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P28715 (ERCC5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 172. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1186 AA.
Sequence statusComplete.
Protein existenceEvidence 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.19 Ref.20 Ref.21 Ref.22 Ref.23

Sequence similarities

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

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCockayne syndrome
Deafness
Disease mutation
Dwarfism
Xeroderma pigmentosum
   LigandDNA-binding
Magnesium
Metal-binding
   Molecular functionEndonuclease
Hydrolase
Nuclease
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA catabolic process, endonucleolytic

Inferred from direct assay PubMed 12644470Ref.11. Source: GOC

DNA repair

Traceable author statement. Source: Reactome

UV protection

Inferred from genetic interaction Ref.2. Source: MGI

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 16167068. Source: UniProtKB

nucleotide-excision repair

Traceable author statement. Source: Reactome

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

Inferred from direct assay PubMed 8710877. 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_componentintermediate filament cytoskeleton

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 8710877. Source: UniProtKB

   Molecular_functionbubble 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

endonuclease activity

Traceable author statement. Source: Reactome

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein N-terminus binding

Inferred from physical interaction PubMed 8652557. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 15358233PubMed 16246722PubMed 8652557Ref.14. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction PubMed 10026181. Source: UniProtKB

single-stranded DNA binding

Inferred from direct assay PubMed 12644470. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 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.
Isoform 3 (identifier: P28715-3)

The sequence of this isoform differs from the canonical sequence as follows:
     225-232: ESDDFSQY → VYLPLLQP
     233-1186: Missing.
Note: No experimental confirmation available. Includes a cryptic exon found in intron 6.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11861186DNA repair protein complementing XP-G cells
PRO_0000154031

Regions

Region1 – 9595N-domain
Region753 – 881129I-domain
Region981 – 100929Interaction with PCNA
Motif1057 – 107317Nuclear localization signal Potential

Sites

Metal binding301Magnesium 1 By similarity
Metal binding771Magnesium 1 By similarity
Metal binding7891Magnesium 1 By similarity
Metal binding7911Magnesium 1 By similarity
Metal binding8101Magnesium 2 By similarity
Metal binding8121Magnesium 2 By similarity
Metal binding8611Magnesium 2 By similarity

Amino acid modifications

Modified residue81N6-acetyllysine Ref.17
Modified residue3841Phosphoserine By similarity

Natural variations

Alternative sequence1 – 767767Missing in isoform 2.
VSP_035380
Alternative sequence225 – 2328ESDDFSQY → VYLPLLQP in isoform 3.
VSP_053828
Alternative sequence233 – 1186954Missing in isoform 3.
VSP_053829
Natural variant721P → H in XP-G; combined with features of Cockayne syndrome. Ref.21
VAR_015280
Natural variant1451V → I.
Corresponds to variant rs4987063 [ dbSNP | Ensembl ].
VAR_020431
Natural variant1811H → R. Ref.6
Corresponds to variant rs4150295 [ dbSNP | Ensembl ].
VAR_023120
Natural variant2541M → V. Ref.2 Ref.3 Ref.5 Ref.6
Corresponds to variant rs1047769 [ dbSNP | Ensembl ].
VAR_007732
Natural variant2561Q → R. Ref.6
Corresponds to variant rs4150313 [ dbSNP | Ensembl ].
VAR_020432
Natural variant3111S → C. Ref.6
Corresponds to variant rs2307491 [ dbSNP | Ensembl ].
VAR_014829
Natural variant3991E → K. Ref.6
Corresponds to variant rs4150315 [ dbSNP | Ensembl ].
VAR_023121
Natural variant5291C → S. Ref.6
Corresponds to variant rs2227869 [ dbSNP | Ensembl ].
VAR_020433
Natural variant5901V → I. Ref.6
Corresponds to variant rs4150318 [ dbSNP | Ensembl ].
VAR_023122
Natural variant5971V → L. Ref.6
Corresponds to variant rs4150319 [ dbSNP | Ensembl ].
VAR_023123
Natural variant6701F → L.
Corresponds to variant rs1803542 [ dbSNP | Ensembl ].
VAR_046373
Natural variant6801Q → R.
Corresponds to variant rs4987168 [ dbSNP | Ensembl ].
VAR_020434
Natural variant7921A → V in XP-G; mild form. Ref.19 Ref.20
VAR_007733
Natural variant8581L → P in XP-G; reduced stability and greatly impaired endonuclease activity. Ref.22
VAR_017097
Natural variant8741A → T in XP-G; mild form; residual activity. Ref.23
Corresponds to variant rs28929496 [ dbSNP | Ensembl ].
VAR_017096
Natural variant8791N → S. Ref.6
Corresponds to variant rs4150342 [ dbSNP | Ensembl ].
VAR_020435
Natural variant10091R → H. Ref.6
Corresponds to variant rs4150387 [ dbSNP | Ensembl ].
VAR_023124
Natural variant10531G → R. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6 Ref.8
Corresponds to variant rs9514066 [ dbSNP | Ensembl ].
VAR_046374
Natural variant10801G → Q Requires 2 nucleotide substitutions. Ref.6
VAR_023125
Natural variant10801G → R. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6 Ref.8
Corresponds to variant rs9514067 [ dbSNP | Ensembl ].
VAR_046375
Natural variant11041D → H. Ref.1
Corresponds to variant rs17655 [ dbSNP | Ensembl ].
VAR_007734
Natural variant11191A → V.
Corresponds to variant rs2227871 [ dbSNP | Ensembl ].
VAR_020436

