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Transcription initiation factor IIA subunit 1 (General transcription factor IIA subunit 1) (TFIIAL) (Transcription initiation factor TFIIA 42 kDa subunit) (TFIIA-42) [Cleaved into: Transcription initiation factor IIA alpha chain (TFIIA p35 subunit); Transcription initiation factor IIA beta chain (TFIIA p19 subunit)]

 TF2AA_HUMAN             Reviewed;         376 AA.
P52655; Q3KNQ9;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-OCT-2017, entry version 181.
RecName: Full=Transcription initiation factor IIA subunit 1;
AltName: Full=General transcription factor IIA subunit 1;
AltName: Full=TFIIAL;
AltName: Full=Transcription initiation factor TFIIA 42 kDa subunit;
Short=TFIIA-42;
Contains:
RecName: Full=Transcription initiation factor IIA alpha chain;
AltName: Full=TFIIA p35 subunit;
Contains:
RecName: Full=Transcription initiation factor IIA beta chain;
AltName: Full=TFIIA p19 subunit;
Name=GTF2A1; Synonyms=TF2A1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=8224850; DOI=10.1101/gad.7.11.2246;
Ma D., Watanabe H., Mermelstein F., Admon A., Oguri K., Sun X.,
Wada T., Imai T., Shiroya T., Reinberg D., Handa H.;
"Isolation of a cDNA encoding the largest subunit of TFIIA reveals
functions important for activated transcription.";
Genes Dev. 7:2246-2257(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=8224848; DOI=10.1101/gad.7.11.2220;
Dejong J., Roeder R.G.;
"A single cDNA, hTFIIA/alpha, encodes both the p35 and p19 subunits of
human TFIIA.";
Genes Dev. 7:2220-2234(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Watanabe H., Oguri K., Wada T., Imai T., Shiroya T., Handa H.;
Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[6]
FUNCTION, SUBUNIT, AND IDENTIFICATION IN A COMPLEX WITH GTF2A2 AND
TBP.
PubMed=11030333; DOI=10.1016/S1097-2765(00)00052-6;
Mitsiou D.J., Stunnenberg H.G.;
"TAC, a TBP-sans-TAFs complex containing the unprocessed
TFIIAalphabeta precursor and the TFIIAgamma subunit.";
Mol. Cell 6:527-537(2000).
[7]
PHOSPHORYLATION AT SER-280; SER-281; SER-316 AND SER-321, AND
MUTAGENESIS OF SER-280; SER-281; SER-316 AND SER-321.
PubMed=11278496; DOI=10.1074/jbc.M009385200;
Solow S., Salunek M., Ryan R., Lieberman P.M.;
"Taf(II) 250 phosphorylates human transcription factor IIA on serine
residues important for TBP binding and transcription activity.";
J. Biol. Chem. 276:15886-15892(2001).
[8]
PROTEIN SEQUENCE OF 278-289, AND MUTAGENESIS OF VAL-270; GLN-272;
VAL-273; ASP-274; GLY-275; THR-276; GLY-277; ASP-278; SER-280 AND
GLU-282.
PubMed=15257296; DOI=10.1038/sj.emboj.7600304;
Hoiby T., Mitsiou D.J., Zhou H., Erdjument-Bromage H., Tempst P.,
Stunnenberg H.G.;
"Cleavage and proteasome-mediated degradation of the basal
transcription factor TFIIA.";
EMBO J. 23:3083-3091(2004).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316 AND SER-321, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[10]
FUNCTION OF THE GTF2A1 PRECURSOR, AND CLEAVAGE BY TASP1.
PubMed=16537915; DOI=10.1128/MCB.26.7.2728-2735.2006;
Zhou H., Spicuglia S., Hsieh J.J., Mitsiou D.J., Hoiby T.,
Veenstra G.J., Korsmeyer S.J., Stunnenberg H.G.;
"Uncleaved TFIIA is a substrate for taspase 1 and active in
transcription.";
Mol. Cell. Biol. 26:2728-2735(2006).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
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).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
VARIANT [LARGE SCALE ANALYSIS] VAL-30.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: TFIIA is a component of the transcription machinery of
RNA polymerase II and plays an important role in transcriptional
activation. TFIIA in a complex with TBP mediates transcriptional
activity. {ECO:0000269|PubMed:11030333,
ECO:0000269|PubMed:16537915}.
-!- SUBUNIT: TFIIA is a heterodimer of the large unprocessed subunit 1
and a small subunit gamma. It was originally believed to be a
heterotrimer of an alpha (p35), a beta (p19) and a gamma subunit
(p12). TFIIA forms a complex with TBP.
{ECO:0000269|PubMed:11030333}.
