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P78527 (PRKDC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA-dependent protein kinase catalytic subunit

Short name=DNA-PK catalytic subunit
Short name=DNA-PKcs
EC=2.7.11.1
Alternative name(s):
DNPK1
p460
Gene names
Name:PRKDC
Synonyms:HYRC, HYRC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length4128 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine-protein kinase that acts as a molecular sensor for DNA damage. Involved in DNA nonhomologous 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. Ref.23 Ref.33 Ref.38 Ref.41

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Inhibited by wortmannin. Activity of the enzyme seems to be attenuated by autophosphorylation. Ref.22

Subunit structure

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. Ref.19 Ref.23 Ref.24 Ref.29 Ref.36 Ref.37 Ref.38 Ref.39 Ref.43 Ref.44 Ref.45 Ref.55 Ref.56 Ref.57

Subcellular location

Nucleus. Nucleusnucleolus Ref.31 Ref.41 Ref.61.

Post-translational modification

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. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.18 Ref.20 Ref.21 Ref.26 Ref.27 Ref.28 Ref.30 Ref.31 Ref.32 Ref.34 Ref.35 Ref.40 Ref.41 Ref.42 Ref.47

S-nitrosylated by GAPDH By similarity.

Sequence similarities

Belongs to the PI3/PI4-kinase family.

Contains 1 FAT domain.

Contains 1 FATC domain.

Contains 2 HEAT repeats.

Contains 1 PI3K/PI4K domain.

Contains 3 TPR repeats.

Ontologies

Keywords
   Biological processDNA damage
DNA recombination
DNA repair
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
TPR repeat
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell lineage commitment

Inferred from electronic annotation. Source: Ensembl

DNA repair

Traceable author statement. Source: Reactome

T cell differentiation in thymus

Inferred from electronic annotation. Source: Ensembl

T cell lineage commitment

Inferred from electronic annotation. Source: Ensembl

T cell receptor V(D)J recombination

Inferred from electronic annotation. Source: Ensembl

brain development

Inferred from electronic annotation. Source: Ensembl

cellular protein modification process

Traceable author statement Ref.1. Source: ProtInc

cellular response to insulin stimulus

Inferred from mutant phenotype PubMed 19303849. Source: BHF-UCL

double-strand break repair

Traceable author statement. Source: Reactome

double-strand break repair via nonhomologous end joining

Traceable author statement. Source: Reactome

ectopic germ cell programmed cell death

Inferred from electronic annotation. Source: Ensembl

heart development

Inferred from electronic annotation. Source: Ensembl

immunoglobulin V(D)J recombination

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from electronic annotation. Source: Ensembl

peptidyl-serine phosphorylation

Inferred from direct assay PubMed 19303849. Source: BHF-UCL

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 19303849. Source: BHF-UCL

positive regulation of type I interferon production

Traceable author statement. Source: Reactome

pro-B cell differentiation

Inferred from electronic annotation. Source: Ensembl

protein destabilization

Inferred from electronic annotation. Source: Ensembl

response to gamma radiation

Inferred from electronic annotation. Source: Ensembl

somitogenesis

Inferred from electronic annotation. Source: Ensembl

telomere maintenance

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentDNA-dependent protein kinase-DNA ligase 4 complex

Inferred from direct assay PubMed 15194694. Source: MGI

cytosol

Traceable author statement. Source: Reactome

nonhomologous end joining complex

Inferred from direct assay PubMed 20383123. Source: UniProtKB

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

transcription factor complex

Inferred from direct assay PubMed 19303849. Source: BHF-UCL

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA-dependent protein kinase activity

Inferred from direct assay PubMed 15194694. Source: MGI

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein kinase activity

Traceable author statement Ref.1. Source: ProtInc

protein serine/threonine kinase activity

Inferred from direct assay PubMed 19303849. Source: BHF-UCL

transcription factor binding

Inferred from physical interaction PubMed 19303849. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P78527-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P78527-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 41284128DNA-dependent protein kinase catalytic subunit
PRO_0000225598

