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Protein

BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1

Gene

BAK1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Dual specificity kinase acting on both serine/threonine- and tyrosine-containing substrates. Controls the expression of genes associated with innate immunity in the absence of pathogens or elicitors. Involved in brassinosteroid (BR) signal transduction. Phosphorylates BRI1. May be involved in changing the equilibrium between plasma membrane-located BRI1 homodimers and endocytosed BRI1-BAK1 heterodimers. Interaction with MSBP1 stimulates the endocytosis of BAK1 and suppresses brassinosteroid signaling. Acts in pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI) via its interactions with FLS2 and EFR, and the phosphorylation of BIK1. Involved in programmed cell death (PCD) control. Positively regulates the BR-dependent plant growth pathway and negatively regulates the BR-independent cell-death pathway (PubMed:17583510, PubMed:17600708, PubMed:18667726, PubMed:18694562, PubMed:19124768, PubMed:20018402, PubMed:20404519, PubMed:21350342, PubMed:21693696). Phosphorylates BIR2 and thus promotes interaction with BIR2 (PubMed:24388849, PubMed:24556575). This interaction prevents interaction with FLS2 in the absence of pathogen-associated molecular patterns (PAMP) (PubMed:24388849, PubMed:24556575). Required for PSK promotion of seedling growth and protoplast expansion (PubMed:26071421). CNGC17 and AHAs form a functional cation-translocating unit that is activated by PSKR1/BAK1 and possibly other BAK1/RLK complexes (PubMed:26071421).12 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei52flg221 Publication1
Binding sitei54flg22; via amide nitrogen1 Publication1
Binding sitei297ATP; via carbonyl oxygen1 Publication1
Binding sitei317ATPPROSITE-ProRule annotation1
Active sitei416Proton acceptorPROSITE-ProRule annotation1
Binding sitei418ATP1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi295 – 303ATPPROSITE-ProRule annotation9
Nucleotide bindingi364 – 366ATP1 Publication3

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 11 Publication (EC:2.7.10.1Curated, EC:2.7.11.1Curated)
Short name:
AtBAK11 Publication
Short name:
BRI1-associated receptor kinase 11 Publication
Alternative name(s):
Protein ELONGATED
Somatic embryogenesis receptor kinase 31 Publication
Short name:
AtSERK31 Publication
Somatic embryogenesis receptor-like kinase 31 Publication
Gene namesi
Name:BAK11 Publication
Synonyms:ELG, SERK31 Publication
Ordered Locus Names:At4g33430Imported
ORF Names:F17M5.190Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G33430.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini26 – 225ExtracellularSequence analysisAdd BLAST200
Transmembranei226 – 246HelicalSequence analysisAdd BLAST21
Topological domaini247 – 615CytoplasmicSequence analysisAdd BLAST369

GO - Cellular componenti

  • endosome membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Disruption phenotypei

Semi-dwarfed phenotype, altered leaf morphology and reduced sensitivity to brassinolide and flagellin. Enhanced chlorosis and lesion formation upon pathogen infection. Bak1 and bkk1 double mutants are seedling lethal.4 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi30D → Y: No effect on flg22 induced FLS2-BAK1 heterodimerization. 1 Publication1
Mutagenesisi32L → E: Loss of binding to BRI1, but no effect on kinase activity. 1 Publication1
Mutagenesisi46L → E: Loss of binding to BRI1 and loss of kinase activity. 1 Publication1
Mutagenesisi60F → A: Loss of flg22 induced FLS2-BAK1 heterodimerization. 1 Publication1
Mutagenesisi64C → Y: No effect. 1 Publication1
Mutagenesisi94L → E: No effect. 1 Publication1
Mutagenesisi96Y → A: Loss of flg22 induced FLS2-BAK1 heterodimerization. 1 Publication1
Mutagenesisi121L → E: No effect. 1 Publication1
Mutagenesisi122D → N: Hypersensitivity to brassinosteroids and enhanced high-light phototropism. 1 Publication1
Mutagenesisi144F → A: Loss of flg22 induced FLS2-BAK1 heterodimerization. 1 Publication1
Mutagenesisi172S → F: No effect. 1 Publication1
Mutagenesisi286S → A: No effect. 1
Mutagenesisi286S → D: Loss of kinase activity. 1
Mutagenesisi290S → A: Reduced kinase activity. Reduced interaction with BIR2. 1 Publication1
Mutagenesisi290S → D: Normal interaction with BIR2. 1 Publication1
Mutagenesisi304Y → F: No effect on autophosphorylation. 1 Publication1
Mutagenesisi312T → A: No effect on the kinase activity or on the binding to the FHA domain of KAPP. Reduced interaction with BIR2. 2 Publications1
Mutagenesisi312T → D: Reduced interaction with BIR2. 1 Publication1
Mutagenesisi317K → E: Loss of kinase activity and loss of interaction with hopAB2/AvrPtoB, but no effect on the binding to the FHA domain of KAPP. Reduced interaction with BIR2. 5 Publications1
Mutagenesisi363Y → F: No effect on autophosphorylation. 1 Publication1
Mutagenesisi363Y → G or A: Loss of autophosphorylation. 1 Publication1
Mutagenesisi365Y → F: No effect on autophosphorylation. 1 Publication1
Mutagenesisi403Y → F: No effect on autophosphorylation. 1 Publication1
Mutagenesisi416D → A: Loss of phosphorylation. 1 Publication1
Mutagenesisi421N → A: Loss of phosphorylation. 1 Publication1
Mutagenesisi439K → A: No effect on some phosphorylation sites. 1 Publication1
Mutagenesisi443Y → F: No effect on autophosphorylation. 1 Publication1
Mutagenesisi446T → A or D: No effect. Reduced interaction with BIR2. Loss of kinase activity; when associated with D-449 and D-450. 2 Publications1
Mutagenesisi449T → A or D: Slight decrease of kinase activity but loss of interaction with hopAB2/AvrPtoB. Reduced interaction with BIR2. Loss of kinase activity; when associated with A-446 and D-450. 3 Publications1
Mutagenesisi450T → A or D: Loss of interaction with hopAB2/AvrPtoB and loss of phosphorylation. Reduced interaction with BIR2. Loss of kinase activity; when associated with A-446 and D-449. 4 Publications1
Mutagenesisi451A → E: Loss of kinase activity and loss of interaction with hopAB2/AvrPtoB. Reduced interaction with BIR2. 2 Publications1
Mutagenesisi452V → D: Strongly decreased kinase activity and loss of interaction with hopAB2/AvrPtoB. 1 Publication1
Mutagenesisi453R → A: No effect on some phosphorylation sites. 1 Publication1
Mutagenesisi455T → A, D or E: Loss of kinase activity. 2 Publications1
Mutagenesisi455T → N: Loss of kinase activity and loss of interaction with hopAB2/AvrPtoB. 1 Publication1
Mutagenesisi456I → D: Loss of kinase activity and loss of interaction with hopAB2/AvrPtoB. 1 Publication1
Mutagenesisi458H → D: Loss of kinase activity, loss of phosphorylation and loss of interaction with hopAB2/AvrPtoB. 2 Publications1
Mutagenesisi463Y → F: Loss of kinase activity and loss of autophosphorylation. 1 Publication1
Mutagenesisi464L → D: Loss of kinase activity and loss of interaction with hopAB2/AvrPtoB. 1 Publication1
Mutagenesisi478Y → F: No effect on autophosphorylation. 1 Publication1
Mutagenesisi495A → E: Loss of kinase activity and loss of interaction with hopAB2/AvrPtoB. 1 Publication1
Mutagenesisi530Y → F: No effect on autophosphorylation. 1 Publication1
Mutagenesisi546T → A: 60% decrease of binding to the FHA domain of KAPP. 1 Publication1
Mutagenesisi587Y → F: No effect on autophosphorylation. 1 Publication1
Mutagenesisi610Y → E: Loss of brassinosteroid signaling but no effect on programmed cell death inhibition. 1 Publication1
Mutagenesisi610Y → F: Decreased autophosphorylation on tyrosine, loss of transphosphorylation and activation of BRI1 but no effect on the binding to BRI1. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
ChainiPRO_000002430426 – 615BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1Add BLAST590

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi57 ↔ 642 Publications
Glycosylationi79N-linked (GlcNAc...)Sequence analysis1
Glycosylationi103N-linked (GlcNAc...)Sequence analysis1
Glycosylationi114N-linked (GlcNAc...)Sequence analysis1
Glycosylationi127N-linked (GlcNAc...)Sequence analysis1
Glycosylationi149N-linked (GlcNAc...)Sequence analysis1
Glycosylationi183N-linked (GlcNAc...)Sequence analysis1
Modified residuei286Phosphoserine1 Publication1
Modified residuei290Phosphoserine4 Publications1
Modified residuei312Phosphothreonine2 Publications1
Modified residuei370PhosphoserineBy similarity1
Modified residuei373PhosphoserineBy similarity1
Modified residuei446Phosphothreonine5 Publications1
Modified residuei449Phosphothreonine5 Publications1
Modified residuei450Phosphothreonine4 Publications1
Modified residuei455Phosphothreonine4 Publications1
Modified residuei463PhosphotyrosineBy similarity1
Modified residuei465PhosphoserineBy similarity1
Modified residuei466PhosphothreonineBy similarity1
Modified residuei470PhosphoserineBy similarity1
Modified residuei546PhosphothreonineCurated1
Modified residuei589Phosphothreonine1 Publication1
Modified residuei595Phosphoserine1 Publication1
Modified residuei604Phosphoserine1 Publication1
Modified residuei610Phosphotyrosine1 Publication1
Modified residuei612Phosphoserine1 Publication1

Post-translational modificationi

Autophosphorylated on Ser-290, Thr-312, Thr-446, Thr-449, Thr-455 and Tyr-610. Probable autophosphorylation on additional Tyr residues. Transphosphorylated by BRI1. It is not sure whether Thr-589 or Ser-595 is the target of the phosphorylation. The phosphorylations on Thr and Tyr are induced by brassinolide. Phosphorylation on Tyr-610 is required for brassinolide signaling, but not for flagellin signaling. Phosphorylation at Ser-286, Ser-290 Thr-446 or Thr-449 is not critical for flagellin signaling.9 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEiQ94F62.

PTM databases

iPTMnetiQ94F62.

Expressioni

Tissue specificityi

Expressed ubiquitously.1 Publication

Inductioni

Up-regulated by flagellin and harpin.1 Publication

Gene expression databases

ExpressionAtlasiQ94F62. baseline and differential.
GenevisibleiQ94F62. AT.

Interactioni

Subunit structurei

Interacts constitutively with BIR2, thereby preventing interaction with the ligand-binding LRR-RLK FLS2. Upon infection, pathogen-associated molecular patterns (PAMP) perception leads to BIR2 release from the BAK1 complex and enables the recruitment of BAK1 into the FLS2 complex (PubMed:24388849, PubMed:24556575). Heterodimer with FLS2 (PubMed:24114786). Monomer. Heterodimer with BRI1 in the endosomes. Component of the SERK1 signaling complex, composed of KAPP, CDC48A, GRF6 or GRF7, SERK1, SERK2, SERK3/BAK1 and BRI1. Interacts with the P.syringae AvrPto and hopAB2/AvrPtoB, ERD13, PEPR1 and PEPR2. Interacts (via extracellular region) with MSBP1. Interacts with the EF-Tu receptor EFR and FLS2 in a specific ligand-induced manner. Interacts with TMK4/BARK1. Part of a functional complex containing PSKR1, BAK1, CNGC17, and AHA (PubMed:26071421). Interacts with CNGC17 and PSKR1 (PubMed:26071421).22 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
At5g48380Q9ASS44EBI-617138,EBI-6298290
BRI1O224765EBI-617138,EBI-1797828
BRL1Q9ZWC85EBI-617138,EBI-590903
FLS2Q9FL283EBI-617138,EBI-1799448

GO - Molecular functioni

  • receptor serine/threonine kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi14764. 23 interactors.
DIPiDIP-34976N.
IntActiQ94F62. 8 interactors.

Structurei

Secondary structure

1615
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi27 – 37Combined sources11
Helixi45 – 48Combined sources4
Beta strandi53 – 59Combined sources7
Beta strandi62 – 64Combined sources3
Beta strandi70 – 74Combined sources5
Beta strandi81 – 83Combined sources3
Helixi86 – 90Combined sources5
Beta strandi96 – 98Combined sources3
Helixi110 – 114Combined sources5
Beta strandi120 – 122Combined sources3
Helixi134 – 137Combined sources4
Beta strandi144 – 146Combined sources3
Helixi158 – 161Combined sources4
Beta strandi167 – 169Combined sources3
Beta strandi183 – 186Combined sources4
Turni192 – 194Combined sources3
Beta strandi195 – 198Combined sources4
Helixi280 – 283Combined sources4
Turni284 – 287Combined sources4
Helixi291 – 293Combined sources3
Beta strandi294 – 296Combined sources3
Beta strandi299 – 306Combined sources8
Beta strandi309 – 311Combined sources3
Beta strandi314 – 318Combined sources5
Helixi330 – 336Combined sources7
Helixi337 – 339Combined sources3
Beta strandi351 – 353Combined sources3
Beta strandi360 – 364Combined sources5
Helixi371 – 376Combined sources6
Helixi387 – 406Combined sources20
Beta strandi407 – 410Combined sources4
Beta strandi421 – 424Combined sources4
Beta strandi430 – 432Combined sources3
Beta strandi439 – 441Combined sources3
Beta strandi443 – 446Combined sources4
Helixi456 – 458Combined sources3
Helixi461 – 466Combined sources6
Beta strandi467 – 469Combined sources3
Helixi471 – 487Combined sources17
Helixi494 – 497Combined sources4
Turni498 – 500Combined sources3
Helixi505 – 509Combined sources5
Turni510 – 513Combined sources4
Helixi518 – 520Combined sources3
Helixi524 – 526Combined sources3
Beta strandi527 – 530Combined sources4
Helixi532 – 545Combined sources14
Helixi550 – 552Combined sources3
Helixi556 – 564Combined sources9
Beta strandi569 – 571Combined sources3
Helixi577 – 581Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3TL8X-ray2.50A/D/G/H250-590[»]
3UIMX-ray2.20A258-583[»]
3ULZX-ray2.60A258-583[»]
4M7EX-ray3.60C/D26-220[»]
4MN8X-ray3.06B1-220[»]
ProteinModelPortaliQ94F62.
SMRiQ94F62.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati93 – 116LRR 1Add BLAST24
Repeati117 – 140LRR 2Add BLAST24
Repeati141 – 163LRR 3Add BLAST23
Repeati165 – 187LRR 4Add BLAST23
Domaini289 – 576Protein kinasePROSITE-ProRule annotationAdd BLAST288

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni59 – 62Brassinolide binding1 Publication4

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi57 – 64Cys pair8

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi191 – 217Pro-richAdd BLAST27

Domaini

Contains one leucine-zipper motif and one pair of conservatively spaced Cys (Cys pair) involved in forming heterodimers.

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 4 LRR (leucine-rich) repeats.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000116554.
InParanoidiQ94F62.
KOiK13416.
PhylomeDBiQ94F62.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR011009. Kinase-like_dom.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR013210. LRR_N_plant-typ.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR031048. SERK.
[Graphical view]
PANTHERiPTHR27001:SF1. PTHR27001:SF1. 1 hit.
PfamiPF00560. LRR_1. 1 hit.
PF13855. LRR_8. 1 hit.
PF08263. LRRNT_2. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q94F62-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MERRLMIPCF FWLILVLDLV LRVSGNAEGD ALSALKNSLA DPNKVLQSWD
60 70 80 90 100
ATLVTPCTWF HVTCNSDNSV TRVDLGNANL SGQLVMQLGQ LPNLQYLELY
110 120 130 140 150
SNNITGTIPE QLGNLTELVS LDLYLNNLSG PIPSTLGRLK KLRFLRLNNN
160 170 180 190 200
SLSGEIPRSL TAVLTLQVLD LSNNPLTGDI PVNGSFSLFT PISFANTKLT
210 220 230 240 250
PLPASPPPPI SPTPPSPAGS NRITGAIAGG VAAGAALLFA VPAIALAWWR
260 270 280 290 300
RKKPQDHFFD VPAEEDPEVH LGQLKRFSLR ELQVASDNFS NKNILGRGGF
310 320 330 340 350
GKVYKGRLAD GTLVAVKRLK EERTQGGELQ FQTEVEMISM AVHRNLLRLR
360 370 380 390 400
GFCMTPTERL LVYPYMANGS VASCLRERPE SQPPLDWPKR QRIALGSARG
410 420 430 440 450
LAYLHDHCDP KIIHRDVKAA NILLDEEFEA VVGDFGLAKL MDYKDTHVTT
460 470 480 490 500
AVRGTIGHIA PEYLSTGKSS EKTDVFGYGV MLLELITGQR AFDLARLAND
510 520 530 540 550
DDVMLLDWVK GLLKEKKLEA LVDVDLQGNY KDEEVEQLIQ VALLCTQSSP
560 570 580 590 600
MERPKMSEVV RMLEGDGLAE RWEEWQKEEM FRQDFNYPTH HPAVSGWIIG
610
DSTSQIENEY PSGPR
Length:615
Mass (Da):68,161
Last modified:March 28, 2003 - v2
Checksum:i547B3F38FB46E1DD
GO

Sequence cautioni

The sequence CAB38801 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAB80060 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti12W → G in AAK68074 (PubMed:11706164).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF384970 mRNA. Translation: AAK68074.1.
FJ708762 mRNA. Translation: ACN59355.1.
AL035678 Genomic DNA. Translation: CAB38801.1. Sequence problems.
AL161583 Genomic DNA. Translation: CAB80060.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE86223.1.
PIRiT05994.
RefSeqiNP_567920.1. NM_119497.5. [Q94F62-1]
UniGeneiAt.376.

Genome annotation databases

EnsemblPlantsiAT4G33430.1; AT4G33430.1; AT4G33430. [Q94F62-1]
GeneIDi829480.
GrameneiAT4G33430.1; AT4G33430.1; AT4G33430.
KEGGiath:AT4G33430.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

PlantP kinase Classification PPC

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF384970 mRNA. Translation: AAK68074.1.
FJ708762 mRNA. Translation: ACN59355.1.
AL035678 Genomic DNA. Translation: CAB38801.1. Sequence problems.
AL161583 Genomic DNA. Translation: CAB80060.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE86223.1.
PIRiT05994.
RefSeqiNP_567920.1. NM_119497.5. [Q94F62-1]
UniGeneiAt.376.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3TL8X-ray2.50A/D/G/H250-590[»]
3UIMX-ray2.20A258-583[»]
3ULZX-ray2.60A258-583[»]
4M7EX-ray3.60C/D26-220[»]
4MN8X-ray3.06B1-220[»]
ProteinModelPortaliQ94F62.
SMRiQ94F62.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi14764. 23 interactors.
DIPiDIP-34976N.
IntActiQ94F62. 8 interactors.

PTM databases

iPTMnetiQ94F62.

Proteomic databases

PRIDEiQ94F62.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G33430.1; AT4G33430.1; AT4G33430. [Q94F62-1]
GeneIDi829480.
GrameneiAT4G33430.1; AT4G33430.1; AT4G33430.
KEGGiath:AT4G33430.

Organism-specific databases

TAIRiAT4G33430.

Phylogenomic databases

HOGENOMiHOG000116554.
InParanoidiQ94F62.
KOiK13416.
PhylomeDBiQ94F62.

Miscellaneous databases

PROiQ94F62.

Gene expression databases

ExpressionAtlasiQ94F62. baseline and differential.
GenevisibleiQ94F62. AT.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR011009. Kinase-like_dom.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR013210. LRR_N_plant-typ.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR031048. SERK.
[Graphical view]
PANTHERiPTHR27001:SF1. PTHR27001:SF1. 1 hit.
PfamiPF00560. LRR_1. 1 hit.
PF13855. LRR_8. 1 hit.
PF08263. LRRNT_2. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBAK1_ARATH
AccessioniPrimary (citable) accession number: Q94F62
Secondary accession number(s): C0LGS0, Q9SZC0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: March 28, 2003
Last modified: November 30, 2016
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Interaction with BRI1 activates both receptor kinases and the full activation of either receptor kinase requires transphosphorylation by their partners. This interaction in vitro is magnesium dependent. Instantaneous heteromeric complex formation between FLS2 and BAK1 and reciprocal transphosphorylation after binding of the flagellin flg22 ligand to FLS2. The kinase activity is not required for the complex formation.
The interaction with the bacterial effectors AvrPto and AvrPtoB/hopAB2 interfers with FLS2 binding and plant immunity.
Phosphorylated residues T-450 and T-455 have stronger functional effects than other phosphorylated residues by interacting with both the catalytic and activation loops to achieve a conformational stability, locking BAK1 kinase in the active conformation.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.