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
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