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P78527

- PRKDC_HUMAN

UniProt

P78527 - PRKDC_HUMAN

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Protein

DNA-dependent protein kinase catalytic subunit

Gene

PRKDC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Serine/threonine-protein kinase that acts as a molecular sensor for DNA damage. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break (DSB) repair and V(D)J recombination. Must be bound to DNA to express its catalytic properties. Promotes processing of hairpin DNA structures in V(D)J recombination by activation of the hairpin endonuclease artemis (DCLRE1C). The assembly of the DNA-PK complex at DNA ends is also required for the NHEJ ligation step. Required to protect and align broken ends of DNA. May also act as a scaffold protein to aid the localization of DNA repair proteins to the site of damage. Found at the ends of chromosomes, suggesting a further role in the maintenance of telomeric stability and the prevention of chromosomal end fusion. Also involved in modulation of transcription. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates 'Ser-139' of histone variant H2AX/H2AFX, thereby regulating DNA damage response mechanism. Phosphorylates DCLRE1C, c-Abl/ABL1, histone H1, HSPCA, c-jun/JUN, p53/TP53, PARP1, POU2F1, DHX9, SRF, XRCC1, XRCC1, XRCC4, XRCC5, XRCC6, WRN, MYC and RFA2. Can phosphorylate C1D not only in the presence of linear DNA but also in the presence of supercoiled DNA. Ability to phosphorylate p53/TP53 in the presence of supercoiled DNA is dependent on C1D. 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 machanism. Interacts with CRY1 and CRY2; negatively regulates CRY1 phosphorylation.4 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Inhibited by wortmannin. Activity of the enzyme seems to be attenuated by autophosphorylation.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei2020 – 20212Cleavage; by caspase-3Curated

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. DNA binding Source: UniProtKB-KW
  3. DNA-dependent protein kinase activity Source: MGI
  4. poly(A) RNA binding Source: UniProtKB
  5. protein kinase activity Source: ProtInc
  6. protein serine/threonine kinase activity Source: BHF-UCL
  7. transcription factor binding Source: BHF-UCL

GO - Biological processi

  1. B cell lineage commitment Source: Ensembl
  2. brain development Source: Ensembl
  3. cellular protein modification process Source: ProtInc
  4. cellular response to insulin stimulus Source: BHF-UCL
  5. DNA repair Source: Reactome
  6. double-strand break repair Source: Reactome
  7. double-strand break repair via nonhomologous end joining Source: Reactome
  8. ectopic germ cell programmed cell death Source: Ensembl
  9. heart development Source: Ensembl
  10. immunoglobulin V(D)J recombination Source: Ensembl
  11. innate immune response Source: Reactome
  12. intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl
  13. negative regulation of protein phosphorylation Source: UniProtKB
  14. peptidyl-serine phosphorylation Source: BHF-UCL
  15. positive regulation of apoptotic process Source: Ensembl
  16. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  17. positive regulation of type I interferon production Source: Reactome
  18. pro-B cell differentiation Source: Ensembl
  19. protein destabilization Source: Ensembl
  20. regulation of circadian rhythm Source: UniProtKB
  21. response to gamma radiation Source: Ensembl
  22. rhythmic process Source: UniProtKB-KW
  23. signal transduction involved in mitotic G1 DNA damage checkpoint Source: UniProtKB
  24. somitogenesis Source: Ensembl
  25. T cell differentiation in thymus Source: Ensembl
  26. T cell lineage commitment Source: Ensembl
  27. T cell receptor V(D)J recombination Source: Ensembl
  28. telomere maintenance Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Biological rhythms, DNA damage, DNA recombination, DNA repair

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_1022. Nonhomologous End-joining (NHEJ).
REACT_1201. Processing of DNA ends prior to end rejoining.
REACT_163993. IRF3-mediated induction of type I IFN.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-dependent protein kinase catalytic subunit (EC:2.7.11.1)
Short name:
DNA-PK catalytic subunit
Short name:
DNA-PKcs
Alternative name(s):
DNPK1
p460
Gene namesi
Name:PRKDC
Synonyms:HYRC, HYRC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:9413. PRKDC.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. DNA-dependent protein kinase-DNA ligase 4 complex Source: MGI
  3. membrane Source: UniProtKB
  4. nonhomologous end joining complex Source: UniProtKB
  5. nucleoplasm Source: Reactome
  6. nucleus Source: HPA
  7. transcription factor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1510 – 15101L → P: Loss of interaction with C1D. 1 Publication
Mutagenesisi1516 – 15172EL → PD: Loss of interaction with C1D. 1 Publication
Mutagenesisi2609 – 26091T → A: Leads to radiation sensitivity and impaired DSB joining. Gives rise to reduced phosphorylation; when associated with A-2612. 1 Publication
Mutagenesisi2612 – 26121S → A: Reduced phosphorylation; when associated with A-2609.
Mutagenesisi2638 – 26381T → A: Alleviates phosphorylation, leaves a fully active enzyme with compromised cellular resistance to ionizing radiation without affecting DNA end joining; when associated with A-2647. 1 Publication
Mutagenesisi2647 – 26471T → A: Alleviates phosphorylation, leaves a fully active enzyme with compromised cellular resistance to ionizing radiation without affecting DNA end joining; when associated with A-2638. 1 Publication

Organism-specific databases

Orphaneti317425. Severe combined immunodeficiency due to DNA-PKcs deficiency.
PharmGKBiPA33776.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 41284128DNA-dependent protein kinase catalytic subunitPRO_0000225598Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei117 – 1171N6-acetyllysine1 Publication
Modified residuei828 – 8281N6-acetyllysine1 Publication
Modified residuei893 – 8931Phosphoserine1 Publication
Modified residuei1209 – 12091N6-acetyllysine1 Publication
Modified residuei1970 – 19701N6-acetyllysine1 Publication
Modified residuei2056 – 20561Phosphoserine; by autocatalysis1 Publication
Modified residuei2259 – 22591N6-acetyllysine1 Publication
Modified residuei2609 – 26091Phosphothreonine; by autocatalysis3 Publications
Modified residuei2612 – 26121Phosphoserine; by autocatalysis3 Publications
Modified residuei2638 – 26381Phosphothreonine; by autocatalysis1 Publication
Modified residuei2647 – 26471Phosphothreonine; by autocatalysis1 Publication
Modified residuei3205 – 32051Phosphoserine7 Publications
Modified residuei3241 – 32411N6-acetyllysine1 Publication
Modified residuei3260 – 32601N6-acetyllysine1 Publication
Modified residuei3621 – 36211N6-acetyllysine1 Publication
Modified residuei3638 – 36381N6-acetyllysine1 Publication
Modified residuei3642 – 36421N6-acetyllysine1 Publication
Modified residuei4026 – 40261Phosphoserine3 Publications

