KSG5_ARATH
ID KSG5_ARATH Reviewed; 410 AA.
AC Q8VZD5; Q9LYJ6;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Shaggy-related protein kinase epsilon;
DE EC=2.7.11.1;
DE AltName: Full=ASK-epsilon;
DE AltName: Full=Shaggy-related protein kinase 13 {ECO:0000303|PubMed:28575660};
DE Short=AtSK13 {ECO:0000303|PubMed:28575660};
GN Name=ASK5; Synonyms=SK13 {ECO:0000303|PubMed:28575660};
GN OrderedLocusNames=At5g14640 {ECO:0000312|Araport:AT5G14640};
GN ORFNames=T15N1.130 {ECO:0000312|EMBL:CAB87631.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
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 [3]
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 [4]
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. {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB87631.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL163792; CAB87631.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED92057.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68202.1; -; Genomic_DNA.
DR EMBL; AY065043; AAL57679.1; -; mRNA.
DR EMBL; BT010466; AAQ65089.1; -; mRNA.
DR PIR; T48637; T48637.
DR RefSeq; NP_001329975.1; NM_001343350.1.
DR RefSeq; NP_196968.2; NM_121468.4.
DR AlphaFoldDB; Q8VZD5; -.
DR SMR; Q8VZD5; -.
DR BioGRID; 16593; 1.
DR IntAct; Q8VZD5; 1.
DR STRING; 3702.AT5G14640.1; -.
DR iPTMnet; Q8VZD5; -.
DR PaxDb; Q8VZD5; -.
DR PRIDE; Q8VZD5; -.
DR ProteomicsDB; 237111; -.
DR EnsemblPlants; AT5G14640.1; AT5G14640.1; AT5G14640.
DR EnsemblPlants; AT5G14640.2; AT5G14640.2; AT5G14640.
DR GeneID; 831316; -.
DR Gramene; AT5G14640.1; AT5G14640.1; AT5G14640.
DR Gramene; AT5G14640.2; AT5G14640.2; AT5G14640.
DR KEGG; ath:AT5G14640; -.
DR Araport; AT5G14640; -.
DR TAIR; locus:2222642; AT5G14640.
DR eggNOG; KOG0658; Eukaryota.
DR HOGENOM; CLU_000288_181_20_1; -.
DR InParanoid; Q8VZD5; -.
DR OMA; TSEFHKE; -.
DR OrthoDB; 990896at2759; -.
DR PhylomeDB; Q8VZD5; -.
DR PRO; PR:Q8VZD5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8VZD5; baseline and differential.
DR Genevisible; Q8VZD5; 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:0006972; P:hyperosmotic response; IEP:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; HDA:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP: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..410
FT /note="Shaggy-related protein kinase epsilon"
FT /id="PRO_0000086220"
FT DOMAIN 74..358
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 199
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 80..88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 103
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 234
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q39011"
SQ SEQUENCE 410 AA; 46074 MW; EF0D1ABFD8887E45 CRC64;
MASVGTLPAS SMATKQSNAS ICAEKLPEGI NEMKIKDDKE MEAAVVDGNG TETGHIIVTT
IGGKNGQPKQ TISYMAERIV GQGSFGIVFQ AKCLETGETV AIKKVLQDKR YKNRELQTMR
LLDHPNVVSL KHCFFSTTEK DELYLNLVLE YVPETVYRVS KHYSRANQRM PIIYVKLYTY
QICRALAYIH GGVGVCHRDI KPQNLLVNPH THQVKLCDFG SAKVLVKGEP NISYICSRYY
RAPELIFGAT EYTTTIDIWS AGCVLAELLL GQPLFPGESG VDQLVEIIKV LGTPTREEIK
CMNPNYTEFK FPQIKAHPWH KIFHKRTPPE AVDLVSRLLQ YSPNLRSTAM EAIVHPFFDE
LRDPNTRLPN GRALPPLFNF KPQELKGASL ELLSKLIPDH ARKQCSFLAL
