{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P78527","secondaryAccessions":["P78528","Q13327","Q13337","Q14175","Q59H99","Q7Z611","Q96SE6","Q9UME3"],"uniProtkbId":"PRKDC_HUMAN","entryAudit":{"firstPublicDate":"2001-04-27","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2003-10-31","entryVersion":248,"sequenceVersion":3},"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":"DNA-dependent protein kinase catalytic subunit"},"shortNames":[{"value":"DNA-PK catalytic subunit"},{"value":"DNA-PKcs"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15262962"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26237645"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32103174"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35460603"}],"value":"2.7.11.1"}]},"alternativeNames":[{"fullName":{"value":"DNPK1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"15262962"}],"value":"Ser-473 kinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"15262962"}],"value":"S473K"}]},{"fullName":{"value":"p460"}}]},"genes":[{"geneName":{"value":"PRKDC"},"synonyms":[{"value":"HYRC"},{"value":"HYRC1"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P97313"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10026262"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10467406"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11889123"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11955432"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12509254"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12649176"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14599745"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14612514"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14627815"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14704337"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14734805"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15177042"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15262962"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15574326"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1597196"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16046194"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16397295"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18644470"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2247066"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2507541"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26237645"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26666690"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28712728"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29478807"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30247612"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32103174"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33273464"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33854234"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34352203"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35460603"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8407951"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8464713"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9139719"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9362500"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9363941"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9679063"}],"value":"Serine/threonine-protein kinase that acts as a molecular sensor for DNA damage (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:33854234). Involved in DNA non-homologous end joining (NHEJ) required for double-strand break (DSB) repair and V(D)J recombination (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:33854234, PubMed:34352203). Must be bound to DNA to express its catalytic properties (PubMed:11955432). Promotes processing of hairpin DNA structures in V(D)J recombination by activation of the hairpin endonuclease artemis (DCLRE1C) (PubMed:11955432). Recruited by XRCC5 and XRCC6 to DNA ends and is required to (1) protect and align broken ends of DNA, thereby preventing their degradation, (2) and sequester the DSB for repair by NHEJ (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:15574326, PubMed:33854234). Acts as a scaffold protein to aid the localization of DNA repair proteins to the site of damage (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:15574326). The assembly of the DNA-PK complex at DNA ends is also required for the NHEJ ligation step (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:15574326). Found at the ends of chromosomes, suggesting a further role in the maintenance of telomeric stability and the prevention of chromosomal end fusion (By similarity). Also involved in modulation of transcription (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:15574326). As part of the DNA-PK complex, involved in the early steps of ribosome assembly by promoting the processing of precursor rRNA into mature 18S rRNA in the small-subunit processome (PubMed:32103174). Binding to U3 small nucleolar RNA, recruits PRKDC and XRCC5/Ku86 to the small-subunit processome (PubMed:32103174). Recognizes the substrate consensus sequence [ST]-Q (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:15574326). Phosphorylates 'Ser-139' of histone variant H2AX, thereby regulating DNA damage response mechanism (PubMed:14627815, PubMed:16046194). Phosphorylates ASF1A, DCLRE1C, c-Abl/ABL1, histone H1, HSPCA, c-jun/JUN, p53/TP53, PARP1, POU2F1, DHX9, FH, SRF, NHEJ1/XLF, XRCC1, XRCC4, XRCC5, XRCC6, WRN, MYC and RFA2 (PubMed:10026262, PubMed:10467406, PubMed:11889123, PubMed:12509254, PubMed:14599745, PubMed:14612514, PubMed:14704337, PubMed:15177042, PubMed:1597196, PubMed:16397295, PubMed:18644470, PubMed:2247066, PubMed:2507541, PubMed:26237645, PubMed:26666690, PubMed:28712728, PubMed:29478807, PubMed:30247612, PubMed:8407951, PubMed:8464713, PubMed:9139719, PubMed:9362500). Can phosphorylate C1D not only in the presence of linear DNA but also in the presence of supercoiled DNA (PubMed:9679063). Ability to phosphorylate p53/TP53 in the presence of supercoiled DNA is dependent on C1D (PubMed:9363941). Acts as a regulator of the phosphatidylinositol 3-kinase/protein kinase B signal transduction by mediating phosphorylation of 'Ser-473' of protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), promoting their activation (PubMed:15262962). Contributes to the determination of the circadian period length by antagonizing phosphorylation of CRY1 'Ser-588' and increasing CRY1 protein stability, most likely through an indirect mechanism (By similarity). Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728). Also regulates the cGAS-STING pathway by catalyzing phosphorylation of CGAS, thereby impairing CGAS oligomerization and activation (PubMed:33273464). Also regulates the cGAS-STING pathway by mediating phosphorylation of PARP1 (PubMed:35460603)"}],"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":"2.7.11.1","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15262962"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29478807"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32103174"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:17990"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15262962"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29478807"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32103174"}]}]},{"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":"2.7.11.1","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26237645"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32103174"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35460603"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:46609"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26237645"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32103174"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35460603"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32103174"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9766667"}],"value":"Activity seems to be attenuated by autophosphorylation. Binding to the SL1 region of U3 small nucleolar RNA promotes auto-phosphorylation activity (PubMed:32103174). Inhibited by wortmannin (PubMed:9766667)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11955432"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14744996"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15071507"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15456891"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15574326"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15758953"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15811628"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15936993"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20427287"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20801936"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20810650"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22977523"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23149945"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25574025"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25670504"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25852083"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25941166"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28712728"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32832608"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33854234"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34352203"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9372844"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9442054"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9679063"}],"value":"DNA-PK is a heterotrimer of PRKDC and the Ku dimer (composed of XRCC6/Ku70 and XRCC5/Ku86) (PubMed:15758953, PubMed:25670504). Formation of this complex may be promoted by interaction with ILF3 (PubMed:9442054). Component of the core long-range non-homologous end joining (NHEJ) complex (also named DNA-PK complex) composed of PRKDC, LIG4, XRCC4, XRCC6/Ku70, XRCC5/Ku86 and NHEJ1/XLF (PubMed:15758953, PubMed:25670504, PubMed:33854234, PubMed:34352203). Additional component of the NHEJ complex includes PAXX (PubMed:25574025, PubMed:25941166). Following autophosphorylation, PRKDC dissociates from DNA (PubMed:33854234). Interacts with DNA-PKcs-interacting protein (KIP) with the region upstream the kinase domain (PubMed:9372844). PRKDC alone also interacts with and phosphorylates DCLRE1C, thereby activating the latent endonuclease activity of this protein (PubMed:11955432, PubMed:14744996, PubMed:15071507, PubMed:15456891, PubMed:15574326, PubMed:15811628, PubMed:15936993). Interacts with C1D (PubMed:9679063). Interacts with TTI1 and TELO2 (PubMed:20427287, PubMed:20801936, PubMed:20810650). Interacts with CIB1 (PubMed:9372844). Interacts with SETX (PubMed:23149945). Interacts with NR4A3; the DNA-dependent protein kinase complex DNA-PK phosphorylates and activates NR4A3 and prevents NR4A3 ubiquitination and degradation (PubMed:25852083). Interacts with BRAT1 (PubMed:22977523). Part of the HDP-RNP complex composed of at least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1 RNA (PubMed:28712728). Interacts with KAT5 (PubMed:32832608)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P78527","intActId":"EBI-352053"},"interactantTwo":{"uniProtKBAccession":"O43918","geneName":"AIRE","intActId":"EBI-1753081"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P78527","intActId":"EBI-352053"},"interactantTwo":{"uniProtKBAccession":"P10275","geneName":"AR","intActId":"EBI-608057"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P78527","intActId":"EBI-352053"},"interactantTwo":{"uniProtKBAccession":"Q96SD1","geneName":"DCLRE1C","intActId":"EBI-11694104"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P78527","intActId":"EBI-352053"},"interactantTwo":{"uniProtKBAccession":"P14921","geneName":"ETS1","intActId":"EBI-913209"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P78527","intActId":"EBI-352053"},"interactantTwo":{"uniProtKBAccession":"P50549","geneName":"ETV1","intActId":"EBI-3905068"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P78527","intActId":"EBI-352053"},"interactantTwo":{"uniProtKBAccession":"P09629","geneName":"HOXB7","intActId":"EBI-1248457"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P78527","intActId":"EBI-352053"},"interactantTwo":{"uniProtKBAccession":"Q9BPZ7","geneName":"MAPKAP1","intActId":"EBI-749938"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P78527","intActId":"EBI-352053"},"interactantTwo":{"uniProtKBAccession":"Q96RI1-2","geneName":"NR1H4","intActId":"EBI-9640524"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P78527","intActId":"EBI-352053"},"interactantTwo":{"uniProtKBAccession":"P10276","geneName":"RARA","intActId":"EBI-413374"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P78527","intActId":"EBI-352053"},"interactantTwo":{"uniProtKBAccession":"P17947","geneName":"SPI1","intActId":"EBI-2293548"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P78527","intActId":"EBI-352053"},"interactantTwo":{"uniProtKBAccession":"P13010","geneName":"XRCC5","intActId":"EBI-357997"},"numberOfExperiments":9,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P78527","intActId":"EBI-352053"},"interactantTwo":{"uniProtKBAccession":"P12956","geneName":"XRCC6","intActId":"EBI-353208"},"numberOfExperiments":8,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P78527","intActId":"EBI-352053"},"interactantTwo":{"uniProtKBAccession":"P25490","geneName":"YY1","intActId":"EBI-765538"},"numberOfExperiments":2,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12231622"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14734805"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15262962"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22002106"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22002106"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32103174"}],"value":"Nucleus, nucleolus","id":"SL-0188"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15262962"}],"value":"Cytoplasm, cytosol","id":"SL-0091"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["P78527-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["P78527-2"],"sequenceIds":["VSP_004708"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P97313"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12186630"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12231622"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14734805"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33854234"}],"value":"Autophosphorylated at two clusters, the T2609 cluster and the S2056 cluster (PubMed:33854234). Autophosphorylated on Ser-2056, Thr-2609, Thr-2638 and Thr-2647 (PubMed:12186630, PubMed:12231622, PubMed:14734805, PubMed:33854234). Ser-2056 and Thr-2609 are DNA damage-inducible phosphorylation sites (inducible with ionizing radiation, IR) dephosphorylated by PPP5C (PubMed:12186630, PubMed:12231622, PubMed:14734805). Autophosphorylation induces a conformational change that leads to remodeling of the DNA-PK complex, requisite for efficient end processing and DNA repair (PubMed:12186630, PubMed:12231622, PubMed:14734805). Autophosphorylation in trans within DNA-PK complexes loaded on DNA ends leads to the dissociation of PRKDC from DNA and the transition into the short-range NHEJ complex (PubMed:33854234). 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