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Protein

cAMP-dependent protein kinase type II-beta regulatory subunit

Gene

Prkar2b

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 sitei221cAMP 11
Binding sitei230cAMP 11
Binding sitei350cAMP 21
Binding sitei359cAMP 21

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi152 – 273cAMP 1Add BLAST122
Nucleotide bindingi274 – 416cAMP 2Add BLAST143

GO - Molecular functioni

  • cAMP binding Source: RGD
  • cAMP-dependent protein kinase inhibitor activity Source: Ensembl
  • cAMP-dependent protein kinase regulator activity Source: RGD
  • protein domain specific binding Source: RGD
  • protein kinase A catalytic subunit binding Source: RGD

GO - Biological processi

  • fatty acid metabolic process Source: Ensembl
  • learning Source: Ensembl
  • negative regulation of cAMP-dependent protein kinase activity Source: Ensembl
  • regulation of protein kinase activity Source: RGD
  • response to antipsychotic drug Source: RGD
  • response to clozapine Source: RGD
Complete GO annotation...

Keywords - Ligandi

cAMP, 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-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-RNO-380259. Loss of Nlp from mitotic centrosomes.
R-RNO-380270. Recruitment of mitotic centrosome proteins and complexes.
R-RNO-381676. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
R-RNO-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-RNO-5610787. Hedgehog 'off' state.
R-RNO-5620912. Anchoring of the basal body to the plasma membrane.
R-RNO-8854518. AURKA Activation by TPX2.
R-RNO-983231. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP-dependent protein kinase type II-beta regulatory subunit
Gene namesi
Name:Prkar2b
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi3394. Prkar2b.

Subcellular locationi

  • Cytoplasm By similarity
  • Cell membrane By similarity

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

GO - Cellular componenti

  • cAMP-dependent protein kinase complex Source: RGD
  • centrosome Source: Ensembl
  • ciliary base Source: Ensembl
  • cytoplasm Source: RGD
  • dendrite Source: RGD
  • dendritic shaft Source: ParkinsonsUK-UCL
  • dendritic spine Source: ParkinsonsUK-UCL
  • extracellular exosome Source: Ensembl
  • membrane raft Source: RGD
  • mitochondrial inner membrane Source: RGD
  • neuronal cell body Source: RGD
  • perinuclear region of cytoplasm Source: RGD
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002053921 – 416cAMP-dependent protein kinase type II-beta regulatory subunitAdd BLAST416

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei69PhosphothreonineBy similarity1
Modified residuei83PhosphoserineCombined sources1
Modified residuei85PhosphoserineCombined sources1
Modified residuei112PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated by the activated catalytic chain.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP12369.
PRIDEiP12369.

PTM databases

iPTMnetiP12369.
PhosphoSitePlusiP12369.

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. Brain. Present in a few pyramidal neurons and mostly in mossy fibers. Colocalizes with PJA2 in dentate granule cells and at postsynaptic sites of primary hippocampal neurons.1 Publication

Gene expression databases

ExpressionAtlasiP12369. baseline and differential.
GenevisibleiP12369. RN.

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 the phosphorylated form of PJA2 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
LRRK2Q5S0073EBI-6096160,EBI-5323863From a different organism.
PRKACAP176122EBI-6096160,EBI-476586From a different organism.

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi246811. 1 interactor.
DIPiDIP-61323N.
IntActiP12369. 2 interactors.
STRINGi10116.ENSRNOP00000012415.

Structurei

Secondary structure

1416
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi137 – 147Combined sources11
Helixi151 – 154Combined sources4
Helixi158 – 167Combined sources10
Beta strandi169 – 173Combined sources5
Beta strandi178 – 180Combined sources3
Beta strandi188 – 203Combined sources16
Beta strandi206 – 215Combined sources10
Helixi221 – 224Combined sources4
Beta strandi231 – 246Combined sources16
Helixi247 – 259Combined sources13
Helixi273 – 275Combined sources3
Beta strandi276 – 278Combined sources3
Helixi280 – 289Combined sources10
Beta strandi291 – 295Combined sources5
Beta strandi300 – 302Combined sources3
Beta strandi310 – 324Combined sources15
Beta strandi336 – 342Combined sources7
Beta strandi347 – 349Combined sources3
Helixi351 – 355Combined sources5
Beta strandi360 – 375Combined sources16
Helixi376 – 382Combined sources7
Helixi384 – 386Combined sources3
Helixi387 – 405Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CX4X-ray2.45A112-416[»]
3IDBX-ray1.62B108-268[»]
3IDCX-ray2.70B102-265[»]
4JVAX-ray2.50A112-416[»]
ProteinModelPortaliP12369.
SMRiP12369.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12369.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 151Dimerization and phosphorylationAdd BLAST150

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1113. Eukaryota.
COG0664. LUCA.
GeneTreeiENSGT00530000062947.
HOGENOMiHOG000196668.
HOVERGENiHBG002025.
InParanoidiP12369.
KOiK04739.
OMAiLADCFYI.
OrthoDBiEOG091G0F1K.
PhylomeDBiP12369.
TreeFamiTF314920.