Post-translational modificationi

Autophosphorylated on Ser-2056, Thr-2609, Thr-2638 and Thr-2647. Ser-2056 and Thr-2609 are DNA damage-inducible phosphorylation sites (inducible with ionizing radiation, IR) dephosphorylated by PPP5C. Autophosphorylation induces a conformational change that leads to remodeling of the DNA-PK complex, requisite for efficient end processing and DNA repair.28 Publications
S-nitrosylated by GAPDH.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP78527.
PaxDbiP78527.
PRIDEiP78527.

2D gel databases

SWISS-2DPAGEP78527.

PTM databases

PhosphoSiteiP78527.

Expressioni

Gene expression databases

BgeeiP78527.
ExpressionAtlasiP78527. baseline and differential.
GenevestigatoriP78527.

Organism-specific databases

HPAiCAB005167.
HPA035174.

Interactioni

Subunit structurei

DNA-PK is a heterotrimer of PRKDC and the Ku p70-p86 (XRCC6-XRCC5) dimer. Formation of this complex may be promoted by interaction with ILF3. Associates with the DNA-bound Ku heterodimer, but it can also bind to and be activated by free DNA. Interacts with DNA-PKcs-interacting protein (KIP) with the region upstream the kinase domain. PRKDC alone also interacts with and phosphorylates DCLRE1C, thereby activating the latent endonuclease activity of this protein. Interacts with C1D. Interacts with TTI1 and TELO2. Interacts with CIB1.14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AIREO439182EBI-352053,EBI-1753081
CASP2P425754EBI-352053,EBI-520342
ETS1P149212EBI-352053,EBI-913209
ETV1P505492EBI-352053,EBI-3905068
HOXB7P096292EBI-352053,EBI-1248457
IGFBP3P179362EBI-352053,EBI-715709
MAPKAP1Q9BPZ72EBI-352053,EBI-749938
PIDD1Q9HB756EBI-352053,EBI-520427
SPI1P179472EBI-352053,EBI-2293548
XRCC5P130106EBI-352053,EBI-357997
XRCC6P129565EBI-352053,EBI-353208
YY1P254902EBI-352053,EBI-765538

Protein-protein interaction databases

BioGridi111577. 216 interactions.
DIPiDIP-24186N.
IntActiP78527. 70 interactions.
MINTiMINT-5006046.

Structurei

3D structure databases

ProteinModelPortaliP78527.
SMRiP78527. Positions 3724-3998.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati288 – 32336HEAT 1Add
BLAST
Repeati1004 – 104037HEAT 2Add
BLAST
Repeati1723 – 175634TPR 1Add
BLAST
Domaini2883 – 3539657FATPROSITE-ProRule annotationAdd
BLAST
Repeati2920 – 294829TPR 2Add
BLAST
Repeati2949 – 298234TPR 3Add
BLAST
Domaini3747 – 4015269PI3K/PI4KPROSITE-ProRule annotationAdd
BLAST
Domaini4096 – 412833FATCPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1503 – 153836Interaction with C1DAdd
BLAST
Regioni1503 – 153836Leucine-zipperAdd
BLAST
Regioni2436 – 3212777KIP-bindingAdd
BLAST

Sequence similaritiesi

Belongs to the PI3/PI4-kinase family.Curated
Contains 1 FAT domain.PROSITE-ProRule annotation
Contains 1 FATC domain.PROSITE-ProRule annotation
Contains 2 HEAT repeats.Curated
Contains 1 PI3K/PI4K domain.PROSITE-ProRule annotation
Contains 3 TPR repeats.Curated

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiCOG5032.
GeneTreeiENSGT00770000120527.
HOVERGENiHBG053681.
InParanoidiP78527.
KOiK06642.
OrthoDBiEOG7DNNT7.
PhylomeDBiP78527.
TreeFamiTF324494.

Family and domain databases

Gene3Di1.10.1070.11. 3 hits.
1.25.10.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR003152. FATC.
IPR011009. Kinase-like_dom.
IPR012582. NUC194.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003151. PIK-rel_kinase_FAT.
IPR014009. PIK_FAT.
[Graphical view]
PfamiPF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF08163. NUC194. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
[Graphical view]
SMARTiSM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 8 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS51189. FAT. 1 hit.
PS51190. FATC. 1 hit.
PS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P78527-1) [UniParc]FASTAAdd to Basket

