Q9XF67 · PDPK1_ARATH
- Protein3-phosphoinositide-dependent protein kinase 1
- GenePDPK1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids491 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Activity regulation
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 54-56 | ATP (UniProtKB | ChEBI) | ||||
Sequence: SYS | ||||||
Binding site | 73 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 122-124 | ATP (UniProtKB | ChEBI) | ||||
Sequence: ESC | ||||||
Binding site | 128 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 167 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 171 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 185 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | membrane | |
Molecular Function | ATP binding | |
Molecular Function | kinase activity | |
Molecular Function | phosphatidic acid binding | |
Molecular Function | phosphatidylinositol binding | |
Molecular Function | protein kinase activity | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | positive regulation of protein kinase activity | |
Biological Process | protein autophosphorylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name3-phosphoinositide-dependent protein kinase 1
- EC number
- Short namesAtPDK1
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ9XF67
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 167 | Abolishes autophosphorylation. | ||||
Sequence: D → A | ||||||
Mutagenesis | 176 | Strongly reduces autophosphorylation. | ||||
Sequence: T → A | ||||||
Mutagenesis | 177 | Reduces autophosphorylation. | ||||
Sequence: S → A | ||||||
Mutagenesis | 211 | Strongly reduces autophosphorylation. | ||||
Sequence: T → A | ||||||
Mutagenesis | 276 | Abolishes autophosphorylation. | ||||
Sequence: S → A | ||||||
Mutagenesis | 382 | Slightly reduces autophosphorylation. | ||||
Sequence: S → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 25 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_0000399902 | 1-491 | 3-phosphoinositide-dependent protein kinase 1 | |||
Sequence: MLAMEKEFDSKLVLQGNSSNGANVSRSKSFSFKAPQENFTSHDFEFGKIYGVGSYSKVVRAKKKETGTVYALKIMDKKFITKENKTAYVKLERIVLDQLEHPGIIKLYFTFQDTSSLYMALESCEGGELFDQITRKGRLSEDEARFYTAEVVDALEYIHSMGLIHRDIKPENLLLTSDGHIKIADFGSVKPMQDSQITVLPNAASDDKACTFVGTAAYVPPEVLNSSPATFGNDLWALGCTLYQMLSGTSPFKDASEWLIFQRIIARDIKFPNHFSEAARDLIDRLLDTEPSRRPGAGSEGYVALKRHPFFNGVDWKNLRSQTPPKLAPDPASQTASPERDDTHGSPWNLTHIGDSLATQNEGHSAPPTSSESSGSITRLASIDSFDSRWQQFLEPGESVLMISAVKKLQKITSKKVQLILTNKPKLIYVDPSKLVVKGNIIWSDNSNDLNVVVTSPSHFKICTPKKVLSFEDAKQRASVWKKAIETLQNR | ||||||
Modified residue | 177 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 211 | Phosphothreonine; by autocatalysis | ||||
Sequence: T | ||||||
Modified residue | 276 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 337 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 382 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with the C-terminal PIF domain of the protein kinases D6PK/AGC1-1, OXI1/AGC2-1 and PID (PubMed:14749726, PubMed:16601102).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9XF67 | AGC1-5 Q9LTW5 | 3 | EBI-1103587, EBI-1103747 | |
