P28715 (ERCC5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA repair protein complementing XP-G cells
EC=3.1.-.-

Alternative name(s):
DNA excision repair protein ERCC-5
Xeroderma pigmentosum group G-complementing protein

Gene names

Name:	ERCC5
Synonyms:	ERCM2, XPG, XPGC

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1186 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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 structure	Interacts with PCNA. Ref.14
Subcellular location	Nucleus Ref.13.
Involvement in disease	Xeroderma pigmentosum complementation group G (XP-G) [MIM:278780]: 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. The skin develops marked freckling and other pigmentation abnormalities. Some XP-G patients present features of Cockayne syndrome, cachectic dwarfism, pigmentary retinopathy, ataxia, decreased nerve conduction velocities. The phenotype combining xeroderma pigmentosum and Cockayne syndrome traits is referred to as XP-CS complex. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.27 Ref.28 Ref.29 Ref.30 Ref.31
Sequence similarities	Belongs to the XPG/RAD2 endonuclease family. XPG subfamily.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Cockayne syndrome Deafness Disease mutation Dwarfism Xeroderma pigmentosum
Ligand	DNA-binding Magnesium Metal-binding
Molecular function	Endonuclease Hydrolase Nuclease
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	UV protection Inferred from genetic interaction Ref.2. Source: MGI determination of adult lifespan Inferred from electronic annotation. Source: Compara multicellular organism growth Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from mutant phenotype PubMed 16167068. Source: UniProtKB nucleotide-excision repair, DNA damage removal Traceable author statement. Source: Reactome nucleotide-excision repair, DNA incision, 3'-to lesion Inferred from direct assay Ref.11. Source: UniProtKB response to UV-C Inferred from mutant phenotype PubMed 17208056. Source: UniProtKB transcription-coupled nucleotide-excision repair Inferred from mutant phenotype PubMed 16246722. Source: UniProtKB
Cellular_component	nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	bubble DNA binding Inferred from direct assay PubMed 16246722. Source: UniProtKB double-stranded DNA binding Inferred from direct assay PubMed 12644470Ref.11. Source: UniProtKB endodeoxyribonuclease activity Inferred from direct assay PubMed 12644470Ref.11. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW single-stranded DNA binding Inferred from direct assay PubMed 12644470. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P28715-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P28715-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-767: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1186	1186	DNA repair protein complementing XP-G cells		PRO_0000154031
Regions
	Region	1 – 95	95	N-domain
	Region	753 – 881	129	I-domain
	Region	981 – 1009	29	Interaction with PCNA
	Motif	1057 – 1073	17	Nuclear localization signal Potential
Sites
	Metal binding	30	1	Magnesium 1 By similarity
	Metal binding	77	1	Magnesium 1 By similarity
	Metal binding	789	1	Magnesium 1 By similarity
	Metal binding	791	1	Magnesium 1 By similarity
	Metal binding	810	1	Magnesium 2 By similarity
	Metal binding	812	1	Magnesium 2 By similarity
	Metal binding	861	1	Magnesium 2 By similarity
Amino acid modifications
	Modified residue	8	1	N6-acetyllysine Ref.23
	Modified residue	156	1	Phosphoserine Ref.21 Ref.26
	Modified residue	157	1	Phosphoserine Ref.21 Ref.26
	Modified residue	338	1	Phosphothreonine Ref.21
	Modified residue	341	1	Phosphoserine Ref.21
	Modified residue	355	1	Phosphoserine Ref.24
	Modified residue	356	1	Phosphoserine Ref.24
	Modified residue	357	1	Phosphoserine Ref.21 Ref.24
	Modified residue	363	1	Phosphoserine Ref.24
	Modified residue	384	1	Phosphoserine Ref.24 Ref.26
	Modified residue	423	1	Phosphoserine Ref.21
	Modified residue	428	1	Phosphoserine Ref.21
	Modified residue	559	1	Phosphoserine Ref.21 Ref.22
	Modified residue	562	1	Phosphoserine Ref.21 Ref.22 Ref.24
	Modified residue	563	1	Phosphoserine Ref.21 Ref.22 Ref.24 Ref.26
	Modified residue	705	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	1 – 767	767	Missing in isoform 2.		VSP_035380
	Natural variant	72	1	P → H in XP-G; combined with features of Cockayne syndrome. Ref.29		VAR_015280
	Natural variant	145	1	V → I. Corresponds to variant rs4987063 [ dbSNP | Ensembl ].		VAR_020431
	Natural variant	181	1	H → R. Ref.6 Corresponds to variant rs4150295 [ dbSNP | Ensembl ].		VAR_023120
	Natural variant	254	1	M → V. Ref.2 Ref.3 Ref.5 Ref.6 Corresponds to variant rs1047769 [ dbSNP | Ensembl ].		VAR_007732
	Natural variant	256	1	Q → R. Ref.6 Corresponds to variant rs4150313 [ dbSNP | Ensembl ].		VAR_020432
	Natural variant	311	1	S → C. Ref.6 Corresponds to variant rs2307491 [ dbSNP | Ensembl ].		VAR_014829
	Natural variant	399	1	E → K. Ref.6 Corresponds to variant rs4150315 [ dbSNP | Ensembl ].		VAR_023121
	Natural variant	529	1	C → S. Ref.6 Corresponds to variant rs2227869 [ dbSNP | Ensembl ].		VAR_020433
	Natural variant	590	1	V → I. Ref.6 Corresponds to variant rs4150318 [ dbSNP | Ensembl ].		VAR_023122
	Natural variant	597	1	V → L. Ref.6 Corresponds to variant rs4150319 [ dbSNP | Ensembl ].		VAR_023123
	Natural variant	670	1	F → L. Corresponds to variant rs1803542 [ dbSNP | Ensembl ].		VAR_046373
	Natural variant	680	1	Q → R. Corresponds to variant rs4987168 [ dbSNP | Ensembl ].		VAR_020434
	Natural variant	792	1	A → V in XP-G; mild form. Ref.27 Ref.28		VAR_007733
	Natural variant	858	1	L → P in XP-G; reduced stability and greatly impaired endonuclease activity. Ref.30		VAR_017097
	Natural variant	874	1	A → T in XP-G; mild form; residual activity. Ref.31 Corresponds to variant rs28929496 [ dbSNP | Ensembl ].		VAR_017096
	Natural variant	879	1	N → S. Ref.6 Corresponds to variant rs4150342 [ dbSNP | Ensembl ].		VAR_020435
	Natural variant	1009	1	R → H. Ref.6 Corresponds to variant rs4150387 [ dbSNP | Ensembl ].		VAR_023124
	Natural variant	1053	1	G → R. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6 Ref.8 Corresponds to variant rs9514066 [ dbSNP | Ensembl ].		VAR_046374
	Natural variant	1080	1	G → Q. Ref.6		VAR_023125
	Natural variant	1080	1	G → R. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6 Ref.8 Corresponds to variant rs9514067 [ dbSNP | Ensembl ].		VAR_046375
	Natural variant	1104	1	D → H. Ref.1 Corresponds to variant rs17655 [ dbSNP | Ensembl ].		VAR_007734
	Natural variant	1119	1	A → V. Corresponds to variant rs2227871 [ dbSNP | Ensembl ].		VAR_020436
Experimental info
	Sequence conflict	55	1	L → P in BAA03812. Ref.2
	Sequence conflict	120 – 122	3	KTA → QTS in BAA03812. Ref.2
	Sequence conflict	126	1	K → Q in BAA03812. Ref.2
	Sequence conflict	264 – 266	3	RQY → SSH in BAA03812. Ref.2
	Sequence conflict	760	1	I → F in BAA03812. Ref.2
	Sequence conflict	796	1	I → V in BAA03812. Ref.2
	Sequence conflict	864 – 872	9	EGIPTVGCV → GNTNCGLC in BAA03812. Ref.2
	Sequence conflict	959	1	R → S in BAA03812. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 2, 2008. Version 3. Checksum: B0A844D617C53F2E	FASTA	1,186	133,108
	10 20 30 40 50 60 MGVQGLWKLL ECSGRQVSPE ALEGKILAVD ISIWLNQALK GVRDRHGNSI ENPHLLTLFH 70 80 90 100 110 120 RLCKLLFFRI RPIFVFDGDA PLLKKQTLVK RRQRKDLASS DSRKTTEKLL KTFLKRQAIK 130 140 150 160 170 180 TAFRSKRDEA LPSLTQVRRE NDLYVLPPLQ EEEKHSSEEE DEKEWQERMN QKQALQEEFF 190 200 210 220 230 240 HNPQAIDIES EDFSSLPPEV KHEILTDMKE FTKRRRTLFE AMPEESDDFS QYQLKGLLKK 250 260 270 280 290 300 NYLNQHIEHV QKEMNQQHSG HIRRQYEDEG GFLKEVESRR VVSEDTSHYI LIKGIQAKTV 310 320 330 340 350 360 AEVDSESLPS SSKMHGMSFD VKSSPCEKLK TEKEPDATPP SPRTLLAMQA ALLGSSSEEE 370 380 390 400 410 420 LESENRRQAR GRNAPAAVDE