Regions

Repeat288 – 32336HEAT 1
Repeat1004 – 104037HEAT 2
Repeat1723 – 175634TPR 1
Domain2883 – 3539657FAT
Repeat2920 – 294829TPR 2
Repeat2949 – 298234TPR 3
Domain3747 – 4015269PI3K/PI4K
Domain4096 – 412833FATC
Region1503 – 153836Interaction with C1D
Region1503 – 153836Leucine-zipper
Region2436 – 3212777KIP-binding

Sites

Site2020 – 20212Cleavage; by caspase-3 Probable

Amino acid modifications

Modified residue1171N6-acetyllysine Ref.54
Modified residue8281N6-acetyllysine Ref.54
Modified residue8931Phosphoserine Ref.52
Modified residue12091N6-acetyllysine Ref.54
Modified residue19701N6-acetyllysine Ref.54
Modified residue20561Phosphoserine; by autocatalysis Ref.41
Modified residue22591N6-acetyllysine Ref.54
Modified residue26091Phosphothreonine; by autocatalysis Ref.28 Ref.31 Ref.41
Modified residue26121Phosphoserine; by autocatalysis Ref.28 Ref.52 Ref.60
Modified residue26381Phosphothreonine; by autocatalysis Ref.28
Modified residue26471Phosphothreonine; by autocatalysis Ref.28
Modified residue32051Phosphoserine Ref.46 Ref.50 Ref.51 Ref.52 Ref.53 Ref.58 Ref.60
Modified residue32411N6-acetyllysine Ref.54
Modified residue32601N6-acetyllysine Ref.54
Modified residue36211N6-acetyllysine Ref.54
Modified residue36381N6-acetyllysine Ref.54
Modified residue36421N6-acetyllysine Ref.54
Modified residue40261Phosphoserine Ref.50 Ref.52 Ref.58

