ID TF2H2_HUMAN Reviewed; 395 AA. AC Q13888; Q15570; Q15571; Q9BS41; DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 228. DE RecName: Full=General transcription factor IIH subunit 2; DE AltName: Full=Basic transcription factor 2 44 kDa subunit; DE Short=BTF2 p44 {ECO:0000303|PubMed:8194529}; DE AltName: Full=General transcription factor IIH polypeptide 2; DE AltName: Full=TFIIH basal transcription factor complex p44 subunit {ECO:0000303|PubMed:11319235, ECO:0000303|PubMed:8194529}; GN Name=GTF2H2; Synonyms=BTF2P44; 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; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 35-40; 46-54; 60-68; RP 117-125 AND 214-229, FUNCTION, AND SUBUNIT. RX PubMed=8194529; DOI=10.1002/j.1460-2075.1994.tb06523.x; RA Humbert S., van Vuuren H.A., Lutz Y., Hoeijmakers J.H.J., Egly J.-M., RA Moncollin V.; RT "p44 and p34 subunits of the BTF2/TFIIH transcription factor have RT homologies with SSL1, a yeast protein involved in DNA repair."; RL EMBO J. 13:2393-2398(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Pituitary tumor; RA Zhang Q., Huang Q., Song H., Peng J., Fu G., Mao M., Dai M., Mao Y., RA Zhou J., Chen Z., Chen J.; RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-130 AND 327-395. RC TISSUE=Pre-B cell; RX PubMed=7552146; DOI=10.1159/000472281; RA van der Steege G., Draaijers T.G., Grootscholten P.M., Osinga J., RA Anzevino R., Velona I., Den Dunnen J.T., Scheffer H., Brahe C., RA van Ommen G.J.B., Buys C.H.C.M.; RT "A provisional transcript map of the spinal muscular atrophy (SMA) critical RT region."; RL Eur. J. Hum. Genet. 3:87-95(1995). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 253-395. RC TISSUE=Brain; RX PubMed=9503025; DOI=10.1006/geno.1997.5141; RA Chen Q., Baird S.D., Mahadevan M., Besner-Johnston A., Farahani R., RA Xuan J.-Y., Kang X., Lefebvre C., Ikeda J.-E., Korneluk R.G., RA MacKenzie A.E.; RT "Sequence of a 131-kb region of 5q13.1 containing the spinal muscular RT atrophy candidate genes SMN and NAIP."; RL Genomics 48:121-127(1998). RN [6] RP IDENTIFICATION IN THE TFIIH BASAL TRANSCRIPTION FACTOR, AND FUNCTION. RX PubMed=9852112; DOI=10.1074/jbc.273.51.34444; RA Kershnar E., Wu S.-Y., Chiang C.-M.; RT "Immunoaffinity purification and functional characterization of human RT transcription factor IIH and RNA polymerase II from clonal cell lines that RT conditionally express epitope-tagged subunits of the multiprotein RT complexes."; RL J. Biol. Chem. 273:34444-34453(1998). RN [7] RP MUTAGENESIS OF CYS-291; CYS-308; CYS-345; CYS-360; CYS-363; HIS-376; RP HIS-380 AND CYS-382, FUNCTION, AND SUBUNIT. RX PubMed=11319235; DOI=10.1074/jbc.m102457200; RA Tremeau-Bravard A., Perez C., Egly J.