; O49404: BEH3; NbExp=3; IntAct=EBI-1238323, EBI-25514571;
CC Q39010; Q9FKQ7: MNA5.2; NbExp=3; IntAct=EBI-1238323, EBI-25521920;
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; X94938; CAA64408.1; -; mRNA.
DR EMBL; Y09300; CAA70483.1; -; Genomic_DNA.
DR EMBL; AC004669; AAC20732.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08470.1; -; Genomic_DNA.
DR EMBL; AY064020; AAL36376.1; -; mRNA.
DR EMBL; AY094423; AAM19796.1; -; mRNA.
DR EMBL; AY096698; AAM20332.1; -; mRNA.
DR EMBL; AY087542; AAM65084.1; -; mRNA.
DR PIR; A84715; A84715.
DR PIR; S71266; S71266.
DR RefSeq; NP_180655.1; NM_128652.4.
DR AlphaFoldDB; Q39010; -.
DR SMR; Q39010; -.
DR BioGRID; 2998; 16.
DR IntAct; Q39010; 11.
DR STRING; 3702.AT2G30980.1; -.
DR iPTMnet; Q39010; -.
DR PaxDb; Q39010; -.
DR PRIDE; Q39010; -.
DR ProteomicsDB; 237067; -.
DR EnsemblPlants; AT2G30980.1; AT2G30980.1; AT2G30980.
DR GeneID; 817649; -.
DR Gramene; AT2G30980.1; AT2G30980.1; AT2G30980.
DR KEGG; ath:AT2G30980; -.
DR Araport; AT2G30980; -.
DR TAIR; locus:2052861; AT2G30980.
DR eggNOG; KOG0658; Eukaryota.
DR HOGENOM; CLU_000288_181_20_1; -.
DR InParanoid; Q39010; -.
DR OMA; QAAHNFF; -.
DR OrthoDB; 990896at2759; -.
DR PhylomeDB; Q39010; -.
DR BRENDA; 2.7.11.26; 399.
DR PRO; PR:Q39010; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q39010; baseline and differential.
DR Genevisible; Q39010; 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; IBA:GO_Central.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IPI: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 ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..412
FT /note="Shaggy-related protein kinase zeta"
FT /id="PRO_0000086221"
FT DOMAIN 72..356
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 197
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 78..86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 136
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 137
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 232
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q39011"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 293
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 346
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT CONFLICT 198
FT /note="V -> I (in Ref. 1; CAA64408 and 2; CAA70483)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="L -> H (in Ref. 1; CAA64408 and 2; CAA70483)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="A -> P (in Ref. 1; CAA64408 and 2; CAA70483)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="A -> S (in Ref. 6; AAM65084)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="Q -> R (in Ref. 6; AAM65084)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 412 AA; 46455 MW; 2D59622EF1501B8F CRC64;
MTSIPLGPPQ PPSLAPQPPH LHGGDSLKRR PDIDNDKEMS AAVIEGNDAV TGHIISTTIG
GKNGEPKQTI SYMAERVVGT GSFGIVFQAK CLETGESVAI KKVLQDRRYK NRELQLMRLM
DHPNVVSLKH CFFSTTTRDE LFLNLVMEYV PETLYRVLKH YTSSNQRMPI FYVKLYTYQI
FRGLAYIHTA PGVCHRDVKP QNLLVDPLTH QCKLCDFGSA KVLVKGEANI SYICSRYYRA
PELIFGATEY TSSIDIWSAG CVLAELLLGQ PLFPGENSVD QLVEIIKVLG TPTREEIRCM
NPNYTDFRFP QIKAHPWHKV FHKRMPPEAI DLASRLLQYS PSLRCTALEA CAHPFFNELR
EPNARLPNGR PLPPLFNFKQ ELSGASPELI NRLIPEHVRR QMNGGFPFQA GP
