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P12956

- XRCC6_HUMAN

UniProt

P12956 - XRCC6_HUMAN

Protein

X-ray repair cross-complementing protein 6

Gene

XRCC6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 180 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      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.7 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei31 – 311Schiff-base intermediate with DNA; for 5'-deoxyribose-5-phosphate lyase activityCurated

    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: ProtInc
    4. damaged DNA binding Source: InterPro
    5. DNA binding Source: UniProtKB
    6. double-stranded DNA binding Source: ProtInc
    7. poly(A) RNA binding Source: UniProtKB
    8. protein binding Source: UniProtKB
    9. protein C-terminus binding Source: UniProtKB
    10. telomeric DNA binding Source: InterPro
    11. transcription regulatory region DNA binding Source: BHF-UCL

    GO - Biological processi

    1. brain development Source: Ensembl
    2. cellular hyperosmotic salinity response Source: Ensembl
    3. cellular response to X-ray Source: Ensembl
    4. DNA duplex unwinding Source: GOC
    5. DNA ligation Source: ProtInc
    6. DNA repair Source: Reactome
    7. double-strand break repair Source: Reactome
    8. double-strand break repair via nonhomologous end joining Source: UniProtKB
    9. establishment of integrated proviral latency Source: Reactome
    10. innate immune response Source: Reactome
    11. negative regulation of transcription, DNA-templated Source: UniProtKB
    12. positive regulation of neurogenesis Source: Ensembl
    13. positive regulation of transcription, DNA-templated Source: UniProtKB
    14. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    15. positive regulation of type I interferon production Source: Reactome
    16. telomere maintenance Source: BHF-UCL
    17. transcription, DNA-templated Source: UniProtKB-KW
    18. V(D)J recombination Source: Ensembl
    19. viral process Source: Reactome

    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_1022. Nonhomologous End-joining (NHEJ).
    REACT_1201. Processing of DNA ends prior to end rejoining.
    REACT_163993. IRF3-mediated induction of type I IFN.
    REACT_9058. 2-LTR circle formation.

    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 lyase Ku70
    70 kDa subunit of Ku antigen
    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
    Lupus Ku autoantigen protein p70
    Short name:
    Ku70
    Thyroid-lupus autoantigen
    Short name:
    TLAA
    X-ray repair complementing defective repair in Chinese hamster cells 6
    Gene namesi
    Name:XRCC6
    Synonyms:G22P1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:4055. XRCC6.

    Subcellular locationi

    Nucleus 1 Publication. Chromosome 1 Publication

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. Ku70:Ku80 complex Source: UniProtKB
    3. membrane Source: UniProtKB
    4. nonhomologous end joining complex Source: UniProtKB
    5. nuclear telomere cap complex Source: BHF-UCL
    6. nucleolus Source: Ensembl
    7. nucleoplasm Source: Reactome
    8. nucleus Source: HPA
    9. transcription factor complex Source: UniProtKB

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi31 – 311K → A: Diminishes the ability to form a Schiff base. Abolishes adduct formation; when associated with A-160 and A-164. 1 Publication
    Mutagenesisi160 – 1601K → A: Abolishes adduct formation; when associated with A-31 and A-160. 1 Publication
    Mutagenesisi164 – 1641K → A: Abolishes adduct formation; when associated with A-31 and A-164. 1 Publication

    Keywords - Diseasei

    Systemic lupus erythematosus

    Organism-specific databases

    PharmGKBiPA28467.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 609608X-ray repair cross-complementing protein 6PRO_0000210179Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei6 – 61Phosphoserine; by PRKDC2 Publications
    Modified residuei31 – 311N6-acetyllysine1 Publication
    Modified residuei51 – 511Phosphoserine; by PRKDC2 Publications
    Modified residuei331 – 3311N6-acetyllysine1 Publication
    Modified residuei338 – 3381N6-acetyllysine1 Publication
    Modified residuei455 – 4551Phosphothreonine3 Publications
    Modified residuei461 – 4611N6-acetyllysine1 Publication
    Modified residuei477 – 4771Phosphoserine2 Publications
    Modified residuei520 – 5201Phosphoserine2 Publications
    Modified residuei550 – 5501Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylation by PRKDC may enhance helicase activity. Phosphorylation of Ser-51 does not affect DNA repair.7 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP12956.
    PaxDbiP12956.
    PRIDEiP12956.

    2D gel databases

    SWISS-2DPAGEP12956.

    PTM databases

    PhosphoSiteiP12956.

    Miscellaneous databases

    PMAP-CutDBP12956.

    Expressioni

    Developmental stagei

    Expression does not increase during promyelocyte differentiation.1 Publication

    Inductioni

    In osteoblasts, by FGF2.

    Gene expression databases

    ArrayExpressiP12956.
    BgeeiP12956.
    CleanExiHS_XRCC6.
    GenevestigatoriP12956.

    Organism-specific databases

    HPAiCAB004254.
    HPA047549.

    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. Interacts with CLU By similarity. Binds to CDK9 isoform 2. 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 similarity10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARAP1Q96P482EBI-353208,EBI-710003
    BAXQ078122EBI-353208,EBI-516580
    COILP384323EBI-353208,EBI-945751
    HMBOX1Q6NT762EBI-353208,EBI-2549423
    HTTP428583EBI-353208,EBI-466029
    NDRG1Q925972EBI-353208,EBI-716486
    PPIDQ087524EBI-353208,EBI-716596
    PRKDCP785275EBI-353208,EBI-352053
    SIRT1Q96EB67EBI-353208,EBI-1802965
    TCF7L2Q9NQB09EBI-353208,EBI-924724
    TP53P046372EBI-353208,EBI-366083
    WRNQ141914EBI-353208,EBI-368417
    XRCC5P130109EBI-353208,EBI-357997

    Protein-protein interaction databases

    BioGridi108822. 228 interactions.
    DIPiDIP-24188N.
    IntActiP12956. 121 interactions.
    MINTiMINT-1416738.
    STRINGi9606.ENSP00000352257.

    Structurei

    Secondary structure

    1
    609
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi35 – 439
    Helixi46 – 494
    Beta strandi53 – 564
    Helixi59 – 7618
    Beta strandi82 – 898
    Beta strandi102 – 1098
    Helixi113 – 1208
    Helixi124 – 13512
    Helixi143 – 15513
    Beta strandi161 – 17111
    Turni175 – 1784
    Helixi180 – 19617
    Beta strandi198 – 2058
    Turni213 – 2164
    Helixi217 – 2193
    Helixi239 – 25012
    Beta strandi256 – 26611
    Beta strandi268 – 2747
    Beta strandi286 – 2894
    Turni290 – 2923
    Beta strandi295 – 30410
    Turni305 – 3073
    Helixi313 – 3153
    Beta strandi316 – 3227
    Beta strandi325 – 3295
    Helixi331 – 3366
    Beta strandi343 – 35210
    Helixi353 – 3553
    Helixi358 – 3603
    Beta strandi366 – 3705
    Turni372 – 3743
    Helixi378 – 39114
    Beta strandi394 – 4018
    Beta strandi403 – 4053
    Beta strandi409 – 4168
    Beta strandi426 – 4283
    Beta strandi430 – 4367
    Helixi440 – 4423
    Helixi456 – 46813
    Helixi481 – 49414
    Helixi511 – 5188
    Helixi521 – 5299
    Helixi561 – 5699
    Helixi573 – 5753
    Helixi578 – 58710
    Helixi596 – 60712

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JEQX-ray2.70A1-609[»]
    1JEYX-ray2.50A1-609[»]
    1JJRNMR-A556-609[»]
    3RZXX-ray2.61B537-558[»]
    ProteinModelPortaliP12956.
    SMRiP12956. Positions 34-609.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12956.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini261 – 468208KuAdd
    BLAST
    Domaini573 – 60735SAPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni550 – 60960Interaction with DEAF1Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi2 – 6160Ser-rich (potentially targets for phosphorylation)Add
    BLAST
    Compositional biasi11 – 2919Asp/Glu-rich (acidic)Add
    BLAST
    Compositional biasi330 – 34213Asp/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.
    HOGENOMiHOG000006588.
    HOVERGENiHBG006236.
    InParanoidiP12956.
    KOiK10884.
    OMAiCRYTPRK.
    OrthoDBiEOG7QG43F.
    PhylomeDBiP12956.
    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.
    [Graphical view]
    SUPFAMiSSF100939. SSF100939. 1 hit.
    SSF53300. SSF53300. 1 hit.
    TIGRFAMsiTIGR00578. ku70. 1 hit.
    PROSITEiPS50800. SAP. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P12956-1) [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

    MSGWESYYKT EGDEEAEEEQ EENLEASGDY KYSGRDSLIF LVDASKAMFE    50
    SQSEDELTPF DMSIQCIQSV YISKIISSDR DLLAVVFYGT EKDKNSVNFK 100
    NIYVLQELDN PGAKRILELD QFKGQQGQKR FQDMMGHGSD YSLSEVLWVC 150
    ANLFSDVQFK MSHKRIMLFT NEDNPHGNDS AKASRARTKA GDLRDTGIFL 200
    DLMHLKKPGG FDISLFYRDI ISIAEDEDLR VHFEESSKLE DLLRKVRAKE 250
    TRKRALSRLK LKLNKDIVIS VGIYNLVQKA LKPPPIKLYR ETNEPVKTKT 300
    RTFNTSTGGL LLPSDTKRSQ IYGSRQIILE KEETEELKRF DDPGLMLMGF 350
    KPLVLLKKHH YLRPSLFVYP EESLVIGSST LFSALLIKCL EKEVAALCRY 400
    TPRRNIPPYF VALVPQEEEL DDQKIQVTPP GFQLVFLPFA DDKRKMPFTE 450
    KIMATPEQVG KMKAIVEKLR FTYRSDSFEN PVLQQHFRNL EALALDLMEP 500
    EQAVDLTLPK VEAMNKRLGS LVDEFKELVY PPDYNPEGKV TKRKHDNEGS 550
    GSKRPKVEYS EEELKTHISK GTLGKFTVPM LKEACRAYGL KSGLKKQELL 600
    EALTKHFQD 609
    Length:609
    Mass (Da):69,843
    Last modified:January 23, 2007 - v2
    Checksum:iBBD3CD434526DFCB
    GO
    Isoform 2 (identifier: P12956-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         65-105: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:568
    Mass (Da):65,149
    Checksum:iB6DBBED4C80118C1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti20 – 201Q → D AA sequence (PubMed:1537839)Curated
    Sequence conflicti101 – 1011N → K AA sequence (PubMed:8605992)Curated
    Sequence conflicti103 – 1031Y → L AA sequence (PubMed:8605992)Curated
    Sequence conflicti116 – 1161I → S AA sequence (PubMed:8605992)Curated
    Sequence conflicti125 – 1251Q → S AA sequence (PubMed:8605992)Curated
    Sequence conflicti181 – 1811A → T in CAG47015. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei65 – 10541Missing in isoform 2. 1 PublicationVSP_056030Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04607 mRNA. Translation: AAA61177.1.
    J04611 mRNA. Translation: AAA51733.1.
    M32865 mRNA. Translation: AAA36155.1.
    S38729 mRNA. Translation: AAB22381.1.
    AK055786 mRNA. Translation: BAG51575.1.
    CR542219 mRNA. Translation: CAG47015.1.
    AY870329 Genomic DNA. Translation: AAW34364.1.
    Z83840 Genomic DNA. Translation: CAB46206.1.
    CH471095 Genomic DNA. Translation: EAW60448.1.
    BC008343 mRNA. Translation: AAH08343.1.
    BC010034 mRNA. Translation: AAH10034.1.
    BC012154 mRNA. Translation: AAH12154.1.
    BC018259 mRNA. Translation: AAH18259.1.
    BC072449 mRNA. Translation: AAH72449.1.
    CCDSiCCDS14021.1.
    PIRiA30299. A30894.
    RefSeqiNP_001275905.1. NM_001288976.1.
    NP_001275906.1. NM_001288977.1.
    NP_001460.1. NM_001469.4.
    UniGeneiHs.292493.
    Hs.730702.

    Genome annotation databases

    EnsembliENST00000359308; ENSP00000352257; ENSG00000196419.
    ENST00000360079; ENSP00000353192; ENSG00000196419.
    ENST00000402580; ENSP00000384941; ENSG00000196419.
    ENST00000405878; ENSP00000384257; ENSG00000196419.
    GeneIDi2547.
    KEGGihsa:2547.
    UCSCiuc003bao.1. human.

    Polymorphism databases

    DMDMi125729.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04607 mRNA. Translation: AAA61177.1 .
    J04611 mRNA. Translation: AAA51733.1 .
    M32865 mRNA. Translation: AAA36155.1 .
    S38729 mRNA. Translation: AAB22381.1 .
    AK055786 mRNA. Translation: BAG51575.1 .
    CR542219 mRNA. Translation: CAG47015.1 .
    AY870329 Genomic DNA. Translation: AAW34364.1 .
    Z83840 Genomic DNA. Translation: CAB46206.1 .
    CH471095 Genomic DNA. Translation: EAW60448.1 .
    BC008343 mRNA. Translation: AAH08343.1 .
    BC010034 mRNA. Translation: AAH10034.1 .
    BC012154 mRNA. Translation: AAH12154.1 .
    BC018259 mRNA. Translation: AAH18259.1 .
    BC072449 mRNA. Translation: AAH72449.1 .
    CCDSi CCDS14021.1.
    PIRi A30299. A30894.
    RefSeqi NP_001275905.1. NM_001288976.1.
    NP_001275906.1. NM_001288977.1.
    NP_001460.1. NM_001469.4.
    UniGenei Hs.292493.
    Hs.730702.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JEQ X-ray 2.70 A 1-609 [» ]
    1JEY X-ray 2.50 A 1-609 [» ]
    1JJR NMR - A 556-609 [» ]
    3RZX X-ray 2.61 B 537-558 [» ]
    ProteinModelPortali P12956.
    SMRi P12956. Positions 34-609.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108822. 228 interactions.
    DIPi DIP-24188N.
    IntActi P12956. 121 interactions.
    MINTi MINT-1416738.
    STRINGi 9606.ENSP00000352257.

    PTM databases

    PhosphoSitei P12956.

    Polymorphism databases

    DMDMi 125729.

    2D gel databases

    SWISS-2DPAGE P12956.

    Proteomic databases

    MaxQBi P12956.
    PaxDbi P12956.
    PRIDEi P12956.

    Protocols and materials databases

    DNASUi 2547.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000359308 ; ENSP00000352257 ; ENSG00000196419 .
    ENST00000360079 ; ENSP00000353192 ; ENSG00000196419 .
    ENST00000402580 ; ENSP00000384941 ; ENSG00000196419 .
    ENST00000405878 ; ENSP00000384257 ; ENSG00000196419 .
    GeneIDi 2547.
    KEGGi hsa:2547.
    UCSCi uc003bao.1. human.

    Organism-specific databases

    CTDi 2547.
    GeneCardsi GC22P042017.
    HGNCi HGNC:4055. XRCC6.
    HPAi CAB004254.
    HPA047549.
    MIMi 152690. gene.
    neXtProti NX_P12956.
    PharmGKBi PA28467.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG305318.
    HOGENOMi HOG000006588.
    HOVERGENi HBG006236.
    InParanoidi P12956.
    KOi K10884.
    OMAi CRYTPRK.
    OrthoDBi EOG7QG43F.
    PhylomeDBi P12956.
    TreeFami TF315101.

    Enzyme and pathway databases

    Reactomei REACT_1022. Nonhomologous End-joining (NHEJ).
    REACT_1201. Processing of DNA ends prior to end rejoining.
    REACT_163993. IRF3-mediated induction of type I IFN.
    REACT_9058. 2-LTR circle formation.

    Miscellaneous databases

    EvolutionaryTracei P12956.
    GeneWikii Ku70.
    GenomeRNAii 2547.
    NextBioi 10043.
    PMAP-CutDB P12956.
    PROi P12956.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P12956.
    Bgeei P12956.
    CleanExi HS_XRCC6.
    Genevestigatori P12956.

    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.
    [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. "Cloning and characterization of a cDNA that encodes a 70-kDa novel human thyroid autoantigen."
      Chan J.Y., Lerman M.I., Prabhakar B.S., Isozaki O., Santisteban P., Kuppers R.C., Oates E.L., Notkins A.L., Kohn L.D.
      J. Biol. Chem. 264:3651-3654(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Molecular cloning of cDNA encoding the p70 (Ku) lupus autoantigen."
      Reeves W.H., Sthoeger Z.M.
      J. Biol. Chem. 264:5047-5052(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, ROLE IN LUPUS ERYTHEMATOSUS.
    3. "Nucleotide sequence and genomic structure analyses of the p70 subunit of the human Ku autoantigen: evidence for a family of genes encoding Ku (p70)-related polypeptides."
      Griffith A.J., Craft J., Evans J., Mimori T., Hardin J.A.
      Mol. Biol. Rep. 16:91-97(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Kidney.
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. NIEHS SNPs program
      Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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] (ISOFORM 1).
      Tissue: Brain, Kidney, Lung, Placenta and Skin.
    10. "Identification of proteins binding to interferon-inducible transcriptional enhancers in hematopoietic cells."
      Wedrychowski A., Henzel W., Huston L., Paslidis N., Ellerson D., McRae M., Seong D., Howard O.M.Z., Deisseroth A.
      J. Biol. Chem. 267:4533-4540(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 10-30 AND 299-317.
    11. "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: PROTEIN SEQUENCE OF 101-114 AND 116-125, DEVELOPMENTAL STAGE.
      Tissue: Cervix carcinoma.
    12. "The interaction between Ku antigen and REF1 protein mediates negative gene regulation by extracellular calcium."
      Chung U., Igarashi T., Nishishita T., Iwanari H., Iwamatsu A., Suwa A., Mimori T., Hata K., Ebisu S., Ogata E., Fujita T., Okazaki T.
      J. Biol. Chem. 271:8593-8598(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 288-293 AND 300-312, FUNCTION, INTERACTION WITH APEX1.
    13. "Purification of the sequence-specific transcription factor CTCBF, involved in the control of human collagen IV genes: subunits with homology to Ku antigen."
      Genersch E., Eckerskorn C., Lottspeich F., Herzog C., Kuehn K., Poeschl E.
      EMBO J. 14:791-800(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 301-308 AND 556-565.
    14. "Human DNA helicase II: a novel DNA unwinding enzyme identified as the Ku autoantigen."
      Tuteja N., Tuteja R., Ochem A., Taneja P., Huang N.W., Simoncsits A., Susic S., Rahman K., Marusic L., Chen J., Zhang J., Wang S., Pongor S., Falaschi A.
      EMBO J. 13:4991-5001(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 346-352, FUNCTION.
    15. "Double-strand break repair by Ku70 requires heterodimerization with Ku80 and DNA binding functions."
      Jin S., Weaver D.T.
      EMBO J. 16:6874-6885(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-51.
    16. "Productive and nonproductive complexes of Ku and DNA-dependent protein kinase at DNA termini."
      West R.B., Yaneva M., Lieber M.R.
      Mol. Cell. Biol. 18:5908-5920(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PRKDC.
    17. "DNA-dependent protein kinase phosphorylation sites in Ku 70/80 heterodimer."
      Chan D.W., Ye R., Veillette C.J., Lees-Miller S.P.
      Biochemistry 38:1819-1828(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-6.
    18. "Ku, a DNA repair protein with multiple cellular functions?"
