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P13010

- XRCC5_HUMAN

UniProt

P13010 - XRCC5_HUMAN

Protein

X-ray repair cross-complementing protein 5

Gene

XRCC5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 3 (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. In association with NAA15, the XRCC5/6 dimer binds to the osteocalcin promoter and activates osteocalcin expression. The XRCC5/6 dimer 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. XRCC5 probably acts as the catalytic subunit of 5'-dRP activity, and 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.4 Publications

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ATP-dependent DNA helicase activity Source: ProtInc
    3. damaged DNA binding Source: InterPro
    4. DNA binding Source: UniProtKB
    5. double-stranded DNA binding Source: ProtInc
    6. poly(A) RNA binding Source: UniProtKB
    7. protein binding Source: UniProtKB
    8. protein C-terminus binding Source: UniProtKB
    9. telomeric DNA binding Source: BHF-UCL
    10. transcription regulatory region DNA binding Source: BHF-UCL
    11. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. brain development Source: Ensembl
    2. cell proliferation Source: Ensembl
    3. cellular hyperosmotic salinity response Source: Ensembl
    4. cellular response to fatty acid Source: Ensembl
    5. cellular response to X-ray Source: Ensembl
    6. DNA duplex unwinding Source: GOC
    7. DNA recombination Source: ProtInc
    8. DNA repair Source: Reactome
    9. double-strand break repair Source: Reactome
    10. double-strand break repair via nonhomologous end joining Source: UniProtKB
    11. establishment of integrated proviral latency Source: Reactome
    12. hematopoietic stem cell differentiation Source: Ensembl
    13. innate immune response Source: Reactome
    14. negative regulation of transcription, DNA-templated Source: UniProtKB
    15. positive regulation of neurogenesis Source: Ensembl
    16. positive regulation of type I interferon production Source: Reactome
    17. response to drug Source: Ensembl
    18. telomere maintenance Source: BHF-UCL
    19. transcription, DNA-templated Source: UniProtKB-KW
    20. viral process Source: Reactome

    Keywords - Molecular functioni

    Activator, Helicase, Hydrolase

    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 5 (EC:3.6.4.-)
    Alternative name(s):
    86 kDa subunit of Ku antigen
    ATP-dependent DNA helicase 2 subunit 2
    ATP-dependent DNA helicase II 80 kDa subunit
    CTC box-binding factor 85 kDa subunit
    Short name:
    CTC85
    Short name:
    CTCBF
    DNA repair protein XRCC5
    Ku80
    Ku86
    Lupus Ku autoantigen protein p86
    Nuclear factor IV
    Thyroid-lupus autoantigen
    Short name:
    TLAA
    X-ray repair complementing defective repair in Chinese hamster cells 5 (double-strand-break rejoining)
    Gene namesi
    Name:XRCC5
    Synonyms:G22P2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:12833. XRCC5.

    Subcellular locationi

    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 chromosome, telomeric region Source: BHF-UCL
    6. nuclear telomere cap complex Source: BHF-UCL
    7. nucleoplasm Source: Reactome
    8. nucleus Source: HPA

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi720 – 7212EE → AA: Abolishes interaction with PRKDC and its recruitment to sites of DNA damage. 1 Publication
    Mutagenesisi726 – 7272DD → AA: Abolishes interaction with PRKDC and its recruitment to sites of DNA damage. 1 Publication

    Keywords - Diseasei

    Systemic lupus erythematosus

    Organism-specific databases

    PharmGKBiPA37425.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 732731X-ray repair cross-complementing protein 5PRO_0000084340Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei144 – 1441N6-acetyllysine1 Publication
    Modified residuei265 – 2651N6-acetyllysine1 Publication
    Modified residuei332 – 3321N6-acetyllysine1 Publication
    Modified residuei577 – 5771Phosphoserine; by PRKDC1 Publication
    Modified residuei579 – 5791Phosphoserine; by PRKDC1 Publication
    Modified residuei580 – 5801Phosphoserine; by PRKDC1 Publication
    Modified residuei660 – 6601N6-acetyllysine1 Publication
    Modified residuei665 – 6651N6-acetyllysine1 Publication
    Modified residuei715 – 7151Phosphothreonine; by PRKDC1 Publication

    Post-translational modificationi

    Phosphorylated on serine residues. Phosphorylation by PRKDC may enhance helicase activity.1 Publication
    Sumoylated.1 Publication
    Ubiquitinated by RNF8 via 'Lys-48'-linked ubiquitination following DNA damage, leading to its degradation and removal from DNA damage sites.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP13010.
    PaxDbiP13010.
    PRIDEiP13010.

    2D gel databases

    SWISS-2DPAGEP13010.

    PTM databases

    PhosphoSiteiP13010.

    Miscellaneous databases

    PMAP-CutDBP13010.

    Expressioni

    Developmental stagei

    Expression increases during promyelocyte differentiation.1 Publication

    Inductioni

    In osteoblasts, by FGF2.

    Gene expression databases

    ArrayExpressiP13010.
    BgeeiP13010.
    CleanExiHS_XRCC5.
    GenevestigatoriP13010.

    Organism-specific databases

    HPAiCAB004468.
    HPA025813.

    Interactioni

    Subunit structurei

    Heterodimer of a 70 kDa and a 80 kDa 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 displays DNA binding activity towards the osteocalcin FGF response element (OCFRE). In addition, the 80 kDa subunit binds to the osteoblast-specific transcription factors MSX2 and RUNX2. Interacts with ELF3. May interact with APLF. The XRCC5/6 dimer associates in a DNA-dependent manner with APEX1. Identified in a complex with DEAF1 and XRCC6.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    APLFQ8IW1912EBI-357997,EBI-1256044
    COILP384326EBI-357997,EBI-945751
    GOLPH3Q9H4A62EBI-357997,EBI-2465479
    HOXB7P096299EBI-357997,EBI-1248457
    PRKDCP785276EBI-357997,EBI-352053
    XRCC6P129569EBI-357997,EBI-353208

    Protein-protein interaction databases

    BioGridi113353. 168 interactions.
    DIPiDIP-31379N.
    IntActiP13010. 51 interactions.
    MINTiMINT-131739.
    STRINGi9606.ENSP00000329528.

    Structurei

    Secondary structure

    1
    732
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 158
    Helixi18 – 214
    Helixi30 – 4718
    Beta strandi53 – 608
    Turni70 – 723
    Beta strandi77 – 848
    Helixi88 – 958
    Helixi107 – 12115
    Beta strandi122 – 1254
    Beta strandi128 – 1358
    Helixi144 – 1463
    Helixi147 – 15610
    Beta strandi159 – 1679
    Turni194 – 1963
    Helixi199 – 21618
    Helixi218 – 2236
    Beta strandi224 – 2263
    Helixi227 – 2304
    Turni235 – 2373
    Helixi238 – 2403
    Beta strandi247 – 2537
    Turni254 – 2563
    Beta strandi257 – 26711
    Beta strandi277 – 2804
    Turni281 – 2833
    Beta strandi289 – 30113
    Helixi307 – 3093
    Beta strandi310 – 3167
    Beta strandi319 – 3224
    Helixi325 – 3317
    Beta strandi338 – 34710
    Helixi348 – 3503
    Helixi353 – 3553
    Beta strandi357 – 36610
    Helixi371 – 38616
    Beta strandi389 – 40113
    Beta strandi404 – 4129
    Beta strandi417 – 4237
    Helixi427 – 4293
    Beta strandi438 – 4403
    Beta strandi442 – 4443
    Helixi448 – 46013
    Beta strandi464 – 4674
    Turni468 – 4714
    Beta strandi474 – 4763
    Helixi479 – 4813
    Helixi485 – 49915
    Beta strandi501 – 5033
    Helixi510 – 5167
    Helixi520 – 53617
    Beta strandi581 – 5866
    Beta strandi588 – 5925
    Helixi594 – 6018
    Beta strandi603 – 6053
    Turni608 – 6103
    Helixi611 – 62616
    Helixi629 – 64921
    Helixi652 – 66716
    Helixi673 – 6808
    Beta strandi691 – 6933
    Helixi698 – 7014
    Turni702 – 7043

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JEQX-ray2.70B1-565[»]
    1JEYX-ray2.50B1-565[»]
    1Q2ZNMR-A590-709[»]
    1RW2NMR-A566-710[»]
    3RZ9X-ray2.29B559-571[»]
    ProteinModelPortaliP13010.
    SMRiP13010. Positions 6-545, 566-710.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP13010.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini251 – 460210KuAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni138 – 16528Leucine-zipperAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi720 – 7289EEXXXDL motif

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi478 – 51942Pro-richAdd
    BLAST

    Domaini

    The EEXXXDDL motif is required for the interaction with catalytic subunit PRKDC and its recruitment to sites of DNA damage.1 Publication

    Sequence similaritiesi

    Belongs to the ku80 family.Curated
    Contains 1 Ku domain.Curated

    Phylogenomic databases

    eggNOGiNOG299744.
    HOVERGENiHBG006237.
    InParanoidiP13010.
    KOiK10885.
    OMAiFLPFPIG.
    OrthoDBiEOG7DVD9X.
    PhylomeDBiP13010.
    TreeFamiTF101205.

