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Literature summary for 3.6.1.71 extracted from

  • Becherel, O.J.; Jakob, B.; Cherry, A.L.; Gueven, N.; Fusser, M.; Kijas, A.W.; Peng, C.; Katyal, S.; McKinnon, P.J.; Chen, J.; Epe, B.; Smerdon, S.J.; Taucher-Scholz, G.; Lavin, M.F.
    CK2 phosphorylation-dependent interaction between aprataxin and MDC1 in the DNA damage response (2010), Nucleic Acids Res., 38, 1489-1503.
    View publication on PubMedView publication on EuropePMC
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Crystallization (Commentary)

Crystallization (Comment) Organism
aprataxin forkhead-associated domain and modeling of the pSDpTD peptide into the apo structure. pT recognition is provided by residues Arg29 and Ser41 Homo sapiens

Protein Variants

Protein Variants Comment Organism
R29A mutation of forkhead-associated domain residue, prevents its interaction with mediator of DNA-damage checkpoint protein MDC1 and recruitment to sites of DNA damage Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
nucleolus aprataxin localizes at sites of DNA damage induced by high low linear energy transfer radiation Homo sapiens 5730
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Organism

Organism UniProt Comment Textmining
Homo sapiens Q7Z2E3
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Source Tissue

Source Tissue Comment Organism Textmining
fibroblast
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 Homo sapiens
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HeLa cell
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 Homo sapiens
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General Information

General Information Comment Organism
physiological function aprataxin localizes at sites of DNA damage induced by high low linear energy transfer radiation and binds to mediator of DNA-damage checkpoint protein MDC1/NFBD1 through a phosphorylation-dependent interaction. This interaction is mediated via the aprataxin forkhead-associated domain and multiple casein kinase 2 diphosphorylated S-D-T-D motifs in MDC1 Homo sapiens