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P31324

- KAP3_MOUSE

UniProt

P31324 - KAP3_MOUSE

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Protein

cAMP-dependent protein kinase type II-beta regulatory subunit

Gene
Prkar2b
Organism
Mus musculus (Mouse)
Status
Reviewed - 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 1 By similarity
Binding sitei230 – 2301cAMP 1 By similarity
Binding sitei350 – 3501cAMP 2 By similarity
Binding sitei359 – 3591cAMP 2 By similarity

Regions

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

GO - Molecular functioni

  1. cAMP binding Source: UniProtKB-KW
  2. cAMP-dependent protein kinase inhibitor activity Source: Ensembl
  3. cAMP-dependent protein kinase regulator activity Source: MGI
  4. protein binding Source: IntAct
  5. protein kinase binding Source: ParkinsonsUK-UCL

GO - Biological processi

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

Keywords - Ligandi

cAMP, cAMP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_196635. Regulation of PLK1 Activity at G2/M Transition.
REACT_198649. Factors involved in megakaryocyte development and platelet production.
REACT_203795. DARPP-32 events.
REACT_213947. Regulation of water balance by renal Aquaporins.
REACT_220108. PKA activation.
REACT_220758. PKA activation in glucagon signalling.

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: 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

  1. cAMP-dependent protein kinase complex Source: InterPro
  2. centrosome Source: Ensembl
  3. ciliary base Source: MGI
  4. cytoplasm Source: UniProtKB-SubCell
  5. dendritic shaft Source: ParkinsonsUK-UCL
  6. dendritic spine Source: ParkinsonsUK-UCL
  7. plasma membrane Source: UniProtKB-SubCell
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 – 831Phosphoserine By similarity
Modified residuei85 – 851Phosphoserine By 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

ArrayExpressiP31324.
BgeeiP31324.
GenevestigatoriP31324.

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.1 Publication

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.

Structurei

Secondary structure

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

3D structure databases

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

Family & Domainsi

Region

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

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0664.
GeneTreeiENSGT00530000062947.
HOGENOMiHOG000196668.
HOVERGENiHBG002025.
InParanoidiB1B199.
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

MSIEIPAGLT ELLQGFTVEV LRHQPADLLE FALQHFTRLQ QENERKGAAR    50
FGHEGRTWGD AGAAAGGGIP SKGVNFAEEP MRSDSENGEE EEAAEAGAFN 100
APVINRFTRR ASVCAEAYNP DEEEDDAESR IIHPKTDDQR NRLQEACKDI 150
LLFKNLDPEQ MSQVLDAMFE KLVKEGEHVI DQGDDGDNFY VIDRGTFDIY 200
VKCDGVGRCV GNYDNRGSFG ELALMYNTPR AATITATSPG ALWGLDRVTF 250
RRIIVKNNAK KRKMYESFIE SLPFLKSLEV SERLKVVDVI GTKVYNDGEQ 300
IIAQGDLADS FFIVESGEVK ITMKRKGKSE VEENGAVEIA RCFRGQYFGE 350
LALVTNKPRA ASAHAIGTVK CLAMDVQAFE RLLGPCMEIM KRNIATYEEQ 400
LVALFGTNMD IVEPTA 416
Length:416
Mass (Da):46,167
Last modified:January 23, 2007 - v3
Checksum:i24196C3037789827
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 691I → T in AAH48710. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_006515014.1.
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS25869.1.
PIRi PQ0161.
RefSeqi NP_035288.2. NM_011158.3.
XP_006515077.1. XM_006515014.1.
UniGenei Mm.25594.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3TNP X-ray 2.30 B/E 1-416 [» ]
3TNQ X-ray 3.10 A 1-416 [» ]
ProteinModelPortali P31324.
SMRi P31324. Positions 8-408.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202369. 5 interactions.
DIPi DIP-31571N.
IntActi P31324. 11 interactions.
MINTi MINT-4099351.

PTM databases

PhosphoSitei P31324.

Proteomic databases

MaxQBi P31324.
PaxDbi P31324.
PRIDEi P31324.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000003079 ; ENSMUSP00000003079 ; ENSMUSG00000002997 .
ENSMUST00000036497 ; ENSMUSP00000039797 ; ENSMUSG00000002997 .
GeneIDi 19088.
KEGGi mmu:19088.
UCSCi uc007nhx.2. mouse.

Organism-specific databases

CTDi 5577.
MGIi MGI:97760. Prkar2b.

Phylogenomic databases

eggNOGi COG0664.
GeneTreei ENSGT00530000062947.
HOGENOMi HOG000196668.
HOVERGENi HBG002025.
InParanoidi B1B199.
KOi K04739.
OMAi PMHSDSE.
OrthoDBi EOG76T9RR.
PhylomeDBi P31324.
TreeFami TF314920.

Enzyme and pathway databases

Reactomei REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
REACT_198649. Factors involved in megakaryocyte development and platelet production.
REACT_203795. DARPP-32 events.
REACT_213947. Regulation of water balance by renal Aquaporins.
REACT_220108. PKA activation.
REACT_220758. PKA activation in glucagon signalling.

Miscellaneous databases

ChiTaRSi PRKAR2B. mouse.
NextBioi 295636.
PROi P31324.
SOURCEi Search...

Gene expression databases

ArrayExpressi P31324.
Bgeei P31324.
Genevestigatori P31324.

Family and domain databases

Gene3Di 2.60.120.10. 2 hits.
InterProi 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 ]
Pfami PF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view ]
PIRSFi PIRSF000548. PK_regulatory. 1 hit.
PRINTSi PR00103. CAMPKINASE.
SMARTi SM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
[Graphical view ]
SUPFAMi SSF47391. SSF47391. 1 hit.
SSF51206. SSF51206. 2 hits.
PROSITEi PS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view ]
ProtoNeti Search...

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 RAT 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: September 3, 2014
This is version 129 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

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