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P13010 (XRCC5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 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 names
Name:XRCC5
Synonyms:G22P2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length732 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. 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. Ref.9 Ref.13 Ref.17 Ref.25

Subunit structure

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. Ref.13 Ref.17 Ref.18 Ref.21 Ref.22 Ref.28

Subcellular location

Nucleus. Nucleusnucleolus. Chromosome Ref.27 Ref.28.

Developmental stage

Expression increases during promyelocyte differentiation. Ref.10

Induction

In osteoblasts, by FGF2.

Domain

The EEXXXDDL motif is required for the interaction with catalytic subunit PRKDC and its recruitment to sites of DNA damage. Ref.20

Post-translational modification

Phosphorylated on serine residues. Phosphorylation by PRKDC may enhance helicase activity. Ref.16

Sumoylated. Ref.19

Ubiquitinated by RNF8 via 'Lys-48'-linked ubiquitination following DNA damage, leading to its degradation and removal from DNA damage sites. Ref.29

Miscellaneous

Individuals with systemic lupus erythematosus (SLE) and related disorders produce extremely large amounts of autoantibodies to XRCC6 and XRCC5.

Sequence similarities

Belongs to the ku80 family.

Contains 1 Ku domain.

Ontologies

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

Traceable author statement Ref.9. Source: GOC

DNA recombination

Traceable author statement PubMed 8073286. Source: ProtInc

DNA repair

Traceable author statement. Source: Reactome

brain development

Inferred from electronic annotation. Source: Ensembl

cell proliferation

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

cellular response to fatty acid

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.25. Source: UniProtKB

establishment of integrated proviral latency

Traceable author statement. Source: Reactome

hematopoietic stem cell differentiation

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

negative regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.13. Source: UniProtKB

positive regulation of neurogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of type I interferon production

Traceable author statement. Source: Reactome

response to drug

Inferred from electronic annotation. Source: Ensembl

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.25. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nonhomologous end joining complex

Inferred from direct assay Ref.25. Source: UniProtKB

nuclear chromosome, telomeric region

Inferred from direct assay PubMed 10535943. Source: BHF-UCL

nuclear telomere cap complex

Traceable author statement PubMed 15100233. Source: BHF-UCL

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent DNA helicase activity

Traceable author statement Ref.9. Source: ProtInc

DNA binding

Non-traceable author statement Ref.14. Source: UniProtKB

damaged DNA binding

Inferred from electronic annotation. Source: InterPro

double-stranded DNA binding

Traceable author statement Ref.9. 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 direct assay PubMed 10535943. Source: BHF-UCL

transcription regulatory region DNA binding

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

ubiquitin protein ligase binding

Inferred from physical interaction Ref.29. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9 Ref.10
Chain2 – 732731X-ray repair cross-complementing protein 5
PRO_0000084340

Regions

Domain251 – 460210Ku
Region138 – 16528Leucine-zipper
Motif720 – 7289EEXXXDL motif
Compositional bias478 – 51942Pro-rich

Amino acid modifications

Modified residue1441N6-acetyllysine Ref.24
Modified residue2651N6-acetyllysine Ref.24
Modified residue3321N6-acetyllysine Ref.24
Modified residue5771Phosphoserine; by PRKDC Ref.16
Modified residue5791Phosphoserine; by PRKDC Probable
Modified residue5801Phosphoserine; by PRKDC Ref.16
Modified residue6601N6-acetyllysine Ref.24
Modified residue6651N6-acetyllysine Ref.24
Modified residue7151Phosphothreonine; by PRKDC Probable

Natural variations

Natural variant4631L → F.
Corresponds to variant rs1805380 [ dbSNP | Ensembl ].
VAR_014724
Natural variant5081I → V.
Corresponds to variant rs2287558 [ dbSNP | Ensembl ].
VAR_053784

Experimental info

Mutagenesis720 – 7212EE → AA: Abolishes interaction with PRKDC and its recruitment to sites of DNA damage. Ref.20
Mutagenesis726 – 7272DD → AA: Abolishes interaction with PRKDC and its recruitment to sites of DNA damage. Ref.20
Sequence conflict14 – 163MDV → YSY AA sequence Ref.10
Sequence conflict1171V → A in BAF83429. Ref.3
Sequence conflict1341I → V in BAD96323. Ref.4
Sequence conflict1781R → S in BAD96323. Ref.4
Sequence conflict3151R → L in CAA40736. Ref.11
Sequence conflict4611M → R AA sequence Ref.10
Sequence conflict4791T → G AA sequence Ref.10
Sequence conflict5401I → T in BAF83429. Ref.3

Secondary structure

................................................................................................................ 732
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13010 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 2363CA84834E74A3

FASTA73282,705
        10         20         30         40         50         60 
MVRSGNKAAV VLCMDVGFTM SNSIPGIESP FEQAKKVITM FVQRQVFAEN KDEIALVLFG 

        70         80         90        100        110        120 
TDGTDNPLSG GDQYQNITVH RHLMLPDFDL LEDIESKIQP GSQQADFLDA LIVSMDVIQH 

