ID   T2EB_MOUSE              Reviewed;         292 AA.
AC   Q9D902; Q3U5Y7; Q8BTZ2; Q8VE14;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 2.
DT   27-MAR-2024, entry version 156.
DE   RecName: Full=General transcription factor IIE subunit 2;
DE   AltName: Full=Transcription initiation factor IIE subunit beta;
DE            Short=TFIIE-beta;
GN   Name=Gtf2e2;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Bone marrow, Pancreas, Thymus, and Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary gland;
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung, and 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).
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-75, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- FUNCTION: Recruits TFIIH to the initiation complex and stimulates the
CC       RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase
CC       activities of TFIIH. Both TFIIH and TFIIE are required for promoter
CC       clearance by RNA polymerase. {ECO:0000250|UniProtKB:P29084}.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains. Interacts with FACT
CC       subunit SUPT16H. Interacts with ATF7IP. Interacts with SND1. Part of
CC       TBP-based Pol II pre-initiation complex (PIC), in which Pol II core
CC       assembles with general transcription factors and other specific
CC       initiation factors including GTF2E1, GTF2E2, GTF2F1, GTF2F2, TCEA1,
CC       ERCC2, ERCC3, GTF2H2, GTF2H3, GTF2H4, GTF2H5, GTF2A1, GTF2A2, GTF2B and
CC       TBP; this large multi-subunit PIC complex mediates DNA unwinding and
CC       targets Pol II core to the transcription start site where the first
CC       phosphodiester bond forms. {ECO:0000250|UniProtKB:P29084}.
CC   -!- INTERACTION:
CC       Q9D902; Q7TNS8: Epop; NbExp=2; IntAct=EBI-309435, EBI-16024836;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P29084}.
CC   -!- SIMILARITY: Belongs to the TFIIE beta subunit family. {ECO:0000305}.
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DR   EMBL; AK007492; BAB25066.1; -; mRNA.
DR   EMBL; AK088342; BAC40294.1; -; mRNA.
DR   EMBL; AK150415; BAE29539.1; -; mRNA.
DR   EMBL; AK153370; BAE31938.1; -; mRNA.
DR   EMBL; AK158783; BAE34662.1; -; mRNA.
DR   EMBL; BC020016; AAH20016.1; -; mRNA.
DR   CCDS; CCDS22236.1; -.
DR   RefSeq; NP_001161393.1; NM_001167921.1.
DR   RefSeq; NP_001161394.1; NM_001167922.1.
DR   RefSeq; NP_080860.3; NM_026584.3.
DR   RefSeq; XP_006509249.1; XM_006509186.1.
DR   RefSeq; XP_006509250.1; XM_006509187.1.
DR   RefSeq; XP_006509251.1; XM_006509188.3.
DR   AlphaFoldDB; Q9D902; -.
DR   SMR; Q9D902; -.
DR   BioGRID; 212686; 22.
DR   DIP; DIP-49546N; -.
DR   IntAct; Q9D902; 22.
DR   MINT; Q9D902; -.
DR   STRING; 10090.ENSMUSP00000132287; -.
DR   iPTMnet; Q9D902; -.
DR   PhosphoSitePlus; Q9D902; -.
DR   SwissPalm; Q9D902; -.
DR   EPD; Q9D902; -.
DR   MaxQB; Q9D902; -.
DR   PaxDb; 10090-ENSMUSP00000126284; -.
DR   PeptideAtlas; Q9D902; -.
DR   ProteomicsDB; 263200; -.
DR   Pumba; Q9D902; -.
DR   Antibodypedia; 4040; 317 antibodies from 32 providers.
DR   DNASU; 68153; -.
DR   Ensembl; ENSMUST00000167264.8; ENSMUSP00000129834.2; ENSMUSG00000031585.14.
DR   Ensembl; ENSMUST00000170705.8; ENSMUSP00000126284.2; ENSMUSG00000031585.14.
DR   Ensembl; ENSMUST00000171010.8; ENSMUSP00000132287.2; ENSMUSG00000031585.14.
DR   GeneID; 68153; -.
DR   KEGG; mmu:68153; -.
DR   UCSC; uc009lkh.2; mouse.
DR   AGR; MGI:1915403; -.
DR   CTD; 2961; -.
DR   MGI; MGI:1915403; Gtf2e2.
DR   VEuPathDB; HostDB:ENSMUSG00000031585; -.
DR   eggNOG; KOG3095; Eukaryota.
DR   GeneTree; ENSGT00390000011749; -.
DR   HOGENOM; CLU_086770_0_0_1; -.
DR   InParanoid; Q9D902; -.
DR   OMA; HMKARHQ; -.
DR   OrthoDB; 3061109at2759; -.
DR   PhylomeDB; Q9D902; -.
DR   TreeFam; TF105901; -.
DR   Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
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-75953; RNA Polymerase II Transcription Initiation.
DR   Reactome; R-MMU-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR   BioGRID-ORCS; 68153; 21 hits in 77 CRISPR screens.
DR   ChiTaRS; Gtf2e2; mouse.
DR   PRO; PR:Q9D902; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q9D902; Protein.
DR   Bgee; ENSMUSG00000031585; Expressed in otic placode and 265 other cell types or tissues.
DR   ExpressionAtlas; Q9D902; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005669; C:transcription factor TFIID complex; ISO:MGI.
DR   GO; GO:0005673; C:transcription factor TFIIE complex; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; ISO:MGI.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IBA:GO_Central.
DR   CDD; cd07977; TFIIE_beta_winged_helix; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR040501; TFA2_Winged_2.
DR   InterPro; IPR016656; TFIIE-bsu.
DR   InterPro; IPR003166; TFIIE_bsu_DNA-bd.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR12716:SF8; TRANSCRIPTION INITIATION FACTOR IIE SUBUNIT BETA; 1.
DR   PANTHER; PTHR12716; TRANSCRIPTION INITIATION FACTOR IIE, BETA SUBUNIT; 1.
DR   Pfam; PF18121; TFA2_Winged_2; 1.
DR   Pfam; PF02186; TFIIE_beta; 1.
DR   PIRSF; PIRSF016398; TFIIE-beta; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS51351; TFIIE_BETA_C; 1.
DR   Genevisible; Q9D902; MM.
PE   1: Evidence at protein level;
KW   Acetylation; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..292
FT                   /note="General transcription factor IIE subunit 2"
FT                   /id="PRO_0000211227"
FT   DNA_BIND        67..147
FT                   /note="TFIIE beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00682"
FT   REGION          17..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..274
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P29084"
FT   MOD_RES         62
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P29084"
FT   MOD_RES         75
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   CONFLICT        20
FT                   /note="P -> L (in Ref. 1; BAB25066)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        80
FT                   /note="A -> S (in Ref. 1; BAB25066)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   292 AA;  33047 MW;  4D74B98C7ACBA60B CRC64;
     MDPSLLRDRE LFKKRALSTP VVEKRAVPSE SPSSSSSKKK KAKVEHGGSS GSKQNSDHNN
     GSFNLKALSG SSGYKFGVLA KIVNYMKTRH QRGDTHPLTL EEILDETQHL DIGLKQKQWL
     MTEALVNNPK IEVVDGKYAF KPKYNLKDKK ALLRLLDNHD QRGLGGILLE DIEEGLPNSQ
     KAVKALGDQI LFVSRPDKKK ILFFNDKSCQ FSVDEEFQKL WRSVTVDSMD EEKIEEYLKR
     QGISSMQESG PKKVASIQRR KKPASQKKRR FKTHNEHLAG VLKDYSDITP GK
//