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P97313

- PRKDC_MOUSE

UniProt

P97313 - PRKDC_MOUSE

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
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    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. 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. 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

    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

    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

    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

    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.
    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.

    « Hide

    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

    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:
    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. 5 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

    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: October 1, 2014
    This is version 141 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