ERCC2: Difference between revisions

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Latest revision as of 17:41, 5 December 2017

ERCC2, or XPD is a protein involved in transcription-coupled nucleotide excision repair.

The XPD (ERCC2) gene encodes for a 2.3-kb mRNA containing 22 exons and 21 introns. The XPD protein is a 760 amino acids polypeptide with a size of 87kDa. Defects in this gene can result in three different disorders: the cancer-prone syndrome xeroderma pigmentosum complementation group D, photosensitive trichothiodystrophy, and Cockayne syndrome.^[1]

Just like XPB, XPD is also a part of human transcriptional initiation factor TFIIH and has ATP-dependent helicase activity.^[2] It belongs to the RAD3/XPD subfamily of helicases.

XPD is essential for the viability of cells. Deletion of XPD in mice is embryonic lethal.

Consequences of mutations in ERCC2

The ERCC2/XPD protein participates in nucleotide excision repair (NER), and is employed in unwinding the DNA double helix after damage is initially recognized. NER is a multi-step pathway that removes a wide range of different damages that distort normal base pairing. Such damages include bulky chemical adducts, UV-induced pyrimidine dimers, and several forms of oxidative damage. Mutations in the ERCC2/XPD gene can lead to various syndromes, either xeroderma pigmentosum (XP), trichothiodystrophy (TTD) or a combination of XP and TTD (XPTTD), or a combination of XP and Cockayne syndrome (XPCS).^[3] TTD and CS both display features of premature aging. These features may include sensorineural deafness, retinal degeneration, white matter hypomethylation, central nervous system calcification, reduced stature, and cachexia (loss of subcutaneous fat tissue).^[3]^[4] XPCS and TTD fibroblasts from ERCC2/XPD mutant human and mouse show evidence of defective repair of oxidative DNA damages that may underlie the segmental progeroid (premature aging) symptoms^[5] (see DNA damage theory of aging).

Interactions

ERCC2 has been shown to interact with:

ERCC5,^[6]
GTF2H1,^[7]^[8]
GTF2H2,^[9]^[10] and
XPB.^[7]^[6]^[11]^[12]

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles.^{[§ 1]}

[[File:

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<imagemap> Image:FluoropyrimidineActivity_WP1601.png

|{{{bSize}}}px|alt=Fluorouracil (5-FU) Activity edit]]

Fluorouracil (5-FU) Activity edit

↑ The interactive pathway map can be edited at WikiPathways: "FluoropyrimidineActivity_WP1601".

