P00515 · KAP2_BOVIN
- ProteincAMP-dependent protein kinase type II-alpha regulatory subunit
- GenePRKAR2A
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids401 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase (By similarity).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 136-257 | 3',5'-cyclic AMP 1 (UniProtKB | ChEBI) | ||||
Sequence: LFKNLDPEQLSQVLDAMFERTVKVDEHVIDQGDDGDNFYVIERGTYDILVTKDNQTRSVGQYDNHGSFGELALMYNTPRAATIVATSEGSLWGLDRVTFRRIIVKNNAKKRKMFESFIESVP | ||||||
Binding site | 205 | 3',5'-cyclic AMP 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 214 | 3',5'-cyclic AMP 1 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 258-401 | 3',5'-cyclic AMP 2 (UniProtKB | ChEBI) | ||||
Sequence: LLKSLEVSERMKIVDVIGEKVYKDGERIITQGEKADSFYIIESGEVSILIKSKTKVNKDGENQEVEIARCHKGQYFGELALVTNKPRAASAYAVGDVKCLVMDVQAFERLLGPCMDIMKRNISHYEEQLVKMFGSSMDLIDPGQ | ||||||
Binding site | 335 | 3',5'-cyclic AMP 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 344 | 3',5'-cyclic AMP 2 (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | axoneme | |
Cellular Component | cAMP-dependent protein kinase complex | |
Cellular Component | centrosome | |
Cellular Component | cytosol | |
Cellular Component | nucleotide-activated protein kinase complex | |
Cellular Component | plasma membrane raft | |
Molecular Function | cAMP binding | |
Molecular Function | cAMP-dependent protein kinase inhibitor activity | |
Molecular Function | protein domain specific binding | |
Molecular Function | protein kinase A catalytic subunit binding | |
Molecular Function | ubiquitin protein ligase binding | |
Biological Process | regulation of protein phosphorylation |
Keywords
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namecAMP-dependent protein kinase type II-alpha regulatory subunit
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionP00515
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Colocalizes with PJA2 in the cytoplasm and the cell membrane.
Keywords
- Cellular component
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylserine | ||||
Sequence: S | ||||||
Chain | PRO_0000205384 | 2-401 | cAMP-dependent protein kinase type II-alpha regulatory subunit | |||
Sequence: SHIQIPPGLTELLQGYTVEVLRQRPPDLVDFAVDYFTRLREARSRASTPPAAPPSGSQDFDPGAGLVADAVADSESEDEEDLDVPIPGRFDRRVSVCAETYNPDEEEEDTDPRVIHPKTDQQRCRLQEACKDILLFKNLDPEQLSQVLDAMFERTVKVDEHVIDQGDDGDNFYVIERGTYDILVTKDNQTRSVGQYDNHGSFGELALMYNTPRAATIVATSEGSLWGLDRVTFRRIIVKNNAKKRKMFESFIESVPLLKSLEVSERMKIVDVIGEKVYKDGERIITQGEKADSFYIIESGEVSILIKSKTKVNKDGENQEVEIARCHKGQYFGELALVTNKPRAASAYAVGDVKCLVMDVQAFERLLGPCMDIMKRNISHYEEQLVKMFGSSMDLIDPGQ | ||||||
Modified residue | 48 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 75 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 77 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 96 | Phosphoserine; by PKA | ||||
Sequence: S | ||||||
Modified residue | 212 | Phosphothreonine; by PDPK1 | ||||
Sequence: T | ||||||
Modified residue | 347 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 392 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
A second phosphorylation site has not been located.
Phosphorylation of Thr-212 by PDPK1 seems to attenuate the activity of PKA, perhaps by strengthening interaction between the regulatory and the catalytic subunits.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Four types of regulatory chains are found: I-alpha, I-beta, II-alpha, and II-beta. Their expression varies among tissues and is in some cases constitutive and in others inducible.
Gene expression databases
Interaction
Subunit
The inactive form of the enzyme is composed of two regulatory chains and two catalytic chains. Activation by cAMP produces two active catalytic monomers and a regulatory dimer that binds four cAMP molecules. Interacts with AKAP4 and CBFA2T3 (By similarity).
Interacts with the phosphorylated form of PJA2 (By similarity).
Interacts with MYRIP; this interaction may link PKA to components of the exocytosis machinery, thus facilitating exocytosis, including insulin release (By similarity).
Forms a complex composed of PRKAR2A, GSK3B and GSKIP through GSKIP interaction; facilitates PKA-induced phosphorylation and regulates GSK3B activity (By similarity).
Interacts with ADCY8; inhibits adenylate cyclase activity through PKA phosphorylation (By similarity).
Interacts with the phosphorylated form of PJA2 (By similarity).
Interacts with MYRIP; this interaction may link PKA to components of the exocytosis machinery, thus facilitating exocytosis, including insulin release (By similarity).
Forms a complex composed of PRKAR2A, GSK3B and GSKIP through GSKIP interaction; facilitates PKA-induced phosphorylation and regulates GSK3B activity (By similarity).
Interacts with ADCY8; inhibits adenylate cyclase activity through PKA phosphorylation (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | P00515 | C Q6XGM8 | 3 | EBI-7634955, EBI-8037154 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 2-135 | Dimerization and phosphorylation | ||||
Sequence: SHIQIPPGLTELLQGYTVEVLRQRPPDLVDFAVDYFTRLREARSRASTPPAAPPSGSQDFDPGAGLVADAVADSESEDEEDLDVPIPGRFDRRVSVCAETYNPDEEEEDTDPRVIHPKTDQQRCRLQEACKDIL | ||||||
Region | 43-65 | Disordered | ||||
Sequence: ARSRASTPPAAPPSGSQDFDPGA |
Sequence similarities
Belongs to the cAMP-dependent kinase regulatory chain family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length401
- Mass (Da)45,094
- Last updated2007-04-17 v2
- Checksum8FEA32E5B39A545A
Keywords
- Technical term