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P05132

- KAPCA_MOUSE

UniProt

P05132 - KAPCA_MOUSE

Protein

cAMP-dependent protein kinase catalytic subunit alpha

Gene

Prkaca

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 183 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Phosphorylates a large number of substrates in the cytoplasm and the nucleus. Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. Phosphorylates CDC25B, ABL1, NFKB1, CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA and VASP. RORA is activated by phosphorylation. Required for glucose-mediated adipogenic differentiation increase and osteogenic differentiation inhibition from osteoblasts. Involved in the regulation of platelets in response to thrombin and collagen; maintains circulating platelets in a resting state by phosphorylating proteins in numerous platelet inhibitory pathways when in complex with NF-kappa-B (NFKB1 and NFKB2) and I-kappa-B-alpha (NFKBIA), but thrombin and collagen disrupt these complexes and free active PRKACA stimulates platelets and leads to platelet aggregation by phosphorylating VASP. Prevents the antiproliferative and anti-invasive effects of alpha-difluoromethylornithine in breast cancer cells when activated. RYR2 channel activity is potentiated by phosphorylation in presence of luminal Ca2+, leading to reduced amplitude and increased frequency of store overload-induced Ca2+ release (SOICR) characterized by an increased rate of Ca2+ release and propagation velocity of spontaneous Ca2+ waves, despite reduced wave amplitude and resting cytosolic Ca2+. PSMC5/RPT6 activation by phosphorylation stimulates proteasome. Negatively regulates tight junctions (TJs) in ovarian cancer cells via CLDN3 phosphorylation. NFKB1 phosphorylation promotes NF-kappa-B p50-p50 DNA binding. Involved in embryonic development by down-regulating the Hedgehog (Hh) signaling pathway that determines embryo pattern formation and morphogenesis. Prevents meiosis resumption in prophase-arrested oocytes via CDC25B inactivation by phosphorylation. May also regulate rapid eye movement (REM) sleep in the pedunculopontine tegmental (PPT). Phosphorylates APOBEC3G and AICDA. Isoform 2 phosphorylates and activates ABL1 in sperm flagellum to promote spermatozoa capacitation By similarity.By similarity

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Allosterically activated by various compounds, including ATP. Activated by cAMP; the nucleotide acts as a dynamic and allosteric activator by coupling the two lobes of apo PKA, enhancing the enzyme dynamics synchronously and priming it for catalysis.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei73 – 731ATP
    Active sitei167 – 1671Proton acceptor

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi50 – 589ATP
    Nucleotide bindingi122 – 1287ATP
    Nucleotide bindingi169 – 1724ATP

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cAMP-dependent protein kinase activity Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein kinase activity Source: MGI
    5. protein serine/threonine/tyrosine kinase activity Source: MGI
    6. protein serine/threonine kinase activity Source: MGI

    GO - Biological processi

    1. cellular response to glucose stimulus Source: Ensembl
    2. cellular response to parathyroid hormone stimulus Source: MGI
    3. mesoderm formation Source: MGI
    4. negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning Source: MGI
    5. neural tube closure Source: MGI
    6. peptidyl-serine phosphorylation Source: MGI
    7. peptidyl-threonine phosphorylation Source: MGI
    8. positive regulation of cell cycle arrest Source: UniProtKB
    9. positive regulation of protein export from nucleus Source: MGI
    10. protein autophosphorylation Source: MGI
    11. protein phosphorylation Source: MGI
    12. regulation of osteoblast differentiation Source: Ensembl
    13. regulation of proteasomal protein catabolic process Source: Ensembl
    14. regulation of protein processing Source: MGI
    15. regulation of synaptic transmission Source: MGI
    16. regulation of tight junction assembly Source: Ensembl
    17. sperm capacitation Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, cAMP, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.11. 3474.
    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_213852. PKA-mediated phosphorylation of CREB.
    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 catalytic subunit alpha (EC:2.7.11.11)
    Short name:
    PKA C-alpha
    Gene namesi
    Name:Prkaca
    Synonyms:Pkaca
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:97592. Prkaca.

