P97313 (PRKDC_MOUSE) 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):
p460

Gene names

Name:	Prkdc
Synonyms:	Xrcc7

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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, C1D, c-Abl/ABL1, histone H1, HSPCA, c-jun/JUN, p53/TP53, PARP1, POU2F1, DHX9, SRF, 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 By similarity. Ref.12
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Inhibited by wortmannin. Activity of the enzyme seems to be attenuated by autophosphorylation By similarity.
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 By similarity. Interacts with TTI1 and TELO2 By similarity.
Subcellular location	Nucleus. Nucleus › nucleolus By similarity.
Post-translational modification	Autophosphorylated on Thr-2605, Thr-2634 and Thr-2643. Thr-2605 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 By similarity. Ref.11 S-nitrosylated by GAPDH.
Involvement in disease	Defects in Prkdc are the cause of severe combined immune deficiency (SCID) which is characterized by a lack of mature functional lymphocytes and a high susceptibility to lethal opportunistic infections if not chronically treated with antibiotics. The lack of B- and T-cell immunity resembles severe combined immunodeficiency syndrome in human infants. Ref.1
Sequence similarities	Belongs to the PI3/PI4-kinase family. Contains 1 FAT domain. Contains 1 FATC domain. Contains 3 HEAT repeats. Contains 1 PI3K/PI4K domain. Contains 3 TPR repeats.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation SCID
Domain	Repeat TPR repeat
Ligand	ATP-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 mutant phenotype PubMed 8788039. Source: MGI T cell differentiation in thymus Inferred from mutant phenotype PubMed 9768755. Source: MGI T cell lineage commitment Inferred from mutant phenotype PubMed 8788039. Source: MGI T cell receptor V(D)J recombination Inferred from mutant phenotype PubMed 9768755. Source: MGI apoptotic process Inferred from mutant phenotype PubMed 12604618. Source: MGI brain development Inferred from genetic interaction PubMed 16687486. Source: MGI cellular response to insulin stimulus Inferred from electronic annotation. Source: Compara double-strand break repair Inferred from mutant phenotype PubMed 11751629PubMed 12604618. Source: MGI double-strand break repair via nonhomologous end joining Inferred from electronic annotation. Source: InterPro germ cell programmed cell death Inferred from mutant phenotype PubMed 17145779. Source: MGI heart development Inferred from genetic interaction PubMed 16687486. Source: MGI immunoglobulin V(D)J recombination Inferred from mutant phenotype PubMed 9768755. Source: MGI peptidyl-serine phosphorylation Inferred from electronic annotation. Source: Compara positive regulation of apoptotic process Inferred from mutant phenotype PubMed 17145779. Source: MGI positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara pro-B cell differentiation Inferred from mutant phenotype PubMed 9768755. Source: MGI protein destabilization Inferred from direct assay PubMed 15194694. Source: MGI response to gamma radiation Inferred from mutant phenotype PubMed 9768755. Source: MGI somitogenesis Inferred from genetic interaction PubMed 16687486. Source: MGI telomere maintenance Inferred from mutant phenotype PubMed 15010310. Source: MGI
Cellular_component	DNA-dependent protein kinase-DNA ligase 4 complex Inferred from electronic annotation. Source: Compara nonhomologous end joining complex Inferred from sequence or structural similarity. Source: UniProtKB nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay PubMed 12604618. Source: MGI transcription factor complex Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Inferred from electronic annotation. Source: InterPro DNA-dependent protein kinase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: A number of isoforms are produced.

Isoform 1 (identifier: P97313-1)

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: P97313-2)

The sequence of this isoform differs from the canonical sequence as follows:
     842-852: DEALSLEEIRI → VRNPFLILYLK
     853-4128: Missing.

Note: No experimental confirmation available.