References

↑ "Entrez Gene: ERCC2 excision repair cross-complementing rodent repair deficiency, complementation group 2 (xeroderma pigmentosum D)".
↑ Lee TI, Young RA (2000). "Transcription of eukaryotic protein-coding genes". Annual Review of Genetics. 34: 77–137. doi:10.1146/annurev.genet.34.1.77. PMID 11092823.
↑ ^3.0 ^3.1 Andressoo JO, Hoeijmakers JH, Mitchell JR (2006). "Nucleotide excision repair disorders and the balance between cancer and aging". Cell Cycle. 5 (24): 2886–8. doi:10.4161/cc.5.24.3565. PMID 17172862.
↑ Fuss JO, Tainer JA (2011). "XPB and XPD helicases in TFIIH orchestrate DNA duplex opening and damage verification to coordinate repair with transcription and cell cycle via CAK kinase". DNA Repair (Amst.). 10 (7): 697–713. doi:10.1016/j.dnarep.2011.04.028. PMC 3234290. PMID 21571596.
↑ Andressoo JO, Mitchell JR, de Wit J, Hoogstraten D, Volker M, Toussaint W, Speksnijder E, Beems RB, van Steeg H, Jans J, de Zeeuw CI, Jaspers NG, Raams A, Lehmann AR, Vermeulen W, Hoeijmakers JH, van der Horst GT (2006). "An Xpd mouse model for the combined xeroderma pigmentosum/Cockayne syndrome exhibiting both cancer predisposition and segmental progeria". Cancer Cell. 10 (2): 121–32. doi:10.1016/j.ccr.2006.05.027. PMID 16904611.
↑ ^6.0 ^6.1 Iyer N, Reagan MS, Wu KJ, Canagarajah B, Friedberg EC (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. 35 (7): 2157–67. doi:10.1021/bi9524124. PMID 8652557.
↑ ^7.0 ^7.1 Drapkin R, Reardon JT, Ansari A, Huang JC, Zawel L, Ahn K, Sancar A, Reinberg D (Apr 1994). "Dual role of TFIIH in DNA excision repair and in transcription by RNA polymerase II". Nature. 368 (6473): 769–72. doi:10.1038/368769a0. PMID 8152490.
↑ Rossignol M, Kolb-Cheynel I, Egly JM (Apr 1997). "Substrate specificity of the cdk-activating kinase (CAK) is altered upon association with TFIIH". The EMBO Journal. 16 (7): 1628–37. doi:10.1093/emboj/16.7.1628. PMC 1169767. PMID 9130708.
↑ Coin F, Marinoni JC, Rodolfo C, Fribourg S, Pedrini AM, Egly JM (Oct 1998). "Mutations in the XPD helicase gene result in XP and TTD phenotypes, preventing interaction between XPD and the p44 subunit of TFIIH". Nature Genetics. 20 (2): 184–8. doi:10.1038/2491. PMID 9771713.
↑ Vermeulen W, Bergmann E, Auriol J, Rademakers S, Frit P, Appeldoorn E, Hoeijmakers JH, Egly JM (Nov 2000). "Sublimiting concentration of TFIIH transcription/DNA repair factor causes TTD-A trichothiodystrophy disorder". Nature Genetics. 26 (3): 307–13. doi:10.1038/81603. PMID 11062469.
↑ Giglia-Mari G, Coin F, Ranish JA, Hoogstraten D, Theil A, Wijgers N, Jaspers NG, Raams A, Argentini M, van der Spek PJ, Botta E, Stefanini M, Egly JM, Aebersold R, Hoeijmakers JH, Vermeulen W (Jul 2004). "A new, tenth subunit of TFIIH is responsible for the DNA repair syndrome trichothiodystrophy group A". Nature Genetics. 36 (7): 714–9. doi:10.1038/ng1387. PMID 15220921.
↑ Marinoni JC, Roy R, Vermeulen W, Miniou P, Lutz Y, Weeda G, Seroz T, Gomez DM, Hoeijmakers JH, Egly JM (Mar 1997). "Cloning and characterization of p52, the fifth subunit of the core of the transcription/DNA repair factor TFIIH". The EMBO Journal. 16 (5): 1093–102. doi:10.1093/emboj/16.5.1093. PMC 1169708. PMID 9118947.

External links

GeneReviews/NIH/NCBI/UW entry on Xeroderma Pigmentosum
ERCC2+Protein at the US National Library of Medicine Medical Subject Headings (MeSH)

[WikiPathways-13] The interactive pathway map can be edited at WikiPathways: "FluoropyrimidineActivity_WP1601".

[1] "Entrez Gene: ERCC2 excision repair cross-complementing rodent repair deficiency, complementation group 2 (xeroderma pigmentosum D)".

[pmid11092823-2] Lee TI, Young RA (2000). "Transcription of eukaryotic protein-coding genes". Annual Review of Genetics. 34: 77–137. doi:10.1146/annurev.genet.34.1.77. PMID 11092823.

[Andressoo-3] 3.0 ^3.1 Andressoo JO, Hoeijmakers JH, Mitchell JR (2006). "Nucleotide excision repair disorders and the balance between cancer and aging". Cell Cycle. 5 (24): 2886–8. doi:10.4161/cc.5.24.3565. PMID 17172862.

