TF2H2_HUMAN
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 03-AUG-2022, entry version 219.
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}.
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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. [Q13888-1]
DR RefSeq; XP_016864893.1; XM_017009404.1. [Q13888-1]
DR RefSeq; XP_016864894.1; XM_017009405.1.
DR RefSeq; XP_016864895.1; XM_017009406.1. [Q13888-1]
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 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 AlphaFoldDB; Q13888; -.
DR SMR; Q13888; -.
DR BioGRID; 109221; 39.
DR BioGRID; 608768; 24.
DR CORUM; Q13888; -.
DR DIP; DIP-786N; -.
DR IntAct; Q13888; 18.
DR MINT; Q13888; -.
DR STRING; 9606.ENSP00000328901; -.
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; Q13888; -.
DR PeptideAtlas; Q13888; -.
DR PRIDE; Q13888; -.
DR ProteomicsDB; 59716; -. [Q13888-1]
DR Antibodypedia; 12115; 228 antibodies from 28 providers.
DR DNASU; 2966; -.
DR Ensembl; ENST00000274400.9; ENSP00000274400.5; ENSG00000145736.14. [Q13888-1]
DR Ensembl; ENST00000330280.11; ENSP00000328901.6; ENSG00000145736.14. [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 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; CMCHIEN; -.
DR OrthoDB; 768809at2759; -.
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; 348 hits in 968 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 100 other tissues.
DR ExpressionAtlas; Q13888; baseline and differential.
DR Genevisible; Q13888; HS.
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:0047485; F:protein N-terminus binding; IPI: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 from RNA polymerase II promoter; IDA:GO_Central.
DR CDD; cd01453; vWA_transcription_factor_IIH_type; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.50.410; -; 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 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; SSF53300; SSF53300; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR TIGRFAMs; TIGR00622; ssl1; 1.
DR PROSITE; PS50234; VWFA; 1.
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 STRAND 59..66
FT /evidence="ECO:0007829|PDB:6RO4"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:6RO4"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:6RO4"
FT HELIX 80..98
FT /evidence="ECO:0007829|PDB:6RO4"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:6RO4"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:6RO4"
FT TURN 124..127
FT /evidence="ECO:0007829|PDB:6RO4"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:6RO4"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:6RO4"
FT HELIX 146..154
FT /evidence="ECO:0007829|PDB:6RO4"
FT TURN 155..158
FT /evidence="ECO:0007829|PDB:6RO4"
FT STRAND 163..171
FT /evidence="ECO:0007829|PDB:6RO4"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:6RO4"
FT HELIX 185..191
FT /evidence="ECO:0007829|PDB:6RO4"
FT STRAND 195..203
FT /evidence="ECO:0007829|PDB:6RO4"
FT HELIX 206..215
FT /evidence="ECO:0007829|PDB:6RO4"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:6RO4"
FT HELIX 225..233
FT /evidence="ECO:0007829|PDB:6RO4"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:7AD8"
FT TURN 286..289
FT /evidence="ECO:0007829|PDB:6RO4"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:6RO4"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:6RO4"
FT HELIX 315..319
FT /evidence="ECO:0007829|PDB:6RO4"
FT TURN 320..323
FT /evidence="ECO:0007829|PDB:6RO4"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:6RO4"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:1Z60"
FT HELIX 336..339
FT /evidence="ECO:0007829|PDB:1Z60"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:5O85"
FT STRAND 355..358
FT /evidence="ECO:0007829|PDB:1Z60"
FT TURN 361..363
FT /evidence="ECO:0007829|PDB:5O85"
FT HELIX 369..377
FT /evidence="ECO:0007829|PDB:5O85"
FT HELIX 383..386
FT /evidence="ECO:0007829|PDB:5O85"
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
