{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P17252","secondaryAccessions":["B5BU22","Q15137","Q32M72","Q96RE4"],"uniProtkbId":"KPCA_HUMAN","entryAudit":{"firstPublicDate":"1990-08-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2011-01-11","entryVersion":260,"sequenceVersion":4},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Protein kinase C alpha type"},"shortNames":[{"value":"PKC-A"},{"value":"PKC-alpha"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20969574"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25313067"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36040231"}],"value":"2.7.11.13"}]}},"genes":[{"geneName":{"value":"PRKCA"},"synonyms":[{"value":"PKCA"},{"value":"PRKACA"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P20444"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10848585"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11909826"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12724315"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12832403"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15016832"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15504744"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15526160"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18056764"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19176525"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20969574"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21576361"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21806543"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23990668"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25313067"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28028151"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36040231"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9738012"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9830023"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9873035"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9927633"}],"value":"Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in positive and negative regulation of cell proliferation, apoptosis, differentiation, migration and adhesion, tumorigenesis, cardiac hypertrophy, angiogenesis, platelet function and inflammation, by directly phosphorylating targets such as RAF1, BCL2, CSPG4, TNNT2/CTNT, or activating signaling cascade involving MAPK1/3 (ERK1/2) and RAP1GAP. Involved in cell proliferation and cell growth arrest by positive and negative regulation of the cell cycle. Can promote cell growth by phosphorylating and activating RAF1, which mediates the activation of the MAPK/ERK signaling cascade, and/or by up-regulating CDKN1A, which facilitates active cyclin-dependent kinase (CDK) complex formation in glioma cells. In intestinal cells stimulated by the phorbol ester PMA, can trigger a cell cycle arrest program which is associated with the accumulation of the hyper-phosphorylated growth-suppressive form of RB1 and induction of the CDK inhibitors CDKN1A and CDKN1B. Exhibits anti-apoptotic function in glioma cells and protects them from apoptosis by suppressing the p53/TP53-mediated activation of IGFBP3, and in leukemia cells mediates anti-apoptotic action by phosphorylating BCL2. During macrophage differentiation induced by macrophage colony-stimulating factor (CSF1), is translocated to the nucleus and is associated with macrophage development. After wounding, translocates from focal contacts to lamellipodia and participates in the modulation of desmosomal adhesion. Plays a role in cell motility by phosphorylating CSPG4, which induces association of CSPG4 with extensive lamellipodia at the cell periphery and polarization of the cell accompanied by increases in cell motility. During chemokine-induced CD4(+) T cell migration, phosphorylates CDC42-guanine exchange factor DOCK8 resulting in its dissociation from LRCH1 and the activation of GTPase CDC42 (PubMed:28028151). Is highly expressed in a number of cancer cells where it can act as a tumor promoter and is implicated in malignant phenotypes of several tumors such as gliomas and breast cancers. Negatively regulates myocardial contractility and positively regulates angiogenesis, platelet aggregation and thrombus formation in arteries. Mediates hypertrophic growth of neonatal cardiomyocytes, in part through a MAPK1/3 (ERK1/2)-dependent signaling pathway, and upon PMA treatment, is required to induce cardiomyocyte hypertrophy up to heart failure and death, by increasing protein synthesis, protein-DNA ratio and cell surface area. Regulates cardiomyocyte function by phosphorylating cardiac troponin T (TNNT2/CTNT), which induces significant reduction in actomyosin ATPase activity, myofilament calcium sensitivity and myocardial contractility. In angiogenesis, is required for full endothelial cell migration, adhesion to vitronectin (VTN), and vascular endothelial growth factor A (VEGFA)-dependent regulation of kinase activation and vascular tube formation. Involved in the stabilization of VEGFA mRNA at post-transcriptional level and mediates VEGFA-induced cell proliferation. In the regulation of calcium-induced platelet aggregation, mediates signals from the CD36/GP4 receptor for granule release, and activates the integrin heterodimer ITGA2B-ITGB3 through the RAP1GAP pathway for adhesion. During response to lipopolysaccharides (LPS), may regulate selective LPS-induced macrophage functions involved in host defense and inflammation. But in some inflammatory responses, may negatively regulate NF-kappa-B-induced genes, through IL1A-dependent induction of NF-kappa-B inhibitor alpha (NFKBIA/IKBA). Upon stimulation with 12-O-tetradecanoylphorbol-13-acetate (TPA), phosphorylates EIF4G1, which modulates EIF4G1 binding to MKNK1 and may be involved in the regulation of EIF4E phosphorylation. Phosphorylates KIT, leading to inhibition of KIT activity. Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription. Phosphorylates SOCS2 at 'Ser-52' facilitating its ubiquitination and proteasomal degradation (By similarity). Phosphorylates KLHL3 in response to angiotensin II signaling, decreasing the interaction between KLHL3 and WNK4 (PubMed:25313067). Phosphorylates and activates LRRK1, which phosphorylates RAB proteins involved in intracellular trafficking (PubMed:36040231). Acts as a regulator of dopamine signaling by mediating constitutive phosphorylation of dopamine receptor DRD1, inhibiting G protein-coupled receptor signaling (PubMed:20969574)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17989"},{"database":"Rhea","id":"RHEA-COMP:9863"},{"database":"Rhea","id":"RHEA-COMP:11604"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29999"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:83421"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.13","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20969574"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36040231"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46608"},{"database":"Rhea","id":"RHEA-COMP:11060"},{"database":"Rhea","id":"RHEA-COMP:11605"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30013"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:61977"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.13","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25313067"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36040231"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Ca(2+)","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00041"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29108"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P05696"}],"value":"Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domain."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21806543"}],"value":"Classical (or conventional) PKCs (PRKCA, PRKCB and PRKCG) are activated by calcium and diacylglycerol (DAG) in the presence of phosphatidylserine. Three specific sites; Thr-497 (activation loop of the kinase domain), Thr-638 (turn motif) and Ser-657 (hydrophobic region), need to be phosphorylated for its full activation"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P05696"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P20444"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12893243"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15247289"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15504744"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17893151"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27925688"}],"value":"Recruited in a circadian manner into a nuclear complex which also includes BMAL1 and RACK1 (By similarity). Interacts with ADAP1/CENTA1 (PubMed:12893243). Interacts with CSPG4 (PubMed:15504744). Binds to CAVIN2 in the presence of phosphatidylserine (By similarity). Interacts with PRKCABP/PICK1 (via PDZ domain) (PubMed:15247289). Interacts with TRIM41 (PubMed:17893151). Interacts with PARD3 (PubMed:27925688). Interacts with SOCS2 (By 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(PK-like)"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51285","properties":[{"key":"EntryName","value":"AGC_KINASE_CTER"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50004","properties":[{"key":"EntryName","value":"C2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00107","properties":[{"key":"EntryName","value":"PROTEIN_KINASE_ATP"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50011","properties":[{"key":"EntryName","value":"PROTEIN_KINASE_DOM"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00108","properties":[{"key":"EntryName","value":"PROTEIN_KINASE_ST"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00479","properties":[{"key":"EntryName","value":"ZF_DAG_PE_1"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS50081","properties":[{"key":"EntryName","value":"ZF_DAG_PE_2"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MADVFPGNDSTASQDVANRFARKGALRQKNVHEVKDHKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHTYGSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKQCVINVPSLCGMDHTEKRGRIYLKAEVADEKLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFTFKLKPSDKDRRLSVEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKLLNQEEGEYYNVPIPEGDEEGNMELRQKFEKAKLGPAGNKVISPSEDRKQPSNNLDRVKLTDFNFLMVLGKGSFGKVMLADRKGTEELYAIKILKKDVVIQDDDVECTMVEKRVLALLDKPPFLTQLHSCFQTVDRLYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISIGLFFLHKRGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMMDGVTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSVCKGLMTKHPAKRLGCGPEGERDVREHAFFRRIDWEKLENREIQPPFKPKVCGKGAENFDKFFTRGQPVLTPPDQLVIANIDQSDFEGFSYVNPQFVHPILQSAV","length":672,"molWeight":76750,"crc64":"9EB157789A062349","md5":"F1E89AA299309140E47590A95EB78C41"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"ACTIVITY REGULATION":1,"SUBUNIT":1,"INTERACTION":91,"SUBCELLULAR LOCATION":1,"PTM":1,"SIMILARITY":1},"countByFeatureType":{"Initiator methionine":1,"Chain":1,"Domain":3,"Zinc finger":2,"Active site":1,"Binding site":17,"Modified residue":14,"Natural variant":4,"Mutagenesis":1,"Sequence conflict":1,"Turn":2,"Beta strand":22,"Helix":25},"uniParcId":"UPI000013DD98"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P17612","secondaryAccessions":["Q32P54","Q9H2Y0","Q9NRB4","Q9NRH9"],"uniProtkbId":"KAPCA_HUMAN","entryAudit":{"firstPublicDate":"1990-08-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2007-01-23","entryVersion":260,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"cAMP-dependent protein kinase catalytic subunit alpha"},"shortNames":[{"value":"PKA C-alpha"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16705181"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21812984"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27028580"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31112131"}],"value":"2.7.11.11"}]}},"genes":[{"geneName":{"value":"PRKACA"},"synonyms":[{"value":"PKACA"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P05132"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P27791"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15178447"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15642694"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15905176"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16387847"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16705181"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17333334"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17565987"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17693412"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18836454"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19949837"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20356841"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21085490"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21423175"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21514275"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21812984"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21852232"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27028580"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31112131"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33934390"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36202993"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39138140"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41652173"}],"value":"Phosphorylates a large number of substrates in the cytoplasm and the nucleus (PubMed:15642694, PubMed:15905176, PubMed:16387847, PubMed:17333334, PubMed:17565987, PubMed:17693412, PubMed:18836454, PubMed:19949837, PubMed:20356841, PubMed:21085490, PubMed:21514275, PubMed:21812984, PubMed:21852232, PubMed:31112131, PubMed:41652173). Phosphorylates CDC25B, ABL1, NFKB1, CLDN3, histone H1.4 (H1-4), PSMC5/RPT6, PJA2, RYR2, RORA, SLC6A6, SOX9, UHRF1 and VASP (PubMed:15178447, PubMed:15642694, PubMed:15905176, PubMed:16387847, PubMed:17333334, PubMed:17565987, PubMed:17693412, PubMed:18836454, PubMed:19949837, PubMed:20356841, PubMed:21085490, PubMed:21514275, PubMed:21812984, PubMed:41652173). 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 (PubMed:21423175). RORA is activated by phosphorylation (PubMed:21514275). Required for glucose-mediated adipogenic differentiation increase and osteogenic differentiation inhibition from osteoblasts (PubMed:19949837). Involved in chondrogenesis by mediating phosphorylation of SOX9 (By similarity). 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 (PubMed:15642694, PubMed:20356841). Prevents the antiproliferative and anti-invasive effects of alpha-difluoromethylornithine in breast cancer cells when activated (PubMed:17333334). RYR2 channel activity is potentiated by phosphorylation in presence of luminal Ca(2+), leading to reduced amplitude and increased frequency of store overload-induced Ca(2+) release (SOICR) characterized by an increased rate of Ca(2+) release and propagation velocity of spontaneous Ca(2+) waves, despite reduced wave amplitude and resting cytosolic Ca(2+) (PubMed:17693412). PSMC5/RPT6 activation by phosphorylation stimulates proteasome (PubMed:17565987). Negatively regulates tight junctions (TJs) in ovarian cancer cells via CLDN3 phosphorylation (PubMed:15905176). NFKB1 phosphorylation promotes NF-kappa-B p50-p50 DNA binding (PubMed:15642694). Acts as a key inhibitor of smoothened signaling pathway by mediating phosphorylation of GLI (GLI1, GLI2 and GLI3) transcription factors in absence of hedgehog (DHH, IHH or SHH) morphogens: GLI phosphorylation promotes their processing and prevents transcriptional activation of smoothened target genes (PubMed:16705181). GLI transcription factor phosphorylation is inhibited by interaction of PRKACA with SMO which sequesters PRKACA at the cell membrane (PubMed:36202993, PubMed:39138140). Also inhibits the smoothened signaling pathway in embryonic development by catalyzing phosphorylation of OFD1 in ciliogenesis (PubMed:33934390). Prevents meiosis resumption in prophase-arrested oocytes via CDC25B inactivation by phosphorylation (By similarity). May also regulate rapid eye movement (REM) sleep in the pedunculopontine tegmental (PPT) (By similarity). Phosphorylates APOBEC3G and AICDA (PubMed:16387847, PubMed:18836454). Phosphorylates HSF1; this phosphorylation promotes HSF1 nuclear localization and transcriptional activity upon heat shock (PubMed:21085490). Acts as a negative regulator of mTORC1 by mediating phosphorylation of RPTOR (PubMed:31112131). Phosphorylates AKAP19 (PubMed:27028580)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P05132"}],"value":"Phosphorylates and activates ABL1 in sperm flagellum to promote spermatozoa capacitation"}],"commentType":"FUNCTION","molecule":"Isoform 