[pmid21571596-4] Fuss JO, Tainer JA (2011). "XPB and XPD helicases in TFIIH orchestrate DNA duplex opening and damage verification to coordinate repair with transcription and cell cycle via CAK kinase". DNA Repair (Amst.). 10 (7): 697–713. doi:10.1016/j.dnarep.2011.04.028. PMC 3234290. PMID 21571596.

[pmid16904611-5] Andressoo JO, Mitchell JR, de Wit J, Hoogstraten D, Volker M, Toussaint W, Speksnijder E, Beems RB, van Steeg H, Jans J, de Zeeuw CI, Jaspers NG, Raams A, Lehmann AR, Vermeulen W, Hoeijmakers JH, van der Horst GT (2006). "An Xpd mouse model for the combined xeroderma pigmentosum/Cockayne syndrome exhibiting both cancer predisposition and segmental progeria". Cancer Cell. 10 (2): 121–32. doi:10.1016/j.ccr.2006.05.027. PMID 16904611.

[pmid8652557-6] 6.0 ^6.1 Iyer N, Reagan MS, Wu KJ, Canagarajah B, Friedberg EC (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. 35 (7): 2157–67. doi:10.1021/bi9524124. PMID 8652557.

[pmid8152490-7] 7.0 ^7.1 Drapkin R, Reardon JT, Ansari A, Huang JC, Zawel L, Ahn K, Sancar A, Reinberg D (Apr 1994). "Dual role of TFIIH in DNA excision repair and in transcription by RNA polymerase II". Nature. 368 (6473): 769–72. doi:10.1038/368769a0. PMID 8152490.

[pmid9130708-8] Rossignol M, Kolb-Cheynel I, Egly JM (Apr 1997). "Substrate specificity of the cdk-activating kinase (CAK) is altered upon association with TFIIH". The EMBO Journal. 16 (7): 1628–37. doi:10.1093/emboj/16.7.1628. PMC 1169767. PMID 9130708.

[pmid9771713-9] Coin F, Marinoni JC, Rodolfo C, Fribourg S, Pedrini AM, Egly JM (Oct 1998). "Mutations in the XPD helicase gene result in XP and TTD phenotypes, preventing interaction between XPD and the p44 subunit of TFIIH". Nature Genetics. 20 (2): 184–8. doi:10.1038/2491. PMID 9771713.

[pmid11062469-10] Vermeulen W, Bergmann E, Auriol J, Rademakers S, Frit P, Appeldoorn E, Hoeijmakers JH, Egly JM (Nov 2000). "Sublimiting concentration of TFIIH transcription/DNA repair factor causes TTD-A trichothiodystrophy disorder". Nature Genetics. 26 (3): 307–13. doi:10.1038/81603. PMID 11062469.

[pmid15220921-11] Giglia-Mari G, Coin F, Ranish JA, Hoogstraten D, Theil A, Wijgers N, Jaspers NG, Raams A, Argentini M, van der Spek PJ, Botta E, Stefanini M, Egly JM, Aebersold R, Hoeijmakers JH, Vermeulen W (Jul 2004). "A new, tenth subunit of TFIIH is responsible for the DNA repair syndrome trichothiodystrophy group A". Nature Genetics. 36 (7): 714–9. doi:10.1038/ng1387. PMID 15220921.

[pmid9118947-12] Marinoni JC, Roy R, Vermeulen W, Miniou P, Lutz Y, Weeda G, Seroz T, Gomez DM, Hoeijmakers JH, Egly JM (Mar 1997). "Cloning and characterization of p52, the fifth subunit of the core of the transcription/DNA repair factor TFIIH". The EMBO Journal. 16 (5): 1093–102. doi:10.1093/emboj/16.5.1093. PMC 1169708. PMID 9118947.

