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P12368

- KAP2_RAT

UniProt

P12368 - KAP2_RAT

Protein

cAMP-dependent protein kinase type II-alpha regulatory subunit

Gene

Prkar2a

Organism
Rattus norvegicus (Rat)
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 sitei205 – 2051cAMP 1By similarity
    Binding sitei214 – 2141cAMP 1By similarity
    Binding sitei335 – 3351cAMP 2By similarity
    Binding sitei344 – 3441cAMP 2By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi136 – 257122cAMP 1By similarityAdd
    BLAST
    Nucleotide bindingi258 – 401144cAMP 2By similarityAdd
    BLAST

    GO - Molecular functioni

    1. cAMP binding Source: RGD
    2. cAMP-dependent protein kinase regulator activity Source: RGD
    3. protein binding Source: RGD
    4. protein domain specific binding Source: RGD
    5. protein homodimerization activity Source: RGD
    6. protein kinase A catalytic subunit binding Source: RGD
    7. small molecule binding Source: RGD

    GO - Biological processi

    1. protein heterooligomerization Source: RGD
    2. regulation of protein kinase activity Source: RGD
    3. response to clozapine Source: RGD

    Keywords - Ligandi

    cAMP, cAMP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    cAMP-dependent protein kinase type II-alpha regulatory subunit
    Gene namesi
    Name:Prkar2a
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi3393. Prkar2a.

    Subcellular locationi

    Cytoplasm By similarity. Cell membrane By similarity
    Note: Colocalizes with PJA2 in the cytoplasm and the cell membrane.By similarity

    GO - Cellular componenti

    1. cAMP-dependent protein kinase complex Source: RGD
    2. cytoplasm Source: RGD
    3. perinuclear region of cytoplasm Source: RGD
    4. protein complex Source: RGD
    5. T-tubule Source: RGD

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 401400cAMP-dependent protein kinase type II-alpha regulatory subunitPRO_0000205388Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei48 – 481PhosphoserineBy similarity
    Modified residuei75 – 751PhosphoserineBy similarity
    Modified residuei77 – 771PhosphoserineBy similarity
    Modified residuei97 – 971Phosphoserine1 Publication
    Modified residuei212 – 2121Phosphothreonine; by PDPK1By similarity

    Post-translational modificationi

    Phosphorylated by the activated catalytic chain.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP12368.
    PRIDEiP12368.

    PTM databases

    PhosphoSiteiP12368.

    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

    GenevestigatoriP12368.

    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 AKAP4 and CBFA2T3 By similarity. Interacts with the phosphorylated form of PJA2 By similarity. Interacts with MYRIP; his interaction may link PKA to components of the exocytosis machinery, thus facilitating exocytosis, including insulin release.By similarity1 Publication

    Protein-protein interaction databases

    DIPiDIP-555N.
    IntActiP12368. 4 interactions.
    MINTiMINT-4564663.
    STRINGi10116.ENSRNOP00000027552.

    Structurei

    Secondary structure

    1
    401
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 2415
    Helixi29 – 4315

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DRNNMR-A/B1-45[»]
    2H9RNMR-A/B1-45[»]
    2HWNX-ray1.60A/B/C/D1-45[»]
    3TMHX-ray3.80B/C/F/G1-45[»]
    ProteinModelPortaliP12368.
    SMRiP12368. Positions 1-45, 93-393.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12368.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 135134Dimerization and phosphorylationAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0664.
    HOGENOMiHOG000196668.
    HOVERGENiHBG002025.
    InParanoidiP12368.
    KOiK04739.
    PhylomeDBiP12368.

    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.