      Featherstone C., Jackson S.P.
      Mutat. Res. 434:3-15(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    19. Cited for: INTERACTION WITH XRCC6BP1.
      Tissue: Liver.
    20. "Defining interactions between DNA-PK and ligase IV/XRCC4."
      Hsu H.-L., Yannone S.M., Chen D.J.
      DNA Repair 1:225-235(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRKDC.
    21. "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: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH NAA15; MSX2; RUNX2 AND DLX5.
      Tissue: Heart and Osteoblast.
    22. "Coordinated assembly of Ku and p460 subunits of the DNA-dependent protein kinase on DNA ends is necessary for XRCC4-ligase IV recruitment."
      Calsou P., Delteil C., Frit P., Drouet J., Salles B.
      J. Mol. Biol. 326:93-103(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH G22P2; PRKDC AND XRCC4, PHOSPHORYLATION.
    23. "Positive and negative modulation of the transcriptional activity of the ETS factor ESE-1 through interaction with p300, CREB-binding protein, and Ku 70/86."
      Wang H., Fang R., Cho J.-Y., Libermann T.A., Oettgen P.
      J. Biol. Chem. 279:25241-25250(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ELF3.
    24. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    26. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-520, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    27. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-31; LYS-331; LYS-338 AND LYS-461, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "55K isoform of CDK9 associates with Ku70 and is involved in DNA repair."
      Liu H., Herrmann C.H., Chiang K., Sung T.L., Moon S.H., Donehower L.A., Rice A.P.
      Biochem. Biophys. Res. Commun. 397:245-250(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DNA REPAIR, INTERACTION WITH CDK9.
    29. "Ku is a 5'-dRP/AP lyase that excises nucleotide damage near broken ends."
      Roberts S.A., Strande N., Burkhalter M.D., Strom C., Havener J.M., Hasty P., Ramsden D.A.
      Nature 464:1214-1217(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A 5'-DRP LYASE, MUTAGENESIS OF LYS-31; LYS-160 AND LYS-164.
    30. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-455 AND SER-550, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    31. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    32. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-455, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    33. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    34. "Deformed epidermal autoregulatory factor-1 (DEAF1) interacts with the Ku70 subunit of the DNA-dependent protein kinase complex."
      Jensik P.J., Huggenvik J.I., Collard M.W.
      PLoS ONE 7:E33404-E33404(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING, IDENTIFICATION IN A COMPLEX WITH DEAF1 AND XRCC5, INTERACTION WITH DEAF1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    35. "The three-dimensional structure of the C-terminal DNA-binding domain of human Ku70."
      Zhang Z., Zhu L., Lin D., Chen F., Chen D.J., Chen Y.
      J. Biol. Chem. 276:38231-38236(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 557-610.
    36. "Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair."
      Walker J.R., Corpina R.A., Goldberg J.
      Nature 412:607-614(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 36-609 IN COMPLEX WITH G22P2.

    Entry informationi

    Entry nameiXRCC6_HUMAN
    AccessioniPrimary (citable) accession number: P12956
    Secondary accession number(s): B1AHC8
    , Q6FG89, Q9UCQ2, Q9UCQ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 180 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Individuals with systemic lupus erythematosus (SLE) and related disorders produce extremely large amounts of autoantibodies to XRCC5 and XRCC6. Existence of a major autoantigenic epitope or epitopes on the C-terminal 190 amino acids of XRCC6 containing the leucine repeat. The majority of autoantibodies to XRCC6 in most sera from patients with SLE seem to be reactive with this region.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3