FOSB_HUMAN
ID FOSB_HUMAN Reviewed; 338 AA.
AC P53539; A8K9K5; A8VJE1; A8VJE6; A8VJF0; A8VJF3; A8VJF7; A8VJG1; A8VJG5;
AC A8VJG9; E7EPR6; E9PHJ3; K7EKC1; K7EMJ6; Q49AD7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Protein FosB {ECO:0000305};
DE AltName: Full=FosB proto-oncogene, AP-1 transcription factor subunit {ECO:0000312|HGNC:HGNC:3797};
DE AltName: Full=G0/G1 switch regulatory protein 3;
DE AltName: Full=Transcription factor AP-1 subunit FosB {ECO:0000305};
GN Name=FOSB; Synonyms=G0S3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1301997; DOI=10.1038/ng0492-34;
RA Martin-Gallardo A., McCombie W.R., Gocayne J.D., Fitzgerald M.G.,
RA Wallace S., Lee B.M., Lamerdin J.E., Trapp S., Kelley J.M., Liu L.-I.,
RA Dubnick M., Johnston-Dow L.A., Kerlavage A.R., de Jong P., Carrano A.,
RA Fields C., Venter J.C.;
RT "Automated DNA sequencing and analysis of 106 kilobases from human
RT chromosome 19q13.3.";
RL Nat. Genet. 1:34-39(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Blood;
RX PubMed=8985116; DOI=10.1089/dna.1996.15.1025;
RA Heximer S.P., Cristillo A.D., Russell L., Forsdyke D.R.;
RT "Sequence analysis and expression in cultured lymphocytes of the human FOSB
RT gene (G0S3).";
RL DNA Cell Biol. 15:1025-1038(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5; 6; 7; 8 AND 9), AND
RP ALTERNATIVE SPLICING.
RA Xiong F., Zeng Z., Xiong W.;
RT "Novel transcript variants of human FOSB gene.";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-33.
RG NIEHS SNPs program;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Thyroid;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 10).
RC TISSUE=Blood, and Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP FUNCTION.
RX PubMed=12618758; DOI=10.1038/sj.onc.1206126;
RA Baumann S., Hess J., Eichhorst S.T., Krueger A., Angel P., Krammer P.H.,
RA Kirchhoff S.;
RT "An unexpected role for FosB in activation-induced cell death of T cells.";
RL Oncogene 22:1333-1339(2003).
RN [10]
RP TISSUE SPECIFICITY.
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] {ECO:0007744|PDB:5VPA, ECO:0007744|PDB:5VPB, ECO:0007744|PDB:5VPC, ECO:0007744|PDB:5VPD, ECO:0007744|PDB:5VPE, ECO:0007744|PDB:5VPF}
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 153-219 IN COMPLEX WITH JUND AND
RP DNA, FUNCTION, SUBUNIT, INTERACTION WITH JUND, DOMAIN, AND DISULFIDE BOND.
RX PubMed=28981703; DOI=10.1093/nar/gkx795;
RA Yin Z., Machius M., Nestler E.J., Rudenko G.;
RT "Activator Protein-1: redox switch controlling structure and DNA-binding.";
RL Nucleic Acids Res. 45:11425-11436(2017).
RN [12] {ECO:0007744|PDB:6UCI, ECO:0007744|PDB:6UCL, ECO:0007744|PDB:6UCM}
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 153-219, SUBUNIT (ISOFORM 11),
RP AND DOMAIN.
RX PubMed=32542236; DOI=10.1016/j.crstbi.2019.12.001;
RA Yin Z., Venkannagari H., Lynch H., Aglyamova G., Bhandari M., Machius M.,
RA Nestler E.J., Robison A.J., Rudenko G.;
RT "Self-assembly of the bZIP transcription factor FosB.";
RL Curr. Res. Struct. Biol. 2:1-13(2020).
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:12618758, PubMed:28981703). 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 (By similarity). 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
CC (PubMed:12618758). Exhibits transactivation activity in vitro (By
CC similarity). Involved in the display of nurturing behavior towards
CC newborns (By similarity). May play a role in neurogenesis in the
CC hippocampus and in learning and memory-related tasks by regulating the
CC expression of various genes involved in neurogenesis, depression and
CC epilepsy (By similarity). Implicated in behavioral responses related to
CC morphine reward and spatial memory (By similarity).
CC {ECO:0000250|UniProtKB:P13346, ECO:0000269|PubMed:12618758,
CC ECO:0000269|PubMed:28981703}.
CC -!- FUNCTION: [Isoform 11]: Exhibits lower transactivation activity than
CC isoform 1 in vitro (By similarity). The heterodimer with JUN does not
CC display any transcriptional activity, and may thereby act as an
CC transcriptional inhibitor (By similarity). May be involved in the
CC regulation of neurogenesis in the hippocampus (By similarity). May play
CC 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 (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:P13346}.
CC -!- SUBUNIT: Heterodimer; binds to DNA as heterodimer (PubMed:28981703).
CC Component of an AP-1 transcription factor complex; composed of FOS-JUN
CC heterodimers (By similarity). As part of the AP-1 transcription factor
CC complex, forms heterodimers with JUN, JUNB or JUND, thereby binding to
CC the AP-1 consensus sequence and stimulating transcription
CC (PubMed:28981703). Interacts with the BAF multiprotein chromatin-
CC remodeling complex subunits SMARCB1 and SMARCD1 (By similarity).
