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P97313

- PRKDC_MOUSE

UniProt

P97313 - PRKDC_MOUSE

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Protein

DNA-dependent protein kinase catalytic subunit

Gene

Prkdc

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Serine/threonine-protein kinase that acts as a molecular sensor for DNA damage. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break (DSB) repair and V(D)J recombination. Must be bound to DNA to express its catalytic properties. Promotes processing of hairpin DNA structures in V(D)J recombination by activation of the hairpin endonuclease artemis (DCLRE1C). The assembly of the DNA-PK complex at DNA ends is also required for the NHEJ ligation step. Required to protect and align broken ends of DNA. May also act as a scaffold protein to aid the localization of DNA repair proteins to the site of damage. Found at the ends of chromosomes, suggesting a further role in the maintenance of telomeric stability and the prevention of chromosomal end fusion. Also involved in modulation of transcription. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates 'Ser-139' of histone variant H2AX/H2AFX, thereby regulating DNA damage response mechanism. Phosphorylates DCLRE1C, 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. Contributes to the determination of the circadian period length by antagonizing phosphorylation of CRY1 'Ser-588' and increasing CRY1 protein stability, most likely through an indirect machanism.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Inhibited by wortmannin. Activity of the enzyme seems to be attenuated by autophosphorylation (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei2017 – 20182Cleavage; by caspase-3By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. DNA binding Source: InterPro
  3. DNA-dependent protein kinase activity Source: Ensembl
  4. enzyme binding Source: UniProtKB
  5. poly(A) RNA binding Source: Ensembl

GO - Biological processi

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

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Biological rhythms, DNA damage, DNA repair

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_196447. IRF3-mediated induction of type I IFN.
REACT_224809. Processing of DNA ends prior to end rejoining.
REACT_254501. Nonhomologous End-joining (NHEJ).

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-dependent protein kinase catalytic subunit (EC:2.7.11.1)
Short name:
DNA-PK catalytic subunit
Short name:
DNA-PKcs
Alternative name(s):
p460
Gene namesi
Name:Prkdc
Synonyms:Xrcc7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 16

Organism-specific databases

MGIiMGI:104779. Prkdc.

Subcellular locationi

Nucleus. Nucleusnucleolus By similarity

GO - Cellular componenti

  1. DNA-dependent protein kinase-DNA ligase 4 complex Source: Ensembl
  2. nonhomologous end joining complex Source: UniProtKB
  3. nucleus Source: MGI
  4. transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

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.

Keywords - Diseasei

Disease mutation, SCID

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 41284128DNA-dependent protein kinase catalytic subunitPRO_0000225599Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei117 – 1171N6-acetyllysineBy similarity
Modified residuei891 – 8911PhosphoserineBy similarity
Modified residuei1206 – 12061N6-acetyllysineBy similarity
Modified residuei1967 – 19671N6-acetyllysineBy similarity
Modified residuei2053 – 20531Phosphoserine; by autocatalysisBy similarity
Modified residuei2255 – 22551N6-acetyllysineBy similarity
Modified residuei2605 – 26051Phosphothreonine; by autocatalysisBy similarity
Modified residuei2608 – 26081Phosphoserine; by autocatalysisBy similarity
Modified residuei2634 – 26341Phosphothreonine; by autocatalysisBy similarity
Modified residuei2643 – 26431Phosphothreonine; by autocatalysisBy similarity
Modified residuei3206 – 32061PhosphoserineBy similarity
Modified residuei3241 – 32411N6-acetyllysineBy similarity
Modified residuei3260 – 32601N6-acetyllysineBy similarity
Modified residuei3638 – 36381N6-acetyllysineBy similarity
Modified residuei3642 – 36421N6-acetyllysineBy similarity
Modified residuei4026 – 40261PhosphoserineBy similarity

Post-translational modificationi

Autophosphorylated on Ser-2053, Thr-2605, Thr-2634 and Thr-2643. Ser-2053 and Thr-2605 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 (By similarity).By similarity
S-nitrosylated by GAPDH.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation

Proteomic databases

MaxQBiP97313.
PaxDbiP97313.
PRIDEiP97313.