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_0000225599
Regions
	Repeat	288 – 323	36	HEAT 1
	Repeat	1001 – 1037	37	HEAT 2
	Repeat	1050 – 1086	37	HEAT 3
	Repeat	1720 – 1753	34	TPR 1
	Domain	2884 – 3539	656	FAT
	Repeat	2921 – 2954	34	TPR 2
	Repeat	2956 – 2983	28	TPR 3
	Domain	3747 – 4015	269	PI3K/PI4K
	Domain	4096 – 4128	33	FATC
	Region	1501 – 1536	36	Interaction with C1D By similarity
	Region	1501 – 1536	36	Leucine-zipper
	Region	2432 – 3213	782	KIP-binding By similarity
Sites
	Site	2017 – 2018	2	Cleavage; by caspase-3 By similarity
Amino acid modifications
	Modified residue	117	1	N6-acetyllysine By similarity
	Modified residue	891	1	Phosphoserine By similarity
	Modified residue	1206	1	N6-acetyllysine By similarity
	Modified residue	1967	1	N6-acetyllysine By similarity
	Modified residue	2255	1	N6-acetyllysine By similarity
	Modified residue	2605	1	Phosphothreonine; by autocatalysis By similarity
	Modified residue	2608	1	Phosphoserine; by autocatalysis By similarity
	Modified residue	2634	1	Phosphothreonine; by autocatalysis By similarity
	Modified residue	2643	1	Phosphothreonine; by autocatalysis By similarity
	Modified residue	3206	1	Phosphoserine By similarity
	Modified residue	3241	1	N6-acetyllysine By similarity
	Modified residue	3260	1	N6-acetyllysine By similarity
	Modified residue	3638	1	N6-acetyllysine By similarity
	Modified residue	3642	1	N6-acetyllysine By similarity
	Modified residue	4026	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	842 – 852	11	DEALSLEEIRI → VRNPFLILYLK in isoform 2.		VSP_017361
	Alternative sequence	853 – 4128	3276	Missing in isoform 2.		VSP_017362
	Natural variant	2140	1	R → C. Ref.1 Ref.2 Ref.3
	Natural variant	3191	1	L → P.
	Natural variant	4046 – 4128	83	Missing in SCID.
Experimental info
	Sequence conflict	3300	1	M → T in BAA19566. Ref.1
	Sequence conflict	3300	1	M → T in BAA28873. Ref.2
	Sequence conflict	3300	1	M → T in BAA28875. Ref.2
	Sequence conflict	3300	1	M → T in BAB91149. Ref.3
	Sequence conflict	3844	1	M → V in AAB36939. Ref.10
	Sequence conflict	3844	1	M → V in AAB36940. Ref.10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: B143922D57F4331E	FASTA	4,128	471,471
