ERCC2
entrez
2068
canonical
uniprot
P18074
canonical
ensembl
ENSG00000104884
resolver
ensp
ENSP00000375805
resolver
ensp
ENSP00000375809
resolver
ensp
ENSP00000431229
resolver
ensp
ENSP00000507775
resolver
ensp
ENSP00000561983
resolver
enst
ENST00000684407
resolver
genesymbol
ERCC2
resolver
genesymbol_syn
XPD
resolver
genesymbol_syn
XPDC
resolver
hgnc
HGNC:3434
resolver
uniprot
A0A804HK53
resolver
uniprot
Q2TB78
resolver
uniprot
Q2YDY2
resolver
uniprot
Q7KZU6
resolver
uniprot
Q8N721
resolver
uniprot_entry
A0A804HK53_HUMAN
resolver
uniprot_entry
ERCC2_HUMAN
resolver
uniprot_sec
Q2TB78
resolver
uniprot_sec
Q2YDY2
resolver
uniprot_sec
Q7KZU6
resolver
uniprot_sec
Q8N721
resolver
activity_regulation
ACTIVITY REGULATION: Interaction with GTF2H2 (p44) results in stimulation of the 5'-3' helicase activity of this subunit (PubMed:9771713). DNA unwinding by this subunit in TFIIH is stimulated 4-fold by XPA and 20-fold by ERCC5/XPG (PubMed:31253769). {ECO:0000269|PubMed:31253769, ECO:0000269|PubMed:9771713}.
uniprot
proteins
amino_acid_sequence
MKLNVDGLLVYFPYDYIYPEQFSYMRELKRTLDAKGHGVLEMPSGTGKTVSLLALIMAYQRAYPLEVTKLIYCSRTVPEIEKVIEELRKLLNFYEKQEGEKLPFLGLALSSRKNLCIHPEVTPLRFGKDVDGKCHSLTASYVRAQYQHDTSLPHCRFYEEFDAHGREVPLPAGIYNLDDLKALGRRQGWCPYFLARYSILHANVVVYSYHYLLDPKIADLVSKELARKAVVVFDEAHNIDNVCIDSMSVNLTRRTLDRCQGNLETLQKTVLRIKETDEQRLRDEYRRLVEGLREASAARETDAHLANPVLPDEVLQEAVPGSIRTAEHFLGFLRRLLEYVKWRLRVQHVVQESPPAFLSGLAQRVCIQRKPLRFCAERLRSLLHTLEITDLADFSPLTLLANFATLVSTYAKGFTIIIEPFDDRTPTIANPILHFSCMDASLAIKPVFERFQSVIITSGTLSPLDIYPKILDFHPVTMATFTMTLARVCLCPMIIGRGNDQVAISSKFETREDIAVIRNYGNLLLEMSAVVPDGIVAFFTSYQYMESTVASWYEQGILENIQRNKLLFIETQDGAETSVALEKYQEACENGRGAILLSVARGKVSEGIDFVHHYGRAVIMFGVPYVYTQSRILKARLEYLRDQFQIRENDFLTFDAMRHAAQCVGRAIRGKTDYGLMVFADKRFARGDKRGKLPRWIQEHLTDANLNLTVDEGVQVAKYFLRQMAQPFHREDQLGLSLLSLEQLESEETLKRIEQIAQQL
uniprot
proteins
disease_involvement
DISEASE: Xeroderma pigmentosum complementation group D (XP-D) [MIM:278730]: 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-D patients present features of Cockayne syndrome, including 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:11156600, ECO:0000269|PubMed:11709541, ECO:0000269|PubMed:15494306, ECO:0000269|PubMed:17466626, ECO:0000269|PubMed:7585650, ECO:0000269|PubMed:7825573, ECO:0000269|PubMed:7849702, ECO:0000269|PubMed:9101292, ECO:0000269|PubMed:9238033}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Trichothiodystrophy 1, photosensitive (TTD1) [MIM:601675]: A form of trichothiodystrophy, an autosomal recessive disease characterized by sulfur-deficient brittle hair and multisystem variable abnormalities. The spectrum of clinical features varies from mild disease with only hair involvement to severe disease with cutaneous, neurologic and profound developmental defects. Ichthyosis, intellectual and developmental disabilities, decreased fertility, abnormal characteristics at birth, ocular abnormalities, short stature, and infections are common manifestations. There are both photosensitive and non-photosensitive forms of the disorder. TTD1 patients manifest cutaneous photosensitivity. {ECO:0000269|PubMed:11156600, ECO:0000269|PubMed:11242112, ECO:0000269|PubMed:17466626, ECO:0000269|PubMed:7920640, ECO:0000269|PubMed:8571952, ECO:0000269|PubMed:9195225, ECO:0000269|PubMed:9238033, ECO:0000269|PubMed:9758621, ECO:0000269|PubMed:9771713}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Cerebro-oculo-facio-skeletal syndrome 2 (COFS2) [MIM:610756]: 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:11443545}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
5.6.2.3
uniprot
proteins
function