Experimental info

Sequence conflict551L → P in BAA03812. Ref.2
Sequence conflict120 – 1223KTA → QTS in BAA03812. Ref.2
Sequence conflict1261K → Q in BAA03812. Ref.2
Sequence conflict264 – 2663RQY → SSH in BAA03812. Ref.2
Sequence conflict7601I → F in BAA03812. Ref.2
Sequence conflict7961I → V in BAA03812. Ref.2
Sequence conflict864 – 8729EGIPTVGCV → GNTNCGLC in BAA03812. Ref.2
Sequence conflict9591R → S in BAA03812. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 2, 2008. Version 3.
Checksum: B0A844D617C53F2E

FASTA1,186133,108
        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 

« Hide

Isoform 2 [UniParc].

Checksum: A26C01C3C1DFAC28
Show »

FASTA41947,319
Isoform 3 [UniParc].

Checksum: E2808BE7528D94F1
Show »

FASTA23227,259

References

« Hide '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], ALTERNATIVE SPLICING (ISOFORMS 1 AND 3).
[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. expand/collapse author list , 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]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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].
[19]"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.
[20]"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.
[21]"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.
[22]"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.
[23]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X69978 mRNA. Translation: CAA49598.1.
D16305 mRNA. Translation: BAA03812.1.
L20046 mRNA. Translation: AAC37533.1.
AF255436 expand/collapse EMBL AC list , AF255431, AF255433, AF255434, AF255435 Genomic DNA. Translation: AAF89178.1.
AF255442 expand/collapse EMBL AC list , 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.
CCDSCCDS32004.1. [P28715-1]
PIRI58009.
S35993.
RefSeqNP_000114.2. NM_000123.3.
UniGeneHs.258429.

3D structure databases

ProteinModelPortalP28715.
SMRP28715. Positions 2-95, 711-977.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108385. 14 interactions.
DIPDIP-750N.
IntActP28715. 3 interactions.
MINTMINT-192239.
STRING9606.ENSP00000347978.

Chemistry

BindingDBP28715.
ChEMBLCHEMBL4736.

PTM databases

PhosphoSiteP28715.

Polymorphism databases

DMDM205371791.

Proteomic databases

MaxQBP28715.
PaxDbP28715.
PRIDEP28715.

Protocols and materials databases

DNASU2073.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000355739; ENSP00000347978; ENSG00000134899. [P28715-1]
ENST00000375954; ENSP00000365121; ENSG00000134899. [P28715-2]
ENST00000535557; ENSP00000442117; ENSG00000134899.
GeneID2073.
KEGGhsa:2073.
UCSCuc001vpw.3. human. [P28715-1]

Organism-specific databases

CTD2073.
GeneCardsGC13P103497.
GeneReviewsERCC5.
HGNCHGNC:3437. ERCC5.
HPAHPA045845.
HPA050374.
MIM133530. gene.
278780. phenotype.
neXtProtNX_P28715.
Orphanet1466. COFS syndrome.
276267. Xeroderma pigmentosum complementation group G.
PharmGKBPA27851.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0258.
HOVERGENHBG051501.
InParanoidP28715.
KOK10846.
OMAHDTKVKR.
OrthoDBEOG72ZCD4.
PhylomeDBP28715.
TreeFamTF101235.

Enzyme and pathway databases

ReactomeREACT_216. DNA Repair.

Gene expression databases

ArrayExpressP28715.
BgeeP28715.
CleanExHS_ERCC5.
GenevestigatorP28715.

Family and domain databases

Gene3D3.40.50.1010. 2 hits.
InterProIPR020045. 5-3_exonuclease_C.
IPR008918. HhH2.
IPR029060. PIN_domain-like.
IPR006086. XPG-I_dom.
IPR001044. XPG/Rad2_eukaryotes.
IPR019974. XPG_CS.
IPR006085. XPG_DNA_repair_N.
[Graphical view]
PfamPF00867. XPG_I. 1 hit.
PF00752. XPG_N. 1 hit.
[Graphical view]
PRINTSPR00066. XRODRMPGMNTG.
SMARTSM00279. HhH2. 1 hit.
SM00484. XPGI. 1 hit.
SM00485. XPGN. 1 hit.
[Graphical view]
SUPFAMSSF47807. SSF47807. 2 hits.
SSF88723. SSF88723. 2 hits.
TIGRFAMsTIGR00600. rad2. 1 hit.
PROSITEPS00841. XPG_1. 1 hit.
PS00842. XPG_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiERCC5.
GenomeRNAi2073.
NextBio8433.
PROP28715.
SOURCESearch...

Entry information

Entry nameERCC5_HUMAN
AccessionPrimary (citable) accession number: P28715
Secondary accession number(s): A6NGT4 expand/collapse secondary AC list , Q5JUS4, Q5JUS5, Q7Z2V3, Q8IZL6, Q8N1B7, Q9HD59, Q9HD60
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: September 2, 2008
Last modified: July 9, 2014
This is version 172 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM