ID FOSB_MOUSE Reviewed; 338 AA. AC P13346; A0A140LIE4; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 24-JAN-2024, entry version 173. DE RecName: Full=Protein FosB {ECO:0000305}; DE AltName: Full=FBJ osteosarcoma oncogene B {ECO:0000312|MGI:MGI:95575}; DE AltName: Full=Transcription factor AP-1 subunit FosB {ECO:0000305}; GN Name=Fosb {ECO:0000312|MGI:MGI:95575}; 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 [MRNA] (ISOFORM 1), FUNCTION, IDENTIFICATION IN AN AP-1 RP COMPLEX, SUBUNIT, INTERACTION WITH JUN AND JUNB, SUBCELLULAR LOCATION, AND RP INDUCTION BY GROWTH FACTORS. RX PubMed=2498083; DOI=10.1002/j.1460-2075.1989.tb03441.x; 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 RT JUN proteins enhancing their DNA binding activity."; RL EMBO J. 8:805-813(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1741260; DOI=10.1093/nar/20.2.343; RA Lazo P.S., Dorfman K., Noguchi T., Mattei M.-G., Bravo R.; RT "Structure and mapping of the fosB gene. FosB downregulates the activity of RT the fosB promoter."; RL Nucleic Acids Res. 20:343-350(1992). RN [3] {ECO:0000312|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP FUNCTION, AND SUBUNIT. RX PubMed=1900040; DOI=10.1016/0092-8674(91)90504-r; RA Nakabeppu Y., Nathans D.; RT "A naturally occurring truncated form of FosB that inhibits Fos/Jun RT transcriptional activity."; RL Cell 64:751-759(1991). RN [5] RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE. RX PubMed=8706134; DOI=10.1016/s0092-8674(00)80101-4; RA Brown J.R., Ye H., Bronson R.T., Dikkes P., Greenberg M.E.; RT "A defect in nurturing in mice lacking the immediate early gene fosB."; RL Cell 86:297-309(1996). RN [6] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY COCAINE, RP AND DISRUPTION PHENOTYPE. RX PubMed=9294222; DOI=10.1073/pnas.94.19.10397; RA Hiroi N., Brown J.R., Haile C.N., Ye H., Greenberg M.E., Nestler E.J.; RT "FosB mutant mice: loss of chronic cocaine induction of Fos-related RT proteins and heightened sensitivity to cocaine's psychomotor and rewarding RT effects."; RL Proc. Natl. Acad. Sci. U.S.A. 94:10397-10402(1997). RN [7] RP FUNCTION, PHOSPHORYLATION AT SER-27, AND MUTAGENESIS OF SER-27. RX PubMed=16687504; DOI=10.1523/jneurosci.4970-05.2006; RA Ulery P.G., Rudenko G., Nestler E.J.; RT "Regulation of DeltaFosB stability by phosphorylation."; RL J. Neurosci. 26:5131-5142(2006). RN [8] RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-27. RX PubMed=17241283; DOI=10.1111/j.1460-9568.2006.05262.x; RA Ulery P.G., Nestler E.J.; RT "Regulation of DeltaFosB transcriptional activity by Ser27 RT phosphorylation."; RL Eur. J. Neurosci. 25:224-230(2007). RN [9] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=18407360; DOI=10.1016/j.bbr.2008.02.040; RA Solecki W., Krowka T., Kubik J., Kaczmarek L., Przewlocki R.; RT "Role of fosB in behaviours related to morphine reward and spatial RT memory."; RL Behav. Brain Res. 190:212-217(2008). RN [10] RP TISSUE SPECIFICITY, AND INDUCTION BY CHRONIC SOCIAL DEFEAT STRESS. RX PubMed=20473292; DOI=10.1038/nn.2551; RA Vialou V., Robison A.J., Laplant Q.C., Covington H.E. III, Dietz D.M., RA Ohnishi Y.N., Mouzon E., Rush A.J. III, Watts E.L., Wallace D.L., RA Iniguez S.D., Ohnishi Y.H., Steiner M.A., Warren B.L., Krishnan V., RA Bolanos C.A., Neve R.L., Ghose S., Berton O., Tamminga C.A., Nestler E.J.; RT "DeltaFosB in brain reward circuits mediates resilience to stress and RT antidepressant responses."; RL Nat. Neurosci. 13:745-752(2010). RN [11] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY KAINIC RP ACID, AND DISRUPTION PHENOTYPE. RX PubMed=23303048; DOI=10.1038/npp.2012.260; RA Yutsudo N., Kamada T., Kajitani K., Nomaru H., Katogi A., Ohnishi Y.H., RA Ohnishi Y.N., Takase K., Sakumi K., Shigeto H., Nakabeppu Y.; RT "fosB-null mice display impaired adult hippocampal neurogenesis and RT spontaneous epilepsy with depressive behavior."; RL Neuropsychopharmacology 38:895-906(2013). RN [12] RP FUNCTION (ISOFORM 2). RX PubMed=23319622; DOI=10.1073/pnas.1221742110; RA Grueter B.A., Robison A.J., Neve R.L., Nestler E.J., Malenka R.C.; RT "DeltaFosB differentially modulates nucleus accumbens direct and indirect RT pathway function."; RL Proc. Natl. Acad. Sci. U.S.A. 110:1923-1928(2013). RN [13] RP TISSUE SPECIFICITY, AND INDUCTION BY NOVELTY EXPOSURE. RX PubMed=26446228; DOI=10.1523/jneurosci.2083-15.2015; RA Eagle A.L., Gajewski P.A., Yang M., Kechner M.E., Al Masraf B.S., RA Kennedy P.J., Wang H., Mazei-Robison M.S., Robison A.J.; RT "Experience-Dependent Induction of Hippocampal DeltaFosB Controls RT Learning."; RL J. Neurosci. 35:13773-13783(2015). RN [14] RP FUNCTION, AND INTERACTION WITH SMARCB1; SMARCD1; ARID1A AND JUN. RX PubMed=29272704; DOI=10.1016/j.molcel.2017.11.026; RA Vierbuchen T., Ling E., Cowley C.J., Couch C.H., Wang X., Harmin D.A., RA Roberts C.W.M., Greenberg M.E.; RT "AP-1 Transcription Factors and the BAF Complex Mediate Signal-Dependent RT Enhancer Selection."; RL Mol. Cell 68:1067-1082.e12(2017). RN [15] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION RP PHENOTYPE. RX PubMed=30902680; DOI=10.1016/j.neuroscience.2019.03.022; RA Manning C.E., Eagle A.L., Kwiatkowski C.C., Achargui R., Woodworth H., RA Potter E., Ohnishi Y., Leinninger G.M., Robison A.J.; RT "Hippocampal Subgranular Zone FosB Expression Is Critical for Neurogenesis RT and Learning."; RL Neuroscience 406:225-233(2019). CC -!- FUNCTION: Heterodimerizes with proteins of the JUN family to form an CC AP-1 transcription factor complex, thereby enhancing their DNA binding CC activity to gene promoters containing an AP-1 consensus sequence 5'- CC TGA[GC]TCA-3' and enhancing their transcriptional activity CC (PubMed:2498083, PubMed:1900040). As part of the AP-1 complex, CC facilitates enhancer selection together with cell-type-specific CC transcription factors by collaboratively binding to nucleosomal CC enhancers and recruiting the SWI/SNF (BAF) chromatin remodeling complex CC to establish accessible chromatin (PubMed:29272704). Together with JUN, CC plays a role in activation-induced cell death of T cells by binding to CC the AP-1 promoter site of FASLG/CD95L, and inducing its transcription CC in response to activation of the TCR/CD3 signaling pathway (By CC similarity). Exhibits transactivation activity in vitro CC (PubMed:17241283). Involved in the display of nurturing behavior CC towards newborns (PubMed:8706134). May play a role in neurogenesis in CC the hippocampus and in learning and memory-related tasks by regulating CC the expression of various genes involved in neurogenesis, depression CC and epilepsy (PubMed:23303048, PubMed:30902680). Implicated in CC behavioral responses related to morphine reward and spatial memory CC (PubMed:9294222, PubMed:18407360). {ECO:0000250|UniProtKB:P53539, CC ECO:0000269|PubMed:17241283, ECO:0000269|PubMed:18407360, CC ECO:0000269|PubMed:1900040, ECO:0000269|PubMed:23303048, CC ECO:0000269|PubMed:2498083, ECO:0000269|PubMed:29272704, CC ECO:0000269|PubMed:30902680, ECO:0000269|PubMed:8706134, CC ECO:0000269|PubMed:9294222}. CC -!- FUNCTION: [Isoform 2]: Exhibits lower transactivation activity than CC isoform 1 in vitro (PubMed:17241283). The heterodimer with JUN does not CC display any transcriptional activity, and may thereby act as an CC transcriptional inhibitor (PubMed:1900040). May be involved in the CC regulation of neurogenesis in the hippocampus (PubMed:23303048). May CC play a role in synaptic modifications in nucleus accumbens medium spiny CC neurons and thereby play a role in adaptive and pathological reward- CC dependent learning, including maladaptive responses involved in drug CC addiction (PubMed:23319622). Seems to be more stably expressed with a CC half-life of ~9.5 hours in cell culture as compared to 1.5 hours half- CC life of isoform 1 (PubMed:18407360). {ECO:0000269|PubMed:17241283, CC ECO:0000269|PubMed:18407360, ECO:0000269|PubMed:1900040, CC ECO:0000269|PubMed:23303048, ECO:0000269|PubMed:23319622}. CC -!- SUBUNIT: Heterodimer; binds to DNA as heterodimer (PubMed:2498083, CC PubMed:1900040). Component of an AP-1 transcription factor complex; CC composed of FOS-JUN heterodimers (PubMed:2498083, PubMed:1900040). As CC part of the AP-1 transcription factor complex, forms heterodimers with CC JUN, JUNB or JUND, thereby binding to the AP-1 consensus sequence and CC stimulating transcription (PubMed:2498083, PubMed:1900040). Interacts CC with the BAF multiprotein chromatin-remodeling complex subunits SMARCB1 CC and SMARCD1 (PubMed:29272704). Interacts with ARID1A and JUN CC (PubMed:29272704). {ECO:0000269|PubMed:1900040, CC ECO:0000269|PubMed:2498083, ECO:0000269|PubMed:29272704}. CC -!- SUBUNIT: [Isoform 2]: Homodimer under oxidizing conditions and monomer CC under reducing conditions (in vitro) (By similarity). Heterodimer; CC binds to DNA as heterodimer (PubMed:1900040). Forms heterodimers with CC JUNB, JUN or JUND; thereby binding to the AP-1 consensus sequence but CC does not stimulate transcription (PubMed:1900040). Forms heterodimers CC with JUND under oxidizing conditions (By similarity). CC {ECO:0000250|UniProtKB:P53539, ECO:0000269|PubMed:1900040}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17241283, CC ECO:0000269|PubMed:23303048, ECO:0000269|PubMed:2498083, CC ECO:0000269|PubMed:30902680, ECO:0000269|PubMed:9294222}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P13346-1; Sequence=Displayed; CC Name=2; Synonyms=deltaFosB {ECO:0000303|PubMed:1900040}, FosB2 CC {ECO:0000303|PubMed:16687504}, FosB[short form] CC {ECO:0000303|PubMed:16687504}; CC IsoId=P13346-2; Sequence=VSP_061375; CC -!- TISSUE SPECIFICITY: Expressed in brain, including the preoptic area of CC the hypothalamus, the main and accessory olfactory bulbs, the pyriform CC cortex and the hippocampus (at protein level) (PubMed:8706134, CC PubMed:23303048). Expressed in the neurons of the subgranular zone of CC the dentate gyrus in the hippocampus (at protein level) CC (PubMed:23303048, PubMed:30902680). Expressed in pyramidal cells in CA1 CC and CA3, in the dentate gyrus and the nucleus accumbens of the striatum CC (at protein level) (PubMed:9294222, PubMed:26446228). CC {ECO:0000269|PubMed:23303048, ECO:0000269|PubMed:26446228, CC ECO:0000269|PubMed:30902680, ECO:0000269|PubMed:8706134, CC ECO:0000269|PubMed:9294222}. CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in the core and shell of the CC nucleus accumbens of the striatum (at protein level) (PubMed:20473292). CC Expressed in the neurons of the subgranular zone of the dentate gyrus CC in the hippocampus (at protein level) (PubMed:23303048). CC {ECO:0000269|PubMed:20473292, ECO:0000269|PubMed:23303048}. CC -!- INDUCTION: Induced by growth factors (PubMed:2498083). Up-regulated in CC the preoptic area of the hypothalamus after 6 hours of exposure to pups CC (PubMed:8706134). Induced by cocaine in the striatum (PubMed:9294222). CC Induced by kainic acid (PubMed:23303048). Induced in the hippocampus by CC novelty exposure and spatial learning (PubMed:26446228). CC {ECO:0000269|PubMed:23303048, ECO:0000269|PubMed:2498083, CC ECO:0000269|PubMed:26446228, ECO:0000269|PubMed:8706134, CC ECO:0000269|PubMed:9294222}. CC -!- INDUCTION: [Isoform 1]: Induced by cocaine in the striatum. CC {ECO:0000269|PubMed:9294222}. CC -!- INDUCTION: [Isoform 2]: Induced by cocaine in the striatum CC (PubMed:9294222). Induced by chronic social defeat stress, with CC resilient mice showing the greatest induction in both core and shell CC nucleus accumbens subregions (PubMed:20473292). CC {ECO:0000269|PubMed:20473292, ECO:0000269|PubMed:9294222}. CC -!- DOMAIN: Binds DNA via bZIP domain; DNA-binding is under control of CC cellular redox homeostasis (in vitro) (By similarity). To enable DNA CC binding, the bZIP domain must undergo a conformational rearrangement CC which requires the reduction of the interchain disulfide bond between CC FosB and JunD (in vitro) (By similarity). The bZIP domain is able to CC form homomeric oligomers via formation of interchain disulfide bonds CC under non-reducing conditions (in vitro) (By similarity). Under CC reducing conditions, the disulfide-bonded homomeric species dissociates CC into monomers (in vitro) (By similarity). CC {ECO:0000250|UniProtKB:P53539}. CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:16687504}. CC -!- PTM: [Isoform 2]: Phosphorylated at Ser-27 by CSNK2A1; phosphorylation CC increases protein stability and transactivation potential. CC {ECO:0000269|PubMed:16687504, ECO:0000269|PubMed:17241283}. CC -!- DISRUPTION PHENOTYPE: Deficiency in the ability to nurture young CC animals and the majority of pups die within 1-2 days of birth CC (PubMed:8706134). Impaired nurturing behavior towards newborns is CC observed in postpartum mothers as well as in young females and males CC (PubMed:8706134). Failure in AP-1 binding activity after repeated CC cocaine administration (PubMed:9294222). Exaggerated locomotor CC activation in response to initial cocaine exposures as well as robust CC conditioned place preference to a lower dose of cocaine, but lack of CC increment in cocaine-induced hyperactivity over 6 days (i.e. CC sensitization) (PubMed:9294222). Decreased sensitivity to rewarding CC properties of morphine and spatial memory impairment (PubMed:18407360). CC Decreased proliferation and increased ectopic migration of neural CC progenitor cells in the hippocampus (PubMed:23303048). Exhibit impaired CC adult hippocampal neurogenesis and spontaneous epilepsy with depressive CC behavior (PubMed:23303048). Altered gene expression in the hippocampus, CC including genes implicated in neurogenesis, depression, or epilepsy CC (PubMed:23303048). Knockout in hippocampal neurons, including neurons CC of the subgranular zone of the dentate gyrus, leads to a reduction of CC antidepressant-induced neurogenesis and impedes hippocampus-dependent CC learning in the novel object recognition task (PubMed:30902680). CC {ECO:0000269|PubMed:18407360, ECO:0000269|PubMed:23303048, CC ECO:0000269|PubMed:30902680, ECO:0000269|PubMed:8706134, CC ECO:0000269|PubMed:9294222}. CC -!- SIMILARITY: Belongs to the bZIP family. Fos subfamily. {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; X14897; CAA33026.1; -; mRNA. DR EMBL; AF093624; AAD13196.1; -; Genomic_DNA. DR CCDS; CCDS20897.1; -. [P13346-1] DR CCDS; CCDS85225.1; -. [P13346-2] DR PIR; S35477; TVMSFB. DR RefSeq; NP_001334515.1; NM_001347586.1. [P13346-2] DR RefSeq; NP_032062.1; NM_008036.2. [P13346-1] DR RefSeq; XP_006539606.1; XM_006539543.2. DR AlphaFoldDB; P13346; -. DR SMR; P13346; -. DR BioGRID; 199727; 2. DR DIP; DIP-1067N; -. DR IntAct; P13346; 1. DR STRING; 10090.ENSMUSP00000003640; -. DR iPTMnet; P13346; -. DR PhosphoSitePlus; P13346; -. DR MaxQB; P13346; -. DR PaxDb; 10090-ENSMUSP00000003640; -. DR ProteomicsDB; 271710; -. DR ProteomicsDB; 346702; -. DR Antibodypedia; 4139; 684 antibodies from 39 providers. DR DNASU; 14282; -. DR Ensembl; ENSMUST00000003640.4; ENSMUSP00000003640.3; ENSMUSG00000003545.4. [P13346-1] DR Ensembl; ENSMUST00000208446.2; ENSMUSP00000146789.2; ENSMUSG00000003545.4. [P13346-2] DR GeneID; 14282; -. DR KEGG; mmu:14282; -. DR UCSC; uc009flk.1; mouse. [P13346-1] DR AGR; MGI:95575; -. DR CTD; 2354; -. DR MGI; MGI:95575; Fosb. DR VEuPathDB; HostDB:ENSMUSG00000003545; -. DR eggNOG; KOG1414; Eukaryota. DR GeneTree; ENSGT00940000160358; -. DR HOGENOM; CLU_049742_0_0_1; -. DR InParanoid; P13346; -. DR OMA; MMQEVAF; -. DR OrthoDB; 4260878at2759; -. DR PhylomeDB; P13346; -. DR TreeFam; TF326301; -. DR BioGRID-ORCS; 14282; 1 hit in 78 CRISPR screens. DR ChiTaRS; Fosb; mouse. DR PRO; PR:P13346; -. DR Proteomes; UP000000589; Chromosome 7. DR RNAct; P13346; Protein. DR Bgee; ENSMUSG00000003545; Expressed in granulocyte and 87 other cell types or tissues. DR ExpressionAtlas; P13346; baseline and differential. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISO:MGI. DR GO; GO:0003677; F:DNA binding; IDA:MGI. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB. DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central. DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB. DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI. DR GO; GO:0071277; P:cellular response to calcium ion; IDA:MGI. DR GO; GO:0032870; P:cellular response to hormone stimulus; IEA:Ensembl. DR GO; GO:0007565; P:female pregnancy; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl. DR GO; GO:0051412; P:response to corticosterone; IEA:Ensembl. DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl. DR GO; GO:0032570; P:response to progesterone; IEA:Ensembl. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl. DR GO; GO:0006366; P:transcription by RNA polymerase II; ISO:MGI. DR CDD; cd14721; bZIP_Fos; 1. DR Gene3D; 1.20.5.170; -; 1. DR InterPro; IPR000837; AP-1. DR InterPro; IPR004827; bZIP. DR InterPro; IPR046347; bZIP_sf. DR PANTHER; PTHR23351; FOS TRANSCRIPTION FACTOR-RELATED; 1. DR PANTHER; PTHR23351:SF3; PROTEIN FOSB; 1. DR Pfam; PF00170; bZIP_1; 1. DR PRINTS; PR00042; LEUZIPPRFOS. DR SMART; SM00338; BRLZ; 1. DR SUPFAM; SSF57959; Leucine zipper domain; 1. DR PROSITE; PS50217; BZIP; 1. DR PROSITE; PS00036; BZIP_BASIC; 1. DR Genevisible; P13346; MM. PE 1: Evidence at protein level; KW Alternative splicing; Disulfide bond; DNA-binding; Nucleus; Phosphoprotein; KW Reference proteome. FT CHAIN 1..338 FT /note="Protein FosB" FT /id="PRO_0000076477" FT DOMAIN 155..218 FT /note="bZIP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978" FT REGION 1..54 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 80..179 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 157..182 FT /note="Basic motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978" FT REGION 183..211 FT /note="Leucine-zipper" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978" FT REGION 222..276 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 316..338 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 10..38 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 103..134 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 140..163 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 254..269 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 27 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:16687504" FT DISULFID 172 FT /note="Interchain (with C-279 in JUND)" FT /evidence="ECO:0000250|UniProtKB:P53539" FT VAR_SEQ 238..338 FT /note="Missing (in isoform 2)" FT /id="VSP_061375" FT MUTAGEN 27 FT /note="S->A: Increased degradation by the proteasome and a FT decrease in isoform 2/deltaFosB transactivation activity." FT /evidence="ECO:0000269|PubMed:16687504" FT MUTAGEN 27 FT /note="S->D: Increased protein stability." FT /evidence="ECO:0000269|PubMed:16687504" SQ SEQUENCE 338 AA; 35977 MW; E9D031A4BEAE48EC CRC64; MFQAFPGDYD SGSRCSSSPS AESQYLSSVD SFGSPPTAAA SQECAGLGEM PGSFVPTVTA ITTSQDLQWL VQPTLISSMA QSQGQPLASQ PPAVDPYDMP GTSYSTPGLS AYSTGGASGS GGPSTSTTTS GPVSARPARA RPRRPREETL TPEEEEKRRV RRERNKLAAA KCRNRRRELT DRLQAETDQL EEEKAELESE IAELQKEKER LEFVLVAHKP GCKIPYEEGP GPGPLAEVRD LPGSTSAKED GFGWLLPPPP PPPLPFQSSR DAPPNLTASL FTHSEVQVLG DPFPVVSPSY TSSFVLTCPE VSAFAGAQRT SGSEQPSDPL NSPSLLAL //