    Family and domain databases

    Gene3Di1.10.1600.10. 1 hit.
    1.25.40.240. 1 hit.
    2.40.290.10. 1 hit.
    3.40.50.410. 1 hit.
    InterProiIPR006164. Ku70/Ku80_beta-barrel_dom.
    IPR024193. Ku80.
    IPR005160. Ku_C.
    IPR005161. Ku_N.
    IPR014893. Ku_PK_bind.
    IPR016194. SPOC_like_C_dom.
    IPR002035. VWF_A.
    [Graphical view]
    PANTHERiPTHR12604:SF3. PTHR12604:SF3. 1 hit.
    PfamiPF02735. Ku. 1 hit.
    PF03730. Ku_C. 1 hit.
    PF03731. Ku_N. 1 hit.
    PF08785. Ku_PK_bind. 1 hit.
    [Graphical view]
    PIRSFiPIRSF016570. Ku80. 1 hit.
    SMARTiSM00559. Ku78. 1 hit.
    SM00327. VWA. 1 hit.
    [Graphical view]
    SUPFAMiSSF100939. SSF100939. 1 hit.
    SSF101420. SSF101420. 1 hit.
    SSF53300. SSF53300. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P13010-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVRSGNKAAV VLCMDVGFTM SNSIPGIESP FEQAKKVITM FVQRQVFAEN    50
    KDEIALVLFG TDGTDNPLSG GDQYQNITVH RHLMLPDFDL LEDIESKIQP 100
    GSQQADFLDA LIVSMDVIQH ETIGKKFEKR HIEIFTDLSS RFSKSQLDII 150
    IHSLKKCDIS LQFFLPFSLG KEDGSGDRGD GPFRLGGHGP SFPLKGITEQ 200
    QKEGLEIVKM VMISLEGEDG LDEIYSFSES LRKLCVFKKI ERHSIHWPCR 250
    LTIGSNLSIR IAAYKSILQE RVKKTWTVVD AKTLKKEDIQ KETVYCLNDD 300
    DETEVLKEDI IQGFRYGSDI VPFSKVDEEQ MKYKSEGKCF SVLGFCKSSQ 350
    VQRRFFMGNQ VLKVFAARDD EAAAVALSSL IHALDDLDMV AIVRYAYDKR 400
    ANPQVGVAFP HIKHNYECLV YVQLPFMEDL RQYMFSSLKN SKKYAPTEAQ 450
    LNAVDALIDS MSLAKKDEKT DTLEDLFPTT KIPNPRFQRL FQCLLHRALH 500
    PREPLPPIQQ HIWNMLNPPA EVTTKSQIPL SKIKTLFPLI EAKKKDQVTA 550
    QEIFQDNHED GPTAKKLKTE QGGAHFSVSS LAEGSVTSVG SVNPAENFRV 600
    LVKQKKASFE EASNQLINHI EQFLDTNETP YFMKSIDCIR AFREEAIKFS 650
    EEQRFNNFLK ALQEKVEIKQ LNHFWEIVVQ DGITLITKEE ASGSSVTAEE 700
    AKKFLAPKDK PSGDTAAVFE EGGDVDDLLD MI 732
    Length:732
    Mass (Da):82,705
    Last modified:January 23, 2007 - v3
    Checksum:i2363CA84834E74A3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 163MDV → YSY AA sequence (PubMed:8605992)Curated
    Sequence conflicti117 – 1171V → A in BAF83429. (PubMed:14702039)Curated
    Sequence conflicti134 – 1341I → V in BAD96323. 1 PublicationCurated
    Sequence conflicti178 – 1781R → S in BAD96323. 1 PublicationCurated
    Sequence conflicti315 – 3151R → L in CAA40736. (PubMed:2212941)Curated
    Sequence conflicti461 – 4611M → R AA sequence (PubMed:8605992)Curated
    Sequence conflicti479 – 4791T → G AA sequence (PubMed:8605992)Curated
    Sequence conflicti540 – 5401I → T in BAF83429. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti463 – 4631L → F.
    Corresponds to variant rs1805380 [ dbSNP | Ensembl ].
    VAR_014724
    Natural varianti508 – 5081I → V.
    Corresponds to variant rs2287558 [ dbSNP | Ensembl ].
    VAR_053784

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04977 mRNA. Translation: AAA59475.1.
    M30938 mRNA. Translation: AAA36154.1.
    AK290740 mRNA. Translation: BAF83429.1.
    AK222603 mRNA. Translation: BAD96323.1.
    DQ787434 Genomic DNA. Translation: ABG46942.1.
    CH471063 Genomic DNA. Translation: EAW70562.1.
    BC019027 mRNA. Translation: AAH19027.1.
    BC095442 mRNA. Translation: AAH95442.1.
    X57500 mRNA. Translation: CAA40736.1.
    CCDSiCCDS2402.1.
    PIRiA35051. A32626.
    D42397.
    S62889.
    RefSeqiNP_066964.1. NM_021141.3.
    UniGeneiHs.388739.

    Genome annotation databases

    EnsembliENST00000392132; ENSP00000375977; ENSG00000079246.
    ENST00000392133; ENSP00000375978; ENSG00000079246.
    GeneIDi7520.
    KEGGihsa:7520.
    UCSCiuc002vfy.3. human.

    Polymorphism databases

    DMDMi125731.

    Keywords - Coding sequence diversityi

    Polymorphism

    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
    J04977 mRNA. Translation: AAA59475.1 .
    M30938 mRNA. Translation: AAA36154.1 .
    AK290740 mRNA. Translation: BAF83429.1 .
    AK222603 mRNA. Translation: BAD96323.1 .
    DQ787434 Genomic DNA. Translation: ABG46942.1 .
    CH471063 Genomic DNA. Translation: EAW70562.1 .
    BC019027 mRNA. Translation: AAH19027.1 .
    BC095442 mRNA. Translation: AAH95442.1 .
    X57500 mRNA. Translation: CAA40736.1 .
    CCDSi CCDS2402.1.
    PIRi A35051. A32626.
    D42397.
    S62889.
    RefSeqi NP_066964.1. NM_021141.3.
    UniGenei Hs.388739.

    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 B 1-565 [» ]
    1JEY X-ray 2.50 B 1-565 [» ]
    1Q2Z NMR - A 590-709 [» ]
    1RW2 NMR - A 566-710 [» ]
    3RZ9 X-ray 2.29 B 559-571 [» ]
    ProteinModelPortali P13010.
    SMRi P13010. Positions 6-545, 566-710.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113353. 168 interactions.
    DIPi DIP-31379N.
    IntActi P13010. 51 interactions.
    MINTi MINT-131739.
    STRINGi 9606.ENSP00000329528.

    PTM databases

    PhosphoSitei P13010.

    Polymorphism databases

    DMDMi 125731.

    2D gel databases

    SWISS-2DPAGE P13010.

    Proteomic databases

    MaxQBi P13010.
    PaxDbi P13010.
    PRIDEi P13010.

    Protocols and materials databases

    DNASUi 7520.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000392132 ; ENSP00000375977 ; ENSG00000079246 .
    ENST00000392133 ; ENSP00000375978 ; ENSG00000079246 .
    GeneIDi 7520.
    KEGGi hsa:7520.
    UCSCi uc002vfy.3. human.

    Organism-specific databases

    CTDi 7520.
    GeneCardsi GC02P216972.
    HGNCi HGNC:12833. XRCC5.
    HPAi CAB004468.
    HPA025813.
    MIMi 194364. gene.
    neXtProti NX_P13010.
    PharmGKBi PA37425.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG299744.
    HOVERGENi HBG006237.
    InParanoidi P13010.
    KOi K10885.
    OMAi FLPFPIG.
    OrthoDBi EOG7DVD9X.
    PhylomeDBi P13010.
    TreeFami TF101205.

    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

    ChiTaRSi XRCC5. human.
    EvolutionaryTracei P13010.
    GeneWikii Ku80.
    GenomeRNAii 7520.
    NextBioi 29431.
    PMAP-CutDB P13010.
    PROi P13010.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P13010.
    Bgeei P13010.
    CleanExi HS_XRCC5.
    Genevestigatori P13010.

    Family and domain databases

    Gene3Di 1.10.1600.10. 1 hit.
    1.25.40.240. 1 hit.
    2.40.290.10. 1 hit.
    3.40.50.410. 1 hit.
    InterProi IPR006164. Ku70/Ku80_beta-barrel_dom.
    IPR024193. Ku80.
    IPR005160. Ku_C.
    IPR005161. Ku_N.
    IPR014893. Ku_PK_bind.
    IPR016194. SPOC_like_C_dom.
    IPR002035. VWF_A.
    [Graphical view ]
    PANTHERi PTHR12604:SF3. PTHR12604:SF3. 1 hit.
    Pfami PF02735. Ku. 1 hit.
    PF03730. Ku_C. 1 hit.
    PF03731. Ku_N. 1 hit.
    PF08785. Ku_PK_bind. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF016570. Ku80. 1 hit.
    SMARTi SM00559. Ku78. 1 hit.
    SM00327. VWA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF100939. SSF100939. 1 hit.
    SSF101420. SSF101420. 1 hit.
    SSF53300. SSF53300. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "cDNA-derived amino acid sequence of the 86-kDa subunit of the Ku antigen."
      Yaneva M., Wen J., Ayala A., Cook R.
      J. Biol. Chem. 264:13407-13411(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 4-22.
    2. "Isolation and characterization of cDNA encoding the 80-kDa subunit protein of the human autoantigen Ku (p70/p80) recognized by autoantibodies from patients with scleroderma-polymyositis overlap syndrome."
      Mimori T., Ohosone Y., Hama N., Suwa A., Akizuki M., Homma M., Griffith A.J., Hardin J.A.
      Proc. Natl. Acad. Sci. U.S.A. 87:1777-1781(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "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].
      Tissue: Neuroblastoma.
    4. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Coronary artery.
    5. NIEHS SNPs program
      Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Thyroid and Uterus.
    8. "Purification and characterization of proximal sequence element-binding protein 1, a transcription activating protein related to Ku and TREF that binds the proximal sequence element of the human U1 promoter."
      Knuth M.W., Gunderson S.I., Thompson N.E., Strasheim L.A., Burgess R.R.
      J. Biol. Chem. 265:17911-17920(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-22.
    9. "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 2-20, FUNCTION, INVOLVEMENT IN LUPUS ERYTHEMATOSUS.
    10. "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 2-16; 98-113; 443-461 AND 473-479, DEVELOPMENTAL STAGE.
      Tissue: Cervix carcinoma.
    11. "The autoantigen Ku is indistinguishable from NF IV, a protein forming multimeric protein-DNA complexes."
      Stuiver M.H., Coenjaerts F.E.J., van der Vlied P.C.
      J. Exp. Med. 172:1049-1054(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 105-732, PARTIAL PROTEIN SEQUENCE.
    12. "DNA-dependent ATPase from HeLa cells is related to human Ku autoantigen."
      Cao Q.P., Pitt S., Leszyk J., Baril E.F.
      Biochemistry 33:8548-8557(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 186-193; 317-326; 545-559 AND 656-661.
    13. "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 526-531; 535-542 AND 704-708, FUNCTION, INTERACTION WITH APEX1.
    14. "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 526-565 AND 709-732.
    15. "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 534-542.
    16. "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-577; SER-579; SER-580 AND THR-715.
    17. "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 AND RUNX2.
      Tissue: Heart and Osteoblast.
    18. "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.
    19. "Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates."
      Gocke C.B., Yu H., Kang J.
      J. Biol. Chem. 280:5004-5012(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION.
    20. "Conserved modes of recruitment of ATM, ATR and DNA-PKcs to sites of DNA damage."
      Falck J., Coates J., Jackson S.P.
      Nature 434:605-611(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN, MUTAGENESIS OF 720-GLU-GLU-721 AND 726-ASP-ASP-727.
    21. "A novel human AP endonuclease with conserved zinc-finger-like motifs involved in DNA strand break responses."
      Kanno S., Kuzuoka H., Sasao S., Hong Z., Lan L., Nakajima S., Yasui A.
      EMBO J. 26:2094-2103(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APLF.
    22. "APLF (C2orf13) is a novel human protein involved in the cellular response to chromosomal DNA strand breaks."
      Iles N., Rulten S., El-Khamisy S.F., Caldecott K.W.
      Mol. Cell. Biol. 27:3793-3803(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APLF.
    23. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    24. "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-144; LYS-265; LYS-332; LYS-660 AND LYS-665, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "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.
    26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "Systematic analysis of protein pools, isoforms, and modifications affecting turnover and subcellular localization."
      Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.
      Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    28. "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 XRCC6 AND DEAF1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    29. "The E3 ligase RNF8 regulates KU80 removal and NHEJ repair."
      Feng L., Chen J.
      Nat. Struct. Mol. Biol. 19:201-206(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION BY RNF8.
    30. "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 7-565 IN COMPLEX WITH XRCC6.

    Entry informationi

    Entry nameiXRCC5_HUMAN
    AccessioniPrimary (citable) accession number: P13010
    Secondary accession number(s): A8K3X5
    , Q0Z7V0, Q4VBQ5, Q53HH7, Q7M4N0, Q9UCQ0, Q9UCQ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 169 of the entry and version 3 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 XRCC6 and XRCC5.

    Keywords - Technical termi

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

    Documents

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

    External Data

    Dasty 3