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XPG

Protein FULL name:

DNA-repair protein complementing XP-G cells (Xeroderma pigmentosum group G-complementing protein) (DNA excision repair protein ERCC-5).


Protein SHORT name:

XPG, XP-G, ERCC5, ERCC-5


XPG (Homo sapiens) is product of expression of ERCC5 gene.

Human diseases related to this protein:

XPG is involved in:

NER in Homo sapiens
     


Keywords:



FUNCTION: Single-stranded structure-specific DNA endonuclease involved in DNA excision repair. Makes the 3'incision in DNA nucleotide excision repair (NER). Acts as a cofactor for a DNA glycosylase that removes oxidized pyrimidines from DNA. May also be involved in transcription-coupled repair of this kind of damage, in transcription by RNA polymerase II, and perhaps in other processes too.

COFACTOR: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding (By similarity).

SUBUNIT: Interacts with PCNA.

SUBCELLULAR LOCATION: Nucleus.

DISEASE: Defects in ERCC5 are the cause of xeroderma pigmentosum complementation group G (XP-G) [MIM:278780]; also known as xeroderma pigmentosum VII (XP7). Xeroderma pigmentosum is an autosomal recessive pigmentary skin disorder characterized by solar hypersensitivity of the skin, high predisposition for developing cancers on areas exposed to sunlight and, in some cases, neurological abnormalities. Some XP-G patients present features of Cockayne syndrome, including dwarfism, sensorineural deafness, microcephaly, mental retardation, pigmentary retinopathy, ataxia, decreased nerve conduction velocities.

SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. XPG subfamily.

WEB RESOURCE: Name=Allelic variations of the XP genes; [LINK]

WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; [LINK]

WEB RESOURCE: Name=GeneReviews; [LINK]

WEB RESOURCE: Name=NIEHS-SNPs; [LINK]


NCBI GenPept GI number(s): 160332328
51988900
267420
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot P28715 P28715
PFAM: PF00867
PF00752
PF00867
PF00752
InterPro: IPR008918
IPR006085
IPR006086
IPR001044
IPR006084
IPR008918
IPR006085
IPR006086
IPR001044
IPR006084
CATH: - -
SCOP: - -
PDB: - -


Protein sequence:
MGVQGLWKLLECSGRQVSPEALEGKILAVDISIWLNQALKGVRDRHGNSI
ENPHLLTLFHRLCKLLFFRIRPIFVFDGDAPLLKKQTLVKRRQRKDLASS
DSRKTTEKLLKTFLKRQAIKTAFRSKRDEALPSLTQVRRENDLYVLPPLQ
EEEKHSSEEEDEKEWQERMNQKQALQEEFFHNPQAIDIESEDFSSLPPEV
KHEILTDMKEFTKRRRTLFEAMPEESDDFSQYQLKGLLKKNYLNQHIEHV
QKEMNQQHSGHIRRQYEDEGGFLKEVESRRVVSEDTSHYILIKGIQAKTV
AEVDSESLPSSSKMHGMSFDVKSSPCEKLKTEKEPDATPPSPRTLLAMQA
ALLGSSSEEELESENRRQARGRNAPAAVDEGSISPRTLSAIKRALDDDED
VKVCAGDDVQTGGPGAEEMRINSSTENSDEGLKVRDGKGIPFTATLASSS
VNSAEEHVASTNEGREPTDSVPKEQMSLVHVGTEAFPISDESMIKDRKDR
LPLESAVVRHSDAPGLPNGRELTPASPTCTNSVSKNETHAEVLEQQNELC
PYESKFDSSLLSSDDETKCKPNSASEVIGPVSLQETSSIVSVPSEAVDNV
ENVVSFNAKEHENFLETIQEQQTTESAGQDLISIPKAVEPMEIDSEESES
DGSFIEVQSVISDEELQAEFPETSKPPSEQGEEELVGTREGEAPAESESL
LRDNSERDDVDGEPQEAEKDAEDSLHEWQDINLEELETLESNLLAQQNSL
KAQKQQQERIAATVTGQMFLESQELLRLFGIPYIQAPMEAEAQCAILDLT
DQTSGTITDDSDIWLFGARHVYRNFFNKNKFVEYYQYVDFHNQLGLDRNK
LINLAYLLGSDYTEGIPTVGCVTAMEILNEFPGHGLEPLLKFSEWWHEAQ
KNPKIRPNPHDTKVKKKLRTLQLTPGFPNPAVAEAYLKPVVDDSKGSFLW
GKPDLDKIREFCQRYFGWNRTKTDESLFPVLKQLDAQQTQLRIDSFFRLA
QQEKEDAKRIKSQRLNRAVTCMLRKEKEAAASEIEAVSVAMEKEFELLDK
AKRKTQKRGITNTLEESSSLKRKRLSDSKRKNTCGGFLGETCLSESSDGS
SSEDAESSSLMNVQRRTAAKEPKTSASDSQNSVKEAPVKNGGATTSSSSD
SDDDGGKEKMVLVTARSVFGKKRRKLRRARGRKRKT

