KSG2_ARATH
ID KSG2_ARATH Reviewed; 431 AA.
AC O23145; O81710;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Shaggy-related protein kinase beta {ECO:0000303|PubMed:9804971};
DE EC=2.7.11.1;
DE AltName: Full=ASK-beta {ECO:0000303|PubMed:9804971};
GN Name=ASK2 {ECO:0000303|PubMed:9804971};
GN OrderedLocusNames=At3g61160 {ECO:0000312|Araport:AT3G61160};
GN ORFNames=T20K12.60 {ECO:0000312|EMBL:CAB71046.1};
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 / MRNA].
RC STRAIN=cv. Columbia; TISSUE=Pollen;
RX PubMed=9804971; DOI=10.1016/s0167-4781(98)00187-0;
RA Tichtinsky G., Tavares R., Takvorian A., Schwebel-Dugue N., Twell D.,
RA Kreis M.;
RT "An evolutionary conserved group of plant GSK-3/shaggy-like protein kinase
RT genes preferentially expressed in developing pollen.";
RL Biochim. Biophys. Acta 1442:261-273(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10809443; DOI=10.1023/a:1006368316413;
RA Tavares R., Aubourg S., Lecharny A., Kreis M.;
RT "Organization and structural evolution of four multigene families in
RT Arabidopsis thaliana: AtLCAD, AtLGT, AtMYST and AtHD-GL2.";
RL Plant Mol. Biol. 42:703-717(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O23145-1; Sequence=Displayed;
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; AJ002280; CAA05292.1; -; mRNA.
DR EMBL; AJ224338; CAA11903.2; -; Genomic_DNA.
DR EMBL; AL137898; CAB71046.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80162.1; -; Genomic_DNA.
DR PIR; T47908; T47908.
DR RefSeq; NP_191675.1; NM_115980.4. [O23145-1]
DR AlphaFoldDB; O23145; -.
DR SMR; O23145; -.
DR BioGRID; 10602; 7.
DR IntAct; O23145; 7.
DR STRING; 3702.AT3G61160.2; -.
DR iPTMnet; O23145; -.
DR PaxDb; O23145; -.
DR PRIDE; O23145; -.
DR EnsemblPlants; AT3G61160.1; AT3G61160.1; AT3G61160. [O23145-1]
DR GeneID; 825288; -.
DR Gramene; AT3G61160.1; AT3G61160.1; AT3G61160. [O23145-1]
DR KEGG; ath:AT3G61160; -.
DR Araport; AT3G61160; -.
DR eggNOG; KOG0658; Eukaryota.
DR HOGENOM; CLU_000288_181_20_1; -.
DR InParanoid; O23145; -.
DR PhylomeDB; O23145; -.
DR BRENDA; 2.7.11.26; 399.
DR PRO; PR:O23145; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O23145; baseline and differential.
DR Genevisible; O23145; 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 Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..431
FT /note="Shaggy-related protein kinase beta"
FT /id="PRO_0000086217"
FT DOMAIN 102..386
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 12..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 227
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 108..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 262
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q39011"
SQ SEQUENCE 431 AA; 49313 MW; 1FB3E6BE19BA8AD0 CRC64;
MNVVRRLTSI ASGRNFVSSD NVGETETPRS KPNQNREETE STETTSYEKD SVSSSENSDH
LPKEIREDMD CGIIKGNGTE SGRIITTKKK GLNDQKDKTI SYRAEHVIGT GSFGVVFQAK
CLETEEKVAI KKVLQDKRYK NRELQIMRML DHPNVVELKH SFFSTTEKDE LYLNLVLEYV
PETIYRASRS YTKMNQHMPL IYIQLYTYQI CRAMNYLHQV VGVCHRDIKP QNLLVNNVTH
EVKICDFGSA KMLIPGEPNI SYICSRYYRA PELIFGATEY TSAIDMWSVG CVMAELFLGH
PLFPGETSVD QLVEIIKILG TPAREEIKNM NPRYNDFKFP QIKAQPWHKI FRRQVSPEAM
DLASRLLQYS PNLRCTALEA CAHPFFDDLR DPRASLPNGR ALPPLFDFTA QELAGASVEL
RHRLIPEHAR K