    Subcellular locationi

    Cytoplasm 1 Publication. Cell membrane By similarity. Nucleus By similarity. Mitochondrion 1 Publication
    Note: Translocates into the nucleus (monomeric catalytic subunit) By similarity. The inactive holoenzyme is found in the cytoplasm. Distributed throughout the cytoplasm in meiotically incompetent oocytes. Associated to mitochondrion as meiotic competence is acquired. Aggregates around the germinal vesicles (GV) at the immature GV stage oocytes.By similarity
    Isoform 2 : Cell projectionciliumflagellum By similarity
    Note: Expressed in the midpiece region of the sperm flagellum.By similarity

    GO - Cellular componenti

    1. AMP-activated protein kinase complex Source: Ensembl
    2. centrosome Source: Ensembl
    3. ciliary base Source: MGI
    4. cytoplasm Source: MGI
    5. cytosol Source: Reactome
    6. mitochondrion Source: MGI
    7. neuromuscular junction Source: MGI
    8. nucleoplasm Source: Reactome
    9. nucleus Source: MGI
    10. plasma membrane Source: MGI
    11. sperm midpiece Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cilium, Cytoplasm, Flagellum, Membrane, Mitochondrion, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Frequent early postnatal lethality. Survivals are runted accompanied with mature sperm exhibiting defective forward motility.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi198 – 1981T → D: No phosphorylation by PDPK1.
    Mutagenesisi286 – 2861K → P: Impaired inhibition by the R-subunit. 1 Publication
    Mutagenesisi328 – 3281F → A: Reduced catalytic activity and impaired inhibition by the R-subunit. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 351350cAMP-dependent protein kinase catalytic subunit alphaPRO_0000086053Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine1 Publication
    Modified residuei3 – 31Deamidated asparagine; partial1 Publication
    Modified residuei11 – 111Phosphoserine; by autocatalysis2 Publications
    Modified residuei49 – 491PhosphothreonineBy similarity
    Modified residuei140 – 1401Phosphoserine1 Publication
    Modified residuei196 – 1961PhosphothreonineBy similarity
    Modified residuei198 – 1981Phosphothreonine; by PDPK12 Publications
    Modified residuei202 – 2021PhosphothreonineBy similarity
    Modified residuei331 – 3311Phosphotyrosine1 Publication
    Modified residuei339 – 3391Phosphoserine1 Publication

    Post-translational modificationi

    Autophosphorylated. Phosphorylation is enhanced by vitamin K2 By similarity. Phosphorylated on threonine and serine residues. Phosphorylation on Thr-198 is required for full activity.By similarity2 Publications
    Asn-3 is partially deaminated to Asp-3 giving rise to 2 major isoelectric variants, called CB and CA respectively.
    When myristoylated, Ser-11 is autophosphorylated probably in conjunction with deamidation of Asn-3.2 Publications
    Phosphorylated at Tyr-331 by activated receptor tyrosine kinases EGFR and PDGFR; this increases catalytic efficienncy.1 Publication

    Keywords - PTMi

    Lipoprotein, Myristate, Phosphoprotein

    Proteomic databases

    MaxQBiP05132.
    PaxDbiP05132.
    PRIDEiP05132.

    PTM databases

    PhosphoSiteiP05132.

    Expressioni

    Tissue specificityi

    Isoform 2 is sperm specific.

    Developmental stagei

    Accumulates in oocytes before fertilization but fades out after fertilization.1 Publication

    Gene expression databases

    BgeeiP05132.
    CleanExiMM_PRKACA.
    GenevestigatoriP05132.

    Interactioni

    Subunit structurei

    A number of inactive tetrameric holoenzymes are produced by the combination of homo- or heterodimers of the different regulatory subunits associated with two catalytic subunits. Protein kinase A holoenzyme is comprised of two catalytic (C) and two regulatory (R) subunits which keep the enzyme in an inhibited state before activation by cyclic-AMP. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. The cAMP-dependent protein kinase catalytic subunit binds PJA2. Both isoforms 1 and 2 forms activate cAMP-sensitive PKAI and PKAII holoenzymes by interacting with regulatory subunit (R) of PKA, PRKAR1A/PKR1 and PRKAR2A/PKR2, respectively. Interacts with NFKB1, NFKB2 and NFKBIA in platelets; these interactions are disrupted by thrombin and collagen. Binds to ABL1 in spermatozoa and with CDC25B in oocytes. Interacts with APOBEC3G and AICDA By similarity. Interacts with RAB13; downstream effector of RAB13 involved in tight junction assembly By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Prkar2bP313243EBI-400564,EBI-455340

    Protein-protein interaction databases

    BioGridi202192. 17 interactions.
    DIPiDIP-6086N.
    IntActiP05132. 13 interactions.
    MINTiMINT-4051347.
    STRINGi10090.ENSMUSP00000005606.

