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DNA repair protein complementing XP-G cells; xeroderma pigmentosum group G-complementing protein; DNA excision repair protein ERCC-5 (ERCC5, ERCM2, XPG, XPGC)

Function: - involved in DNA excision repair - structure-specific nuclease - cleaves Y-type structures at the junction of double-stranded & single-stranded DNA regions - the XP G-correcting protein cuts on the strand that leads off from the junction in the 3'-5' direction (3'incision) - XP G-correcting protein probably works in coordination with the ERCC1/XPF complex in excision repair, the two nucleases cleaving the same DNA strand on opposite sides of DNA damage - acts as a cofactor for a DNA glycosylase that removes oxidized pyrimidines from DNA - may also be involved in transcription-coupled DNA repair & in transcription by RNA polymerase 2 - interacts with PCNA Cofactor: - binds 2 Mg+2 per subunit - may bind an additional third Mg+2 after substrate binding Structure: - belongs to the XPG/RAD2 endonuclease family, XPG subfamily Compartment: nucleus Alternative splicing: named isoforms=2 Pathology: - defects in ERCC5 are the cause of xeroderma pigmentosum complementation group G Comparative biology: - Xeroderma Pigmentosum complementation group G-correcting protein (XPGC) in humans - Excision Repair Cross Complement-5 (ERCC5) protein in rodents - RAD2-protein in yeast

Related

ERCC1/XPF heterodimer XP G-correcting protein gene, ERCC-5 or RAD2

General

endodeoxyribonuclease excision repair cross complement (ERCC) or excision repair cross-complementing rodent repair deficiency, complementation group phosphoprotein Xeroderma pigmentosum group complementing protein

Properties

SIZE: entity length = 1186 aa MW = 133 kD COMPARTMENT: cell nucleus MOTIF: N {1-95} MOTIF: Mg+2-binding site SITE: 30-30 Mg+2-binding site SITE: 77-77 Ser phosphorylation site {S156} Ser phosphorylation site {S157} Thr phosphorylation site {T338} Ser phosphorylation site {S341} Ser phosphorylation site {S355} Ser phosphorylation site {S356} Ser phosphorylation site {S357} Ser phosphorylation site {S382} Ser phosphorylation site {S384} Ser phosphorylation site {S423} Ser phosphorylation site {S424} Ser phosphorylation site {S428} Ser phosphorylation site {S526} Ser phosphorylation site {S559} Ser phosphorylation site {S562} Ser phosphorylation site {S563} Ser phosphorylation site {S705} Ser phosphorylation site {S724} I {753-881} MOTIF: Mg+2-binding site SITE: 789-789 Mg+2-binding site SITE: 791-791 Mg+2-binding site SITE: 810-810 Mg+2-binding site SITE: 812-812 Mg+2-binding site SITE: 861-861 PCNA interaction {981-1009} peptide motif {1057-1073}

References

  1. Bootsma D & Hoeijmakers JH DNA repair. Engagement with transcription. Nature 363:114 1993 PMID: 8483493
  2. He Z, Henricksen LA, Wold MS, Ingles CJ. RPA involvement in the damage-recognition and incision steps of nucleotide excision repair. Nature. 1995 Apr 6;374(6522):566-9. PMID: 7700386 (RFA binding)
  3. PROSITE :accession PS00841
  4. Lehmann AR. Nucleotide excision repair and the link with transcription. Trends Biochem Sci. 1995 Oct;20(10):402-5. Review. PMID: 8533152
  5. Entrez Gene :accession 2073
  6. UniProt :accession P28715
  7. Allelic variations of the XP genes http://www.xpmutations.org/
  8. Atlas of Genetics & Cytogenetics in Oncology & Haematology http://atlasgeneticsoncology.org/genes/XPGID300.html
  9. GeneReviews https://www.genecards.org/cgi-bin/carddisp.pl?gene=ERCC5
  10. NIEHS-SNPs http://egp.gs.washington.edu/data/ercc5/

Databases & Figures

OMIM correlations MORBIDMAP 133530 UniProt P28715 PFAM correlations Entrez Gene 2073 Kegg hsa:2073 Model for nucleotide excision repair (v2)