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Protein

cAMP-dependent protein kinase type II-beta regulatory subunit

Gene

Prkar2b

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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei221 – 2211cAMP 1By similarity
Binding sitei230 – 2301cAMP 1By similarity
Binding sitei350 – 3501cAMP 2By similarity
Binding sitei359 – 3591cAMP 2By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi152 – 273122cAMP 1Add
BLAST
Nucleotide bindingi274 – 416143cAMP 2Add
BLAST

GO - Molecular functioni

GO - Biological processi

  • fatty acid metabolic process Source: MGI
  • learning Source: MGI
  • negative regulation of cAMP-dependent protein kinase activity Source: MGI
Complete GO annotation...

Keywords - Ligandi

cAMP, cAMP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_272448. Recruitment of mitotic centrosome proteins and complexes.
REACT_276302. Loss of Nlp from mitotic centrosomes.
REACT_278699. Hedgehog 'off' state.
REACT_280010. Factors involved in megakaryocyte development and platelet production.
REACT_286537. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_286837. Vasopressin regulates renal water homeostasis via Aquaporins.
REACT_295338. PKA activation in glucagon signalling.
REACT_310977. PKA activation.
REACT_325290. DARPP-32 events.
REACT_328862. Anchoring of the basal body to the plasma membrane.
REACT_345278. Regulation of PLK1 Activity at G2/M Transition.

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP-dependent protein kinase type II-beta regulatory subunit
Gene namesi
Name:Prkar2b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:97760. 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: InterPro
  • centrosome Source: MGI
  • ciliary base Source: MGI
  • cytoplasm Source: MGI
  • dendritic shaft Source: ParkinsonsUK-UCL
  • dendritic spine Source: ParkinsonsUK-UCL
  • extracellular exosome Source: MGI
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 416416cAMP-dependent protein kinase type II-beta regulatory subunitPRO_0000205391Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei83 – 831PhosphoserineBy similarity
Modified residuei85 – 851PhosphoserineBy similarity
Modified residuei112 – 1121Phosphoserine3 Publications

Post-translational modificationi

Phosphorylated by the activated catalytic chain.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP31324.
PaxDbiP31324.
PRIDEiP31324.

PTM databases

PhosphoSiteiP31324.

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.

Gene expression databases

BgeeiP31324.
ExpressionAtlasiP31324. baseline and differential.
GenevisibleiP31324. MM.

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

Protein-protein interaction databases

BioGridi202369. 5 interactions.
DIPiDIP-31571N.
IntActiP31324. 11 interactions.
MINTiMINT-4099351.
STRINGi10090.ENSMUSP00000003079.

Structurei

Secondary structure

1
416
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi137 – 14711Combined sources
Helixi151 – 1544Combined sources
Helixi158 – 16710Combined sources
Beta strandi169 – 1735Combined sources
Beta strandi178 – 1803Combined sources
Beta strandi188 – 1947Combined sources
Beta strandi196 – 2027Combined sources
Beta strandi207 – 2159Combined sources
Helixi221 – 2244Combined sources
Beta strandi231 – 24616Combined sources
Helixi247 – 26115Combined sources
Beta strandi262 – 2687Combined sources
Helixi269 – 2713Combined sources
Helixi273 – 2753Combined sources
Helixi280 – 28910Combined sources
Beta strandi291 – 2955Combined sources
Beta strandi300 – 3023Combined sources
Beta strandi310 – 32213Combined sources
Beta strandi338 – 3425Combined sources
Beta strandi347 – 3493Combined sources
Helixi350 – 3534Combined sources
Beta strandi360 – 37516Combined sources
Helixi376 – 3838Combined sources
Helixi386 – 3905Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TNPX-ray2.30B/E1-416[»]
3TNQX-ray3.10A1-416[»]
ProteinModelPortaliP31324.
SMRiP31324. Positions 8-408.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 151151Dimerization and phosphorylationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0664.
GeneTreeiENSGT00530000062947.
HOGENOMiHOG000196668.
HOVERGENiHBG002025.
InParanoidiP31324.
KOiK04739.
OMAiPMHSDSE.
OrthoDBiEOG76T9RR.
PhylomeDBiP31324.
TreeFamiTF314920.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR002373. 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]
PfamiPF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view]
PIRSFiPIRSF000548. PK_regulatory. 1 hit.
PRINTSiPR00103. CAMPKINASE.
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.

P31324-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIEIPAGLT ELLQGFTVEV LRHQPADLLE FALQHFTRLQ QENERKGAAR
60 70 80 90 100
FGHEGRTWGD AGAAAGGGIP 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
IIAQGDLADS FFIVESGEVK ITMKRKGKSE VEENGAVEIA RCFRGQYFGE
360 370 380 390 400
LALVTNKPRA ASAHAIGTVK CLAMDVQAFE RLLGPCMEIM KRNIATYEEQ
410
LVALFGTNMD IVEPTA
Length:416
Mass (Da):46,167
Last modified:January 23, 2007 - v3
Checksum:i24196C3037789827
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 691I → T in AAH48710 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS25869.1.
PIRiPQ0161.
RefSeqiNP_035288.2. NM_011158.3.
XP_006515077.1. XM_006515014.2.
UniGeneiMm.25594.

Genome annotation databases

EnsembliENSMUST00000003079; ENSMUSP00000003079; ENSMUSG00000002997.
ENSMUST00000036497; ENSMUSP00000039797; ENSMUSG00000002997.
GeneIDi19088.
KEGGimmu:19088.
UCSCiuc007nhx.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS25869.1.
PIRiPQ0161.
RefSeqiNP_035288.2. NM_011158.3.
XP_006515077.1. XM_006515014.2.
UniGeneiMm.25594.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TNPX-ray2.30B/E1-416[»]
3TNQX-ray3.10A1-416[»]
ProteinModelPortaliP31324.
SMRiP31324. Positions 8-408.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202369. 5 interactions.
DIPiDIP-31571N.
IntActiP31324. 11 interactions.
MINTiMINT-4099351.
STRINGi10090.ENSMUSP00000003079.

PTM databases

PhosphoSiteiP31324.

Proteomic databases

MaxQBiP31324.
PaxDbiP31324.
PRIDEiP31324.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000003079; ENSMUSP00000003079; ENSMUSG00000002997.
ENSMUST00000036497; ENSMUSP00000039797; ENSMUSG00000002997.
GeneIDi19088.
KEGGimmu:19088.
UCSCiuc007nhx.2. mouse.

Organism-specific databases

CTDi5577.
MGIiMGI:97760. Prkar2b.

Phylogenomic databases

eggNOGiCOG0664.
GeneTreeiENSGT00530000062947.
HOGENOMiHOG000196668.
HOVERGENiHBG002025.
InParanoidiP31324.
KOiK04739.
OMAiPMHSDSE.
OrthoDBiEOG76T9RR.
PhylomeDBiP31324.
TreeFamiTF314920.

Enzyme and pathway databases

ReactomeiREACT_272448. Recruitment of mitotic centrosome proteins and complexes.
REACT_276302. Loss of Nlp from mitotic centrosomes.
REACT_278699. Hedgehog 'off' state.
REACT_280010. Factors involved in megakaryocyte development and platelet production.
REACT_286537. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_286837. Vasopressin regulates renal water homeostasis via Aquaporins.
REACT_295338. PKA activation in glucagon signalling.
REACT_310977. PKA activation.
REACT_325290. DARPP-32 events.
REACT_328862. Anchoring of the basal body to the plasma membrane.
REACT_345278. Regulation of PLK1 Activity at G2/M Transition.

Miscellaneous databases

ChiTaRSiPrkar2b. mouse.
NextBioi295636.
PROiP31324.
SOURCEiSearch...

Gene expression databases

BgeeiP31324.
ExpressionAtlasiP31324. baseline and differential.
GenevisibleiP31324. MM.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR002373. 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]
PfamiPF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view]
PIRSFiPIRSF000548. PK_regulatory. 1 hit.
PRINTSiPR00103. CAMPKINASE.
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...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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 PRKACA, SUBUNIT.

Entry informationi

Entry nameiKAP3_MOUSE
AccessioniPrimary (citable) accession number: P31324
Secondary accession number(s): B1B199
, Q3UTZ1, Q80ZM4, Q8BRZ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 138 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. 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

External Data

Dasty 3

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 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.