    Structurei

    Secondary structure

    1
    351
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 75
    Turni9 – 124
    Helixi16 – 3217
    Helixi41 – 433
    Beta strandi44 – 529
    Beta strandi57 – 637
    Turni64 – 663
    Beta strandi69 – 768
    Helixi77 – 826
    Helixi86 – 9611
    Beta strandi107 – 1126
    Beta strandi114 – 1229
    Helixi129 – 1368
    Helixi141 – 16020
    Beta strandi162 – 1643
    Helixi170 – 1723
    Beta strandi173 – 1753
    Beta strandi181 – 1833
    Helixi186 – 1883
    Helixi203 – 2053
    Helixi208 – 2114
    Helixi219 – 23416
    Helixi244 – 25310
    Helixi264 – 27310
    Turni278 – 2803
    Turni282 – 2843
    Turni286 – 2894
    Helixi290 – 2934
    Helixi296 – 2983
    Helixi303 – 3075
    Beta strandi321 – 3266
    Turni345 – 3506

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1APMX-ray2.00E2-351[»]
    1ATPX-ray2.20E2-351[»]
    1BKXX-ray2.60A2-351[»]
    1BX6X-ray2.10A2-351[»]
    1FMOX-ray2.20E2-351[»]
    1J3HX-ray2.90A/B2-351[»]
    1JBPX-ray2.20E2-351[»]
    1JLUX-ray2.25E2-351[»]
    1L3RX-ray2.00E2-351[»]
    1PVKmodel-B16-351[»]
    1RDQX-ray1.26E2-351[»]
    1RE8X-ray2.10A2-351[»]
    1REJX-ray2.20A2-351[»]
    1REKX-ray2.30A2-351[»]
    1SYKX-ray2.80A/B2-351[»]
    2CPKX-ray2.70E2-351[»]
    2ERZX-ray2.20E1-351[»]
    2QCSX-ray2.20A2-351[»]
    2QURX-ray2.50A2-351[»]
    2QVSX-ray2.50E2-351[»]
    3FHIX-ray2.00A2-351[»]
    3FJQX-ray1.60E2-351[»]
    3IDBX-ray1.62A2-351[»]
    3IDCX-ray2.70A2-351[»]
    3J4Qelectron microscopy35.00D/E1-351[»]
    3J4Relectron microscopy35.00D/E1-351[»]
    3O7LX-ray2.80B/D2-351[»]
    3OW3X-ray1.90A2-351[»]
    3PVBX-ray3.30A7-351[»]
    3QALX-ray1.70E2-351[»]
    3QAMX-ray1.92E2-351[»]
    4DFXX-ray1.35E2-351[»]
    4DFYX-ray3.00A/E1-351[»]
    4DFZX-ray2.00E2-351[»]
    4DG0X-ray2.00E2-351[»]
    4DG2X-ray2.00E2-351[»]
    4DG3X-ray1.80E1-351[»]
    4DH1X-ray2.00A16-351[»]
    4DH3X-ray2.20A2-351[»]
    4DH5X-ray2.20A2-351[»]
    4DH7X-ray1.80A2-351[»]
    4DH8X-ray2.30A2-351[»]
    4DINX-ray3.70A2-351[»]
    4HPTX-ray2.15E2-351[»]
    4HPUX-ray1.55E2-351[»]
    4IACX-ray2.15A2-351[»]
    4IADX-ray1.90A2-351[»]
    4IAFX-ray2.20A2-351[»]
    4IAIX-ray1.55A2-351[»]
    4IAKX-ray1.60A2-351[»]
    4IAYX-ray2.00A2-351[»]
    4IAZX-ray1.85A2-351[»]
    4IB0X-ray1.87A2-351[»]
    4IB1X-ray1.63A2-351[»]
    4IB3X-ray2.20A2-351[»]
    4O21X-ray1.95A16-351[»]
    4O22X-ray1.70A16-351[»]
    ProteinModelPortaliP05132.
    SMRiP05132. Positions 2-351.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05132.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini44 – 298255Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini299 – 35153AGC-kinase C-terminalAdd
    BLAST

    Sequence similaritiesi

    Contains 1 AGC-kinase C-terminal domain.Curated
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00550000074358.
    HOGENOMiHOG000233033.
    HOVERGENiHBG108317.
    InParanoidiP05132.
    KOiK04345.
    OMAiGQHFAMK.
    OrthoDBiEOG7VX8WD.
    PhylomeDBiP05132.
    TreeFamiTF313399.

    Family and domain databases

    InterProiIPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P05132-1) [UniParc]FASTAAdd to Basket

    Also known as: C-alpha-1

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGNAAAAKKG SEQESVKEFL AKAKEDFLKK WETPSQNTAQ LDQFDRIKTL    50
    GTGSFGRVML VKHKESGNHY AMKILDKQKV VKLKQIEHTL NEKRILQAVN 100
    FPFLVKLEFS FKDNSNLYMV MEYVAGGEMF SHLRRIGRFS EPHARFYAAQ 150
    IVLTFEYLHS LDLIYRDLKP ENLLIDQQGY IQVTDFGFAK RVKGRTWTLC 200
    GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF ADQPIQIYEK 250
    IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVN DIKNHKWFAT 300
    TDWIAIYQRK VEAPFIPKFK GPGDTSNFDD YEEEEIRVSI NEKCGKEFTE 350
    F 351
    Length:351
    Mass (Da):40,571
    Last modified:January 23, 2007 - v3
    Checksum:i02F85D66EB21A1FA
    GO
    Isoform 2 (identifier: P05132-2) [UniParc]FASTAAdd to Basket

    Also known as: C-alpha-2, C-alpha-S, C(s)

    The sequence of this isoform differs from the canonical sequence as follows:
         2-15: GNAAAAKKGSEQES → MASSSND

    Show »
    Length:344
    Mass (Da):39,934
    Checksum:i67F650302774793D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti33 – 331T → D in AAA39936. (PubMed:3456589)Curated
    Sequence conflicti287 – 2871N → D in AAA39936. (PubMed:3456589)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 1514GNAAA…SEQES → MASSSND in isoform 2. 1 PublicationVSP_004760Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19960
    , M18240, M18241, M19953, M19954, M19955, M19956, M19957, M19958, M19959 Genomic DNA. Translation: AAA39937.1.
    M12303 mRNA. Translation: AAA39936.1.
    BC003238 mRNA. Translation: AAH03238.1.
    BC054834 mRNA. Translation: AAH54834.1.
    AF239743 mRNA. Translation: AAF76425.1.
    CCDSiCCDS22463.1. [P05132-1]
    PIRiA28619. OKMSCA.
    RefSeqiNP_001264827.1. NM_001277898.1.
    NP_032880.1. NM_008854.5. [P05132-1]
    UniGeneiMm.19111.

    Genome annotation databases

    EnsembliENSMUST00000005606; ENSMUSP00000005606; ENSMUSG00000005469. [P05132-1]
    GeneIDi18747.
    KEGGimmu:18747.
    UCSCiuc009mll.2. mouse. [P05132-1]
    uc009mlm.1. mouse. [P05132-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19960
    , M18240 , M18241 , M19953 , M19954 , M19955 , M19956 , M19957 , M19958 , M19959 Genomic DNA. Translation: AAA39937.1 .
    M12303 mRNA. Translation: AAA39936.1 .
    BC003238 mRNA. Translation: AAH03238.1 .
    BC054834 mRNA. Translation: AAH54834.1 .
    AF239743 mRNA. Translation: AAF76425.1 .
    CCDSi CCDS22463.1. [P05132-1 ]
    PIRi A28619. OKMSCA.
    RefSeqi NP_001264827.1. NM_001277898.1.
    NP_032880.1. NM_008854.5. [P05132-1 ]
    UniGenei Mm.19111.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1APM X-ray 2.00 E 2-351 [» ]
    1ATP X-ray 2.20 E 2-351 [» ]
    1BKX X-ray 2.60 A 2-351 [» ]
    1BX6 X-ray 2.10 A 2-351 [» ]
    1FMO X-ray 2.20 E 2-351 [» ]
    1J3H X-ray 2.90 A/B 2-351 [» ]
    1JBP X-ray 2.20 E 2-351 [» ]
    1JLU X-ray 2.25 E 2-351 [» ]
    1L3R X-ray 2.00 E 2-351 [» ]
    1PVK model - B 16-351 [» ]
    1RDQ X-ray 1.26 E 2-351 [» ]
    1RE8 X-ray 2.10 A 2-351 [» ]
    1REJ X-ray 2.20 A 2-351 [» ]
    1REK X-ray 2.30 A 2-351 [» ]
    1SYK X-ray 2.80 A/B 2-351 [» ]
    2CPK X-ray 2.70 E 2-351 [» ]
    2ERZ X-ray 2.20 E 1-351 [» ]
    2QCS X-ray 2.20 A 2-351 [» ]
    2QUR X-ray 2.50 A 2-351 [» ]
    2QVS X-ray 2.50 E 2-351 [» ]
    3FHI X-ray 2.00 A 2-351 [» ]
    3FJQ X-ray 1.60 E 2-351 [» ]
    3IDB X-ray 1.62 A 2-351 [» ]
    3IDC X-ray 2.70 A 2-351 [» ]
    3J4Q electron microscopy 35.00 D/E 1-351 [» ]
    3J4R electron microscopy 35.00 D/E 1-351 [» ]
    3O7L X-ray 2.80 B/D 2-351 [» ]
    3OW3 X-ray 1.90 A 2-351 [» ]
    3PVB X-ray 3.30 A 7-351 [» ]
    3QAL X-ray 1.70 E 2-351 [» ]
    3QAM X-ray 1.92 E 2-351 [» ]
    4DFX X-ray 1.35 E 2-351 [» ]
    4DFY X-ray 3.00 A/E 1-351 [» ]
    4DFZ X-ray 2.00 E 2-351 [» ]
    4DG0 X-ray 2.00 E 2-351 [» ]
    4DG2 X-ray 2.00 E 2-351 [» ]
    4DG3 X-ray 1.80 E 1-351 [» ]
    4DH1 X-ray 2.00 A 16-351 [» ]
    4DH3 X-ray 2.20 A 2-351 [» ]
    4DH5 X-ray 2.20 A 2-351 [» ]
    4DH7 X-ray 1.80 A 2-351 [» ]
    4DH8 X-ray 2.30 A 2-351 [» ]
    4DIN X-ray 3.70 A 2-351 [» ]
    4HPT X-ray 2.15 E 2-351 [» ]
    4HPU X-ray 1.55 E 2-351 [» ]
    4IAC X-ray 2.15 A 2-351 [» ]
    4IAD X-ray 1.90 A 2-351 [» ]
    4IAF X-ray 2.20 A 2-351 [» ]
    4IAI X-ray 1.55 A 2-351 [» ]
    4IAK X-ray 1.60 A 2-351 [» ]
    4IAY X-ray 2.00 A 2-351 [» ]
    4IAZ X-ray 1.85 A 2-351 [» ]
    4IB0 X-ray 1.87 A 2-351 [» ]
    4IB1 X-ray 1.63 A 2-351 [» ]
    4IB3 X-ray 2.20 A 2-351 [» ]
    4O21 X-ray 1.95 A 16-351 [» ]
    4O22 X-ray 1.70 A 16-351 [» ]
    ProteinModelPortali P05132.
    SMRi P05132. Positions 2-351.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202192. 17 interactions.
    DIPi DIP-6086N.
    IntActi P05132. 13 interactions.
    MINTi MINT-4051347.
    STRINGi 10090.ENSMUSP00000005606.

    Chemistry

    BindingDBi P05132.

    PTM databases

    PhosphoSitei P05132.

    Proteomic databases

    MaxQBi P05132.
    PaxDbi P05132.
    PRIDEi P05132.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000005606 ; ENSMUSP00000005606 ; ENSMUSG00000005469 . [P05132-1 ]
    GeneIDi 18747.
    KEGGi mmu:18747.
    UCSCi uc009mll.2. mouse. [P05132-1 ]
    uc009mlm.1. mouse. [P05132-2 ]

    Organism-specific databases

    CTDi 5566.
    MGIi MGI:97592. Prkaca.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00550000074358.
    HOGENOMi HOG000233033.
    HOVERGENi HBG108317.
    InParanoidi P05132.
    KOi K04345.
    OMAi GQHFAMK.
    OrthoDBi EOG7VX8WD.
    PhylomeDBi P05132.
    TreeFami TF313399.

    Enzyme and pathway databases

    BRENDAi 2.7.11.11. 3474.
    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_213852. PKA-mediated phosphorylation of CREB.
    REACT_213947. Regulation of water balance by renal Aquaporins.
    REACT_220108. PKA activation.
    REACT_220758. PKA activation in glucagon signalling.

    Miscellaneous databases

    ChiTaRSi PRKACA. mouse.
    EvolutionaryTracei P05132.
    NextBioi 294909.
    PROi P05132.
    SOURCEi Search...

    Gene expression databases

    Bgeei P05132.
    CleanExi MM_PRKACA.
    Genevestigatori P05132.

    Family and domain databases

    InterProi IPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of genomic clones coding for the C alpha and C beta subunits of mouse cAMP-dependent protein kinase."
      Chrivia J.C., Uhler M.D., McKnight G.S.
      J. Biol. Chem. 263:5739-5744(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    2. "Isolation of cDNA clones coding for the catalytic subunit of mouse cAMP-dependent protein kinase."
      Uhler M.D., Carmichael D.F., Lee D.C., Chrivia J.C., Krebs E.G., McKnight G.S.
      Proc. Natl. Acad. Sci. U.S.A. 83:1300-1304(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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] (ISOFORM 1).
      Strain: FVB/N-3.
      Tissue: Mammary tumor.
    4. "The unique catalytic subunit of sperm cAMP-dependent protein kinase is the product of an alternative C-alpha mRNA expressed specifically in spermatogenic cells."
      San Agustin J.T., Wilkerson C.G., Witman G.B.
      Mol. Biol. Cell 11:3031-3044(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-153 (ISOFORM 2).
      Tissue: Testis.
    5. "Identification of phosphorylation sites in the recombinant catalytic subunit of cAMP-dependent protein kinase."
      Yonemoto W., Garrod S.M., Bell S.M., Taylor S.S.
      J. Biol. Chem. 268:18626-18632(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-11; SER-140; THR-198 AND SER-339.
    6. "Phosphorylation and activation of cAMP-dependent protein kinase by phosphoinositide-dependent protein kinase."
      Cheng X., Ma Y., Moore M., Hemmings B.A., Taylor S.S.
      Proc. Natl. Acad. Sci. U.S.A. 95:9849-9854(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-198 BY PDPK1.
    7. "Influence of myristoylation, phosphorylation, and deamidation on the structural behavior of the N-terminus of the catalytic subunit of cAMP-dependent protein kinase."
      Tholey A., Pipkorn R., Bossemeyer D., Kinzel V., Reed J.
      Biochemistry 40:225-231(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: MYRISTOYLATION AT GLY-2, PHOSPHORYLATION AT SER-11, DEAMIDATION AT ASN-3.
    8. "Mutation of the Calpha subunit of PKA leads to growth retardation and sperm dysfunction."
      Skaalhegg B.S., Huang Y., Su T., Idzerda R.L., McKnight G.S., Burton K.A.
      Mol. Endocrinol. 16:630-639(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    9. "Sperm-specific protein kinase A catalytic subunit Calpha2 orchestrates cAMP signaling for male fertility."
      Nolan M.A., Babcock D.F., Wennemuth G., Brown W., Burton K.A., McKnight G.S.
      Proc. Natl. Acad. Sci. U.S.A. 101:13483-13488(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SPERMATOZOA CAPACITATION (ISOFORM 2), TISSUE SPECIFICITY (ISOFORM 2).
    10. "Developmentally acquired PKA localisation in mouse oocytes and embryos."
      Webb R.J., Tinworth L., Thomas G.M., Zaccolo M., Carroll J.
      Dev. Biol. 317:36-45(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
    11. "Protein kinase A regulates resumption of meiosis by phosphorylation of Cdc25B in mammalian oocytes."
      Pirino G., Wescott M.P., Donovan P.J.
      Cell Cycle 8:665-670(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MEIOSIS RESUMPTION, FUNCTION AS CDC25B KINASE, INTERACTION WITH CDC25B.
    12. "Phosphorylation and consequent stimulation of the tyrosine kinase c-Abl by PKA in mouse spermatozoa; its implications during capacitation."
      Baker M.A., Hetherington L., Curry B., Aitken R.J.
      Dev. Biol. 333:57-66(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SPERMATOZOA CAPACITATION, FUNCTION AS ABL1 KINASE, INTERACTION WITH ABL1.
    13. "Direct modulation of the protein kinase A catalytic subunit alpha by growth factor receptor tyrosine kinases."
      Caldwell G.B., Howe A.K., Nickl C.K., Dostmann W.R., Ballif B.A., Deming P.B.
      J. Cell. Biochem. 113:39-48(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-331.
    14. "Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase."
      Knighton D.R., Zheng J., ten Eyck L.F., Ashford V.A., Xuong N.-H., Taylor S.S., Sowadski J.M.
      Science 253:407-414(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
    15. "Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor."
      Zheng J., Knighton D.R., ten Eyck L.F., Karlsson R., Xuong N.-H., Taylor S.S., Sowadski J.M.
      Biochemistry 32:2154-2161(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH INHIBITOR.
    16. "Crystal structure of a polyhistidine-tagged recombinant catalytic subunit of cAMP-dependent protein kinase complexed with the peptide inhibitor PKI(5-24) and adenosine."
      Narayana N., Cox S., Shaltiel S., Taylor S.S., Xuong N.
      Biochemistry 36:4438-4448(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF COMPLEX WITH INHIBITOR.
    17. "A binary complex of the catalytic subunit of cAMP-dependent protein kinase and adenosine further defines conformational flexibility."
      Narayana N., Cox S., Nguyen-Huu X., ten Eyck L.F., Taylor S.S.
      Structure 5:921-935(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
    18. "PKA-I holoenzyme structure reveals a mechanism for cAMP-dependent activation."
      Kim C., Cheng C.Y., Saldanha S.A., Taylor S.S.
      Cell 130:1032-1043(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH ATP ANALOG.
    19. "PKA type IIalpha holoenzyme reveals a combinatorial strategy for isoform diversity."
      Wu J., Brown S.H., von Daake S., Taylor S.S.
      Science 318:274-279(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS).
    20. "Contribution of non-catalytic core residues to activity and regulation in protein kinase A."
      Yang J., Kennedy E.J., Wu J., Deal M.S., Pennypacker J., Ghosh G., Taylor S.S.
      J. Biol. Chem. 284:6241-6248(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH ADP, SUBUNIT, MUTAGENESIS OF LYS-286 AND PHE-328.
    21. "Novel isoform-specific interfaces revealed by PKA RIIbeta holoenzyme structures."
      Brown S.H.J., Wu J., Kim C., Alberto K., Taylor S.S.
      J. Mol. Biol. 393:1070-1082(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) IN COMPLEX WITH ATP ANALOGS.
    22. "Dynamics connect substrate recognition to catalysis in protein kinase A."
      Masterson L.R., Cheng C., Yu T., Tonelli M., Kornev A., Taylor S.S., Veglia G.
      Nat. Chem. Biol. 6:821-828(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH ATP ANALOG AND SUBSTRATE PEPTIDE, ENZYME REGULATION.

    Entry informationi

    Entry nameiKAPCA_MOUSE
    AccessioniPrimary (citable) accession number: P05132
    Secondary accession number(s): Q9JID0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 183 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3