Q6A1A2 · PDPK2_HUMAN
- ProteinPutative 3-phosphoinositide-dependent protein kinase 2
- GenePDPK2P
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids396 (go to sequence)
- Protein existenceUncertain
- Annotation score4/5
Function
function
Phosphorylates and activates not only PKB/AKT, but also PKA, PKC-zeta, RPS6KA1 and RPS6KB1. May play a general role in signaling processes and in development (By similarity).
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 65-67 | ATP (UniProtKB | ChEBI) | ||||
Sequence: SFS | ||||||
Binding site | 84 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 133-135 | ATP (UniProtKB | ChEBI) | ||||
Sequence: SYA | ||||||
Binding site | 139 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 178 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 182 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 196 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | membrane | |
Molecular Function | ATP binding | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | intracellular signal transduction |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePutative 3-phosphoinositide-dependent protein kinase 2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ6A1A2
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000341967 | 1-396 | UniProt | Putative 3-phosphoinositide-dependent protein kinase 2 | |||
Sequence: MVRTQTESSTPPGIPGGSRQGPAMDGTAAEPRPGAGSLQHAQPPPQPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMYIQITDFGTAKVLSPESKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFRAGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLDATKRLGCEEMEGYGPLKAHPFFESVTWENLHQQTPPKLTAYLPAMSEDDEDCYGNVSWPGWRARQVALGPPCTGLHARAPDPRVICSRKGRVSVPLRQACWWL | |||||||
Modified residue (large scale data) | 9 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 10 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 37 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 214 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 218 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Phosphorylated on tyrosine and serine/threonine.
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-15 | Polar residues | ||||
Sequence: MVRTQTESSTPPGIP | ||||||
Region | 1-53 | Disordered | ||||
Sequence: MVRTQTESSTPPGIPGGSRQGPAMDGTAAEPRPGAGSLQHAQPPPQPRKKRPE | ||||||
Domain | 55-315 | Protein kinase | ||||
Sequence: FKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMYIQITDFGTAKVLSPESKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFRAGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLDATKRLGCEEMEGYGPLKAHPFF | ||||||
Region | 86-130 | PIF-pocket | ||||
Sequence: LEKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYF |
Domain
The PIF-pocket is a small lobe in the catalytic domain required by the enzyme for the binding to the hydrophobic motif of its substrates. It is an allosteric regulatory site that can accommodate small compounds acting as allosteric inhibitors.
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length396
- Mass (Da)44,765
- Last updated2004-09-13 v1
- ChecksumA0661913B473D8DF
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-15 | Polar residues | ||||
Sequence: MVRTQTESSTPPGIP |
Keywords
- Technical term