Q9HEP7 · KAPR_BLUGR
- ProteincAMP-dependent protein kinase regulatory subunit
- Genepkar
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids389 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 129-258 | 3',5'-cyclic AMP 1 (UniProtKB | ChEBI) | ||||
Sequence: LFNHLDDEQSAQVLGALVEKPIPVKDIKVISQGDQGDFFYVVEKGSFDVYVNPAGSVQPGLGGLGNKVATIEPGGSFGELALMYNAPRAATVISAEGSCTLWSLDRITFRRILMDSTFKCRRLYESFLEE | ||||||
Binding site | 207 | 3',5'-cyclic AMP 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 216 | 3',5'-cyclic AMP 1 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 261-377 | 3',5'-cyclic AMP 2 (UniProtKB | ChEBI) | ||||
Sequence: LLSTLTKYERSKIADALVTLKYPAGTTIKEGDVGEEFYLLESGEAEAFKAGCQNAVKCYSKGDYFGELALLNDAPRAASVVSKTEVKVAKLGKDGFQRLLGPVESIMRRTKYEGVEE | ||||||
Binding site | 327 | 3',5'-cyclic AMP 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 336 | 3',5'-cyclic AMP 2 (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cAMP-dependent protein kinase complex | |
Molecular Function | cAMP binding | |
Molecular Function | cAMP-dependent protein kinase regulator activity | |
Biological Process | regulation of protein phosphorylation |
Keywords
- Ligand
Names & Taxonomy
Protein names
- Recommended namecAMP-dependent protein kinase regulatory subunit
- Short namesPKA regulatory subunit
Gene names
Organism names
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Leotiomycetes > Erysiphales > Erysiphaceae > Blumeria
Accessions
- Primary accessionQ9HEP7
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000205403 | 1-389 | cAMP-dependent protein kinase regulatory subunit | |||
Sequence: MSENTFPGRLGINPFGPESRAANTEKPSTSHIVRVTERDEDKVNPTFNNKPLKKFAGDRATNTPLQAFKLGASDGFPEHYGMGRRTSVSAESLNPNPTASSNESWTPPYHRKTPEQLERLKKSISGNFLFNHLDDEQSAQVLGALVEKPIPVKDIKVISQGDQGDFFYVVEKGSFDVYVNPAGSVQPGLGGLGNKVATIEPGGSFGELALMYNAPRAATVISAEGSCTLWSLDRITFRRILMDSTFKCRRLYESFLEEVTLLSTLTKYERSKIADALVTLKYPAGTTIKEGDVGEEFYLLESGEAEAFKAGCQNAVKCYSKGDYFGELALLNDAPRAASVVSKTEVKVAKLGKDGFQRLLGPVESIMRRTKYEGVEEIDREFPGSAAAL | ||||||
Modified residue | 87 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Interaction
Subunit
Tetramer, composed of 2 regulatory (R) and 2 catalytic (C) subunits. In the presence of cAMP it dissociates into 2 active monomeric C subunits and an R dimer (By similarity).
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-57 | Disordered | ||||
Sequence: MSENTFPGRLGINPFGPESRAANTEKPSTSHIVRVTERDEDKVNPTFNNKPLKKFAG | ||||||
Region | 1-128 | Dimerization and phosphorylation | ||||
Sequence: MSENTFPGRLGINPFGPESRAANTEKPSTSHIVRVTERDEDKVNPTFNNKPLKKFAGDRATNTPLQAFKLGASDGFPEHYGMGRRTSVSAESLNPNPTASSNESWTPPYHRKTPEQLERLKKSISGNF | ||||||
Compositional bias | 31-47 | Basic and acidic residues | ||||
Sequence: HIVRVTERDEDKVNPTF | ||||||
Compositional bias | 87-109 | Polar residues | ||||
Sequence: SVSAESLNPNPTASSNESWTPPY | ||||||
Region | 87-110 | Disordered | ||||
Sequence: SVSAESLNPNPTASSNESWTPPYH |
Sequence similarities
Belongs to the cAMP-dependent kinase regulatory chain family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length389
- Mass (Da)42,559
- Last updated2001-03-01 v1
- ChecksumC8E6F38E21CE7B5F
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 31-47 | Basic and acidic residues | ||||
Sequence: HIVRVTERDEDKVNPTF | ||||||
Compositional bias | 87-109 | Polar residues | ||||
Sequence: SVSAESLNPNPTASSNESWTPPY |