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P12369 (KAP3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
cAMP-dependent protein kinase type II-beta regulatory subunit
Gene names
Name:Prkar2b
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

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 the phosphorylated form of PJA2 By similarity.

Subcellular location

Cytoplasm By similarity. Cell membrane By similarity. Note: Colocalizes with PJA2 in the cytoplasm and at the cell membrane 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. Brain. Present in a few pyramidal neurons and mostly in mossy fibers. Colocalizes with PJA2 in dentate granule cells and at postsynaptic sites of primary hippocampal neurons. Ref.5

Post-translational modification

Phosphorylated by the activated catalytic chain.

Sequence similarities

Belongs to the cAMP-dependent kinase regulatory chain family.

Contains 2 cyclic nucleotide-binding domains.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Membrane
   DomainRepeat
   LigandcAMP
cAMP-binding
Nucleotide-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processregulation of protein kinase activity

Inferred from direct assay PubMed 11907174PubMed 16816331. Source: RGD

response to antipsychotic drug

Inferred from expression pattern PubMed 11907174. Source: RGD

response to clozapine

Inferred from expression pattern PubMed 11907174. Source: RGD

   Cellular_componentcAMP-dependent protein kinase complex

Inferred from direct assay PubMed 11907174PubMed 16816331. Source: RGD

cytoplasm

Inferred from direct assay PubMed 18550536. Source: RGD

membrane raft

Inferred from direct assay PubMed 12573460. Source: RGD

mitochondrial inner membrane

Inferred from direct assay PubMed 16996504. Source: RGD

perinuclear region of cytoplasm

Inferred from direct assay PubMed 18550536. Source: RGD

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncAMP binding

Inferred from direct assay PubMed 11907174PubMed 14625280. Source: RGD

cAMP-dependent protein kinase regulator activity

Inferred from direct assay PubMed 11907174PubMed 16816331. Source: RGD

protein binding

Inferred from physical interaction PubMed 24464040. Source: IntAct

protein domain specific binding

Inferred from mutant phenotype PubMed 16996504. Source: RGD

protein kinase A catalytic subunit binding

Inferred by curator PubMed 16816331. Source: RGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LRRK2Q5S0073EBI-6096160,EBI-5323863From a different organism.
PRKACAP176122EBI-6096160,EBI-476586From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Probable
Chain2 – 416415cAMP-dependent protein kinase type II-beta regulatory subunit
PRO_0000205392

Regions

Nucleotide binding152 – 273122cAMP 1
Nucleotide binding274 – 416143cAMP 2
Region2 – 151150Dimerization and phosphorylation

Sites

Binding site2211cAMP 1
Binding site2301cAMP 1
Binding site3501cAMP 2
Binding site3591cAMP 2

Amino acid modifications

Modified residue21N-acetylserine Probable
Modified residue831Phosphoserine By similarity
Modified residue851Phosphoserine By similarity
Modified residue1121Phosphoserine Ref.4

Secondary structure

........................................... 416
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12369 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 8BC984E325FA3612

FASTA41646,123
        10         20         30         40         50         60 
MSIEIPAGLT ELLQGFTVEV LRHQPADLLE FALQHFTRLQ QENERKGAAR FGHEGRTWGD 

        70         80         90        100        110        120 
AGAAAGGGTP SKGVNFAEEP MRSDSENGEE EEAAEAGAFN APVINRFTRR ASVCAEAYNP 

       130        140        150        160        170        180 
DEEEDDAESR IIHPKTDDQR NRLQEACKDI LLFKNLDPEQ MSQVLDAMFE KLVKEGEHVI 

       190        200        210        220        230        240 
DQGDDGDNFY VIDRGTFDIY VKCDGVGRCV GNYDNRGSFG ELALMYNTPR AATITATSPG 

       250        260        270        280        290        300 
ALWGLDRVTF RRIIVKNNAK KRKMYESFIE SLPFLKSLEV SERLKVVDVI GTKVYNDGEQ 

