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Q9DBC7

- KAP0_MOUSE

UniProt

Q9DBC7 - KAP0_MOUSE

Protein

cAMP-dependent protein kinase type I-alpha regulatory subunit

Gene

Prkar1a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (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.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei202 – 2021cAMP 1
    Binding sitei211 – 2111cAMP 1
    Binding sitei326 – 3261cAMP 2
    Binding sitei335 – 3351cAMP 2

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi137 – 254118cAMP 1Add
    BLAST
    Nucleotide bindingi255 – 381127cAMP 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: UniProtKB

    GO - Biological processi

    1. cardiac muscle cell proliferation Source: MGI
    2. cell proliferation Source: MGI
    3. female meiotic division Source: Ensembl
    4. heart development Source: MGI
    5. mesoderm formation Source: MGI
    6. negative regulation of cAMP-dependent protein kinase activity Source: Ensembl
    7. negative regulation of meiosis Source: Ensembl
    8. negative regulation of protein kinase activity Source: MGI
    9. organ morphogenesis Source: MGI
    10. protein phosphorylation Source: MGI
    11. sarcomere organization Source: MGI

    Keywords - Ligandi

    cAMP, cAMP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_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 I-alpha regulatory subunit
    Cleaved into the following chain:
    Gene namesi
    Name:Prkar1a
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:104878. Prkar1a.

    Subcellular locationi

    Cell membrane By similarity

    GO - Cellular componenti

    1. AMP-activated protein kinase complex Source: Ensembl
    2. cAMP-dependent protein kinase complex Source: Ensembl
    3. cytoplasm Source: MGI
    4. neuromuscular junction Source: MGI
    5. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 381381cAMP-dependent protein kinase type I-alpha regulatory subunitPRO_0000205378Add
    BLAST
    Initiator methioninei1 – 11Removed; alternateBy similarity
    Chaini2 – 381380cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processedPRO_0000421786Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei2 – 21N-acetylalanineCurated
    Disulfide bondi18 – 18Interchain (with C-39)By similarity
    Disulfide bondi39 – 39Interchain (with C-18)By similarity
    Modified residuei83 – 831Phosphoserine2 Publications
    Modified residuei101 – 1011Phosphoserine1 Publication

    Post-translational modificationi

    The pseudophosphorylation site binds to the substrate-binding region of the catalytic chain, resulting in the inhibition of its activity.By similarity

    Keywords - PTMi

    Acetylation, Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiQ9DBC7.
    PaxDbiQ9DBC7.
    PRIDEiQ9DBC7.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00762049.
    Q9DBC7.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9DBC7.
    BgeeiQ9DBC7.
    GenevestigatoriQ9DBC7.

    Interactioni

    Subunit structurei

    The inactive holoenzyme is composed of two regulatory chains and two catalytic chains. Activation by cAMP releases the two active catalytic monomers and the regulatory dimer. PRKAR1A also interacts with RFC2; the complex may be involved in cell survival. Interacts with AKAP4. Interacts with RARA; the interaction occurs in the presence of cAMP or FSH and regulates RARA transcriptional activity. Interacts with the phosphorylated form of PJA2. Interacts with PRKX; regulates this cAMP-dependent protein kinase By similarity. Interacts with CBFA2T3. Interacts with smAKAP; this interaction may target PRKAR1A to the plasma membrane. Interacts with AICDA By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Bcl2l11O54918-12EBI-645677,EBI-526076

    Protein-protein interaction databases

    IntActiQ9DBC7. 13 interactions.
    MINTiMINT-1741651.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9DBC7.
    SMRiQ9DBC7. Positions 14-380.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 136136Dimerization and phosphorylationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi96 – 1005Pseudophosphorylation motif

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0664.
    GeneTreeiENSGT00530000062947.
    HOVERGENiHBG002025.
    InParanoidiQ9DBC7.
    KOiK04739.
    OMAiFSAEVYT.
    OrthoDBiEOG72JWG6.
    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9DBC7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASGSMATSE EERSLRECEL YVQKHNIQAL LKDSIVQLCT TRPERPMAFL    50
    REYFERLEKE EARQIQCLQK TGIRTDSRED EISPPPPNPV VKGRRRRGAI 100
    SAEVYTEEDA ASYVRKVIPK DYKTMAALAK AIEKNVLFSH LDDNERSDIF 150
    DAMFPVSFIA GETVIQQGDE GDNFYVIDQG EMDVYVNNEW ATSVGEGGSF 200
    GELALIYGTP RAATVKAKTN VKLWGIDRDS YRRILMGSTL RKRKMYEEFL 250
    SKVSILESLD KWERLTVADA LEPVQFEDGQ KIVVQGEPGD EFFIILEGTA 300
    AVLQRRSENE EFVEVGRLGP SDYFGEIALL MNRPRAATVV ARGPLKCVKL 350
    DRPRFERVLG PCSDILKRNI QQYNSFVSLS V 381
    Length:381
    Mass (Da):43,185
    Last modified:January 23, 2007 - v3
    Checksum:i08F164BB4528C63B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK005039 mRNA. Translation: BAB23766.1.
    AK027916 mRNA. Translation: BAC25664.1.
    AK051068 mRNA. Translation: BAC34516.1.
    AK145797 mRNA. Translation: BAE26655.1.
    AK145860 mRNA. Translation: BAE26704.1.
    AK147188 mRNA. Translation: BAE27748.1.
    AK150427 mRNA. Translation: BAE29550.1.
    AK151124 mRNA. Translation: BAE30132.1.
    AK153227 mRNA. Translation: BAE31820.1.
    BC003461 mRNA. Translation: AAH03461.1.
    BC005697 mRNA. Translation: AAH05697.1.
    AJ278427 Genomic DNA. Translation: CAB94778.1.
    AJ278429 Genomic DNA. Translation: CAB94718.1.
    CCDSiCCDS25583.1.
    RefSeqiNP_068680.1. NM_021880.2.
    XP_006532574.1. XM_006532511.1.
    UniGeneiMm.30039.