2"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17989"},{"database":"Rhea","id":"RHEA-COMP:9863"},{"database":"Rhea","id":"RHEA-COMP:11604"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29999"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:83421"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.11","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15178447"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16705181"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21812984"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21852232"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27028580"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31112131"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41652173"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46608"},{"database":"Rhea","id":"RHEA-COMP:11060"},{"database":"Rhea","id":"RHEA-COMP:11605"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30013"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:61977"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.11","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21812984"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17909264"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18178622"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19949837"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20137943"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20481595"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20732331"}],"value":"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. Inhibited by H89 (N-[2-[[3-(4-Bromophenyl)-2-propenyl]amino]ethyl]-5-isoquinolinesulfonamide), spiroindoline, azole-based inhibitors, (3s)-amino-aminomethylbenzamide analogs, ARC-1032 (6-{[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]formamido}-N-[(1R)-4-carbamimidamido-1-carbamoylbutyl]hexanamide), ARC-1034 (6-{[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]formamido}-N-[(1R)-4-carbamimidamido-1-{[(1R)-4-carbamimidamido-1-carbamoylbutyl]carbamoyl}butyl]hexanamide), ARC-582, ARC-902 (Adc-6-aminohexanoic acid-(D-Arg)(6)-NH(2)), ARC-1012 ((2R)-6-amino-2-(6-{[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]formamido}hexanamido)-N-(5-{[(1R)-4-carbamimidamido-1-{[(1R)-4-carbamimidamido-1-carbamoylbutyl]carbamoyl}butyl]carbamoyl}pentyl)hexanamide) and ARC-1039 (6-{[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]formamido}-N-[(1R)-1-[(5-{[(1R)-4-carbamimidamido-1-{[(1R)-4-carbamimidamido-1-carbamoylbutyl]carbamoyl}butyl]carbamoyl}pentyl)carbamoyl]ethyl]he xanamide)"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"maximumVelocities":[{"velocity":1.07,"unit":"umol/sec/mg","enzyme":"enzyme toward AKAP19","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27028580"}]}],"michaelisConstants":[{"constant":11.91,"unit":"uM","substrate":"AKAP19","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27028580"}]}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P05132"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15096524"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16387847"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18836454"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20356841"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20732331"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21085490"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21774789"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21812984"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33058759"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33934390"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36202993"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39138140"}],"value":"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. 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 PRKAR1A and PRKAR2B (PubMed:33058759). 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. Interacts with RAB13; downstream effector of RAB13 involved in tight junction assembly. Found in a complex at least composed of MROH2B, PRKACA isoform 2 and TCP11 (By similarity). Interacts with MROH2B (By similarity). Isoform 2 interacts with TCP11 (By similarity). Interacts with HSF1 (PubMed:21085490). Interacts with TBC1D31; in regulation of OFD1 (PubMed:33934390). Interacts in free form with SMO (via C-terminus); the interaction leads to sequestration of PRKACA at the membrane, preventing PRKACA-mediated phosphorylation of GLI transcription factors (PubMed:36202993, PubMed:39138140)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P17612","intActId":"EBI-476586"},"interactantTwo":{"uniProtKBAccession":"Q9GZX7","geneName":"AICDA","intActId":"EBI-3834328"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P17612","intActId":"EBI-476586"},"interactantTwo":{"uniProtKBAccession":"P54819","geneName":"AK2","intActId":"EBI-1056291"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P17612","intActId":"EBI-476586"},"interactantTwo":{"uniProtKBAccession":"Q9NQ31","geneName":"AKIP1","intActId":"EBI-517035"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P17612","intActId":"EBI-476586"},"interactantTwo":{"uniProtKBAccession":"P31749","geneName":"AKT1","intActId":"EBI-296087"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P17612","intActId":"EBI-476586"},"interactantTwo":{"uniProtKBAccession":"P09917","geneName":"ALOX5","intActId":"EBI-79934"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P17612","intActId":"EBI-476586"},"interactantTwo":{"uniProtKBAccession":"Q02410","geneName":"APBA1","intActId":"EBI-368690"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P17612","intActId":"EBI-476586"},"interactantTwo":{"uniProtKBAccession":"Q99767","geneName":"APBA2","intActId":"EBI-81711"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P17612","intActId":"EBI-476586"},"interactantTwo":{"uniProtKBAccession":"Q92870-2","geneName":"APBB2","intActId":"EBI-21535880"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P17612","intActId":"EBI-476586"},"interactantTwo":{"uniProtKBAccession":"Q9HC16","geneName":"APOBEC3G","intActId":"EBI-717839"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P17612","intActId":"EBI-476586"},"interactantTwo":{"uniProtKBAccession":"P05067","geneName":"APP","intActId":"EBI-77613"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P17612","intActId":"EBI-476586"},"interactantTwo":{"uniProtKBAccession":"P54253","geneName":"ATXN1","intActId":"EBI-930964"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P17612","intActId":"EBI-476586"},"interactantTwo":{"uniProtKBAccession":"P54252","geneName":"ATXN3","intActId":"EBI-946046"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P17612","intActId":"EBI-476586"},"interactantTwo":{"uniProtKBAccession":"Q4VBR4","geneName":"ATXN3","intActId":"EBI-12928880"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P17612","intActId":"EBI-476586"},"interactantTwo":{"uniProtKBAccession":"Q5T686","geneName":"AVPI1","intActId":"EBI-8640233"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P17612","intActId":"EBI-476586"},"interactantTwo":{"uniProtKBAccession":"O95816","geneName":"BAG2","intActId":"EBI-355275"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P17612","intActId":"EBI-476586"},"interactantTwo":{"uniProtKBAccession":"P23560-2","geneName":"BDNF","intActId":"EBI-12275524"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P17612","intActId":"EBI-476586"},"interactantTwo":{"uniProtKBAccession":"P35520","geneName":"CBS","intActId":"EBI-740135"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P17612","intActId":"EBI-476586"},"interactantTwo":{"uniProtKBAccession":"P40227","geneName":"CCT6A","intActId":"EBI-356687"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P17612","intActId":"EBI-476586"},"interactantTwo":{"uniProtKBAccession":"P12830","geneName":"CDH1","intActId":"EBI-727477"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P17612","intActId":"EBI-476586"},"interactantTwo":{"uniProtKBAccession":"Q8NE08","geneName":"COL25A1","intActId":"EBI-25836642"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P17612","intActId":"EBI-476586"},"interactantTwo":{"uniProtKBAccession":"P48730-2","geneName":"CSNK1D","intActId":"EBI-9087876"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P17612","intActId":"EBI-476586"},"interactantTwo":{"uniProtKBAccession":"Q12959","geneName":"DLG1","intActId":"EBI-357481"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P17612","intActId":"EBI-476586"},"interactantTwo":{"uniProtKBAccession":"Q92796","geneName":"DLG3","intActId":"EBI-80440"},"numberOfExperiments":3,"org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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). Colocalizes with HSF1 in nuclear stress bodies (nSBs) upon heat shock (PubMed:21085490). Recruited to the cell membrane through interaction with SMO (By similarity)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21085490"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21423175"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19210988"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21423175"}],"value":"Cell membrane","id":"SL-0039"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Lipid-anchor","id":"SL-9901"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21085490"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P05132"}],"value":"Mitochondrion","id":"SL-0173"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Isoform 2","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P05132"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10906071"}],"value":"Expressed in the midpiece region of the sperm flagellum (PubMed:10906071). Colocalizes with MROH2B and TCP11 on the acrosome and tail regions in round spermatids and spermatozoa regardless of the capacitation status of the sperm (By similarity)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10906071"}],"value":"Cell projection, cilium, flagellum","id":"SL-0117"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P05132"}],"value":"Cytoplasmic vesicle, secretory vesicle, acrosome","id":"SL-0007"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"synonyms":[{"value":"C-alpha-1"}],"isoformIds":["P17612-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"synonyms":[{"value":"C-alpha-2"},{"value":"C-alpha-S"},{"value":"C(s)"}],"isoformIds":["P17612-2"],"sequenceIds":["VSP_004759"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10906071"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21812984"}],"value":"Isoform 1 is ubiquitous. Isoform 2 is sperm-specific and is enriched in pachytene spermatocytes but is not detected in round spermatids"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P05132"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12372837"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16765046"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17909264"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20137943"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20481595"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20732331"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21774789"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.50"}],"value":"Autophosphorylated. Phosphorylation is enhanced by vitamin K(2) (PubMed:12372837, PubMed:17909264). Phosphorylated on threonine and serine residues. Phosphorylation on Thr-198 is required for full activity (PubMed:16765046, PubMed:20137943, PubMed:20481595, PubMed:20732331, PubMed:21774789, Ref.50). Phosphorylated at Tyr-331 by activated receptor tyrosine kinases EGFR and PDGFR; this increases catalytic efficiency (By similarity)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P05132"}],"value":"Asn-3 is partially deaminated to Asp-3 giving rise to 2 major isoelectric variants, called CB and CA respectively"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P05132"}],"value":"When myristoylated, Ser-11 is autophosphorylated probably in conjunction with deamidation of Asn-3"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Primary pigmented nodular adrenocortical disease 4","diseaseAccession":"DI-04115","acronym":"PPNAD4","description":"A rare bilateral adrenal defect causing ACTH-independent Cushing syndrome. Macroscopic appearance of the adrenals is characteristic with small pigmented micronodules observed in the cortex. 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