-M.; RT "A role of the C-terminal part of p44 in the promoter escape activity of RT transcription factor IIH."; RL J. Biol. Chem. 276:27693-27697(2001). RN [8] RP INTERACTION WITH VARICELLA-ZOSTER VIRUS IE63 PROTEIN. RX PubMed=15843171; DOI=10.1515/bc.2005.031; RA Di Valentin E., Bontems S., Habran L., Jolois O., Markine-Goriaynoff N., RA Vanderplasschen A., Sadzot-Delvaux C., Piette J.; RT "Varicella-zoster virus IE63 protein represses the basal transcription RT machinery by disorganizing the pre-initiation complex."; RL Biol. Chem. 386:255-267(2005). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [10] {ECO:0007744|PDB:5IVW, ECO:0007744|PDB:5IY6, ECO:0007744|PDB:5IY7, ECO:0007744|PDB:5IY8, ECO:0007744|PDB:5IY9} RP STRUCTURE BY ELECTRON MICROSCOPY (6.30 ANGSTROMS), SUBUNIT, SUBCELLULAR RP LOCATION, AND FUNCTION. RX PubMed=27193682; DOI=10.1038/nature17970; RA He Y., Yan C., Fang J., Inouye C., Tjian R., Ivanov I., Nogales E.; RT "Near-atomic resolution visualization of human transcription promoter RT opening."; RL Nature 533:359-365(2016). RN [11] RP VARIANTS MET-151 AND LEU-236, AND TISSUE SPECIFICITY. RX PubMed=9063743; DOI=10.1093/hmg/6.2.229; RA Carter T.A., Bonnemann C.G., Wang C.H., Obici S., Parano E., Bonaldo M.F., RA Ross B.M., Penchaszadeh G.K., Mackenzie A.E., Soares M.B., Kunkel L.M., RA Gilliam T.C.; RT "A multicopy transcription-repair gene, BTF2p44, maps to the SMA region and RT demonstrates SMA associated deletions."; RL Hum. Mol. Genet. 6:229-236(1997). CC -!- FUNCTION: Component of the general transcription and DNA repair factor CC IIH (TFIIH) core complex, which is involved in general and CC transcription-coupled nucleotide excision repair (NER) of damaged DNA CC and, when complexed to CAK, in RNA transcription by RNA polymerase II. CC In NER, TFIIH acts by opening DNA around the lesion to allow the CC excision of the damaged oligonucleotide and its replacement by a new CC DNA fragment. In transcription, TFIIH has an essential role in CC transcription initiation. When the pre-initiation complex (PIC) has CC been established, TFIIH is required for promoter opening and promoter CC escape. Phosphorylation of the C-terminal tail (CTD) of the largest CC subunit of RNA polymerase II by the kinase module CAK controls the CC initiation of transcription. The N-terminus of GTF2H2 interacts with CC and regulates XPD whereas an intact C-terminus is required for a CC successful escape of RNAP II form the promoter. CC {ECO:0000269|PubMed:11319235, ECO:0000269|PubMed:27193682, CC ECO:0000269|PubMed:8194529, ECO:0000269|PubMed:9852112}. CC -!- SUBUNIT: Component of the TFIID-containing RNA polymerase II pre- CC initiation complex that is composed of TBP and at least GTF2A1, GTF2A2, CC GTF2E1, GTF2E2, GTF2F1, GTF2H2, GTF2H3, GTF2H4, GTF2H5, GTF2B, TCEA1, CC ERCC2 and ERCC3 (PubMed:27193682). Component of the 7-subunit TFIIH CC core complex composed of XPB/ERCC3, XPD/ERCC2, GTF2H1, GTF2H2, GTF2H3, CC GTF2H4 and GTF2H5, which is active in NER. The core complex associates CC with the 3-subunit CDK-activating kinase (CAK) module composed of CC CCNH/cyclin H, CDK7 and MNAT1 to form the 10-subunit holoenzyme (holo- CC TFIIH) active in transcription (PubMed:9852112, PubMed:11319235). CC Interacts with XPB, XPD, GTF2H1 and GTF2H3 (PubMed:11319235). CC {ECO:0000269|PubMed:11319235, ECO:0000269|PubMed:27193682, CC ECO:0000269|PubMed:8194529, ECO:0000269|PubMed:9852112}. CC -!- SUBUNIT: (Microbial infection) Interacts with varicella-zoster virus CC IE63 protein. {ECO:0000269|PubMed:15843171}. CC -!- INTERACTION: CC Q13888; P18074: ERCC2; NbExp=9; IntAct=EBI-1565170, EBI-6380590; CC Q13888; P32780: GTF2H1; NbExp=5; IntAct=EBI-1565170, EBI-715539; CC Q13888; Q6ZYL4: GTF2H5; NbExp=4; IntAct=EBI-1565170, EBI-6380438; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27193682}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=A number of isoforms may be produced. The isoforms may be CC also produced by incomplete gene duplication.; CC Name=1; CC IsoId=Q13888-1; Sequence=Displayed; CC -!- TISSUE SPECIFICITY: Widely expressed, with higher expression in CC skeletal muscle. {ECO:0000269|PubMed:9063743}. CC -!- SIMILARITY: Belongs to the GTF2H2 family. {ECO:0000305}. 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; Z30094; CAA82910.1; -; mRNA. DR EMBL; AF078847; AAD44479.1; -; mRNA. DR EMBL; U21911; AAA64502.1; -; mRNA. DR EMBL; U21910; AAA64503.1; -; mRNA. DR EMBL; BC005345; AAH05345.1; -; mRNA. DR EMBL; U80017; AAC52046.1; -; Genomic_DNA. DR CCDS; CCDS34183.1; -. [Q13888-1] DR PIR; S44454; S44454. DR RefSeq; NP_001506.1; NM_001515.3. [Q13888-1] DR RefSeq; XP_016864892.1; XM_017009403.1. DR RefSeq; XP_016864893.1; XM_017009404.1. DR RefSeq; XP_016864894.1; XM_017009405.1. DR RefSeq; XP_016864895.1; XM_017009406.1. DR PDB; 1Z60; NMR; -; A=328-386. DR PDB; 5IVW; EM; 10.00 A; 0=1-395. DR PDB; 5IY6; EM; 7.20 A; 0=1-395. DR PDB; 5IY7; EM; 8.60 A; 0=1-395. DR PDB; 5IY8; EM; 7.90 A; 0=1-395. DR PDB; 5IY9; EM; 6.30 A; 0=1-395. DR PDB; 5O85; X-ray; 3.40 A; B/D=1-395. DR PDB; 5OF4; EM; 4.40 A; E=1-395. DR PDB; 6NMI; EM; 3.70 A; E=51-387. DR PDB; 6O9L; EM; 7.20 A; 6=1-395. DR PDB; 6O9M; EM; 4.40 A; 6=1-395. DR PDB; 6RO4; EM; 3.50 A; D=1-395. DR PDB; 7AD8; EM; 3.50 A; D=1-395. DR PDB; 7EGB; EM; 3.30 A; 2=1-395. DR PDB; 7EGC; EM; 3.90 A; 2=1-395. DR PDB; 7ENA; EM; 4.07 A; 2=1-395. DR PDB; 7ENC; EM; 4.13 A; 2=1-395. DR PDB; 7LBM; EM; 4.80 A; a=1-395. DR PDB; 7NVR; EM; 4.50 A; 6=1-395. DR PDB; 7NVW; EM; 4.30 A; 6=1-395. DR PDB; 7NVX; EM; 3.90 A; 6=1-395. DR PDB; 7NVY; EM; 7.30 A; 6=1-395. DR PDB; 7NVZ; EM; 7.20 A; 6=1-395. DR PDB; 7NW0; EM; 6.60 A; 6=1-395. DR PDB; 8BVW; EM; 4.00 A; 4=1-395. DR PDB; 8BYQ; EM; 4.10 A; 4=1-395. DR PDB; 8EBS; EM; 4.00 A; E=1-395. DR PDB; 8EBT; EM; 3.90 A; E=8-387. DR PDB; 8EBU; EM; 3.30 A; E=1-395. DR PDB; 8EBV; EM; 7.10 A; E=1-395. DR PDB; 8EBW; EM; 5.60 A; E=1-395. DR PDB; 8EBX; EM; 3.60 A; E=1-395. DR PDB; 