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P31324 (KAP3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
cAMP-dependent protein kinase type II-beta regulatory subunit
Gene names
Name:Prkar2b
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.8

Subcellular location

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

Tissue specificity

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.

Post-translational modification

Phosphorylated by the activated catalytic chain.

Sequence similarities

Belongs to the cAMP-dependent kinase regulatory chain family.

Contains 2 cyclic nucleotide-binding domains.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Membrane
   DomainRepeat
   LigandcAMP
cAMP-binding
Nucleotide-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfatty acid metabolic process

Inferred from mutant phenotype PubMed 8757131. Source: MGI

learning

Inferred from mutant phenotype PubMed 9570795. Source: MGI

negative regulation of cAMP-dependent protein kinase activity

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcAMP-dependent protein kinase complex

Inferred from electronic annotation. Source: InterPro

centrosome

Inferred from electronic annotation. Source: Ensembl

ciliary base

Inferred from direct assay PubMed 22007132. Source: MGI

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

dendritic shaft

Inferred from direct assay PubMed 24464040. Source: ParkinsonsUK-UCL

dendritic spine

Inferred from direct assay PubMed 24464040. Source: ParkinsonsUK-UCL

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncAMP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cAMP-dependent protein kinase inhibitor activity

Inferred from electronic annotation. Source: Ensembl

cAMP-dependent protein kinase regulator activity

Inferred from direct assay PubMed 7775586. Source: MGI

protein binding

Inferred from physical interaction PubMed 24464040. Source: IntAct

protein kinase binding

Inferred from physical interaction PubMed 24464040. Source: ParkinsonsUK-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Lrrk2Q5S0063EBI-455340,EBI-2693710
PrkacaP051323EBI-455340,EBI-400564

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 416416cAMP-dependent protein kinase type II-beta regulatory subunit
PRO_0000205391

Regions

Nucleotide binding152 – 273122cAMP 1
Nucleotide binding274 – 416143cAMP 2
Region1 – 151151Dimerization and phosphorylation

Sites

Binding site2211cAMP 1 By similarity
Binding site2301cAMP 1 By similarity
Binding site3501cAMP 2 By similarity
Binding site3591cAMP 2 By similarity

Amino acid modifications

Modified residue831Phosphoserine By similarity
Modified residue851Phosphoserine By similarity
Modified residue1121Phosphoserine Ref.5 Ref.6 Ref.7

Experimental info

Sequence conflict691I → T in AAH48710. Ref.3

Secondary structure

............................................ 416
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P31324 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 24196C3037789827

FASTA41646,167
        10         20         30         40         50         60 
MSIEIPAGLT ELLQGFTVEV LRHQPADLLE FALQHFTRLQ QENERKGAAR FGHEGRTWGD 

        70         80         90        100        110        120 
AGAAAGGGIP SKGVNFAEEP MRSDSENGEE EEAAEAGAFN APVINRFTRR ASVCAEAYNP 

       130        140        150        160        170        180 
DEEEDDAESR IIHPKTDDQR NRLQEACKDI LLFKNLDPEQ MSQVLDAMFE KLVKEGEHVI 

       190        200        210        220        230        240 
DQGDDGDNFY VIDRGTFDIY VKCDGVGRCV GNYDNRGSFG ELALMYNTPR AATITATSPG 

       250        260        270        280        290        300 
ALWGLDRVTF RRIIVKNNAK KRKMYESFIE SLPFLKSLEV SERLKVVDVI GTKVYNDGEQ 

       310        320        330        340        350        360 
IIAQGDLADS FFIVESGEVK ITMKRKGKSE VEENGAVEIA RCFRGQYFGE LALVTNKPRA 

       370        380        390        400        410 
ASAHAIGTVK CLAMDVQAFE RLLGPCMEIM KRNIATYEEQ LVALFGTNMD IVEPTA 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Aorta and Vein.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Limb.
[4]"Molecular cloning and characterization of the promoter region of the mouse regulatory subunit RII beta of type II cAMP-dependent protein kinase."
Singh I.S., Luo Z., Eng A., Erlichman J.
Biochem. Biophys. Res. Commun. 178:221-226(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100.
[5]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[6]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[7]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[8]"Structure and allostery of the PKA RIIbeta tetrameric holoenzyme."
Zhang P., Smith-Nguyen E.V., Keshwani M.M., Deal M.S., Kornev A.P., Taylor S.S.
Science 335:712-716(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH RAT PRKACA, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK041013 mRNA. Translation: BAC30779.1.
AK138963 mRNA. Translation: BAE23838.1.
CT010463 Genomic DNA. Translation: CAM17140.1.
BC048710 mRNA. Translation: AAH48710.1.
M68861 Genomic DNA. Translation: AAA40057.1.
CCDSCCDS25869.1.
PIRPQ0161.
RefSeqNP_035288.2. NM_011158.3.
XP_006515077.1. XM_006515014.1.
UniGeneMm.25594.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3TNPX-ray2.30B/E1-416[»]
3TNQX-ray3.10A1-416[»]
ProteinModelPortalP31324.
SMRP31324. Positions 8-408.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202369. 5 interactions.
DIPDIP-31571N.
IntActP31324. 11 interactions.
MINTMINT-4099351.

PTM databases

PhosphoSiteP31324.

Proteomic databases

MaxQBP31324.
PaxDbP31324.
PRIDEP31324.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000003079; ENSMUSP00000003079; ENSMUSG00000002997.
ENSMUST00000036497; ENSMUSP00000039797; ENSMUSG00000002997.
GeneID19088.
KEGGmmu:19088.
UCSCuc007nhx.2. mouse.

Organism-specific databases

CTD5577.
MGIMGI:97760. Prkar2b.

Phylogenomic databases

eggNOGCOG0664.
GeneTreeENSGT00530000062947.
HOGENOMHOG000196668.
HOVERGENHBG002025.
InParanoidB1B199.
KOK04739.
OMAPMHSDSE.
OrthoDBEOG76T9RR.
PhylomeDBP31324.
TreeFamTF314920.

Gene expression databases

ArrayExpressP31324.
BgeeP31324.
GenevestigatorP31324.

Family and domain databases

Gene3D2.60.120.10. 2 hits.
InterProIPR002373. cAMP/cGMP_kin.
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.
[Graphical view]
PfamPF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view]
PIRSFPIRSF000548. PK_regulatory. 1 hit.
PRINTSPR00103. CAMPKINASE.
SMARTSM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
[Graphical view]
SUPFAMSSF47391. SSF47391. 1 hit.
SSF51206. SSF51206. 2 hits.
PROSITEPS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPRKAR2B. mouse.
NextBio295636.
PROP31324.
SOURCESearch...

Entry information

Entry nameKAP3_MOUSE
AccessionPrimary (citable) accession number: P31324
Secondary accession number(s): B1B199 expand/collapse secondary AC list , Q3UTZ1, Q80ZM4, Q8BRZ7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 128 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot