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P13010

- XRCC5_HUMAN

UniProt

P13010 - XRCC5_HUMAN

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Protein

X-ray repair cross-complementing protein 5

Gene
XRCC5, G22P2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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

Nucleus. Nucleusnucleolus. Chromosome 2 Publications

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. Ku70:Ku80 complex Source: UniProtKB
  3. nonhomologous end joining complex Source: UniProtKB
  4. nuclear chromosome, telomeric region Source: BHF-UCL
  5. nuclear telomere cap complex Source: BHF-UCL
  6. nucleoplasm Source: Reactome
  7. nucleus Source: HPA
Complete GO annotation...

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 PRKDC Inferred
Modified residuei580 – 5801Phosphoserine; by PRKDC1 Publication
Modified residuei660 – 6601N6-acetyllysine1 Publication
Modified residuei665 – 6651N6-acetyllysine1 Publication
Modified residuei715 – 7151Phosphothreonine; by PRKDC Inferred

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 XRCC6.6 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. 50 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.

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.
Contains 1 Ku domain.

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

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 conflict

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

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. 50 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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 168 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

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