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Protein

cAMP-dependent protein kinase type II-alpha regulatory subunit

Gene

PRKAR2A

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -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 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei205cAMP 11
Binding sitei214cAMP 11
Binding sitei335cAMP 21
Binding sitei344cAMP 21

Regions

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

LigandcAMP, cAMP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-BTA-163615 PKA activation
R-BTA-164378 PKA activation in glucagon signalling
R-BTA-180024 DARPP-32 events
R-BTA-432040 Vasopressin regulates renal water homeostasis via Aquaporins
R-BTA-5610787 Hedgehog 'off' state
R-BTA-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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 22

Organism-specific databases

VGNCiVGNC:33325 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

ChEMBLiCHEMBL2111446

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity1 Publication
ChainiPRO_00002053842 – 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 residuei96Phosphoserine; by PKABy similarity1
Modified residuei212Phosphothreonine; by PDPK11 Publication1
Modified residuei347PhosphoserineBy similarity1
Modified residuei392PhosphoserineBy similarity1

Post-translational modificationi

A second phosphorylation site has not been located.1 Publication
Phosphorylation of Thr-212 by PDPK1 seems to attenuate the activity of PKA, perhaps by strengthening interaction between the regulatory and the catalytic subunits.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP00515
PeptideAtlasiP00515
PRIDEiP00515

PTM databases

iPTMnetiP00515

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

BgeeiENSBTAG00000014205

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; 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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CQ6XGM83EBI-7634955,EBI-8037154From Hepatitis B virus.

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-546N
ELMiP00515
IntActiP00515, 4 interactors
MINTiP00515
STRINGi9913.ENSBTAP00000018886

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2APKmodel-A2-401[»]
2BPKmodel-A2-401[»]
ProteinModelPortaliP00515
SMRiP00515
ModBaseiSearch...
MobiDBiSearch...

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
InParanoidiP00515
KOiK04739
OMAiSHIQIPP
OrthoDBiEOG091G0F1K
TreeFamiTF314920

Family and domain databases

CDDicd00038 CAP_ED, 2 hits
Gene3Di2.60.120.10, 2 hits
InterProiView protein in InterPro
IPR012198 cAMP_dep_PK_reg_su
IPR003117 cAMP_dep_PK_reg_su_I/II_a/b
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
SUPFAMiSSF51206 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.

P00515-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHIQIPPGL TELLQGYTVE VLRQRPPDLV DFAVDYFTRL REARSRASTP
60 70 80 90 100
PAAPPSGSQD FDPGAGLVAD AVADSESEDE EDLDVPIPGR FDRRVSVCAE
110 120 130 140 150
TYNPDEEEED TDPRVIHPKT DQQRCRLQEA CKDILLFKNL DPEQLSQVLD
160 170 180 190 200
AMFERTVKVD EHVIDQGDDG DNFYVIERGT YDILVTKDNQ TRSVGQYDNH
210 220 230 240 250
GSFGELALMY NTPRAATIVA TSEGSLWGLD RVTFRRIIVK NNAKKRKMFE
260 270 280 290 300
SFIESVPLLK SLEVSERMKI VDVIGEKVYK DGERIITQGE KADSFYIIES
310 320 330 340 350
GEVSILIKSK TKVNKDGENQ EVEIARCHKG QYFGELALVT NKPRAASAYA
360 370 380 390 400
VGDVKCLVMD VQAFERLLGP CMDIMKRNIS HYEEQLVKMF GSSMDLIDPG

Q
Length:401
Mass (Da):45,094
Last modified:April 17, 2007 - v2
Checksum:i8FEA32E5B39A545A
GO

Sequence databases

PIRiA00618 OKBO2R
RefSeqiNP_001178296.1, NM_001191367.1

Genome annotation databases

EnsembliENSBTAT00000018886; ENSBTAP00000018886; ENSBTAG00000014205
GeneIDi100139910
KEGGibta:100139910

Similar proteinsi

Entry informationi

Entry nameiKAP2_BOVIN
AccessioniPrimary (citable) accession number: P00515
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 17, 2007
Last modified: March 28, 2018
This is version 158 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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