    P12368-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSHIQIPPGL TELLQGYTVE VLRQQPPDLV DFAVEYFTRL REARRQESDS    50
    FIAPPTTFHA QESSGVPVIE EDGESESDSD DEDLEVPIPS KFTRRVSVCA 100
    ETFNPDEEED NDPRVVHPKT DEQRYRLQEA CKDILLFKNL DQEQLSQVLD 150
    AMFEKIVKTD EHVIDQGDDG DNFYVIERGT YDILVTKDNQ TRSVGQYDNR 200
    GSFGELALMY NTPRAATIVA TSDGSLWGLD RVTFRRIIVK NNAKKRKMFE 250
    SFIESVPLFK SLEMSERMKI VDVIGEKIYK DGERIITQGE KADSFYIIES 300
    GEVSILIRSK TKTNKNGGNQ EVEIAHCHKG QYFGELALVT NKPRAASAYA 350
    VGDVKCLVMD VQAFERLLGP CMDIMKRNIS HYEEQLVKMF GSNLDLLDPG 400
    Q 401
    Length:401
    Mass (Da):45,540
    Last modified:January 23, 2007 - v3
    Checksum:i026FEBFCFACA9C7D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti74 – 741E → Q in AAA41856. (PubMed:3037538)Curated
    Sequence conflicti90 – 901S → A in AAA41856. (PubMed:3037538)Curated
    Sequence conflicti125 – 1251Y → C in AAA41856. (PubMed:3037538)Curated
    Sequence conflicti154 – 1552EK → KR in AAA41856. (PubMed:3037538)Curated
    Sequence conflicti198 – 1981D → A in AAA41856. (PubMed:3037538)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF533978 mRNA. Translation: AAM97689.1.
    J02934 mRNA. Translation: AAA41856.1.
    PIRiA28325. OKRT2R.
    RefSeqiNP_062137.1. NM_019264.2.
    UniGeneiRn.9742.

    Genome annotation databases

    GeneIDi29699.
    KEGGirno:29699.
    UCSCiRGD:3393. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF533978 mRNA. Translation: AAM97689.1 .
    J02934 mRNA. Translation: AAA41856.1 .
    PIRi A28325. OKRT2R.
    RefSeqi NP_062137.1. NM_019264.2.
    UniGenei Rn.9742.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DRN NMR - A/B 1-45 [» ]
    2H9R NMR - A/B 1-45 [» ]
    2HWN X-ray 1.60 A/B/C/D 1-45 [» ]
    3TMH X-ray 3.80 B/C/F/G 1-45 [» ]
    ProteinModelPortali P12368.
    SMRi P12368. Positions 1-45, 93-393.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-555N.
    IntActi P12368. 4 interactions.
    MINTi MINT-4564663.
    STRINGi 10116.ENSRNOP00000027552.

    PTM databases

    PhosphoSitei P12368.

    Proteomic databases

    PaxDbi P12368.
    PRIDEi P12368.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 29699.
    KEGGi rno:29699.
    UCSCi RGD:3393. rat.

    Organism-specific databases

    CTDi 5576.
    RGDi 3393. Prkar2a.

    Phylogenomic databases

    eggNOGi COG0664.
    HOGENOMi HOG000196668.
    HOVERGENi HBG002025.
    InParanoidi P12368.
    KOi K04739.
    PhylomeDBi P12368.

    Miscellaneous databases

    EvolutionaryTracei P12368.
    NextBioi 610099.
    PROi P12368.

    Gene expression databases

    Genevestigatori P12368.

    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. "cDNA sequence and complete coding region of cAMP-dependent protein kinase type II regulatory subunit from a rat testicular germ cell cDNA library."
      Ziemba A.J., Collard M.W.
      Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.
      Tissue: Testis.
    2. "The molecular cloning of a type II regulatory subunit of the cAMP-dependent protein kinase from rat skeletal muscle and mouse brain."
      Scott J.D., Glaccum M.B., Zoller M.J., Uhler M.D., Helfman D.M., McKnight G.S., Krebs E.G.
      Proc. Natl. Acad. Sci. U.S.A. 84:5192-5196(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-401.
      Tissue: Skeletal muscle.
    3. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
      Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
      Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    4. Cited for: INTERACTION WITH MYRIP.

    Entry informationi

    Entry nameiKAP2_RAT
    AccessioniPrimary (citable) accession number: P12368
    Secondary accession number(s): Q8K1M2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3