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Protein

X-ray repair cross-complementing protein 5

Gene

XRCC5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 (PubMed:12145306, PubMed:20383123, PubMed:7957065, PubMed:8621488). 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 (PubMed:20383123). 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 (PubMed:8621488).4 Publications

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent DNA helicase activity Source: ProtInc
  • damaged DNA binding Source: GO_Central
  • DNA binding Source: UniProtKB
  • double-stranded DNA binding Source: ProtInc
  • macromolecular complex binding Source: BHF-UCL
  • poly(A) RNA binding Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB
  • telomeric DNA binding Source: BHF-UCL
  • transcription regulatory region DNA binding Source: BHF-UCL
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  • cell proliferation Source: Ensembl
  • cellular response to gamma radiation Source: GO_Central
  • cellular response to X-ray Source: GO_Central
  • DNA recombination Source: ProtInc
  • double-strand break repair Source: BHF-UCL
  • double-strand break repair via nonhomologous end joining Source: UniProtKB
  • establishment of integrated proviral latency Source: Reactome
  • hematopoietic stem cell differentiation Source: Ensembl
  • negative regulation of t-circle formation Source: BHF-UCL
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of neurogenesis Source: Ensembl
  • positive regulation of type I interferon production Source: Reactome
  • regulation of smooth muscle cell proliferation Source: UniProtKB
  • telomere maintenance Source: BHF-UCL
  • transcription, DNA-templated Source: UniProtKB-KW
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

ReactomeiR-HSA-164843. 2-LTR circle formation.
R-HSA-1834949. Cytosolic sensors of pathogen-associated DNA.
R-HSA-3270619. IRF3-mediated induction of type I IFN.
R-HSA-5693571. Nonhomologous End-Joining (NHEJ).
SIGNORiP13010.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:12833. XRCC5.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • Ku70:Ku80 complex Source: UniProtKB
  • membrane Source: UniProtKB
  • nonhomologous end joining complex Source: UniProtKB
  • nuclear chromosome, telomeric region Source: BHF-UCL
  • nuclear telomere cap complex Source: BHF-UCL
  • nucleolus Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • nucleus Source: HPA
  • plasma membrane 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.

Polymorphism and mutation databases

BioMutaiXRCC5.
DMDMi125731.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 732731X-ray repair cross-complementing protein 5PRO_0000084340Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei144 – 1441N6-acetyllysineCombined sources
Modified residuei255 – 2551PhosphoserineCombined sources
Modified residuei258 – 2581PhosphoserineCombined sources
Modified residuei265 – 2651N6-acetyllysineCombined sources
Modified residuei318 – 3181PhosphoserineCombined sources
Modified residuei332 – 3321N6-acetyllysineCombined sources
Modified residuei535 – 5351PhosphothreonineCombined sources
Cross-linki568 – 568Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei577 – 5771Phosphoserine; by PRKDCCombined sources1 Publication
Modified residuei579 – 5791Phosphoserine; by PRKDC1 Publication
Modified residuei580 – 5801Phosphoserine; by PRKDC1 Publication
Modified residuei660 – 6601N6-acetyllysineCombined sources
Modified residuei665 – 6651N6-acetyllysineCombined sources
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 (PubMed:22266820). Ubiquitinated by RNF138, leading to remove the Ku complex from DNA breaks (PubMed:26502055).2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP13010.
MaxQBiP13010.
PaxDbiP13010.
PeptideAtlasiP13010.
PRIDEiP13010.

2D gel databases

SWISS-2DPAGEP13010.

PTM databases

iPTMnetiP13010.
PhosphoSiteiP13010.
SwissPalmiP13010.

Miscellaneous databases

PMAP-CutDBP13010.

Expressioni

Developmental stagei

Expression increases during promyelocyte differentiation.1 Publication

Inductioni

In osteoblasts, by FGF2.

Gene expression databases

BgeeiENSG00000079246.
CleanExiHS_XRCC5.
ExpressionAtlasiP13010. baseline and differential.
GenevisibleiP13010. HS.

Organism-specific databases

HPAiCAB004468.
HPA025813.
HPA064685.

Interactioni

Subunit structurei

Heterodimer composed of XRCC5/Ku80 and XRCC6/Ku70. 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 to form the core of the non-homologous end joining (NHEJ) complex (PubMed:25941166, PubMed:25670504, PubMed:11493912, PubMed:22442688). Additional components of the NHEJ complex include NHEJ1/XLF and C9orf142/PAXX (PubMed:25574025, PubMed:25941166, PubMed:25670504). The dimer also associates with NAA15, and this complex displays DNA binding activity towards the osteocalcin FGF response element (OCFRE) (PubMed:12145306). In addition, XRCC5 binds to the osteoblast-specific transcription factors MSX2 and RUNX2 (PubMed:12145306). Interacts with ELF3 (PubMed:15075319). May interact with APLF (PubMed:17353262, PubMed:17396150). The XRCC5/XRCC6 dimer associates in a DNA-dependent manner with APEX1 (PubMed:8621488). Identified in a complex with DEAF1 and XRCC6. Interacts with NR4A3; the DNA-dependent protein kinase complex DNA-PK phosphorylates and activates NR4A3 and prevents NR4A3 ubiquitinylation and degradation (PubMed:25852083). Interacts with RNF138 (PubMed:26502055).12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APLFQ8IW1912EBI-357997,EBI-1256044
COILP384326EBI-357997,EBI-945751
GOLPH3Q9H4A62EBI-357997,EBI-2465479
HOXB7P096299EBI-357997,EBI-1248457
HSPB1P047922EBI-357997,EBI-352682
PRKDCP785277EBI-357997,EBI-352053
XRCC6P1295611EBI-357997,EBI-353208

GO - Molecular functioni

  • protein C-terminus binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi113353. 219 interactions.
DIPiDIP-31379N.
IntActiP13010. 96 interactions.
MINTiMINT-131739.
STRINGi9606.ENSP00000375977.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

eggNOGiKOG2326. Eukaryota.
ENOG410YKH9. LUCA.
GeneTreeiENSGT00390000015674.
HOVERGENiHBG006237.
InParanoidiP13010.
KOiK10885.
OMAiYTFRESL.
OrthoDBiEOG091G11VD.
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:SF4. PTHR12604:SF4. 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

        10         20         30         40         50
MVRSGNKAAV VLCMDVGFTM SNSIPGIESP FEQAKKVITM FVQRQVFAEN
60 70 80 90 100
KDEIALVLFG TDGTDNPLSG GDQYQNITVH RHLMLPDFDL LEDIESKIQP
110 120 130 140 150
GSQQADFLDA LIVSMDVIQH ETIGKKFEKR HIEIFTDLSS RFSKSQLDII
160 170 180 190 200
IHSLKKCDIS LQFFLPFSLG KEDGSGDRGD GPFRLGGHGP SFPLKGITEQ
210 220 230 240 250
QKEGLEIVKM VMISLEGEDG LDEIYSFSES LRKLCVFKKI ERHSIHWPCR
260 270 280 290 300
LTIGSNLSIR IAAYKSILQE RVKKTWTVVD AKTLKKEDIQ KETVYCLNDD
310 320 330 340 350
DETEVLKEDI IQGFRYGSDI VPFSKVDEEQ MKYKSEGKCF SVLGFCKSSQ
360 370 380 390 400
VQRRFFMGNQ VLKVFAARDD EAAAVALSSL IHALDDLDMV AIVRYAYDKR
410 420 430 440 450
ANPQVGVAFP HIKHNYECLV YVQLPFMEDL RQYMFSSLKN SKKYAPTEAQ
460 470 480 490 500
LNAVDALIDS MSLAKKDEKT DTLEDLFPTT KIPNPRFQRL FQCLLHRALH
510 520 530 540 550
PREPLPPIQQ HIWNMLNPPA EVTTKSQIPL SKIKTLFPLI EAKKKDQVTA
560 570 580 590 600
QEIFQDNHED GPTAKKLKTE QGGAHFSVSS LAEGSVTSVG SVNPAENFRV
610 620 630 640 650
LVKQKKASFE EASNQLINHI EQFLDTNETP YFMKSIDCIR AFREEAIKFS
660 670 680 690 700
EEQRFNNFLK ALQEKVEIKQ LNHFWEIVVQ DGITLITKEE ASGSSVTAEE
710 720 730
AKKFLAPKDK PSGDTAAVFE EGGDVDDLLD MI
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 (Ref. 4) Curated
Sequence conflicti178 – 1781R → S in BAD96323 (Ref. 4) Curated
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:
EMBLi
GenBanki
DDBJi
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.4. human.

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi113353. 219 interactions.
DIPiDIP-31379N.
IntActiP13010. 96 interactions.
MINTiMINT-131739.
STRINGi9606.ENSP00000375977.

PTM databases

iPTMnetiP13010.
PhosphoSiteiP13010.
SwissPalmiP13010.

Polymorphism and mutation databases

BioMutaiXRCC5.
DMDMi125731.

2D gel databases

SWISS-2DPAGEP13010.

Proteomic databases

EPDiP13010.
MaxQBiP13010.
PaxDbiP13010.
PeptideAtlasiP13010.
PRIDEiP13010.

Protocols and materials databases

DNASUi7520.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000392132; ENSP00000375977; ENSG00000079246.
ENST00000392133; ENSP00000375978; ENSG00000079246.
GeneIDi7520.
KEGGihsa:7520.
UCSCiuc002vfy.4. human.

Organism-specific databases

CTDi7520.
GeneCardsiXRCC5.
HGNCiHGNC:12833. XRCC5.
HPAiCAB004468.
HPA025813.
HPA064685.
MIMi194364. gene.
neXtProtiNX_P13010.
PharmGKBiPA37425.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2326. Eukaryota.
ENOG410YKH9. LUCA.
GeneTreeiENSGT00390000015674.
HOVERGENiHBG006237.
InParanoidiP13010.
KOiK10885.
OMAiYTFRESL.
OrthoDBiEOG091G11VD.
PhylomeDBiP13010.
TreeFamiTF101205.

Enzyme and pathway databases

ReactomeiR-HSA-164843. 2-LTR circle formation.
R-HSA-1834949. Cytosolic sensors of pathogen-associated DNA.
R-HSA-3270619. IRF3-mediated induction of type I IFN.
R-HSA-5693571. Nonhomologous End-Joining (NHEJ).
SIGNORiP13010.

Miscellaneous databases

ChiTaRSiXRCC5. human.
EvolutionaryTraceiP13010.
GeneWikiiKu80.
GenomeRNAii7520.
PMAP-CutDBP13010.
PROiP13010.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000079246.
CleanExiHS_XRCC5.
ExpressionAtlasiP13010. baseline and differential.
GenevisibleiP13010. HS.

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:SF4. PTHR12604:SF4. 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.
ProtoNetiSearch...

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 7, 2016
This is version 191 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 XRCC5.1 Publication

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.