TF2H2_RAT
ID TF2H2_RAT Reviewed; 396 AA.
AC A0JN27;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 109.
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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-95, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
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; BC126097; AAI26098.1; -; mRNA.
DR RefSeq; NP_001070896.1; NM_001077428.1.
DR RefSeq; XP_006231906.1; XM_006231844.3.
DR RefSeq; XP_006231907.1; XM_006231845.3.
DR AlphaFoldDB; A0JN27; -.
DR SMR; A0JN27; -.
DR STRING; 10116.ENSRNOP00000057895; -.
DR iPTMnet; A0JN27; -.
DR PhosphoSitePlus; A0JN27; -.
DR PaxDb; A0JN27; -.
DR PeptideAtlas; A0JN27; -.
DR PRIDE; A0JN27; -.
DR Ensembl; ENSRNOT00000061183; ENSRNOP00000057895; ENSRNOG00000018230.
DR GeneID; 294693; -.
DR KEGG; rno:294693; -.
DR UCSC; RGD:1310499; rat.
DR CTD; 2966; -.
DR RGD; 1310499; Gtf2h2.
DR eggNOG; KOG2807; Eukaryota.
DR GeneTree; ENSGT00490000043395; -.
DR HOGENOM; CLU_028556_1_0_1; -.
DR InParanoid; A0JN27; -.
DR OMA; CMCHIEN; -.
DR OrthoDB; 768809at2759; -.
DR PhylomeDB; A0JN27; -.
DR TreeFam; TF314037; -.
DR Reactome; R-RNO-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-RNO-113418; Formation of the Early Elongation Complex.
DR Reactome; R-RNO-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-RNO-5696400; Dual Incision in GG-NER.
DR Reactome; R-RNO-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-RNO-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-RNO-6782135; Dual incision in TC-NER.
DR Reactome; R-RNO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-RNO-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-RNO-72086; mRNA Capping.
DR Reactome; R-RNO-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-RNO-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-RNO-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-RNO-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-RNO-73863; RNA Polymerase I Transcription Termination.
DR Reactome; R-RNO-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-RNO-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-RNO-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-RNO-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR PRO; PR:A0JN27; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000018230; Expressed in ovary and 19 other tissues.
DR Genevisible; A0JN27; RN.
DR GO; GO:0000438; C:core TFIIH complex portion of holo TFIIH complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005675; C:transcription factor TFIIH holo complex; ISS:UniProtKB.
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 DNA damage; DNA repair; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..396
FT /note="General transcription factor IIH subunit 2"
FT /id="PRO_0000327566"
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:0007744|PubMed:16641100"
SQ SEQUENCE 396 AA; 44703 MW; 2812ED7B0DC5B3C8 CRC64;
MDEEPERTKR WEGGYERTWE ILKEDESGSL KATIEDILFK AKRKRVFEHH GQVRLGMMRH
LYVVVDGSRT MEDQDLKPNR LTCTLKLLEY FVEEYFDQNP ISQIGIIVTK SKRAEKLTEL
SGNPRKHITS LKKAVDMTCH GEPSLYNSLS MAMQTLKHMP GHTSREVLII FSSLTTCDPS
NIYDLIKTLK TAKIRVSVIG LSAEVRVCTV LARETGGTYH VILDETHYKE LLARHVSPPP
ASSGSECSLI RMGFPQHTIA SLSDQDAKPS FSMAHLDNNS TEPGLTLGGY FCPQCRAKYC
ELPVECKICG LTLVSAPHLA RSYHHLFPLD AFQEIPLEEY KGERFCYGCQ GELKDQHVYV
CTVCRNVFCV DCDVFVHDSL HCCPGCVHKI PTQSGV
