Q1PDV6 · PBL27_ARATH
- ProteinSerine/threonine-protein kinase PBL27
- GenePBL27
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids513 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Receptor-like cytoplasmic kinase involved in the transduction of signal between the host cell surface chitin receptor complex CERK1-LYK5 and the intracellular MAPKKK5-dependent mitogen-activated protein kinase (MAPK) cascade that leads to chitin-induced immunity (PubMed:24750441, PubMed:27679653).
Phosphorylates and activates MAPKKK5 when phosphorylated by CERK1 after elicitation by chitin (PubMed:27679653).
Phosphorylates and activates MAPKKK5 when phosphorylated by CERK1 after elicitation by chitin (PubMed:27679653).
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | protein kinase activity | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | cellular response to chitin | |
Biological Process | defense response to fungus | |
Biological Process | innate immune response | |
Biological Process | positive regulation of defense response to bacterium | |
Biological Process | positive regulation of MAPK cascade | |
Biological Process | regulation of defense response to fungus | |
Biological Process | regulation of innate immune response |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein kinase PBL27
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ1PDV6
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Impaired chitin-induced defense responses such as MAPK activation (e.g. MPK3/6) and callose deposition leading to reduced disease resistance against fungal (e.g. A.brassicicola) and bacterial (e.g. P.syringae pv. tomato DC3000 hrcC) infections.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 112 | No autophosphorylation activity. Directly phosphorylated by CERK1 in vitro. Impaired CERK1-mediated phosphorylation; when associated with A-244; A-245 and A-250. | ||||
Sequence: K → E | ||||||
Mutagenesis | 244 | Impaired CERK1-mediated phosphorylation; when associated with E-112; A-245 and A-250. | ||||
Sequence: S → A | ||||||
Mutagenesis | 245 | Impaired CERK1-mediated phosphorylation; when associated with E-112; A-244 and A-250. | ||||
Sequence: T → A | ||||||
Mutagenesis | 250 | Impaired CERK1-mediated phosphorylation; when associated with E-112; A-244 and A-245. | ||||
Sequence: T → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 11 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, lipidation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000438618 | 1-513 | Serine/threonine-protein kinase PBL27 | |||
Sequence: MSGCLPCFGSSAKDAASKDSVKKELSAKDGSVTQSHHISLDKSKSRRGPEQKKELTAPKEGPTAHIAAQTFTFRELAAATKNFRPECLLGEGGFGRVYKGRLETTGQIVAVKQLDRNGLQGNREFLVEVLMLSLLHHPNLVNLIGYCADGDQRLLVYEYMPLGSLEDHLHDLPPDKEPLDWSTRMTIAAGAAKGLEYLHDKANPPVIYRDLKSSNILLGDGYHPKLSDFGLAKLGPVGDKTHVSTRVMGTYGYCAPEYAMTGQLTLKSDVYSFGVVFLELITGRKAIDNARAPGEHNLVAWARPLFKDRRKFPKMADPSLQGRYPMRGLYQALAVAAMCLQEQAATRPLIGDVVTALTYLASQTFDPNAPSGQNSRSGSGPPFIRTRDDRRSLGDGSSLDSPAETRSRLGSPATHKNSPDYRRRDMVREVNAGSEGGSETGGGSGRKWGLSDLEGQESQRGSPASVGRSSRGTPRNRDLDRERAVAEAKVWGENWRERKRATNGPGSFDSTND | ||||||
Lipidation | 4 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Lipidation | 7 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Modified residue | 244 | Phosphoserine; by CERK1 | ||||
Sequence: S | ||||||
Modified residue | 245 | Phosphothreonine; by CERK1 | ||||
Sequence: T | ||||||
Modified residue | 250 | Phosphothreonine; by CERK1 | ||||
Sequence: T | ||||||
Modified residue | 392 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 401 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated by CERK1 upon elicitation by chitin.
Palmitoylation at Cys-4 and Cys-7 are required for plasma membrane location.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
Levels are regulated in a proteasome-dependent manner (at proteome level).
