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P28715

- ERCC5_HUMAN

UniProt

P28715 - ERCC5_HUMAN

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Protein
DNA repair protein complementing XP-G cells
Gene
ERCC5, ERCM2, XPG, XPGC
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

Cofactori

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi30 – 301Magnesium 1 By similarity
Metal bindingi77 – 771Magnesium 1 By similarity
Metal bindingi789 – 7891Magnesium 1 By similarity
Metal bindingi791 – 7911Magnesium 1 By similarity
Metal bindingi810 – 8101Magnesium 2 By similarity
Metal bindingi812 – 8121Magnesium 2 By similarity
Metal bindingi861 – 8611Magnesium 2 By similarity

GO - Molecular functioni

  1. bubble DNA binding Source: UniProtKB
  2. double-stranded DNA binding Source: UniProtKB
  3. endodeoxyribonuclease activity Source: UniProtKB
  4. endonuclease activity Source: Reactome
  5. metal ion binding Source: UniProtKB-KW
  6. protein N-terminus binding Source: UniProtKB
  7. protein binding Source: UniProtKB
  8. protein homodimerization activity Source: UniProtKB
  9. single-stranded DNA binding Source: UniProtKB

GO - Biological processi

  1. DNA catabolic process, endonucleolytic Source: GOC
  2. DNA repair Source: Reactome
  3. UV protection Source: MGI
  4. negative regulation of apoptotic process Source: UniProtKB
  5. nucleotide-excision repair Source: Reactome
  6. nucleotide-excision repair, DNA damage removal Source: Reactome
  7. nucleotide-excision repair, DNA incision, 3'-to lesion Source: UniProtKB
  8. response to UV Source: UniProtKB
  9. response to UV-C Source: UniProtKB
  10. transcription-coupled nucleotide-excision repair Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

DNA-binding, Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_2222. Dual incision reaction in TC-NER.
REACT_257. Formation of incision complex in GG-NER.
REACT_311. Dual incision reaction in GG-NER.

Names & Taxonomyi

Protein namesi
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 namesi
Name:ERCC5
Synonyms:ERCM2, XPG, XPGC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:3437. ERCC5.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. intermediate filament cytoskeleton Source: HPA
  2. nucleoplasm Source: Reactome
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

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.5 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti72 – 721P → H in XP-G; combined with features of Cockayne syndrome. 1 Publication
VAR_015280
Natural varianti792 – 7921A → V in XP-G; mild form. 2 Publications
VAR_007733
Natural varianti858 – 8581L → P in XP-G; reduced stability and greatly impaired endonuclease activity. 1 Publication
VAR_017097
Natural varianti874 – 8741A → T in XP-G; mild form; residual activity. 1 Publication
Corresponds to variant rs28929496 [ dbSNP | Ensembl ].
VAR_017096

Keywords - Diseasei

Cockayne syndrome, Deafness, Disease mutation, Dwarfism, Xeroderma pigmentosum

Organism-specific databases

MIMi278780. phenotype.
Orphaneti1466. COFS syndrome.
276267. Xeroderma pigmentosum complementation group G.
PharmGKBiPA27851.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11861186DNA repair protein complementing XP-G cells
PRO_0000154031Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81N6-acetyllysine1 Publication
Modified residuei384 – 3841Phosphoserine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP28715.
PaxDbiP28715.
PRIDEiP28715.

PTM databases

PhosphoSiteiP28715.

Expressioni

Gene expression databases

ArrayExpressiP28715.
BgeeiP28715.
CleanExiHS_ERCC5.
GenevestigatoriP28715.

Organism-specific databases

HPAiHPA045845.
HPA050374.

Interactioni

Subunit structurei

Interacts with PCNA.1 Publication

Protein-protein interaction databases

BioGridi108385. 14 interactions.
DIPiDIP-750N.
IntActiP28715. 3 interactions.
MINTiMINT-192239.
STRINGi9606.ENSP00000347978.

Structurei

3D structure databases

ProteinModelPortaliP28715.
SMRiP28715. Positions 2-95, 711-977.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 9595N-domain
Add
BLAST
Regioni753 – 881129I-domain
Add
BLAST
Regioni981 – 100929Interaction with PCNA
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1057 – 107317Nuclear localization signal Reviewed prediction
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0258.
HOVERGENiHBG051501.
InParanoidiP28715.
KOiK10846.
OMAiHDTKVKR.
OrthoDBiEOG72ZCD4.
PhylomeDBiP28715.
TreeFamiTF101235.

Family and domain databases

Gene3Di3.40.50.1010. 2 hits.
InterProiIPR020045. 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]
PfamiPF00867. XPG_I. 1 hit.
PF00752. XPG_N. 1 hit.
[Graphical view]
PRINTSiPR00066. XRODRMPGMNTG.
SMARTiSM00279. HhH2. 1 hit.
SM00484. XPGI. 1 hit.
SM00485. XPGN. 1 hit.
[Graphical view]
SUPFAMiSSF47807. SSF47807. 2 hits.
SSF88723. SSF88723. 2 hits.
TIGRFAMsiTIGR00600. rad2. 1 hit.
PROSITEiPS00841. XPG_1. 1 hit.
PS00842. XPG_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P28715-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MGVQGLWKLL ECSGRQVSPE ALEGKILAVD ISIWLNQALK GVRDRHGNSI     50
ENPHLLTLFH RLCKLLFFRI RPIFVFDGDA PLLKKQTLVK RRQRKDLASS 100
DSRKTTEKLL KTFLKRQAIK TAFRSKRDEA LPSLTQVRRE NDLYVLPPLQ 150
EEEKHSSEEE DEKEWQERMN QKQALQEEFF HNPQAIDIES EDFSSLPPEV 200
KHEILTDMKE FTKRRRTLFE AMPEESDDFS QYQLKGLLKK NYLNQHIEHV 250
QKEMNQQHSG HIRRQYEDEG GFLKEVESRR VVSEDTSHYI LIKGIQAKTV 300
AEVDSESLPS SSKMHGMSFD VKSSPCEKLK TEKEPDATPP SPRTLLAMQA 350
ALLGSSSEEE LESENRRQAR GRNAPAAVDE GSISPRTLSA IKRALDDDED 400
VKVCAGDDVQ TGGPGAEEMR INSSTENSDE GLKVRDGKGI PFTATLASSS 450
VNSAEEHVAS TNEGREPTDS VPKEQMSLVH VGTEAFPISD ESMIKDRKDR 500
LPLESAVVRH SDAPGLPNGR ELTPASPTCT NSVSKNETHA EVLEQQNELC 550
PYESKFDSSL LSSDDETKCK PNSASEVIGP VSLQETSSIV SVPSEAVDNV 600
ENVVSFNAKE HENFLETIQE QQTTESAGQD LISIPKAVEP MEIDSEESES 650
DGSFIEVQSV ISDEELQAEF PETSKPPSEQ GEEELVGTRE GEAPAESESL 700
LRDNSERDDV DGEPQEAEKD AEDSLHEWQD INLEELETLE SNLLAQQNSL 750
KAQKQQQERI AATVTGQMFL ESQELLRLFG IPYIQAPMEA EAQCAILDLT 800
DQTSGTITDD SDIWLFGARH VYRNFFNKNK FVEYYQYVDF HNQLGLDRNK 850
LINLAYLLGS DYTEGIPTVG CVTAMEILNE FPGHGLEPLL KFSEWWHEAQ 900
KNPKIRPNPH DTKVKKKLRT LQLTPGFPNP AVAEAYLKPV VDDSKGSFLW 950
GKPDLDKIRE FCQRYFGWNR TKTDESLFPV LKQLDAQQTQ LRIDSFFRLA 1000
QQEKEDAKRI KSQRLNRAVT CMLRKEKEAA ASEIEAVSVA MEKEFELLDK 1050
AKGKTQKRGI TNTLEESSSL KRKRLSDSKG KNTCGGFLGE TCLSESSDGS 1100
SSEDAESSSL MNVQRRTAAK EPKTSASDSQ NSVKEAPVKN GGATTSSSSD 1150
SDDDGGKEKM VLVTARSVFG KKRRKLRRAR GRKRKT 1186
Length:1,186
Mass (Da):133,108
Last modified:September 2, 2008 - v3
Checksum:iB0A844D617C53F2E
GO
Isoform 2 (identifier: P28715-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:419
Mass (Da):47,319
Checksum:iA26C01C3C1DFAC28
GO
Isoform 3 (identifier: P28715-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:232
Mass (Da):27,259
Checksum:iE2808BE7528D94F1
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti72 – 721P → H in XP-G; combined with features of Cockayne syndrome. 1 Publication
VAR_015280
Natural varianti145 – 1451V → I.
Corresponds to variant rs4987063 [ dbSNP | Ensembl ].
VAR_020431
Natural varianti181 – 1811H → R.1 Publication
Corresponds to variant rs4150295 [ dbSNP | Ensembl ].
VAR_023120
Natural varianti254 – 2541M → V.4 Publications
Corresponds to variant rs1047769 [ dbSNP | Ensembl ].
VAR_007732
Natural varianti256 – 2561Q → R.1 Publication
Corresponds to variant rs4150313 [ dbSNP | Ensembl ].
VAR_020432
Natural varianti311 – 3111S → C.1 Publication
Corresponds to variant rs2307491 [ dbSNP | Ensembl ].
VAR_014829
Natural varianti399 – 3991E → K.1 Publication
Corresponds to variant rs4150315 [ dbSNP | Ensembl ].
VAR_023121
Natural varianti529 – 5291C → S.1 Publication
Corresponds to variant rs2227869 [ dbSNP | Ensembl ].
VAR_020433
Natural varianti590 – 5901V → I.1 Publication
Corresponds to variant rs4150318 [ dbSNP | Ensembl ].
VAR_023122
Natural varianti597 – 5971V → L.1 Publication
Corresponds to variant rs4150319 [ dbSNP | Ensembl ].
VAR_023123
Natural varianti670 – 6701F → L.
Corresponds to variant rs1803542 [ dbSNP | Ensembl ].
VAR_046373
Natural varianti680 – 6801Q → R.
Corresponds to variant rs4987168 [ dbSNP | Ensembl ].
VAR_020434
Natural varianti792 – 7921A → V in XP-G; mild form. 2 Publications
VAR_007733
Natural varianti858 – 8581L → P in XP-G; reduced stability and greatly impaired endonuclease activity. 1 Publication
VAR_017097
Natural varianti874 – 8741A → T in XP-G; mild form; residual activity. 1 Publication
Corresponds to variant rs28929496 [ dbSNP | Ensembl ].
VAR_017096
Natural varianti879 – 8791N → S.1 Publication
Corresponds to variant rs4150342 [ dbSNP | Ensembl ].
VAR_020435
Natural varianti1009 – 10091R → H.1 Publication
Corresponds to variant rs4150387 [ dbSNP | Ensembl ].
VAR_023124
Natural varianti1053 – 10531G → R.6 Publications
Corresponds to variant rs9514066 [ dbSNP | Ensembl ].
VAR_046374
Natural varianti1080 – 10801G → Q Requires 2 nucleotide substitutions. 1 Publication
VAR_023125
Natural varianti1080 – 10801G → R.6 Publications
Corresponds to variant rs9514067 [ dbSNP | Ensembl ].
VAR_046375
Natural varianti1104 – 11041D → H.1 Publication
Corresponds to variant rs17655 [ dbSNP | Ensembl ].
VAR_007734
Natural varianti1119 – 11191A → V.
Corresponds to variant rs2227871 [ dbSNP | Ensembl ].
VAR_020436

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 767767Missing in isoform 2.
VSP_035380Add
BLAST
Alternative sequencei225 – 2328ESDDFSQY → VYLPLLQP in isoform 3.
VSP_053828
Alternative sequencei233 – 1186954Missing in isoform 3.
VSP_053829Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551L → P in BAA03812. 1 Publication
Sequence conflicti120 – 1223KTA → QTS in BAA03812. 1 Publication
Sequence conflicti126 – 1261K → Q in BAA03812. 1 Publication
Sequence conflicti264 – 2663RQY → SSH in BAA03812. 1 Publication
Sequence conflicti760 – 7601I → F in BAA03812. 1 Publication
Sequence conflicti796 – 7961I → V in BAA03812. 1 Publication
Sequence conflicti864 – 8729EGIPTVGCV → GNTNCGLC in BAA03812. 1 Publication
Sequence conflicti959 – 9591R → S in BAA03812. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X69978 mRNA. Translation: CAA49598.1.
D16305 mRNA. Translation: BAA03812.1.
L20046 mRNA. Translation: AAC37533.1.
AF255436
, AF255431, AF255433, AF255434, AF255435 Genomic DNA. Translation: AAF89178.1.
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.
CCDSiCCDS32004.1. [P28715-1]
PIRiI58009.
S35993.
RefSeqiNP_000114.2. NM_000123.3.
UniGeneiHs.258429.

Genome annotation databases

EnsembliENST00000355739; ENSP00000347978; ENSG00000134899. [P28715-1]
ENST00000375954; ENSP00000365121; ENSG00000134899. [P28715-2]
ENST00000535557; ENSP00000442117; ENSG00000134899.
GeneIDi2073.
KEGGihsa:2073.
UCSCiuc001vpw.3. human. [P28715-1]

Polymorphism databases

DMDMi205371791.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Allelic variations of the XP genes
Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X69978 mRNA. Translation: CAA49598.1 .
D16305 mRNA. Translation: BAA03812.1 .
L20046 mRNA. Translation: AAC37533.1 .
AF255436
, AF255431 , AF255433 , AF255434 , AF255435 Genomic DNA. Translation: AAF89178.1 .
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 .
CCDSi CCDS32004.1. [P28715-1 ]
PIRi I58009.
S35993.
RefSeqi NP_000114.2. NM_000123.3.
UniGenei Hs.258429.

3D structure databases

ProteinModelPortali P28715.
SMRi P28715. Positions 2-95, 711-977.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108385. 14 interactions.
DIPi DIP-750N.
IntActi P28715. 3 interactions.
MINTi MINT-192239.
STRINGi 9606.ENSP00000347978.

Chemistry

BindingDBi P28715.
ChEMBLi CHEMBL4736.

PTM databases

PhosphoSitei P28715.

Polymorphism databases

DMDMi 205371791.

Proteomic databases

MaxQBi P28715.
PaxDbi P28715.
PRIDEi P28715.

Protocols and materials databases

DNASUi 2073.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000355739 ; ENSP00000347978 ; ENSG00000134899 . [P28715-1 ]
ENST00000375954 ; ENSP00000365121 ; ENSG00000134899 . [P28715-2 ]
ENST00000535557 ; ENSP00000442117 ; ENSG00000134899 .
GeneIDi 2073.
KEGGi hsa:2073.
UCSCi uc001vpw.3. human. [P28715-1 ]

Organism-specific databases

CTDi 2073.
GeneCardsi GC13P103497.
GeneReviewsi ERCC5.
HGNCi HGNC:3437. ERCC5.
HPAi HPA045845.
HPA050374.
MIMi 133530. gene.
278780. phenotype.
neXtProti NX_P28715.
Orphaneti 1466. COFS syndrome.
276267. Xeroderma pigmentosum complementation group G.
PharmGKBi PA27851.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0258.
HOVERGENi HBG051501.
InParanoidi P28715.
KOi K10846.
OMAi HDTKVKR.
OrthoDBi EOG72ZCD4.
PhylomeDBi P28715.
TreeFami TF101235.

Enzyme and pathway databases

Reactomei REACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_2222. Dual incision reaction in TC-NER.
REACT_257. Formation of incision complex in GG-NER.
REACT_311. Dual incision reaction in GG-NER.

Miscellaneous databases

GeneWikii ERCC5.
GenomeRNAii 2073.
NextBioi 8433.
PROi P28715.
SOURCEi Search...

Gene expression databases

ArrayExpressi P28715.
Bgeei P28715.
CleanExi HS_ERCC5.
Genevestigatori P28715.

Family and domain databases

Gene3Di 3.40.50.1010. 2 hits.
InterProi IPR020045. 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 ]
Pfami PF00867. XPG_I. 1 hit.
PF00752. XPG_N. 1 hit.
[Graphical view ]
PRINTSi PR00066. XRODRMPGMNTG.
SMARTi SM00279. HhH2. 1 hit.
SM00484. XPGI. 1 hit.
SM00485. XPGN. 1 hit.
[Graphical view ]
SUPFAMi SSF47807. SSF47807. 2 hits.
SSF88723. SSF88723. 2 hits.
TIGRFAMsi TIGR00600. rad2. 1 hit.
PROSITEi PS00841. XPG_1. 1 hit.
PS00842. XPG_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. Cited for: VARIANT XP-G THR-874.

Entry informationi

Entry nameiERCC5_HUMAN
AccessioniPrimary (citable) accession number: P28715
Secondary accession number(s): A6NGT4
, Q5JUS4, Q5JUS5, Q7Z2V3, Q8IZL6, Q8N1B7, Q9HD59, Q9HD60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: September 2, 2008
Last modified: September 3, 2014
This is version 173 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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