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

AC T00291 XX ID T00291 XX DT 15.10.1992 (created); ewi. DT 27.01.2012 (updated); pch. CO Copyright (C), QIAGEN. XX FA FosB XX SY Fos-B. XX OS mouse, Mus musculus OC eukaryota; animalia; metazoa; chordata; vertebrata; tetrapoda; mammalia; eutheria; rodentia; myomorpha; muridae; murinae XX GE G000509 Fosb. XX CL C0008; bZIP. XX SZ 338 AA; 36.0 kDa (cDNA) (calc.), 40 kDa (SDS) XX SQ MFQAFPGDYDSGSRCSSSPSAESQYLSSVDSFGSPPTAAASQECAGLGEMPGSFVPTVTA SQ ITTSQDLQWLVQPTLISSMAQSQGQPLASQPPAVDPYDMPGTSYSTPGLSAYSTGGASGS SQ GGPSTSTTTSGPVSARPARARPRRPREETLTPEEEEKRRVRRERNKLAAAKCRNRRRELT SQ DRLQAETDQLEEEKAELESEIAELQKEKERLEFVLVAHKPGCKIPYEEGPGPGPLAEVRD SQ LPGSTSAKEDGFGWLLPPPPPPPLPFQSSRDAPPNLTASLFTHSEVQVLGDPFPVVSPSY SQ TSSFVLTCPEVSAFAGAQRTSGSEQPSDPLNSPSLLAL XX SC Swiss-Prot#P13346 XX FT 54 78 N-terminal trans-activation domain (N-TA) [10]. FT 153 217 SM00338; brlzneu. FT 154 207 PF07716; Basic region leucine zipper. FT 155 218 PS50217; BZIP. FT 243 282 proline-rich trans-activation domain [11]. FT 284 338 TBP-binding [11]. FT 304 310 TBP-binding motif (TBM) [11]. XX SF no homodimerization, but heterodimerization with Jun family members; SF C-terminal half is responsible for transforming activity [4]; SF splice variant: deltaFosB T02198 [5] [6] [7] [9] [12]; SF N-terminal sequences which are conserved among Fos-family members augment trans-activation and are required for transformation as well [8]; XX FF activator, even stronger transformation property than c-Fos [4]; FF main function during Go-G1 transition [3]; FF represses c-fos expression [5]; XX IN T00131 c-Jun; mouse, Mus musculus. IN T00132 c-Jun; rat, Rattus norvegicus. IN T00133 c-Jun; human, Homo sapiens. IN T00134 c-Jun; chick, Gallus gallus. IN T00135 c-Jun; hamster, Cricetulus sp. IN T09366 foxl2; mouse, Mus musculus. IN T00436 JunB; mouse, Mus musculus. IN T00437 JunD; mouse, Mus musculus. IN T00796 TBP; mouse, Mus musculus. XX MX M00517 V$AP1_01. MX M00924 V$AP1_Q2_01. MX M00926 V$AP1_Q4_01. MX M00925 V$AP1_Q6_01. XX BS R05052. XX DR TRANSPATH: MO000024840. DR EMBL: AF093624; AF093624. DR EMBL: M77748; DR EMBL: X14897; DR UniProtKB: P13346; XX RN [1]; RE0000421. RX PUBMED: 2498083. RA Zerial M., Toschi L., Ryseck R.-P., Schuermann M., Mueller R., Bravo R. RT The product of a novel growth factor activated gene, fos B, interacts with JUN proteins enhancing their DNA binding activity RL EMBO J. 8:805-813 (1989). RN [2]; RE0004817. RX PUBMED: 7504176. RA Wisdom R., Verma I. M. RT Transformation by Fos proteins requires a C-terminal transactivation domain RL Mol. Cell. Biol. 13:7429-7438 (1993). RN [3]; RE0004865. RX PUBMED: 1406676. RA Kovary K., Bravo R. RT Existence of different Fos/Jun complexes during the G0-to-G1 transition and during exponential growth in mouse fibroblasts: differential role of Fos proteins RL Mol. Cell. Biol. 12:5015-5023 (1992). RN [4]; RE0004880. RX PUBMED: 1903195. RA Schuermann M., Jooss K., Mueller R. RT fosB is a transforming gene encoding a transcriptional activator RL Oncogene 6:567-576 (1991). RN [5]; RE0004881. RX PUBMED: 1922060. RA Dobrazanski P., Noguchi T., Kovary K., Rizzo C. A., Lazo P. S., Bravo R. RT Both products of the fosB gene, FosB and its short form, FosB/SF, are transcriptional activators in fibroblasts RL Mol. Cell. Biol. 11:5470-5478 (1991). RN [6]; RE0004882. RX PUBMED: 1900040. RA Nakabeppu Y., Nathans D. RT A naturally occurring truncated form of FosB that inhibits Fos/Jun transcriptional activity RL Cell 64:751-759 (1991). RN [7]; RE0004883. RX PUBMED: 1905017. RA Yen J., Wisdom R. M., Tratner I., Verma I. M. RT An alternative spliced form of FosB is a negative regulator of transcriptional activation and transformation by Fos proteins RL Proc. Natl. Acad. Sci. USA 88:5077-5081 (1991). RN [8]; RE0004884. RX PUBMED: 8474434. RA Wisdom R., Verma I. M. RT Proto-oncogene FosB: the amino terminus encodes a regulatory function required for transformation RL Mol. Cell. Biol. 13:2635-2643 (1993). RN [9]; RE0004885. RX PUBMED: 8321220. RA Nakabeppu Y., Oda S., Sekiguchi M. RT Proliferative activation of quiescent Rat-1A cells by deltaFosB RL Mol. Cell. Biol. 13:4157-4166 (1993). RN [10]; RE0004887. RX PUBMED: 8137828. RA Jooss K. U., Funk M., Mueller R. RT An autonomous N-terminal transactivation domain in Fos protein plays a crucial role in transformation RL EMBO J. 13:1467-1475 (1994). RN [11]; RE0004888. RX PUBMED: 8070410. RA Metz R., Kouzarides T., Bravo R. RT A C-terminal domain in FosB, absent in FosB/SF and Fra-1, which is able to interact with the TATA binding protein, is required for altered cell growth RL EMBO J. 13:3832-3842 (1994). RN [12]; RE0004889. RX PUBMED: 1648531. RA Mumberg D., Lucibello F. C., Schuermann M., Mueller R. RT Alternative splicing of fosB transcripts results in differentially expressed mRNAs encoding functionally antagonistic proteins RL Genes Dev. 5:1212-1223 (1991). RN [13]; RE0004890. RX PUBMED: 1373118. RA Wisdom R., Verma I. M. RT Transformation by FosB requires a trans-activation domain missing in FosB2 that can be substituted by heterologous activation domains RL Genes Dev. 6:667-675 (1992). XX //