T2EB_MOUSE
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 03-AUG-2022, entry version 147.
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 (By similarity).
CC {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.
CC {ECO:0000250|UniProtKB:P29084}.
CC -!- INTERACTION:
CC Q9D902; Q7TNS8: Epop; NbExp=2; IntAct=EBI-309435, EBI-16024836;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00682}.
CC -!- SIMILARITY: Belongs to the TFIIE beta subunit family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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.ENSMUSP00000126284; -.
DR iPTMnet; Q9D902; -.
DR PhosphoSitePlus; Q9D902; -.
DR EPD; Q9D902; -.
DR MaxQB; Q9D902; -.
DR PaxDb; Q9D902; -.
DR PeptideAtlas; Q9D902; -.
DR PRIDE; Q9D902; -.
DR ProteomicsDB; 263200; -.
DR Antibodypedia; 4040; 289 antibodies from 32 providers.
DR DNASU; 68153; -.
DR Ensembl; ENSMUST00000167264; ENSMUSP00000129834; ENSMUSG00000031585.
DR Ensembl; ENSMUST00000170705; ENSMUSP00000126284; ENSMUSG00000031585.
DR Ensembl; ENSMUST00000171010; ENSMUSP00000132287; ENSMUSG00000031585.
DR GeneID; 68153; -.
DR KEGG; mmu:68153; -.
DR UCSC; uc009lkh.2; mouse.
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; NTDHSNG; -.
DR OrthoDB; 1160863at2759; -.
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 72 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 262 other tissues.
DR ExpressionAtlas; Q9D902; baseline and differential.
DR Genevisible; Q9D902; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; 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 from RNA polymerase II promoter; IBA:GO_Central.
DR CDD; cd07977; TFIIE_beta_winged_helix; 1.
DR Gene3D; 1.10.10.10; -; 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; PTHR12716; 1.
DR Pfam; PF18121; TFA2_Winged_2; 1.
DR Pfam; PF02186; TFIIE_beta; 1.
DR PIRSF; PIRSF016398; TFIIE-beta; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS51351; TFIIE_BETA_C; 1.
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