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.

P12369-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIEIPAGLT ELLQGFTVEV LRHQPADLLE FALQHFTRLQ QENERKGAAR
60 70 80 90 100
FGHEGRTWGD AGAAAGGGTP SKGVNFAEEP MRSDSENGEE EEAAEAGAFN
110 120 130 140 150
APVINRFTRR ASVCAEAYNP DEEEDDAESR IIHPKTDDQR NRLQEACKDI
160 170 180 190 200
LLFKNLDPEQ MSQVLDAMFE KLVKEGEHVI DQGDDGDNFY VIDRGTFDIY
210 220 230 240 250
VKCDGVGRCV GNYDNRGSFG ELALMYNTPR AATITATSPG ALWGLDRVTF
260 270 280 290 300
RRIIVKNNAK KRKMYESFIE SLPFLKSLEV SERLKVVDVI GTKVYNDGEQ
310 320 330 340 350
IIAQGDSADS FFIVESGEVR ITMKRKGKSD IEENGAVEIA RCLRGQYFGE
360 370 380 390 400
LALVTNKPRA ASAHAIGTVK CLAMDVQAFE RLLGPCMEIM KRNIATYEEQ
410
LVALFGTNMD IVEPTA
Length:416
Mass (Da):46,123
Last modified:January 23, 2007 - v3
Checksum:i8BC984E325FA3612
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12492 mRNA. Translation: AAA42047.1.
PIRiA28893. OKRTR2.
RefSeqiNP_001025191.1. NM_001030020.1.
UniGeneiRn.164375.
Rn.4075.

Genome annotation databases

EnsembliENSRNOT00000012415; ENSRNOP00000012415; ENSRNOG00000009079.
GeneIDi24679.
KEGGirno:24679.
UCSCiRGD:3394. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12492 mRNA. Translation: AAA42047.1.
PIRiA28893. OKRTR2.
RefSeqiNP_001025191.1. NM_001030020.1.
UniGeneiRn.164375.
Rn.4075.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CX4X-ray2.45A112-416[»]
3IDBX-ray1.62B108-268[»]
3IDCX-ray2.70B102-265[»]
4JVAX-ray2.50A112-416[»]
ProteinModelPortaliP12369.
SMRiP12369.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246811. 1 interactor.
DIPiDIP-61323N.
IntActiP12369. 2 interactors.
STRINGi10116.ENSRNOP00000012415.

PTM databases

iPTMnetiP12369.
PhosphoSitePlusiP12369.

Proteomic databases

PaxDbiP12369.
PRIDEiP12369.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000012415; ENSRNOP00000012415; ENSRNOG00000009079.
GeneIDi24679.
KEGGirno:24679.
UCSCiRGD:3394. rat.

Organism-specific databases

CTDi5577.
RGDi3394. Prkar2b.

Phylogenomic databases

eggNOGiKOG1113. Eukaryota.
COG0664. LUCA.
GeneTreeiENSGT00530000062947.
HOGENOMiHOG000196668.
HOVERGENiHBG002025.
InParanoidiP12369.
KOiK04739.
OMAiLADCFYI.
OrthoDBiEOG091G0F1K.
PhylomeDBiP12369.
TreeFamiTF314920.

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-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-RNO-380259. Loss of Nlp from mitotic centrosomes.
R-RNO-380270. Recruitment of mitotic centrosome proteins and complexes.
R-RNO-381676. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
R-RNO-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-RNO-5610787. Hedgehog 'off' state.
R-RNO-5620912. Anchoring of the basal body to the plasma membrane.
R-RNO-8854518. AURKA Activation by TPX2.
R-RNO-983231. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

EvolutionaryTraceiP12369.
PROiP12369.

Gene expression databases

ExpressionAtlasiP12369. baseline and differential.
GenevisibleiP12369. RN.

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 nameiKAP3_RAT
AccessioniPrimary (citable) accession number: P12369
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 147 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.