KSG1_ARATH
ID KSG1_ARATH Reviewed; 405 AA.
AC P43288; O04625; O23151; Q93VJ5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Shaggy-related protein kinase alpha {ECO:0000303|PubMed:7509023};
DE EC=2.7.11.1;
DE AltName: Full=ASK-alpha {ECO:0000303|PubMed:7509023};
DE AltName: Full=Shaggy-related protein kinase 11 {ECO:0000303|PubMed:28575660};
DE Short=AtSK11 {ECO:0000303|PubMed:28575660};
GN Name=ASK1 {ECO:0000303|PubMed:7509023};
GN Synonyms=SK11 {ECO:0000303|PubMed:28575660};
GN OrderedLocusNames=At5g26751 {ECO:0000312|Araport:AT5G26751};
GN ORFNames=F2P16.21 {ECO:0000312|EMBL:AAB61055.1};
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=Shoot;
RX PubMed=7509023; DOI=10.1007/bf00280424;
RA Bianchi M.W., Guivarc'H D., Thomas M., Woodgett J.R., Kreis M.;
RT "Arabidopsis homologs of the shaggy and GSK-3 protein kinases: molecular
RT cloning and functional expression in Escherichia coli.";
RL Mol. Gen. Genet. 242:337-345(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Dornelas M.C., Kreis M.;
RT "Plant homologues of SGG/GSK-3 protein kinases.";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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.
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 -!- INTERACTION:
CC P43288; Q94AH6: CUL1; NbExp=2; IntAct=EBI-4463633, EBI-532411;
CC -!- TISSUE SPECIFICITY: Roots, shoots and leaves.
CC -!- PTM: Autophosphorylated mainly on threonine and serine residues.
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=AAB61055.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA04265.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X68525; CAA48538.1; -; mRNA.
DR EMBL; X75432; CAA53181.1; -; mRNA.
DR EMBL; AJ000732; CAA04265.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF007270; AAB61055.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED93596.1; -; Genomic_DNA.
DR EMBL; AF428327; AAL16257.1; -; mRNA.
DR EMBL; AY046024; AAK76698.1; -; mRNA.
DR EMBL; AY142595; AAN13164.1; -; mRNA.
DR PIR; S41596; S41596.
DR PIR; T01756; T01756.
DR RefSeq; NP_568486.1; NM_122557.3.
DR AlphaFoldDB; P43288; -.
DR SMR; P43288; -.
DR BioGRID; 18008; 1.
DR DIP; DIP-46124N; -.
DR IntAct; P43288; 3.
DR STRING; 3702.AT5G26751.1; -.
DR iPTMnet; P43288; -.
DR PaxDb; P43288; -.
DR PRIDE; P43288; -.
DR ProteomicsDB; 237109; -.
DR EnsemblPlants; AT5G26751.1; AT5G26751.1; AT5G26751.
DR GeneID; 832733; -.
DR Gramene; AT5G26751.1; AT5G26751.1; AT5G26751.
DR KEGG; ath:AT5G26751; -.
DR Araport; AT5G26751; -.
DR TAIR; locus:2832141; AT5G26751.
DR eggNOG; KOG0658; Eukaryota.
DR HOGENOM; CLU_000288_181_20_1; -.
DR InParanoid; P43288; -.
DR OMA; TNYDENE; -.
DR OrthoDB; 990896at2759; -.
DR PhylomeDB; P43288; -.
DR BRENDA; 2.7.11.26; 399.
DR PRO; PR:P43288; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P43288; baseline and differential.
DR Genevisible; P43288; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:TAIR.
DR GO; GO:0042538; P:hyperosmotic salinity response; IMP:TAIR.
DR GO; GO:0009933; P:meristem structural organization; IMP:TAIR.
DR GO; GO:1901002; P:positive regulation of response to salt stress; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0009651; P:response to salt stress; IMP: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:0007744|PubMed:22223895"
FT CHAIN 2..405
FT /note="Shaggy-related protein kinase alpha"
FT /id="PRO_0000086216"
FT DOMAIN 69..353
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 194
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 75..83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 98
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:0007744|PubMed:22223895"
FT MOD_RES 229
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q39011"
FT CONFLICT 281
FT /note="E -> H (in Ref. 1; CAA53181/CAA48538 and 2;
FT CAA04265)"
FT /evidence="ECO:0000305"
FT CONFLICT 372..374
FT /note="LFN -> AFH (in Ref. 1; CAA53181/CAA48538 and 2;
FT CAA04265)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 405 AA; 46035 MW; ACC949DD58479FBB CRC64;
MASVGIAPNP GARDSTGVDK LPEEMNDMKI RDDKEMEATV VDGNGTETGH IIVTTIGGRN
GQPKQTISYM AERVVGHGSF GVVFQAKCLE TGETVAIKKV LQDRRYKNRE LQTMRLLDHP
NVVSLKHCFF STTEKDELYL NLVLEYVPET VHRVIKHYNK LNQRMPLIYV KLYTYQIFRA
LSYIHRCIGV CHRDIKPQNL LVNPHTHQVK LCDFGSAKVL VKGEPNISYI CSRYYRAPEL
IFGATEYTTA IDVWSAGCVL AELLLGQPLF PGESGVDQLV EIIKVLGTPT REEIKCMNPN
YTEFKFPQIK AHPWHKIFHK RMPPEAVDLV SRLLQYSPNL RSAALDTLVH PFFDELRDPN
ARLPNGRFLP PLFNFKPHEL KGVPLEMVAK LVPEHARKQC PWLGL