       130        140        150        160        170        180 
ETIGKKFEKR HIEIFTDLSS RFSKSQLDII IHSLKKCDIS LQFFLPFSLG KEDGSGDRGD 

       190        200        210        220        230        240 
GPFRLGGHGP SFPLKGITEQ QKEGLEIVKM VMISLEGEDG LDEIYSFSES LRKLCVFKKI 

       250        260        270        280        290        300 
ERHSIHWPCR LTIGSNLSIR IAAYKSILQE RVKKTWTVVD AKTLKKEDIQ KETVYCLNDD 

       310        320        330        340        350        360 
DETEVLKEDI IQGFRYGSDI VPFSKVDEEQ MKYKSEGKCF SVLGFCKSSQ VQRRFFMGNQ 

       370        380        390        400        410        420 
VLKVFAARDD EAAAVALSSL IHALDDLDMV AIVRYAYDKR ANPQVGVAFP HIKHNYECLV 

       430        440        450        460        470        480 
YVQLPFMEDL RQYMFSSLKN SKKYAPTEAQ LNAVDALIDS MSLAKKDEKT DTLEDLFPTT 

       490        500        510        520        530        540 
KIPNPRFQRL FQCLLHRALH PREPLPPIQQ HIWNMLNPPA EVTTKSQIPL SKIKTLFPLI 

       550        560        570        580        590        600 
EAKKKDQVTA QEIFQDNHED GPTAKKLKTE QGGAHFSVSS LAEGSVTSVG SVNPAENFRV 

       610        620        630        640        650        660 
LVKQKKASFE EASNQLINHI EQFLDTNETP YFMKSIDCIR AFREEAIKFS EEQRFNNFLK 

       670        680        690        700        710        720 
ALQEKVEIKQ LNHFWEIVVQ DGITLITKEE ASGSSVTAEE AKKFLAPKDK PSGDTAAVFE 

       730 
EGGDVDDLLD MI 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"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].
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA32626. A35051.
D42397.
S62889.
RefSeqNP_066964.1. NM_021141.3.
UniGeneHs.388739.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JEQX-ray2.70B1-565[»]
1JEYX-ray2.50B1-565[»]
1Q2ZNMR-A592-708[»]
1RW2NMR-A566-709[»]
3RZ9X-ray2.29B559-571[»]
ProteinModelPortalP13010.
SMRP13010. Positions 6-545, 566-710.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113353. 159 interactions.
DIPDIP-31379N.
IntActP13010. 50 interactions.
MINTMINT-131739.
STRING9606.ENSP00000329528.

PTM databases

PhosphoSiteP13010.

Polymorphism databases

DMDM125731.

2D gel databases

SWISS-2DPAGEP13010.

Proteomic databases

PaxDbP13010.
PRIDEP13010.

Protocols and materials databases

DNASU7520.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000392132; ENSP00000375977; ENSG00000079246.
ENST00000392133; ENSP00000375978; ENSG00000079246.
GeneID7520.
KEGGhsa:7520.
UCSCuc002vfy.3. human.

Organism-specific databases

CTD7520.
GeneCardsGC02P216972.
HGNCHGNC:12833. XRCC5.
HPACAB004468.
HPA025813.
MIM194364. gene.
neXtProtNX_P13010.
PharmGKBPA37425.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG299744.
HOVERGENHBG006237.
InParanoidP13010.
KOK10885.
OMAFLPFPIG.
OrthoDBEOG7DVD9X.
PhylomeDBP13010.
TreeFamTF101205.

Enzyme and pathway databases

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

Gene expression databases

ArrayExpressP13010.
BgeeP13010.
CleanExHS_XRCC5.
GenevestigatorP13010.

Family and domain databases

Gene3D1.10.1600.10. 1 hit.
1.25.40.240. 1 hit.
2.40.290.10. 1 hit.
3.40.50.410. 1 hit.
InterProIPR006164. 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]
PANTHERPTHR12604:SF3. PTHR12604:SF3. 1 hit.
PfamPF02735. Ku. 1 hit.
PF03730. Ku_C. 1 hit.
PF03731. Ku_N. 1 hit.
PF08785. Ku_PK_bind. 1 hit.
[Graphical view]
PIRSFPIRSF016570. Ku80. 1 hit.
SMARTSM00559. Ku78. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMSSF100939. SSF100939. 1 hit.
SSF101420. SSF101420. 1 hit.
SSF53300. SSF53300. 1 hit.
ProtoNetSearch...

Other

ChiTaRSXRCC5. human.
EvolutionaryTraceP13010.
GeneWikiKu80.
GenomeRNAi7520.
NextBio29431.
PMAP-CutDBP13010.
PROP13010.
SOURCESearch...

Entry information

Entry nameXRCC5_HUMAN
AccessionPrimary (citable) accession number: P13010
Secondary accession number(s): A8K3X5 expand/collapse secondary AC list , Q0Z7V0, Q4VBQ5, Q53HH7, Q7M4N0, Q9UCQ0, Q9UCQ1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 164 of the entry and version 3 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM