ERCC5
entrez
2073
canonical
uniprot
P28715
canonical
ensembl
ENSG00000134899
resolver
ensp
ENSP00000498881
resolver
genesymbol
ERCC5
resolver
genesymbol_syn
ERCM2
resolver
genesymbol_syn
XPG
resolver
genesymbol_syn
XPGC
resolver
hgnc
HGNC:3437
resolver
uniprot
A6NGT4
resolver
uniprot
Q5JUS4
resolver
uniprot
Q5JUS5
resolver
uniprot
Q7Z2V3
resolver
uniprot
Q8IZL6
resolver
uniprot
Q8N1B7
resolver
uniprot
Q9HD59
resolver
uniprot
Q9HD60
resolver
uniprot_entry
ERCC5_HUMAN
resolver
uniprot_sec
A6NGT4
resolver
uniprot_sec
Q5JUS4
resolver
uniprot_sec
Q5JUS5
resolver
uniprot_sec
Q7Z2V3
resolver
uniprot_sec
Q8IZL6
resolver
uniprot_sec
Q8N1B7
resolver
uniprot_sec
Q9HD59
resolver
uniprot_sec
Q9HD60
resolver
amino_acid_sequence
MGVQGLWKLLECSGRQVSPEALEGKILAVDISIWLNQALKGVRDRHGNSIENPHLLTLFHRLCKLLFFRIRPIFVFDGDAPLLKKQTLVKRRQRKDLASSDSRKTTEKLLKTFLKRQAIKTAFRSKRDEALPSLTQVRRENDLYVLPPLQEEEKHSSEEEDEKEWQERMNQKQALQEEFFHNPQAIDIESEDFSSLPPEVKHEILTDMKEFTKRRRTLFEAMPEESDDFSQYQLKGLLKKNYLNQHIEHVQKEMNQQHSGHIRRQYEDEGGFLKEVESRRVVSEDTSHYILIKGIQAKTVAEVDSESLPSSSKMHGMSFDVKSSPCEKLKTEKEPDATPPSPRTLLAMQAALLGSSSEEELESENRRQARGRNAPAAVDEGSISPRTLSAIKRALDDDEDVKVCAGDDVQTGGPGAEEMRINSSTENSDEGLKVRDGKGIPFTATLASSSVNSAEEHVASTNEGREPTDSVPKEQMSLVHVGTEAFPISDESMIKDRKDRLPLESAVVRHSDAPGLPNGRELTPASPTCTNSVSKNETHAEVLEQQNELCPYESKFDSSLLSSDDETKCKPNSASEVIGPVSLQETSSIVSVPSEAVDNVENVVSFNAKEHENFLETIQEQQTTESAGQDLISIPKAVEPMEIDSEESESDGSFIEVQSVISDEELQAEFPETSKPPSEQGEEELVGTREGEAPAESESLLRDNSERDDVDGEPQEAEKDAEDSLHEWQDINLEELETLESNLLAQQNSLKAQKQQQERIAATVTGQMFLESQELLRLFGIPYIQAPMEAEAQCAILDLTDQTSGTITDDSDIWLFGARHVYRNFFNKNKFVEYYQYVDFHNQLGLDRNKLINLAYLLGSDYTEGIPTVGCVTAMEILNEFPGHGLEPLLKFSEWWHEAQKNPKIRPNPHDTKVKKKLRTLQLTPGFPNPAVAEAYLKPVVDDSKGSFLWGKPDLDKIREFCQRYFGWNRTKTDESLFPVLKQLDAQQTQLRIDSFFRLAQQEKEDAKRIKSQRLNRAVTCMLRKEKEAAASEIEAVSVAMEKEFELLDKAKGKTQKRGITNTLEESSSLKRKRLSDSKGKNTCGGFLGETCLSESSDGSSSEDAESSSLMNVQRRTAAKEPKTSASDSQNSVKEAPVKNGGATTSSSSDSDDDGGKEKMVLVTARSVFGKKRRKLRRARGRKRKT
uniprot
proteins
disease_involvement
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. {ECO:0000269|PubMed:10447254, ECO:0000269|PubMed:11228268, ECO:0000269|PubMed:11841555, ECO:0000269|PubMed:12060391, ECO:0000269|PubMed:23255472, ECO:0000269|PubMed:7951246}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Cerebro-oculo-facio-skeletal syndrome 3 (COFS3) [MIM:616570]: A disorder of prenatal onset characterized by microcephaly, congenital cataracts, facial dysmorphism, neurogenic arthrogryposis, growth failure and severe psychomotor retardation. COFS is considered to be part of the nucleotide-excision repair disorders spectrum that include also xeroderma pigmentosum, trichothiodystrophy and Cockayne syndrome. {ECO:0000269|PubMed:24700531}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.1.-.-
uniprot
proteins
function
FUNCTION: Single-stranded structure-specific DNA endonuclease involved in DNA excision repair (PubMed:32522879, PubMed:32821917, PubMed:7651464, PubMed:8078765, PubMed:8090225, PubMed:8206890). Makes the 3'incision in DNA nucleotide excision repair (NER) (PubMed:32522879, PubMed:32821917, PubMed:8078765, PubMed:8090225). Binds and bends DNA repair bubble substrate and breaks base stacking at the single-strand/double-strand DNA junction of the DNA bubble (PubMed:32522879). Plays a role in base excision repair (BER) by promoting the binding of DNA glycosylase NTHL1 to its substrate and increasing NTHL1 catalytic activity that removes oxidized pyrimidines from DNA (PubMed:9927729). Involved in transcription-coupled nucleotide excision repair (TCR) which allows RNA polymerase II-blocking lesions to be rapidly removed from the transcribed strand of active genes (PubMed:16246722). Functions during the initial step of TCR in cooperation with ERCC6/CSB to recognized stalled RNA polymerase II (PubMed:16246722). Also, stimulates ERCC6/CSB binding to the DNA repair bubble and ERCC6/CSB ATPase activity (PubMed:16246722). Required for DNA replication fork maintenance and preservation of genomic stability (PubMed:26833090, PubMed:32522879). Involved in homologous recombination repair (HRR) induced by DNA replication stress by recruiting RAD51, BRCA2, and PALB2 to the damaged DNA site (PubMed:26833090). In TFIIH stimulates the 5'-3' helicase activity of XPD/ERCC2 and the DNA translocase activity of XPB/ERCC3 (PubMed:31253769). During HRR, binds to the replication fork with high specificity and stabilizes it (PubMed:32522879). Also, acts upstream of HRR, to promote the release of BRCA1 from DNA (PubMed:26833090). {ECO:0000269|PubMed:16246722, ECO:0000269|PubMed:26833090, ECO:0000269|PubMed:31253769, ECO:0000269|PubMed:32522879, ECO:0000269|PubMed:32821917, ECO:0000269|PubMed:7651464, ECO:0000269|PubMed:8078765, ECO:0000269|PubMed:8090225, ECO:0000269|PubMed:8206890, ECO:0000269|PubMed:9927729}.
uniprot
proteins
mass_dalton
133108
uniprot
proteins
mutagenesis
MUTAGEN 67..68; /note="FF->AA: Slight reduction in endonuclease activity. Increased affinity for bubble DNA."; /evidence="ECO:0000269|PubMed:32522879"; MUTAGEN 955..956; /note="LD->AA: Reduced protein stability, two-fold decrease in 15-nt bubble DNA incision activity and smaller decrease in YDNA incision activity; when associated with A-978 and A-981."; /evidence="ECO:0000269|PubMed:32522879"; MUTAGEN 978; /note="F->A: Reduced protein stability, two-fold decrease in 15-nt bubble DNA incision activity and smaller decrease in YDNA incision activity; when associated with 955-A-A-956 and A-981."; /evidence="ECO:0000269|PubMed:32522879"; MUTAGEN 981; /note="L->A: Reduced protein stability, two-fold decrease in 15-nt bubble DNA incision activity and smaller decrease in YDNA incision activity; when associated with 955-A-A-956 and A-978."; /evidence="ECO:0000269|PubMed:32522879
uniprot
proteins
protein_family
XPG subfamily
uniprot
proteins
protein_family
XPG/RAD2 endonuclease family
uniprot
proteins
pubmed
10447254
uniprot
proteins
pubmed
11228268
uniprot
proteins
pubmed
11266544
uniprot
proteins
pubmed
11841555
uniprot
proteins
pubmed
12060391
uniprot
proteins
pubmed
14726017
uniprot
proteins
pubmed
15057823
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16246722
uniprot
proteins
pubmed
17179216
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23255472
uniprot
proteins
pubmed
24700531
uniprot
proteins
pubmed
26812207
uniprot
proteins
pubmed
26833090
uniprot
proteins
pubmed
30533531
uniprot
proteins
pubmed
31253769
uniprot
proteins
pubmed
32522879
uniprot
proteins
pubmed
32821917
uniprot
proteins
pubmed
7510366
uniprot
proteins
pubmed
7651464
uniprot
proteins
pubmed
7951246
uniprot
proteins
pubmed
8078765
uniprot
proteins
pubmed
8088806
uniprot
proteins
pubmed
8090225
uniprot
proteins
pubmed
8206890
uniprot
proteins
pubmed
8413238
uniprot
proteins
pubmed
8483504
uniprot
proteins
pubmed
9096355
uniprot
proteins
pubmed
9305916
uniprot
proteins
pubmed
9927729
uniprot
proteins
sequence_length
1186
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16246722, ECO:0000269|PubMed:26833090, ECO:0000269|PubMed:7651464}. Chromosome {ECO:0000269|PubMed:26833090}. Note=Colocalizes with RAD51 to nuclear foci in S phase (PubMed:26833090). Localizes to DNA double-strand breaks (DSB) during replication stress (PubMed:26833090). Colocalizes with BRCA2 to nuclear foci following DNA replication stress (PubMed:26833090). {ECO:0000269|PubMed:26833090}.
uniprot
proteins