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General transcription factor IIH subunit 2 (Basic transcription factor 2 44 kDa subunit) (BTF2 p44) (General transcription factor IIH polypeptide 2) (TFIIH basal transcription factor complex p44 subunit)

 TF2H2_HUMAN             Reviewed;         395 AA.
Q13888; Q15570; Q15571; Q9BS41;
18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 186.
RecName: Full=General transcription factor IIH subunit 2;
AltName: Full=Basic transcription factor 2 44 kDa subunit;
Short=BTF2 p44 {ECO:0000303|PubMed:8194529};
AltName: Full=General transcription factor IIH polypeptide 2;
AltName: Full=TFIIH basal transcription factor complex p44 subunit {ECO:0000303|PubMed:11319235, ECO:0000303|PubMed:8194529};
Name=GTF2H2; Synonyms=BTF2P44;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 35-40; 46-54; 60-68;
117-125 AND 214-229, FUNCTION, AND SUBUNIT.
PubMed=8194529;
Humbert S., van Vuuren H.A., Lutz Y., Hoeijmakers J.H.J., Egly J.-M.,
Moncollin V.;
"p44 and p34 subunits of the BTF2/TFIIH transcription factor have
homologies with SSL1, a yeast protein involved in DNA repair.";
EMBO J. 13:2393-2398(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Pituitary tumor;
Zhang Q., Huang Q., Song H., Peng J., Fu G., Mao M., Dai M., Mao Y.,
Zhou J., Chen Z., Chen J.;
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-130 AND 327-395.
TISSUE=Pre-B cell;
PubMed=7552146;
van der Steege G., Draaijers T.G., Grootscholten P.M., Osinga J.,
Anzevino R., Velona I., Den Dunnen J.T., Scheffer H., Brahe C.,
van Ommen G.J.B., Buys C.H.C.M.;
"A provisional transcript map of the spinal muscular atrophy (SMA)
critical region.";
Eur. J. Hum. Genet. 3:87-95(1995).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 253-395.
TISSUE=Brain;
PubMed=9503025; DOI=10.1006/geno.1997.5141;
Chen Q., Baird S.D., Mahadevan M., Besner-Johnston A., Farahani R.,
Xuan J.-Y., Kang X., Lefebvre C., Ikeda J.-E., Korneluk R.G.,
MacKenzie A.E.;
"Sequence of a 131-kb region of 5q13.1 containing the spinal muscular
atrophy candidate genes SMN and NAIP.";
Genomics 48:121-127(1998).
[6]
IDENTIFICATION IN THE TFIIH BASAL TRANSCRIPTION FACTOR, AND FUNCTION.
PubMed=9852112; DOI=10.1074/jbc.273.51.34444;
Kershnar E., Wu S.-Y., Chiang C.-M.;
"Immunoaffinity purification and functional characterization of human
transcription factor IIH and RNA polymerase II from clonal cell lines
that conditionally express epitope-tagged subunits of the multiprotein
complexes.";
J. Biol. Chem. 273:34444-34453(1998).
[7]
MUTAGENESIS OF CYS-291; CYS-308; CYS-345; CYS-360; CYS-363; HIS-376;
HIS-380 AND CYS-382, FUNCTION, AND SUBUNIT.
PubMed=11319235; DOI=10.1074/jbc.M102457200;
Tremeau-Bravard A., Perez C., Egly J.-M.;
"A role of the C-terminal part of p44 in the promoter escape activity
of transcription factor IIH.";
J. Biol. Chem. 276:27693-27697(2001).
[8]
INTERACTION WITH VARICELLA-ZOSTER VIRUS IE63 PROTEIN.