    Genome annotation databases

    EnsembliENSMUST00000049527; ENSMUSP00000056500; ENSMUSG00000020612.
    ENSMUST00000106677; ENSMUSP00000102288; ENSMUSG00000020612.
    GeneIDi19084.
    KEGGimmu:19084.
    UCSCiuc007mcu.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK005039 mRNA. Translation: BAB23766.1 .
    AK027916 mRNA. Translation: BAC25664.1 .
    AK051068 mRNA. Translation: BAC34516.1 .
    AK145797 mRNA. Translation: BAE26655.1 .
    AK145860 mRNA. Translation: BAE26704.1 .
    AK147188 mRNA. Translation: BAE27748.1 .
    AK150427 mRNA. Translation: BAE29550.1 .
    AK151124 mRNA. Translation: BAE30132.1 .
    AK153227 mRNA. Translation: BAE31820.1 .
    BC003461 mRNA. Translation: AAH03461.1 .
    BC005697 mRNA. Translation: AAH05697.1 .
    AJ278427 Genomic DNA. Translation: CAB94778.1 .
    AJ278429 Genomic DNA. Translation: CAB94718.1 .
    CCDSi CCDS25583.1.
    RefSeqi NP_068680.1. NM_021880.2.
    XP_006532574.1. XM_006532511.1.
    UniGenei Mm.30039.

    3D structure databases

    ProteinModelPortali Q9DBC7.
    SMRi Q9DBC7. Positions 14-380.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9DBC7. 13 interactions.
    MINTi MINT-1741651.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00762049.
    Q9DBC7.

    Proteomic databases

    MaxQBi Q9DBC7.
    PaxDbi Q9DBC7.
    PRIDEi Q9DBC7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000049527 ; ENSMUSP00000056500 ; ENSMUSG00000020612 .
    ENSMUST00000106677 ; ENSMUSP00000102288 ; ENSMUSG00000020612 .
    GeneIDi 19084.
    KEGGi mmu:19084.
    UCSCi uc007mcu.1. mouse.

    Organism-specific databases

    CTDi 5573.
    MGIi MGI:104878. Prkar1a.

    Phylogenomic databases

    eggNOGi COG0664.
    GeneTreei ENSGT00530000062947.
    HOVERGENi HBG002025.
    InParanoidi Q9DBC7.
    KOi K04739.
    OMAi FSAEVYT.
    OrthoDBi EOG72JWG6.
    TreeFami TF314920.

    Enzyme and pathway databases

    Reactomei 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 PRKAR1A. mouse.
    NextBioi 295622.
    PROi Q9DBC7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9DBC7.
    Bgeei Q9DBC7.
    Genevestigatori Q9DBC7.

    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: Bone marrow, Kidney, Liver and Placenta.
    2. "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].
      Strain: FVB/N.
      Tissue: Mammary tumor.
    3. "Alternative 5'-exons of the mouse cAMP-dependent protein kinase subunit RIalpha gene are conserved and expressed in both a ubiquitous and tissue-restricted fashion."
      Barradeau S., Imaizumi-Scherrer T., Weiss M.C., Faust D.M.
      FEBS Lett. 476:272-276(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-60 AND 259-382.
    4. "Identification of tethering domains for protein kinase A type Ialpha regulatory subunits on sperm fibrous sheath protein FSC1."
      Miki K., Eddy E.M.
      J. Biol. Chem. 273:34384-34390(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AKAP4.
    5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    7. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
      Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
      J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    8. "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-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    9. "Myeloid translocation gene 16b is a dual A-kinase anchoring protein that interacts selectively with plexins in a phospho-regulated manner."
      Fiedler S.E., Schillace R.V., Daniels C.J., Andrews S.F., Carr D.W.
      FEBS Lett. 584:873-877(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CBFA2T3.

    Entry informationi

    Entry nameiKAP0_MOUSE
    AccessioniPrimary (citable) accession number: Q9DBC7
    Secondary accession number(s): Q3UKU7, Q9JHR5, Q9JHR6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 112 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Two types of regulatory chains are found: type I, which predominates in skeletal muscle, and type II, which predominates in cardiac muscle.By similarity

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3