GSISPRTLSA IKRALDDDED VKVCAGDDVQ TGGPGAEEMR 430 440 450 460 470 480 INSSTENSDE GLKVRDGKGI PFTATLASSS VNSAEEHVAS TNEGREPTDS VPKEQMSLVH 490 500 510 520 530 540 VGTEAFPISD ESMIKDRKDR LPLESAVVRH SDAPGLPNGR ELTPASPTCT NSVSKNETHA 550 560 570 580 590 600 EVLEQQNELC PYESKFDSSL LSSDDETKCK PNSASEVIGP VSLQETSSIV SVPSEAVDNV 610 620 630 640 650 660 ENVVSFNAKE HENFLETIQE QQTTESAGQD LISIPKAVEP MEIDSEESES DGSFIEVQSV 670 680 690 700 710 720 ISDEELQAEF PETSKPPSEQ GEEELVGTRE GEAPAESESL LRDNSERDDV DGEPQEAEKD 730 740 750 760 770 780 AEDSLHEWQD INLEELETLE SNLLAQQNSL KAQKQQQERI AATVTGQMFL ESQELLRLFG 790 800 810 820 830 840 IPYIQAPMEA EAQCAILDLT DQTSGTITDD SDIWLFGARH VYRNFFNKNK FVEYYQYVDF 850 860 870 880 890 900 HNQLGLDRNK LINLAYLLGS DYTEGIPTVG CVTAMEILNE FPGHGLEPLL KFSEWWHEAQ 910 920 930 940 950 960 KNPKIRPNPH DTKVKKKLRT LQLTPGFPNP AVAEAYLKPV VDDSKGSFLW GKPDLDKIRE 970 980 990 1000 1010 1020 FCQRYFGWNR TKTDESLFPV LKQLDAQQTQ LRIDSFFRLA QQEKEDAKRI KSQRLNRAVT 1030 1040 1050 1060 1070 1080 CMLRKEKEAA ASEIEAVSVA MEKEFELLDK AKGKTQKRGI TNTLEESSSL KRKRLSDSKG 1090 1100 1110 1120 1130 1140 KNTCGGFLGE TCLSESSDGS SSEDAESSSL MNVQRRTAAK EPKTSASDSQ NSVKEAPVKN 1150 1160 1170 1180 GGATTSSSSD SDDDGGKEKM VLVTARSVFG KKRRKLRRAR GRKRKT
	Isoform 2 [UniParc]. Checksum: A26C01C3C1DFAC28	FASTA	419	47,319
	10 20 30 40 50 60 MFLESQELLR LFGIPYIQAP MEAEAQCAIL DLTDQTSGTI TDDSDIWLFG ARHVYRNFFN 70 80 90 100 110 120 KNKFVEYYQY VDFHNQLGLD RNKLINLAYL LGSDYTEGIP TVGCVTAMEI LNEFPGHGLE 130 140 150 160 170 180 PLLKFSEWWH EAQKNPKIRP NPHDTKVKKK LRTLQLTPGF PNPAVAEAYL KPVVDDSKGS 190 200 210 220 230 240 FLWGKPDLDK IREFCQRYFG WNRTKTDESL FPVLKQLDAQ QTQLRIDSFF RLAQQEKEDA 250 260 270 280 290 300 KRIKSQRLNR AVTCMLRKEK EAAASEIEAV SVAMEKEFEL LDKAKGKTQK RGITNTLEES 310 320 330 340 350 360 SSLKRKRLSD SKGKNTCGGF LGETCLSESS DGSSSEDAES SSLMNVQRRT AAKEPKTSAS 370 380 390 400 410 DSQNSVKEAP VKNGGATTSS SSDSDDDGGK EKMVLVTARS VFGKKRRKLR RARGRKRKT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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 S.G. Nature 363:182-185(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ARG-1053; ARG-1080 AND HIS-1104.
[2]	"An ERCC5 gene with homology to yeast RAD2 is involved in group G Xeroderma pigmentosum." Shiomi T., Harada Y.-N., Saito T., Shiomi N., Okuno Y., Yamaizumi M. Mutat. Res. 314:167-175(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS VAL-254; ARG-1053 AND ARG-1080.
[3]	"Human ERCC5 cDNA-cosmid complementation for excision repair and bipartite amino acid domains conserved with RAD proteins of Saccharomyces cerevisiae and Schizosaccharomyces pombe." Macinnes M.A., Dickson J.A., Hernandez R.R., Learmonth D., Lin G.Y., Mudgett J.S., Park M.S., Schauer S., Reynolds R.J., Strniste G.F., Yu J.Y. Mol. Cell. Biol. 13:6393-6402(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS VAL-254; ARG-1053 AND ARG-1080.
[4]	"The human XPG gene: gene architecture, alternative splicing and single nucleotide polymorphisms." Emmert S., Schneider T.D., Khan S.G., Kraemer K.H. Nucleic Acids Res. 29:1443-1452(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	Zan Q., Guo J.H., Yu L. Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS VAL-254; ARG-1053 AND ARG-1080. Tissue: Bone marrow.
[6]	NIEHS SNPs program Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-181; VAL-254; ARG-256; CYS-311; LYS-399; SER-529; ILE-590; LEU-597; SER-879; HIS-1009 AND ARG-1053; ARG-1080 AND GLN-1080.
[7]	"The DNA sequence and analysis of human chromosome 13." Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T. Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS ARG-1053 AND ARG-1080. Tissue: Eye.
[9]	"The human gene for Xeroderma pigmentosum complementation group G (XPG) maps to 13q33 by fluorescence in situ hybridization." Samec S., Jones T.A., Corlet J., Scherly D., Sheer D., Wood R.D., Clarkson S.G. Genomics 21:283-285(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-88.
[10]	"Isolation of active recombinant XPG protein, a human DNA repair endonuclease." O'Donovan A., Scherly D., Clarkson S.G., Wood R.D. J. Biol. Chem. 269:15965-15968(1994) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[11]	"XPG endonuclease makes the 3' incision in human DNA nucleotide excision repair." O'Donovan A., Davies A.A., Moggs J.G., West S.C., Wood R.D. Nature 371:432-435(1994) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[12]	"Human Xeroderma pigmentosum group G gene encodes a DNA endonuclease." Habraken Y., Sung P., Prakash L., Prakash S. Nucleic Acids Res. 22:3312-3316(1994) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[13]	"XPG protein has a structure-specific endonuclease activity." Cloud K.G., Shen B., Strniste G.F., Park M.S. Mutat. Res. 347:55-60(1995) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, SUBCELLULAR LOCATION.
[14]	"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 D.L., Cornelius H.L., MacInnes M.A., Park M.S. J. Biol. Chem. 272:24522-24529(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PCNA.
[15]	"The XPG story." Clarkson S.G. Biochimie 85:1113-1121(2003) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[16]	"A summary of mutations in the UV-sensitive disorders: xeroderma pigmentosum, Cockayne syndrome, and trichothiodystrophy." Cleaver J.E., Thompson L.H., Richardson A.S., States J.C. Hum. Mutat. 14:9-22(1999) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON VARIANTS XP-G.
[17]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[18]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[19]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[20]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[21]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156; SER-157; THR-338; SER-341; SER-357; SER-423; SER-428; SER-559; SER-562 AND SER-563, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559; SER-562 AND SER-563, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[23]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-8, MASS SPECTROMETRY.
[24]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355; SER-356; SER-357; SER-363; SER-384; SER-562 AND SER-563, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[25]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156; SER-157; SER-384 AND SER-563, MASS SPECTROMETRY.
[27]	"Mutations that disable the DNA repair gene XPG in a Xeroderma pigmentosum group G patient." Nouspikel T., Clarkson S.G. Hum. Mol. Genet. 3:963-967(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT XP-G VAL-792.
[28]	"A common mutational pattern in Cockayne syndrome patients from Xeroderma pigmentosum group G: implications for a second XPG function." Nouspikel T., Lalle P., Leadon S.A., Cooper P.K., Clarkson S.G. Proc. Natl. Acad. Sci. U.S.A. 94:3116-3121(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT XP-G VAL-792.
[29]	"Xeroderma pigmentosum group G with severe neurological involvement and features of Cockayne syndrome in infancy." Zafeiriou D.I., Thorel F., Andreou A., Kleijer W.J., Raams A., Garritsen V.H., Gombakis N., Jaspers N.G.J., Clarkson S.G. Pediatr. Res. 49:407-412(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT XP-G HIS-72.
[30]	"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 S.G. J. Invest. Dermatol. 118:344-351(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT XP-G PRO-858.
[31]	"Relationship of neurologic degeneration to genotype in three xeroderma pigmentosum group G patients." Emmert S., Slor H., Busch D.B., Batko S., Albert R.B., Coleman D., Khan S.G., Abu-Libdeh B., DiGiovanna J.J., Cunningham B.B., Lee M.M., Crollick J., Inui H., Ueda T., Hedayati M., Grossman L., Shahlavi T., Cleaver J.E., Kraemer K.H. J. Invest. Dermatol. 118:972-982(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT XP-G THR-874.
+	Additional computationally mapped references.

Web resources

Allelic variations of the XP genes

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	X69978 mRNA. Translation: CAA49598.1. D16305 mRNA. Translation: BAA03812.1. L20046 mRNA. Translation: AAC37533.1. AF255442 , AF255431, AF255433, AF255434, AF255435, AF255436, AF255437, AF255438, AF255439, AF255440, AF255441 Genomic DNA. Translation: AAF89179.1. AF462447 mRNA. Translation: AAP97715.1. AF550128 Genomic DNA. Translation: AAN46091.1. AL157769 Genomic DNA. Translation: CAI14530.1. AL157769 Genomic DNA. Translation: CAI14531.1. BC031522 mRNA. Translation: AAH31522.1. X71341, X71342 Genomic DNA. Translation: CAA50481.1.
IPI	IPI00477535. IPI00848102.
PIR	I58009. S35993.
RefSeq	NP_000114.2. NM_000123.3.
UniGene	Hs.258429.
3D structure databases
ProteinModelPortal	P28715.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-750N.
IntAct	P28715. 2 interactions.
MINT	MINT-192239.
STRING	9606.ENSP00000347978.
PTM databases
PhosphoSite	P28715.
Polymorphism databases
DMDM	205371791.
Proteomic databases
PaxDb	P28715.
PRIDE	P28715.
Protocols and materials databases
DNASU	2073.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000355739; ENSP00000347978; ENSG00000134899. ENST00000375954; ENSP00000365121; ENSG00000134899.
GeneID	2073.
KEGG	hsa:2073.
UCSC	uc001vpw.3. human.
Organism-specific databases
CTD	2073.
GeneCards	GC13P103459.
HGNC	HGNC:3437. ERCC5.
HPA	HPA045845. HPA050374.
MIM	133530. gene. 278780. phenotype.
neXtProt	NX_P28715.
Orphanet	1466. COFS syndrome. 276267. Xeroderma pigmentosum complementation group G. 220295. Xeroderma pigmentosum/Cockayne syndrome complex.
PharmGKB	PA27851.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0258.
HOVERGEN	HBG051501.
InParanoid	P28715.
KO	K10846.
OrthoDB	EOG4CNQQZ.
Enzyme and pathway databases
Reactome	REACT_216. DNA Repair.
Gene expression databases
ArrayExpress	P28715.
Bgee	P28715.
CleanEx	HS_ERCC5.
Genevestigator	P28715.
GermOnline	ENSG00000134899. Homo sapiens.
Family and domain databases
InterPro	IPR020045. 5-3_exonuclease_C. IPR008918. HhH2. IPR006086. XPG-I_dom. IPR006084. XPG/Rad2. IPR001044. XPG/Rad2_eukaryotes. IPR019974. XPG_CS. IPR006085. XPG_DNA_repair_N. [Graphical view]
PANTHER	PTHR11081. PTHR11081. 1 hit. PTHR11081:SF1. PTHR11081:SF1. 1 hit.
Pfam	PF00867. XPG_I. 1 hit. PF00752. XPG_N. 1 hit. [Graphical view]
PRINTS	PR00853. XPGRADSUPER. PR00066. XRODRMPGMNTG.
SMART	SM00279. HhH2. 1 hit. SM00484. XPGI. 1 hit. SM00485. XPGN. 1 hit. [Graphical view]
SUPFAM	SSF47807. 5_3_exo_C. 1 hit.
TIGRFAMs	TIGR00600. rad2. 1 hit.
PROSITE	PS00841. XPG_1. 1 hit. PS00842. XPG_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P28715.
ChEMBL	CHEMBL4736.
GenomeRNAi	2073.
NextBio	8433.
SOURCE	Search...

Entry information

Entry name

ERCC5_HUMAN

Accession

Primary (citable) accession number: P28715
Secondary accession number(s): A6NGT4 , Q5JUS4, Q5JUS5, Q7Z2V3, Q8IZL6, Q8N1B7, Q9HD59

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	September 2, 2008
Last modified:	May 1, 2013
This is version 159 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.