TF2H2_MOUSE
ID TF2H2_MOUSE Reviewed; 396 AA.
AC Q9JIB4;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=General transcription factor IIH subunit 2;
DE AltName: Full=Basic transcription factor 2 44 kDa subunit;
DE Short=BTF2 p44;
DE AltName: Full=General transcription factor IIH polypeptide 2;
DE AltName: Full=TFIIH basal transcription factor complex p44 subunit;
GN Name=Gtf2h2; Synonyms=Btf2p44;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10958627; DOI=10.1101/gr.10.8.1095;
RA Endrizzi M.G., Hadinoto V., Growney J.D., Miller W., Dietrich W.F.;
RT "Genomic sequence analysis of the mouse Naip gene array.";
RL Genome Res. 10:1095-1102(2000).
RN [2]
RP PROTEIN SEQUENCE OF 188-195, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000250|UniProtKB:Q13888}.
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. Component of the 7-subunit TFIIH core complex composed
CC of XPB/ERCC3, XPD/ERCC2, GTF2H1, GTF2H2, GTF2H3, GTF2H4 and GTF2H5,
CC which is active in NER. The core complex associates with the 3-subunit
CC CDK-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 XPB, XPD, GTF2H1 and GTF2H3.
CC {ECO:0000250|UniProtKB:Q13888}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13888}.
CC -!- SIMILARITY: Belongs to the GTF2H2 family. {ECO:0000305}.
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DR EMBL; AF242432; AAF82753.1; -; Genomic_DNA.
DR CCDS; CCDS26730.1; -.
DR RefSeq; NP_071294.3; NM_022011.4.
DR AlphaFoldDB; Q9JIB4; -.
DR SMR; Q9JIB4; -.
DR BioGRID; 204782; 6.
DR IntAct; Q9JIB4; 4.
DR STRING; 10090.ENSMUSP00000065228; -.
DR iPTMnet; Q9JIB4; -.
DR PhosphoSitePlus; Q9JIB4; -.
DR EPD; Q9JIB4; -.
DR MaxQB; Q9JIB4; -.
DR PaxDb; Q9JIB4; -.
DR PRIDE; Q9JIB4; -.
DR ProteomicsDB; 259011; -.
DR DNASU; 23894; -.
DR Ensembl; ENSMUST00000066984; ENSMUSP00000065228; ENSMUSG00000021639.
DR GeneID; 23894; -.
DR KEGG; mmu:23894; -.
DR UCSC; uc007rqu.2; mouse.
DR CTD; 2966; -.
DR MGI; MGI:1345669; Gtf2h2.
DR VEuPathDB; HostDB:ENSMUSG00000021639; -.
DR eggNOG; KOG2807; Eukaryota.
DR GeneTree; ENSGT00490000043395; -.
DR HOGENOM; CLU_028556_1_0_1; -.
DR InParanoid; Q9JIB4; -.
DR OrthoDB; 768809at2759; -.
DR PhylomeDB; Q9JIB4; -.
DR TreeFam; TF314037; -.
DR Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-MMU-113418; Formation of the Early Elongation Complex.
DR Reactome; R-MMU-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-MMU-5696400; Dual Incision in GG-NER.
DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-MMU-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-MMU-6782135; Dual incision in TC-NER.
DR Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-MMU-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-MMU-72086; mRNA Capping.
DR Reactome; R-MMU-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-MMU-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-MMU-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-MMU-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-MMU-73863; RNA Polymerase I Transcription Termination.
DR Reactome; R-MMU-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-MMU-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-MMU-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-MMU-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR BioGRID-ORCS; 23894; 25 hits in 109 CRISPR screens.
DR ChiTaRS; Gtf2h2; mouse.
DR PRO; PR:Q9JIB4; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9JIB4; protein.
DR Bgee; ENSMUSG00000021639; Expressed in embryonic post-anal tail and 261 other tissues.
DR ExpressionAtlas; Q9JIB4; baseline and differential.
DR Genevisible; Q9JIB4; MM.
DR GO; GO:0000438; C:core TFIIH complex portion of holo TFIIH complex; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005669; C:transcription factor TFIID complex; ISO:MGI.
DR GO; GO:0000439; C:transcription factor TFIIH core complex; ISO:MGI.
DR GO; GO:0005675; C:transcription factor TFIIH holo complex; ISS:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006289; P:nucleotide-excision repair; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB.
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 Direct protein sequencing; DNA damage; DNA repair; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..396
FT /note="General transcription factor IIH subunit 2"
FT /id="PRO_0000119249"
FT DOMAIN 60..236
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT ZN_FING 292..309
FT /note="C4-type"
FT MOD_RES 95
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:A0JN27"
SQ SEQUENCE 396 AA; 44687 MW; 1BC57AFD464AA83F CRC64;
MDEEPERTKR WEGGYERTWE ILKEDETGSL KATIEDILFK AKRKRVFEHH GQVRLGMMRH
LYVVVDGSRT MEDQDLKPNR LTCTLKLLEY FVEEYFDQNP ISQIGIIVTK SKRAEKLTEL
SGNPRKHITS LKKAVDMTCH GEPSLYNSLS MAMQTLKHMP GHTSREVLII FSSLTTCDPS
NIYDLIKTLK TAKIRVSVIG LSAEVRVCTV LARETGGTYH VILDETHYKE LLAHHVSPPP
ASSSSECSLI RMGFPQHTIA SLSDQDAKPS FSMAHLDNNS TEPGLTLGGY FCPQCRAKYC
ELPVECKICG LTLVSAPHLA RSYHHLFPLD AFQEISLEEY KGERFCYGCQ GELKDQHVYV
CTVCQNVFCV DCDVFVHDSL HCCPGCIHKI PTPSGI
