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P23475

- XRCC6_MOUSE

UniProt

P23475 - XRCC6_MOUSE

Protein

X-ray repair cross-complementing protein 6

Gene

Xrcc6

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 5 (05 Feb 2008)
      Previous versions | rss
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    Functioni

    Single-stranded DNA-dependent ATP-dependent helicase. Has a role in chromosome translocation. The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner. It works in the 3'-5' direction. Binding to DNA may be mediated by XRCC6. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The XRCC5/6 dimer acts as regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold. The XRCC5/6 dimer is probably involved in stabilizing broken DNA ends and bringing them together. The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step. Required for osteocalcin gene expression. Probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site near double-strand breaks. 5'-dRP lyase activity allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined. The XRCC5/6 dimer together with APEX1 acts as a negative regulator of transcription.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei29 – 291Schiff-base intermediate with DNA; for 5'-deoxyribose-5-phosphate lyase activityBy similarity

    GO - Molecular functioni

    1. 5'-deoxyribose-5-phosphate lyase activity Source: UniProtKB
    2. ATP binding Source: UniProtKB-KW
    3. ATP-dependent DNA helicase activity Source: InterPro
    4. damaged DNA binding Source: InterPro
    5. double-stranded telomeric DNA binding Source: Ensembl
    6. transcription regulatory region DNA binding Source: Ensembl

    GO - Biological processi

    1. brain development Source: Ensembl
    2. cellular hyperosmotic salinity response Source: Ensembl
    3. cellular response to DNA damage stimulus Source: MGI
    4. cellular response to X-ray Source: Ensembl
    5. double-strand break repair Source: MGI
    6. double-strand break repair via nonhomologous end joining Source: UniProtKB
    7. negative regulation of transcription, DNA-templated Source: UniProtKB
    8. positive regulation of neurogenesis Source: MGI
    9. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    10. response to ionizing radiation Source: MGI
    11. telomere maintenance Source: InterPro
    12. transcription, DNA-templated Source: UniProtKB-KW
    13. V(D)J recombination Source: MGI

    Keywords - Molecular functioni

    Activator, Helicase, Hydrolase, Lyase

    Keywords - Biological processi

    DNA damage, DNA recombination, DNA repair, Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, DNA-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:
    X-ray repair cross-complementing protein 6 (EC:3.6.4.-, EC:4.2.99.-)
    Alternative name(s):
    5'-deoxyribose-5-phosphate lyase Ku70
    Short name:
    5'-dRP/AP lyase Ku70
    ATP-dependent DNA helicase 2 subunit 1
    ATP-dependent DNA helicase II 70 kDa subunit
    CTC box-binding factor 75 kDa subunit
    Short name:
    CTC75
    Short name:
    CTCBF
    DNA repair protein XRCC6
    Ku autoantigen protein p70 homolog
    Short name:
    Ku70
    Gene namesi
    Name:Xrcc6
    Synonyms:G22p1, Ku70
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:95606. Xrcc6.

    Subcellular locationi

    GO - Cellular componenti

    1. chromosome Source: UniProtKB-SubCell
    2. cytoplasm Source: MGI
    3. Ku70:Ku80 complex Source: UniProtKB
    4. nonhomologous end joining complex Source: UniProtKB
    5. nucleolus Source: Ensembl
    6. nucleus Source: MGI
    7. transcription factor complex Source: Ensembl

    Keywords - Cellular componenti

    Chromosome, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 608607X-ray repair cross-complementing protein 6PRO_0000210180Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei6 – 61Phosphoserine; by PRKDCBy similarity
    Modified residuei29 – 291N6-acetyllysineBy similarity
    Modified residuei49 – 491Phosphoserine; by PRKDCBy similarity
    Modified residuei329 – 3291N6-acetyllysineBy similarity
    Modified residuei336 – 3361N6-acetyllysineBy similarity
    Modified residuei459 – 4591N6-acetyllysineBy similarity
    Modified residuei475 – 4751PhosphoserineBy similarity
    Modified residuei518 – 5181PhosphoserineBy similarity
    Modified residuei548 – 5481PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylation by PRKDC may enhance helicase activity. Phosphorylation of Ser-49 does not affect DNA repair By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP23475.
    PaxDbiP23475.
    PRIDEiP23475.

    PTM databases

    PhosphoSiteiP23475.

    Expressioni

    Developmental stagei

    Expression increases during promyelocyte differentiation.1 Publication

    Gene expression databases

    ArrayExpressiP23475.
    BgeeiP23475.
    GenevestigatoriP23475.

    Interactioni

    Subunit structurei

    Heterodimer of a 70 kDa (XRCC6) and a 80 kDa (XRCC5) subunit. The dimer associates in a DNA-dependent manner with PRKDC to form the DNA-dependent protein kinase complex DNA-PK, and with the LIG4-XRCC4 complex. The dimer also associates with NAA15, and this complex binds to the osteocalcin promoter and activates osteocalcin expression. In addition, XRCC6 interacts with the osteoblast-specific transcription factors MSX2, RUNX2 and DLX5. Interacts with ELF3. Interacts with XRCC6BP1. The XRCC5/6 dimer associates in a DNA-dependent manner with APEX1. Binds to CDK9 By similarity. Identified in a complex with DEAF1 and XRCC5. Interacts with DEAF1 (via the SAND domain); the interaction is direct and may be inhibited by DNA-binding By similarity. Interacts with CLU.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi199785. 4 interactions.
    IntActiP23475. 4 interactions.
    MINTiMINT-2568472.

    Structurei

    3D structure databases

    ProteinModelPortaliP23475.
    SMRiP23475. Positions 32-606.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini259 – 466208KuAdd
    BLAST
    Domaini571 – 60535SAPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni548 – 60760Interaction with DEAF1By similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi11 – 2717Asp/Glu-rich (acidic)Add
    BLAST
    Compositional biasi328 – 34013Asp/Glu-rich (acidic)Add
    BLAST

    Sequence similaritiesi

    Belongs to the ku70 family.Curated
    Contains 1 Ku domain.Curated
    Contains 1 SAP domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG305318.
    GeneTreeiENSGT00390000001422.
    HOVERGENiHBG006236.
    InParanoidiP23475.
    KOiK10884.
    OrthoDBiEOG7QG43F.
    TreeFamiTF315101.

    Family and domain databases

    Gene3Di1.10.1600.10. 1 hit.
    1.10.720.30. 1 hit.
    2.40.290.10. 1 hit.
    3.40.50.410. 1 hit.
    4.10.970.10. 1 hit.
    InterProiIPR006165. Ku70.
    IPR006164. Ku70/Ku80_beta-barrel_dom.
    IPR027388. Ku70_bridge/pillars_dom.
    IPR005160. Ku_C.
    IPR005161. Ku_N.
    IPR003034. SAP_dom.
    IPR016194. SPOC_like_C_dom.
    IPR002035. VWF_A.
    [Graphical view]
    PANTHERiPTHR12604:SF2. PTHR12604:SF2. 1 hit.
    PfamiPF02735. Ku. 1 hit.
    PF03730. Ku_C. 1 hit.
    PF03731. Ku_N. 1 hit.
    PF02037. SAP. 1 hit.
    [Graphical view]
    PIRSFiPIRSF003033. Ku70. 1 hit.
    SMARTiSM00559. Ku78. 1 hit.
    SM00513. SAP. 1 hit.
    SM00327. VWA. 1 hit.
    [Graphical view]
    SUPFAMiSSF100939. SSF100939. 1 hit.
    SSF53300. SSF53300. 1 hit.
    TIGRFAMsiTIGR00578. ku70. 1 hit.
    PROSITEiPS50800. SAP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P23475-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEWESYYKT EGEEEEEEEE SPDTGGEYKY SGRDSLIFLV DASRAMFESQ    50
    GEDELTPFDM SIQCIQSVYT SKIISSDRDL LAVVFYGTEK DKNSVNFKNI 100
    YVLQDLDNPG AKRVLELDQF KGQQGKKHFR DTVGHGSDYS LSEVLWVCAN 150
    LFSDVQLKMS HKRIMLFTNE DDPHGRDSAK ASRARTKASD LRDTGIFLDL 200
    MHLKKPGGFD VSVFYRDIIT TAEDEDLGVH FEESSKLEDL LRKVRAKETK 250
    KRVLSRLKFK LGEDVVLMVG IYNLVQKANK PFPVRLYRET NEPVKTKTRT 300
    FNVNTGSLLL PSDTKRSLTY GTRQIVLEKE ETEELKRFDE PGLILMGFKP 350
    TVMLKKQHYL RPSLFVYPEE SLVSGSSTLF SALLTKCVEK KVIAVCRYTP 400
    RKNVSPYFVA LVPQEEELDD QNIQVTPGGF QLVFLPYADD KRKVPFTEKV 450
    TANQEQIDKM KAIVQKLRFT YRSDSFENPV LQQHFRNLEA LALDMMESEQ 500
    VVDLTLPKVE AIKKRLGSLA DEFKELVYPP GYNPEGKVAK RKQDDEGSTS 550
    KKPKVELSEE ELKAHFRKGT LGKLTVPTLK DICKAHGLKS GPKKQELLDA 600
    LIRHLEKN 608
    Length:608
    Mass (Da):69,484
    Last modified:February 5, 2008 - v5
    Checksum:i1C27DBF1DB7A1154
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti225 – 2251E → G in BAE27139. (PubMed:16141072)Curated
    Sequence conflicti225 – 2251E → G in BAE27137. (PubMed:16141072)Curated
    Sequence conflicti225 – 2251E → G in BAE27135. (PubMed:16141072)Curated
    Sequence conflicti391 – 3911K → E in BAE25441. (PubMed:11471062)Curated
    Sequence conflicti391 – 3911K → E in AAL90775. (PubMed:11471062)Curated
    Sequence conflicti391 – 3911K → E in AAL90774. (PubMed:11471062)Curated
    Sequence conflicti400 – 4001P → H in AAA39396. (PubMed:1701785)Curated
    Sequence conflicti466 – 4672KL → NV in AAC52675. (PubMed:8661113)Curated
    Sequence conflicti466 – 4672KL → NV in AAA39396. (PubMed:1701785)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U50378
    , U50367, U50368, U50369, U50370, U50371, U50372, U50373, U50374, U50375, U50376, U50377 Genomic DNA. Translation: AAC52675.1.
    U34878 Genomic DNA. Translation: AAC53575.1.
    AB010282 mRNA. Translation: BAA28874.1.
    AF483500 mRNA. Translation: AAL90774.1.
    AF483501 mRNA. Translation: AAL90775.1.
    AK143570 mRNA. Translation: BAE25441.1.
    AK146392 mRNA. Translation: BAE27135.1.
    AK146394 mRNA. Translation: BAE27137.1.
    AK146396 mRNA. Translation: BAE27139.1.
    BC031422 mRNA. Translation: AAH31422.1.
    Z14157 mRNA. Translation: CAA78526.1.
    M38700 mRNA. Translation: AAA39396.1.
    CCDSiCCDS37153.1.
    PIRiA43534.
    S25149.
    RefSeqiNP_034377.2. NM_010247.2.
    XP_006520503.1. XM_006520440.1.
    XP_006520504.1. XM_006520441.1.
    XP_006520505.1. XM_006520442.1.
    XP_006520506.1. XM_006520443.1.
    UniGeneiMm.288809.

    Genome annotation databases

    EnsembliENSMUST00000069530; ENSMUSP00000068559; ENSMUSG00000022471.
    ENSMUST00000100399; ENSMUSP00000097968; ENSMUSG00000022471.
    GeneIDi14375.
    KEGGimmu:14375.
    UCSCiuc007wxy.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U50378
    , U50367 , U50368 , U50369 , U50370 , U50371 , U50372 , U50373 , U50374 , U50375 , U50376 , U50377 Genomic DNA. Translation: AAC52675.1 .
    U34878 Genomic DNA. Translation: AAC53575.1 .
    AB010282 mRNA. Translation: BAA28874.1 .
    AF483500 mRNA. Translation: AAL90774.1 .
    AF483501 mRNA. Translation: AAL90775.1 .
    AK143570 mRNA. Translation: BAE25441.1 .
    AK146392 mRNA. Translation: BAE27135.1 .
    AK146394 mRNA. Translation: BAE27137.1 .
    AK146396 mRNA. Translation: BAE27139.1 .
    BC031422 mRNA. Translation: AAH31422.1 .
    Z14157 mRNA. Translation: CAA78526.1 .
    M38700 mRNA. Translation: AAA39396.1 .
    CCDSi CCDS37153.1.
    PIRi A43534.
    S25149.
    RefSeqi NP_034377.2. NM_010247.2.
    XP_006520503.1. XM_006520440.1.
    XP_006520504.1. XM_006520441.1.
    XP_006520505.1. XM_006520442.1.
    XP_006520506.1. XM_006520443.1.
    UniGenei Mm.288809.

    3D structure databases

    ProteinModelPortali P23475.
    SMRi P23475. Positions 32-606.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199785. 4 interactions.
    IntActi P23475. 4 interactions.
    MINTi MINT-2568472.

    PTM databases

    PhosphoSitei P23475.

