KSG10_ARATH
ID KSG10_ARATH Reviewed; 421 AA.
AC Q39019; O04506; Q96244;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 21-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Shaggy-related protein kinase kappa;
DE Short=AtHIR1;
DE EC=2.7.11.1;
DE AltName: Full=ASK-kappa;
DE Short=AtK-1;
DE AltName: Full=Shaggy-related protein kinase 41;
DE Short=AtSK41;
GN Name=ASK10; Synonyms=HIR1, SK41;
GN OrderedLocusNames=At1g09840 {ECO:0000312|Araport:AT1G09840};
GN ORFNames=F21M12.23 {ECO:0000312|EMBL:AAB60754.1};
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 [GENOMIC DNA].
RX PubMed=7865793; DOI=10.1007/bf00019194;
RA Jonak C., Heberle-Bors E., Hirt H.;
RT "Inflorescence-specific expression of AtK-1, a novel Arabidopsis thaliana
RT homologue of shaggy/glycogen synthase kinase-3.";
RL Plant Mol. Biol. 27:217-221(1995).
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 47-421.
RC STRAIN=cv. Columbia;
RA Carnier M.C., Kreis M., Dornelas M.C.;
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
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 -!- TISSUE SPECIFICITY: Expressed exclusively in inflorescences.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB60754.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X79279; CAA55866.1; -; Genomic_DNA.
DR EMBL; AC000132; AAB60754.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28501.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28502.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28503.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28504.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28505.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28506.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60294.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60295.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60296.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60298.1; -; Genomic_DNA.
DR EMBL; AY092987; AAM12986.1; -; mRNA.
DR EMBL; BT000132; AAN15451.1; -; mRNA.
DR EMBL; Y07597; CAA68872.1; -; mRNA.
DR PIR; F86232; F86232.
DR PIR; S51938; S51938.
DR RefSeq; NP_001031013.1; NM_001035936.1.
DR RefSeq; NP_001077498.1; NM_001084029.2.
DR RefSeq; NP_001077499.1; NM_001084030.2.
DR RefSeq; NP_001318967.1; NM_001331857.1.
DR RefSeq; NP_001322592.1; NM_001331858.1.
DR RefSeq; NP_001322593.1; NM_001331859.1.
DR RefSeq; NP_001322595.1; NM_001331855.1.
DR RefSeq; NP_172455.1; NM_100858.5.
DR RefSeq; NP_849627.1; NM_179296.1.
DR RefSeq; NP_973801.1; NM_202072.2.
DR AlphaFoldDB; Q39019; -.
DR SMR; Q39019; -.
DR BioGRID; 22757; 7.
DR IntAct; Q39019; 6.
DR STRING; 3702.AT1G09840.3; -.
DR iPTMnet; Q39019; -.
DR PaxDb; Q39019; -.
DR PRIDE; Q39019; -.
DR ProteomicsDB; 250767; -.
DR EnsemblPlants; AT1G09840.1; AT1G09840.1; AT1G09840.
DR EnsemblPlants; AT1G09840.10; AT1G09840.10; AT1G09840.
DR EnsemblPlants; AT1G09840.2; AT1G09840.2; AT1G09840.
DR EnsemblPlants; AT1G09840.3; AT1G09840.3; AT1G09840.
DR EnsemblPlants; AT1G09840.4; AT1G09840.4; AT1G09840.
DR EnsemblPlants; AT1G09840.5; AT1G09840.5; AT1G09840.
DR EnsemblPlants; AT1G09840.6; AT1G09840.6; AT1G09840.
DR EnsemblPlants; AT1G09840.7; AT1G09840.7; AT1G09840.
DR EnsemblPlants; AT1G09840.8; AT1G09840.8; AT1G09840.
DR EnsemblPlants; AT1G09840.9; AT1G09840.9; AT1G09840.
DR GeneID; 837516; -.
DR Gramene; AT1G09840.1; AT1G09840.1; AT1G09840.
DR Gramene; AT1G09840.10; AT1G09840.10; AT1G09840.
DR Gramene; AT1G09840.2; AT1G09840.2; AT1G09840.
DR Gramene; AT1G09840.3; AT1G09840.3; AT1G09840.
DR Gramene; AT1G09840.4; AT1G09840.4; AT1G09840.
DR Gramene; AT1G09840.5; AT1G09840.5; AT1G09840.
DR Gramene; AT1G09840.6; AT1G09840.6; AT1G09840.
DR Gramene; AT1G09840.7; AT1G09840.7; AT1G09840.
DR Gramene; AT1G09840.8; AT1G09840.8; AT1G09840.
DR Gramene; AT1G09840.9; AT1G09840.9; AT1G09840.
DR KEGG; ath:AT1G09840; -.
DR Araport; AT1G09840; -.
DR TAIR; locus:2024341; AT1G09840.
DR eggNOG; KOG0658; Eukaryota.
DR HOGENOM; CLU_000288_181_20_1; -.
DR InParanoid; Q39019; -.
DR OMA; EVCSHEF; -.
DR OrthoDB; 990896at2759; -.
DR PhylomeDB; Q39019; -.
DR BRENDA; 2.7.11.26; 399.
DR PRO; PR:Q39019; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q39019; baseline and differential.
DR Genevisible; Q39019; 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:0006468; P:protein phosphorylation; IEA:InterPro.
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 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..421
FT /note="Shaggy-related protein kinase kappa"
FT /id="PRO_0000086225"
FT DOMAIN 83..367
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 208
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 89..97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 243
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q39011"
FT CONFLICT 313
FT /note="P -> G (in Ref. 1; CAA55866 and 5; CAA68872)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 421 AA; 47669 MW; 5810423888792453 CRC64;
MASSGLGNGV GTSRSAKGLK SSSSSVDWLT RDLAETRIRD KVETDDERDS EPDIIDGAGA
EPGHVIRTTL RGRNGQSRQT VSYISEHVVG TGSFGMVFQA KCRETGEVVA IKKVLQDKRY
KNRELQIMQM LDHPNAVALK HSFFSRTDNE EVYLNLVLEF VPETVNRVAR SYSRTNQLMP
LIYVKLYTYQ ICRALAYIHN SFGLCHRDIK PQNLLVNPHT HQLKICDFGS AKVLVKGEPN
VSYICSRYYR APELIFGASE YTTAIDIWST GCVMAELLLG QPLFPGESGV DQLVEIIKVL
GTPTREEIKC MNPNYTEFKF PQIKPHPWHK VFQKRLPPEA VDLLCRFFQY SPNLRCTALE
ACIHPLFDEL RDPNTRLPNG RPLPPLFNFK PQELSGIPPE IVNRLVPEHA RKQNLFMALH
S
