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Protein

cAMP-dependent protein kinase type II-alpha regulatory subunit

Gene

Prkar2a

Organism
Mus musculus (Mouse)
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.

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

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP-dependent protein kinase type II-alpha regulatory subunit
Gene namesi
Name:Prkar2a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:108025 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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00002053862 – 401cAMP-dependent protein kinase type II-alpha regulatory subunitAdd BLAST400

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarityCurated1
Modified residuei47PhosphoserineBy similarity1
Modified residuei74PhosphoserineBy similarity1
Modified residuei76PhosphoserineBy similarity1
Modified residuei96PhosphoserineCombined 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

EPDiP12367
MaxQBiP12367
PaxDbiP12367
PeptideAtlasiP12367
PRIDEiP12367

PTM databases

iPTMnetiP12367
PhosphoSitePlusiP12367

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. Interacts with 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

GO - Molecular functioni

Protein-protein interaction databases

CORUMiP12367
IntActiP12367, 11 interactors
MINTiP12367
STRINGi10090.ENSMUSP00000035220

Structurei

Secondary structure

1401
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP12367
SMRiP12367
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12367

Family & Domainsi

Region

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

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1113 Eukaryota
COG0664 LUCA
HOVERGENiHBG002025
InParanoidiP12367
PhylomeDBiP12367

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, 1 hit
PS50042 CNMP_BINDING_3, 2 hits

Sequence (1+)i

Sequence statusi: Complete.

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

This entry has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All

P12367-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSHIQIPPGL TELLQGYTVE VGQQPPDLVD FAVEYFTRLR EARRQESDTF
60 70 80 90 100
IVSPTTFHTQ ESSAVPVIEE DGESDSDSED ADLEVPVPSK FTRRVSVCAE
110 120 130 140 150
TFNPDEEEED NDPRVVHPKT DEQRCRLQEA CKDILLFKNL DQEQLSQVLD
160 170 180 190 200
AMFEKIVKTD EHVIDQGDDG DNFYVIERGT YDILVTKDNQ TRSVGQYDNR
210 220 230 240 250
GSFGELALMY NTPRAATIIA TSEGSLWGLD RVTFRRIIVK NNAKKRKMFE
260 270 280 290 300
SFIESVPLFK SLEMSERMKI VDVIGEKIYK DGERIIAQGE KADSFYIIES
310 320 330 340 350
GEVSILIRSK TKSNKNGGNQ EVEIAHCHKG QYFGELALVT NKPRAASAYG
360 370 380 390 400
VGDVKCLVMD VQAFERLLGP CMDIMKRNIS HYEEQLVKMF GSNLDLMDPG

Q
Length:401
Mass (Da):45,389
Last modified:January 23, 2007 - v2
Checksum:iE4191DAC197A9E39
GO

Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q8K1M3Q8K1M3_MOUSE
Protein kinase, cAMP dependent regu...
Prkar2a mCG_16488
402Annotation score:
A0A0A6YX73A0A0A6YX73_MOUSE
cAMP-dependent protein kinase type ...
Prkar2a
380Annotation score:
A0A0A6YY28A0A0A6YY28_MOUSE
cAMP-dependent protein kinase type ...
Prkar2a
200Annotation score:
A0A0A6YWE5A0A0A6YWE5_MOUSE
cAMP-dependent protein kinase type ...
Prkar2a
47Annotation score:

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02935 mRNA Translation: AAA39932.1
PIRiB28325 OKMS2R
UniGeneiMm.253102
Mm.486392

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02935 mRNA Translation: AAA39932.1
PIRiB28325 OKMS2R
UniGeneiMm.253102
Mm.486392

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KMUmodel-R114-383[»]
1KMWmodel-R114-383[»]
1L6ENMR-A/B1-44[»]
1R2ANMR-A/B3-44[»]
2IZYX-ray2.20A/B/C/D/E/F/G/H3-44[»]
2QVSX-ray2.50B92-401[»]
3J4Qelectron microscopy35.00B/C1-401[»]
3J4Relectron microscopy35.00B/C1-401[»]
ProteinModelPortaliP12367
SMRiP12367
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

CORUMiP12367
IntActiP12367, 11 interactors
MINTiP12367
STRINGi10090.ENSMUSP00000035220

PTM databases

iPTMnetiP12367
PhosphoSitePlusiP12367

Proteomic databases

EPDiP12367
MaxQBiP12367
PaxDbiP12367
PeptideAtlasiP12367
PRIDEiP12367

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:108025 Prkar2a

Phylogenomic databases

eggNOGiKOG1113 Eukaryota
COG0664 LUCA
HOVERGENiHBG002025
InParanoidiP12367
PhylomeDBiP12367

Miscellaneous databases

ChiTaRSiPrkar2a mouse
EvolutionaryTraceiP12367
PROiPR:P12367
SOURCEiSearch...

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, 1 hit
PS50042 CNMP_BINDING_3, 2 hits
ProtoNetiSearch...

Entry informationi

Entry nameiKAP2_MOUSE
AccessioniPrimary (citable) accession number: P12367
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: November 7, 2018
This is version 160 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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