20250201201808032018032820250201IID00846General transcription factor IIH subunit 5General transcription factor IIH polypeptide 5TFB5 orthologTFIIH basal transcription factor complex TTD-A subunitTFIIH subunit p8Homo sapiens71Q6ZYL4Q0P5V8Component 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. 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. Necessary for the stability of the TFIIH complex and for the presence of normal levels of TFIIH in the cell.Cytoplasm, Perinuclear region.SL-0198unkownNucleus.SL-0191unkown00Phosphothreonine6969GTF2H5General transcription factor IIHMVNVLKGVLIECDPAMKQFLLYLDESNALGKKFIIQDIDDTHVFVIAELVNVLQERVGELMDQNAFSLTQK12jnjA171order122jnjB171order141ydlA371order252jnjB6571high_rmsd162jnjA6571high_rmsd112jnjNMR17350038M.VITORINO,F.COIN,O.ZLOBINSKAYA,R.A.ATKINSON,D.MORAS,J.M.EGLY,A.POTERSZMAN,B.KIEFFERSOLUTION STRUCTURE AND SELF-ASSOCIATION PROPERTIES OF THE P8 TFIIH SUBUNIT RESPONSIBLE FOR TRICHOTHIODYSTROPHY2007J.MOL.BIOL.368473nmr2jnjA1711000nmr2jnjB171100012jnj5386Homo dimer2jnjBQ6ZYL4IID008462jnjAQ6ZYL4IID008462jnjB-2jnjA21ydlX-RAY293K7.5F.FOROUHAR,W.EDSTROM,R.XIAO,T.B.ACTON,G.T.MONTELIONE,L.TONG,J.F.HUNTCRYSTAL STRUCTURE OF THE HUMAN TFIIH, NORTHEAST STRUCTURAL GENOMICS TARGET HR2045.TO BE PUBLISHEDx-ray1ydlA37194011ydl_14259Monomer monomer1ydlAQ6ZYL4IID00846P23025-1XPA/ERCC1Solution structure of a ERCC1-XPA heterodimerQ01831-2XPC/GTF2H1Solution structure of the complex between XPC acidic domain and TFIIH p62 PH domain6-25,32-56,59-59,62-621-5,26-31,57-58,60-61,63-711-6768-7168-71