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[§ 1]

@@ Line 1: / Line 1: @@
-{{PBB|geneid=2068}}
+{{Infobox_gene}}
-{{SI}}
+__NOTOC__
+'''ERCC2''', or '''XPD''' is a protein involved in [[transcription-coupled nucleotide excision repair]].
+The XPD (ERCC2) gene encodes for a 2.3-kb mRNA containing 22 [[exons]] and 21 [[introns]]. The XPD protein is a 760 [[amino acids]] polypeptide with a size of 87kDa. Defects in this gene can result in three different disorders: the cancer-prone syndrome [[xeroderma pigmentosum]] complementation group D, photosensitive [[trichothiodystrophy]], and [[Cockayne syndrome]].<ref>{{cite web | title = Entrez Gene: ERCC2 excision repair cross-complementing rodent repair deficiency, complementation group 2 (xeroderma pigmentosum D)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2068| accessdate = }}</ref>
-'''ERCC2''', or '''XPD''' is a protein involved in [[transcription-coupled repair|transcription-coupled]] [[nucleotide excision repair]].
+Just like [[XPB]], XPD is also a part of human transcriptional [[initiation factor]] [[TFIIH]] and has ATP-dependent [[helicase]] activity.<ref name="pmid11092823">{{cite journal | vauthors = Lee TI, Young RA | title = Transcription of eukaryotic protein-coding genes | journal = Annual Review of Genetics | volume = 34 | issue =  | pages = 77–137 | year = 2000 | pmid = 11092823 | doi = 10.1146/annurev.genet.34.1.77 }}</ref> It belongs to the RAD3/XPD subfamily of helicases.
-The XPD (ERCC2) gene encodes for a 2.3-kb mRNA containing 22 [[exons]] and 21 [[introns]]. The XPD protein is a 760 [[amino acids]] polypeptide with a size of 87kDa. Defects in this gene can result in three different disorders: the cancer-prone syndrome [[xeroderma pigmentosum]] complementation group D, [[trichothiodystrophy]], and [[Cockayne syndrome]].<ref>{{cite web | title = Entrez Gene: ERCC2 excision repair cross-complementing rodent repair deficiency, complementation group 2 (xeroderma pigmentosum D)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2068| accessdate = }}</ref>
+XPD is essential for the viability of cells. Deletion of XPD in mice is embryonic lethal.
+==Consequences of mutations in ERCC2==
+The ERCC2/XPD protein participates in [[nucleotide excision repair]] (NER), and is employed in unwinding the [[DNA]] double helix after damage is initially recognized.  NER is a multi-step pathway that removes a wide range of different damages that distort normal base pairing.  Such damages include bulky chemical adducts, UV-induced pyrimidine dimers, and several forms of [[DNA damage (naturally occurring)|oxidative damage]].  Mutations in the ERCC2/XPD gene can lead to various syndromes, either [[xeroderma pigmentosum]] (XP), [[trichothiodystrophy]] (TTD) or a combination of XP and TTD (XPTTD), or a combination of XP and [[Cockayne syndrome]] (XPCS).<ref name=Andressoo>{{cite journal |vauthors=Andressoo JO, Hoeijmakers JH, Mitchell JR |title=Nucleotide excision repair disorders and the balance between cancer and aging |journal=Cell Cycle |volume=5 |issue=24 |pages=2886–8 |year=2006 |pmid=17172862 |doi=10.4161/cc.5.24.3565 |url=}}</ref>  TTD and CS both display features of premature aging.  These features may include [[Sensorineural hearing loss|sensorineural deafness]], retinal degeneration, white matter hypomethylation, central nervous system calcification, reduced stature, and [[cachexia]] (loss of subcutaneous fat tissue).<ref name=Andressoo /><ref name="pmid21571596">{{cite journal |vauthors=Fuss JO, Tainer JA |title=XPB and XPD helicases in TFIIH orchestrate DNA duplex opening and damage verification to coordinate repair with transcription and cell cycle via CAK kinase |journal=DNA Repair (Amst.) |volume=10 |issue=7 |pages=697–713 |year=2011 |pmid=21571596 |pmc=3234290 |doi=10.1016/j.dnarep.2011.04.028 |url=}}</ref>  XPCS and TTD fibroblasts from ERCC2/XPD mutant human and mouse show evidence of defective repair of oxidative DNA damages that may underlie the segmental progeroid (premature aging) symptoms<ref name="pmid16904611">{{cite journal |vauthors=Andressoo JO, Mitchell JR, de Wit J, Hoogstraten D, Volker M, Toussaint W, Speksnijder E, Beems RB, van Steeg H, Jans J, de Zeeuw CI, Jaspers NG, Raams A, Lehmann AR, Vermeulen W, Hoeijmakers JH, van der Horst GT |title=An Xpd mouse model for the combined xeroderma pigmentosum/Cockayne syndrome exhibiting both cancer predisposition and segmental progeria |journal=Cancer Cell |volume=10 |issue=2 |pages=121–32 |year=2006 |pmid=16904611 |doi=10.1016/j.ccr.2006.05.027 |url=}}</ref> (see [[DNA damage theory of aging]]).
+== Interactions ==
-Just like [[XPB]], XPD is also a part of human transcriptional [[initiation factor]] [[TFIIH]] and has ATP-dependent [[helicase]] activity.<ref name="pmid11092823">{{cite journal | author = Lee TI, Young RA | title = Transcription of eukaryotic protein-coding genes | journal = Annu. Rev. Genet. | volume = 34 | issue = | pages = 77–137 | year = 2000 | pmid = 11092823 | doi = 10.1146/annurev.genet.34.1.77}}</ref> It belongs to the RAD3/XPD subfamily of helicases.
+ERCC2 has been shown to [[Protein-protein interaction|interact]] with:
+* [[ERCC5]],<ref name = pmid8652557>{{cite journal | vauthors = Iyer N, Reagan MS, Wu KJ, Canagarajah B, Friedberg EC | title = 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 | journal = Biochemistry | volume = 35 | issue = 7 | pages = 2157–67 | date = Feb 1996 | pmid = 8652557 | doi = 10.1021/bi9524124 }}</ref>
+* [[GTF2H1]],<ref name = pmid8152490>{{cite journal | vauthors = Drapkin R, Reardon JT, Ansari A, Huang JC, Zawel L, Ahn K, Sancar A, Reinberg D | title = Dual role of TFIIH in DNA excision repair and in transcription by RNA polymerase II | journal = Nature | volume = 368 | issue = 6473 | pages = 769–72 | date = Apr 1994 | pmid = 8152490 | doi = 10.1038/368769a0 }}</ref><ref name = pmid9130708>{{cite journal | vauthors = Rossignol M, Kolb-Cheynel I, Egly JM | title = Substrate specificity of the cdk-activating kinase (CAK) is altered upon association with TFIIH | journal = The EMBO Journal | volume = 16 | issue = 7 | pages = 1628–37 | date = Apr 1997 | pmid = 9130708 | pmc = 1169767 | doi = 10.1093/emboj/16.7.1628 }}</ref>
+* [[GTF2H2]],<ref name = pmid9771713>{{cite journal | vauthors = Coin F, Marinoni JC, Rodolfo C, Fribourg S, Pedrini AM, Egly JM | title = Mutations in the XPD helicase gene result in XP and TTD phenotypes, preventing interaction between XPD and the p44 subunit of TFIIH | journal = Nature Genetics | volume = 20 | issue = 2 | pages = 184–8 | date = Oct 1998 | pmid = 9771713 | doi = 10.1038/2491 }}</ref><ref name = pmid11062469>{{cite journal | vauthors = Vermeulen W, Bergmann E, Auriol J, Rademakers S, Frit P, Appeldoorn E, Hoeijmakers JH, Egly JM | title = Sublimiting concentration of TFIIH transcription/DNA repair factor causes TTD-A trichothiodystrophy disorder | journal = Nature Genetics | volume = 26 | issue = 3 | pages = 307–13 | date = Nov 2000 | pmid = 11062469 | doi = 10.1038/81603 }}</ref>  and
