P78527 (PRKDC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	4128 AA.
Sequence status	Complete.
Protein existence	Evidence 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
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. Ref.23 Ref.24 Ref.29 Ref.36 Ref.37 Ref.38 Ref.39 Ref.42 Ref.43 Ref.44 Ref.54 Ref.55 Ref.56
Subcellular location	Nucleus. Nucleus › nucleolus Ref.31 Ref.60.
Post-translational modification	Autophosphorylated on Thr-2609, Thr-2638 and Thr-2647. Thr-2609 is a DNA damage-inducible phosphorylation site (inducible with ionizing radiation, IR). 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.46 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 process	DNA damage DNA recombination DNA repair
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat TPR repeat
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein S-nitrosylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B cell lineage commitment Inferred from electronic annotation. Source: Compara T cell differentiation in thymus Inferred from electronic annotation. Source: Compara T cell lineage commitment Inferred from electronic annotation. Source: Compara T cell receptor V(D)J recombination Inferred from electronic annotation. Source: Compara apoptotic process Inferred from electronic annotation. Source: Compara brain development Inferred from electronic annotation. Source: Compara cellular response to insulin stimulus Inferred from mutant phenotype PubMed 19303849. Source: BHF-UCL double-strand break repair via nonhomologous end joining Traceable author statement. Source: Reactome germ cell programmed cell death Inferred from electronic annotation. Source: Compara heart development Inferred from electronic annotation. Source: Compara immunoglobulin V(D)J recombination Inferred from electronic annotation. Source: Compara peptidyl-serine phosphorylation Inferred from direct assay PubMed 19303849. Source: BHF-UCL positive regulation of apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 19303849. Source: BHF-UCL pro-B cell differentiation Inferred from electronic annotation. Source: Compara protein destabilization Inferred from electronic annotation. Source: Compara response to gamma radiation Inferred from electronic annotation. Source: Compara somitogenesis Inferred from electronic annotation. Source: Compara telomere maintenance Inferred from electronic annotation. Source: Compara
Cellular_component	DNA-dependent protein kinase-DNA ligase 4 complex Inferred from direct assay PubMed 15194694. Source: MGI nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell transcription factor complex Inferred from direct assay PubMed 19303849. Source: BHF-UCL
Molecular_function	ATP 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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AIRE	O43918	2	EBI-352053,EBI-1753081
CASP2	P42575	4	EBI-352053,EBI-520342
ETS1	P14921	2	EBI-352053,EBI-913209
ETV1	P50549	2	EBI-352053,EBI-3905068
HOXB7	P09629	2	EBI-352053,EBI-1248457
PIDD	Q9HB75	6	EBI-352053,EBI-520427
SPI1	P17947	2	EBI-352053,EBI-2293548
XRCC5	P13010	6	EBI-352053,EBI-357997
XRCC6	P12956	5	EBI-352053,EBI-353208
YY1	P25490	2	EBI-352053,EBI-765538

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 4128	4128	DNA-dependent protein kinase catalytic subunit		PRO_0000225598
Regions
	Repeat	288 – 323	36	HEAT 1
	Repeat	1004 – 1040	37	HEAT 2
	Repeat	1723 – 1756	34	TPR 1
	Domain	2883 – 3539	657	FAT
	Repeat	2920 – 2948	29	TPR 2
	Repeat	2949 – 2982	34	TPR 3
	Domain	3747 – 4015	269	PI3K/PI4K
	Domain	4096 – 4128	33	FATC
	Region	1503 – 1538	36	Interaction with C1D
	Region	1503 – 1538	36	Leucine-zipper
	Region	2436 – 3212	777	KIP-binding
Sites
	Site	2020 – 2021	2	Cleavage; by caspase-3 Probable
Amino acid modifications
	Modified residue	117	1	N6-acetyllysine Ref.53
	Modified residue	828	1	N6-acetyllysine Ref.53
	Modified residue	893	1	Phosphoserine Ref.51
	Modified residue	1209	1	N6-acetyllysine Ref.53
	Modified residue	1970	1	N6-acetyllysine Ref.53
	Modified residue	2259	1	N6-acetyllysine Ref.53
	Modified residue	2609	1	Phosphothreonine; by autocatalysis Ref.28 Ref.31
	Modified residue	2612	1	Phosphoserine; by autocatalysis Ref.28 Ref.51 Ref.59
	Modified residue	2638	1	Phosphothreonine; by autocatalysis Ref.28
	Modified residue	2647	1	Phosphothreonine; by autocatalysis Ref.28
	Modified residue	3205	1	Phosphoserine Ref.45 Ref.49 Ref.50 Ref.51 Ref.52 Ref.57 Ref.59
	Modified residue	3241	1	N6-acetyllysine Ref.53
	Modified residue	3260	1	N6-acetyllysine Ref.53
	Modified residue	3621	1	N6-acetyllysine Ref.53
	Modified residue	3638	1	N6-acetyllysine Ref.53
	Modified residue	3642	1	N6-acetyllysine Ref.53
	Modified residue	4026	1	Phosphoserine Ref.49 Ref.51 Ref.57
Natural variations
	Alternative sequence	3799 – 3829	31	Missing in isoform 2.		VSP_004708
	Natural variant	6	1	A → S. Ref.3 Ref.61 Corresponds to variant rs8177999 [ dbSNP | Ensembl ].		VAR_019179
	Natural variant	263	1	K → N in a lung adenocarcinoma sample; somatic mutation. Ref.61		VAR_041602
	Natural variant	333	1	M → I. Ref.3 Ref.61 Corresponds to variant rs8178017 [ dbSNP | Ensembl ].		VAR_019180
	Natural variant	420	1	V → I. Ref.61 Corresponds to variant rs55925466 [ dbSNP | Ensembl ].		VAR_041603
	Natural variant	500	1	G → S in a metastatic melanoma sample; somatic mutation. Ref.61		VAR_041604
	Natural variant	605	1	T → S. Ref.3 Ref.61 Corresponds to variant rs8178033 [ dbSNP | Ensembl ].		VAR_019181
	Natural variant	649	1	F → L. Ref.61 Corresponds to variant rs55811715 [ dbSNP | Ensembl ].		VAR_041605
	Natural variant	680	1	I → M. Ref.3 Corresponds to variant rs8178040 [ dbSNP | Ensembl ].		VAR_019182
	Natural variant	695	1	P → S. Ref.3 Ref.61 Corresponds to variant rs8178046 [ dbSNP | Ensembl ].		VAR_019183
	Natural variant	1071	1	N → S. Ref.3 Corresponds to variant rs8178070 [ dbSNP | Ensembl ].		VAR_019184
	Natural variant	1136	1	R → H in a colorectal adenocarcinoma sample; somatic mutation. Ref.61		VAR_041606
	Natural variant	1190	1	L → V. Ref.61 Corresponds to variant rs34598508 [ dbSNP | Ensembl ].		VAR_041607
	Natural variant	1237	1	A → T. Ref.61		VAR_041608
	Natural variant	1279	1	L → F. Ref.61		VAR_041609
	Natural variant	1314	1	G → V. Ref.3 Corresponds to variant rs8178090 [ dbSNP | Ensembl ].		VAR_019185
	Natural variant	1447	1	R → M in a lung squamous cell carcinoma sample; somatic mutation. Ref.61		VAR_041610
	Natural variant	1588	1	D → V. Ref.3 Corresponds to variant rs8178104 [ dbSNP | Ensembl ].		VAR_019186
	Natural variant	1603	1	Q → H. Ref.3 Corresponds to variant rs8178106 [ dbSNP | Ensembl ].		VAR_019187
	Natural variant	1619	1	A → G. Ref.61 Corresponds to variant rs56182356 [ dbSNP | Ensembl ].		VAR_041611
	Natural variant	1680	1	A → V in a metastatic melanoma sample; somatic mutation. Ref.61 Corresponds to variant rs55735910 [ dbSNP | Ensembl ].		VAR_041612
	Natural variant	2023	1	S → P. Ref.61 Corresponds to variant rs56042895 [ dbSNP | Ensembl ].		VAR_041613
	Natural variant	2095	1	A → V. Ref.3 Corresponds to variant rs8178147 [ dbSNP | Ensembl ].		VAR_019188
	Natural variant	2598	1	R → Q. Ref.61 Corresponds to variant rs55923149 [ dbSNP | Ensembl ].		VAR_041614
	Natural variant	2702	1	K → E. Ref.3 Corresponds to variant rs8178178 [ dbSNP | Ensembl ].		VAR_019189
	Natural variant	2810	1	S → N in a metastatic melanoma sample; somatic mutation. Ref.61		VAR_041615
	Natural variant	2899	1	R → C. Ref.3 Ref.61 Corresponds to variant rs4278157 [ dbSNP | Ensembl ].		VAR_019190
	Natural variant	2941	1	G → A in a lung neuroendocrine carcinoma sample; somatic mutation. Ref.61		VAR_041616
	Natural variant	3085	1	E → D. Ref.61 Corresponds to variant rs56135402 [ dbSNP | Ensembl ].		VAR_041617
	Natural variant	3149	1	G → D. Ref.3 Ref.61 Corresponds to variant rs8178208 [ dbSNP | Ensembl ].		VAR_019191
	Natural variant	3198	1	T → S. Ref.61 Corresponds to variant rs55793951 [ dbSNP | Ensembl ].		VAR_041618
	Natural variant	3201	1	P → S. Ref.3 Ref.61 Corresponds to variant rs8178216 [ dbSNP | Ensembl ].		VAR_019192
	Natural variant	3404	1	G → E. Ref.3 Ref.61 Corresponds to variant rs8178225 [ dbSNP | Ensembl ].		VAR_019193
	Natural variant	3434	1	I → T. Ref.3 Ref.61 Corresponds to variant rs7830743 [ dbSNP | Ensembl ].		VAR_019194
	Natural variant	3459	1	N → S. Ref.3 Corresponds to variant rs8178228 [ dbSNP | Ensembl ].		VAR_019195
	Natural variant	3562	1	L → M. Ref.3 Ref.61 Corresponds to variant rs8178232 [ dbSNP | Ensembl ].		VAR_019196
	Natural variant	3584	1	L → F. Ref.61		VAR_041619
	Natural variant	3702	1	P → L. Corresponds to variant rs8178236 [ dbSNP | Ensembl ].		VAR_050534
	Natural variant	3800	1	L → I. Ref.61		VAR_041620
	Natural variant	3836	1	P → L. Ref.3 Ref.61 Corresponds to variant rs8178245 [ dbSNP | Ensembl ].		VAR_019197
	Natural variant	3932	1	M → V. Ref.3		VAR_019198
	Natural variant	3936	1	G → S. Ref.61		VAR_041621
	Natural variant	3937	1	V → M. Ref.61		VAR_041622
Experimental info
	Mutagenesis	1510	1	L → P: Loss of interaction with C1D. Ref.23
	Mutagenesis	1516 – 1517	2	EL → PD: Loss of interaction with C1D.
	Mutagenesis	2609	1	T → A: Leads to radiation sensitivity and impaired DSB joining. Gives rise to reduced phosphorylation; when associated with A-2612. Ref.31
	Mutagenesis	2612	1	S → A: Reduced phosphorylation; when associated with A-2609.
	Mutagenesis	2638	1	T → 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
	Mutagenesis	2647	1	T → 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 conflict	405	1	D → Y in AAC50210. Ref.2
	Sequence conflict	1008	1	A → S in AAC50210. Ref.2
	Sequence conflict	3660	1	N → T Ref.8
	Sequence conflict	3817	1	L → W Ref.8
	Sequence conflict	3862	1	A → P Ref.8
	Sequence conflict	4031	1	I → V Ref.9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 31, 2003. Version 3. Checksum: AC6E747FEB09F3E5	FASTA	4,128	469,089
	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
	Isoform 2 [UniParc]. Checksum: B698F749065D319B	FASTA	4,097	465,501
	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 YSVVPMTSSD PRAPPCEYKD WLTKMSGKHD VGAYMLMYKG ANRTETVTSF 3850 3860 3870 3880 3890 3900 RKRESKVPAD LLKRAFVRMS TSPEAFLALR SHFASSHALI CISHWILGIG DRHLNNFMVA 3910 3920 3930 3940 3950 3960 METGGVIGID FGHAFGSATQ FLPVPELMPF RLTRQFINLM LPMKETGLMY SIMVHALRAF 3970 3980 3990 4000 4010 4020 RSDPGLLTNT MDVFVKEPSF DWKNFEQKML KKGGSWIQEI NVAEKNWYPR QKICYAKRKL 4030 4040 4050 4060 4070 4080 AGANPAVITC DELLLGHEKA PAFRDYVAVA RGSKDHNIRA QEPESGLSEE TQVKCLMDQA 4090 TDPNILGRTW EGWEPWM

References

	« Hide 'large scale' referencesShow 'large scale' references »
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[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.
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[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: MASS SPECTROMETRY, PHOSPHORYLATION AT THR-2609, MUTAGENESIS OF THR-2609, SUBCELLULAR LOCATION.
[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.
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[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.
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[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-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.
[42]	"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.
[43]	"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.
[44]	"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.
[45]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[46]	"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.
[47]	"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.
[48]	"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.
[49]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[50]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[51]	"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, MASS SPECTROMETRY.
[52]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[53]	"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, MASS SPECTROMETRY.
[54]	"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.
[55]	"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.
[56]	"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.
[57]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[58]	"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].
[59]	"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, MASS SPECTROMETRY.
[60]	"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].
[61]	"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.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

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.
IPI	IPI00296337. IPI00376215.
PIR	A57099. G02083.
RefSeq	NP_001075109.1. NM_001081640.1. NP_008835.5. NM_006904.6.
UniGene	Hs.491682.
3D structure databases
ProteinModelPortal	P78527.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-24186N.
IntAct	P78527. 54 interactions.
MINT	MINT-5006046.
PTM databases
PhosphoSite	P78527.
Polymorphism databases
DMDM	38258929.
2D gel databases
SWISS-2DPAGE	P78527.
Proteomic databases
PaxDb	P78527.
PRIDE	P78527.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000314191; ENSP00000313420; ENSG00000253729.
GeneID	5591.
KEGG	hsa:5591.
UCSC	uc003xqi.3. human. uc003xqj.3. human.
Organism-specific databases
CTD	5591.
GeneCards	GC08M048685.
HGNC	HGNC:9413. PRKDC.
HPA	CAB005167.
MIM	600899. gene.
neXtProt	NX_P78527.
PharmGKB	PA33776.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5032.
HOVERGEN	HBG053681.
InParanoid	P78527.
KO	K06642.
Enzyme and pathway databases
Pathway_Interaction_DB	bard1pathway. BARD1 signaling events. pi3kciaktpathway. Class I PI3K signaling events mediated by Akt. ar_pathway. Coregulation of Androgen receptor activity. faspathway. FAS signaling pathway (CD95).
Reactome	REACT_216. DNA Repair.
Gene expression databases
ArrayExpress	P78527.
Bgee	P78527.
Genevestigator	P78527.
GermOnline	ENSG00000121031. Homo sapiens.
Family and domain databases
Gene3D	1.10.1070.11. 3 hits. 1.25.10.10. 3 hits.
InterPro	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]
Pfam	PF02259. FAT. 1 hit. PF02260. FATC. 1 hit. PF08163. NUC194. 1 hit. PF00454. PI3_PI4_kinase. 1 hit. [Graphical view]
SMART	SM00146. PI3Kc. 1 hit. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 3 hits. SSF56112. Kinase_like. 1 hit.
PROSITE	PS51189. FAT. 1 hit. PS51190. FATC. 1 hit. PS50077. HEAT_REPEAT. False negative. PS00915. PI3_4_KINASE_1. 1 hit. PS00916. PI3_4_KINASE_2. 1 hit. PS50290. PI3_4_KINASE_3. 1 hit. PS50005. TPR. False negative. PS50293. TPR_REGION. False negative. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P78527.
ChEMBL	CHEMBL3142.
ChiTaRS	PRKDC. human.
GenomeRNAi	5591.
NextBio	21692.
SOURCE	Search...

Entry information

Entry name

PRKDC_HUMAN

Accession

Primary (citable) accession number: P78527
Secondary accession number(s): P78528 , 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:	May 1, 2013
This is version 145 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.