	10 20 30 40 50 60 MAEEGTGVRC WLLQLQEFLS AADRCSAAGA SYQLIRSLGQ ECVLSTSSAV QALQISLVFS 70 80 90 100 110 120 RDFGLLVFIR KSLSIEDFRD CREEALKFLC VFLEKIDQKV MHYSLDIKNT CTSVYTKDRT 130 140 150 160 170 180 AKCKIPALDL LIKLLQILRS TRLMDEFKIG ELFNKFYGEL ASKSKLPDTV LEKVYELLGV 190 200 210 220 230 240 LGEVHPSEMI NHSENLFRAF LGELKTQMTS TVREPKFPVL AGCLKGLSSL LCNFTKSMEE 250 260 270 280 290 300 DPQTSKEIFG FTFKAIRPQI EMKRYAVPLA GLRLLTLHAS QFTACLLDNY ITLFEVLSKW 310 320 330 340 350 360 CSHTNVELKK AAHSALESFL RQISFTVAED AELHKSRLKY FMEQFYGIIR NTDSNNKELA 370 380 390 400 410 420 IAIRGYGLFA GPCKVINAKD VDFMYVELIQ RCKQMFLTHA DASEDHVYQM PSFLQSIASV 430 440 450 460 470 480 LLYLDTVPEV YTPVLEHLMV VQIDSFPQYS PKMQLVCCKA IIKLFLALSE KGPVHWNCIS 490 500 510 520 530 540 AVVHQGLIRI CSKPVVLQKD VESRSDNRSA SEEVRTGRWK VPTYKDYVDL FQHLLGCDQM 550 560 570 580 590 600 EDFILGDETF LFVNSSLKSL NHLLYDEFIR SVLKIVEKLD LTLEKQTVGE QEDGSTADVW 610 620 630 640 650 660 VIPTSDPAAN LHPAKPSDFS ALINLVEFCR EILPRKHVGF FEPWVYSFAY ELILQSTRLP 670 680 690 700 710 720 LISGFYKLLS IAVKNARKIK YFEGISPKSL KHSPEDTEKY SCFALFAKFG KEVSVKMKQY 730 740 750 760 770 780 KDELLASCLT FVLSLPHDII ELDVRAYVPA LQMAFKLGLS HMPLAEIGLH ALKEWSVHID 790 800 810 820 830 840 KSILQPYYKD ILPCLDGYLN TSTLSDETKS HWGLSALSRA AQKGFNRHVV KHLKRTRNSS 850 860 870 880 890 900 PDEALSLEEI RIKVVQILGS LGGQINKSLV TATSGERMKK YVAWDAERRL SFAVPFREMK 910 920 930 940 950 960 PVIYLDVFLP RVTELALSAS DRQTKVAACE LLHSMVMFML GRATQMPEGQ GLPPMYQLYK 970 980 990 1000 1010 1020 HTFPVLLQLA CDVDQVTRQL YEPLVMQLIH WLTNNKKFES QDTVALLEAI LDGIVDPVDS 1030 1040 1050 1060 1070 1080 TLRDFCGRCV QEFLKWSIKQ TTPQQQEKSP VNSKSLFKRL YSLALHPNAF KRLGAALAFN 1090 1100 1110 1120 1130 1140 HIYKEFREEG SLVEQFVFEA LVTYMESLAL AHEDEKSLGT VQQCCDAIDH LRRIIEKKHV 1150 1160 1170 1180 1190 1200 SLNKAKKRRL PQGFPPLTSL CLLDLVEWLL AHCGRPQTEC RHKSMELFYK FVPLLPGNKS 1210 1220 1230 1240 1250 1260 PSLWLKDLIK KKGISFLINT FEGGASSSDQ PAGILAQPTL VYLQGPISLR GVLQWLDLLL 1270 1280 1290 1300 1310 1320 AALECYNTFI EKETVQGQEV LGAEVQSSLL KSVAFFLESI ATHSARAVEQ RFGSGAPGPP 1330 1340 1350 1360 1370 1380 SLHEEEKYNY SKCTVLVRIM EFTTTLLIAS PEDCKLLEKD LCNTNLMQVL VKMICEPMSL 1390 1400 1410 1420 1430 1440 GFNIGDVQVM NHLPSICVNL LKALRKSPYR DMLETHLKEK VTVQSVEELC SINLCSSGAR 1450 1460 1470 1480 1490 1500 QERSKLLSIL SACKQLHKAG FSHVISPSQS TALNHSVGMR LLSLVYKGIV PAEERQCLQS 1510 1520 1530 1540 1550 1560 LDPSCKSLAN GLLELAFGFG GLCDHLVSLL LNSAMLSTQY LGSSQRNISF SHGEYFYSLF 1570 1580 1590 1600 1610 1620 SEVINSELLK NLDIAVSRLM ESSSDNPKMV STVLNGMLDT SFRDRAVQKH QGLKLATAIL 1630 1640 1650 1660 1670 1680 QNWRKCDSWW APDSAPESKT TVLSLLAKML QIDSALSFDT NHSSFSEIFT TYASLLADTK 1690 1700 1710 1720 1730 1740 LGLHLKGQAI ILLPFFTSLR EGSLENLKHI LEKLIVCNFP MKSDEFPPDS LKYNNYVDCM 1750 1760 1770 1780 1790 1800 KKFLDALELS QSPMLFQLMT DILCREQRHI MEELFQTTFK RIARQSPCVT QLNLLESVYT 1810 1820 1830 1840 1850 1860 MFRKADLPSN VTRQAFVDRS LLTLLWHCDL