+* [[XPB]].<ref name = pmid8152490/><ref name = pmid8652557/><ref name = pmid15220921>{{cite journal | vauthors = Giglia-Mari G, Coin F, Ranish JA, Hoogstraten D, Theil A, Wijgers N, Jaspers NG, Raams A, Argentini M, van der Spek PJ, Botta E, Stefanini M, Egly JM, Aebersold R, Hoeijmakers JH, Vermeulen W | title = A new, tenth subunit of TFIIH is responsible for the DNA repair syndrome trichothiodystrophy group A | journal = Nature Genetics | volume = 36 | issue = 7 | pages = 714–9 | date = Jul 2004 | pmid = 15220921 | doi = 10.1038/ng1387 }}</ref><ref name = pmid9118947>{{cite journal | vauthors = Marinoni JC, Roy R, Vermeulen W, Miniou P, Lutz Y, Weeda G, Seroz T, Gomez DM, Hoeijmakers JH, Egly JM | title = Cloning and characterization of p52, the fifth subunit of the core of the transcription/DNA repair factor TFIIH | journal = The EMBO Journal | volume = 16 | issue = 5 | pages = 1093–102 | date = Mar 1997 | pmid = 9118947 | pmc = 1169708 | doi = 10.1093/emboj/16.5.1093 }}</ref>
-XPD is essential for the viability of cells. Deletion of XPD in mice is embryonic lethal.
+== Interactive pathway map ==
+{{FluoropyrimidineActivity WP1601|highlight=ERCC2}}
-==See also==
+== See also ==
 *[[Excision repair cross-complementing]]
-==References==
+== References ==
-{{reflist|2}}
+{{reflist|33em}}
-==Further reading==
-{{refbegin | 2}}
+== Further reading ==
-{{PBB_Further_reading
+{{refbegin|33em}}
-| citations =
+* {{cite journal | vauthors = Broughton BC, Thompson AF, Harcourt SA, Vermeulen W, Hoeijmakers JH, Botta E, Stefanini M, King MD, Weber CA, Cole J | title = Molecular and cellular analysis of the DNA repair defect in a patient in xeroderma pigmentosum complementation group D who has the clinical features of xeroderma pigmentosum and Cockayne syndrome | journal = American Journal of Human Genetics | volume = 56 | issue = 1 | pages = 167–74 | date = Jan 1995 | pmid = 7825573 | pmc = 1801309 | doi =  }}
-*{{cite journal  | author=Broughton BC, Thompson AF, Harcourt SA, ''et al.'' |title=Molecular and cellular analysis of the DNA repair defect in a patient in xeroderma pigmentosum complementation group D who has the clinical features of xeroderma pigmentosum and Cockayne syndrome. |journal=Am. J. Hum. Genet. |volume=56 |issue= 1 |pages= 167–74 |year= 1995 |pmid= 7825573 |doi=  }}
+* {{cite journal | vauthors = Jeang KT | title = Tat, Tat-associated kinase, and transcription | journal = Journal of Biomedical Science | volume = 5 | issue = 1 | pages = 24–7 | year = 1998 | pmid = 9570510 | doi = 10.1007/BF02253352 }}
-*{{cite journal  | author=Jeang KT |title=Tat, Tat-associated kinase, and transcription. |journal=J. Biomed. Sci. |volume=5 |issue= 1 |pages= 24–7 |year= 1998 |pmid= 9570510 |doi=  }}
+* {{cite journal | vauthors = Yankulov K, Bentley D | title = Transcriptional control: Tat cofactors and transcriptional elongation | journal = Current Biology | volume = 8 | issue = 13 | pages = R447-9 | date = Jun 1998 | pmid = 9651670 | doi = 10.1016/S0960-9822(98)70289-1 }}