PTM databases

PhosphoSiteiP97313.

Expressioni

Gene expression databases

BgeeiP97313.
ExpressionAtlasiP97313. baseline and differential.
GenevestigatoriP97313.

Interactioni

Subunit structurei

DNA-PK is a heterotrimer of PRKDC and the Ku p70-p86 (XRCC6-XRCC5) dimer. Formation of this complex may be promoted by interaction with ILF3. Associates with the DNA-bound Ku heterodimer, but it can also bind to and be activated by free DNA. Interacts with DNA-PKcs-interacting protein (KIP) with the region upstream the kinase domain. PRKDC alone also interacts with and phosphorylates DCLRE1C, thereby activating the latent endonuclease activity of this protein. Interacts with C1D. Interacts with TTI1 and TELO2. Interacts with CIB1. Interacts with CRY1 and CRY2; negatively regulates CRY1 phosphorylation.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
EGFRP005334EBI-2272005,EBI-297353From a different organism.

Protein-protein interaction databases

BioGridi202371. 7 interactions.
IntActiP97313. 5 interactions.
MINTiMINT-4108568.
STRINGi10090.ENSMUSP00000023352.

Structurei

3D structure databases

ProteinModelPortaliP97313.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati288 – 32336HEAT 1Add
BLAST
Repeati1001 – 103737HEAT 2Add
BLAST
Repeati1050 – 108637HEAT 3Add
BLAST
Repeati1720 – 175334TPR 1Add
BLAST
Domaini2884 – 3539656FATPROSITE-ProRule annotationAdd
BLAST
Repeati2921 – 295434TPR 2Add
BLAST
Repeati2956 – 298328TPR 3Add
BLAST
Domaini3747 – 4015269PI3K/PI4KPROSITE-ProRule annotationAdd
BLAST
Domaini4096 – 412833FATCPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1501 – 153636Interaction with C1DBy similarityAdd
BLAST
Regioni1501 – 153636Leucine-zipperAdd
BLAST
Regioni2432 – 3213782KIP-bindingBy similarityAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiCOG5032.
GeneTreeiENSGT00770000120527.
HOVERGENiHBG053681.
InParanoidiP97313.
KOiK06642.
OMAiLVEQFVF.
OrthoDBiEOG7DNNT7.
TreeFamiTF324494.

Family and domain databases

Gene3Di1.10.1070.11. 3 hits.
1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR003152. FATC.
IPR011009. Kinase-like_dom.
IPR012582. NUC194.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003151. PIK-rel_kinase_FAT.
IPR014009. PIK_FAT.
[Graphical view]
PfamiPF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF08163. NUC194. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
[Graphical view]
SMARTiSM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 9 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS51189. FAT. 1 hit.
PS51190. FATC. 1 hit.
PS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Note: A number of isoforms are produced.

Isoform 1 (identifier: P97313-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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        10         20         30         40         50
MAEEGTGVRC WLLQLQEFLS AADRCSAAGA SYQLIRSLGQ ECVLSTSSAV
60 70 80 90 100
QALQISLVFS RDFGLLVFIR KSLSIEDFRD CREEALKFLC VFLEKIDQKV
110 120 130 140 150
MHYSLDIKNT CTSVYTKDRT AKCKIPALDL LIKLLQILRS TRLMDEFKIG
160 170 180 190 200
ELFNKFYGEL ASKSKLPDTV LEKVYELLGV LGEVHPSEMI NHSENLFRAF
210 220 230 240 250
LGELKTQMTS TVREPKFPVL AGCLKGLSSL LCNFTKSMEE DPQTSKEIFG
260 270 280 290 300
FTFKAIRPQI EMKRYAVPLA GLRLLTLHAS QFTACLLDNY ITLFEVLSKW
310 320 330 340 350
CSHTNVELKK AAHSALESFL RQISFTVAED AELHKSRLKY FMEQFYGIIR
360 370 380 390 400
NTDSNNKELA IAIRGYGLFA GPCKVINAKD VDFMYVELIQ RCKQMFLTHA
410 420 430 440 450
DASEDHVYQM PSFLQSIASV LLYLDTVPEV YTPVLEHLMV VQIDSFPQYS
460 470 480 490 500
PKMQLVCCKA IIKLFLALSE KGPVHWNCIS AVVHQGLIRI CSKPVVLQKD
510 520 530 540 550
VESRSDNRSA SEEVRTGRWK VPTYKDYVDL FQHLLGCDQM EDFILGDETF
560 570 580 590 600
LFVNSSLKSL NHLLYDEFIR SVLKIVEKLD LTLEKQTVGE QEDGSTADVW
610 620 630 640 650
VIPTSDPAAN LHPAKPSDFS ALINLVEFCR EILPRKHVGF FEPWVYSFAY
660 670 680 690 700
ELILQSTRLP LISGFYKLLS IAVKNARKIK YFEGISPKSL KHSPEDTEKY
710 720 730 740 750
SCFALFAKFG KEVSVKMKQY KDELLASCLT FVLSLPHDII ELDVRAYVPA
760 770 780 790 800
LQMAFKLGLS HMPLAEIGLH ALKEWSVHID KSILQPYYKD ILPCLDGYLN
810 820 830 840 850
TSTLSDETKS HWGLSALSRA AQKGFNRHVV KHLKRTRNSS PDEALSLEEI
860 870 880 890 900
RIKVVQILGS LGGQINKSLV TATSGERMKK YVAWDAERRL SFAVPFREMK
910 920 930 940 950
PVIYLDVFLP RVTELALSAS DRQTKVAACE LLHSMVMFML GRATQMPEGQ
960 970 980 990 1000
GLPPMYQLYK HTFPVLLQLA CDVDQVTRQL YEPLVMQLIH WLTNNKKFES
1010 1020 1030 1040 1050
QDTVALLEAI LDGIVDPVDS TLRDFCGRCV QEFLKWSIKQ TTPQQQEKSP
1060 1070 1080 1090 1100
VNSKSLFKRL YSLALHPNAF KRLGAALAFN HIYKEFREEG SLVEQFVFEA
1110 1120 1130 1140 1150
LVTYMESLAL AHEDEKSLGT VQQCCDAIDH LRRIIEKKHV SLNKAKKRRL
1160 1170 1180 1190 1200
PQGFPPLTSL CLLDLVEWLL AHCGRPQTEC RHKSMELFYK FVPLLPGNKS
1210 1220 1230 1240 1250
PSLWLKDLIK KKGISFLINT FEGGASSSDQ PAGILAQPTL VYLQGPISLR
1260 1270 1280 1290 1300
GVLQWLDLLL AALECYNTFI EKETVQGQEV LGAEVQSSLL KSVAFFLESI
1310 1320 1330 1340 1350
ATHSARAVEQ RFGSGAPGPP SLHEEEKYNY SKCTVLVRIM EFTTTLLIAS
1360 1370 1380 1390 1400
PEDCKLLEKD LCNTNLMQVL VKMICEPMSL GFNIGDVQVM NHLPSICVNL
1410 1420 1430 1440 1450
LKALRKSPYR DMLETHLKEK VTVQSVEELC SINLCSSGAR QERSKLLSIL
1460 1470 1480 1490 1500
SACKQLHKAG FSHVISPSQS TALNHSVGMR LLSLVYKGIV PAEERQCLQS
1510 1520 1530 1540 1550
LDPSCKSLAN GLLELAFGFG GLCDHLVSLL LNSAMLSTQY LGSSQRNISF
1560 1570 1580 1590 1600
SHGEYFYSLF SEVINSELLK NLDIAVSRLM ESSSDNPKMV STVLNGMLDT
1610 1620 1630 1640 1650
SFRDRAVQKH QGLKLATAIL QNWRKCDSWW APDSAPESKT TVLSLLAKML
1660 1670 1680 1690 1700
QIDSALSFDT NHSSFSEIFT TYASLLADTK LGLHLKGQAI ILLPFFTSLR
1710 1720 1730 1740 1750
EGSLENLKHI LEKLIVCNFP MKSDEFPPDS LKYNNYVDCM KKFLDALELS
1760 1770 1780 1790 1800
QSPMLFQLMT DILCREQRHI MEELFQTTFK RIARQSPCVT QLNLLESVYT
1810 1820 1830 1840 1850
MFRKADLPSN VTRQAFVDRS LLTLLWHCDL DTLKEFFSRI VVDAIDVLKS
1860 1870 1880 1890 1900
RFTKLNEFTF DTQITKKMCY YKMLAVMYSR LLKDDVHSKE AKINQAFHGS
1910 1920 1930 1940 1950
RVAEGNELTK TLLKLCHDAF TENMVGESQL LEKRRLYHCA AYNCAISLIS
1960 1970 1980 1990 2000
CVFNELKFYQ GFLFNEKPEK NLFIFENLID LKRCYTFPIE VEVPMERKKK
2010 2020 2030 2040 2050
YIEIRKEARD AANGASGSPH YMSSLSYLTD SSLSEEMSQF DFSTGVQSYS
2060 2070 2080 2090 2100
YSSQDRKPTT GHFQRREHQD SMTQDDIMEL EMDELNQHEC MAPMIALIKH
2110 2120 2130 2140 2150
MQRNVIAPKG EEGSIPKDLP PWMKFLHDKL GNASVSLNIR LFLAKLVINT
2160 2170 2180 2190 2200
EEVFRPYAKH WLSPLLQLAV CENNREGIHY MMVEIVATIL SWTGLATPTG
2210 2220 2230 2240 2250
VPKDEVLANR LLRFLMKHVF HPKRAVFRHN LEIIKTLVEC WKECLSIPYR
2260 2270 2280 2290 2300
LIFEKFSHKD PNSKDNSVGI QLLGIVIANN LPPYDPNCDI TSAMYFEALV
2310 2320 2330 2340 2350
NNMSFVKYKE VYAAAAEVLG LILQYITERK HVIAELVCEL VIKQLKQHQN
2360 2370 2380 2390 2400
TMEDKFIVCL NKIAKGFPPL ADRFLNALFF LLPKFHGVMK TLCLEVVLCR
2410 2420 2430 2440 2450
AEEITGLYLQ LKSKDFLQVM RHRDDERQKV CLDIVYKMVA KLKPIELREL
2460 2470 2480 2490 2500
LNPVVEFVSH PSPTCREQMY NILMWIHDNY RDQESQNDED SQEIFKLAKD
2510 2520 2530 2540 2550
VLIQGLIDEN VGLQLIIRNF WSHETRLPSN TLDRLLALNS LYSPKIEVHF
2560 2570 2580 2590 2600
LSLATNFLLE MTRMSPDYLN PIFEHPLSEC EFQEYTIDPD WRFRSTVLTP
2610 2620 2630 2640 2650
MFIETQASPS ILHTQTQEGP LSDQRQKPGQ VRATQQQYDF TPTQASVERS
2660 2670 2680 2690 2700
SFDWLTGSSI DLLADHTVFS SETLSSSLLF SHKRTEKSQR MSCKSVGPDF
2710 2720 2730 2740 2750
GTKKLGLPDD EVDNQVKSGT PSQADILRLR RRFLKDREKL SLLYAKRGLM
2760 2770 2780 2790 2800
EQKLEKDIKS EFKMKQDAQV VLYRSYRHGD LPDIQIQHSG LITPLQAVAQ
2810 2820 2830 2840 2850
KDPIIAKQLF SSLFSGILKE MNKFKTTSEK NIITQNLLQD FNRFLNTTFL
2860 2870 2880 2890 2900
FFPPFVSCIQ EISCQHPDFL TLDPASVRVG CLASLQQPGG IRLLEEALLR
2910 2920 2930 2940 2950
LMPKEPPTKR VRGKTCLPPD VLRWMELAKL YRSIGEYDVL RGIFSSELGT
2960 2970 2980 2990 3000
TQDTQNALLA EARSDYCQAA KLYDEALNKL EWVDGEPTEA EKEFWELASL
3010 3020 3030 3040 3050
DCYNNLSKWK ELEYCSTVNI VSENSLDLSK MWSEPFYQET YLPYVIRSKL
3060 3070 3080 3090 3100
KLLLQGEGNQ SLLTFVDEAM NKELQKTVLE LQYSQELSLL YILQDDIDRA
3110 3120 3130 3140 3150
TYYIKNGIQI FMQNYSSIDV LLYRSRLAKL QSVQTLAEIE EFLSFICKHG
3160 3170 3180 3190 3200
DLSSLGPLRR LLKTWTSRYP DVVTDPMHIW DDIITNRCFF LSKIEERLTA
3210 3220 3230 3240 3250
PSGDHSMSVD EDEESIDREV YEPKEDVRCM LQSCRFTMKM KMIESAWKQS
3260 3270 3280 3290 3300
NFSLSMKLLK EMHKESKTRE IWRVQWLHSY SQLNHCRSHT QSPREQVLNM
3310 3320 3330 3340 3350
LKTITLLDES DISNYLNKNI QASCDQSILL GTTCRIMADA LSREPACLSD
3360 3370 3380 3390 3400
LEENKVNSIL TLSGSNAENT ETVITGLYQR AFHHLSKAVQ SAEEETQLSC
3410 3420 3430 3440 3450
WGHEAAAERA HAYMTLVGFC DQQLRKVEES ASQKTSAEME AYPALVVEKM
3460 3470 3480 3490 3500
LRALKLNSSE ARLKFPRLLQ IIEQYSEETL NIMTKEISSI PCWQFIGWIS
3510 3520 3530 3540 3550
HMMALLDKEE AIAVQHTVEE IADNYPQAII YPFIISSESY SFKNTSSGHN
3560 3570 3580 3590 3600
NKAFVERIKS KLDHGEVIHS FINALDQLSN PDLLFKDWVS DTKDELGKNP
3610 3620 3630 3640 3650
VNKKNIEKLY ERMYAALGDL RAPGLGPFRR RFIQAFGKEF VKSFGNGGSK
3660 3670 3680 3690 3700
LLTMKVDDFC KITGSLLVRM KKDSKLPGNL KEYSPWMSEF KAQFLKNELE
3710 3720 3730 3740 3750
IPGQYDGKSK PLPEYHVRIS GFDERVKVML SLRKPKRIVI RGHDEKEYPF
3760 3770 3780 3790 3800
LVKGGEDLRQ DQRIEQIFEV MNAILSQDAA CSQRNMQLRT YRVVPMTSRL
3810 3820 3830 3840 3850
GLIEWIENTM TLKDLLLSNM SQEEKVANNS DPKAPIRDYK DWLMKVSGKS
3860 3870 3880 3890 3900
DAGAYVLMYS RANRTETVVA FRRRESQVPP DLLKRAFVKM STSPEAFLAL
3910 3920 3930 3940 3950
RSHFASSHAL LCISHWLLGI GDRHLNNFMV AMETGSVIGI DFGHAFGSAT
3960 3970 3980 3990 4000
QFLPVPELMP FRLTRQFVSL MLPMKETGLM CTVMVHALRA FRSCAGLLTD
4010 4020 4030 4040 4050
TMEIFVKEPS FDWKSFEQTM LRKGGSWIQE INVTEKNWYP QHKIRYAKRK
4060 4070 4080 4090 4100
LAGANPAVIT CDELYLGHEA SSAFRSYTAV ARGNRDYNIR AQEPESGLSE
4110 4120
ETQVKCLVDQ ATDPNILGRT WEGWEPWM
Length:4,128
Mass (Da):471,471
Last modified:July 27, 2011 - v3
Checksum:iB143922D57F4331E
GO
Isoform 2 (identifier: P97313-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:852
Mass (Da):96,914
Checksum:i813746121866A369
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3300 – 33001M → T in BAA19566. (PubMed:9122213)Curated
Sequence conflicti3300 – 33001M → T in BAA28873. (PubMed:9582343)Curated
Sequence conflicti3300 – 33001M → T in BAA28875. (PubMed:9582343)Curated
Sequence conflicti3300 – 33001M → T in BAB91149. (PubMed:9339376)Curated
Sequence conflicti3844 – 38441M → V in AAB36939. (PubMed:8816463)Curated
Sequence conflicti3844 – 38441M → V in AAB36940. (PubMed:8816463)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2140 – 21401R → C.3 Publications
Natural varianti3191 – 31911L → P.
Natural varianti4046 – 412883Missing in SCID. 1 Publication
Add
BLAST

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei842 – 85211DEALSLEEIRI → VRNPFLILYLK in isoform 2. 1 PublicationVSP_017361Add
BLAST
Alternative sequencei853 – 41283276Missing in isoform 2. 1 PublicationVSP_017362Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS27978.1. [P97313-1]
PIRiJC6306.
RefSeqiNP_035289.2. NM_011159.2. [P97313-1]
UniGeneiMm.71.

Genome annotation databases

EnsembliENSMUST00000023352; ENSMUSP00000023352; ENSMUSG00000022672. [P97313-1]
GeneIDi19090.
KEGGimmu:19090.
UCSCiuc007yhs.1. mouse. [P97313-2]
uc007yht.1. mouse. [P97313-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS27978.1. [P97313-1 ]
PIRi JC6306.
RefSeqi NP_035289.2. NM_011159.2. [P97313-1 ]
UniGenei Mm.71.

3D structure databases

ProteinModelPortali P97313.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202371. 7 interactions.
IntActi P97313. 5 interactions.
MINTi MINT-4108568.
STRINGi 10090.ENSMUSP00000023352.

Chemistry

BindingDBi P97313.
ChEMBLi CHEMBL2176779.

PTM databases

PhosphoSitei P97313.

Proteomic databases

MaxQBi P97313.
PaxDbi P97313.
PRIDEi P97313.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000023352 ; ENSMUSP00000023352 ; ENSMUSG00000022672 . [P97313-1 ]
GeneIDi 19090.
KEGGi mmu:19090.
UCSCi uc007yhs.1. mouse. [P97313-2 ]
uc007yht.1. mouse. [P97313-1 ]

Organism-specific databases

CTDi 5591.
MGIi MGI:104779. Prkdc.

Phylogenomic databases

eggNOGi COG5032.
GeneTreei ENSGT00770000120527.
HOVERGENi HBG053681.
InParanoidi P97313.
KOi K06642.
OMAi LVEQFVF.
OrthoDBi EOG7DNNT7.
TreeFami TF324494.

Enzyme and pathway databases

Reactomei REACT_196447. IRF3-mediated induction of type I IFN.
REACT_224809. Processing of DNA ends prior to end rejoining.
REACT_254501. Nonhomologous End-joining (NHEJ).

Miscellaneous databases

NextBioi 295644.
PROi P97313.
SOURCEi Search...

Gene expression databases

Bgeei P97313.
ExpressionAtlasi P97313. baseline and differential.
Genevestigatori P97313.

Family and domain databases

Gene3Di 1.10.1070.11. 3 hits.
1.25.10.10. 1 hit.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR003152. FATC.
IPR011009. Kinase-like_dom.
IPR012582. NUC194.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003151. PIK-rel_kinase_FAT.
IPR014009. PIK_FAT.
[Graphical view ]
Pfami PF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF08163. NUC194. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
[Graphical view ]
SMARTi SM00146. PI3Kc. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 9 hits.
SSF56112. SSF56112. 2 hits.
PROSITEi PS51189. FAT. 1 hit.
PS51190. FATC. 1 hit.
PS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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. 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. Cited for: S-NITROSYLATION BY GAPDH.
  14. "Phosphorylation of the cryptochrome 1 C-terminal tail regulates circadian period length."
    Gao P., Yoo S.H., Lee K.J., Rosensweig C., Takahashi J.S., Chen B.P., Green C.B.
    J. Biol. Chem. 288:35277-35286(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CYRCADIAN CLOCK, INTERACTION WITH CRY1 AND CRY2.

Entry informationi

Entry nameiPRKDC_MOUSE
AccessioniPrimary (citable) accession number: P97313
Secondary accession number(s): E9QN15
, O88187, P97928, Q307W9, Q3V2W8, Q8C2A7, Q9Z341
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 143 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3