BSK6_ARATH
ID BSK6_ARATH Reviewed; 490 AA.
AC Q9M324; Q8LEG7;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Serine/threonine-protein kinase BSK6 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Brassinosteroid-signaling kinase 6 {ECO:0000303|PubMed:23496207};
GN Name=BSK6 {ECO:0000303|PubMed:23496207};
GN OrderedLocusNames=At3g54030 {ECO:0000312|Araport:AT3G54030};
GN ORFNames=F5K20_330 {ECO:0000312|EMBL:CAB88365.1};
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=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 [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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-373, AND
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [9]
RP FUNCTION, INTERACTION WITH BRI1; ASK7/BIN2; ASK9/BIL2; BSK1; BSK5; BSK8 AND
RP BSK11, PHOSPHORYLATION, AND MUTAGENESIS OF SER-210.
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: Probable serine/threonine kinase that acts as positive
CC regulator of brassinosteroid (BR) signaling downstream of the receptor
CC kinase BRI1. Functions redundantly with BSK3, BSK4, BSK7 and BSK8.
CC {ECO:0000269|PubMed:23496207}.
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 -!- SUBUNIT: Interacts with BRI1, ASK7/BIN2, ASK9/BIL2, BSK1, BSK5, BSK8
CC and BSK11. {ECO:0000269|PubMed:23496207}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:12912986};
CC Lipid-anchor {ECO:0000305|PubMed:12912986}.
CC -!- PTM: Phosphorylated by BRI1, ASK7/BIN2 and ASK9/BIL2.
CC {ECO:0000269|PubMed:23496207}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
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DR EMBL; AL132960; CAB88365.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79177.1; -; Genomic_DNA.
DR EMBL; AY054503; AAK96694.1; -; mRNA.
DR EMBL; BT002089; AAN72100.1; -; mRNA.
DR EMBL; AY085422; AAM62649.1; -; mRNA.
DR RefSeq; NP_190971.1; NM_115263.4.
DR AlphaFoldDB; Q9M324; -.
DR SMR; Q9M324; -.
DR STRING; 3702.AT3G54030.1; -.
DR iPTMnet; Q9M324; -.
DR PaxDb; Q9M324; -.
DR PRIDE; Q9M324; -.
DR ProteomicsDB; 240482; -.
DR EnsemblPlants; AT3G54030.1; AT3G54030.1; AT3G54030.
DR GeneID; 824570; -.
DR Gramene; AT3G54030.1; AT3G54030.1; AT3G54030.
DR KEGG; ath:AT3G54030; -.
DR Araport; AT3G54030; -.
DR TAIR; locus:2084475; AT3G54030.
DR eggNOG; ENOG502QS12; Eukaryota.
DR HOGENOM; CLU_000288_15_0_1; -.
DR InParanoid; Q9M324; -.
DR OMA; GQWIAIK; -.
DR OrthoDB; 560276at2759; -.
DR PhylomeDB; Q9M324; -.
DR PRO; PR:Q9M324; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M324; baseline and differential.
DR GO; GO:0005886; C:plasma membrane; HDA: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; 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; Kinase;
KW Lipoprotein; Membrane; Myristate; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12912986"
FT CHAIN 2..490
FT /note="Serine/threonine-protein kinase BSK6"
FT /id="PRO_0000443236"
FT DOMAIN 56..310
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
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 MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:14506206,
FT ECO:0007744|PubMed:15308754, ECO:0007744|PubMed:19245862"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15308754"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:12912986"
FT MUTAGEN 210
FT /note="S->A: Slightly reduces BSK6 protein
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:23496207"
FT CONFLICT 445
FT /note="A -> T (in Ref. 4; AAM62649)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 490 AA; 54789 MW; 94C34BE1D4F2FC57 CRC64;
MGARCSKFSF CLFPSHFKSA SVLESPDIEN GGKVWPTFKE FKLEQLKSAT GGFSSDNIVS
EHGEKAPNVV YRGRLDDGRL IAVKRFNRLA WADHRQFLDE AKAVGSLRSD RLANLIGCCF
EGEERLLVAE FMPHETLAKH LFHWENNPMK WAMRLRVALC LAQALEYCSN KGRALYHDLN
AYRVLFDKDG NPRLSCFGLM KNSRDGKSYS TNLAFTPPEY LRTGRVTPES VVFSFGTVLL
DLMSGKHIPP SHALDLIRGK NCAMLMDSAL EGHFSNEDGT ELVRLATRCL QYEARERPNV
KSLVTSLVTL QKESDVASYV LMGIPHETEA EEESPLSLTP FGDACLRVDL TAIQEILSKI
GYKDDEGIAN ELSFQMWTNQ MQESLNSKKQ GDLAFRSKDF TTAVDCYTQF IDGGTMVSPT
VHARRCLSYL MNDNAQEALT DALQAQVVSP DWPTALYLQA ACLFKLGMEA DAQQALKDGT
TLEAKKSNKR
