Serine/threonine-protein kinase BIK1 - Arabidopsis thaliana (Mouse-ear cress)

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O48814 (BIK1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 97. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

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)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › 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. Phosphorylates FLS2 and BAK1. Ref.4 Ref.6
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Interacts with FLS2 and BAK1. Ref.6
Subcellular location	Cell membrane; Lipid-anchor Ref.4.
Induction	By infection with necrotrophic pathogens and by paraquat. Not induced by salicylic acid, jasmonate or 1-aminocyclopropane-1-carboxylate (ACC). Ref.4
Post-translational modification	Phosphorylation level varies significantly during early response to general elicitors. Phosphrylated by FLS2 and BAK1.
Disruption phenotype	Plants show some altered growth traits and a severely impaired resistance to Botrytis and A.brassicicola. Ref.4
Miscellaneous	The association with FLS2 and BAK1 is reduced after flagellin perception, BIK1 being probably released from the receptor complex upon phosphorylation.
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 Reference proteome
Gene Ontology (GO)
Biological process	defense response to fungus Inferred from mutant phenotype Ref.4. Source: TAIR pathogen-associated molecular pattern dependent induction by symbiont of host innate immune response Inferred from mutant phenotype. Source: TAIR protein autophosphorylation Inferred from direct assay Ref.4. Source: TAIR
Cellular component	cytoplasm Inferred from direct assay. Source: TAIR nucleolus Inferred from direct assay. Source: TAIR plasma membrane Inferred from direct assay Ref.4 Ref.5. Source: TAIR
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Potential

Chain

2 – 395

394

Serine/threonine-protein kinase BIK1

PRO_0000311118

Regions

Domain

67 – 356

290

Protein kinase

Nucleotide binding

73 – 81

ATP By similarity

Sites

Active site

202

Proton acceptor By similarity

Binding site

105

ATP By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.5

Modified residue

237

Phosphothreonine Ref.6

Lipidation

N-myristoyl glycine Potential

Lipidation

S-palmitoyl cysteine Potential

Sequences

Sequence

Length

Mass (Da)

Tools

O48814 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 4C06B1FD01889440
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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

« Hide

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. Venter J.C. Nature 402:761-768(1999) [PubMed: 10617197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"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. Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"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.
[5]	"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. Strain: cv. Columbia.
[6]	"Phosphorylation of receptor-like cytoplasmic kinases by bacterial flagellin." Lu D., Wu S., He P., Shan L. Plant Signal. Behav. 5:598-600(2010) [PubMed: 20404519] [Abstract] Cited for: FUNCTION, INTERACTION WITH FLS2 AND BAK1, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT THR-237.
+	Additional computationally mapped references.

Web resources

PlantP kinase Classification PPC

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC003674 Genomic DNA. Translation: AAB97121.1. AC004218 Genomic DNA. Translation: AAM14921.1. CP002685 Genomic DNA. Translation: AEC09703.1. 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. NM_129522.4.
UniGene	At.21254.
3D structure databases
ProteinModelPortal	O48814.
SMR	O48814. Positions 57-354.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-51510N.
IntAct	O48814. 2 interactions.
STRING	O48814.
Proteomic databases
PRIDE	O48814.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G39660.1; AT2G39660.1; AT2G39660.
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.
Phylogenomic databases
eggNOG	KOG1187.
GeneTree	EPGT00050000000099.
HOGENOM	HBG755340.
InParanoid	O48814.
OMA	ADIFHNG.
PhylomeDB	O48814.
ProtClustDB	CLSN2683363.
Gene expression databases
ArrayExpress	O48814.
Genevestigator	O48814.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR001245. Ser-Thr/Tyr_kinase. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF07714. Pkinase_Tyr. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
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:	December 14, 2011
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents