Search Results

Overview

Uniprot IDP78527
Protein NameDNA-dependent protein kinase catalytic subunit
Gene NamePRKDC
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1057 EKSPVNTKSLFKRLY
1422 LETHLREKITAQSIE
1456 AAVVSACKQLHRAGL
1627 TTILQHWKKCDSWWA
163 FYGELALKKKIPDTV
164 YGELALKKKIPDTVL
263 IRPQIDLKRYAVPSA
2694 RLQRAPLKSVGPDFG
2702 SVGPDFGKKRLGLPG
2703 VGPDFGKKRLGLPGD
2715 PGDEVDNKVKGAAGR
2746 LSLMYARKGVAEQKR
2752 RKGVAEQKREKEIKS
2829 KFKTLSEKNNITQKL
2908 LPAELPAKRVRGKAR
310 HTNVELKKAALSALE
3248 KMIDSARKQNNFSLA
3355 LAEIEEDKARRILEL
3455 EKMLKALKLNSNEAR
4070 ELLLGHEKAPAFRDY
493 GLIRICSKPVVLPKG
692 GVSPKSLKHSPEDPE
832 GFNKVVLKHLKKTKN

Function

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)

Protein Sequence

10 MAGSGAGVRC 20 SLLRLQETLS 30 AADRCGAALA 40 GHQLIRGLGQ 50 ECVLSSSPAV 60 LALQTSLVFS 70 RDFGLLVFVR 80 KSLNSIEFRE 90 CREEILKFLC 100 IFLEKMGQKI 110 APYSVEIKNT 120 CTSVYTKDRA 130 AKCKIPALDL 140 LIKLLQTFRS 150 SRLMDEFKIG 160 ELFSKFYGEL 170 ALKKKIPDTV 180 LEKVYELLGL 190 LGEVHPSEMI 200 NNAENLFRAF 210 LGELKTQMTS 220 AVREPKLPVL 230 AGCLKGLSSL 240 LCNFTKSMEE 250 DPQTSREIFN 260 FVLKAIRPQI 270 DLKRYAVPSA 280 GLRLFALHAS 290 QFSTCLLDNY 300 VSLFEVLLKW 310 CAHTNVELKK 320 AALSALESFL 330 KQVSNMVAKN 340 AEMHKNKLQY 350 FMEQFYGIIR 360 NVDSNNKELS 370 IAIRGYGLFA 380 GPCKVINAKD 390 VDFMYVELIQ 400 RCKQMFLTQT 410 DTGDDRVYQM 420 PSFLQSVASV 430 LLYLDTVPEV 440 YTPVLEHLVV 450 MQIDSFPQYS 460 PKMQLVCCRA 470 IVKVFLALAA 480 KGPVLRNCIS 490 TVVHQGLIRI 500 CSKPVVLPKG 510 PESESEDHRA 520 SGEVRTGKWK 530 VPTYKDYVDL 540 FRHLLSSDQM 550 MDSILADEAF 560 FSVNSSSESL 570 NHLLYDEFVK 580 SVLKIVEKLD 590 LTLEIQTVGE 600 QENGDEAPGV 610 WMIPTSDPAA 620 NLHPAKPKDF 630 SAFINLVEFC 640 REILPEKQAE 650 FFEPWVYSFS 660 YELILQSTRL 670 PLISGFYKLL 680 SITVRNAKKI 690 KYFEGVSPKS 700 LKHSPEDPEK 710 YSCFALFVKF 720 GKEVAVKMKQ 730 YKDELLASCL 740 TFLLSLPHNI 750 IELDVRAYVP 760 ALQMAFKLGL 770 SYTPLAEVGL 780 NALEEWSIYI 790 DRHVMQPYYK 800 DILPCLDGYL 810 KTSALSDETK 820 NNWEVSALSR 830 AAQKGFNKVV 840 LKHLKKTKNL 850 SSNEAISLEE 860 IRIRVVQMLG 870 SLGGQINKNL 880 LTVTSSDEMM 890 KSYVAWDREK 900 RLSFAVPFRE 910 MKPVIFLDVF 920 LPRVTELALT 930 ASDRQTKVAA 940 CELLHSMVMF 950 MLGKATQMPE 960 GGQGAPPMYQ 970 LYKRTFPVLL 980 RLACDVDQVT 990 RQLYEPLVMQ 1000 LIHWFTNNKK 1010 FESQDTVALL 1020 EAILDGIVDP 1030 VDSTLRDFCG 1040 RCIREFLKWS 1050 IKQITPQQQE 1060 KSPVNTKSLF 1070 KRLYSLALHP 1080 NAFKRLGASL 1090 AFNNIYREFR 1100 EEESLVEQFV 1110 FEALVIYMES 1120 LALAHADEKS 1130 LGTIQQCCDA 1140 IDHLCRIIEK 1150 KHVSLNKAKK 1160 RRLPRGFPPS 1170 ASLCLLDLVK 1180 WLLAHCGRPQ 1190 TECRHKSIEL 1200 FYKFVPLLPG 1210 NRSPNLWLKD 1220 VLKEEGVSFL 1230 INTFEGGGCG 1240 QPSGILAQPT 1250 LLYLRGPFSL 1260 QATLCWLDLL 1270 LAALECYNTF 1280 IGERTVGALQ 1290 VLGTEAQSSL 1300 LKAVAFFLES 1310 IAMHDIIAAE 1320 KCFGTGAAGN 1330 RTSPQEGERY 1340 NYSKCTVVVR 1350 IMEFTTTLLN 1360 TSPEGWKLLK 1370 KDLCNTHLMR 1380 VLVQTLCEPA 1390 SIGFNIGDVQ 1400 VMAHLPDVCV 1410 NLMKALKMSP 1420 YKDILETHLR 1430 EKITAQSIEE 1440 LCAVNLYGPD 1450 AQVDRSRLAA 1460 VVSACKQLHR 1470 AGLLHNILPS 1480 QSTDLHHSVG 1490 TELLSLVYKG 1500 IAPGDERQCL 1510 PSLDLSCKQL 1520 ASGLLELAFA 1530 FGGLCERLVS 1540 LLLNPAVLST 1550 ASLGSSQGSV 1560 IHFSHGEYFY 1570 SLFSETINTE 1580 LLKNLDLAVL 1590 ELMQSSVDNT 1600 KMVSAVLNGM 1610 LDQSFRERAN 1620 QKHQGLKLAT 1630 TILQHWKKCD 1640 SWWAKDSPLE 1650 TKMAVLALLA 1660 KILQIDSSVS 1670 FNTSHGSFPE 1680 VFTTYISLLA 1690 DTKLDLHLKG 1700 QAVTLLPFFT 1710 SLTGGSLEEL 1720 RRVLEQLIVA 1730 HFPMQSREFP 1740 PGTPRFNNYV 1750 DCMKKFLDAL 1760 ELSQSPMLLE 1770 LMTEVLCREQ 1780 QHVMEELFQS 1790 SFRRIARRGS 1800 CVTQVGLLES 1810 VYEMFRKDDP 1820 RLSFTRQSFV 1830 DRSLLTLLWH 1840 CSLDALREFF 1850 STIVVDAIDV 1860 LKSRFTKLNE 1870 STFDTQITKK 1880 MGYYKILDVM 1890 YSRLPKDDVH 1900 AKESKINQVF 1910 HGSCITEGNE 1920 LTKTLIKLCY 1930 DAFTENMAGE 1940 NQLLERRRLY 1950 HCAAYNCAIS 1960 VICCVFNELK 1970 FYQGFLFSEK 1980 PEKNLLIFEN 1990 LIDLKRRYNF 2000 PVEVEVPMER 2010 KKKYIEIRKE 2020 AREAANGDSD 2030 GPSYMSSLSY 2040 LADSTLSEEM 2050 SQFDFSTGVQ 2060 SYSYSSQDPR 2070 PATGRFRRRE 2080 QRDPTVHDDV 2090 LELEMDELNR 2100 HECMAPLTAL 2110 VKHMHRSLGP 2120 PQGEEDSVPR 2130 DLPSWMKFLH 2140 GKLGNPIVPL 2150 NIRLFLAKLV 2160 INTEEVFRPY 2170 AKHWLSPLLQ 2180 LAASENNGGE 2190 GIHYMVVEIV 2200 ATILSWTGLA 2210 TPTGVPKDEV 2220 LANRLLNFLM 2230 KHVFHPKRAV 2240 FRHNLEIIKT 2250 LVECWKDCLS 2260 IPYRLIFEKF 2270 SGKDPNSKDN 2280 SVGIQLLGIV 2290 MANDLPPYDP 2300 QCGIQSSEYF 2310 QALVNNMSFV 2320 RYKEVYAAAA 2330 EVLGLILRYV 2340 MERKNILEES 2350 LCELVAKQLK 2360 QHQNTMEDKF 2370 IVCLNKVTKS 2380 FPPLADRFMN 2390 AVFFLLPKFH 2400 GVLKTLCLEV 2410 VLCRVEGMTE 2420 LYFQLKSKDF 2430 VQVMRHRDDE 2440 RQKVCLDIIY 2450 KMMPKLKPVE 2460 LRELLNPVVE 2470 FVSHPSTTCR 2480 EQMYNILMWI 2490 HDNYRDPESE 2500 TDNDSQEIFK 2510 LAKDVLIQGL 2520 IDENPGLQLI 2530 IRNFWSHETR 2540 LPSNTLDRLL 2550 ALNSLYSPKI 2560 EVHFLSLATN 2570 FLLEMTSMSP 2580 DYPNPMFEHP 2590 LSECEFQEYT 2600 IDSDWRFRST 2610 VLTPMFVETQ 2620 ASQGTLQTRT 2630 QEGSLSARWP 2640 VAGQIRATQQ 2650 QHDFTLTQTA 2660 DGRSSFDWLT 2670 GSSTDPLVDH 2680 TSPSSDSLLF 2690 AHKRSERLQR 2700 APLKSVGPDF 2710 GKKRLGLPGD 2720 EVDNKVKGAA 2730 GRTDLLRLRR 2740 RFMRDQEKLS 2750 LMYARKGVAE 2760 QKREKEIKSE 2770 LKMKQDAQVV 2780 LYRSYRHGDL 2790 PDIQIKHSSL 2800 ITPLQAVAQR 2810 DPIIAKQLFS 2820 SLFSGILKEM 2830 DKFKTLSEKN 2840 NITQKLLQDF 2850 NRFLNTTFSF 2860 FPPFVSCIQD 2870 ISCQHAALLS 2880 LDPAAVSAGC 2890 LASLQQPVGI 2900 RLLEEALLRL 2910 LPAELPAKRV 2920 RGKARLPPDV 2930 LRWVELAKLY 2940 RSIGEYDVLR 2950 GIFTSEIGTK 2960 QITQSALLAE 2970 ARSDYSEAAK 2980 QYDEALNKQD 2990 WVDGEPTEAE 3000 KDFWELASLD 3010 CYNHLAEWKS 3020 LEYCSTASID 3030 SENPPDLNKI 3040 WSEPFYQETY 3050 LPYMIRSKLK 3060 LLLQGEADQS 3070 LLTFIDKAMH 3080 GELQKAILEL 3090 HYSQELSLLY 3100 LLQDDVDRAK 3110 YYIQNGIQSF 3120 MQNYSSIDVL 3130 LHQSRLTKLQ 3140 SVQALTEIQE 3150 FISFISKQGN 3160 LSSQVPLKRL 3170 LNTWTNRYPD 3180 AKMDPMNIWD 3190 DIITNRCFFL 3200 SKIEEKLTPL 3210 PEDNSMNVDQ 3220 DGDPSDRMEV 3230 QEQEEDISSL 3240 IRSCKFSMKM 3250 KMIDSARKQN 3260 NFSLAMKLLK 3270 ELHKESKTRD 3280 DWLVSWVQSY 3290 CRLSHCRSRS 3300 QGCSEQVLTV 3310 LKTVSLLDEN 3320 NVSSYLSKNI 3330 LAFRDQNILL 3340 GTTYRIIANA 3350 LSSEPACLAE 3360 IEEDKARRIL 3370 ELSGSSSEDS 3380 EKVIAGLYQR 3390 AFQHLSEAVQ 3400 AAEEEAQPPS 3410 WSCGPAAGVI 3420 DAYMTLADFC 3430 DQQLRKEEEN 3440 ASVIDSAELQ 3450 AYPALVVEKM 3460 LKALKLNSNE 3470 ARLKFPRLLQ 3480 IIERYPEETL 3490 SLMTKEISSV 3500 PCWQFISWIS 3510 HMVALLDKDQ 3520 AVAVQHSVEE 3530 ITDNYPQAIV 3540 YPFIISSESY 3550 SFKDTSTGHK 3560 NKEFVARIKS 3570 KLDQGGVIQD 3580 FINALDQLSN 3590 PELLFKDWSN 3600 DVRAELAKTP 3610 VNKKNIEKMY 3620 ERMYAALGDP 3630 KAPGLGAFRR 3640 KFIQTFGKEF 3650 DKHFGKGGSK 3660 LLRMKLSDFN 3670 DITNMLLLKM 3680 NKDSKPPGNL 3690 KECSPWMSDF 3700 KVEFLRNELE 3710 IPGQYDGRGK 3720 PLPEYHVRIA 3730 GFDERVTVMA 3740 SLRRPKRIII 3750 RGHDEREHPF 3760 LVKGGEDLRQ 3770 DQRVEQLFQV 3780 MNGILAQDSA 3790 CSQRALQLRT 3800 YSVVPMTSRL 3810 GLIEWLENTV 3820 TLKDLLLNTM 3830 SQEEKAAYLS 3840 DPRAPPCEYK 3850 DWLTKMSGKH 3860 DVGAYMLMYK 3870 GANRTETVTS 3880 FRKRESKVPA 3890 DLLKRAFVRM 3900 STSPEAFLAL 3910 RSHFASSHAL 3920 ICISHWILGI 3930 GDRHLNNFMV 3940 AMETGGVIGI 3950 DFGHAFGSAT 3960 QFLPVPELMP 3970 FRLTRQFINL 3980 MLPMKETGLM 3990 YSIMVHALRA 4000 FRSDPGLLTN 4010 TMDVFVKEPS 4020 FDWKNFEQKM 4030 LKKGGSWIQE 4040 INVAEKNWYP 4050 RQKICYAKRK 4060 LAGANPAVIT 4070 CDELLLGHEK 4080 APAFRDYVAV 4090 ARGSKDHNIR 4100 AQEPESGLSE 4110 ETQVKCLMDQ 4120 ATDPNILGRT WEGWEPWM

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
Cellular Component GO:0000781 chromosome, telomeric region
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005958 DNA-dependent protein kinase-DNA ligase 4 complex
Cellular Component GO:0016020 membrane
Cellular Component GO:0070419 nonhomologous end joining complex
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0032991 protein-containing complex
Cellular Component GO:0032993 protein-DNA complex
Cellular Component GO:0032040 small-subunit processome
Cellular Component GO:0005667 transcription regulator complex
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0004677 DNA-dependent protein kinase activity
Molecular Function GO:0003690 double-stranded DNA binding
Molecular Function GO:0019899 enzyme binding
Molecular Function GO:0035979 histone H2AXS139 kinase activity
Molecular Function GO:0019904 protein domain specific binding
Molecular Function GO:0004672 protein kinase activity
Molecular Function GO:0106310 protein serine kinase activity
Molecular Function GO:0004674 protein serine/threonine kinase activity
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0061629 RNA polymerase II-specific DNA-binding transcription factor binding
Molecular Function GO:0034511 U3 snoRNA binding
Biological Process GO:0002218 activation of innate immune response
Biological Process GO:0032869 cellular response to insulin stimulus
Biological Process GO:0006974 DNA damage response
Biological Process GO:0006302 double-strand break repair
Biological Process GO:0097681 double-strand break repair via alternative nonhomologous end joining
Biological Process GO:0006303 double-strand break repair via nonhomologous end joining
Biological Process GO:0033152 immunoglobulin V(D)J recombination
Biological Process GO:0045087 innate immune response
Biological Process GO:0008630 intrinsic apoptotic signaling pathway in response to DNA damage
Biological Process GO:0000460 maturation of 5.8S rRNA
Biological Process GO:0031571 mitotic G1 DNA damage checkpoint signaling
Biological Process GO:0043066 negative regulation of apoptotic process
Biological Process GO:0160049 negative regulation of cGAS/STING signaling pathway
Biological Process GO:0001933 negative regulation of protein phosphorylation
Biological Process GO:0018105 peptidyl-serine phosphorylation
Biological Process GO:0018107 peptidyl-threonine phosphorylation
Biological Process GO:2001034 positive regulation of double-strand break repair via nonhomologous end joining
Biological Process GO:0045648 positive regulation of erythrocyte differentiation
Biological Process GO:0045621 positive regulation of lymphocyte differentiation
Biological Process GO:1905221 positive regulation of platelet formation
Biological Process GO:0045944 positive regulation of transcription by RNA polymerase II
Biological Process GO:0045727 positive regulation of translation
Biological Process GO:0036211 protein modification process
Biological Process GO:0006468 protein phosphorylation
Biological Process GO:0042752 regulation of circadian rhythm
Biological Process GO:0050678 regulation of epithelial cell proliferation
Biological Process GO:1902036 regulation of hematopoietic stem cell differentiation
Biological Process GO:0048660 regulation of smooth muscle cell proliferation
Biological Process GO:0048511 rhythmic process
Biological Process GO:0034462 small-subunit processome assembly
Biological Process GO:0016233 telomere capping
Biological Process GO:0000723 telomere maintenance

Reference

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[6] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.

[7] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[8] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[9] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[10] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[11] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[12] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.