BINARY | Q9XF67 | AGC1-7 Q1PFB9 | 2 | EBI-1103587, EBI-1103730 | |
BINARY | Q9XF67 | D6PK Q9FG74 | 2 | EBI-1103587, EBI-1103570 | |
BINARY | Q9XF67 | D6PKL1 Q9SUA3 | 3 | EBI-1103587, EBI-1103605 | |
BINARY | Q9XF67 | D6PKL2 Q39183 | 4 | EBI-1103587, EBI-1103628 | |
BINARY | Q9XF67 | D6PKL3 Q05999 | 2 | EBI-1103587, EBI-1103648 | |
BINARY | Q9XF67 | KIPK2 Q9SJM3 | 2 | EBI-1103587, EBI-1103882 | |
BINARY | Q9XF67 | PAXL Q9LUK3 | 2 | EBI-1103587, EBI-1103691 | |
BINARY | Q9XF67 | PID O64682 | 3 | EBI-1103587, EBI-1393382 | |
BINARY | Q9XF67 | PID2 Q64FQ2 | 2 | EBI-1103587, EBI-1103769 | |
BINARY | Q9XF67 | Q8RY37 | 2 | EBI-1103587, EBI-1103670 | |
BINARY | Q9XF67 | RHS3 F4I4F2 | 2 | EBI-1103587, EBI-1103713 | |
BINARY | Q9XF67 | T18B22.10 Q9M1P3 | 2 | EBI-1103587, EBI-1103792 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 44-311 | Protein kinase | ||||
Sequence: FEFGKIYGVGSYSKVVRAKKKETGTVYALKIMDKKFITKENKTAYVKLERIVLDQLEHPGIIKLYFTFQDTSSLYMALESCEGGELFDQITRKGRLSEDEARFYTAEVVDALEYIHSMGLIHRDIKPENLLLTSDGHIKIADFGSVKPMQDSQITVLPNAASDDKACTFVGTAAYVPPEVLNSSPATFGNDLWALGCTLYQMLSGTSPFKDASEWLIFQRIIARDIKFPNHFSEAARDLIDRLLDTEPSRRPGAGSEGYVALKRHPFF | ||||||
Region | 75-119 | PIF-pocket | ||||
Sequence: MDKKFITKENKTAYVKLERIVLDQLEHPGIIKLYFTFQDTSSLYM | ||||||
Region | 77-112 | PIF-binding | ||||
Sequence: KKFITKENKTAYVKLERIVLDQLEHPGIIKLYFTFQ | ||||||
Region | 185-222 | Activation loop | ||||
Sequence: DFGSVKPMQDSQITVLPNAASDDKACTFVGTAAYVPPE | ||||||
Region | 321-377 | Disordered | ||||
Sequence: SQTPPKLAPDPASQTASPERDDTHGSPWNLTHIGDSLATQNEGHSAPPTSSESSGSI | ||||||
Compositional bias | 336-377 | Polar residues | ||||
Sequence: ASPERDDTHGSPWNLTHIGDSLATQNEGHSAPPTSSESSGSI | ||||||
Domain | 386-491 | PH | ||||
Sequence: FDSRWQQFLEPGESVLMISAVKKLQKITSKKVQLILTNKPKLIYVDPSKLVVKGNIIWSDNSNDLNVVVTSPSHFKICTPKKVLSFEDAKQRASVWKKAIETLQNR |
Domain
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
This entry describes 1 isoforms produced by Alternative splicing. A number of isoforms are produced. According to EST sequences.
Q9XF67-1
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
- Length491
- Mass (Da)54,711
- Last updated1999-11-01 v1
- Checksum2319EE69CDB5CB38
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F4JWB0 | F4JWB0_ARATH | PDK1 | 408 | ||
A0A1P8BAG1 | A0A1P8BAG1_ARATH | PDK1 | 305 |
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 336-377 | Polar residues | ||||
Sequence: ASPERDDTHGSPWNLTHIGDSLATQNEGHSAPPTSSESSGSI |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF132742 EMBL· GenBank· DDBJ | AAD37165.1 EMBL· GenBank· DDBJ | mRNA | ||
AL162875 EMBL· GenBank· DDBJ | CAB85557.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
CP002688 EMBL· GenBank· DDBJ | AED90755.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF360326 EMBL· GenBank· DDBJ | AAK26036.1 EMBL· GenBank· DDBJ | mRNA | ||
AY056336 EMBL· GenBank· DDBJ | AAL07185.1 EMBL· GenBank· DDBJ | mRNA |