8EBY; EM; 3.60 A; E=1-395. DR PDB; 8GXQ; EM; 5.04 A; HG=1-395. DR PDB; 8GXS; EM; 4.16 A; HG=1-395. DR PDB; 8WAK; EM; 5.47 A; 2=1-395. DR PDB; 8WAL; EM; 8.52 A; 2=1-395. DR PDB; 8WAN; EM; 6.07 A; 2=1-395. DR PDB; 8WAO; EM; 6.40 A; 2=1-395. DR PDB; 8WAP; EM; 5.85 A; 2=1-395. DR PDB; 8WAQ; EM; 6.29 A; 2=1-395. DR PDB; 8WAR; EM; 7.20 A; 2=1-395. DR PDB; 8WAS; EM; 6.13 A; 2=1-395. DR PDBsum; 1Z60; -. DR PDBsum; 5IVW; -. DR PDBsum; 5IY6; -. DR PDBsum; 5IY7; -. DR PDBsum; 5IY8; -. DR PDBsum; 5IY9; -. DR PDBsum; 5O85; -. DR PDBsum; 5OF4; -. DR PDBsum; 6NMI; -. DR PDBsum; 6O9L; -. DR PDBsum; 6O9M; -. DR PDBsum; 6RO4; -. DR PDBsum; 7AD8; -. DR PDBsum; 7EGB; -. DR PDBsum; 7EGC; -. DR PDBsum; 7ENA; -. DR PDBsum; 7ENC; -. DR PDBsum; 7LBM; -. DR PDBsum; 7NVR; -. DR PDBsum; 7NVW; -. DR PDBsum; 7NVX; -. DR PDBsum; 7NVY; -. DR PDBsum; 7NVZ; -. DR PDBsum; 7NW0; -. DR PDBsum; 8BVW; -. DR PDBsum; 8BYQ; -. DR PDBsum; 8EBS; -. DR PDBsum; 8EBT; -. DR PDBsum; 8EBU; -. DR PDBsum; 8EBV; -. DR PDBsum; 8EBW; -. DR PDBsum; 8EBX; -. DR PDBsum; 8EBY; -. DR PDBsum; 8GXQ; -. DR PDBsum; 8GXS; -. DR PDBsum; 8WAK; -. DR PDBsum; 8WAL; -. DR PDBsum; 8WAN; -. DR PDBsum; 8WAO; -. DR PDBsum; 8WAP; -. DR PDBsum; 8WAQ; -. DR PDBsum; 8WAR; -. DR PDBsum; 8WAS; -. DR AlphaFoldDB; Q13888; -. DR EMDB; EMD-0452; -. DR EMDB; EMD-16274; -. DR EMDB; EMD-16331; -. DR EMDB; EMD-27997; -. DR EMDB; EMD-31111; -. DR SMR; Q13888; -. DR BioGRID; 109221; 45. DR BioGRID; 608768; 46. DR ComplexPortal; CPX-2395; General transcription factor TFIIH complex. DR CORUM; Q13888; -. DR DIP; DIP-786N; -. DR IntAct; Q13888; 18. DR MINT; Q13888; -. DR STRING; 9606.ENSP00000274400; -. DR iPTMnet; Q13888; -. DR PhosphoSitePlus; Q13888; -. DR SwissPalm; Q13888; -. DR BioMuta; GTF2H2; -. DR DMDM; 17380326; -. DR EPD; Q13888; -. DR jPOST; Q13888; -. DR MassIVE; Q13888; -. DR MaxQB; Q13888; -. DR PaxDb; 9606-ENSP00000328901; -. DR PeptideAtlas; Q13888; -. DR ProteomicsDB; 59716; -. [Q13888-1] DR Pumba; Q13888; -. DR Antibodypedia; 12115; 256 antibodies from 28 providers. DR DNASU; 2966; -. DR Ensembl; ENST00000274400.10; ENSP00000274400.5; ENSG00000145736.15. [Q13888-1] DR Ensembl; ENST00000330280.11; ENSP00000328901.6; ENSG00000145736.15. [Q13888-1] DR Ensembl; ENST00000612581.4; ENSP00000480548.1; ENSG00000276910.4. [Q13888-1] DR Ensembl; ENST00000617228.4; ENSP00000479262.1; ENSG00000275045.4. [Q13888-1] DR Ensembl; ENST00000619997.4; ENSP00000477954.1; ENSG00000275045.4. [Q13888-1] DR Ensembl; ENST00000628423.2; ENSP00000486014.1; ENSG00000276910.4. [Q13888-1] DR GeneID; 2966; -. DR KEGG; hsa:2966; -. DR MANE-Select; ENST00000274400.10; ENSP00000274400.5; NM_001515.4; NP_001506.1. DR UCSC; uc003kau.6; human. [Q13888-1] DR AGR; HGNC:4656; -. DR CTD; 2966; -. DR DisGeNET; 2966; -. DR GeneCards; GTF2H2; -. DR HGNC; HGNC:4656; GTF2H2. DR HPA; ENSG00000145736; Low tissue specificity. DR MIM; 601748; gene. DR neXtProt; NX_Q13888; -. DR OpenTargets; ENSG00000145736; -. DR PharmGKB; PA29042; -. DR VEuPathDB; HostDB:ENSG00000145736; -. DR eggNOG; KOG2807; Eukaryota. DR GeneTree; ENSGT00490000043395; -. DR HOGENOM; CLU_028556_1_0_1; -. DR InParanoid; Q13888; -. DR OMA; INWVEVP; -. DR OrthoDB; 276422at2759; -. DR PhylomeDB; Q13888; -. DR TreeFam; TF314037; -. DR PathwayCommons; Q13888; -. DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex. DR Reactome; R-HSA-113418; Formation of the Early Elongation Complex. DR Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat. DR Reactome; R-HSA-167158; Formation of the HIV-1 Early Elongation Complex. DR Reactome; R-HSA-167160; RNA Pol II CTD phosphorylation and interaction with CE during HIV infection. DR Reactome; R-HSA-167161; HIV Transcription Initiation. DR Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape. DR Reactome; R-HSA-167172; Transcription of the HIV genome. DR Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat. DR Reactome; R-HSA-167246; Tat-mediated elongation of the HIV-1 transcript. DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression. DR Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER. DR Reactome; R-HSA-5696400; Dual Incision in GG-NER. DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events. DR Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex. DR Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER). DR Reactome; R-HSA-6782135; Dual incision in TC-NER. DR Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER. DR Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes. DR Reactome; R-HSA-72086; mRNA Capping. DR Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation. DR Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape. DR Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape. DR Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening. DR Reactome; R-HSA-73863; RNA Polymerase I Transcription Termination. DR Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation. DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation. DR Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance. DR Reactome; R-HSA-77075; RNA Pol II CTD phosphorylation and interaction with CE. DR SignaLink; Q13888; -. DR SIGNOR; Q13888; -. DR BioGRID-ORCS; 2966; 357 hits in 1035 CRISPR screens. DR ChiTaRS; GTF2H2; human. DR EvolutionaryTrace; Q13888; -. DR GeneWiki; GTF2H2; -. DR GenomeRNAi; 2966; -. DR Pharos; Q13888; Tbio. DR PRO; PR:Q13888; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; Q13888; Protein. DR Bgee; ENSG00000145736; Expressed in endometrium and 101 other cell types or tissues. DR ExpressionAtlas; Q13888; baseline and differential. DR GO; GO:0000438; C:core TFIIH complex portion of holo TFIIH complex; IDA:UniProtKB. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB. DR GO; GO:0000439; C:transcription factor TFIIH core complex; IDA:UniProtKB. DR GO; GO:0005675; C:transcription factor TFIIH holo complex; IDA:UniProtKB. DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IDA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0002031; P:G protein-coupled receptor internalization; IMP:UniProtKB. DR GO; GO:0006289; P:nucleotide-excision repair; IBA:GO_Central. DR GO; GO:1905776; P:positive regulation of DNA helicase activity; IDA:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0009411; P:response to UV; TAS:ProtInc. DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IDA:GO_Central. DR CDD; cd01453; vWA_transcription_factor_IIH_type; 1. DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR046349; C1-like_sf. DR InterPro; IPR007198; Ssl1-like. DR InterPro; IPR004595; TFIIH_C1-like_dom. DR InterPro; IPR012170; TFIIH_SSL1/p44. DR InterPro; IPR002035; VWF_A. DR InterPro; IPR036465; vWFA_dom_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR NCBIfam; TIGR00622; ssl1; 1. DR PANTHER; PTHR12695; GENERAL TRANSCRIPTION FACTOR IIH SUBUNIT 2; 1. DR PANTHER; PTHR12695:SF2; GENERAL TRANSCRIPTION FACTOR IIH SUBUNIT 2-RELATED; 1. DR Pfam; PF07975; C1_4; 1. DR Pfam; PF04056; Ssl1; 1. DR PIRSF; PIRSF015919; TFIIH_SSL1; 1. DR SMART; SM01047; C1_4; 1. DR SMART; SM00327; VWA; 1. DR SUPFAM; SSF57889; Cysteine-rich domain; 1. DR SUPFAM; SSF53300; vWA-like; 1. DR PROSITE; PS50234; VWFA; 1. DR Genevisible; Q13888; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Direct protein sequencing; DNA damage; KW DNA repair; Host-virus interaction; Metal-binding; Nucleus; Phosphoprotein; KW Reference proteome; Transcription; Transcription regulation; Zinc; KW Zinc-finger. FT CHAIN 1..395 FT /note="General transcription factor IIH subunit 2" FT /id="PRO_0000119248" FT DOMAIN 60..236 FT /note="VWFA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219" FT ZN_FING 291..308 FT /note="C4-type" FT MOD_RES 95 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:A0JN27" FT VARIANT 151 FT /note="I -> M (in dbSNP:rs2576895)" FT /evidence="ECO:0000269|PubMed:9063743" FT /id="VAR_011664" FT VARIANT 236 FT /note="V -> L (in dbSNP:rs201102513)" FT /evidence="ECO:0000269|PubMed:9063743" FT /id="VAR_011665" FT MUTAGEN 291 FT /note="C->A: Reconstituted TFIIH complex lacks p62 and has FT no transcriptional activity." FT /evidence="ECO:0000269|PubMed:11319235" FT MUTAGEN 308 FT /note="C->A: Reconstituted TFIIH complex lacks p62 and has FT no transcriptional activity." FT /evidence="ECO:0000269|PubMed:11319235" FT MUTAGEN 345 FT /note="C->A: No effect on the transcriptional activity of FT the reconstituted TFIIH complex." FT /evidence="ECO:0000269|PubMed:11319235" FT MUTAGEN 360 FT /note="C->A: No effect on the transcriptional activity of FT the reconstituted TFIIH complex." FT /evidence="ECO:0000269|PubMed:11319235" FT MUTAGEN 363 FT /note="C->A: No effect on the transcriptional activity of FT the