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Protein

cAMP-dependent protein kinase type II-alpha regulatory subunit

Gene

Prkar2a

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei205cAMP 1By similarity1
Binding sitei214cAMP 1By similarity1
Binding sitei335cAMP 2By similarity1
Binding sitei344cAMP 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi136 – 257cAMP 1By similarityAdd BLAST122
Nucleotide bindingi258 – 401cAMP 2By similarityAdd BLAST144

GO - Molecular functioni

  • beta-2 adrenergic receptor binding Source: ARUK-UCL
  • cAMP binding Source: RGD
  • cAMP-dependent protein kinase inhibitor activity Source: RGD
  • cAMP-dependent protein kinase regulator activity Source: RGD
  • protein domain specific binding Source: RGD
  • protein homodimerization activity Source: RGD
  • protein kinase A catalytic subunit binding Source: RGD
  • small molecule binding Source: RGD
  • ubiquitin protein ligase binding Source: RGD

GO - Biological processi

  • negative regulation of cAMP-dependent protein kinase activity Source: RGD
  • protein heterooligomerization Source: RGD
  • regulation of protein kinase activity Source: RGD
  • response to clozapine Source: RGD

Keywordsi

LigandcAMP, cAMP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-163615. PKA activation.
R-RNO-164378. PKA activation in glucagon signalling.
R-RNO-180024. DARPP-32 events.
R-RNO-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-RNO-5610787. Hedgehog 'off' state.
R-RNO-983231. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP-dependent protein kinase type II-alpha regulatory subunit
Gene namesi
Name:Prkar2a
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 8

Organism-specific databases

RGDi3393. Prkar2a.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Chemistry databases

GuidetoPHARMACOLOGYi1474.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002053882 – 401cAMP-dependent protein kinase type II-alpha regulatory subunitAdd BLAST400

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei48PhosphoserineBy similarity1
Modified residuei75PhosphoserineBy similarity1
Modified residuei77PhosphoserineBy similarity1
Modified residuei97PhosphoserineCombined sources1
Modified residuei212Phosphothreonine; by PDPK1By similarity1
Modified residuei347PhosphoserineBy similarity1
Modified residuei392PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated by the activated catalytic chain.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP12368.
PRIDEiP12368.

PTM databases

iPTMnetiP12368.
PhosphoSitePlusiP12368.

Expressioni

Tissue specificityi

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

BgeeiENSRNOG00000020284.

Interactioni

Subunit structurei

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; his interaction may link PKA to components of the exocytosis machinery, thus facilitating exocytosis, including insulin release. Forms a complex composed of PRKAR2A, GSK3B and GSKIP through GSKIP interaction; facilitates PKA-induced phosphorylation and regulates GSK3B activity (By similarity).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PDE4DIPQ5VU43-112EBI-919521,EBI-10769071From a different organism.

GO - Molecular functioni

  • beta-2 adrenergic receptor binding Source: ARUK-UCL
  • protein domain specific binding Source: RGD
  • protein homodimerization activity Source: RGD
  • protein kinase A catalytic subunit binding Source: RGD
  • ubiquitin protein ligase binding Source: RGD

Protein-protein interaction databases

CORUMiP12368.
DIPiDIP-555N.
IntActiP12368. 5 interactors.
MINTiMINT-4564663.
STRINGi10116.ENSRNOP00000027552.

Structurei

Secondary structure

1401
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 24Combined sources15
Helixi29 – 43Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DRNNMR-A/B1-45[»]
2H9RNMR-A/B1-45[»]
2HWNX-ray1.60A/B/C/D1-45[»]
3TMHX-ray3.80B/C/F/G1-45[»]
ProteinModelPortaliP12368.
SMRiP12368.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12368.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 135Dimerization and phosphorylationAdd BLAST134

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1113. Eukaryota.
COG0664. LUCA.
GeneTreeiENSGT00530000062947.
HOGENOMiHOG000196668.
HOVERGENiHBG002025.
InParanoidiP12368.
KOiK04739.
PhylomeDBiP12368.
TreeFamiTF314920.

Family and domain databases

CDDicd00038. CAP_ED. 2 hits.
Gene3Di1.20.890.10. 1 hit.
2.60.120.10. 2 hits.
InterProiView protein in InterPro
IPR012198. cAMP_dep_PK_reg_su.
IPR003117. cAMP_dep_PK_reg_su_I/II_a/b.
IPR036536. cAMP_dep_PK_reg_su_sf.
IPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR014710. RmlC-like_jellyroll.
PfamiView protein in Pfam
PF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
PIRSFiPIRSF000548. PK_regulatory. 1 hit.
SMARTiView protein in SMART
SM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
SUPFAMiSSF47391. SSF47391. 1 hit.
SSF51206. SSF51206. 2 hits.
PROSITEiView protein in PROSITE
PS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P12368-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHIQIPPGL TELLQGYTVE VLRQQPPDLV DFAVEYFTRL REARRQESDS
60 70 80 90 100
FIAPPTTFHA QESSGVPVIE EDGESESDSD DEDLEVPIPS KFTRRVSVCA
110 120 130 140 150
ETFNPDEEED NDPRVVHPKT DEQRCRLQEA CKDILLFKNL DQEQLSQVLD
160 170 180 190 200
AMFEKIVKTD EHVIDQGDDG DNFYVIERGT YDILVTKDNQ TRSVGQYDNR
210 220 230 240 250
GSFGELALMY NTPRAATIVA TSDGSLWGLD RVTFRRIIVK NNAKKRKMFE
260 270 280 290 300
SFIESVPLFK SLEMSERMKI VDVIGEKIYK DGERIITQGE KADSFYIIES
310 320 330 340 350
GEVSILIRSK TKTNKNGGNQ EVEIAHCHKG QYFGELALVT NKPRAASAYA
360 370 380 390 400
VGDVKCLVMD VQAFERLLGP CMDIMKRNIS HYEEQLVKMF GSNLDLLDPG

Q
Length:401
Mass (Da):45,480
Last modified:August 30, 2017 - v4
Checksum:i0D711A1CFEAFB79D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti74E → Q in AAA41856 (PubMed:3037538).Curated1
Sequence conflicti90S → A in AAA41856 (PubMed:3037538).Curated1
Sequence conflicti125C → Y in AAM97689 (Ref. 1) Curated1
Sequence conflicti154 – 155EK → KR in AAA41856 (PubMed:3037538).Curated2
Sequence conflicti198D → A in AAA41856 (PubMed:3037538).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF533978 mRNA. Translation: AAM97689.1.
AC107280 Genomic DNA. No translation available.
CH473954 Genomic DNA. Translation: EDL77148.1.
CH473954 Genomic DNA. Translation: EDL77146.1.
J02934 mRNA. Translation: AAA41856.1.
PIRiA28325. OKRT2R.
RefSeqiNP_062137.1. NM_019264.2.
UniGeneiRn.9742.

Genome annotation databases

EnsembliENSRNOT00000027552; ENSRNOP00000027552; ENSRNOG00000020284.
GeneIDi29699.
KEGGirno:29699.
UCSCiRGD:3393. rat.

Similar proteinsi

Entry informationi

Entry nameiKAP2_RAT
AccessioniPrimary (citable) accession number: P12368
Secondary accession number(s): G3V8Q6, Q8K1M2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: August 30, 2017
Last modified: November 22, 2017
This is version 151 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families