BSK1_ARATH
ID BSK1_ARATH Reviewed; 512 AA.
AC Q944A7; O65504;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Serine/threonine-protein kinase BSK1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000269|PubMed:23532072};
DE AltName: Full=Brassinosteroid-signaling kinase 1 {ECO:0000303|PubMed:18653891};
GN Name=BSK1 {ECO:0000303|PubMed:18653891};
GN OrderedLocusNames=At4g35230 {ECO:0000312|Araport:AT4G35230};
GN ORFNames=F23E12.210 {ECO:0000312|EMBL:CAA18746.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 MYRISTOYLATION AT GLY-2.
RX PubMed=12912986; DOI=10.1074/jbc.m307321200;
RA Boisson B., Giglione C., Meinnel T.;
RT "Unexpected protein families including cell defense components feature in
RT the N-myristoylome of a higher eukaryote.";
RL J. Biol. Chem. 278:43418-43429(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Seedling;
RX PubMed=17586839; DOI=10.1074/mcp.m700164-mcp200;
RA Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B., Schulze W.X.;
RT "Temporal analysis of sucrose-induced phosphorylation changes in plasma
RT membrane proteins of Arabidopsis.";
RL Mol. Cell. Proteomics 6:1711-1726(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH BRI1,
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-230, AND MUTAGENESIS OF
RP SER-230.
RX PubMed=18653891; DOI=10.1126/science.1156973;
RA Tang W., Kim T.W., Oses-Prieto J.A., Sun Y., Deng Z., Zhu S., Wang R.,
RA Burlingame A.L., Wang Z.Y.;
RT "BSKs mediate signal transduction from the receptor kinase BRI1 in
RT Arabidopsis.";
RL Science 321:557-560(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH FLS2, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF GLY-2; LYS-104 AND ARG-443.
RX PubMed=23532072; DOI=10.1105/tpc.112.107904;
RA Shi H., Shen Q., Qi Y., Yan H., Nie H., Chen Y., Zhao T., Katagiri F.,
RA Tang D.;
RT "BR-SIGNALING KINASE1 physically associates with FLAGELLIN SENSING2 and
RT regulates plant innate immunity in Arabidopsis.";
RL Plant Cell 25:1143-1157(2013).
RN [10]
RP INTERACTION WITH BRI1; ASK7/BIN2; BSK5; BSK6; BSK8 AND BSK11, AND
RP PHOSPHORYLATION.
RX PubMed=23496207; DOI=10.1111/tpj.12175;
RA Sreeramulu S., Mostizky Y., Sunitha S., Shani E., Nahum H., Salomon D.,
RA Hayun L.B., Gruetter C., Rauh D., Ori N., Sessa G.;
RT "BSKs are partially redundant positive regulators of brassinosteroid
RT signaling in Arabidopsis.";
RL Plant J. 74:905-919(2013).
CC -!- FUNCTION: Serine/threonine kinase that acts as positive regulator of
CC brassinosteroid (BR) signaling downstream of the receptor kinase BRI1.
CC Mediates signal transduction from BRI1 by functioning as substrate of
CC BRI1 (PubMed:18653891). Functions as a positive regulator of plant
CC immunity. May be involved in the regulation of pattern-triggered
CC immunity (PTI) downstream of the flagellin receptor FLS2. Possesses
CC kinase activity in vitro. Kinase activity is required for its function
CC in innate immunity (PubMed:23532072). {ECO:0000269|PubMed:18653891,
CC ECO:0000269|PubMed:23532072}.
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 Evidence={ECO:0000269|PubMed:23532072};
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; Evidence={ECO:0000269|PubMed:23532072};
CC -!- SUBUNIT: Interacts with BRI1 (PubMed:18653891, PubMed:23496207).
CC Interacts with ASK7/BIN2, BSK5, BSK6, BSK8 and BSK11 (PubMed:23496207).
CC Interacts with FLS2 (PubMed:23532072). {ECO:0000269|PubMed:18653891,
CC ECO:0000269|PubMed:23496207, ECO:0000269|PubMed:23532072}.
CC -!- INTERACTION:
CC Q944A7; O22476: BRI1; NbExp=4; IntAct=EBI-1797846, EBI-1797828;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18653891,
CC ECO:0000269|PubMed:23532072}; Lipid-anchor
CC {ECO:0000269|PubMed:23532072, ECO:0000305|PubMed:12912986}. Note=Plasma
CC membrane localization is required for its function in innate immunity.
CC {ECO:0000269|PubMed:23532072}.
CC -!- PTM: Phosphorylated at Ser-230 by BRI1 upon brassinolide (BL)
CC treatment. Phosphorylation at Ser-230 weakens the interaction between
CC BSK1 and BRI1 (PubMed:18653891). Phosphorylated by ASK7/BIN2 and
CC ASK9/BIL2 (PubMed:23496207). {ECO:0000269|PubMed:18653891,
CC ECO:0000269|PubMed:23496207}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18746.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80240.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL022604; CAA18746.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161587; CAB80240.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86482.1; -; Genomic_DNA.
DR EMBL; AF439824; AAL27496.1; -; mRNA.
DR EMBL; AY142063; AAM98327.1; -; mRNA.
DR PIR; T06134; T06134.
DR RefSeq; NP_567980.1; NM_119689.4.
DR AlphaFoldDB; Q944A7; -.
DR SMR; Q944A7; -.
DR BioGRID; 14958; 14.
DR IntAct; Q944A7; 1.
DR STRING; 3702.AT4G35230.1; -.
DR iPTMnet; Q944A7; -.
DR PaxDb; Q944A7; -.
DR PRIDE; Q944A7; -.
DR ProteomicsDB; 240506; -.
DR EnsemblPlants; AT4G35230.1; AT4G35230.1; AT4G35230.
DR GeneID; 829676; -.
DR Gramene; AT4G35230.1; AT4G35230.1; AT4G35230.
DR KEGG; ath:AT4G35230; -.
DR Araport; AT4G35230; -.
DR TAIR; locus:2122058; AT4G35230.
DR eggNOG; ENOG502QQT6; Eukaryota.
DR HOGENOM; CLU_000288_15_0_1; -.
DR InParanoid; Q944A7; -.
DR OMA; AIMETNL; -.
DR OrthoDB; 540417at2759; -.
DR PhylomeDB; Q944A7; -.
DR PRO; PR:Q944A7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q944A7; baseline and differential.
DR Genevisible; Q944A7; AT.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IDA:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR045845; BSK.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR45863; PTHR45863; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Brassinosteroid signaling pathway; Cell membrane; Coiled coil;
KW Kinase; Lipoprotein; Membrane; Myristate; Nucleotide-binding;
KW Phosphoprotein; Plant defense; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12912986"
FT CHAIN 2..512
FT /note="Serine/threonine-protein kinase BSK1"
FT /id="PRO_0000324844"
FT DOMAIN 76..331
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 8..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 483..508
FT /evidence="ECO:0000255"
FT COMPBIAS 19..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 198
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 82..90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 230
FT /note="Major phosphorylation site for BRI1"
FT /evidence="ECO:0000269|PubMed:18653891"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18653891"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:12912986"
FT MUTAGEN 2
FT /note="G->A: Abolishes plasma membrane localization;
FT enhances susceptibility to fungal and bacterial pathogens."
FT /evidence="ECO:0000269|PubMed:23532072"
FT MUTAGEN 104
FT /note="K->E: Abolishes kinase activity; enhances
FT susceptibility to fungal and bacterial pathogens."
FT /evidence="ECO:0000269|PubMed:23532072"
FT MUTAGEN 230
FT /note="S->A: Reduces protein phosphorylation 5-fold."
FT /evidence="ECO:0000269|PubMed:18653891"
FT MUTAGEN 443
FT /note="R->Q: In bsk1-1; enhances susceptibility to fungal
FT and bacterial pathogens."
FT /evidence="ECO:0000269|PubMed:23532072"
SQ SEQUENCE 512 AA; 56818 MW; 3087B726C5049864 CRC64;
MGCCQSLFSG DNPLGKDGVQ PQPLSQNNHG GATTADNGGS GGASGVGGGG GGGGIPSFSE
FSFADLKAAT NNFSSDNIVS ESGEKAPNLV YKGRLQNRRW IAVKKFTKMA WPEPKQFAEE
AWGVGKLRHN RLANLIGYCC DGDERLLVAE FMPNDTLAKH LFHWENQTIE WAMRLRVGYY
IAEALDYCST EGRPLYHDLN AYRVLFDEDG DPRLSCFGLM KNSRDGKSYS TNLAYTPPEY
LRNGRVTPES VTYSFGTVLL DLLSGKHIPP SHALDMIRGK NIILLMDSHL EGKFSTEEAT
VVVELASQCL QYEPRERPNT KDLVATLAPL QTKSDVPSYV MLGIKKQEEA PSTPQRPLSP
LGEACSRMDL TAIHQILVMT HYRDDEGTNE LSFQEWTQQM KDMLDARKRG DQSFREKDFK
TAIDCYSQFI DVGTMVSPTV FGRRSLCYLL CDQPDAALRD AMQAQCVYPD WPTAFYMQSV
ALAKLNMNTD AADMLNEAAQ LEEKRQRGGR GS