-!- INTERACTION:
P52657:GTF2A2; NbExp=8; IntAct=EBI-389518, EBI-1045262;
P23511:NFYA; NbExp=3; IntAct=EBI-389518, EBI-389739;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=42 kDa;
IsoId=P52655-1; Sequence=Displayed;
Name=37 kDa;
IsoId=P52655-2; Sequence=VSP_018798;
-!- PTM: The alpha and beta subunits are postranslationally produced
from the precursor form by TASP1. The cleavage promotes
proteasomal degradation. {ECO:0000269|PubMed:16537915}.
-!- SIMILARITY: Belongs to the TFIIA subunit 1 family. {ECO:0000305}.
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EMBL; X75383; CAA53151.1; -; mRNA.
EMBL; X75383; CAA53152.1; -; mRNA.
EMBL; X77225; CAA54442.1; -; mRNA.
EMBL; D14887; BAA03604.1; -; mRNA.
EMBL; D14886; BAA03603.1; -; mRNA.
EMBL; AC010582; AAF26776.1; -; Genomic_DNA.
EMBL; BC107155; AAI07156.1; -; mRNA.
EMBL; BC107156; AAI07157.1; -; mRNA.
CCDS; CCDS9873.1; -. [P52655-1]
CCDS; CCDS9874.1; -. [P52655-2]
PIR; A49077; A49077.
RefSeq; NP_001265869.1; NM_001278940.1.
RefSeq; NP_056943.1; NM_015859.3. [P52655-1]
RefSeq; NP_963889.1; NM_201595.2. [P52655-2]
UniGene; Hs.592334; -.
PDB; 1NVP; X-ray; 2.10 A; B=2-58, C=303-376.
PDB; 5FUR; EM; 8.50 A; B=9-51, C=330-376.
PDB; 5IY6; EM; 7.20 A; N=1-376.
PDB; 5IY7; EM; 8.60 A; N=1-376.
PDB; 5IY8; EM; 7.90 A; N=1-376.
PDB; 5IY9; EM; 6.30 A; N=1-376.
PDB; 5IYA; EM; 5.40 A; N=1-376.
PDB; 5IYB; EM; 3.90 A; N=1-376.
PDB; 5IYC; EM; 3.90 A; N=1-376.
PDB; 5IYD; EM; 3.90 A; N=1-376.
PDBsum; 1NVP; -.
PDBsum; 5FUR; -.
PDBsum; 5IY6; -.
PDBsum; 5IY7; -.
PDBsum; 5IY8; -.
PDBsum; 5IY9; -.
PDBsum; 5IYA; -.
PDBsum; 5IYB; -.
PDBsum; 5IYC; -.
PDBsum; 5IYD; -.
ProteinModelPortal; P52655; -.
SMR; P52655; -.
BioGrid; 109212; 54.
CORUM; P52655; -.
DIP; DIP-33225N; -.
IntAct; P52655; 14.
STRING; 9606.ENSP00000452454; -.
BindingDB; P52655; -.
ChEMBL; CHEMBL4832; -.
iPTMnet; P52655; -.
PhosphoSitePlus; P52655; -.
BioMuta; GTF2A1; -.
DMDM; 1711663; -.
EPD; P52655; -.
MaxQB; P52655; -.
PaxDb; P52655; -.
PeptideAtlas; P52655; -.
PRIDE; P52655; -.
DNASU; 2957; -.
Ensembl; ENST00000434192; ENSP00000409492; ENSG00000165417. [P52655-2]
Ensembl; ENST00000553612; ENSP00000452454; ENSG00000165417. [P52655-1]
GeneID; 2957; -.
KEGG; hsa:2957; -.
UCSC; uc001xvf.4; human. [P52655-1]
CTD; 2957; -.
DisGeNET; 2957; -.
EuPathDB; HostDB:ENSG00000165417.11; -.
GeneCards; GTF2A1; -.
HGNC; HGNC:4646; GTF2A1.
HPA; HPA000869; -.
MIM; 600520; gene.
neXtProt; NX_P52655; -.
OpenTargets; ENSG00000165417; -.
PharmGKB; PA29033; -.
eggNOG; ENOG410IPCF; Eukaryota.
eggNOG; ENOG4111M8K; LUCA.
GeneTree; ENSGT00900000141061; -.
HOGENOM; HOG000015236; -.
HOVERGEN; HBG052771; -.
InParanoid; P52655; -.
KO; K03122; -.
OMA; MLCTYDK; -.
OrthoDB; EOG091G0GC2; -.
PhylomeDB; P52655; -.
TreeFam; TF350445; -.
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-674695; RNA Polymerase II Pre-transcription Events.
Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape.
Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation.
Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
SIGNOR; P52655; -.
ChiTaRS; GTF2A1; human.
EvolutionaryTrace; P52655; -.
GeneWiki; GTF2A1; -.
GenomeRNAi; 2957; -.
PMAP-CutDB; P52655; -.
PRO; PR:P52655; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000165417; -.
ExpressionAtlas; P52655; baseline and differential.
Genevisible; P52655; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005672; C:transcription factor TFIIA complex; IDA:BHF-UCL.
GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:BHF-UCL.
GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; IEA:Ensembl.
GO; GO:0017025; F:TBP-class protein binding; IPI:BHF-UCL.
GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
GO; GO:0008134; F:transcription factor binding; IPI:BHF-UCL.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0042795; P:snRNA transcription from RNA polymerase II 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:BHF-UCL.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
CDD; cd07976; TFIIA_alpha_beta_like; 2.
Gene3D; 2.30.18.10; -; 1.
InterPro; IPR009083; TFIIA_a-hlx.
InterPro; IPR004855; TFIIA_asu/bsu.
InterPro; IPR009088; TFIIA_b-brl.
Pfam; PF03153; TFIIA; 2.
SMART; SM01371; TFIIA; 1.
SUPFAM; SSF47396; SSF47396; 1.
SUPFAM; SSF50784; SSF50784; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative initiation; Complete proteome;
Direct protein sequencing; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Transcription; Transcription regulation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
CHAIN 2 376 Transcription initiation factor IIA
subunit 1.
/FTId=PRO_0000022481.
CHAIN 2 274 Transcription initiation factor IIA alpha
chain.
/FTId=PRO_0000042593.
CHAIN 275 376 Transcription initiation factor IIA beta
chain.
/FTId=PRO_0000042594.
COMPBIAS 71 80 Poly-Gln.
COMPBIAS 81 87 Poly-His.
SITE 274 275 Cleavage; by TASP1.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
MOD_RES 280 280 Phosphoserine; by TAF1.
{ECO:0000269|PubMed:11278496}.
MOD_RES 281 281 Phosphoserine; by TAF1.
{ECO:0000269|PubMed:11278496}.
MOD_RES 316 316 Phosphoserine; by TAF1.
{ECO:0000244|PubMed:17081983,
ECO:0000269|PubMed:11278496}.
MOD_RES 321 321 Phosphoserine; by TAF1.
{ECO:0000244|PubMed:17081983,
ECO:0000269|PubMed:11278496}.
VAR_SEQ 1 39 Missing (in isoform 37 kDa).
{ECO:0000305}.
/FTId=VSP_018798.
VARIANT 30 30 L -> V (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035667.
VARIANT 109 109 A -> P (in dbSNP:rs17111579).
/FTId=VAR_054043.
MUTAGEN 270 270 V->A: Slightly affects cleavage and
yields elevated levels of the precursor.
{ECO:0000269|PubMed:15257296}.
MUTAGEN 272 272 Q->A: Abolishes cleavage.
{ECO:0000269|PubMed:15257296}.
MUTAGEN 273 273 V->A: Abolishes cleavage.
{ECO:0000269|PubMed:15257296}.
MUTAGEN 274 274 D->A: Abolishes cleavage.
{ECO:0000269|PubMed:15257296}.
MUTAGEN 275 275 G->A: Abolishes cleavage.
{ECO:0000269|PubMed:15257296}.
MUTAGEN 276 276 T->A: Does not affect cleavage.
{ECO:0000269|PubMed:15257296}.
MUTAGEN 277 277 G->A: Does not affect cleavage.
{ECO:0000269|PubMed:15257296}.
MUTAGEN 278 278 D->A: Significant reduction of cleavage.
{ECO:0000269|PubMed:15257296}.
MUTAGEN 280 280 S->A: Slightly affects cleavage, yields
elevated levels of the precursor.
Eliminates phosphorylation; when
associated with A-281; A-316 and A-321.
{ECO:0000269|PubMed:11278496,
ECO:0000269|PubMed:15257296}.
MUTAGEN 281 281 S->A: Eliminates phosphorylation; when
associated with A-280; A-316 and A-321.
{ECO:0000269|PubMed:11278496}.
MUTAGEN 282 282 E->A: Slightly affects cleavage and
yields elevated levels of the precursor.
{ECO:0000269|PubMed:15257296}.
MUTAGEN 316 316 S->A: Strongly reduces phosphorylation;
when associated with A-321. Eliminates
phosphorylation; when associated with A-
280; A-281 and A-321.
{ECO:0000269|PubMed:11278496}.
MUTAGEN 321 321 S->A: Strongly reduces phosphorylation;
when associated with A-316. Eliminates
phosphorylation; when associated with A-
280; A-281 and A-316.
{ECO:0000269|PubMed:11278496}.
HELIX 10 32 {ECO:0000244|PDB:1NVP}.
HELIX 36 50 {ECO:0000244|PDB:1NVP}.
STRAND 334 345 {ECO:0000244|PDB:1NVP}.
STRAND 348 360 {ECO:0000244|PDB:1NVP}.
STRAND 363 375 {ECO:0000244|PDB:1NVP}.
SEQUENCE 376 AA; 41514 MW; 4BAE1853E7E89218 CRC64;
MANSANTNTV PKLYRSVIED VINDVRDIFL DDGVDEQVLM ELKTLWENKL MQSRAVDGFH
SEEQQLLLQV QQQHQPQQQQ HHHHHHHQQA QPQQTVPQQA QTQQVLIPAS QQATAPQVIV
PDSKLIQHMN ASNMSAAATA ATLALPAGVT PVQQILTNSG QLLQVVRAAN GAQYIFQPQQ
SVVLQQQVIP QMQPGGVQAP VIQQVLAPLP GGISPQTGVI IQPQQILFTG NKTQVIPTTV
AAPTPAQAQI TATGQQQPQA QPAQTQAPLV LQVDGTGDTS SEEDEDEEED YDDDEEEDKE
KDGAEDGQVE EEPLNSEDDV SDEEGQELFD TENVVVCQYD KIHRSKNKWK FHLKDGIMNL
NGRDYIFSKA IGDAEW


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EIAAB41093 General transcription factor IIE 56 kDa subunit,General transcription factor IIE subunit 1,Gtf2e1,Mouse,Mus musculus,TFIIE-alpha,Transcription initiation factor IIE subunit alpha
EIAAB41323 DN-7,Homo sapiens,Human,Neuronal cell death-related protein 7,TAF9B,TAF9L,Transcription initiation factor TFIID subunit 9B,Transcription initiation factor TFIID subunit 9-like,Transcription-associated
EIAAB41105 ATP-dependent helicase GTF2F2,General transcription factor IIF 30 kDa subunit,General transcription factor IIF subunit 2,GTF2F2,Homo sapiens,Human,RAP30,TFIIF-beta,Transcription initiation factor IIF
EIAAB41272 Homo sapiens,Human,PRO2134,TAF(II)28,TAF11,TAF2I,TAFII28,TAFII-28,TFIID subunit p30-beta,Transcription initiation factor TFIID 28 kDa subunit,Transcription initiation factor TFIID subunit 11
EIAAB41324 Mouse,Mus musculus,Taf9b,Taf9l,Transcription initiation factor TFIID subunit 9B,Transcription initiation factor TFIID subunit 9-like,Transcription-associated factor TAFII31L
EIAAB41310 Homo sapiens,Human,RNA polymerase II TBP-associated factor subunit F,TAF(II)55,TAF2F,TAF7,TAFII55,TAFII55,TAFII-55,Transcription initiation factor TFIID 55 kDa subunit,Transcription initiation factor
EIAAB41322 Mouse,Mus musculus,RNA polymerase II TBP-associated factor subunit G,Taf2g,Taf9,TAFII31,TAFII-31,TAFII32,TAFII-32,Transcription initiation factor TFIID 31 kDa subunit,Transcription initiation factor T
EIAAB41271 Mouse,Mus musculus,TAF(II)28,Taf11,TAFII28,TAFII-28,TFIID subunit p30-beta,Transcription initiation factor TFIID 28 kDa subunit,Transcription initiation factor TFIID subunit 11
EIAAB41273 Rat,Rattus norvegicus,TAF(II)28,Taf11,TAFII28,TAFII-28,TFIID subunit p30-beta,Transcription initiation factor TFIID 28 kDa subunit,Transcription initiation factor TFIID subunit 11
EIAAB41312 Mouse,Mus musculus,RNA polymerase II TBP-associated factor subunit F,TAF(II)55,Taf2f,Taf7,TAFII55,TAFII-55,Transcription initiation factor TFIID 55 kDa subunit,Transcription initiation factor TFIID su
EIAAB41325 Dn7,DN-7,Neuronal cell death-related gene in neuron 7,Rat,Rattus norvegicus,Taf9b,Taf9l,Transcription initiation factor TFIID subunit 9B,Transcription initiation factor TFIID subunit 9-like,Transcript
EIAAB41096 General transcription factor IIE subunit 2,GTF2E2,Homo sapiens,Human,TF2E2,TFIIE-beta,Transcription initiation factor IIE subunit beta


 

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