BSK2_ARATH
ID BSK2_ARATH Reviewed; 489 AA.
AC Q9LS26; Q84WC2;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Serine/threonine-protein kinase BSK2 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Brassinosteroid-signaling kinase 2 {ECO:0000303|PubMed:18653891};
GN Name=BSK2 {ECO:0000303|PubMed:18653891};
GN OrderedLocusNames=At5g46570 {ECO:0000312|Araport:AT5G46570};
GN ORFNames=F10E10.4 {ECO:0000312|EMBL:BAA97528.1};
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, AND
RP PHOSPHORYLATION.
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).
CC -!- FUNCTION: Probable serine/threonine kinase that acts as positive
CC regulator of brassinosteroid (BR) signaling downstream of the receptor
CC kinase BRI1. Mediates signal transduction from BRI1 by functioning as
CC substrate of BRI1. {ECO:0000269|PubMed:18653891}.
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:0000305};
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:0000305};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18653891};
CC Lipid-anchor {ECO:0000305|PubMed:12912986}.
CC -!- PTM: Phosphorylated by BRI1 upon brassinolide (BL) treatment.
CC {ECO:0000269|PubMed:18653891}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
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DR EMBL; AB028605; BAA97528.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95399.1; -; Genomic_DNA.
DR EMBL; BT003996; AAO42035.1; -; mRNA.
DR EMBL; BT015774; AAU90064.1; -; mRNA.
DR RefSeq; NP_199469.1; NM_124027.3.
DR AlphaFoldDB; Q9LS26; -.
DR SMR; Q9LS26; -.
DR IntAct; Q9LS26; 2.
DR STRING; 3702.AT5G46570.1; -.
DR iPTMnet; Q9LS26; -.
DR PaxDb; Q9LS26; -.
DR PRIDE; Q9LS26; -.
DR ProteomicsDB; 240507; -.
DR EnsemblPlants; AT5G46570.1; AT5G46570.1; AT5G46570.
DR GeneID; 834700; -.
DR Gramene; AT5G46570.1; AT5G46570.1; AT5G46570.
DR KEGG; ath:AT5G46570; -.
DR Araport; AT5G46570; -.
DR TAIR; locus:2142315; AT5G46570.
DR eggNOG; ENOG502QS12; Eukaryota.
DR HOGENOM; CLU_000288_15_0_1; -.
DR InParanoid; Q9LS26; -.
DR OMA; CSMENRK; -.
DR OrthoDB; 431053at2759; -.
DR PhylomeDB; Q9LS26; -.
DR PRO; PR:Q9LS26; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LS26; baseline and differential.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
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; IEA:UniProtKB-KW.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IDA:TAIR.
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; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR45863; PTHR45863; 1.
DR Pfam; PF00069; Pkinase; 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; Kinase;
KW Lipoprotein; Membrane; Myristate; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12912986"
FT CHAIN 2..489
FT /note="Serine/threonine-protein kinase BSK2"
FT /id="PRO_0000443232"
FT DOMAIN 56..322
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 62..70
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:12912986"
FT CONFLICT 87
FT /note="S -> F (in Ref. 3; AAO42035)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 489 AA; 54973 MW; C37D9D6CF6F09E8A CRC64;
MGCLHSKTAN LPSSDDPSAP NKPESVNGDQ VDQEIQNFKE FELNELRKAT NGFSPSCIVS
EGGEKAPNVV YRGKLEGNHL VAIKRFSRQS WPDAQQFVVE ATGVGKLRNK RIVSLIGCCA
EGDERLLVAE YMPNDTLSKH LFHWEKQPLP WDMRVRIADY IAEALDYCNI ENRKIYHDLN
AYRILFDEEG DPRLSTFGLM KNSRDGKSYS TNLAYTPPEF LRTGRVIPES VIFSYGTILL
DLLSGKHIPP SHALDIIRGK NALLLMDSSL EGQYANDDAT KLVDLASKCL QSEAKDRPDT
KFLLSAVAPL QKQEEVASHV LMGLPKNTVI LPTMLSPLGK ACAKMDLATF HDILLKTGYR
DEEGAENELS FQEWTQQVQE MLNTKKFGDI AFRDKDFKNS IEYYSKLVGM MPVPSATVFA
RRAFSYLMTD QQELALRDAM QAQVCIPEWP TAFYLQALAL SKLGMETDAQ DMLNDGAAYD
AKRQNSWRC
