ID Q53HW5_HUMAN Unreviewed; 782 AA. AC Q53HW5; DT 24-MAY-2005, integrated into UniProtKB/TrEMBL. DT 24-MAY-2005, sequence version 1. DT 27-NOV-2024, entry version 99. DE RecName: Full=General transcription and DNA repair factor IIH helicase/translocase subunit XPB {ECO:0000256|ARBA:ARBA00044799}; DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808}; DE AltName: Full=DNA 3'-5' helicase/translocase XPB {ECO:0000256|ARBA:ARBA00044810}; DE AltName: Full=DNA excision repair protein ERCC-3 {ECO:0000256|ARBA:ARBA00032205}; DE Flags: Fragment; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAD96185.1}; RN [1] {ECO:0000313|EMBL:BAD96185.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Adipose tissue {ECO:0000313|EMBL:BAD96185.1}; RX PubMed=8125298; DOI=10.1016/0378-1119(94)90802-8; RA Maruyama K., Sugano S.; RT "Oligo-capping: a simple method to replace the cap structure of eukaryotic RT mRNAs with oligoribonucleotides."; RL Gene 138:171-174(1994). RN [2] {ECO:0000313|EMBL:BAD96185.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Adipose tissue {ECO:0000313|EMBL:BAD96185.1}; RX PubMed=9373149; DOI=10.1016/S0378-1119(97)00411-3; RA Suzuki Y., Yoshitomo K., Maruyama K., Suyama A., Sugano S.; RT "Construction and characterization of a full length-enriched and a 5'-end- RT enriched cDNA library."; RL Gene 200:149-156(1997). RN [3] {ECO:0000313|EMBL:BAD96185.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Adipose tissue {ECO:0000313|EMBL:BAD96185.1}; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4; CC Evidence={ECO:0000256|ARBA:ARBA00034618}; CC -!- CATALYTIC ACTIVITY: CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by CC translocating in the 3'-5' direction.; EC=5.6.2.4; CC Evidence={ECO:0000256|ARBA:ARBA00034617}; CC -!- SUBUNIT: Component of the 7-subunit TFIIH core complex composed of CC XPB/ERCC3, XPD/ERCC2, GTF2H1, GTF2H2, GTF2H3, GTF2H4 and GTF2H5, which CC is active in NER. The core complex associates with the 3-subunit CDK- CC activating kinase (CAK) module composed of CCNH/cyclin H, CDK7 and CC MNAT1 to form the 10-subunit holoenzyme (holo-TFIIH) active in CC transcription. Interacts with PUF60. Interacts with ATF7IP. Interacts CC with KAT2A; leading to KAT2A recruitment to promoters and acetylation CC of histones. Part of TBP-based Pol II pre-initiation complex (PIC), in CC which Pol II core assembles with general transcription factors and CC other specific initiation factors including GTF2E1, GTF2E2, GTF2F1, CC GTF2F2, TCEA1, ERCC2, ERCC3, GTF2H2, GTF2H3, GTF2H4, GTF2H5, GTF2A1, CC GTF2A2, GTF2B and TBP; this large multi-subunit PIC complex mediates CC DNA unwinding and targets Pol II core to the transcription start site CC where the first phosphodiester bond forms. CC {ECO:0000256|ARBA:ARBA00046596}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}. CC -!- SIMILARITY: Belongs to the helicase family. RAD25/XPB subfamily. CC {ECO:0000256|ARBA:ARBA00006637}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK222465; BAD96185.1; -; mRNA. DR AlphaFoldDB; Q53HW5; -. DR PeptideAtlas; Q53HW5; -. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro. DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IEA:InterPro. DR CDD; cd18029; DEXHc_XPB; 1. DR CDD; cd18789; SF2_C_XPB; 1. DR FunFam; 3.40.50.300:FF:000077; Probable DNA repair helicase RAD25; 1. DR FunFam; 3.40.50.300:FF:000117; Putative DNA repair helicase rad25; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR InterPro; IPR050615; ATP-dep_DNA_Helicase. DR InterPro; IPR032438; ERCC3_RAD25_C. DR InterPro; IPR006935; Helicase/UvrB_N. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C-like. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001161; XPB/Ssl2. DR InterPro; IPR032830; XPB/Ssl2_N. DR NCBIfam; TIGR00603; rad25; 1. DR PANTHER; PTHR11274:SF0; GENERAL TRANSCRIPTION AND DNA REPAIR FACTOR IIH HELICASE SUBUNIT XPB; 1. DR PANTHER; PTHR11274; RAD25/XP-B DNA REPAIR HELICASE; 1. DR Pfam; PF16203; ERCC3_RAD25_C; 1. DR Pfam; PF13625; Helicase_C_3; 1. DR Pfam; PF04851; ResIII; 1. DR PRINTS; PR00851; XRODRMPGMNTB. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW DNA damage {ECO:0000256|ARBA:ARBA00022763}; KW DNA repair {ECO:0000256|ARBA:ARBA00023204}; KW Helicase {ECO:0000256|ARBA:ARBA00022806}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022806}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242}. FT DOMAIN 327..488 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 542..702 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" FT REGION 1..51 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 220..241 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..22 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 220..239 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:BAD96185.1" SQ SEQUENCE 782 AA; 89149 MW; 8789BBFD5E1F4B6E CRC64; MGKRDRADRD KKKSRKRHYE DEEDDEEDAP GNDPQEAVPS AAGKQVDESG TKVDEYGAKD YRLQMPLKDD HTSRPLWVAP DGHIFLEAFS PVYKYAQDFL VAIAEPVCRP THVHEYKLTA YSLYAAVSVG LQTSDITEYL RKLSKTGVPD GIMQFIKLCT VSYGKVKLVL KHNRYFVESC HPDVIQHLLQ DPVIRECRLR NSEGEATELI TETFTSKSAI PKTAESSGGP STSRVTDPQG KSDIPMDLFD FYEQMDKDEE EEEETQTVSF EVKQEMIEEL QKRCIHLEYP LLAEYDFRND SVNPDINIDL KPTAVLRPYQ EKSLRKMFGN GRARSGVIVL PCGAGKSLVG VTAACTVRKR CLVLGNSAVS VEQWKAQFKM WSTIDDSQIC RFTSDAKDKP IGCSVAISTY SMLGHTTKRS WEAERVMEWL KTQVWGLMIL DEVHTIPAKM FRRVLTIVQA HCKLGLTATL VREDDKIVDL NFLIGPKLYE ANWMELQNNG YIAKVQCAEV WCPMSPEFYR EYVAIKTKKR ILLYTMNPNK FRACQFLIKF HERRNDKIIV FADNVFALKE YAIRLNKSYI YGPTSQGERM QILQNFKHNP KINTIFISKV GDTSFDLPEA NVLIQISSHG GSRRQEAQRL GRVLRAKKGM VAEEYNAFFY SLVSQDTQEM AYSTKRQGFL VDQGYSFKVI TKLAGMEEED LAFSTKEEQQ QLLQKVLAAT DLDAEEEVVA GEFGSRSSQA SRRFGTMSSM SGADDTVYME YHSSRSKAPS KHVHPLFKRF RK //