FUNCTION: ATP-dependent 5'-3' DNA helicase (PubMed:31253769, PubMed:8413672, PubMed:9771713). Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, not absolutely essential for minimal transcription in vitro (PubMed:10024882, PubMed:17466626, PubMed:9771713). Required for transcription-coupled nucleotide excision repair (NER) of damaged DNA; recognizes damaged bases (PubMed:17466626, PubMed:23352696, PubMed:9771713). Sequestered in chromatin on UV-damaged DNA (PubMed:23352696). When complexed to CDK-activating kinase (CAK), involved in transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATP-dependent helicase activity of XPD/ERCC2 is required for DNA opening. Involved in DNA lesion verification (PubMed:31253769). In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription. XPD/ERCC2 acts by forming a bridge between CAK and the core-TFIIH complex. The structure of the TFIIH transcription complex differs from the NER-TFIIH complex; large movements by XPD/ERCC2 and XPB/ERCC3 are stabilized by XPA which allow this subunit to contact ssDNA (PubMed:31253769, PubMed:33902107). Involved in the regulation of vitamin-D receptor activity. As part of the mitotic spindle-associated MMXD complex it plays a role in chromosome segregation. Might have a role in aging process and could play a causative role in the generation of skin cancers. {ECO:0000269|PubMed:10024882, ECO:0000269|PubMed:15494306, ECO:0000269|PubMed:17466626, ECO:0000269|PubMed:20797633, ECO:0000269|PubMed:23352696, ECO:0000269|PubMed:31253769, ECO:0000269|PubMed:33902107, ECO:0000269|PubMed:8413672, ECO:0000269|PubMed:9771713}.
uniprot
proteins
mass_dalton
86909
uniprot
proteins
mutagenesis
MUTAGEN 48; /note="K->R: Decreased transcriptional activity of the reconstituted TFIIH complex. Damaged DNA opening by TFIIH is impeded. Loss of TFIIH 5'-3' helicase activity, still binds GTF2H2. Does not restore nucleotide excision repair (NER) in deficient cells, does not bind UV damaged DNA."; /evidence="ECO:0000269|PubMed:10024882, ECO:0000269|PubMed:17466626, ECO:0000269|PubMed:23352696, ECO:0000269|PubMed:31253769, ECO:0000269|PubMed:9771713"; MUTAGEN 190; /note="C->S: Reduced iron-sulfur-binding. Iron-sulfur-binding is further decreased in absence of MMS19."; /evidence="ECO:0000269|PubMed:22678361"; MUTAGEN 192; /note="Y->A: Does not restore nucleotide excision repair (NER) in deficient cells, does not bind UV damaged DNA, TFIIH is able to transcribe."; /evidence="ECO:0000269|PubMed:23352696"; MUTAGEN 196; /note="R->E: Restores <5% nucleotide excision repair (NER) in deficient cells, does not bind UV damaged DNA, TFIIH is able to transcribe."; /evidence="ECO:0000269|PubMed:23352696"; MUTAGEN 675; /note="G->W: No longer interacts with GTF2H2/p44, has 5'-3' helicase activity."; /evidence="ECO:0000269|PubMed:9771713
uniprot
proteins
post_translational_modification
PTM: ISGylated. {ECO:0000305|PubMed:16884686}.
uniprot
proteins
protein_family
Helicase family
uniprot
proteins
protein_family
RAD3/XPD subfamily
uniprot
proteins
pubmed
10024882
uniprot
proteins
pubmed
10447254
uniprot
proteins
pubmed
11156600
uniprot
proteins
pubmed
11242112
uniprot
proteins
pubmed
11245433
uniprot
proteins
pubmed
11319176
uniprot
proteins
pubmed
11443545
uniprot
proteins
pubmed
11470747
uniprot
proteins
pubmed
11709541
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15494306
uniprot
proteins
pubmed
16884686
uniprot
proteins
pubmed
1729695
uniprot
proteins
pubmed
17466626
uniprot
proteins
pubmed
19106100
uniprot
proteins
pubmed
20797633
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
2184031
uniprot
proteins
pubmed
22678361
uniprot
proteins
pubmed
23352696
uniprot
proteins
pubmed
23585563
uniprot
proteins
pubmed
23891004
uniprot
proteins
pubmed
27193682
uniprot
proteins
pubmed
29320706
uniprot
proteins
pubmed
31253769
uniprot
proteins
pubmed
33902107
uniprot
proteins
pubmed
7585650
uniprot
proteins
pubmed
7724549
uniprot
proteins
pubmed
7825573
uniprot
proteins
pubmed
7849702
uniprot
proteins
pubmed
7920640
uniprot
proteins
pubmed
8413672
uniprot
proteins
pubmed
8571952
uniprot
proteins
pubmed
8786141
uniprot
proteins
pubmed
9101292
uniprot
proteins
pubmed
9195225
uniprot
proteins
pubmed
9238033
uniprot
proteins
pubmed
9758621
uniprot
proteins
pubmed
9771713
uniprot
proteins
pubmed
9852112
uniprot
proteins
sequence_length
760
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20797633, ECO:0000269|PubMed:23352696, ECO:0000269|PubMed:23585563}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:20797633}.
uniprot
proteins