       310        320        330        340        350        360 
IIAQGDSADS FFIVESGEVR ITMKRKGKSD IEENGAVEIA RCLRGQYFGE LALVTNKPRA 

       370        380        390        400        410 
ASAHAIGTVK CLAMDVQAFE RLLGPCMEIM KRNIATYEEQ LVALFGTNMD IVEPTA 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning, cDNA structure and deduced amino acid sequence for the hormone-induced regulatory subunit (RII beta) of cAMP-dependent protein kinase from rat ovarian granulosa cells."
Sandberg M., Levy F.O., Oeyen O., Hansson V., Jahnsen T.
Biochem. Biophys. Res. Commun. 154:705-711(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular cloning, cDNA structure, and regulation of the regulatory subunit of type II cAMP-dependent protein kinase from rat ovarian granulosa cells."
Jahnsen T., Hedin L., Kidd V.J., Beattie W.G., Lohmann S.M., Walter U., Durica J., Schulz T.Z., Schiltz E., Browner M., Lawrence C.B., Goldman D., Ratoosh S.L., Richards J.S.
J. Biol. Chem. 261:12352-12361(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE OF 16-416.
Tissue: Ovarian granulosa cell.
[3]Erratum
Jahnsen T., Hedin L., Kidd V.J., Beattie W.G., Lohmann S.M., Walter U., Durica J., Schulz T.Z., Schiltz E., Browner M., Lawrence C.B., Goldman D., Ratoosh S.L., Richards J.S.
J. Biol. Chem. 263:4041-4041(1988)
[4]"Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[5]"Control of PKA stability and signalling by the RING ligase praja2."
Lignitto L., Carlucci A., Sepe M., Stefan E., Cuomo O., Nistico R., Scorziello A., Savoia C., Garbi C., Annunziato L., Feliciello A.
Nat. Cell Biol. 13:412-422(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[6]"Molecular basis for regulatory subunit diversity in cAMP-dependent protein kinase: crystal structure of the type II beta regulatory subunit."
Diller T.C., Madhusudan X., Xuong N.H., Taylor S.S.
Structure 9:73-82(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 112-416.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M12492 mRNA. Translation: AAA42047.1.
PIROKRTR2. A28893.
RefSeqNP_001025191.1. NM_001030020.1.
UniGeneRn.164375.
Rn.4075.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CX4X-ray2.45A112-416[»]
3IDBX-ray1.62B108-268[»]
3IDCX-ray2.70B102-265[»]
4JVAX-ray2.50A112-416[»]
ProteinModelPortalP12369.
SMRP12369. Positions 3-41, 130-412.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246811. 1 interaction.
IntActP12369. 2 interactions.
STRING10116.ENSRNOP00000012415.

PTM databases

PhosphoSiteP12369.

Proteomic databases

PaxDbP12369.
PRIDEP12369.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID24679.
KEGGrno:24679.
UCSCRGD:3394. rat.

Organism-specific databases

CTD5577.
RGD3394. Prkar2b.

Phylogenomic databases

eggNOGCOG0664.
HOGENOMHOG000196668.
HOVERGENHBG002025.
InParanoidP12369.
KOK04739.
OrthoDBEOG76T9RR.
PhylomeDBP12369.
TreeFamTF314920.

Enzyme and pathway databases

ReactomeREACT_205051. Metabolism.

Gene expression databases

GenevestigatorP12369.

Family and domain databases

Gene3D2.60.120.10. 2 hits.
InterProIPR002373. cAMP/cGMP_kin.
IPR012198. cAMP_dep_PK_reg_su.
IPR003117. cAMP_dep_PK_reg_su_I/II_a/b.
IPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamPF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view]
PIRSFPIRSF000548. PK_regulatory. 1 hit.
PRINTSPR00103. CAMPKINASE.
SMARTSM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
[Graphical view]
SUPFAMSSF47391. SSF47391. 1 hit.
SSF51206. SSF51206. 2 hits.
PROSITEPS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP12369.
NextBio604075.
PROP12369.

Entry information

Entry nameKAP3_RAT
AccessionPrimary (citable) accession number: P12369
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 128 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references