FOSB_MOUSE
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 03-AUG-2022, entry version 165.
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}.
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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_032062.1; NM_008036.2.
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; P13346; -.
DR PRIDE; P13346; -.
DR ProteomicsDB; 271710; -.
DR ProteomicsDB; 346702; -.
DR Antibodypedia; 4139; 564 antibodies from 39 providers.
DR DNASU; 14282; -.
DR Ensembl; ENSMUST00000003640; ENSMUSP00000003640; ENSMUSG00000003545. [P13346-1]
DR Ensembl; ENSMUST00000208446; ENSMUSP00000146789; ENSMUSG00000003545. [P13346-2]
DR GeneID; 14282; -.
DR KEGG; mmu:14282; -.
DR UCSC; uc009flk.1; mouse. [P13346-1]
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; QGMMQEV; -.
DR OrthoDB; 1221590at2759; -.
DR PhylomeDB; P13346; -.
DR TreeFam; TF326301; -.
DR BioGRID-ORCS; 14282; 1 hit in 73 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 86 other tissues.
DR ExpressionAtlas; P13346; baseline and differential.
DR Genevisible; P13346; MM.
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:0043278; P:response to morphine; 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 InterPro; IPR000837; AP-1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR029813; FosB.
DR PANTHER; PTHR23351; PTHR23351; 1.
DR PANTHER; PTHR23351:SF3; PTHR23351:SF3; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR PRINTS; PR00042; LEUZIPPRFOS.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
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