reconstituted TFIIH complex." FT /evidence="ECO:0000269|PubMed:11319235" FT MUTAGEN 376 FT /note="H->A: No effect on the transcriptional activity of FT the reconstituted TFIIH complex." FT /evidence="ECO:0000269|PubMed:11319235" FT MUTAGEN 380 FT /note="H->A: No effect on the transcriptional activity of FT the reconstituted TFIIH complex." FT /evidence="ECO:0000269|PubMed:11319235" FT MUTAGEN 382 FT /note="C->A: No effect on the transcriptional activity of FT the reconstituted TFIIH complex." FT /evidence="ECO:0000269|PubMed:11319235" FT CONFLICT 129 FT /note="T -> S (in Ref. 4)" FT /evidence="ECO:0000305" FT HELIX 18..20 FT /evidence="ECO:0007829|PDB:8EBU" FT STRAND 25..27 FT /evidence="ECO:0007829|PDB:8EBU" FT HELIX 30..41 FT /evidence="ECO:0007829|PDB:8EBU" FT STRAND 59..66 FT /evidence="ECO:0007829|PDB:8EBU" FT HELIX 69..72 FT /evidence="ECO:0007829|PDB:8EBU" FT STRAND 75..78 FT /evidence="ECO:0007829|PDB:8EBU" FT HELIX 80..98 FT /evidence="ECO:0007829|PDB:8EBU" FT STRAND 103..110 FT /evidence="ECO:0007829|PDB:8EBU" FT STRAND 113..122 FT /evidence="ECO:0007829|PDB:8EBU" FT HELIX 124..135 FT /evidence="ECO:0007829|PDB:8EBU" FT HELIX 145..156 FT /evidence="ECO:0007829|PDB:8EBU" FT STRAND 163..171 FT /evidence="ECO:0007829|PDB:8EBU" FT HELIX 182..191 FT /evidence="ECO:0007829|PDB:8EBU" FT STRAND 194..203 FT /evidence="ECO:0007829|PDB:8EBU" FT HELIX 206..215 FT /evidence="ECO:0007829|PDB:8EBU" FT STRAND 219..221 FT /evidence="ECO:0007829|PDB:8EBU" FT HELIX 225..236 FT /evidence="ECO:0007829|PDB:8EBU" FT STRAND 251..253 FT /evidence="ECO:0007829|PDB:8EBU" FT HELIX 273..276 FT /evidence="ECO:0007829|PDB:8EBU" FT STRAND 278..280 FT /evidence="ECO:0007829|PDB:8EBU" FT STRAND 288..290 FT /evidence="ECO:0007829|PDB:8EBU" FT TURN 292..294 FT /evidence="ECO:0007829|PDB:8EBU" FT STRAND 297..304 FT /evidence="ECO:0007829|PDB:8EBU" FT TURN 306..308 FT /evidence="ECO:0007829|PDB:8EBU" FT HELIX 315..319 FT /evidence="ECO:0007829|PDB:8EBU" FT HELIX 322..325 FT /evidence="ECO:0007829|PDB:8EBU" FT STRAND 332..335 FT /evidence="ECO:0007829|PDB:8EBU" FT TURN 336..338 FT /evidence="ECO:0007829|PDB:8EBU" FT TURN 346..348 FT /evidence="ECO:0007829|PDB:8EBU" FT STRAND 354..359 FT /evidence="ECO:0007829|PDB:8EBU" FT TURN 361..363 FT /evidence="ECO:0007829|PDB:8EBU" FT HELIX 369..377 FT /evidence="ECO:0007829|PDB:8EBU" FT HELIX 383..386 FT /evidence="ECO:0007829|PDB:8EBU" SQ SEQUENCE 395 AA; 44419 MW; 56D1BD8841288739 CRC64; MDEEPERTKR WEGGYERTWE ILKEDESGSL KATIEDILFK AKRKRVFEHH GQVRLGMMRH LYVVVDGSRT MEDQDLKPNR LTCTLKLLEY FVEEYFDQNP ISQIGIIVTK SKRAEKLTEL SGNPRKHITS LKKAVDMTCH GEPSLYNSLS IAMQTLKHMP GHTSREVLII FSSLTTCDPS NIYDLIKTLK AAKIRVSVIG LSAEVRVCTV LARETGGTYH VILDESHYKE LLTHHVSPPP ASSSSECSLI RMGFPQHTIA SLSDQDAKPS FSMAHLDGNT EPGLTLGGYF CPQCRAKYCE LPVECKICGL TLVSAPHLAR SYHHLFPLDA FQEIPLEEYN GERFCYGCQG ELKDQHVYVC AVCQNVFCVD CDVFVHDSLH CCPGCIHKIP APSGV //