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Protein

cAMP-dependent protein kinase type II-alpha regulatory subunit

Gene

Prkar2a

Organism
Mus musculus (Mouse)
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 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

Complete GO annotation...

Keywords - Ligandi

cAMP, 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:108025. 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

Complete GO annotation...

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-acetylserineCurated1
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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Akap2O54931-33EBI-645747,EBI-645828
Akap5D3YVF02EBI-645747,EBI-7091108

GO - Molecular functioni

Protein-protein interaction databases

IntActiP12367. 9 interactors.
MINTiMINT-1733887.
STRINGi10090.ENSMUSP00000035220.

Structurei

Secondary structure

1401
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 23Combined sources14
Helixi28 – 44Combined sources17
Helixi121 – 131Combined sources11
Helixi135 – 138Combined sources4
Helixi142 – 151Combined sources10
Beta strandi153 – 157Combined sources5
Beta strandi162 – 164Combined sources3
Beta strandi172 – 178Combined sources7
Beta strandi180 – 187Combined sources8
Beta strandi190 – 199Combined sources10
Helixi205 – 208Combined sources4
Beta strandi215 – 230Combined sources16
Helixi231 – 254Combined sources24
Helixi257 – 259Combined sources3
Helixi264 – 273Combined sources10
Beta strandi275 – 279Combined sources5
Beta strandi284 – 286Combined sources3
Beta strandi294 – 307Combined sources14
Beta strandi311 – 315Combined sources5
Beta strandi322 – 328Combined sources7
Helixi335 – 338Combined sources4
Beta strandi345 – 360Combined sources16
Helixi361 – 368Combined sources8
Helixi371 – 377Combined sources7
Helixi379 – 381Combined sources3
Helixi382 – 390Combined sources9

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...

Miscellaneous databases

EvolutionaryTraceiP12367.

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.
HOVERGENiHBG002025.
InParanoidiP12367.
PhylomeDBiP12367.

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. 1 hit.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

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

Sequence databases

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

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

IntActiP12367. 9 interactors.
MINTiMINT-1733887.
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.
PROiP12367.
SOURCEiSearch...

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. 1 hit.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKAP2_MOUSE
AccessioniPrimary (citable) accession number: P12367
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 146 of the entry and version 2 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.