Natural variations

Alternative sequence3799 – 382931Missing in isoform 2.
VSP_004708
Natural variant61A → S. Ref.3 Ref.62
Corresponds to variant rs8177999 [ dbSNP | Ensembl ].
VAR_019179
Natural variant2631K → N in a lung adenocarcinoma sample; somatic mutation. Ref.62
VAR_041602
Natural variant3331M → I. Ref.3 Ref.62
Corresponds to variant rs8178017 [ dbSNP | Ensembl ].
VAR_019180
Natural variant4201V → I. Ref.62
Corresponds to variant rs55925466 [ dbSNP | Ensembl ].
VAR_041603
Natural variant5001G → S in a metastatic melanoma sample; somatic mutation. Ref.62
VAR_041604
Natural variant6051T → S. Ref.3 Ref.62
Corresponds to variant rs8178033 [ dbSNP | Ensembl ].
VAR_019181
Natural variant6491F → L. Ref.62
Corresponds to variant rs55811715 [ dbSNP | Ensembl ].
VAR_041605
Natural variant6801I → M. Ref.3
Corresponds to variant rs8178040 [ dbSNP | Ensembl ].
VAR_019182
Natural variant6951P → S. Ref.3 Ref.62
Corresponds to variant rs8178046 [ dbSNP | Ensembl ].
VAR_019183
Natural variant10711N → S. Ref.3
Corresponds to variant rs8178070 [ dbSNP | Ensembl ].
VAR_019184
Natural variant11361R → H in a colorectal adenocarcinoma sample; somatic mutation. Ref.62
VAR_041606
Natural variant11901L → V. Ref.62
Corresponds to variant rs34598508 [ dbSNP | Ensembl ].
VAR_041607
Natural variant12371A → T. Ref.62
VAR_041608
Natural variant12791L → F. Ref.62
VAR_041609
Natural variant13141G → V. Ref.3
Corresponds to variant rs8178090 [ dbSNP | Ensembl ].
VAR_019185
Natural variant14471R → M in a lung squamous cell carcinoma sample; somatic mutation. Ref.62
VAR_041610
Natural variant15881D → V. Ref.3
Corresponds to variant rs8178104 [ dbSNP | Ensembl ].
VAR_019186
Natural variant16031Q → H. Ref.3
Corresponds to variant rs8178106 [ dbSNP | Ensembl ].
VAR_019187
Natural variant16191A → G. Ref.62
Corresponds to variant rs56182356 [ dbSNP | Ensembl ].
VAR_041611
Natural variant16801A → V in a metastatic melanoma sample; somatic mutation. Ref.62
Corresponds to variant rs55735910 [ dbSNP | Ensembl ].
VAR_041612
Natural variant20231S → P. Ref.62
Corresponds to variant rs56042895 [ dbSNP | Ensembl ].
VAR_041613
Natural variant20951A → V. Ref.3
Corresponds to variant rs8178147 [ dbSNP | Ensembl ].
VAR_019188
Natural variant25981R → Q. Ref.62
Corresponds to variant rs55923149 [ dbSNP | Ensembl ].
VAR_041614
Natural variant27021K → E. Ref.3
Corresponds to variant rs8178178 [ dbSNP | Ensembl ].
VAR_019189
Natural variant28101S → N in a metastatic melanoma sample; somatic mutation. Ref.62
VAR_041615
Natural variant28991R → C. Ref.3 Ref.62
Corresponds to variant rs4278157 [ dbSNP | Ensembl ].
VAR_019190
Natural variant29411G → A in a lung neuroendocrine carcinoma sample; somatic mutation. Ref.62
VAR_041616
Natural variant30851E → D. Ref.62
Corresponds to variant rs56135402 [ dbSNP | Ensembl ].
VAR_041617
Natural variant31491G → D. Ref.3 Ref.62
Corresponds to variant rs8178208 [ dbSNP | Ensembl ].
VAR_019191
Natural variant31981T → S. Ref.62
Corresponds to variant rs55793951 [ dbSNP | Ensembl ].
VAR_041618
Natural variant32011P → S. Ref.3 Ref.62
Corresponds to variant rs8178216 [ dbSNP | Ensembl ].
VAR_019192
Natural variant34041G → E. Ref.3 Ref.62
Corresponds to variant rs8178225 [ dbSNP | Ensembl ].
VAR_019193
Natural variant34341I → T. Ref.3 Ref.62
Corresponds to variant rs7830743 [ dbSNP | Ensembl ].
VAR_019194
Natural variant34591N → S. Ref.3
Corresponds to variant rs8178228 [ dbSNP | Ensembl ].
VAR_019195
Natural variant35621L → M. Ref.3 Ref.62
Corresponds to variant rs8178232 [ dbSNP | Ensembl ].
VAR_019196
Natural variant35841L → F. Ref.62
VAR_041619
Natural variant37021P → L.
Corresponds to variant rs8178236 [ dbSNP | Ensembl ].
VAR_050534
Natural variant38001L → I. Ref.62
VAR_041620
Natural variant38361P → L. Ref.3 Ref.62
Corresponds to variant rs8178245 [ dbSNP | Ensembl ].
VAR_019197
Natural variant39321M → V. Ref.3
VAR_019198
Natural variant39361G → S. Ref.62
VAR_041621
Natural variant39371V → M. Ref.62
VAR_041622

Experimental info

Mutagenesis15101L → P: Loss of interaction with C1D. Ref.23
Mutagenesis1516 – 15172EL → PD: Loss of interaction with C1D.
Mutagenesis26091T → A: Leads to radiation sensitivity and impaired DSB joining. Gives rise to reduced phosphorylation; when associated with A-2612. Ref.31
Mutagenesis26121S → A: Reduced phosphorylation; when associated with A-2609.
Mutagenesis26381T → 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. Ref.33
Mutagenesis26471T → 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. Ref.33
Sequence conflict4051D → Y in AAC50210. Ref.2
Sequence conflict10081A → S in AAC50210. Ref.2
Sequence conflict36601N → T in AAA79184. Ref.8
Sequence conflict38171L → W in AAA79184. Ref.8
Sequence conflict38621A → P in AAA79184. Ref.8
Sequence conflict40311I → V in AAK40350. Ref.9

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 31, 2003. Version 3.
Checksum: AC6E747FEB09F3E5

FASTA4,128469,089
        10         20         30         40         50         60 
MAGSGAGVRC SLLRLQETLS AADRCGAALA GHQLIRGLGQ ECVLSSSPAV LALQTSLVFS 

        70         80         90        100        110        120 
RDFGLLVFVR KSLNSIEFRE CREEILKFLC IFLEKMGQKI APYSVEIKNT CTSVYTKDRA 

       130        140        150        160        170        180 
AKCKIPALDL LIKLLQTFRS SRLMDEFKIG ELFSKFYGEL ALKKKIPDTV LEKVYELLGL 

       190        200        210        220        230        240 
LGEVHPSEMI NNAENLFRAF LGELKTQMTS AVREPKLPVL AGCLKGLSSL LCNFTKSMEE 

       250        260        270        280        290        300 
DPQTSREIFN FVLKAIRPQI DLKRYAVPSA GLRLFALHAS QFSTCLLDNY VSLFEVLLKW 

       310        320        330        340        350        360 
CAHTNVELKK AALSALESFL KQVSNMVAKN AEMHKNKLQY FMEQFYGIIR NVDSNNKELS 

       370        380        390        400        410        420 
IAIRGYGLFA GPCKVINAKD VDFMYVELIQ RCKQMFLTQT DTGDDRVYQM PSFLQSVASV 

       430        440        450        460        470        480 
LLYLDTVPEV YTPVLEHLVV MQIDSFPQYS PKMQLVCCRA IVKVFLALAA KGPVLRNCIS 

       490        500        510        520        530        540 
TVVHQGLIRI CSKPVVLPKG PESESEDHRA SGEVRTGKWK VPTYKDYVDL FRHLLSSDQM 

       550        560        570        580        590        600 
MDSILADEAF FSVNSSSESL NHLLYDEFVK SVLKIVEKLD LTLEIQTVGE QENGDEAPGV 

       610        620        630        640        650        660 
WMIPTSDPAA NLHPAKPKDF SAFINLVEFC REILPEKQAE FFEPWVYSFS YELILQSTRL 

       670        680        690        700        710        720 
PLISGFYKLL SITVRNAKKI KYFEGVSPKS LKHSPEDPEK YSCFALFVKF GKEVAVKMKQ 

       730        740        750        760        770        780 
YKDELLASCL TFLLSLPHNI IELDVRAYVP ALQMAFKLGL SYTPLAEVGL NALEEWSIYI 

       790        800        810        820        830        840 
DRHVMQPYYK DILPCLDGYL KTSALSDETK NNWEVSALSR AAQKGFNKVV LKHLKKTKNL 

       850        860        870        880        890        900 
SSNEAISLEE IRIRVVQMLG SLGGQINKNL LTVTSSDEMM KSYVAWDREK RLSFAVPFRE 

       910        920        930        940        950        960 
MKPVIFLDVF LPRVTELALT ASDRQTKVAA CELLHSMVMF MLGKATQMPE GGQGAPPMYQ 

       970        980        990       1000       1010       1020 
LYKRTFPVLL RLACDVDQVT RQLYEPLVMQ LIHWFTNNKK FESQDTVALL EAILDGIVDP 

      1030       1040       1050       1060       1070       1080 
VDSTLRDFCG RCIREFLKWS IKQITPQQQE KSPVNTKSLF KRLYSLALHP NAFKRLGASL 

      1090       1100       1110       1120       1130       1140 
AFNNIYREFR EEESLVEQFV FEALVIYMES LALAHADEKS LGTIQQCCDA IDHLCRIIEK 

      1150       1160       1170       1180       1190       1200 
KHVSLNKAKK RRLPRGFPPS ASLCLLDLVK WLLAHCGRPQ TECRHKSIEL FYKFVPLLPG 

      1210       1220       1230       1240       1250       1260 
NRSPNLWLKD VLKEEGVSFL INTFEGGGCG QPSGILAQPT LLYLRGPFSL QATLCWLDLL 

      1270       1280       1290       1300       1310       1320 
LAALECYNTF IGERTVGALQ VLGTEAQSSL LKAVAFFLES IAMHDIIAAE KCFGTGAAGN 

      1330       1340       1350       1360       1370       1380 
RTSPQEGERY NYSKCTVVVR IMEFTTTLLN TSPEGWKLLK KDLCNTHLMR VLVQTLCEPA 