    Proteomic databases

    MaxQBi P23475.
    PaxDbi P23475.
    PRIDEi P23475.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000069530 ; ENSMUSP00000068559 ; ENSMUSG00000022471 .
    ENSMUST00000100399 ; ENSMUSP00000097968 ; ENSMUSG00000022471 .
    GeneIDi 14375.
    KEGGi mmu:14375.
    UCSCi uc007wxy.1. mouse.

    Organism-specific databases

    CTDi 2547.
    MGIi MGI:95606. Xrcc6.

    Phylogenomic databases

    eggNOGi NOG305318.
    GeneTreei ENSGT00390000001422.
    HOVERGENi HBG006236.
    InParanoidi P23475.
    KOi K10884.
    OrthoDBi EOG7QG43F.
    TreeFami TF315101.

    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 285869.
    PROi P23475.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P23475.
    Bgeei P23475.
    Genevestigatori P23475.

    Family and domain databases

    Gene3Di 1.10.1600.10. 1 hit.
    1.10.720.30. 1 hit.
    2.40.290.10. 1 hit.
    3.40.50.410. 1 hit.
    4.10.970.10. 1 hit.
    InterProi IPR006165. Ku70.
    IPR006164. Ku70/Ku80_beta-barrel_dom.
    IPR027388. Ku70_bridge/pillars_dom.
    IPR005160. Ku_C.
    IPR005161. Ku_N.
    IPR003034. SAP_dom.
    IPR016194. SPOC_like_C_dom.
    IPR002035. VWF_A.
    [Graphical view ]
    PANTHERi PTHR12604:SF2. PTHR12604:SF2. 1 hit.
    Pfami PF02735. Ku. 1 hit.
    PF03730. Ku_C. 1 hit.
    PF03731. Ku_N. 1 hit.
    PF02037. SAP. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF003033. Ku70. 1 hit.
    SMARTi SM00559. Ku78. 1 hit.
    SM00513. SAP. 1 hit.
    SM00327. VWA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF100939. SSF100939. 1 hit.
    SSF53300. SSF53300. 1 hit.
    TIGRFAMsi TIGR00578. ku70. 1 hit.
    PROSITEi PS50800. SAP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genomic structure and chromosomal assignment of the mouse Ku70 gene."
      Takiguchi Y., Kurimasa A., Chen F., Pardington P.E., Kuriyama T., Okinaka R.T., Moyzis R., Chen D.J.
      Genomics 35:129-135(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129.
    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].
      Tissue: Mammary carcinoma.
    3. "High-throughput sequence identification of gene coding variants within alcohol-related QTLs."
      Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.
      Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: ILS and ISS.
    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].
      Strain: C57BL/6J and DBA/2.
      Tissue: Spleen.
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Mammary tumor.
    6. "Nucleotide sequence of the 5' region of the murine p70 Ku autoantigen cDNA."
      Baughman G.A., Nemeth J.E., Bourgeois S.
      Submitted (AUG-1992) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-46.
      Strain: BALB/c.
      Tissue: Thymus.
    7. "Antigenic determinants of the Ku (p70/p80) autoantigen are poorly conserved between species."
      Porges A.J., Ng T., Reeves W.H.
      J. Immunol. 145:4222-4228(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 18-608.
    8. "Non-histone protein 1 (NHP1) is a member of the Ku protein family which is upregulated in differentiating mouse myoblasts and human promyelocytes."
      Oderwald H., Hughes M.J., Jost J.-P.
      FEBS Lett. 382:313-318(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.
    9. "Regulation of osteocalcin gene expression by a novel Ku antigen transcription factor complex."
      Willis D.M., Loewy A.P., Charlton-Kachigian N., Shao J.-S., Ornitz D.M., Towler D.A.
      J. Biol. Chem. 277:37280-37291(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Tissue: Osteoblast.
    10. "Synthesis and functional analyses of nuclear clusterin, a cell death protein."
      Leskov K.S., Klokov D.Y., Li J., Kinsella T.J., Boothman D.A.
      J. Biol. Chem. 278:11590-11600(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CLU.

    Entry informationi

    Entry nameiXRCC6_MOUSE
    AccessioniPrimary (citable) accession number: P23475
    Secondary accession number(s): O88212
    , Q3UJL8, Q62027, Q62382, Q62453, Q6GTV8, Q8QZX7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 139 of the entry and version 5 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    In osteoblasts from XRCC6 knockout mice, osteocalcin gene expression is nearly abolished.

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3