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P12956 (XRCC6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 175. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:XRCC6
Synonyms:G22P1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length609 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.10 Ref.12 Ref.14 Ref.19 Ref.26 Ref.27

Subunit structure

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. Ref.10 Ref.14 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.26 Ref.32

Subcellular location

Nucleus. Chromosome Ref.32.

Developmental stage

Expression does not increase during promyelocyte differentiation. Ref.9

Induction

In osteoblasts, by FGF2.

Post-translational modification

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

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.

Sequence similarities

Belongs to the ku70 family.

Contains 1 Ku domain.

Contains 1 SAP domain.

Ontologies

Keywords
   Biological processDNA damage
DNA recombination
DNA repair
Transcription
Transcription regulation
   Cellular componentChromosome
Nucleus
   DiseaseSystemic lupus erythematosus
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionActivator
Helicase
Hydrolase
Lyase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processDNA duplex unwinding

Traceable author statement Ref.12. Source: GOC

DNA ligation

Traceable author statement PubMed 9826654. Source: ProtInc

DNA repair

Traceable author statement. Source: Reactome

V(D)J recombination

Inferred from electronic annotation. Source: Ensembl

brain development

Inferred from electronic annotation. Source: Ensembl

cellular hyperosmotic salinity response

Inferred from electronic annotation. Source: Ensembl

cellular response to X-ray

Inferred from electronic annotation. Source: Ensembl

double-strand break repair

Traceable author statement. Source: Reactome

double-strand break repair via nonhomologous end joining

Inferred from mutant phenotype Ref.27. Source: UniProtKB

establishment of integrated proviral latency

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

negative regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.10. Source: UniProtKB

positive regulation of neurogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 18809223. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.19. Source: UniProtKB

positive regulation of type I interferon production

Traceable author statement. Source: Reactome

telomere maintenance

Traceable author statement PubMed 15824061. Source: BHF-UCL

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

viral process

Traceable author statement. Source: Reactome

   Cellular_componentKu70:Ku80 complex

Inferred from direct assay Ref.27. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

membrane

Traceable author statement Ref.1. Source: ProtInc

nonhomologous end joining complex

Inferred from direct assay Ref.27. Source: UniProtKB

nuclear telomere cap complex

Traceable author statement PubMed 15100233. Source: BHF-UCL

nucleolus

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

transcription factor complex

Inferred from direct assay Ref.19. Source: UniProtKB

   Molecular_function5'-deoxyribose-5-phosphate lyase activity

Inferred from mutant phenotype Ref.27. Source: UniProtKB

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent DNA helicase activity

Traceable author statement Ref.12. Source: ProtInc

DNA binding

Non-traceable author statement Ref.8. Source: UniProtKB

damaged DNA binding

Inferred from electronic annotation. Source: InterPro

double-stranded DNA binding

Traceable author statement Ref.12. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein C-terminus binding

Inferred from physical interaction PubMed 10783163. Source: UniProtKB

telomeric DNA binding

Inferred from electronic annotation. Source: InterPro

transcription regulatory region DNA binding

Inferred from direct assay PubMed 18809223. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.23
Chain2 – 609608X-ray repair cross-complementing protein 6
PRO_0000210179

Regions

Domain261 – 468208Ku
Domain573 – 60735SAP
Region550 – 60960Interaction with DEAF1
Compositional bias2 – 6160Ser-rich (potentially targets for phosphorylation)
Compositional bias11 – 2919Asp/Glu-rich (acidic)
Compositional bias330 – 34213Asp/Glu-rich (acidic)

Sites

Active site311Schiff-base intermediate with DNA; for 5'-deoxyribose-5-phosphate lyase activity Probable

Amino acid modifications

Modified residue21N-acetylserine Ref.23 Ref.31
Modified residue61Phosphoserine; by PRKDC Ref.15
Modified residue311N6-acetyllysine Ref.25
Modified residue511Phosphoserine; by PRKDC Ref.13
Modified residue3311N6-acetyllysine Ref.25
Modified residue3381N6-acetyllysine Ref.25
Modified residue4551Phosphothreonine Ref.28 Ref.30
Modified residue4611N6-acetyllysine Ref.25
Modified residue4771Phosphoserine Ref.22
Modified residue5201Phosphoserine Ref.24
Modified residue5501Phosphoserine Ref.28

Experimental info

Mutagenesis311K → A: Diminishes the ability to form a Schiff base. Abolishes adduct formation; when associated with A-160 and A-164. Ref.27
Mutagenesis1601K → A: Abolishes adduct formation; when associated with A-31 and A-160. Ref.27
Mutagenesis1641K → A: Abolishes adduct formation; when associated with A-31 and A-164. Ref.27
Sequence conflict201Q → D AA sequence Ref.8
Sequence conflict1011N → K AA sequence Ref.9
Sequence conflict1031Y → L AA sequence Ref.9
Sequence conflict1161I → S AA sequence Ref.9
Sequence conflict1251Q → S AA sequence Ref.9
Sequence conflict1811A → T in CAG47015. Ref.4

Secondary structure

........................................................................................ 609
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12956 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: BBD3CD434526DFCB

FASTA60969,843
        10         20         30         40         50         60 
MSGWESYYKT EGDEEAEEEQ EENLEASGDY KYSGRDSLIF LVDASKAMFE SQSEDELTPF 

        70         80         90        100        110        120 
DMSIQCIQSV YISKIISSDR DLLAVVFYGT EKDKNSVNFK NIYVLQELDN PGAKRILELD 

       130        140        150        160        170        180 
QFKGQQGQKR FQDMMGHGSD YSLSEVLWVC ANLFSDVQFK MSHKRIMLFT NEDNPHGNDS 