      1390       1400       1410       1420       1430       1440 
SIGFNIGDVQ VMAHLPDVCV NLMKALKMSP YKDILETHLR EKITAQSIEE LCAVNLYGPD 

      1450       1460       1470       1480       1490       1500 
AQVDRSRLAA VVSACKQLHR AGLLHNILPS QSTDLHHSVG TELLSLVYKG IAPGDERQCL 

      1510       1520       1530       1540       1550       1560 
PSLDLSCKQL ASGLLELAFA FGGLCERLVS LLLNPAVLST ASLGSSQGSV IHFSHGEYFY 

      1570       1580       1590       1600       1610       1620 
SLFSETINTE LLKNLDLAVL ELMQSSVDNT KMVSAVLNGM LDQSFRERAN QKHQGLKLAT 

      1630       1640       1650       1660       1670       1680 
TILQHWKKCD SWWAKDSPLE TKMAVLALLA KILQIDSSVS FNTSHGSFPE VFTTYISLLA 

      1690       1700       1710       1720       1730       1740 
DTKLDLHLKG QAVTLLPFFT SLTGGSLEEL RRVLEQLIVA HFPMQSREFP PGTPRFNNYV 

      1750       1760       1770       1780       1790       1800 
DCMKKFLDAL ELSQSPMLLE LMTEVLCREQ QHVMEELFQS SFRRIARRGS CVTQVGLLES 

      1810       1820       1830       1840       1850       1860 
VYEMFRKDDP RLSFTRQSFV DRSLLTLLWH CSLDALREFF STIVVDAIDV LKSRFTKLNE 

      1870       1880       1890       1900       1910       1920 
STFDTQITKK MGYYKILDVM YSRLPKDDVH AKESKINQVF HGSCITEGNE LTKTLIKLCY 

      1930       1940       1950       1960       1970       1980 
DAFTENMAGE NQLLERRRLY HCAAYNCAIS VICCVFNELK FYQGFLFSEK PEKNLLIFEN 

      1990       2000       2010       2020       2030       2040 
LIDLKRRYNF PVEVEVPMER KKKYIEIRKE AREAANGDSD GPSYMSSLSY LADSTLSEEM 

      2050       2060       2070       2080       2090       2100 
SQFDFSTGVQ SYSYSSQDPR PATGRFRRRE QRDPTVHDDV LELEMDELNR HECMAPLTAL 

      2110       2120       2130       2140       2150       2160 
VKHMHRSLGP PQGEEDSVPR DLPSWMKFLH GKLGNPIVPL NIRLFLAKLV INTEEVFRPY 

      2170       2180       2190       2200       2210       2220 
AKHWLSPLLQ LAASENNGGE GIHYMVVEIV ATILSWTGLA TPTGVPKDEV LANRLLNFLM 

      2230       2240       2250       2260       2270       2280 
KHVFHPKRAV FRHNLEIIKT LVECWKDCLS IPYRLIFEKF SGKDPNSKDN SVGIQLLGIV 

      2290       2300       2310       2320       2330       2340 
MANDLPPYDP QCGIQSSEYF QALVNNMSFV RYKEVYAAAA EVLGLILRYV MERKNILEES 

      2350       2360       2370       2380       2390       2400 
LCELVAKQLK QHQNTMEDKF IVCLNKVTKS FPPLADRFMN AVFFLLPKFH GVLKTLCLEV 

      2410       2420       2430       2440       2450       2460 
VLCRVEGMTE LYFQLKSKDF VQVMRHRDDE RQKVCLDIIY KMMPKLKPVE LRELLNPVVE 

      2470       2480       2490       2500       2510       2520 
FVSHPSTTCR EQMYNILMWI HDNYRDPESE TDNDSQEIFK LAKDVLIQGL IDENPGLQLI 

      2530       2540       2550       2560       2570       2580 
IRNFWSHETR LPSNTLDRLL ALNSLYSPKI EVHFLSLATN FLLEMTSMSP DYPNPMFEHP 

      2590       2600       2610       2620       2630       2640 
LSECEFQEYT IDSDWRFRST VLTPMFVETQ ASQGTLQTRT QEGSLSARWP VAGQIRATQQ 

      2650       2660       2670       2680       2690       2700 
QHDFTLTQTA DGRSSFDWLT GSSTDPLVDH TSPSSDSLLF AHKRSERLQR APLKSVGPDF 

      2710       2720       2730       2740       2750       2760 
GKKRLGLPGD EVDNKVKGAA GRTDLLRLRR RFMRDQEKLS LMYARKGVAE QKREKEIKSE 

      2770       2780       2790       2800       2810       2820 
LKMKQDAQVV LYRSYRHGDL PDIQIKHSSL ITPLQAVAQR DPIIAKQLFS SLFSGILKEM 

      2830       2840       2850       2860       2870       2880 
DKFKTLSEKN NITQKLLQDF NRFLNTTFSF FPPFVSCIQD ISCQHAALLS LDPAAVSAGC 

      2890       2900       2910       2920       2930       2940 
LASLQQPVGI RLLEEALLRL LPAELPAKRV RGKARLPPDV LRWVELAKLY RSIGEYDVLR 

      2950       2960       2970       2980       2990       3000 
GIFTSEIGTK QITQSALLAE ARSDYSEAAK QYDEALNKQD WVDGEPTEAE KDFWELASLD 

      3010       3020       3030       3040       3050       3060 
CYNHLAEWKS LEYCSTASID SENPPDLNKI WSEPFYQETY LPYMIRSKLK LLLQGEADQS 

      3070       3080       3090       3100       3110       3120 
LLTFIDKAMH GELQKAILEL HYSQELSLLY LLQDDVDRAK YYIQNGIQSF MQNYSSIDVL 

      3130       3140       3150       3160       3170       3180 
LHQSRLTKLQ SVQALTEIQE FISFISKQGN LSSQVPLKRL LNTWTNRYPD AKMDPMNIWD 

      3190       3200       3210       3220       3230       3240 
DIITNRCFFL SKIEEKLTPL PEDNSMNVDQ DGDPSDRMEV QEQEEDISSL IRSCKFSMKM 

      3250       3260       3270       3280       3290       3300 
KMIDSARKQN NFSLAMKLLK ELHKESKTRD DWLVSWVQSY CRLSHCRSRS QGCSEQVLTV 

      3310       3320       3330       3340       3350       3360 
LKTVSLLDEN NVSSYLSKNI LAFRDQNILL GTTYRIIANA LSSEPACLAE IEEDKARRIL 

      3370       3380       3390       3400       3410       3420 
ELSGSSSEDS EKVIAGLYQR AFQHLSEAVQ AAEEEAQPPS WSCGPAAGVI DAYMTLADFC 

      3430       3440       3450       3460       3470       3480 
DQQLRKEEEN ASVIDSAELQ AYPALVVEKM LKALKLNSNE ARLKFPRLLQ IIERYPEETL 

      3490       3500       3510       3520       3530       3540 
SLMTKEISSV PCWQFISWIS HMVALLDKDQ AVAVQHSVEE ITDNYPQAIV YPFIISSESY 

      3550       3560       3570       3580       3590       3600 
SFKDTSTGHK NKEFVARIKS KLDQGGVIQD FINALDQLSN PELLFKDWSN DVRAELAKTP 

      3610       3620       3630       3640       3650       3660 
VNKKNIEKMY ERMYAALGDP KAPGLGAFRR KFIQTFGKEF DKHFGKGGSK LLRMKLSDFN 

      3670       3680       3690       3700       3710       3720 
DITNMLLLKM NKDSKPPGNL KECSPWMSDF KVEFLRNELE IPGQYDGRGK PLPEYHVRIA 

      3730       3740       3750       3760       3770       3780 
GFDERVTVMA SLRRPKRIII RGHDEREHPF LVKGGEDLRQ DQRVEQLFQV MNGILAQDSA 

      3790       3800       3810       3820       3830       3840 
CSQRALQLRT YSVVPMTSRL GLIEWLENTV TLKDLLLNTM SQEEKAAYLS DPRAPPCEYK 

