ERCC5

Excision repair cross-complementing rodent repair deficiency, complementation group 5

Identifiers

ERCC5; COFS3; ERCM2; UVDR; XPG; XPGC

External IDs

OMIM: 133530 MGI: 103582 HomoloGene: 37265 GeneCards: ERCC5 Gene

Gene Ontology
Molecular function	• bubble DNA binding • DNA binding • double-stranded DNA binding • single-stranded DNA binding • endonuclease activity • endodeoxyribonuclease activity • protein binding • protein homodimerization activity • metal ion binding • protein N-terminus binding
Cellular component	• nucleus • nucleoplasm • nucleoplasm • holo TFIIH complex • DNA-directed RNA polymerase II, holoenzyme
Biological process	• nucleotide-excision repair, DNA damage removal • DNA repair • transcription-coupled nucleotide-excision repair • transcription-coupled nucleotide-excision repair • nucleotide-excision repair • nucleotide-excision repair, DNA incision, 3'-to lesion • nucleotide-excision repair, DNA incision, 3'-to lesion • determination of adult lifespan • response to UV • response to UV • UV protection • response to UV-C • multicellular organism growth • negative regulation of apoptosis
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 13:
103.46 – 103.53 Mb

Chr 1:
44.2 – 44.24 Mb

PubMed search

[1]

[2]

DNA repair protein complementing XP-G cells is a protein that in humans is encoded by the ERCC5 gene.^[1]^[2]

Excision repair cross-complementing rodent repair deficiency, complementation group 5 (xeroderma pigmentosum, complementation group G) is involved in excision repair of UV-induced DNA damage. Mutations cause Cockayne syndrome, which is characterized by severe growth defects, mental retardation, and cachexia. Multiple alternatively spliced transcript variants encoding distinct isoforms have been described, but the biological validity of all variants has not been determined.^[2]

1 Interactions
2 References
3 External links
4 Further reading

Interactions

ERCC5 has been shown to interact with ERCC2.^[3]

References

^ Samec S, Jones TA, Corlet J, Scherly D, Sheer D, Wood RD, Clarkson SG (Oct 1994). "The human gene for xeroderma pigmentosum complementation group G (XPG) maps to 13q33 by fluorescence in situ hybridization". Genomics 21 (1): 283–5. doi:10.1006/geno.1994.1261. PMID 8088806.
^ ^a ^b "Entrez Gene: ERCC5 excision repair cross-complementing rodent repair deficiency, complementation group 5 (xeroderma pigmentosum, complementation group G (Cockayne syndrome))". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2073.
^ Iyer, N; Reagan M S, Wu K J, Canagarajah B, Friedberg E C (Feb. 1996). "Interactions involving the human RNA polymerase II transcription/nucleotide excision repair complex TFIIH, the nucleotide excision repair protein XPG, and Cockayne syndrome group B (CSB) protein". Biochemistry (UNITED STATES) 35 (7): 2157–67. doi:10.1021/bi9524124. ISSN 0006-2960. PMID 8652557.

External links

GeneReviews/NIH/NCBI/UW entry on Xeroderma Pigmentosum

Miura M (1999). "Detection of chromatin-bound PCNA in mammalian cells and its use to study DNA excision repair". J. Radiat. Res. 40 (1): 1–12. doi:10.1269/jrr.40.1. PMID 10408173.
Cleaver JE, Thompson LH, Richardson AS, States JC (1999). "A summary of mutations in the UV-sensitive disorders: xeroderma pigmentosum, Cockayne syndrome, and trichothiodystrophy". Hum. Mutat. 14 (1): 9–22. doi:10.1002/(SICI)1098-1004(1999)14:1<9::AID-HUMU2>3.0.CO;2-6. PMID 10447254.
Takahashi E, Shiomi N, Shiomi T (1993). "Precise localization of the excision repair gene, ERCC5, to human chromosome 13q32.3-q33.1 by direct R-banding fluorescence in situ hybridization". Jpn. J. Cancer Res. 83 (11): 1117–9. PMID 1483924.
Mudgett JS, MacInnes MA (1991). "Isolation of the functional human excision repair gene ERCC5 by intercosmid recombination". Genomics 8 (4): 623–33. doi:10.1016/0888-7543(90)90248-S. PMID 2276736.
Shiomi T, Harada Y, Saito T, et al. (1994). "An ERCC5 gene with homology to yeast RAD2 is involved in group G xeroderma pigmentosum". Mutat. Res. 314 (2): 167–75. PMID 7510366.
Lehmann AR, Bootsma D, Clarkson SG, et al. (1994). "Nomenclature of human DNA repair genes". Mutat. Res. 315 (1): 41–2. PMID 7517009.
Cloud KG, Shen B, Strniste GF, Park MS (1995). "XPG protein has a structure-specific endonuclease activity". Mutat. Res. 347 (2): 55–60. doi:10.1016/0165-7992(95)90070-5. PMID 7651464.
Matsunaga T, Mu D, Park CH, et al. (1995). "Human DNA repair excision nuclease. Analysis of the roles of the subunits involved in dual incisions by using anti-XPG and anti-ERCC1 antibodies". J. Biol. Chem. 270 (35): 20862–9. doi:10.1074/jbc.270.35.20862. PMID 7657672.
Nouspikel T, Clarkson SG (1994). "Mutations that disable the DNA repair gene XPG in a xeroderma pigmentosum group G patient". Hum. Mol. Genet. 3 (6): 963–7. doi:10.1093/hmg/3.6.963. PMID 7951246.
Habraken Y, Sung P, Prakash L, Prakash S (1994). "Human xeroderma pigmentosum group G gene encodes a DNA endonuclease". Nucleic Acids Res. 22 (16): 3312–6. doi:10.1093/nar/22.16.3312. PMC 523723. PMID 8078765. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=523723.
O'Donovan A, Davies AA, Moggs JG, et al. (1994). "XPG endonuclease makes the 3' incision in human DNA nucleotide excision repair". Nature 371 (6496): 432–5. doi:10.1038/371432a0. PMID 8090225.
O'Donovan A, Scherly D, Clarkson SG, Wood RD (1994). "Isolation of active recombinant XPG protein, a human DNA repair endonuclease". J. Biol. Chem. 269 (23): 15965–8. PMID 8206890.
MacInnes MA, Dickson JA, Hernandez RR, et al. (1993). "Human ERCC5 cDNA-cosmid complementation for excision repair and bipartite amino acid domains conserved with RAD proteins of Saccharomyces cerevisiae and Schizosaccharomyces pombe". Mol. Cell. Biol. 13 (10): 6393–402. PMC 364698. PMID 8413238. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=364698.
Scherly D, Nouspikel T, Corlet J, et al. (1993). "Complementation of the DNA repair defect in xeroderma pigmentosum group G cells by a human cDNA related to yeast RAD2". Nature 363 (6425): 182–5. doi:10.1038/363182a0. PMID 8483504.
O'Donovan A, Wood RD (1993). "Identical defects in DNA repair in xeroderma pigmentosum group G and rodent ERCC group 5". Nature 363 (6425): 185–8. doi:10.1038/363185a0. PMID 8483505.
Iyer N, Reagan MS, Wu KJ, et al. (1996). "Interactions involving the human RNA polymerase II transcription/nucleotide excision repair complex TFIIH, the nucleotide excision repair protein XPG, and Cockayne syndrome group B (CSB) protein". Biochemistry 35 (7): 2157–67. doi:10.1021/bi9524124. PMID 8652557.
Park MS, Knauf JA, Pendergrass SH, et al. (1996). "Ultraviolet-induced movement of the human DNA repair protein, Xeroderma pigmentosum type G, in the nucleus". Proc. Natl. Acad. Sci. U.S.A. 93 (16): 8368–73. doi:10.1073/pnas.93.16.8368. PMC 38677. PMID 8710877. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=38677.
Cooper PK, Nouspikel T, Clarkson SG, Leadon SA (1997). "Defective transcription-coupled repair of oxidative base damage in Cockayne syndrome patients from XP group G". Science 275 (5302): 990–3. doi:10.1126/science.275.5302.990. PMID 9020084.
Nouspikel T, Lalle P, Leadon SA, et al. (1997). "A common mutational pattern in Cockayne syndrome patients from xeroderma pigmentosum group G: implications for a second XPG function". Proc. Natl. Acad. Sci. U.S.A. 94 (7): 3116–21. doi:10.1073/pnas.94.7.3116. PMC 20331. PMID 9096355. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=20331.

DNA repair

Excision repair	Base excision repair/AP site (DNA glycosylase, Uracil-DNA glycosylase, Poly ADP ribose polymerase) • Nucleotide excision repair/ERCC (XPA, XPB, XPC, XPD/ERCC2, XPE/DDB1, XPF/DDB1, XPG/ERCC5, ERCC1, RPA, RAD23A, RAD23B, Excinuclease)

Other forms of repair	Transcription-coupled repair (ERCC6, ERCC8) • DNA mismatch repair (MLH1, MSH2) • Homology directed repair • Non-homologous end joining (Ku) • Microhomology-mediated end joining • Postreplication repair • Photolyase (CRY1, CRY2)

Other/ungrouped proteins	Ogt • PcrA • Proliferating Cell Nuclear Antigen • Homologous recombination (RecA • Sgs1 • Slx4)

Regulation	SOS box • SOS response

Other/ungrouped	8-Oxoguanine • Adaptive response • Meiotic recombination checkpoint • RecF pathway DNA helicase: BLM · WRN FANC proteins: core protein complex (FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL, FANCM), FANCD1, FANCD2, FANCI, FANCJ, FANCN

see also DNA repair-deficiency disorder B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)

ERCC5

Contents

Interactions

References

External links

Further reading