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

        10         20         30         40         50
MAGSGAGVRC SLLRLQETLS AADRCGAALA GHQLIRGLGQ ECVLSSSPAV
60 70 80 90 100
LALQTSLVFS RDFGLLVFVR KSLNSIEFRE CREEILKFLC IFLEKMGQKI
110 120 130 140 150
APYSVEIKNT CTSVYTKDRA AKCKIPALDL LIKLLQTFRS SRLMDEFKIG
160 170 180 190 200
ELFSKFYGEL ALKKKIPDTV LEKVYELLGL LGEVHPSEMI NNAENLFRAF
210 220 230 240 250
LGELKTQMTS AVREPKLPVL AGCLKGLSSL LCNFTKSMEE DPQTSREIFN
260 270 280 290 300
FVLKAIRPQI DLKRYAVPSA GLRLFALHAS QFSTCLLDNY VSLFEVLLKW
310 320 330 340 350
CAHTNVELKK AALSALESFL KQVSNMVAKN AEMHKNKLQY FMEQFYGIIR
360 370 380 390 400
NVDSNNKELS IAIRGYGLFA GPCKVINAKD VDFMYVELIQ RCKQMFLTQT
410 420 430 440 450
DTGDDRVYQM PSFLQSVASV LLYLDTVPEV YTPVLEHLVV MQIDSFPQYS
460 470 480 490 500
PKMQLVCCRA IVKVFLALAA KGPVLRNCIS TVVHQGLIRI CSKPVVLPKG
510 520 530 540 550
PESESEDHRA SGEVRTGKWK VPTYKDYVDL FRHLLSSDQM MDSILADEAF
560 570 580 590 600
FSVNSSSESL NHLLYDEFVK SVLKIVEKLD LTLEIQTVGE QENGDEAPGV
610 620 630 640 650
WMIPTSDPAA NLHPAKPKDF SAFINLVEFC REILPEKQAE FFEPWVYSFS
660 670 680 690 700
YELILQSTRL PLISGFYKLL SITVRNAKKI KYFEGVSPKS LKHSPEDPEK
710 720 730 740 750
YSCFALFVKF GKEVAVKMKQ YKDELLASCL TFLLSLPHNI IELDVRAYVP
760 770 780 790 800
ALQMAFKLGL SYTPLAEVGL NALEEWSIYI DRHVMQPYYK DILPCLDGYL
810 820 830 840 850
KTSALSDETK NNWEVSALSR AAQKGFNKVV LKHLKKTKNL SSNEAISLEE
860 870 880 890 900
IRIRVVQMLG SLGGQINKNL LTVTSSDEMM KSYVAWDREK RLSFAVPFRE
910 920 930 940 950
MKPVIFLDVF LPRVTELALT ASDRQTKVAA CELLHSMVMF MLGKATQMPE
960 970 980 990 1000
GGQGAPPMYQ LYKRTFPVLL RLACDVDQVT RQLYEPLVMQ LIHWFTNNKK
1010 1020 1030 1040 1050
FESQDTVALL EAILDGIVDP VDSTLRDFCG RCIREFLKWS IKQITPQQQE
1060 1070 1080 1090 1100
KSPVNTKSLF KRLYSLALHP NAFKRLGASL AFNNIYREFR EEESLVEQFV
1110 1120 1130 1140 1150
FEALVIYMES LALAHADEKS LGTIQQCCDA IDHLCRIIEK KHVSLNKAKK
1160 1170 1180 1190 1200
RRLPRGFPPS ASLCLLDLVK WLLAHCGRPQ TECRHKSIEL FYKFVPLLPG
1210 1220 1230 1240 1250
NRSPNLWLKD VLKEEGVSFL INTFEGGGCG QPSGILAQPT LLYLRGPFSL
1260 1270 1280 1290 1300
QATLCWLDLL LAALECYNTF IGERTVGALQ VLGTEAQSSL LKAVAFFLES
1310 1320 1330 1340 1350
IAMHDIIAAE KCFGTGAAGN RTSPQEGERY NYSKCTVVVR IMEFTTTLLN
1360 1370 1380 1390 1400
TSPEGWKLLK KDLCNTHLMR VLVQTLCEPA SIGFNIGDVQ VMAHLPDVCV
1410 1420 1430 1440 1450
NLMKALKMSP YKDILETHLR EKITAQSIEE LCAVNLYGPD AQVDRSRLAA
1460 1470 1480 1490 1500
VVSACKQLHR AGLLHNILPS QSTDLHHSVG TELLSLVYKG IAPGDERQCL
1510 1520 1530 1540 1550
PSLDLSCKQL ASGLLELAFA FGGLCERLVS LLLNPAVLST ASLGSSQGSV
1560 1570 1580 1590 1600
IHFSHGEYFY SLFSETINTE LLKNLDLAVL ELMQSSVDNT KMVSAVLNGM
1610 1620 1630 1640 1650
LDQSFRERAN QKHQGLKLAT TILQHWKKCD SWWAKDSPLE TKMAVLALLA
1660 1670 1680 1690 1700
KILQIDSSVS FNTSHGSFPE VFTTYISLLA DTKLDLHLKG QAVTLLPFFT
1710 1720 1730 1740 1750
SLTGGSLEEL RRVLEQLIVA HFPMQSREFP PGTPRFNNYV DCMKKFLDAL
1760 1770 1780 1790 1800
ELSQSPMLLE LMTEVLCREQ QHVMEELFQS SFRRIARRGS CVTQVGLLES
1810 1820 1830 1840 1850
VYEMFRKDDP RLSFTRQSFV DRSLLTLLWH CSLDALREFF STIVVDAIDV
1860 1870 1880 1890 1900
LKSRFTKLNE STFDTQITKK MGYYKILDVM YSRLPKDDVH AKESKINQVF
1910 1920 1930 1940 1950
HGSCITEGNE LTKTLIKLCY DAFTENMAGE NQLLERRRLY HCAAYNCAIS
1960 1970 1980 1990 2000
VICCVFNELK FYQGFLFSEK PEKNLLIFEN LIDLKRRYNF PVEVEVPMER
2010 2020 2030 2040 2050
KKKYIEIRKE AREAANGDSD GPSYMSSLSY LADSTLSEEM SQFDFSTGVQ
2060 2070 2080 2090 2100
SYSYSSQDPR PATGRFRRRE QRDPTVHDDV LELEMDELNR HECMAPLTAL
2110 2120 2130 2140 2150
VKHMHRSLGP PQGEEDSVPR DLPSWMKFLH GKLGNPIVPL NIRLFLAKLV
2160 2170 2180 2190 2200
INTEEVFRPY AKHWLSPLLQ LAASENNGGE GIHYMVVEIV ATILSWTGLA
2210 2220 2230 2240 2250
TPTGVPKDEV LANRLLNFLM KHVFHPKRAV FRHNLEIIKT LVECWKDCLS
2260 2270 2280 2290 2300
IPYRLIFEKF SGKDPNSKDN SVGIQLLGIV MANDLPPYDP QCGIQSSEYF
2310 2320 2330 2340 2350
QALVNNMSFV RYKEVYAAAA EVLGLILRYV MERKNILEES LCELVAKQLK
2360 2370 2380 2390 2400
QHQNTMEDKF IVCLNKVTKS FPPLADRFMN AVFFLLPKFH GVLKTLCLEV
2410 2420 2430 2440 2450
VLCRVEGMTE LYFQLKSKDF VQVMRHRDDE RQKVCLDIIY KMMPKLKPVE
2460 2470 2480 2490 2500
LRELLNPVVE FVSHPSTTCR EQMYNILMWI HDNYRDPESE TDNDSQEIFK
2510 2520 2530 2540 2550
LAKDVLIQGL IDENPGLQLI IRNFWSHETR LPSNTLDRLL ALNSLYSPKI
2560 2570 2580 2590 2600
EVHFLSLATN FLLEMTSMSP DYPNPMFEHP LSECEFQEYT IDSDWRFRST
2610 2620 2630 2640 2650
VLTPMFVETQ ASQGTLQTRT QEGSLSARWP VAGQIRATQQ QHDFTLTQTA
2660 2670 2680 2690 2700
DGRSSFDWLT GSSTDPLVDH TSPSSDSLLF AHKRSERLQR APLKSVGPDF
2710 2720 2730 2740 2750
GKKRLGLPGD EVDNKVKGAA GRTDLLRLRR RFMRDQEKLS LMYARKGVAE
2760 2770 2780 2790 2800
QKREKEIKSE LKMKQDAQVV LYRSYRHGDL PDIQIKHSSL ITPLQAVAQR
2810 2820 2830 2840 2850
DPIIAKQLFS SLFSGILKEM DKFKTLSEKN NITQKLLQDF NRFLNTTFSF
2860 2870 2880 2890 2900
FPPFVSCIQD ISCQHAALLS LDPAAVSAGC LASLQQPVGI RLLEEALLRL
2910 2920 2930 2940 2950
LPAELPAKRV RGKARLPPDV LRWVELAKLY RSIGEYDVLR GIFTSEIGTK
2960 2970 2980 2990 3000
QITQSALLAE ARSDYSEAAK QYDEALNKQD WVDGEPTEAE KDFWELASLD
3010 3020 3030 3040 3050
CYNHLAEWKS LEYCSTASID SENPPDLNKI WSEPFYQETY LPYMIRSKLK
3060 3070 3080 3090 3100
LLLQGEADQS LLTFIDKAMH GELQKAILEL HYSQELSLLY LLQDDVDRAK
3110 3120 3130 3140 3150
YYIQNGIQSF MQNYSSIDVL LHQSRLTKLQ SVQALTEIQE FISFISKQGN
3160 3170 3180 3190 3200
LSSQVPLKRL LNTWTNRYPD AKMDPMNIWD DIITNRCFFL SKIEEKLTPL
3210 3220 3230 3240 3250
PEDNSMNVDQ DGDPSDRMEV QEQEEDISSL IRSCKFSMKM KMIDSARKQN
3260 3270 3280 3290 3300
NFSLAMKLLK ELHKESKTRD DWLVSWVQSY CRLSHCRSRS QGCSEQVLTV
3310 3320 3330 3340 3350
LKTVSLLDEN NVSSYLSKNI LAFRDQNILL GTTYRIIANA LSSEPACLAE
3360 3370 3380 3390 3400
IEEDKARRIL ELSGSSSEDS EKVIAGLYQR AFQHLSEAVQ AAEEEAQPPS
3410 3420 3430 3440 3450
WSCGPAAGVI DAYMTLADFC DQQLRKEEEN ASVIDSAELQ AYPALVVEKM
3460 3470 3480 3490 3500
LKALKLNSNE ARLKFPRLLQ IIERYPEETL SLMTKEISSV PCWQFISWIS
3510 3520 3530 3540 3550
HMVALLDKDQ AVAVQHSVEE ITDNYPQAIV YPFIISSESY SFKDTSTGHK
3560 3570 3580 3590 3600
NKEFVARIKS KLDQGGVIQD FINALDQLSN PELLFKDWSN DVRAELAKTP
3610 3620 3630 3640 3650
VNKKNIEKMY ERMYAALGDP KAPGLGAFRR KFIQTFGKEF DKHFGKGGSK
3660 3670 3680 3690 3700
LLRMKLSDFN DITNMLLLKM NKDSKPPGNL KECSPWMSDF KVEFLRNELE
3710 3720 3730 3740 3750
IPGQYDGRGK PLPEYHVRIA GFDERVTVMA SLRRPKRIII RGHDEREHPF
3760 3770 3780 3790 3800
LVKGGEDLRQ DQRVEQLFQV MNGILAQDSA CSQRALQLRT YSVVPMTSRL
3810 3820 3830 3840 3850
GLIEWLENTV TLKDLLLNTM SQEEKAAYLS DPRAPPCEYK DWLTKMSGKH
3860 3870 3880 3890 3900
DVGAYMLMYK GANRTETVTS FRKRESKVPA DLLKRAFVRM STSPEAFLAL
3910 3920 3930 3940 3950
RSHFASSHAL ICISHWILGI GDRHLNNFMV AMETGGVIGI DFGHAFGSAT
3960 3970 3980 3990 4000
QFLPVPELMP FRLTRQFINL MLPMKETGLM YSIMVHALRA FRSDPGLLTN
4010 4020 4030 4040 4050
TMDVFVKEPS FDWKNFEQKM LKKGGSWIQE INVAEKNWYP RQKICYAKRK
4060 4070 4080 4090 4100
LAGANPAVIT CDELLLGHEK APAFRDYVAV ARGSKDHNIR AQEPESGLSE
4110 4120
ETQVKCLMDQ ATDPNILGRT WEGWEPWM
Length:4,128
Mass (Da):469,089
Last modified:October 31, 2003 - v3
Checksum:iAC6E747FEB09F3E5
GO
Isoform 2 (identifier: P78527-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     3799-3829: Missing.

Show »
Length:4,097
Mass (Da):465,501
Checksum:iB698F749065D319B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti405 – 4051D → Y in AAC50210. 1 PublicationCurated
Sequence conflicti1008 – 10081A → S in AAC50210. 1 PublicationCurated
Sequence conflicti3660 – 36601N → T in AAA79184. (PubMed:7594449)Curated
Sequence conflicti3817 – 38171L → W in AAA79184. (PubMed:7594449)Curated
Sequence conflicti3862 – 38621A → P in AAA79184. (PubMed:7594449)Curated
Sequence conflicti4031 – 40311I → V in AAK40350. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti6 – 61A → S.2 Publications
Corresponds to variant rs8177999 [ dbSNP | Ensembl ].
VAR_019179
Natural varianti263 – 2631K → N in a lung adenocarcinoma sample; somatic mutation. 1 Publication
VAR_041602
Natural varianti333 – 3331M → I.2 Publications
Corresponds to variant rs8178017 [ dbSNP | Ensembl ].
VAR_019180
Natural varianti420 – 4201V → I.1 Publication
Corresponds to variant rs55925466 [ dbSNP | Ensembl ].
VAR_041603
Natural varianti500 – 5001G → S in a metastatic melanoma sample; somatic mutation. 1 Publication
VAR_041604
Natural varianti605 – 6051T → S.2 Publications
Corresponds to variant rs8178033 [ dbSNP | Ensembl ].
VAR_019181
Natural varianti649 – 6491F → L.1 Publication
Corresponds to variant rs55811715 [ dbSNP | Ensembl ].
VAR_041605
Natural varianti680 – 6801I → M.1 Publication
Corresponds to variant rs8178040 [ dbSNP | Ensembl ].
VAR_019182
Natural varianti695 – 6951P → S.2 Publications
Corresponds to variant rs8178046 [ dbSNP | Ensembl ].
VAR_019183
Natural varianti1071 – 10711N → S.1 Publication
Corresponds to variant rs8178070 [ dbSNP | Ensembl ].
VAR_019184
Natural varianti1136 – 11361R → H in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
VAR_041606
Natural varianti1190 – 11901L → V.1 Publication
Corresponds to variant rs34598508 [ dbSNP | Ensembl ].
VAR_041607
Natural varianti1237 – 12371A → T.1 Publication
VAR_041608
Natural varianti1279 – 12791L → F.1 Publication
VAR_041609
Natural varianti1314 – 13141G → V.1 Publication
Corresponds to variant rs8178090 [ dbSNP | Ensembl ].
VAR_019185
Natural varianti1447 – 14471R → M in a lung squamous cell carcinoma sample; somatic mutation. 1 Publication
VAR_041610
Natural varianti1588 – 15881D → V.1 Publication
Corresponds to variant rs8178104 [ dbSNP | Ensembl ].
VAR_019186
Natural varianti1603 – 16031Q → H.1 Publication
Corresponds to variant rs8178106 [ dbSNP | Ensembl ].
VAR_019187
Natural varianti1619 – 16191A → G.1 Publication
Corresponds to variant rs56182356 [ dbSNP | Ensembl ].
VAR_041611
Natural varianti1680 – 16801A → V in a metastatic melanoma sample; somatic mutation. 1 Publication
Corresponds to variant rs55735910 [ dbSNP | Ensembl ].
VAR_041612
Natural varianti2023 – 20231S → P.1 Publication
Corresponds to variant rs56042895 [ dbSNP | Ensembl ].
VAR_041613
Natural varianti2095 – 20951A → V.1 Publication
Corresponds to variant rs8178147 [ dbSNP | Ensembl ].
VAR_019188
Natural varianti2598 – 25981R → Q.1 Publication
Corresponds to variant rs55923149 [ dbSNP | Ensembl ].
VAR_041614
Natural varianti2702 – 27021K → E.1 Publication
Corresponds to variant rs8178178 [ dbSNP | Ensembl ].
VAR_019189
Natural varianti2810 – 28101S → N in a metastatic melanoma sample; somatic mutation. 1 Publication
VAR_041615
Natural varianti2899 – 28991R → C.2 Publications
Corresponds to variant rs4278157 [ dbSNP | Ensembl ].
VAR_019190
Natural varianti2941 – 29411G → A in a lung neuroendocrine carcinoma sample; somatic mutation. 1 Publication
VAR_041616
Natural varianti3085 – 30851E → D.1 Publication
Corresponds to variant rs56135402 [ dbSNP | Ensembl ].
VAR_041617
Natural varianti3149 – 31491G → D.2 Publications
Corresponds to variant rs8178208 [ dbSNP | Ensembl ].
VAR_019191
Natural varianti3198 – 31981T → S.1 Publication
Corresponds to variant rs55793951 [ dbSNP | Ensembl ].
VAR_041618
Natural varianti3201 – 32011P → S.2 Publications
Corresponds to variant rs8178216 [ dbSNP | Ensembl ].
VAR_019192
Natural varianti3404 – 34041G → E.2 Publications
Corresponds to variant rs8178225 [ dbSNP | Ensembl ].
VAR_019193
Natural varianti3434 – 34341I → T.2 Publications
Corresponds to variant rs7830743 [ dbSNP | Ensembl ].
VAR_019194
Natural varianti3459 – 34591N → S.1 Publication
Corresponds to variant rs8178228 [ dbSNP | Ensembl ].
VAR_019195
Natural varianti3562 – 35621L → M.2 Publications
Corresponds to variant rs8178232 [ dbSNP | Ensembl ].
VAR_019196
Natural varianti3584 – 35841L → F.1 Publication
VAR_041619
Natural varianti3702 – 37021P → L.
Corresponds to variant rs8178236 [ dbSNP | Ensembl ].
VAR_050534
Natural varianti3800 – 38001L → I.1 Publication
VAR_041620
Natural varianti3836 – 38361P → L.2 Publications
Corresponds to variant rs8178245 [ dbSNP | Ensembl ].
VAR_019197
Natural varianti3932 – 39321M → V.1 Publication
VAR_019198
Natural varianti3936 – 39361G → S.1 Publication
VAR_041621
Natural varianti3937 – 39371V → M.1 Publication
VAR_041622

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei3799 – 382931Missing in isoform 2. 1 PublicationVSP_004708Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U47077 mRNA. Translation: AAB39925.5.
U34994 mRNA. Translation: AAC50210.3.
AY316117 Genomic DNA. Translation: AAP69525.1.
U63630 Genomic DNA. Translation: AAC52019.2.
U90415 Genomic DNA. Translation: AAB51722.1.
L27425 Genomic DNA. Translation: AAA79244.1.
AB052953 Genomic DNA. Translation: BAB79635.1.
U35835 mRNA. Translation: AAA79184.1.
AY030284 Genomic DNA. Translation: AAK40350.1.
AB208860 mRNA. Translation: BAD92097.1.
CCDSiCCDS75734.1. [P78527-2]
CCDS75735.1. [P78527-1]
PIRiA57099.
G02083.
RefSeqiNP_001075109.1. NM_001081640.1. [P78527-2]
NP_008835.5. NM_006904.6. [P78527-1]
UniGeneiHs.491682.

Genome annotation databases

EnsembliENST00000314191; ENSP00000313420; ENSG00000253729. [P78527-1]
ENST00000338368; ENSP00000345182; ENSG00000253729. [P78527-2]
GeneIDi5591.
KEGGihsa:5591.
UCSCiuc003xqi.3. human. [P78527-1]
uc003xqj.3. human. [P78527-2]

Polymorphism databases

DMDMi38258929.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U47077 mRNA. Translation: AAB39925.5 .
U34994 mRNA. Translation: AAC50210.3 .
AY316117 Genomic DNA. Translation: AAP69525.1 .
U63630 Genomic DNA. Translation: AAC52019.2 .
U90415 Genomic DNA. Translation: AAB51722.1 .
L27425 Genomic DNA. Translation: AAA79244.1 .
AB052953 Genomic DNA. Translation: BAB79635.1 .
U35835 mRNA. Translation: AAA79184.1 .
AY030284 Genomic DNA. Translation: AAK40350.1 .
AB208860 mRNA. Translation: BAD92097.1 .
CCDSi CCDS75734.1. [P78527-2 ]
CCDS75735.1. [P78527-1 ]
PIRi A57099.
G02083.
RefSeqi NP_001075109.1. NM_001081640.1. [P78527-2 ]
NP_008835.5. NM_006904.6. [P78527-1 ]
UniGenei Hs.491682.

3D structure databases

ProteinModelPortali P78527.
SMRi P78527. Positions 3724-3998.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111577. 216 interactions.
DIPi DIP-24186N.
IntActi P78527. 70 interactions.
MINTi MINT-5006046.

Chemistry

BindingDBi P78527.
ChEMBLi CHEMBL3142.
DrugBanki DB00201. Caffeine.

PTM databases

PhosphoSitei P78527.

Polymorphism databases

DMDMi 38258929.

2D gel databases

SWISS-2DPAGE P78527.

Proteomic databases

MaxQBi P78527.
PaxDbi P78527.
PRIDEi P78527.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000314191 ; ENSP00000313420 ; ENSG00000253729 . [P78527-1 ]
ENST00000338368 ; ENSP00000345182 ; ENSG00000253729 . [P78527-2 ]
GeneIDi 5591.
KEGGi hsa:5591.
UCSCi uc003xqi.3. human. [P78527-1 ]
uc003xqj.3. human. [P78527-2 ]

Organism-specific databases

CTDi 5591.
GeneCardsi GC08M048685.
HGNCi HGNC:9413. PRKDC.
HPAi CAB005167.
HPA035174.
MIMi 600899. gene.
neXtProti NX_P78527.
Orphaneti 317425. Severe combined immunodeficiency due to DNA-PKcs deficiency.
PharmGKBi PA33776.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5032.
GeneTreei ENSGT00770000120527.
HOVERGENi HBG053681.
InParanoidi P78527.
KOi K06642.
OrthoDBi EOG7DNNT7.
PhylomeDBi P78527.
TreeFami TF324494.

Enzyme and pathway databases

Reactomei REACT_1022. Nonhomologous End-joining (NHEJ).
REACT_1201. Processing of DNA ends prior to end rejoining.
REACT_163993. IRF3-mediated induction of type I IFN.

Miscellaneous databases

ChiTaRSi PRKDC. human.
GeneWikii DNA-PKcs.
GenomeRNAii 5591.
NextBioi 21692.
PROi P78527.
SOURCEi Search...

Gene expression databases

Bgeei P78527.
ExpressionAtlasi P78527. baseline and differential.
Genevestigatori P78527.

Family and domain databases

Gene3Di 1.10.1070.11. 3 hits.
1.25.10.10. 3 hits.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR003152. FATC.
IPR011009. Kinase-like_dom.
IPR012582. NUC194.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003151. PIK-rel_kinase_FAT.
IPR014009. PIK_FAT.
[Graphical view ]
Pfami PF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF08163. NUC194. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
[Graphical view ]
SMARTi SM00146. PI3Kc. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 8 hits.
SSF56112. SSF56112. 2 hits.
PROSITEi PS51189. FAT. 1 hit.
PS51190. FATC. 1 hit.
PS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "DNA-dependent protein kinase catalytic subunit: a relative of phosphatidylinositol 3-kinase and the ataxia telangiectasia gene product."
    Hartley K.O., Gell D., Smith G.C.M., Zhang H., Divecha N., Connelly M.A., Admon A., Lees-Miller S.P., Anderson C.W., Jackson S.P.
    Cell 82:849-856(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Cervix carcinoma.
  2. Gell D., Anderson C.W.
    Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION, ALTERNATIVE SPLICING.
  3. NIEHS SNPs program
    Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-6; ILE-333; SER-605; MET-680; SER-695; SER-1071; VAL-1314; VAL-1588; HIS-1603; VAL-2095; GLU-2702; CYS-2899; ASP-3149; SER-3201; GLU-3404; THR-3434; SER-3459; MET-3562; LEU-3836 AND VAL-3932.
  4. "Frameshift mutation in PRKDC, the gene for DNA-PKcs, in the DNA repair-defective, human, glioma-derived cell line M059J."
    Anderson C.W., Dunn J.J., Freimuth P.I., Galloway A.M., Allalunis-Turner M.J.
    Radiat. Res. 156:2-9(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1689.
  5. "MCM4 and PRKDC, human genes encoding proteins MCM4 and DNA-PKcs, are close neighbours located on chromosome 8q12-->q13."
    Ladenburger E.M., Fackelmayer F.O., Hameister H., Knippers R.
    Cytogenet. Cell Genet. 77:268-270(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49.
  6. "Gene for the catalytic subunit of the human DNA-activated protein kinase maps to the site of the XRCC7 gene on chromosome 8."
    Sipley J.D., Menninger J.C., Hartley K.O., Ward D.C., Jackson S.P., Anderson C.W.
    Proc. Natl. Acad. Sci. U.S.A. 92:7515-7519(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1789-2203.
    Tissue: Placenta.
  7. Abe M.
    Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2255-2335.
    Tissue: Placenta.
  8. "Human DNA-activated protein kinase (DNA-PK) is homologous to phosphatidylinositol kinases."
    Poltoratsky V.P., Shi X., York J.D., Lieber M.R., Carter T.H.
    J. Immunol. 155:4529-4533(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3199-4128 (ISOFORM 1).
    Tissue: Fetal lung.
  9. "Sequence of the 3' segment (exons 70-86) of PRKDC, the gene for human DNA-PKcs."
    Anderson C.W., Dunn J.J., Freimuth P.I.
    Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3250-4128 (ISOFORM 1).
  10. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno F.R.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3372-4128 (ISOFORM 2).
    Tissue: Brain.
  11. "The human double-stranded DNA-activated protein kinase phosphorylates the 90-kDa heat-shock protein, hsp90 alpha at two NH2-terminal threonine residues."
    Lees-Miller S.P., Anderson C.W.
    J. Biol. Chem. 264:17275-17280(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION OF HSPCA.
  12. "A DNA-activated protein kinase from HeLa cell nuclei."
    Carter T., Vancurova I., Sun I., Lou W., DeLeon S.
    Mol. Cell. Biol. 10:6460-6471(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION OF H1.
  13. "DNA-activated protein kinase in Raji Burkitt's lymphoma cells. Phosphorylation of c-Myc oncoprotein."
    Iijima S., Teraoka H., Date T., Tsukada K.
    Eur. J. Biochem. 206:595-603(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION OF MYC.
  14. "The carboxyl-terminal transactivation domain of human serum response factor contains DNA-activated protein kinase phosphorylation sites."
    Liu S.-H., Ma J.-T., Yueh A.Y., Lees-Miller S.P., Anderson C.W., Ng S.-Y.
    J. Biol. Chem. 268:21147-21154(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION OF SRF.
  15. "c-Jun is phosphorylated by the DNA-dependent protein kinase in vitro; definition of the minimal kinase recognition motif."
    Bannister A.J., Gottlieb T.M., Kouzarides T., Jackson S.P.
    Nucleic Acids Res. 21:1289-1295(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION OF JUN.
  16. "CPP32/Yama/apopain cleaves the catalytic component of DNA-dependent protein kinase in the holoenzyme."
    Teraoka H., Yumoto Y., Watanabe F., Tsukada K., Suwa A., Enari M., Nagata S.
    FEBS Lett. 393:1-6(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE BY CASPASE-3.
  17. "Alternate splice-site utilization in the gene for the catalytic subunit of the DNA-activated protein kinase, DNA-PKcs."
    Connelly M.A., Zhang H., Kieleczawa J., Anderson C.W.
    Gene 175:271-273(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
  18. "DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2."
    Shieh S.-Y., Ikeda M., Taya Y., Prives C.
    Cell 91:325-334(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION OF TP53.
  19. "Interaction between DNA-dependent protein kinase and a novel protein, KIP."
    Wu X., Lieber M.R.
    Mutat. Res. 385:13-20(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, INTERACTION WITH CIB1.
  20. "Double-strand break repair by Ku70 requires heterodimerization with Ku80 and DNA binding functions."
    Jin S., Weaver D.T.
    EMBO J. 16:6874-6885(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION OF XRCC6.
  21. "Mapping of amino acid residues in the p34 subunit of human single-stranded DNA-binding protein phosphorylated by DNA-dependent protein kinase and Cdc2 kinase in vitro."
    Niu H., Erdjument-Bromage H., Pan Z.-Q., Lee S.-H., Tempst P., Hurwitz J.
    J. Biol. Chem. 272:12634-12641(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION OF RFA2.
  22. "Inhibition of phosphoinositide 3-kinase related kinases by the radiosensitizing agent wortmannin."
    Sarkaria J.N., Tibbetts R.S., Busby E.C., Kennedy A.P., Hill D.E., Abraham R.T.
    Cancer Res. 58:4375-4382(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  23. "DNA end-independent activation of DNA-PK mediated via association with the DNA-binding protein C1D."
    Yavuzer U., Smith G.C.M., Bliss T., Werner D., Jackson S.P.
    Genes Dev. 12:2188-2199(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH C1D, MUTAGENESIS OF LEU-1510 AND 1516-GLU-LEU-1517.
  24. "DNA-dependent protein kinase interacts with antigen receptor response element binding proteins NF90 and NF45."
    Ting N.S.Y., Kao P.N., Chan D.W., Lintott L.G., Lees-Miller S.P.
    J. Biol. Chem. 273:2136-2145(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ILF3.
  25. "DNA-dependent protein kinase: DNA binding and activation in the absence of Ku."
    Hammarsten O., Chu G.
    Proc. Natl. Acad. Sci. U.S.A. 95:525-530(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING.
  26. "DNA-dependent protein kinase phosphorylation sites in Ku 70/80 heterodimer."
    Chan D.W., Ye R., Veillette C.J., Lees-Miller S.P.
    Biochemistry 38:1819-1828(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION OF XRCC5 AND XRCC6.
  27. "Suppression of the poly(ADP-ribose) polymerase activity by DNA-dependent protein kinase in vitro."
    Ariumi Y., Masutani M., Copeland T.D., Mimori T., Sugimura T., Shimotohno K., Ueda K., Hatanaka M., Noda M.
    Oncogene 18:4616-4625(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION OF PARP1.
  28. "Identification of in vitro and in vivo phosphorylation sites in the catalytic subunit of the DNA-dependent protein kinase."
    Douglas P., Sapkota G.P., Morrice N., Yu Y., Goodarzi A.A., Merkle D., Meek K., Alessi D.R., Lees-Miller S.P.
    Biochem. J. 368:243-251(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-2609; SER-2612; THR-2638 AND THR-2647.
  29. "Hairpin opening and overhang processing by an Artemis/DNA-dependent protein kinase complex in nonhomologous end joining and V(D)J recombination."
    Ma Y., Pannicke U., Schwarz K., Lieber M.R.
    Cell 108:781-794(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DCLRE1C.
  30. "Defining interactions between DNA-PK and ligase IV/XRCC4."
    Hsu H.-L., Yannone S.M., Chen D.J.
    DNA Repair 1:225-235(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION OF XRCC4.
  31. "Autophosphorylation of the DNA-dependent protein kinase catalytic subunit is required for rejoining of DNA double-strand breaks."
    Chan D.W., Chen B.P., Prithivirajsingh S., Kurimasa A., Story M.D., Qin J., Chen D.J.
    Genes Dev. 16:2333-2338(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-2609, MUTAGENESIS OF THR-2609, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  32. "Werner protein is a target of DNA-dependent protein kinase in vivo and in vitro, and its catalytic activities are regulated by phosphorylation."
    Karmakar P., Piotrowski J., Brosh R.M. Jr., Sommers J.A., Miller S.P., Cheng W.H., Snowden C.M., Ramsden D.A., Bohr V.A.
    J. Biol. Chem. 277:18291-18302(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION OF WRN.
  33. "Threonines 2638/2647 in DNA-PK are essential for cellular resistance to ionizing radiation."
    Soubeyrand S., Pope L., Pakuts B., Hache R.J.
    Cancer Res. 63:1198-1201(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF THR-2638 AND THR-2647.
  34. "Down-regulation of histone H2B by DNA-dependent protein kinase in response to DNA damage through modulation of octamer transcription factor 1."
    Schild-Poulter C., Shih A., Yarymowich N.C., Hache R.J.G.
    Cancer Res. 63:7197-7205(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION OF POU2F1.
  35. "DNA-PK is activated by nucleosomes and phosphorylates H2AX within the nucleosomes in an acetylation-dependent manner."
    Park E.-J., Chan D.W., Park J.-H., Oettinger M.A., Kwon J.
    Nucleic Acids Res. 31:6819-6827(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION OF H2AFX.
  36. "Functional and biochemical dissection of the structure-specific nuclease ARTEMIS."
    Pannicke U., Ma Y., Hopfner K.-P., Niewolik D., Lieber M.R., Schwarz K.
    EMBO J. 23:1987-1997(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DCLRE1C.
  37. "The metallo-beta-lactamase/beta-CASP domain of Artemis constitutes the catalytic core for V(D)J recombination."
    Poinsignon C., Moshous D., Callebaut I., de Chasseval R., Villey I., de Villartay J.-P.
    J. Exp. Med. 199:315-321(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DCLRE1C.
  38. "A biochemically defined system for mammalian nonhomologous DNA end joining."
    Ma Y., Lu H., Tippin B., Goodman M.F., Shimazaki N., Koiwai O., Hsieh C.-L., Schwarz K., Lieber M.R.
    Mol. Cell 16:701-713(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DCLRE1C.
  39. "Artemis is a phosphorylation target of ATM and ATR and is involved in the G2/M DNA damage checkpoint response."
    Zhang X., Succi J., Feng Z., Prithivirajsingh S., Story M.D., Legerski R.J.
    Mol. Cell. Biol. 24:9207-9220(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DCLRE1C.
  40. "DNA-dependent protein kinase (DNA-PK) phosphorylates nuclear DNA helicase II/RNA helicase A and hnRNP proteins in an RNA-dependent manner."
    Zhang S., Schlott B., Goerlach M., Grosse F.
    Nucleic Acids Res. 32:1-10(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION OF DHX9.
  41. Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-2056 AND THR-2609, DEPHOSPHORYLATION AT SER-2056 AND THR-2609.
  42. "DNA-PK is responsible for enhanced phosphorylation of histone H2AX under hypertonic conditions."
    Reitsema T., Klokov D., Banath J.P., Olive P.L.
    DNA Repair 4:1172-1181(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION OF H2AFX.
  43. "Artemis deficiency confers a DNA double-strand break repair defect and Artemis phosphorylation status is altered by DNA damage and cell cycle progression."
    Wang J., Pluth J.M., Cooper P.K., Cowan M.J., Chen D.J., Yannone S.M.
    DNA Repair 4:556-570(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DCLRE1C.
  44. "The Artemis:DNA-PKcs endonuclease cleaves DNA loops, flaps, and gaps."
    Ma Y., Schwarz K., Lieber M.R.
    DNA Repair 4:845-851(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DCLRE1C.
  45. "Conserved modes of recruitment of ATM, ATR and DNA-PKcs to sites of DNA damage."
    Falck J., Coates J., Jackson S.P.
    Nature 434:605-611(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH XRCC5.
  46. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  47. "XRCC1 is phosphorylated by DNA-dependent protein kinase in response to DNA damage."
    Levy N., Martz A., Bresson A., Spenlehauer C., de Murcia G., Menissier-de Murcia J.
    Nucleic Acids Res. 34:32-41(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION OF XRCC1.
  48. Cited for: REVIEW.
  49. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  50. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3205 AND SER-4026, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  51. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  52. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-893; SER-2612; SER-3205 AND SER-4026, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  53. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  54. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-117; LYS-828; LYS-1209; LYS-1970; LYS-2259; LYS-3241; LYS-3260; LYS-3621; LYS-3638 AND LYS-3642, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  55. "A genetic screen identifies the Triple T complex required for DNA damage signaling and ATM and ATR stability."
    Hurov K.E., Cotta-Ramusino C., Elledge S.J.
    Genes Dev. 24:1939-1950(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TTI1.
  56. "Tel2 structure and function in the Hsp90-dependent maturation of mTOR and ATR complexes."
    Takai H., Xie Y., de Lange T., Pavletich N.P.
    Genes Dev. 24:2019-2030(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TELO2.
  57. "Tti1 and Tel2 are critical factors in mammalian target of rapamycin complex assembly."
    Kaizuka T., Hara T., Oshiro N., Kikkawa U., Yonezawa K., Takehana K., Iemura S., Natsume T., Mizushima N.
    J. Biol. Chem. 285:20109-20116(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TELO2 AND TTI1.
  58. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3205 AND SER-4026, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  59. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  60. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2612 AND SER-3205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  61. "Systematic analysis of protein pools, isoforms, and modifications affecting turnover and subcellular localization."
    Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.
    Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  62. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-6; ASN-263; ILE-333; ILE-420; SER-500; SER-605; LEU-649; SER-695; HIS-1136; VAL-1190; THR-1237; PHE-1279; MET-1447; GLY-1619; VAL-1680; VAL-1680; PRO-2023; GLN-2598; ASN-2810; CYS-2899; ALA-2941; ASP-3085; ASP-3149; SER-3198; SER-3201; GLU-3404; THR-3434; MET-3562; PHE-3584; ILE-3800; LEU-3836; SER-3936 AND MET-3937.

Entry informationi

Entry nameiPRKDC_HUMAN
AccessioniPrimary (citable) accession number: P78527
Secondary accession number(s): P78528
, Q13327, Q13337, Q14175, Q59H99, Q7Z611, Q96SE6, Q9UME3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: October 31, 2003
Last modified: November 26, 2014
This is version 162 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3