P42818 · KPK1_ARATH
- ProteinSerine/threonine-protein kinase AtPK1/AtPK6
- GeneATPK1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids465 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Downstream effector of TOR signaling pathway involved in osmotic stress response (PubMed:20683442).
Could be involved in the control of plant growth and development (PubMed:20683442).
Phosphorylates the ribosomal proteins P14, P16 and S6 (PubMed:20683442).
Functions as a repressor of cell proliferation and required for maintenance of chromosome stability and ploidy levels through the RBR1-E2F pathway (PubMed:20683442).
Mediates the phosphorylation of MRFs (e.g. MRF1) (PubMed:29084871).
Could be involved in the control of plant growth and development (PubMed:20683442).
Phosphorylates the ribosomal proteins P14, P16 and S6 (PubMed:20683442).
Functions as a repressor of cell proliferation and required for maintenance of chromosome stability and ploidy levels through the RBR1-E2F pathway (PubMed:20683442).
Mediates the phosphorylation of MRFs (e.g. MRF1) (PubMed:29084871).
Miscellaneous
Plants overexpressing KPK1 are hypersensitive to osmotic stress.
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Activity regulation
Activated by PDK1. Repressed during osmotic stress.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | ATP binding | |
Molecular Function | kinase activity | |
Molecular Function | protein kinase activity | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | negative regulation of cell population proliferation | |
Biological Process | positive regulation of translation | |
Biological Process | protein phosphorylation | |
Biological Process | response to cold | |
Biological Process | response to osmotic stress | |
Biological Process | response to salt stress |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein kinase AtPK1/AtPK6
- EC number
- 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 accessionP42818
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 94 | Binding to RBR1 substantially diminished. | ||||
Sequence: C → R | ||||||
Mutagenesis | 163 | Activity substantially diminished. | ||||
Sequence: K → R | ||||||
Mutagenesis | 449 | Abrogation of the phosphorylation. Reduced MRF1 phosphorylation activity. | ||||
Sequence: T → A | ||||||
Mutagenesis | 449 | Phosphomimetic. No impact MRF1 phosphorylation activity. | ||||
Sequence: T → D |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 23 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000086163 | 1-465 | Serine/threonine-protein kinase AtPK1/AtPK6 | |||
Sequence: MVSSQRPVPNKIQKQQYLSISPSNSVLKDDVELEFSDVFGPLPEEANDIAYDEPAVVYSRSHSLVGPCSLDSHSLKLTKLTLLETEDSIDLVECLEGESLKENDDFSGNDDSDNEKALEGDLVKVSGVVGIDDFEVMKVVGKGAFGKVYQVRKKETSEIYAMKVMRKDHIMEKNHAEYMKAERDILTKIDHPFIVQLKYSFQTKYRLYLVLDFINGGHLFFQLYHQGLFREDLARVYTAEIVSAVSHLHEKGIMHRDLKPENILMDTDGHVMLTDFGLAKEFEENTRSNSMCGTTEYMAPEIVRGKGHDKAADWWSVGILLYEMLTGKPPFLGSKGKIQQKIVKDKIKLPQFLSNEAHAILKGLLQKEPERRLGSGLSGAEEIKQHKWFKGINWKKLEAREVMPSFKPEVSGRQCIANFDKCWTDMSVLDSPASSPSSDPKANPFTNFTYVRPPPSFLHQSTTTL | ||||||
Modified residue | 290 | Phosphoserine; by PDPK1 | ||||
Sequence: S | ||||||
Modified residue | 449 | Phosphothreonine; by TOR | ||||
Sequence: T |
Post-translational modification
Undergoes serine-specific autophosphorylation. Phosphorylated at Thr-449 by TOR.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in all tissues.
Developmental stage
Predominates during high metabolic activity in growing buds, root tips, leaf margins and germinating seeds.
Gene expression databases
Interaction
Subunit
Interacts with RAPTOR1 (PubMed:16377759).
Interacts with RBR1-E2FB complex through its LVxCxE motif (PubMed:20683442).
Interacts with TAP46 (PubMed:25399018).
Binds to MRF1 (PubMed:29084871).
Interacts with RBR1-E2FB complex through its LVxCxE motif (PubMed:20683442).
Interacts with TAP46 (PubMed:25399018).
Binds to MRF1 (PubMed:29084871).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P42818 | E2FB Q9FV71 | 3 | EBI-8107038, EBI-1774719 | |
BINARY | P42818 | RBR1 Q9LKZ3 | 2 | EBI-8107038, EBI-398590 | |
BINARY | P42818 | TIF3C1 O49160 | 2 | EBI-8107038, EBI-1635551 | |
BINARY | P42818 | TIF3H1 Q9C5Z2 | 3 | EBI-8107038, EBI-3387106 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for motif, domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 91-96 | LVxCxE motif | ||||
Sequence: LVECLE | ||||||
Domain | 134-389 | Protein kinase | ||||
Sequence: FEVMKVVGKGAFGKVYQVRKKETSEIYAMKVMRKDHIMEKNHAEYMKAERDILTKIDHPFIVQLKYSFQTKYRLYLVLDFINGGHLFFQLYHQGLFREDLARVYTAEIVSAVSHLHEKGIMHRDLKPENILMDTDGHVMLTDFGLAKEFEENTRSNSMCGTTEYMAPEIVRGKGHDKAADWWSVGILLYEMLTGKPPFLGSKGKIQQKIVKDKIKLPQFLSNEAHAILKGLLQKEPERRLGSGLSGAEEIKQHKWF | ||||||
Region | 275-301 | Activation loop | ||||
Sequence: DFGLAKEFEENTRSNSMCGTTEYMAPE | ||||||
Domain | 390-460 | AGC-kinase C-terminal | ||||
Sequence: KGINWKKLEAREVMPSFKPEVSGRQCIANFDKCWTDMSVLDSPASSPSSDPKANPFTNFTYVRPPPSFLHQ |
Domain
The activation loop within the kinase domain is the target of phosphorylation.
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length465
- Mass (Da)52,588
- Last updated1995-11-01 v1
- Checksum407133D674CA271F
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 232 | in Ref. 6; AAM61496 | ||||
Sequence: D → N |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L29030 EMBL· GenBank· DDBJ | AAA21142.1 EMBL· GenBank· DDBJ | mRNA | ||
D42056 EMBL· GenBank· DDBJ | BAA07656.1 EMBL· GenBank· DDBJ | mRNA | ||
AC012562 EMBL· GenBank· DDBJ | AAG51351.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002686 EMBL· GenBank· DDBJ | AEE74671.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002686 EMBL· GenBank· DDBJ | ANM64030.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY065230 EMBL· GenBank· DDBJ | AAL38706.1 EMBL· GenBank· DDBJ | mRNA | ||
AY096555 EMBL· GenBank· DDBJ | AAM20205.1 EMBL· GenBank· DDBJ | mRNA | ||
AY084935 EMBL· GenBank· DDBJ | AAM61496.1 EMBL· GenBank· DDBJ | mRNA |