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IID00784
UniprotP18074
ProteinGeneral transcription and DNA repair factor IIH helicase subunit XPD
GeneERCC2
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
760
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 245-439 Hetero tetramer : P51948
 Evidence X-RAY 6tun B Reference
       Region 6tun B 245-245 disorder
       Region 6tun B 246-291 order
       Region 6tun B 292-315 disorder
       Region 6tun B 316-439 order
 Evidence X-RAY 6tun A Reference
       Region 6tun A 245-245 disorder
       Region 6tun A 246-294 order
       Region 6tun A 295-315 disorder
       Region 6tun A 316-439 order
 
Prediction
NeProc
Disorder 748-760
Order 1-747
ProS 754-760
AlphaFold
Disorder 219-220,222-224,291-318,509-509,628-629
Order 1-218,221-221,225-290,319-508,510-627,630-760
Pfam Hmmer
PF06733 72-256 9.6e-73
PF06777 257-413 1.1e-112
SEG 734-750
Function
Function in SwissProt
ATP-dependent 5'-3' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA 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. 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. 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.
Biological Process
See also
Diagram with PDB data
XPA/ERCC1Solution structure of a ERCC1-XPA heterodimer
XPC/GTF2H1Solution structure of the complex between XPC acidic domain and TFIIH p62 PH domain