DTLKEFFSRI VVDAIDVLKS RFTKLNEFTF 1870 1880 1890 1900 1910 1920 DTQITKKMCY YKMLAVMYSR LLKDDVHSKE AKINQAFHGS RVAEGNELTK TLLKLCHDAF 1930 1940 1950 1960 1970 1980 TENMVGESQL LEKRRLYHCA AYNCAISLIS CVFNELKFYQ GFLFNEKPEK NLFIFENLID 1990 2000 2010 2020 2030 2040 LKRCYTFPIE VEVPMERKKK YIEIRKEARD AANGASGSPH YMSSLSYLTD SSLSEEMSQF 2050 2060 2070 2080 2090 2100 DFSTGVQSYS YSSQDRKPTT GHFQRREHQD SMTQDDIMEL EMDELNQHEC MAPMIALIKH 2110 2120 2130 2140 2150 2160 MQRNVIAPKG EEGSIPKDLP PWMKFLHDKL GNASVSLNIR LFLAKLVINT EEVFRPYAKH 2170 2180 2190 2200 2210 2220 WLSPLLQLAV CENNREGIHY MMVEIVATIL SWTGLATPTG VPKDEVLANR LLRFLMKHVF 2230 2240 2250 2260 2270 2280 HPKRAVFRHN LEIIKTLVEC WKECLSIPYR LIFEKFSHKD PNSKDNSVGI QLLGIVIANN 2290 2300 2310 2320 2330 2340 LPPYDPNCDI TSAMYFEALV NNMSFVKYKE VYAAAAEVLG LILQYITERK HVIAELVCEL 2350 2360 2370 2380 2390 2400 VIKQLKQHQN TMEDKFIVCL NKIAKGFPPL ADRFLNALFF LLPKFHGVMK TLCLEVVLCR 2410 2420 2430 2440 2450 2460 AEEITGLYLQ LKSKDFLQVM RHRDDERQKV CLDIVYKMVA KLKPIELREL LNPVVEFVSH 2470 2480 2490 2500 2510 2520 PSPTCREQMY NILMWIHDNY RDQESQNDED SQEIFKLAKD VLIQGLIDEN VGLQLIIRNF 2530 2540 2550 2560 2570 2580 WSHETRLPSN TLDRLLALNS LYSPKIEVHF LSLATNFLLE MTRMSPDYLN PIFEHPLSEC 2590 2600 2610 2620 2630 2640 EFQEYTIDPD WRFRSTVLTP MFIETQASPS ILHTQTQEGP LSDQRQKPGQ VRATQQQYDF 2650 2660 2670 2680 2690 2700 TPTQASVERS SFDWLTGSSI DLLADHTVFS SETLSSSLLF SHKRTEKSQR MSCKSVGPDF 2710 2720 2730 2740 2750 2760 GTKKLGLPDD EVDNQVKSGT PSQADILRLR RRFLKDREKL SLLYAKRGLM EQKLEKDIKS 2770 2780 2790 2800 2810 2820 EFKMKQDAQV VLYRSYRHGD LPDIQIQHSG LITPLQAVAQ KDPIIAKQLF SSLFSGILKE 2830 2840 2850 2860 2870 2880 MNKFKTTSEK NIITQNLLQD FNRFLNTTFL FFPPFVSCIQ EISCQHPDFL TLDPASVRVG 2890 2900 2910 2920 2930 2940 CLASLQQPGG IRLLEEALLR LMPKEPPTKR VRGKTCLPPD VLRWMELAKL YRSIGEYDVL 2950 2960 2970 2980 2990 3000 RGIFSSELGT TQDTQNALLA EARSDYCQAA KLYDEALNKL EWVDGEPTEA EKEFWELASL 3010 3020 3030 3040 3050 3060 DCYNNLSKWK ELEYCSTVNI VSENSLDLSK MWSEPFYQET YLPYVIRSKL KLLLQGEGNQ 3070 3080 3090 3100 3110 3120 SLLTFVDEAM NKELQKTVLE LQYSQELSLL YILQDDIDRA TYYIKNGIQI FMQNYSSIDV 3130 3140 3150 3160 3170 3180 LLYRSRLAKL QSVQTLAEIE EFLSFICKHG DLSSLGPLRR LLKTWTSRYP DVVTDPMHIW 3190 3200 3210 3220 3230 3240 DDIITNRCFF LSKIEERLTA PSGDHSMSVD EDEESIDREV YEPKEDVRCM LQSCRFTMKM 3250 3260 3270 3280 3290 3300 KMIESAWKQS NFSLSMKLLK EMHKESKTRE IWRVQWLHSY SQLNHCRSHT QSPREQVLNM 3310 3320 3330 3340 3350 3360 LKTITLLDES DISNYLNKNI QASCDQSILL GTTCRIMADA LSREPACLSD LEENKVNSIL 3370 3380 3390 3400 3410 3420 TLSGSNAENT ETVITGLYQR AFHHLSKAVQ SAEEETQLSC WGHEAAAERA HAYMTLVGFC 3430 3440 3450 3460 3470 3480 DQQLRKVEES ASQKTSAEME AYPALVVEKM LRALKLNSSE ARLKFPRLLQ IIEQYSEETL 3490 3500 3510 3520 3530 3540 NIMTKEISSI PCWQFIGWIS HMMALLDKEE AIAVQHTVEE IADNYPQAII YPFIISSESY 3550 3560 3570 3580 3590 3600 SFKNTSSGHN NKAFVERIKS KLDHGEVIHS FINALDQLSN PDLLFKDWVS DTKDELGKNP 3610 3620 3630 3640 3650 3660 VNKKNIEKLY ERMYAALGDL RAPGLGPFRR RFIQAFGKEF VKSFGNGGSK LLTMKVDDFC 3670 3680 3690 3700 3710 3720 KITGSLLVRM KKDSKLPGNL KEYSPWMSEF KAQFLKNELE IPGQYDGKSK PLPEYHVRIS 3730 3740 3750 3760 3770 3780 GFDERVKVML SLRKPKRIVI RGHDEKEYPF LVKGGEDLRQ DQRIEQIFEV MNAILSQDAA 3790 3800 3810 3820 3830 3840 CSQRNMQLRT YRVVPMTSRL GLIEWIENTM TLKDLLLSNM SQEEKVANNS DPKAPIRDYK 3850 3860 3870 3880 3890 3900 DWLMKVSGKS DAGAYVLMYS RANRTETVVA FRRRESQVPP DLLKRAFVKM STSPEAFLAL 3910 3920 3930 3940 3950 3960 RSHFASSHAL LCISHWLLGI GDRHLNNFMV AMETGSVIGI DFGHAFGSAT QFLPVPELMP 3970 3980 3990 4000 4010 4020 FRLTRQFVSL MLPMKETGLM CTVMVHALRA FRSCAGLLTD TMEIFVKEPS FDWKSFEQTM 4030 4040 4050 4060 4070 4080 LRKGGSWIQE INVTEKNWYP QHKIRYAKRK LAGANPAVIT CDELYLGHEA SSAFRSYTAV 4090 4100 4110 4120 ARGNRDYNIR AQEPESGLSE ETQVKCLVDQ ATDPNILGRT WEGWEPWM
	Isoform 2 [UniParc]. Checksum: 813746121866A369	FASTA	852	96,914
	10 20 30 40 50 60 MAEEGTGVRC WLLQLQEFLS AADRCSAAGA SYQLIRSLGQ ECVLSTSSAV QALQISLVFS 70 80 90 100 110 120 RDFGLLVFIR KSLSIEDFRD CREEALKFLC VFLEKIDQKV MHYSLDIKNT CTSVYTKDRT 130 140 150 160 170 180 AKCKIPALDL LIKLLQILRS TRLMDEFKIG ELFNKFYGEL ASKSKLPDTV LEKVYELLGV 190 200 210 220 230 240 LGEVHPSEMI NHSENLFRAF LGELKTQMTS TVREPKFPVL AGCLKGLSSL LCNFTKSMEE 250 260 270 280 290 300 DPQTSKEIFG FTFKAIRPQI EMKRYAVPLA GLRLLTLHAS QFTACLLDNY ITLFEVLSKW 310 320 330 340 350 360 CSHTNVELKK AAHSALESFL RQISFTVAED AELHKSRLKY FMEQFYGIIR NTDSNNKELA 370 380 390 400 410 420 IAIRGYGLFA GPCKVINAKD VDFMYVELIQ RCKQMFLTHA DASEDHVYQM PSFLQSIASV 430 440 450 460 470 480 LLYLDTVPEV YTPVLEHLMV VQIDSFPQYS PKMQLVCCKA IIKLFLALSE KGPVHWNCIS 490 500 510 520 530 540 AVVHQGLIRI CSKPVVLQKD VESRSDNRSA SEEVRTGRWK VPTYKDYVDL FQHLLGCDQM 550 560 570 580 590 600 EDFILGDETF LFVNSSLKSL NHLLYDEFIR SVLKIVEKLD LTLEKQTVGE QEDGSTADVW 610 620 630 640 650 660 VIPTSDPAAN LHPAKPSDFS ALINLVEFCR EILPRKHVGF FEPWVYSFAY ELILQSTRLP 670 680 690 700 710 720 LISGFYKLLS IAVKNARKIK YFEGISPKSL KHSPEDTEKY SCFALFAKFG KEVSVKMKQY 730 740 750 760 770 780 KDELLASCLT FVLSLPHDII ELDVRAYVPA LQMAFKLGLS HMPLAEIGLH ALKEWSVHID 790 800 810 820 830 840 KSILQPYYKD ILPCLDGYLN TSTLSDETKS HWGLSALSRA AQKGFNRHVV KHLKRTRNSS 850 PVRNPFLILY LK

References

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[1]	"Nonsense mutation at Tyr-4046 in the DNA-dependent protein kinase catalytic subunit of severe combined immune deficiency mice." Araki R., Fujimori A., Hamatani K., Mita K., Saito T., Mori M., Fukumura R., Morimyo M., Muto M., Itoh M., Tatsumi K., Abe M. Proc. Natl. Acad. Sci. U.S.A. 94:2438-2443(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT CYS-2140, VARIANT SCID 4046-TYR--MET-4128 DEL. Strain: C.B17. Tissue: Fibroblast and Leukocyte.
[2]	"Murine cell line SX9 bearing a mutation in the DNA-PKcs gene exhibits aberrant V(D)J recombination not only in the coding joint but also in the signal joint." Fukumura R., Araki R., Fujimori A., Mori M., Saito T., Watanabe F., Sarashi M., Itsukaichi H., Eguch-Kasai K., Sato K., Tatsumi K., Abe M. J. Biol. Chem. 273:13058-13064(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT CYS-2140.
[3]	"The murine DNA-PKcs gene consists of 86 exons dispersed in more than 250 kb." Fujimori A., Araki R., Fukumura R., Saito T., Mori M., Mita K., Tatsumi K., Abe M. Genomics 45:194-199(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT CYS-2140. Strain: 129/SvJ.
[4]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3618-4128. Strain: C57BL/6J and NOD. Tissue: Heart and Thymus.
[5]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[6]	"Mouse Cdc21 only 0.5 kb upstream from DNA-PKcs in a head-to-head organization: an implication of co-evolution of ATM family members and cell cycle regulating genes." Saito T., Matsuda Y., Ishii H., Watanabe F., Mori M., Hayashi A., Araki R., Fujimori A., Fukumura R., Morimyo M., Tatsumi K., Hori T., Abe M. Mamm. Genome 9:769-772(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
[7]	"Nonhomologous end-joining deficiency of L5178Y-S cells is not associated with mutation in the ABCDE autophosphorylation cluster." Brzoska K., Kruszewski M., Szumiel I. Acta Biochim. Pol. 53:233-236(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2550-2658.
[8]	"Cloning and chromosomal mapping of the mouse DNA-dependent protein kinase gene." Hamatani K., Matsuda Y., Araki R., Itoh M., Abe M. Immunogenetics 45:1-5(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3615-4128. Strain: BALB/c. Tissue: Leukocyte.
[9]	"Identification of a nonsense mutation in the carboxyl-terminal region of DNA-dependent protein kinase catalytic subunit in the scid mouse." Blunt T., Gell D., Fox M., Taccioli G.E., Lehmann A.R., Jackson S.P., Jeggo P.A. Proc. Natl. Acad. Sci. U.S.A. 93:10285-10290(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3680-4128.
[10]	"Biochemical and genetic defects in the DNA-dependent protein kinase in murine scid lymphocytes." Danska J.S., Holland D.P., Mariathasan S., Williams K.M., Guidos C.J. Mol. Cell. Biol. 16:5507-5517(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3839-4128. Strain: C.B17.
[11]	"Functional interaction between DNA-PK and c-Abl in response to DNA damage." Kharbanda S., Pandey P., Jin S., Inoue S., Bharti A., Yuan Z.-M., Weichselbaum R., Weaver D., Kufe D. Nature 386:732-735(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION OF ABL1.
[12]	"Functional interaction between DNA-PKcs and telomerase in telomere length maintenance." Espejel S., Franco S., Sgura A., Gae D., Bailey S.M., Taccioli G.E., Blasco M.A. EMBO J. 21:6275-6287(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"GAPDH mediates nitrosylation of nuclear proteins." Kornberg M.D., Sen N., Hara M.R., Juluri K.R., Nguyen J.V., Snowman A.M., Law L., Hester L.D., Snyder S.H. Nat. Cell Biol. 12:1094-1100(2010) [PubMed] [Europe PMC] [Abstract] Cited for: S-NITROSYLATION BY GAPDH.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D87521 mRNA. Translation: BAA19566.1. AB007544 mRNA. Translation: BAA28873.1. AB011543 mRNA. Translation: BAA28875.1. AB030754 Genomic DNA. Translation: BAB91149.1. AK084827 mRNA. Translation: BAE43387.1. AK088981 mRNA. Translation: BAC40685.1. AC111103 Genomic DNA. No translation available. AC154586 Genomic DNA. No translation available. CT010522 Genomic DNA. No translation available. CT030649 Genomic DNA. No translation available. AB000629 Genomic DNA. Translation: BAA34640.1. DQ235257 mRNA. Translation: ABB36568.1. DQ235258 mRNA. Translation: ABB36569.1. D83786 mRNA. Translation: BAA12115.1. U78157 mRNA. Translation: AAB36939.1. U78158 mRNA. Translation: AAB36940.1.
IPI	IPI00123886. IPI00742372.
PIR	JC6306.
RefSeq	NP_035289.2. NM_011159.2.
UniGene	Mm.71.
3D structure databases
ProteinModelPortal	P97313.
ModBase	Search...
Protein-protein interaction databases
IntAct	P97313. 3 interactions.
STRING	10090.ENSMUSP00000023352.
PTM databases
PhosphoSite	P97313.
Proteomic databases
PaxDb	P97313.
PRIDE	P97313.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000023352; ENSMUSP00000023352; ENSMUSG00000022672.
GeneID	19090.
KEGG	mmu:19090.
UCSC	uc007yhs.1. mouse. uc007yht.1. mouse.
Organism-specific databases
CTD	5591.
MGI	MGI:104779. Prkdc.
Phylogenomic databases
eggNOG	COG5032.
GeneTree	ENSGT00700000104541.
HOVERGEN	HBG053681.
InParanoid	P97313.
KO	K06642.
OMA	LVEQFVF.
OrthoDB	EOG461431.
Gene expression databases
ArrayExpress	P97313.
Bgee	P97313.
Genevestigator	P97313.
GermOnline	ENSMUSG00000022672. Mus musculus.
Family and domain databases
Gene3D	1.10.1070.11. 3 hits. 1.25.10.10. 1 hit.
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. 2 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
NextBio	295644.
SOURCE	Search...

Entry information

Entry name

PRKDC_MOUSE

Accession

Primary (citable) accession number: P97313
Secondary accession number(s): E9QN15 , O88187, P97928, Q307W9, Q3V2W8, Q8C2A7, Q9Z341

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 126 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program