Reviewed,
UniProtKB/Swiss-Prot P00515 (KAP2_BOVIN)
Last modified
November 3, 2009.
Version 90.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: cAMP-dependent protein kinase type II-alpha regulatory subunit | ||
| Gene names |
| ||
| Organism | Bos taurus (Bovine) | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Protein attributes
| Sequence length | 401 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Subunit structure | 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. |
| 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. |
| Post-translational modification | A second phosphorylation site has not been located. Phosphorylation of Thr-212 by PDPK seems to attenuate the activity of PKA, perhaps by strengthening interaction between the regulatory and the catalytic subunits. |
| Sequence similarities | Belongs to the cAMP-dependent kinase regulatory chain family. Contains 2 cyclic nucleotide-binding domains. |
Ontologies
| Keywords | |
|---|---|
| Domain | Repeat |
| Ligand | Nucleotide-binding cAMP cAMP-binding |
| PTM | Acetylation Phosphoprotein |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | regulation of protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro signal transductionInferred from electronic annotation. Source: InterPro |
| Cellular component | cAMP-dependent protein kinase complex Inferred from electronic annotation. Source: InterPro |
| Molecular function | cAMP binding Inferred from electronic annotation. Source: UniProtKB-KW cAMP-dependent protein kinase regulator activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.1 | |||||||||||||||||||||||||||
| Chain | 2 – 401 | 400 | cAMP-dependent protein kinase type II-alpha regulatory subunit | PRO_0000205384 | ||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||
| Nucleotide binding | 136 – 257 | 122 | cAMP 1 | |||||||||||||||||||||||||||
| Nucleotide binding | 258 – 401 | 144 | cAMP 2 | |||||||||||||||||||||||||||
| Region | 2 – 135 | 134 | Dimerization and phosphorylation | |||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||
| Binding site | 205 | 1 | cAMP 1 | |||||||||||||||||||||||||||
| Binding site | 214 | 1 | cAMP 1 | |||||||||||||||||||||||||||
| Binding site | 335 | 1 | cAMP 2 | |||||||||||||||||||||||||||
| Binding site | 344 | 1 | cAMP 2 | |||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||
| Modified residue | 2 | 1 | N-acetylserine | |||||||||||||||||||||||||||
| Modified residue | 75 | 1 | Phosphoserine By similarity | |||||||||||||||||||||||||||
| Modified residue | 77 | 1 | Phosphoserine By similarity | |||||||||||||||||||||||||||
| Modified residue | 96 | 1 | Phosphoserine; by PKA By similarity | |||||||||||||||||||||||||||
| Modified residue | 212 | 1 | Phosphothreonine; by PDPK Ref.2 | |||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||
| Helix | 144 – 149 | 6 | ||||||||||||||||||||||||||||
| Beta strand | 154 – 156 | 3 | ||||||||||||||||||||||||||||
| Beta strand | 176 – 184 | 9 | ||||||||||||||||||||||||||||
| Beta strand | 187 – 189 | 3 | ||||||||||||||||||||||||||||
| Beta strand | 192 – 200 | 9 | ||||||||||||||||||||||||||||
| Beta strand | 207 – 210 | 4 | ||||||||||||||||||||||||||||
| Beta strand | 214 – 217 | 4 | ||||||||||||||||||||||||||||
| Beta strand | 223 – 225 | 3 | ||||||||||||||||||||||||||||
| Helix | 230 – 236 | 7 | ||||||||||||||||||||||||||||
| Turn | 237 – 239 | 3 | ||||||||||||||||||||||||||||
| Helix | 242 – 263 | 22 | ||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Primary structure of the regulatory subunit of type II cAMP-dependent protein kinase from bovine cardiac muscle." Takio K., Smith S.B., Krebs E.G., Walsh K.A., Titani K. Proc. Natl. Acad. Sci. U.S.A. 79:2544-2548(1982) [PubMed: 6283532] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-401. Tissue: Heart muscle. |
| [2] | "Phosphorylation of RII subunit and attenuation of cAMP-dependent protein kinase activity by proline-directed protein kinase." Braun R.K., Vulliet P.R., Carbonaro-Hall D.A., Hall F.L. Arch. Biochem. Biophys. 289:187-191(1991) [PubMed: 1654846] [Abstract] Cited for: PROTEIN SEQUENCE OF 155-166, PHOSPHORYLATION AT THR-212. |
| [3] | "Predicted structures of cAMP binding domains of type I and II regulatory subunits of cAMP-dependent protein kinase." Weber I.T., Steitz T.A., Bubis J., Taylor S.S. Biochemistry 26:343-351(1987) [PubMed: 3030405] [Abstract] Cited for: 3D-STRUCTURE MODELING. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| IPI | IPI00693176. | ||||||||||||||||||
| PIR | OKBO2R. A00618. | ||||||||||||||||||
| RefSeq | XP_001790337.1. | ||||||||||||||||||
| UniGene | Bt.95129 | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| |||||||||||||||||||
| SMR | P00515. Positions 114-397. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| DIP | DIP:546N. | ||||||||||||||||||
| STRING | P00515. | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| Ensembl | ENSBTAT00000018886; ENSBTAP00000018886; ENSBTAG00000014205; Bos taurus. [Genome view] | ||||||||||||||||||
| GeneID | 100139910. | ||||||||||||||||||
| KEGG | bta:100139910. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| CTD | 100139910. | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| HOVERGEN | P00515. | ||||||||||||||||||
| OMA | DQQRCRL. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR003117. cAMP-dep_prot_kin_reg_I/II_a/b. IPR002373. cAMP/cGMP_kin. IPR000595. cNMP_bd. IPR018488. cNMP_bd_CS. IPR012198. PK_regulatory. IPR014710. RmlC-like_jellyroll. [Graphical view] | ||||||||||||||||||
| Gene3D | G3DSA:2.60.120.10. RmlC-like_jellyroll. 2 hits. | ||||||||||||||||||
| Pfam | PF00027. cNMP_binding. 2 hits. PF02197. RIIa. 1 hit. [Graphical view] | ||||||||||||||||||
| PIRSF | PIRSF000548. PK_regulatory. 1 hit. | ||||||||||||||||||
| PRINTS | PR00103. CAMPKINASE. | ||||||||||||||||||
| SMART | SM00100. cNMP. 2 hits. SM00394. RIIa. 1 hit. [Graphical view] | ||||||||||||||||||
| PROSITE | PS00888. CNMP_BINDING_1. 2 hits. PS00889. CNMP_BINDING_2. 2 hits. PS50042. CNMP_BINDING_3. 2 hits. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Entry information
| Entry name | KAP2_BOVIN | ||||||||
| Accession | Primary (citable) accession number: P00515 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


