P31324 (KAP3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
cAMP-dependent protein kinase type II-beta regulatory subunit

Gene names

Name:

Prkar2b

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	416 AA.
Sequence status	Complete.
Protein existence	Evidence 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.10
Subcellular location	Cytoplasm By similarity. Cell membrane By similarity. Note: Co-localizes 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 component	Cell membrane Cytoplasm Membrane
Domain	Repeat
Ligand	Nucleotide-binding cAMP cAMP-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell proliferation Traceable author statement PubMed 7775586. Source: MGI fatty acid metabolic process Inferred from mutant phenotype PubMed 8757131. Source: MGI learning Inferred from mutant phenotype PubMed 9570795. Source: MGI organ morphogenesis Traceable author statement PubMed 7775586. Source: MGI protein phosphorylation Traceable author statement PubMed 7775586. Source: MGI response to antipsychotic drug Inferred from electronic annotation. Source: Compara response to clozapine Inferred from electronic annotation. Source: Compara signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	cAMP-dependent protein kinase complex Inferred from electronic annotation. Source: Compara centrosome Inferred from electronic annotation. Source: Compara membrane raft Inferred from electronic annotation. Source: Compara mitochondrial inner membrane Inferred from electronic annotation. Source: Compara perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cAMP binding Inferred from electronic annotation. Source: UniProtKB-KW cAMP-dependent protein kinase regulator activity Inferred from direct assay PubMed 7775586. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 416

416

cAMP-dependent protein kinase type II-beta regulatory subunit

PRO_0000205391

Regions

Nucleotide binding

152 – 273

122

cAMP 1

Nucleotide binding

274 – 416

143

cAMP 2

Region

1 – 151

151

Dimerization and phosphorylation

Sites

Binding site

221

1

cAMP 1 By similarity

Binding site

230

1

cAMP 1 By similarity

Binding site

350

1

cAMP 2 By similarity

Binding site

359

1

cAMP 2 By similarity

Amino acid modifications

Modified residue

83

1

Phosphoserine By similarity

Modified residue

85

1

Phosphoserine By similarity

Modified residue

112

1

Phosphoserine Ref.5 Ref.6 Ref.7 Ref.8 Ref.9

Experimental info

Sequence conflict

69

1

I → T in AAH48710. Ref.3

Secondary structure

1

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416

Helix Strand Turn

Details...

Helix

137 – 147

11

Helix

151 – 154

4

Helix

158 – 167

10

Beta strand

169 – 173

5

Beta strand

178 – 180

3

Beta strand

188 – 194

7

Beta strand

196 – 202

7

Beta strand

207 – 215

9

Helix

221 – 224

4

Beta strand

231 – 246

16

Helix

247 – 261

15

Beta strand

262 – 268

7

Helix

269 – 271

3

Helix

273 – 275

3

Helix

280 – 289

10

Beta strand

291 – 295

5

Beta strand

300 – 302

3

Beta strand

310 – 322

13

Beta strand

338 – 342

5

Beta strand

347 – 349

3

Helix

350 – 353

4

Beta strand

360 – 375

16

Helix

376 – 383

8

Helix

386 – 390

5

Sequences

	Sequence		Length	Mass (Da)
	P31324 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 24196C3037789827	FASTA	416	46,167
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. Tissue: Brain.
[6]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, MASS SPECTROMETRY. Tissue: Liver.
[7]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, MASS SPECTROMETRY. Tissue: Brain cortex.
[8]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, MASS SPECTROMETRY. Tissue: Melanoma.
[9]	"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, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
[10]	"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.

IPI

IPI00224570.

PIR

PQ0161.

RefSeq

NP_035288.2. NM_011158.3.

UniGene

Mm.25594.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3TNP	X-ray	2.30	B/E	1-416	[»]
3TNQ	X-ray	3.10	A	1-416	[»]

ProteinModelPortal

P31324.

SMR

P31324. Positions 8-39, 78-412.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31571N.

IntAct

P31324. 7 interactions.

PTM databases

PhosphoSite

P31324.

Proteomic databases

PaxDb

P31324.

PRIDE

P31324.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000003079; ENSMUSP00000003079; ENSMUSG00000002997.
ENSMUST00000036497; ENSMUSP00000039797; ENSMUSG00000002997.

GeneID

19088.

KEGG

mmu:19088.

UCSC

uc007nhx.1. mouse.

Organism-specific databases

CTD

5577.

MGI

MGI:97760. Prkar2b.

Phylogenomic databases

eggNOG

COG0664.

GeneTree

ENSGT00530000062947.

HOGENOM

HOG000196668.

HOVERGEN

HBG002025.

InParanoid

B1B199.

KO

K04739.

OMA

MYENFIE.

OrthoDB

EOG4RV2RN.

Gene expression databases

ArrayExpress

P31324.

Bgee

P31324.

Genevestigator

P31324.

GermOnline

ENSMUSG00000002997. Mus musculus.

Family and domain databases

Gene3D

2.60.120.10. 2 hits.

InterPro

IPR002373. 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]

Pfam

PF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view]

PIRSF

PIRSF000548. PK_regulatory. 1 hit.

PRINTS

PR00103. CAMPKINASE.

SMART

SM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
[Graphical view]

SUPFAM

SSF47391. cAMP-dep_prot_kin_reg_I/II_a/b. 1 hit.
SSF51206. cNMP_binding. 2 hits.

PROSITE

PS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

PRKAR2B. mouse.

NextBio

295636.

SOURCE

Search...

Entry information

Entry name

KAP3_MOUSE

Accession

Primary (citable) accession number: P31324
Secondary accession number(s): B1B199 , Q3UTZ1, Q80ZM4, Q8BRZ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 115 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program