PubMed=15843171; DOI=10.1515/BC.2005.031;
Di Valentin E., Bontems S., Habran L., Jolois O.,
Markine-Goriaynoff N., Vanderplasschen A., Sadzot-Delvaux C.,
Piette J.;
"Varicella-zoster virus IE63 protein represses the basal transcription
machinery by disorganizing the pre-initiation complex.";
Biol. Chem. 386:255-267(2005).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10] {ECO:0000244|PDB:5IVW, ECO:0000244|PDB:5IY6, ECO:0000244|PDB:5IY7, ECO:0000244|PDB:5IY8, ECO:0000244|PDB:5IY9}
STRUCTURE BY ELECTRON MICROSCOPY (6.30 ANGSTROMS), SUBUNIT,
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=27193682; DOI=10.1038/nature17970;
He Y., Yan C., Fang J., Inouye C., Tjian R., Ivanov I., Nogales E.;
"Near-atomic resolution visualization of human transcription promoter
opening.";
Nature 533:359-365(2016).
[11]
VARIANTS MET-151 AND LEU-236, AND TISSUE SPECIFICITY.
PubMed=9063743; DOI=10.1093/hmg/6.2.229;
Carter T.A., Bonnemann C.G., Wang C.H., Obici S., Parano E.,
Bonaldo M.F., Ross B.M., Penchaszadeh G.K., Mackenzie A.E.,
Soares M.B., Kunkel L.M., Gilliam T.C.;
"A multicopy transcription-repair gene, BTF2p44, maps to the SMA
region and demonstrates SMA associated deletions.";
Hum. Mol. Genet. 6:229-236(1997).
-!- FUNCTION: Component of the core-TFIIH basal transcription factor
involved in nucleotide excision repair (NER) of DNA and, when
complexed to CAK, in RNA transcription by RNA polymerase II. The
N-terminus interacts with and regulates XPD whereas an intact C-
terminus is required for a successful escape of RNAP II form the
promoter. {ECO:0000269|PubMed:11319235,
ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:8194529,
ECO:0000269|PubMed:9852112}.
-!- SUBUNIT: Component of the TFIID-containing RNA polymerase II pre-
initiation complex that is composed of TBP and at least GTF2A1,
GTF2A2, GTF2E1, GTF2E2, GTF2F1, GTF2H2, GTF2H3, GTF2H4, GTF2H5,
GTF2B, TCEA1, ERCC2 and ERCC3 (PubMed:27193682). One of the 6
subunits forming the core-TFIIH basal transcription factor
(PubMed:8194529, PubMed:11319235). The core-TFIIH basal
transcription factor associates with the CAK complex composed of
CDK7, CCNH/cyclin H and MNAT1 to form the TFIIH basal
transcription factor (PubMed:9852112, PubMed:11319235). Interacts
with XPB, XPD, GTF2H1 and GTF2H3 (PubMed:11319235). Interacts with
varicella-zoster virus IE63 protein (PubMed:15843171).
{ECO:0000269|PubMed:11319235, ECO:0000269|PubMed:15843171,
ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:8194529,
ECO:0000269|PubMed:9852112}.
-!- INTERACTION:
Q6ZYL4:GTF2H5; NbExp=3; IntAct=EBI-1565170, EBI-6380438;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27193682}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms may be produced. The isoforms may
be also produced by incomplete gene duplication.;
Name=1;
IsoId=Q13888-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Widely expressed, with higher expression in
skeletal muscle. {ECO:0000269|PubMed:9063743}.
-!- SIMILARITY: Belongs to the GTF2H2 family. {ECO:0000305}.
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EMBL; Z30094; CAA82910.1; -; mRNA.
EMBL; AF078847; AAD44479.1; -; mRNA.
EMBL; U21911; AAA64502.1; -; mRNA.
EMBL; U21910; AAA64503.1; -; mRNA.
EMBL; BC005345; AAH05345.1; -; mRNA.
EMBL; U80017; AAC52046.1; -; Genomic_DNA.
CCDS; CCDS34183.1; -. [Q13888-1]
PIR; S44454; S44454.
RefSeq; NP_001506.1; NM_001515.3. [Q13888-1]
RefSeq; XP_016864892.1; XM_017009403.1. [Q13888-1]
RefSeq; XP_016864893.1; XM_017009404.1. [Q13888-1]
RefSeq; XP_016864894.1; XM_017009405.1. [Q13888-1]
RefSeq; XP_016864895.1; XM_017009406.1. [Q13888-1]
UniGene; Hs.191356; -.
