Gene: XRCC6 - Gallus gallus
Last modified: Dec 09, 2014. Release 1 • Page created: May 19, 2024
Summary
Gene Symbol | : | XRCC6 | ||||||||||||
NCBI Gene ID | : | 395767 | ||||||||||||
Species | : | Gallus gallus | ||||||||||||
Gene Synonyms | : | |||||||||||||
Gene Homologs | : | AgaP_AGAP002690 (Anopheles gambiae) | cku-70 (Caenorhabditis elegans) | Irbp (Drosophila melanogaster) | KLLA0C06226g (Kluyveromyces lactis) | KU70 (Arabidopsis thaliana) | LOC100536337 (Danio rerio) | MGG_01512 (Magnaporthe oryzae) | NCU08290 (Neurospora crassa) | Os07g0184900 (Oryza sativa) | pku70 (Schizosaccharomyces pombe) | XRCC6 (Bos taurus) | XRCC6 (Canis lupus familiaris) | xrcc6 (Danio rerio) | XRCC6 (Gallus gallus) | XRCC6 (Homo sapiens) | XRCC6 (Macaca mulatta) | Xrcc6 (Mus musculus) | XRCC6 (Pan troglodytes) | Xrcc6 (Rattus norvegicus) | YKU70 (Saccharomyces cerevisiae) | ||||||||||||
Ageing Relevance Analysis | : |
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Ageing Factor Stable ID | : | AF_010140 | ||||||||||||
Download | : | XML |
Protein Information
Protein Name | Species | UniProt Accession Number | UniProt Entry Name | Protein Function | Sequence |
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X-ray repair cross-complementing protein 5 | Gallus gallus | O93257 (UniProtKB/Swiss-Prot) | XRCC6_CHICK (UniProtKB/Swiss-Prot) | 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. 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. | View |
Observations
Ageing Phenotype
Data Type 1
no ageing phenotype observation—data type 1 available
Data Type 2
no ageing phenotype observation—data type 2 available
Homology Analysis
Ageing Relevance:
- yes (Exp. Analysis)
- yes, but no ageing factor assigned (Exp. Analysis)
- no (Exp. Analysis)
- putative (Comp. Analysis)
Legend:
- #EGHG:
- Number of Experimentally Confirmed Ageing-related Genes In Homology Group
Sequences
XRCC6_CHICK | O93257 | X-ray repair cross-complementing protein 5 (Gallus gallus) from UniProtKB/Swiss-Prot Length: 632 10 20 30 40 50 60 70 80 90 100 110 120 130 140 150 160 170 180 190 200 210 220 230 240 250 260 270 280 290 300 310 320 330 340 350 360 370 380 390 400 410 420 430 440 450 460 470 480 490 500 510 520 530 540 550 560 570 580 590 600 610 620 630 XRCC6_CHICK 1 MEMWVLGEVGMAVLSAAAMADWVSYYRGDGPDEEEDGEQQEEEGPEAVADYRFSGRDSLIFLVDASKAMFEPYENEEAATPFDMTMQCIRNVYTSKIISSDKDLLSVVFYGMENNKNSADFKHIYVLQELDNPGAKRILELDQYRGDEGRVLFRETFGHNADYSLGEALWACSNLFSDVRVRLSHKRIMLFTNEDNPHANDSAKAKLARTRAGDLRDTGIILDLMHLKKPGGFDISLFYRDIINVAEDEDLGIQPDESGKLEHLMKKVRAKETRKRALSRLNLYLNKDLSFSVGVYNLIQKAYKPYPVKLYRETNEPVKTKTRVFNGKTGSLLLPSDTKRAQTYGNRQIAMEKEETEEVKRFDSPGLFLIGFKPLSMLKQHHHIRPSQFMYPEESLVTGSTTLFNALLMKCLEKEVMALCRYIARRNTPPRIVALIPQEEEVDEQKVQIAPPGFHIIFLPYADDKRNVDFTEKVPANREQVDKMKGIIQKLRFKYRTDSFENPVLQQHFRNLEALALDMLEPEQAEDLTMPKTEEMSRRLGNLVEEFKQLVYPPDYSPEGKAAKRKQAGDAQAEKRPKIEISEDSLRSYVQNGTLGKLTVSALKDTCRHYGLRSGGKKQELIDALTEYFSGR 632
References
no reference information available
Sources
Ageing-related Data Sources
- AgeFactDB Homology Analysis
Additional Data Sources
- AgeFactDB Pipeline
- HomoloGene
- UniProtKB/Swiss-Prot