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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

  • cAMP binding 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

GO - Biological processi

  • protein heterooligomerization Source: RGD
  • regulation of protein kinase activity Source: RGD
  • response to clozapine Source: RGD
Complete GO annotation...

Keywords - Ligandi

cAMP, cAMP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-381676. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3393. Prkar2a.

Subcellular locationi

  • Cytoplasm By similarity
  • Cell membrane By similarity

  • Note: Colocalizes with PJA2 in the cytoplasm and the cell membrane.By similarity

GO - Cellular componenti

  • cAMP-dependent protein kinase complex Source: RGD
  • cytoplasm Source: RGD
  • perinuclear region of cytoplasm Source: RGD
  • protein complex Source: RGD
  • T-tubule Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

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.

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.By similarity1 Publication

Binary interactionsi

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

GO - Molecular functioni

  • protein domain specific binding Source: RGD
  • protein homodimerization activity Source: RGD
  • protein kinase A catalytic subunit binding Source: RGD

Protein-protein interaction databases

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

Contains 2 cyclic nucleotide-binding domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

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

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR012198. 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]
PfamiPF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view]
PIRSFiPIRSF000548. PK_regulatory. 1 hit.
SMARTiSM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
[Graphical view]
SUPFAMiSSF47391. SSF47391. 1 hit.
SSF51206. SSF51206. 2 hits.
PROSITEiPS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view]

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 DEQRYRLQEA 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):45,540
Last modified:January 23, 2007 - v3
Checksum:i026FEBFCFACA9C7D
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 conflicti125Y → C in AAA41856 (PubMed:3037538).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.
J02934 mRNA. Translation: AAA41856.1.
PIRiA28325. OKRT2R.
RefSeqiNP_062137.1. NM_019264.2.
UniGeneiRn.9742.

Genome annotation databases

GeneIDi29699.
KEGGirno:29699.
UCSCiRGD:3393. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF533978 mRNA. Translation: AAM97689.1.
J02934 mRNA. Translation: AAA41856.1.
PIRiA28325. OKRT2R.
RefSeqiNP_062137.1. NM_019264.2.
UniGeneiRn.9742.

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...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP12368.
PhosphoSitePlusiP12368.

Proteomic databases

PaxDbiP12368.
PRIDEiP12368.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29699.
KEGGirno:29699.
UCSCiRGD:3393. rat.

Organism-specific databases

CTDi5576.
RGDi3393. Prkar2a.

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiR-RNO-381676. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.

Miscellaneous databases

EvolutionaryTraceiP12368.
PROiP12368.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR012198. 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]
PfamiPF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view]
PIRSFiPIRSF000548. PK_regulatory. 1 hit.
SMARTiSM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
[Graphical view]
SUPFAMiSSF47391. SSF47391. 1 hit.
SSF51206. SSF51206. 2 hits.
PROSITEiPS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKAP2_RAT
AccessioniPrimary (citable) accession number: P12368
Secondary accession number(s): Q8K1M2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 145 of the entry and version 3 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.