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P31324

- KAP3_MOUSE

UniProt

P31324 - KAP3_MOUSE

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
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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

    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

    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

    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.3 Publications

    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.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.

    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.
    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.
    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

    Experimental Info

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

    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

    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: October 1, 2014
    This is version 130 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