-*{{cite journal  | author=Yankulov K, Bentley D |title=Transcriptional control: Tat cofactors and transcriptional elongation. |journal=Curr. Biol. |volume=8 |issue= 13 |pages= R447–9 |year= 1998 |pmid= 9651670 |doi=  }}
+* {{cite journal | vauthors = Cleaver JE, Thompson LH, Richardson AS, States JC | title = A summary of mutations in the UV-sensitive disorders: xeroderma pigmentosum, Cockayne syndrome, and trichothiodystrophy | journal = Human Mutation | volume = 14 | issue = 1 | pages = 9–22 | year = 1999 | pmid = 10447254 | doi = 10.1002/(SICI)1098-1004(1999)14:1<9::AID-HUMU2>3.0.CO;2-6 }}
-*{{cite journal  | author=Cleaver JE, Thompson LH, Richardson AS, States JC |title=A summary of mutations in the UV-sensitive disorders: xeroderma pigmentosum, Cockayne syndrome, and trichothiodystrophy. |journal=Hum. Mutat. |volume=14 |issue= 1 |pages= 9–22 |year= 1999 |pmid= 10447254 |doi= 10.1002/(SICI)1098-1004(1999)14:1<9::AID-HUMU2>3.0.CO;2-6 |doilabel=10.1002/(SICI)1098-1004(1999)14:1&#60;9::AID-HUMU2&#62;3.0.CO;2-6 }}
+* {{cite journal | vauthors = Lehmann AR | title = The xeroderma pigmentosum group D (XPD) gene: one gene, two functions, three diseases | journal = Genes & Development | volume = 15 | issue = 1 | pages = 15–23 | date = Jan 2001 | pmid = 11156600 | doi = 10.1101/gad.859501 }}
-*{{cite journal  | author=Lehmann AR |title=The xeroderma pigmentosum group D (XPD) gene: one gene, two functions, three diseases. |journal=Genes Dev. |volume=15 |issue= 1 |pages= 15–23 |year= 2001 |pmid= 11156600 |doi=  }}
+* {{cite journal | vauthors = Benhamou S, Sarasin A | title = ERCC2/XPD gene polymorphisms and cancer risk | journal = Mutagenesis | volume = 17 | issue = 6 | pages = 463–9 | date = Nov 2002 | pmid = 12435843 | doi = 10.1093/mutage/17.6.463 }}
-*{{cite journal  | author=Benhamou S, Sarasin A |title=ERCC2/XPD gene polymorphisms and cancer risk. |journal=Mutagenesis |volume=17 |issue= 6 |pages= 463–9 |year= 2003 |pmid= 12435843 |doi=  }}
+* {{cite journal | vauthors = Clarkson SG, Wood RD | title = Polymorphisms in the human XPD (ERCC2) gene, DNA repair capacity and cancer susceptibility: an appraisal | journal = DNA Repair | volume = 4 | issue = 10 | pages = 1068–74 | date = Sep 2005 | pmid = 16054878 | doi = 10.1016/j.dnarep.2005.07.001 }}
-*{{cite journal  | author=Clarkson SG, Wood RD |title=Polymorphisms in the human XPD (ERCC2) gene, DNA repair capacity and cancer susceptibility: an appraisal. |journal=DNA Repair (Amst.) |volume=4 |issue= 10 |pages= 1068–74 |year= 2006 |pmid= 16054878 |doi= 10.1016/j.dnarep.2005.07.001 }}
-}}
 {{refend}}
-==External links==
+== External links ==
+* [https://www.ncbi.nlm.nih.gov/bookshelf/br.fcgi?book=gene&part=xp  GeneReviews/NIH/NCBI/UW entry on Xeroderma Pigmentosum]
 * {{MeshName|ERCC2+Protein}}
-<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
-{{PBB_Controls
+{{DNA repair}}
-| update_page = yes
-| require_manual_inspection = no
+[[Category:Oncogenes]]
-| update_protein_box = yes
-| update_summary = no
-| update_citations = yes
-}}
-{{WH}}
-{{WS}}

v t e 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 DNA mismatch repair MLH1 MSH2
Other forms of repair	Transcription-coupled repair ERCC6 ERCC8 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/RAD51 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