Q94F62 · BAK1_ARATH
- ProteinBRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1
- GeneBAK1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids615 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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).
Component of the RLP23-SOBIR1-BAK1 complex that mediates NLP-triggered immunity (PubMed:27251392).
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).
Required during SCOOP small peptides (e.g. RGF1, SCOOP10 and SCOOP12) perception and signaling; associates with MIK2 as a coreceptor upon MIK2 perception of SCOOP peptides, and relays the signaling through the activation of receptor-like cytosolic kinases (RLCKs) BIK1 and PBL1 (Probable) (PubMed:30715439, PubMed:34535661).
Miscellaneous
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Features
Showing features for site, binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 52 | Interacts with flagellin flg22 | ||||
Sequence: T | ||||||
Site | 54 | Interacts with flagellin flg22; via amide nitrogen | ||||
Sequence: V | ||||||
Binding site | 59 | brassinolide (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 60 | brassinolide (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 61 | brassinolide (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 62 | brassinolide (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 295-303 | ATP (UniProtKB | ChEBI) | ||||
Sequence: LGRGGFGKV | ||||||
Binding site | 317 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 364 | ATP (UniProtKB | ChEBI) | ||||
Sequence: P | ||||||
Binding site | 365 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 366 | ATP (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Active site | 416 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 418 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endosome membrane | |
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | identical protein binding | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Molecular Function | receptor serine/threonine kinase binding | |
Molecular Function | signaling receptor binding | |
Molecular Function | transmembrane receptor protein tyrosine kinase activity | |
Biological Process | defense response |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1
- EC number
- Short namesAtBAK1 ; BRI1-associated receptor kinase 1
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ94F62
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 26-225 | Extracellular | ||||
Sequence: NAEGDALSALKNSLADPNKVLQSWDATLVTPCTWFHVTCNSDNSVTRVDLGNANLSGQLVMQLGQLPNLQYLELYSNNITGTIPEQLGNLTELVSLDLYLNNLSGPIPSTLGRLKKLRFLRLNNNSLSGEIPRSLTAVLTLQVLDLSNNPLTGDIPVNGSFSLFTPISFANTKLTPLPASPPPPISPTPPSPAGSNRITG | ||||||
Transmembrane | 226-246 | Helical | ||||
Sequence: AIAGGVAAGAALLFAVPAIAL | ||||||
Topological domain | 247-615 | Cytoplasmic | ||||
Sequence: AWWRRKKPQDHFFDVPAEEDPEVHLGQLKRFSLRELQVASDNFSNKNILGRGGFGKVYKGRLADGTLVAVKRLKEERTQGGELQFQTEVEMISMAVHRNLLRLRGFCMTPTERLLVYPYMANGSVASCLRERPESQPPLDWPKRQRIALGSARGLAYLHDHCDPKIIHRDVKAANILLDEEFEAVVGDFGLAKLMDYKDTHVTTAVRGTIGHIAPEYLSTGKSSEKTDVFGYGVMLLELITGQRAFDLARLANDDDVMLLDWVKGLLKEKKLEALVDVDLQGNYKDEEVEQLIQVALLCTQSSPMERPKMSEVVRMLEGDGLAERWEEWQKEEMFRQDFNYPTHHPAVSGWIIGDSTSQIENEYPSGPR |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Partially compromised SCOOP10- and SCOOP12-induced root growth inhibition and reactive oxygen species (ROS) production; fully compromised in the double mutant bak1-5 serk4 (PubMed:34535661).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 30 | No effect on flg22 induced FLS2-BAK1 heterodimerization. | ||||
Sequence: D → Y | ||||||
Mutagenesis | 32 | Loss of binding to BRI1, but no effect on kinase activity. | ||||
Sequence: L → E | ||||||
Mutagenesis | 46 | Loss of binding to BRI1 and loss of kinase activity. | ||||
Sequence: L → E | ||||||
Mutagenesis | 60 | Loss of flg22 induced FLS2-BAK1 heterodimerization. | ||||
Sequence: F → A | ||||||
Mutagenesis | 64 | No effect. | ||||
Sequence: C → Y | ||||||
Mutagenesis | 94 | No effect. | ||||
Sequence: L → E | ||||||
Mutagenesis | 96 | Loss of flg22 induced FLS2-BAK1 heterodimerization. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 121 | No effect. | ||||
Sequence: L → E | ||||||
Mutagenesis | 122 | Hypersensitivity to brassinosteroids and enhanced high-light phototropism. | ||||
Sequence: D → N | ||||||
Mutagenesis | 144 | Loss of flg22 induced FLS2-BAK1 heterodimerization. | ||||
Sequence: F → A | ||||||
Mutagenesis | 172 | No effect. | ||||
Sequence: S → F | ||||||
Mutagenesis | 286 | No effect. | ||||
Sequence: S → A | ||||||
Mutagenesis | 286 | Loss of kinase activity. | ||||
Sequence: S → D | ||||||
Mutagenesis | 290 | Reduced kinase activity. Reduced interaction with BIR2. | ||||
Sequence: S → A | ||||||
Mutagenesis | 290 | Normal interaction with BIR2. | ||||
Sequence: S → D | ||||||
Mutagenesis | 312 | No effect on the kinase activity or on the binding to the FHA domain of KAPP. Reduced interaction with BIR2. | ||||
Sequence: T → A | ||||||
Mutagenesis | 312 | Reduced interaction with BIR2. | ||||
Sequence: T → D | ||||||
Mutagenesis | 317 | 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. | ||||
Sequence: K → E | ||||||
Mutagenesis | 363 | Loss of autophosphorylation. | ||||
Sequence: Y → G or A | ||||||
Mutagenesis | 416 | Loss of phosphorylation. | ||||
Sequence: D → A | ||||||
Mutagenesis | 421 | Loss of phosphorylation. | ||||
Sequence: N → A | ||||||
Mutagenesis | 439 | No effect on some phosphorylation sites. | ||||
Sequence: K → A | ||||||
Mutagenesis | 446 | No effect. Reduced interaction with BIR2. Loss of kinase activity; when associated with D-449 and D-450. | ||||
Sequence: T → A or D | ||||||
Mutagenesis | 449 | 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. | ||||
Sequence: T → A or D | ||||||
Mutagenesis | 450 | 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. | ||||
Sequence: T → A or D | ||||||
Mutagenesis | 451 | Loss of kinase activity and loss of interaction with hopAB2/AvrPtoB. Reduced interaction with BIR2. | ||||
Sequence: A → E | ||||||
Mutagenesis | 452 | Strongly decreased kinase activity and loss of interaction with hopAB2/AvrPtoB. | ||||
Sequence: V → D | ||||||
Mutagenesis | 453 | No effect on some phosphorylation sites. | ||||
Sequence: R → A | ||||||
Mutagenesis | 455 | Loss of kinase activity. | ||||
Sequence: T → A, D, or E | ||||||
Mutagenesis | 455 | Loss of kinase activity and loss of interaction with hopAB2/AvrPtoB. | ||||
Sequence: T → N | ||||||
Mutagenesis | 456 | Loss of kinase activity and loss of interaction with hopAB2/AvrPtoB. | ||||
Sequence: I → D | ||||||
Mutagenesis | 458 | Loss of kinase activity, loss of phosphorylation and loss of interaction with hopAB2/AvrPtoB. | ||||
Sequence: H → D | ||||||
Mutagenesis | 464 | Loss of kinase activity and loss of interaction with hopAB2/AvrPtoB. | ||||
Sequence: L → D | ||||||
Mutagenesis | 495 | Loss of kinase activity and loss of interaction with hopAB2/AvrPtoB. | ||||
Sequence: A → E | ||||||
Mutagenesis | 546 | 60% decrease of binding to the FHA domain of KAPP. | ||||
Sequence: T → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 3 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-25 | |||||
Sequence: MERRLMIPCFFWLILVLDLVLRVSG | ||||||
Chain | PRO_0000024304 | 26-615 | BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1 | |||
Sequence: NAEGDALSALKNSLADPNKVLQSWDATLVTPCTWFHVTCNSDNSVTRVDLGNANLSGQLVMQLGQLPNLQYLELYSNNITGTIPEQLGNLTELVSLDLYLNNLSGPIPSTLGRLKKLRFLRLNNNSLSGEIPRSLTAVLTLQVLDLSNNPLTGDIPVNGSFSLFTPISFANTKLTPLPASPPPPISPTPPSPAGSNRITGAIAGGVAAGAALLFAVPAIALAWWRRKKPQDHFFDVPAEEDPEVHLGQLKRFSLRELQVASDNFSNKNILGRGGFGKVYKGRLADGTLVAVKRLKEERTQGGELQFQTEVEMISMAVHRNLLRLRGFCMTPTERLLVYPYMANGSVASCLRERPESQPPLDWPKRQRIALGSARGLAYLHDHCDPKIIHRDVKAANILLDEEFEAVVGDFGLAKLMDYKDTHVTTAVRGTIGHIAPEYLSTGKSSEKTDVFGYGVMLLELITGQRAFDLARLANDDDVMLLDWVKGLLKEKKLEALVDVDLQGNYKDEEVEQLIQVALLCTQSSPMERPKMSEVVRMLEGDGLAERWEEWQKEEMFRQDFNYPTHHPAVSGWIIGDSTSQIENEYPSGPR | ||||||
Disulfide bond | 57↔64 | |||||
Sequence: CTWFHVTC | ||||||
Glycosylation | 79 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 103 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 114 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 127 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 149 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 183 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 286 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 290 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 312 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 370 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 373 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 446 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 449 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 450 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 455 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 463 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 465 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 466 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 470 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 546 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 589 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 595 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 604 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 612 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Induction
Gene expression databases
Interaction
Subunit
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).
Binds to IOS1 which triggers FLS2-BAK1 complex formation upon microbe-associated molecular patterns (MAMPs) treatment (PubMed:27317676).
Interacts with ERECTA in a EPF2-induced manner. Interacts with ERL1 in a EPF1-induced manner. Interacts with TMM (PubMed:26320950).
Component of a trimeric complex composed of RLP23, SOBIR1 and BAK1. BAK1 is recruited into a pre-formed RLP23-SOBIR1 complex in a ligand-dependent manner (PubMed:27251392).
In the presence of the signal peptide RGF1, interacts with RGI3/RGFR1 and RGI4/RGFR2/SKM2 (PubMed:27229311).
Forms a complex with MIK2 in response to SCOOP12 perception (PubMed:33514716, PubMed:34535661).
Binary interactions
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for motif, repeat, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 57-64 | Cys pair | ||||
Sequence: CTWFHVTC | ||||||
Repeat | 67-90 | LRR 1 | ||||
Sequence: DNSVTRVDLGNANLSGQLVMQLGQ | ||||||
Repeat | 91-115 | LRR 2 | ||||
Sequence: LPNLQYLELYSNNITGTIPEQLGNL | ||||||
Repeat | 117-139 | LRR 3 | ||||
Sequence: ELVSLDLYLNNLSGPIPSTLGRL | ||||||
Repeat | 140-163 | LRR 4 | ||||
Sequence: KKLRFLRLNNNSLSGEIPRSLTAV | ||||||
Repeat | 165-188 | LRR 5 | ||||
Sequence: TLQVLDLSNNPLTGDIPVNGSFSL | ||||||
Repeat | 190-209 | LRR 6 | ||||
Sequence: TPISFANTKLTPLPASPPPP | ||||||
Domain | 289-576 | Protein kinase | ||||
Sequence: FSNKNILGRGGFGKVYKGRLADGTLVAVKRLKEERTQGGELQFQTEVEMISMAVHRNLLRLRGFCMTPTERLLVYPYMANGSVASCLRERPESQPPLDWPKRQRIALGSARGLAYLHDHCDPKIIHRDVKAANILLDEEFEAVVGDFGLAKLMDYKDTHVTTAVRGTIGHIAPEYLSTGKSSEKTDVFGYGVMLLELITGQRAFDLARLANDDDVMLLDWVKGLLKEKKLEALVDVDLQGNYKDEEVEQLIQVALLCTQSSPMERPKMSEVVRMLEGDGLAERWEEWQ |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 1 isoforms produced by Alternative splicing. A number of isoforms are produced. According to EST sequences.
Q94F62-1
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.
- Name1
- Length615
- Mass (Da)68,161
- Last updated2003-03-28 v2
- Checksum547B3F38FB46E1DD
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F4JIX9 | F4JIX9_ARATH | BAK1 | 662 |
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 12 | in Ref. 1; AAK68074 | ||||
Sequence: W → G |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF384970 EMBL· GenBank· DDBJ | AAK68074.1 EMBL· GenBank· DDBJ | mRNA | ||
FJ708762 EMBL· GenBank· DDBJ | ACN59355.1 EMBL· GenBank· DDBJ | mRNA | ||
AL035678 EMBL· GenBank· DDBJ | CAB38801.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL161583 EMBL· GenBank· DDBJ | CAB80060.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002687 EMBL· GenBank· DDBJ | AEE86223.1 EMBL· GenBank· DDBJ | Genomic DNA |