      3850       3860       3870       3880       3890       3900 
DWLTKMSGKH DVGAYMLMYK GANRTETVTS FRKRESKVPA DLLKRAFVRM STSPEAFLAL 

      3910       3920       3930       3940       3950       3960 
RSHFASSHAL ICISHWILGI GDRHLNNFMV AMETGGVIGI DFGHAFGSAT QFLPVPELMP 

      3970       3980       3990       4000       4010       4020 
FRLTRQFINL MLPMKETGLM YSIMVHALRA FRSDPGLLTN TMDVFVKEPS FDWKNFEQKM 

      4030       4040       4050       4060       4070       4080 
LKKGGSWIQE INVAEKNWYP RQKICYAKRK LAGANPAVIT CDELLLGHEK APAFRDYVAV 

      4090       4100       4110       4120 
ARGSKDHNIR AQEPESGLSE ETQVKCLMDQ ATDPNILGRT WEGWEPWM 

« Hide

Isoform 2 [UniParc].

Checksum: B698F749065D319B
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FASTA4,097465,501

References

« Hide 'large scale' references
[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]"DNA-PKcs function regulated specifically by protein phosphatase 5."
Wechsler T., Chen B.P., Harper R., Morotomi-Yano K., Huang B.C., Meek K., Cleaver J.E., Chen D.J., Wabl M.
Proc. Natl. Acad. Sci. U.S.A. 101:1247-1252(2004) [PubMed] [Europe PMC] [Abstract]
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]"The life and death of DNA-PK."
Collis S.J., DeWeese T.L., Jeggo P.A., Parker A.R.
Oncogene 24:949-961(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[49]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[52]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA57099.
G02083.
RefSeqNP_001075109.1. NM_001081640.1.
NP_008835.5. NM_006904.6.
UniGeneHs.491682.

3D structure databases

ProteinModelPortalP78527.
SMRP78527. Positions 3724-3998, 4097-4127.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111577. 217 interactions.
DIPDIP-24186N.
IntActP78527. 68 interactions.
MINTMINT-5006046.

Chemistry

BindingDBP78527.
ChEMBLCHEMBL3142.

PTM databases

PhosphoSiteP78527.

Polymorphism databases

DMDM38258929.

2D gel databases

SWISS-2DPAGEP78527.

Proteomic databases

PaxDbP78527.
PRIDEP78527.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000314191; ENSP00000313420; ENSG00000253729.
GeneID5591.
KEGGhsa:5591.
UCSCuc003xqi.3. human. [P78527-1]
uc003xqj.3. human. [P78527-2]

Organism-specific databases

CTD5591.
GeneCardsGC08M048685.
HGNCHGNC:9413. PRKDC.
HPACAB005167.
HPA035174.
MIM600899. gene.
neXtProtNX_P78527.
Orphanet317425. Severe combined immunodeficiency due to DNA-PKcs deficiency.
PharmGKBPA33776.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5032.
HOVERGENHBG053681.
InParanoidP78527.
KOK06642.
OrthoDBEOG7DNNT7.
PhylomeDBP78527.
TreeFamTF324494.

Enzyme and pathway databases

ReactomeREACT_216. DNA Repair.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP78527.
BgeeP78527.
GenevestigatorP78527.

Family and domain databases

Gene3D1.10.1070.11. 3 hits.
1.25.10.10. 3 hits.
InterProIPR011989. 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]
PfamPF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF08163. NUC194. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
[Graphical view]
SMARTSM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 8 hits.
SSF56112. SSF56112. 2 hits.
PROSITEPS51189. 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]
ProtoNetSearch...

Other

ChiTaRSPRKDC. human.
GeneWikiDNA-PKcs.
GenomeRNAi5591.
NextBio21692.
PROP78527.
SOURCESearch...

Entry information

Entry namePRKDC_HUMAN
AccessionPrimary (citable) accession number: P78527
Secondary accession number(s): P78528 expand/collapse secondary AC list , Q13327, Q13337, Q14175, Q59H99, Q7Z611, Q96SE6, Q9UME3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: October 31, 2003
Last modified: April 16, 2014
This is version 155 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM