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P97313

- PRKDC_MOUSE

UniProt

P97313 - PRKDC_MOUSE

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Protein

DNA-dependent protein kinase catalytic subunit

Gene
Prkdc, Xrcc7
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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei2017 – 20182Cleavage; by caspase-3 By 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. protein binding Source: UniProtKB

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. signal transduction involved in mitotic G1 DNA damage checkpoint Source: UniProtKB
  20. somitogenesis Source: MGI
  21. T cell differentiation in thymus Source: MGI
  22. T cell lineage commitment Source: MGI
  23. T cell receptor V(D)J recombination Source: MGI
  24. 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.

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. nucleolus Source: UniProtKB-SubCell
  4. nucleus Source: MGI
  5. 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.1 Publication

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-acetyllysine By similarity
Modified residuei891 – 8911Phosphoserine By similarity
Modified residuei1206 – 12061N6-acetyllysine By similarity
Modified residuei1967 – 19671N6-acetyllysine By similarity
Modified residuei2053 – 20531Phosphoserine; by autocatalysis By similarity
Modified residuei2255 – 22551N6-acetyllysine By similarity
Modified residuei2605 – 26051Phosphothreonine; by autocatalysis By similarity
Modified residuei2608 – 26081Phosphoserine; by autocatalysis By similarity
Modified residuei2634 – 26341Phosphothreonine; by autocatalysis By similarity
Modified residuei2643 – 26431Phosphothreonine; by autocatalysis By similarity
Modified residuei3206 – 32061Phosphoserine By similarity
Modified residuei3241 – 32411N6-acetyllysine By similarity
Modified residuei3260 – 32601N6-acetyllysine By similarity
Modified residuei3638 – 36381N6-acetyllysine By similarity
Modified residuei3642 – 36421N6-acetyllysine By similarity
Modified residuei4026 – 40261Phosphoserine By 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.1 Publication
S-nitrosylated by GAPDH.

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation

Proteomic databases

MaxQBiP97313.
PaxDbiP97313.
PRIDEiP97313.

PTM databases

PhosphoSiteiP97313.

Expressioni

Gene expression databases

ArrayExpressiP97313.
BgeeiP97313.
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

Protein-protein interaction databases

BioGridi202371. 7 interactions.
IntActiP97313. 4 interactions.
MINTiMINT-4108568.
STRINGi10090.ENSMUSP00000023352.

Structurei

3D structure databases

ProteinModelPortaliP97313.

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 – 3539656FATAdd
BLAST
Repeati2921 – 295434TPR 2Add
BLAST
Repeati2956 – 298328TPR 3Add
BLAST
Domaini3747 – 4015269PI3K/PI4KAdd
BLAST
Domaini4096 – 412833FATCAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1501 – 153636Interaction with C1D By similarityAdd
BLAST
Regioni1501 – 153636Leucine-zipperAdd
BLAST
Regioni2432 – 3213782KIP-binding By similarityAdd
BLAST

Sequence similaritiesi

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.

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiCOG5032.
GeneTreeiENSGT00720000108767.
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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MAEEGTGVRC WLLQLQEFLS AADRCSAAGA SYQLIRSLGQ ECVLSTSSAV     50
QALQISLVFS RDFGLLVFIR KSLSIEDFRD CREEALKFLC VFLEKIDQKV 100
MHYSLDIKNT CTSVYTKDRT AKCKIPALDL LIKLLQILRS TRLMDEFKIG 150
ELFNKFYGEL ASKSKLPDTV LEKVYELLGV LGEVHPSEMI NHSENLFRAF 200
LGELKTQMTS TVREPKFPVL AGCLKGLSSL LCNFTKSMEE DPQTSKEIFG 250
FTFKAIRPQI EMKRYAVPLA GLRLLTLHAS QFTACLLDNY ITLFEVLSKW 300
CSHTNVELKK AAHSALESFL RQISFTVAED AELHKSRLKY FMEQFYGIIR 350
NTDSNNKELA IAIRGYGLFA GPCKVINAKD VDFMYVELIQ RCKQMFLTHA 400
DASEDHVYQM PSFLQSIASV LLYLDTVPEV YTPVLEHLMV VQIDSFPQYS 450
PKMQLVCCKA IIKLFLALSE KGPVHWNCIS AVVHQGLIRI CSKPVVLQKD 500
VESRSDNRSA SEEVRTGRWK VPTYKDYVDL FQHLLGCDQM EDFILGDETF 550
LFVNSSLKSL NHLLYDEFIR SVLKIVEKLD LTLEKQTVGE QEDGSTADVW 600
VIPTSDPAAN LHPAKPSDFS ALINLVEFCR EILPRKHVGF FEPWVYSFAY 650
ELILQSTRLP LISGFYKLLS IAVKNARKIK YFEGISPKSL KHSPEDTEKY 700
SCFALFAKFG KEVSVKMKQY KDELLASCLT FVLSLPHDII ELDVRAYVPA 750
LQMAFKLGLS HMPLAEIGLH ALKEWSVHID KSILQPYYKD ILPCLDGYLN 800
TSTLSDETKS HWGLSALSRA AQKGFNRHVV KHLKRTRNSS PDEALSLEEI 850
RIKVVQILGS LGGQINKSLV TATSGERMKK YVAWDAERRL SFAVPFREMK 900
PVIYLDVFLP RVTELALSAS DRQTKVAACE LLHSMVMFML GRATQMPEGQ 950
GLPPMYQLYK HTFPVLLQLA CDVDQVTRQL YEPLVMQLIH WLTNNKKFES 1000
QDTVALLEAI LDGIVDPVDS TLRDFCGRCV QEFLKWSIKQ TTPQQQEKSP 1050
VNSKSLFKRL YSLALHPNAF KRLGAALAFN HIYKEFREEG SLVEQFVFEA 1100
LVTYMESLAL AHEDEKSLGT VQQCCDAIDH LRRIIEKKHV SLNKAKKRRL 1150
PQGFPPLTSL CLLDLVEWLL AHCGRPQTEC RHKSMELFYK FVPLLPGNKS 1200
PSLWLKDLIK KKGISFLINT FEGGASSSDQ PAGILAQPTL VYLQGPISLR 1250
GVLQWLDLLL AALECYNTFI EKETVQGQEV LGAEVQSSLL KSVAFFLESI 1300
ATHSARAVEQ RFGSGAPGPP SLHEEEKYNY SKCTVLVRIM EFTTTLLIAS 1350
PEDCKLLEKD LCNTNLMQVL VKMICEPMSL GFNIGDVQVM NHLPSICVNL 1400
LKALRKSPYR DMLETHLKEK VTVQSVEELC SINLCSSGAR QERSKLLSIL 1450
SACKQLHKAG FSHVISPSQS TALNHSVGMR LLSLVYKGIV PAEERQCLQS 1500
LDPSCKSLAN GLLELAFGFG GLCDHLVSLL LNSAMLSTQY LGSSQRNISF 1550
SHGEYFYSLF SEVINSELLK NLDIAVSRLM ESSSDNPKMV STVLNGMLDT 1600
SFRDRAVQKH QGLKLATAIL QNWRKCDSWW APDSAPESKT TVLSLLAKML 1650
QIDSALSFDT NHSSFSEIFT TYASLLADTK LGLHLKGQAI ILLPFFTSLR 1700
EGSLENLKHI LEKLIVCNFP MKSDEFPPDS LKYNNYVDCM KKFLDALELS 1750
QSPMLFQLMT DILCREQRHI MEELFQTTFK RIARQSPCVT QLNLLESVYT 1800
MFRKADLPSN VTRQAFVDRS LLTLLWHCDL DTLKEFFSRI VVDAIDVLKS 1850
RFTKLNEFTF DTQITKKMCY YKMLAVMYSR LLKDDVHSKE AKINQAFHGS 1900
RVAEGNELTK TLLKLCHDAF TENMVGESQL LEKRRLYHCA AYNCAISLIS 1950
CVFNELKFYQ GFLFNEKPEK NLFIFENLID LKRCYTFPIE VEVPMERKKK 2000
YIEIRKEARD AANGASGSPH YMSSLSYLTD SSLSEEMSQF DFSTGVQSYS 2050
YSSQDRKPTT GHFQRREHQD SMTQDDIMEL EMDELNQHEC MAPMIALIKH 2100
MQRNVIAPKG EEGSIPKDLP PWMKFLHDKL GNASVSLNIR LFLAKLVINT 2150
EEVFRPYAKH WLSPLLQLAV CENNREGIHY MMVEIVATIL SWTGLATPTG 2200
VPKDEVLANR LLRFLMKHVF HPKRAVFRHN LEIIKTLVEC WKECLSIPYR 2250
LIFEKFSHKD PNSKDNSVGI QLLGIVIANN LPPYDPNCDI TSAMYFEALV 2300
NNMSFVKYKE VYAAAAEVLG LILQYITERK HVIAELVCEL VIKQLKQHQN 2350
TMEDKFIVCL NKIAKGFPPL ADRFLNALFF LLPKFHGVMK TLCLEVVLCR 2400
AEEITGLYLQ LKSKDFLQVM RHRDDERQKV CLDIVYKMVA KLKPIELREL 2450
LNPVVEFVSH PSPTCREQMY NILMWIHDNY RDQESQNDED SQEIFKLAKD 2500
VLIQGLIDEN VGLQLIIRNF WSHETRLPSN TLDRLLALNS LYSPKIEVHF 2550
LSLATNFLLE MTRMSPDYLN PIFEHPLSEC EFQEYTIDPD WRFRSTVLTP 2600
MFIETQASPS ILHTQTQEGP LSDQRQKPGQ VRATQQQYDF TPTQASVERS 2650
SFDWLTGSSI DLLADHTVFS SETLSSSLLF SHKRTEKSQR MSCKSVGPDF 2700
GTKKLGLPDD EVDNQVKSGT PSQADILRLR RRFLKDREKL SLLYAKRGLM 2750
EQKLEKDIKS EFKMKQDAQV VLYRSYRHGD LPDIQIQHSG LITPLQAVAQ 2800
KDPIIAKQLF SSLFSGILKE MNKFKTTSEK NIITQNLLQD FNRFLNTTFL 2850
FFPPFVSCIQ EISCQHPDFL TLDPASVRVG CLASLQQPGG IRLLEEALLR 2900
LMPKEPPTKR VRGKTCLPPD VLRWMELAKL YRSIGEYDVL RGIFSSELGT 2950
TQDTQNALLA EARSDYCQAA KLYDEALNKL EWVDGEPTEA EKEFWELASL 3000
DCYNNLSKWK ELEYCSTVNI VSENSLDLSK MWSEPFYQET YLPYVIRSKL 3050
KLLLQGEGNQ SLLTFVDEAM NKELQKTVLE LQYSQELSLL YILQDDIDRA 3100
TYYIKNGIQI FMQNYSSIDV LLYRSRLAKL QSVQTLAEIE EFLSFICKHG 3150
DLSSLGPLRR LLKTWTSRYP DVVTDPMHIW DDIITNRCFF LSKIEERLTA 3200
PSGDHSMSVD EDEESIDREV YEPKEDVRCM LQSCRFTMKM KMIESAWKQS 3250
NFSLSMKLLK EMHKESKTRE IWRVQWLHSY SQLNHCRSHT QSPREQVLNM 3300
LKTITLLDES DISNYLNKNI QASCDQSILL GTTCRIMADA LSREPACLSD 3350
LEENKVNSIL TLSGSNAENT ETVITGLYQR AFHHLSKAVQ SAEEETQLSC 3400
WGHEAAAERA HAYMTLVGFC DQQLRKVEES ASQKTSAEME AYPALVVEKM 3450
LRALKLNSSE ARLKFPRLLQ IIEQYSEETL NIMTKEISSI PCWQFIGWIS 3500
HMMALLDKEE AIAVQHTVEE IADNYPQAII YPFIISSESY SFKNTSSGHN 3550
NKAFVERIKS KLDHGEVIHS FINALDQLSN PDLLFKDWVS DTKDELGKNP 3600
VNKKNIEKLY ERMYAALGDL RAPGLGPFRR RFIQAFGKEF VKSFGNGGSK 3650
LLTMKVDDFC KITGSLLVRM KKDSKLPGNL KEYSPWMSEF KAQFLKNELE 3700
IPGQYDGKSK PLPEYHVRIS GFDERVKVML SLRKPKRIVI RGHDEKEYPF 3750
LVKGGEDLRQ DQRIEQIFEV MNAILSQDAA CSQRNMQLRT YRVVPMTSRL 3800
GLIEWIENTM TLKDLLLSNM SQEEKVANNS DPKAPIRDYK DWLMKVSGKS 3850
DAGAYVLMYS RANRTETVVA FRRRESQVPP DLLKRAFVKM STSPEAFLAL 3900
RSHFASSHAL LCISHWLLGI GDRHLNNFMV AMETGSVIGI DFGHAFGSAT 3950
QFLPVPELMP FRLTRQFVSL MLPMKETGLM CTVMVHALRA FRSCAGLLTD 4000
TMEIFVKEPS FDWKSFEQTM LRKGGSWIQE INVTEKNWYP QHKIRYAKRK 4050
LAGANPAVIT CDELYLGHEA SSAFRSYTAV ARGNRDYNIR AQEPESGLSE 4100
ETQVKCLVDQ ATDPNILGRT WEGWEPWM 4128
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

Natural variant

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei842 – 85211DEALSLEEIRI → VRNPFLILYLK in isoform 2. VSP_017361Add
BLAST
Alternative sequencei853 – 41283276Missing in isoform 2. VSP_017362Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3300 – 33001M → T in BAA19566. 1 Publication
Sequence conflicti3300 – 33001M → T in BAA28873. 1 Publication
Sequence conflicti3300 – 33001M → T in BAA28875. 1 Publication
Sequence conflicti3300 – 33001M → T in BAB91149. 1 Publication
Sequence conflicti3844 – 38441M → V in AAB36939. 1 Publication
Sequence conflicti3844 – 38441M → V in AAB36940. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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. 4 interactions.
MINTi MINT-4108568.
STRINGi 10090.ENSMUSP00000023352.

Chemistry

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 ENSGT00720000108767.
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.

Miscellaneous databases

NextBioi 295644.
PROi P97313.
SOURCEi Search...

Gene expression databases

ArrayExpressi P97313.
Bgeei P97313.
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: September 3, 2014
This is version 140 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

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