UniGene; Hs.607501; -.
PDB; 1Z60; NMR; -; A=328-386.
PDB; 5IVW; EM; 10.00 A; 0=1-395.
PDB; 5IY6; EM; 7.20 A; 0=1-395.
PDB; 5IY7; EM; 8.60 A; 0=1-395.
PDB; 5IY8; EM; 7.90 A; 0=1-395.
PDB; 5IY9; EM; 6.30 A; 0=1-395.
PDB; 5OF4; EM; 4.40 A; E=1-395.
PDBsum; 1Z60; -.
PDBsum; 5IVW; -.
PDBsum; 5IY6; -.
PDBsum; 5IY7; -.
PDBsum; 5IY8; -.
PDBsum; 5IY9; -.
PDBsum; 5OF4; -.
ProteinModelPortal; Q13888; -.
SMR; Q13888; -.
BioGrid; 109221; 21.
BioGrid; 608768; 9.
CORUM; Q13888; -.
DIP; DIP-786N; -.
IntAct; Q13888; 8.
MINT; MINT-3028823; -.
STRING; 9606.ENSP00000274400; -.
iPTMnet; Q13888; -.
PhosphoSitePlus; Q13888; -.
BioMuta; GTF2H2; -.
DMDM; 17380326; -.
EPD; Q13888; -.
MaxQB; Q13888; -.
PaxDb; Q13888; -.
PeptideAtlas; Q13888; -.
PRIDE; Q13888; -.
DNASU; 2966; -.
Ensembl; ENST00000274400; ENSP00000274400; ENSG00000145736. [Q13888-1]
Ensembl; ENST00000330280; ENSP00000328901; ENSG00000145736. [Q13888-1]
Ensembl; ENST00000612581; ENSP00000480548; ENSG00000276910. [Q13888-1]
Ensembl; ENST00000617228; ENSP00000479262; ENSG00000275045. [Q13888-1]
Ensembl; ENST00000619997; ENSP00000477954; ENSG00000275045. [Q13888-1]
Ensembl; ENST00000628423; ENSP00000486014; ENSG00000276910. [Q13888-1]
GeneID; 2966; -.
KEGG; hsa:2966; -.
UCSC; uc003kau.6; human. [Q13888-1]
CTD; 2966; -.
DisGeNET; 2966; -.
EuPathDB; HostDB:ENSG00000145736.14; -.
GeneCards; GTF2H2; -.
HGNC; HGNC:4656; GTF2H2.
HPA; HPA047001; -.
MIM; 601748; gene.
neXtProt; NX_Q13888; -.
OpenTargets; ENSG00000145736; -.
PharmGKB; PA29042; -.
eggNOG; KOG2807; Eukaryota.
eggNOG; COG5151; LUCA.
GeneTree; ENSGT00490000043395; -.
HOGENOM; HOG000159415; -.
HOVERGEN; HBG059468; -.
InParanoid; Q13888; -.
KO; K03142; -.
OMA; DCDIFIH; -.
OrthoDB; EOG091G08ZR; -.
PhylomeDB; Q13888; -.
TreeFam; TF314037; -.
Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
Reactome; R-HSA-113418; Formation of the Early Elongation Complex.
Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat.
Reactome; R-HSA-167158; Formation of the HIV-1 Early Elongation Complex.
Reactome; R-HSA-167160; RNA Pol II CTD phosphorylation and interaction with CE during HIV infection.
Reactome; R-HSA-167161; HIV Transcription Initiation.
Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape.
Reactome; R-HSA-167172; Transcription of the HIV genome.
Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat.
Reactome; R-HSA-167246; Tat-mediated elongation of the HIV-1 transcript.
Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
Reactome; R-HSA-5696400; Dual Incision in GG-NER.
Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
Reactome; R-HSA-6782135; Dual incision in TC-NER.
Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
Reactome; R-HSA-72086; mRNA Capping.
Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape.
Reactome; R-HSA-73777; RNA Polymerase I Chain Elongation.
Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
Reactome; R-HSA-73863; RNA Polymerase I Transcription Termination.
Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation.
Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
Reactome; R-HSA-77075; RNA Pol II CTD phosphorylation and interaction with CE.
EvolutionaryTrace; Q13888; -.
GeneWiki; GTF2H2; -.
PRO; PR:Q13888; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000145736; -.
CleanEx; HS_GTF2H2; -.
ExpressionAtlas; Q13888; baseline and differential.
Genevisible; Q13888; HS.
GO; GO:0000438; C:core TFIIH complex portion of holo TFIIH complex; IDA:UniProtKB.
GO; GO:0005675; C:holo TFIIH complex; IDA:UniProtKB.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB.
GO; GO:0003676; F:nucleic acid binding; TAS:ProtInc.
GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; NAS:ProtInc.
GO; GO:0008135; F:translation factor activity, RNA binding; TAS:ProtInc.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006370; P:7-methylguanosine mRNA capping; TAS:Reactome.
GO; GO:0002031; P:G-protein coupled receptor internalization; IMP:UniProtKB.
GO; GO:0070911; P:global genome nucleotide-excision repair; TAS:Reactome.
GO; GO:0006289; P:nucleotide-excision repair; IBA:GO_Central.
GO; GO:0000717; P:nucleotide-excision repair, DNA duplex unwinding; TAS:Reactome.
GO; GO:0033683; P:nucleotide-excision repair, DNA incision; TAS:Reactome.
GO; GO:0006295; P:nucleotide-excision repair, DNA incision, 3'-to lesion; TAS:Reactome.
GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; TAS:Reactome.
GO; GO:0006294; P:nucleotide-excision repair, preincision complex assembly; TAS:Reactome.
GO; GO:0006293; P:nucleotide-excision repair, preincision complex stabilization; TAS:Reactome.
GO; GO:0006468; P:protein phosphorylation; IEA:GOC.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IBA:GO_Central.
GO; GO:0009411; P:response to UV; TAS:ProtInc.
GO; GO:0006363; P:termination of RNA polymerase I transcription; TAS:Reactome.
GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; TAS:Reactome.
GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; TAS:Reactome.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
CDD; cd01453; vWA_transcription_factor_IIH_t; 1.
Gene3D; 3.40.50.410; -; 1.
InterPro; IPR007198; Ssl1-like.
InterPro; IPR004595; TFIIH_C1-like_dom.
InterPro; IPR012170; TFIIH_SSL1/p44.
InterPro; IPR002035; VWF_A.
InterPro; IPR036465; vWFA_dom_sf.
InterPro; IPR013087; Znf_C2H2_type.
PANTHER; PTHR12695; PTHR12695; 1.
Pfam; PF07975; C1_4; 1.
Pfam; PF04056; Ssl1; 1.
PIRSF; PIRSF015919; TFIIH_SSL1; 1.
SMART; SM01047; C1_4; 1.
SMART; SM00327; VWA; 1.
SUPFAM; SSF53300; SSF53300; 1.
TIGRFAMs; TIGR00622; ssl1; 1.
PROSITE; PS50234; VWFA; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Direct protein sequencing; DNA damage; DNA repair; Metal-binding;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Transcription; Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 395 General transcription factor IIH subunit
2.
/FTId=PRO_0000119248.
DOMAIN 60 236 VWFA. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
ZN_FING 291 308 C4-type.
MOD_RES 95 95 Phosphotyrosine.
{ECO:0000250|UniProtKB:A0JN27}.
VARIANT 151 151 I -> M (in dbSNP:rs200357275).
{ECO:0000269|PubMed:9063743}.
/FTId=VAR_011664.
VARIANT 236 236 V -> L (in dbSNP:rs201102513).
{ECO:0000269|PubMed:9063743}.
/FTId=VAR_011665.
MUTAGEN 291 291 C->A: Reconstituted TFIIH complex lacks
p62 and has no transcriptional activity.
{ECO:0000269|PubMed:11319235}.
MUTAGEN 308 308 C->A: Reconstituted TFIIH complex lacks
p62 and has no transcriptional activity.
{ECO:0000269|PubMed:11319235}.
MUTAGEN 345 345 C->A: No effect on the transcriptional
activity of the reconstituted TFIIH
complex. {ECO:0000269|PubMed:11319235}.
MUTAGEN 360 360 C->A: No effect on the transcriptional
activity of the reconstituted TFIIH
complex. {ECO:0000269|PubMed:11319235}.
MUTAGEN 363 363 C->A: No effect on the transcriptional
activity of the reconstituted TFIIH
complex. {ECO:0000269|PubMed:11319235}.
MUTAGEN 376 376 H->A: No effect on the transcriptional
activity of the reconstituted TFIIH
complex. {ECO:0000269|PubMed:11319235}.
MUTAGEN 380 380 H->A: No effect on the transcriptional
activity of the reconstituted TFIIH
complex. {ECO:0000269|PubMed:11319235}.
MUTAGEN 382 382 C->A: No effect on the transcriptional
activity of the reconstituted TFIIH
complex. {ECO:0000269|PubMed:11319235}.
CONFLICT 129 129 T -> S (in Ref. 4). {ECO:0000305}.
STRAND 333 335 {ECO:0000244|PDB:1Z60}.
HELIX 336 339 {ECO:0000244|PDB:1Z60}.
TURN 346 349 {ECO:0000244|PDB:1Z60}.
STRAND 355 358 {ECO:0000244|PDB:1Z60}.
TURN 361 364 {ECO:0000244|PDB:1Z60}.
HELIX 369 373 {ECO:0000244|PDB:1Z60}.
TURN 374 378 {ECO:0000244|PDB:1Z60}.
STRAND 381 383 {ECO:0000244|PDB:1Z60}.
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


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10-288-22005F TFIIH basal transcription factor complex p62 subunit - Basic transcription factor 62 kDa subunit; BTF2-p62; General transcription factor IIH polypeptide 1 0.05 mg
EIAAB42053 C6orf175,General transcription factor IIH polypeptide 5,General transcription factor IIH subunit 5,GTF2H5,Homo sapiens,Human,TFB5 ortholog,TFIIH basal transcription factor complex TTD-A subunit,TTDA
EIAAB42052 D17Wsu155e,General transcription factor IIH polypeptide 5,General transcription factor IIH subunit 5,Gtf2h5,Mouse,Mus musculus,TFB5 ortholog,TFIIH basal transcription factor complex TTD-A subunit
EIAAB42051 Chicken,Gallus gallus,General transcription factor IIH polypeptide 5,General transcription factor IIH subunit 5,GTF2H5,RCJMB04_10n20,TFB5 ortholog,TFIIH basal transcription factor complex TTD-A subuni
EIAAB41099 General transcription factor IIF 74 kDa subunit,General transcription factor IIF subunit 1,GTF2F1,Homo sapiens,Human,RAP74,TFIIF-alpha,Transcription initiation factor IIF subunit alpha,Transcription i
EIAAB42075 C6orf51,CDA020,General transcription factor 3C polypeptide 6,GTF3C6,Homo sapiens,Human,NPD020,TFIIIC 35 kDa subunit,TFIIIC35,Transcription factor IIIC 35 kDa subunit,Transcription factor IIIC subunit
EIAAB42073 CDABP0017,General transcription factor 3C polypeptide 5,GTF3C5,Homo sapiens,Human,TF3C-epsilon,TFIIIC 63 kDa subunit,TFIIIC63,Transcription factor IIIC 63 kDa subunit,Transcription factor IIIC subunit
EIAAB42068 General transcription factor 3C polypeptide 2,GTF3C2,Homo sapiens,Human,KIAA0011,TF3C-beta,TFIIIC 110 kDa subunit,TFIIIC110,Transcription factor IIIC 110 kDa subunit,Transcription factor IIIC subunit


 

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