Gene expression databases
Interaction
Subunit
Interacts with CERK1 (preferentially unphosphorylated) at the plasma membrane (PubMed:24750441, PubMed:27679653).
Binds to MAPKKK5 at the plasma membrane; disassociation is induced by chitin perception by the CERK1 complex. Associates also with MAPKKK3 (PubMed:27679653).
Binds to MAPKKK5 at the plasma membrane; disassociation is induced by chitin perception by the CERK1 complex. Associates also with MAPKKK3 (PubMed:27679653).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-61 | Disordered | ||||
Sequence: MSGCLPCFGSSAKDAASKDSVKKELSAKDGSVTQSHHISLDKSKSRRGPEQKKELTAPKEG | ||||||
Compositional bias | 16-30 | Basic and acidic residues | ||||
Sequence: ASKDSVKKELSAKDG | ||||||
Compositional bias | 39-59 | Basic and acidic residues | ||||
Sequence: SLDKSKSRRGPEQKKELTAPK | ||||||
Domain | 83-360 | Protein kinase | ||||
Sequence: FRPECLLGEGGFGRVYKGRLETTGQIVAVKQLDRNGLQGNREFLVEVLMLSLLHHPNLVNLIGYCADGDQRLLVYEYMPLGSLEDHLHDLPPDKEPLDWSTRMTIAAGAAKGLEYLHDKANPPVIYRDLKSSNILLGDGYHPKLSDFGLAKLGPVGDKTHVSTRVMGTYGYCAPEYAMTGQLTLKSDVYSFGVVFLELITGRKAIDNARAPGEHNLVAWARPLFKDRRKFPKMADPSLQGRYPMRGLYQALAVAAMCLQEQAATRPLIGDVVTALTYL | ||||||
Compositional bias | 365-381 | Polar residues | ||||
Sequence: FDPNAPSGQNSRSGSGP | ||||||
Region | 365-513 | Disordered | ||||
Sequence: FDPNAPSGQNSRSGSGPPFIRTRDDRRSLGDGSSLDSPAETRSRLGSPATHKNSPDYRRRDMVREVNAGSEGGSETGGGSGRKWGLSDLEGQESQRGSPASVGRSSRGTPRNRDLDRERAVAEAKVWGENWRERKRATNGPGSFDSTND | ||||||
Compositional bias | 398-414 | Polar residues | ||||
Sequence: SLDSPAETRSRLGSPAT | ||||||
Compositional bias | 455-472 | Polar residues | ||||
Sequence: GQESQRGSPASVGRSSRG | ||||||
Compositional bias | 473-503 | Basic and acidic residues | ||||
Sequence: TPRNRDLDRERAVAEAKVWGENWRERKRATN |
Sequence similarities
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length513
- Mass (Da)55,931
- Last updated2011-05-03 v1
- Checksum9FC534796025AB87
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 16-30 | Basic and acidic residues | ||||
Sequence: ASKDSVKKELSAKDG | ||||||
Compositional bias | 39-59 | Basic and acidic residues | ||||
Sequence: SLDKSKSRRGPEQKKELTAPK | ||||||
Compositional bias | 365-381 | Polar residues | ||||
Sequence: FDPNAPSGQNSRSGSGP | ||||||
Compositional bias | 398-414 | Polar residues | ||||
Sequence: SLDSPAETRSRLGSPAT | ||||||
Compositional bias | 455-472 | Polar residues | ||||
Sequence: GQESQRGSPASVGRSSRG | ||||||
Compositional bias | 473-503 | Basic and acidic residues | ||||
Sequence: TPRNRDLDRERAVAEAKVWGENWRERKRATN |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC051627 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC069328 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CP002688 EMBL· GenBank· DDBJ | AED92585.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002688 EMBL· GenBank· DDBJ | AED92586.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002688 EMBL· GenBank· DDBJ | ANM70412.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DQ446962 EMBL· GenBank· DDBJ | ABE66165.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ653292 EMBL· GenBank· DDBJ | ABK28701.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. |