References:

Title Authors Journal
Complementation of the DNA repair defect in xeroderma pigmentosum group G cells by a human cDNA related to yeast RAD2. Scherly D, Nouspikel T, Corlet J, Ucla C, Bairoch A, Clarkson SG Nature May 13, 1993
Human ERCC5 cDNA-cosmid complementation for excision repair and bipartite amino acid domains conserved with RAD proteins of Saccharomyces cerevisiae and Schizosaccharomyces pombe. MacInnes MA, Dickson JA, Hernandez RR, Learmonth D, Lin GY, Mudgett JS, Park MS, Schauer S, Reynolds RJ, Strniste GF, et al. Mol Cell Biol Oct. 1, 1993
An ERCC5 gene with homology to yeast RAD2 is involved in group G xeroderma pigmentosum. Shiomi T, Harada Y, Saito T, Shiomi N, Okuno Y, Yamaizumi M Mutat Res March 1, 1994
The human gene for xeroderma pigmentosum complementation group G (XPG) maps to 13q33 by fluorescence in situ hybridization. Samec S, Jones TA, Corlet J, Scherly D, Sheer D, Wood RD, Clarkson SG Genomics May 1, 1994
Mutations that disable the DNA repair gene XPG in a xeroderma pigmentosum group G patient. Nouspikel T, Clarkson SG Hum Mol Genet June 1, 1994
Isolation of active recombinant XPG protein, a human DNA repair endonuclease. O'Donovan A, Scherly D, Clarkson SG, Wood RD J Biol Chem June 10, 1994
Human xeroderma pigmentosum group G gene encodes a DNA endonuclease. Habraken Y, Sung P, Prakash L, Prakash S Nucleic Acids Res Aug. 25, 1994
XPG endonuclease makes the 3' incision in human DNA nucleotide excision repair. O'Donovan A, Davies AA, Moggs JG, West SC, Wood RD Nature Sept. 1, 1994
XPG protein has a structure-specific endonuclease activity. Cloud KG, Shen B, Strniste GF, Park MS Mutat Res July 1, 1995
A common mutational pattern in Cockayne syndrome patients from xeroderma pigmentosum group G: implications for a second XPG function. Nouspikel T, Lalle P, Leadon SA, Cooper PK, Clarkson SG Proc Natl Acad Sci U S A April 1, 1997
The DNA repair endonuclease XPG binds to proliferating cell nuclear antigen (PCNA) and shares sequence elements with the PCNA-binding regions of FEN-1 and cyclin-dependent kinase inhibitor p21. Gary R, Ludwig DL, Cornelius HL, MacInnes MA, Park MS J Biol Chem Sept. 26, 1997
A summary of mutations in the UV-sensitive disorders: xeroderma pigmentosum, Cockayne syndrome, and trichothiodystrophy. Cleaver JE, Thompson LH, Richardson AS, States JC Hum Mutat Jan. 1, 1999
Xeroderma pigmentosum group G with severe neurological involvement and features of Cockayne syndrome in infancy. Zafeiriou DI, Thorel F, Andreou A, Kleijer WJ, Raams A, Garritsen VH, Gombakis N, Jaspers NG, Clarkson SG Pediatr Res March 1, 2001
The human XPG gene: gene architecture, alternative splicing and single nucleotide polymorphisms. Emmert S, Schneider TD, Khan SG, Kraemer KH Nucleic Acids Res April 1, 2001
The founding members of xeroderma pigmentosum group G produce XPG protein with severely impaired endonuclease activity. Lalle P, Nouspikel T, Constantinou A, Thorel F, Clarkson SG J Invest Dermatol Jan. 1, 2002
Relationship of neurologic degeneration to genotype in three xeroderma pigmentosum group G patients. Emmert S, Slor H, Busch DB, Batko S, Albert RB, Coleman D, Khan SG, Abu-Libdeh B, DiGiovanna JJ, Cunningham BB, Lee MM, Crollick J, Inui H, Ueda T, Hedayati M, Grossman L, Shahlavi T, Cleaver JE, Kraemer KH J Invest Dermatol June 1, 2002
The XPG story. Clarkson SG Biochimie Nov. 1, 2003
The DNA sequence and analysis of human chromosome 13. Dunham A, Matthews LH, Burton J, Ashurst JL, Howe KL, Ashcroft KJ, Beare DM, Burford DC, Hunt SE, Griffiths-Jones S, Jones MC, Keenan SJ, Oliver K, Scott CE, Ainscough R, Almeida JP, Ambrose KD, Andrews DT, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Bannerjee R, Barlow KF, Bates K, Beasley H, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burrill W, Carder C, Carter NP, Chapman JC, Clamp ME, Clark SY, Clarke G, Clee CM, Clegg SC, Cobley V, Collins JE, Corby N, Coville GJ, Deloukas P, Dhami P, Dunham I, Dunn M, Earthrowl ME, Ellington AG, Faulkner L, Frankish AG, Frankland J, French L, Garner P, Garnett J, Gilbert JG, Gilson CJ, Ghori J, Grafham DV, Gribble SM, Griffiths C, Hall RE, Hammond S, Harley JL, Hart EA, Heath PD, Howden PJ, Huckle EJ, Hunt PJ, Hunt AR, Johnson C, Johnson D, Kay M, Kimberley AM, King A, Laird GK, Langford CJ, Lawlor S, Leongamornlert DA, Lloyd DM, Lloyd C, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, McLaren SJ, McMurray A, Milne S, Moore MJ, Nickerson T, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter KM, Rice CM, Searle S, Sehra HK, Shownkeen R, Skuce CD, Smith M, Steward CA, Sycamore N, Tester J, Thomas DW, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Wilming L, Wray PW, Wright MW, Young L, Coulson A, Durbin R, Hubbard T, Sulston JE, Beck S, Bentley DR, Rogers J, Ross MT Nature April 1, 2004
Large-scale characterization of HeLa cell nuclear phosphoproteins. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP Proc Natl Acad Sci U S A Aug. 17, 2004
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J Genome Res Oct. 1, 2004
Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M Cell Nov. 3, 2006
Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y Anal Sci Feb. 1, 2008
Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd J Proteome Res March 1, 2008
A quantitative atlas of mitotic phosphorylation. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP Proc Natl Acad Sci U S A Aug. 5, 2008
Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M Mol Cell Aug. 8, 2008
Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK Sci Signal Jan. 1, 2009
Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S Anal Chem June 1, 2009
Lysine acetylation targets protein complexes and co-regulates major cellular functions. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M Science Aug. 14, 2009


Last modification of this entry: Oct. 19, 2010.

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