       190        200        210        220        230        240 
AKASRARTKA GDLRDTGIFL DLMHLKKPGG FDISLFYRDI ISIAEDEDLR VHFEESSKLE 

       250        260        270        280        290        300 
DLLRKVRAKE TRKRALSRLK LKLNKDIVIS VGIYNLVQKA LKPPPIKLYR ETNEPVKTKT 

       310        320        330        340        350        360 
RTFNTSTGGL LLPSDTKRSQ IYGSRQIILE KEETEELKRF DDPGLMLMGF KPLVLLKKHH 

       370        380        390        400        410        420 
YLRPSLFVYP EESLVIGSST LFSALLIKCL EKEVAALCRY TPRRNIPPYF VALVPQEEEL 

       430        440        450        460        470        480 
DDQKIQVTPP GFQLVFLPFA DDKRKMPFTE KIMATPEQVG KMKAIVEKLR FTYRSDSFEN 

       490        500        510        520        530        540 
PVLQQHFRNL EALALDLMEP EQAVDLTLPK VEAMNKRLGS LVDEFKELVY PPDYNPEGKV 

       550        560        570        580        590        600 
TKRKHDNEGS GSKRPKVEYS EEELKTHISK GTLGKFTVPM LKEACRAYGL KSGLKKQELL 


EALTKHFQD 

« Hide

References

« Hide 'large scale' references
[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].
[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], 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].
[4]"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].
[5]NIEHS SNPs program
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"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. expand/collapse author list , 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].
[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: Brain, Kidney, Lung, Placenta and Skin.
[8]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"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.
[14]"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.
[15]"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.
[16]"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.
[17]"Isolation of Ku70-binding proteins (KUBs)."
Yang C.-R., Yeh S.-Y., Leskov K., Odegaard E., Hsu H.L., Chang C., Kinsella T.J., Chen D.J., Boothman D.A.
Nucleic Acids Res. 27:2165-2174(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH XRCC6BP1.
Tissue: Liver.
[18]"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.
[19]"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.
[20]"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.
[21]"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.
[22]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"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].
[24]"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.
[25]"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].
[26]"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.
[27]"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.
[28]"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.
[29]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"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].
[31]"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].
[32]"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.
[33]"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.
[34]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04607 mRNA. Translation: AAA61177.1.
J04611 mRNA. Translation: AAA51733.1.
M32865 mRNA. Translation: AAA36155.1.
S38729 mRNA. Translation: AAB22381.1.
CR542219 mRNA. Translation: CAG47015.1.
AY870329 Genomic DNA. Translation: AAW34364.1.
Z83840 Genomic DNA. Translation: CAB46206.1.
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.
PIRA30894. A30299.
RefSeqNP_001275905.1. NM_001288976.1.
NP_001460.1. NM_001469.4.
UniGeneHs.292493.
Hs.730702.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JEQX-ray2.70A1-609[»]
1JEYX-ray2.50A1-609[»]
1JJRNMR-A536-609[»]
3RZXX-ray2.61B537-558[»]
ProteinModelPortalP12956.
SMRP12956. Positions 34-609.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108822. 225 interactions.
DIPDIP-24188N.
IntActP12956. 121 interactions.
MINTMINT-1416738.
STRING9606.ENSP00000352257.

PTM databases

PhosphoSiteP12956.

Polymorphism databases

DMDM125729.

2D gel databases

SWISS-2DPAGEP12956.

Proteomic databases

PaxDbP12956.
PRIDEP12956.

Protocols and materials databases

DNASU2547.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359308; ENSP00000352257; ENSG00000196419.
ENST00000360079; ENSP00000353192; ENSG00000196419.
ENST00000405878; ENSP00000384257; ENSG00000196419.
GeneID2547.
KEGGhsa:2547.
UCSCuc003bao.1. human.

Organism-specific databases

CTD2547.
GeneCardsGC22P042017.
HGNCHGNC:4055. XRCC6.
HPACAB004254.
HPA047549.
MIM152690. gene.
neXtProtNX_P12956.
PharmGKBPA28467.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG305318.
HOGENOMHOG000006588.
HOVERGENHBG006236.
InParanoidP12956.
KOK10884.
OMACRYTPRK.
OrthoDBEOG7QG43F.
PhylomeDBP12956.
TreeFamTF315101.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_216. DNA Repair.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP12956.
BgeeP12956.
CleanExHS_XRCC6.
GenevestigatorP12956.

Family and domain databases

Gene3D1.10.1600.10. 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.
InterProIPR006165. 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]
PANTHERPTHR12604:SF2. PTHR12604:SF2. 1 hit.
PfamPF02735. Ku. 1 hit.
PF03730. Ku_C. 1 hit.
PF03731. Ku_N. 1 hit.
PF02037. SAP. 1 hit.
[Graphical view]
PIRSFPIRSF003033. Ku70. 1 hit.
SMARTSM00559. Ku78. 1 hit.
SM00513. SAP. 1 hit.
[Graphical view]
SUPFAMSSF100939. SSF100939. 1 hit.
SSF53300. SSF53300. 1 hit.
TIGRFAMsTIGR00578. ku70. 1 hit.
PROSITEPS50800. SAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP12956.
GeneWikiKu70.
GenomeRNAi2547.
NextBio10043.
PMAP-CutDBP12956.
PROP12956.
SOURCESearch...

Entry information

Entry nameXRCC6_HUMAN
AccessionPrimary (citable) accession number: P12956
Secondary accession number(s): Q6FG89, Q9UCQ2, Q9UCQ3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 175 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM