Reviewed, UniProtKB/Swiss-Prot O48814 (BIK1_ARATH)

Names and origin

Protein names

Recommended name:
    Serine/threonine-protein kinase BIK1
    EC=2.7.11.1
Alternative name(s):
    Protein BOTRYTIS-INDUCED KINASE 1

Gene names

Name:	BIK1
Ordered Locus Names:	At2g39660
ORF Names:	F17A14.3, F12L6.32

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	395 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Required to activate the resistance responses to necrotrophic pathogens. Ref.3
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subcellular location	Cell membrane; Lipid-anchor. Ref.3
Induction	By infection with necrotrophic pathogens and by paraquat. Not induced by salicylic acid, jasmonate or 1-aminocyclopropane-1-carboxylate (ACC). Ref.3
Post-translational modification	Phosphorylation level varies significantly during early response to general elicitors.
Disruption phenotype	Plants show some altered growth traits and a severely impaired resistance to Botrytis and A.brassicicola. Ref.3
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Lipoprotein Myristate Palmitate Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	defense response to fungus Ref.3 Inferred from mutant phenotype. Source: TAIR protein amino acid autophosphorylation Ref.3 Inferred from direct assay. Source: TAIR
Cellular component	cytoplasm Inferred from direct assay. Source: TAIR nucleolus Inferred from direct assay. Source: TAIR plasma membrane Ref.3 Ref.4 Inferred from direct assay. Source: TAIR
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CALM	P62157	1	EBI-1238176,EBI-397403	From a different organism.
CML8	O23320	1	EBI-1238176,EBI-1237764

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Potential
	Chain	2 – 395	394	Serine/threonine-protein kinase BIK1		PRO_0000311118
Regions
	Domain	67 – 356	290	Protein kinase
	Nucleotide binding	73 – 81	9	ATP By similarity
Sites
	Active site	202	1	Proton acceptor By similarity
	Binding site	105	1	ATP By similarity
Amino acid modifications
	Modified residue	28	1	Phosphoserine Ref.4
	Lipidation	2	1	N-myristoyl glycine Potential
	Lipidation	4	1	S-palmitoyl cysteine Potential

Sequences

	Sequence		Length	Mass (Da)
	O48814-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 4C06B1FD01889440	FASTA	395	44,097
	10 20 30 40 50 60 MGSCFSSRVK ADIFHNGKSS DLYGLSLSSR KSSSTVAAAQ KTEGEILSST PVKSFTFNEL 70 80 90 100 110 120 KLATRNFRPD SVIGEGGFGC VFKGWLDEST LTPTKPGTGL VIAVKKLNQE GFQGHREWLT 130 140 150 160 170 180 EINYLGQLSH PNLVKLIGYC LEDEHRLLVY EFMQKGSLEN HLFRRGAYFK PLPWFLRVNV 190 200 210 220 230 240 ALDAAKGLAF LHSDPVKVIY RDIKASNILL DADYNAKLSD FGLARDGPMG DLSYVSTRVM 250 260 270 280 290 300 GTYGYAAPEY MSSGHLNARS DVYSFGVLLL EILSGKRALD HNRPAKEENL VDWARPYLTS 310 320 330 340 350 360 KRKVLLIVDN RLDTQYLPEE AVRMASVAVQ CLSFEPKSRP TMDQVVRALQ QLQDNLGKPS 370 380 390 QTNPVKDTKK LGFKTGTTKS SEKRFTQKPF GRHLV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [PubMed: 10617197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[3]	"The membrane-anchored BOTRYTIS-INDUCED KINASE1 plays distinct roles in Arabidopsis resistance to necrotrophic and biotrophic pathogens." Veronese P., Nakagami H., Bluhm B., AbuQamar S., Chen X., Salmeron J., Dietrich R.A., Hirt H., Mengiste T. Plant Cell 18:257-273(2006) [PubMed: 16339855] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION, DISRUPTION PHENOTYPE.
[4]	"Quantitative phosphoproteomics of early elicitor signaling in Arabidopsis." Benschop J.J., Mohammed S., O'Flaherty M., Heck A.J.R., Slijper M., Menke F.L.H. Mol. Cell. Proteomics 6:1198-1214(2007) [PubMed: 17317660] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AC003674 Genomic DNA. Translation: AAB97121.1. AC004218 Genomic DNA. Translation: AAM14921.1. AF325086 mRNA. Translation: AAK17154.1. AY062493 mRNA. Translation: AAL32571.1. AY065029 mRNA. Translation: AAL57667.1. AY093278 mRNA. Translation: AAM13277.1. AY093997 mRNA. Translation: AAM16258.1.
IPI	IPI00518414.
PIR	T00574.
RefSeq	NP_181496.1.
UniGene	At.21254
3D structure databases
HSSP	HSSP built from PDB template 2HCK based on UniProtKB P08631.
ModBase	Search...
Protein-protein interaction databases
IntAct	O48814. 2 interactions.
Proteomic databases
PRIDE	O48814.
Genome annotation databases
GeneID	818549.
GenomeReviews	Gene locus AT2G39660 in contig CT485783_GR.
KEGG	ath:AT2G39660.
NMPDR	fig|3702.1.peg.11080.
Organism-specific databases
GeneFarm	1713. 129.
TAIR	At2g39660.
Enzyme and pathway databases
BRENDA	2.7.11.1. 302.
Gene expression databases
ArrayExpress	O48814.
Family and domain databases
InterPro	IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BIK1_ARATH

Accession

Primary (citable) accession number: O48814

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	June 1, 1998
Last modified:	July 7, 2009
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)