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TRANSFAC FACTOR TABLE, Release 2017.2 - public - 2017-06-30, (C) QIAGEN


AC T00814 XX ID T00814 XX DT 20.10.1992 (created); ewi. DT 31.03.2009 (updated); ane. CO Copyright (C), QIAGEN. XX FA TFEA-xbb1 XX SY TFE3-S. XX OS mouse, Mus musculus OC eukaryota; animalia; metazoa; chordata; vertebrata; tetrapoda; mammalia; eutheria; rodentia; myomorpha; muridae; murinae XX GE G006798 Tfe3. XX CL C0012; bHLH-ZIP. XX SZ 411 AA; 44.1 kDa (calc.). XX SQ TSGTRRREQAAAAPFPSPAPASPAISVIGVSAGGHTLSRPPPAQVPREVLKVQTHLENPT SQ RYHLQQARRQQVKQYLSTTLGPKLASQALTPPPGPSSAQPLPAPETAHATGPTGSAPNSP SQ MALLTIGSSSEKELPVSGNLLDVYSSQGVATPAITVSNSCPAELPNIKREISETEAKALL SQ KERQKKDNHNLIERRRRFNINDRIKELGTLIPKSNDPEMRWNKGTILKASVDYIRKLQKE SQ QQRSKDLESRQRSLEQANRSLQLRIQELELQAQIHGLPVPPNPGLLSLTTSSVSDSLKPE SQ QLDIEEEGRPSTTFHVSGGPAQNAPPQQPPAPPSDALLDLHFPSDHLGDLGDPFHLGLED SQ ILMEEEGMVGGLSGGALSPLRAASDPLLSSVSPAVSNASSRRSSFSIEEES XX SC translated from EMBL #S76673 and edited XX FT 182 238 PS50888; HLH. FT 185 238 PF00010; Helix-loop-helix DNA-binding domain. FT 190 243 SM00353; finulus. FT 310 411 C-terminal trans-activation domain [3]. XX FF trans-dominant negative regulator; XX IN T00814 TFEA-xbb1; mouse, Mus musculus. IN T00810 TFEA-xbb2; mouse, Mus musculus. IN T00812 tfeb-isoform1; human, Homo sapiens. XX MX M01034 V$EBOX_Q6_01. MX M03890 V$TFEA_Q6. MX M01029 V$TFE_Q6. XX BS R04253. BS R00844. BS R00853. BS R00240. BS R02252. XX DR TRANSPATH: MO000025189. XX RN [1]; RE0002659. RX PUBMED: 1840705. RA Roman C., Cohn L., Calame K. RT A dominant negative form of transcription activator mTFE3 created by differential splicing RL Science 254:94-97 (1991). RN [2]; RE0003076. RX PUBMED: 1732746. RA Roman C., Matera A. G., Cooper C., Artandi S., Blain S., Ward D. C., Calame K. RT mTFE3, an X-linked transcriptional activator containing basic helix-loop-helix and zipper domains, utilizes the zipper to stabilize both DNA binding and multimerization RL Mol. Cell. Biol. 12:817-827 (1992). RN [3]; RE0006694. RX PUBMED: 7479029. RA Artandi S. E., Merrell K., Avtiahl N., Wong K.-K., Calame K. RT TFE3 contains two activation domains, one acidic and the other proline-rich, that synergistically activate transcription RL Nucleic Acids Res. 23:3865-3871 (1995). XX //