CC Interacts with ARID1A and JUN (By similarity).
CC {ECO:0000250|UniProtKB:P13346, ECO:0000269|PubMed:28981703}.
CC -!- SUBUNIT: [Isoform 11]: Homodimer under oxidizing conditions and monomer
CC under reducing conditions (in vitro) (PubMed:32542236). Heterodimer;
CC binds to DNA as heterodimer (By similarity). Forms heterodimers with
CC JUNB, JUN or JUND; thereby binding to the AP-1 consensus sequence but
CC does not stimulate transcription (By similarity). Forms heterodimers
CC with JUND under oxidizing conditions (PubMed:32542236).
CC {ECO:0000250|UniProtKB:P13346, ECO:0000269|PubMed:32542236}.
CC -!- INTERACTION:
CC P53539; P21549: AGXT; NbExp=3; IntAct=EBI-2806743, EBI-727098;
CC P53539; P15336: ATF2; NbExp=3; IntAct=EBI-2806743, EBI-1170906;
CC P53539; Q9BU64: CENPO; NbExp=3; IntAct=EBI-2806743, EBI-745954;
CC P53539; Q02930-3: CREB5; NbExp=3; IntAct=EBI-2806743, EBI-10192698;
CC P53539; Q9UIA0: CYTH4; NbExp=3; IntAct=EBI-2806743, EBI-11521003;
CC P53539; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-2806743, EBI-744099;
CC P53539; Q8WU58: FAM222B; NbExp=3; IntAct=EBI-2806743, EBI-2807642;
CC P53539; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-2806743, EBI-6658203;
CC P53539; Q9BZS1: FOXP3; NbExp=3; IntAct=EBI-2806743, EBI-983719;
CC P53539; Q9BZE0: GLIS2; NbExp=3; IntAct=EBI-2806743, EBI-7251368;
CC P53539; P17275: JUNB; NbExp=6; IntAct=EBI-2806743, EBI-748062;
CC P53539; O43639: NCK2; NbExp=3; IntAct=EBI-2806743, EBI-713635;
CC P53539; Q14511-2: NEDD9; NbExp=3; IntAct=EBI-2806743, EBI-11746523;
CC P53539; Q16236: NFE2L2; NbExp=6; IntAct=EBI-2806743, EBI-2007911;
CC P53539; B7ZLY0: PHC2; NbExp=3; IntAct=EBI-2806743, EBI-14568740;
CC P53539; O43189: PHF1; NbExp=3; IntAct=EBI-2806743, EBI-530034;
CC P53539; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-2806743, EBI-1389308;
CC P53539; P78424: POU6F2; NbExp=5; IntAct=EBI-2806743, EBI-12029004;
CC P53539; Q01974: ROR2; NbExp=3; IntAct=EBI-2806743, EBI-6422642;
CC P53539; Q96A09: TENT5B; NbExp=5; IntAct=EBI-2806743, EBI-752030;
CC P53539; Q08117-2: TLE5; NbExp=3; IntAct=EBI-2806743, EBI-11741437;
CC P53539; O43711: TLX3; NbExp=3; IntAct=EBI-2806743, EBI-3939165;
CC P53539; Q14119: VEZF1; NbExp=3; IntAct=EBI-2806743, EBI-11980193;
CC P53539; Q96K80: ZC3H10; NbExp=3; IntAct=EBI-2806743, EBI-742550;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P13346}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=11;
CC Name=1; Synonyms=FosB-L;
CC IsoId=P53539-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P53539-2; Sequence=VSP_046167;
CC Name=3;
CC IsoId=P53539-3; Sequence=VSP_055563;
CC Name=4;
CC IsoId=P53539-4; Sequence=VSP_055565;
CC Name=5;
CC IsoId=P53539-5; Sequence=VSP_055563, VSP_046167;
CC Name=6;
CC IsoId=P53539-6; Sequence=VSP_046167, VSP_055565;
CC Name=7;
CC IsoId=P53539-7; Sequence=VSP_055563, VSP_055565;
CC Name=8;
CC IsoId=P53539-8; Sequence=VSP_055564;
CC Name=9;
CC IsoId=P53539-9; Sequence=VSP_055564, VSP_055565;
CC Name=10;
CC IsoId=P53539-10; Sequence=VSP_055562;
CC Name=11; Synonyms=deltaFosB {ECO:0000303|PubMed:20473292};
CC IsoId=P53539-11; Sequence=VSP_061374;
CC -!- TISSUE SPECIFICITY: [Isoform 11]: Expressed in the nucleus accumbens of
CC the striatum (at protein level). {ECO:0000269|PubMed:20473292}.
CC -!- DOMAIN: Binds DNA via bZIP domain; DNA-binding is under control of
CC cellular redox homeostasis (in vitro) (PubMed:28981703). 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) (PubMed:28981703). The bZIP domain is able to
CC form homomeric oligomers via formation of interchain disulfide bonds
CC under non-reducing conditions (in vitro) (PubMed:32542236). Under
CC reducing conditions, the disulfide-bonded homomeric species dissociates
CC into monomers (in vitro) (PubMed:32542236).
CC {ECO:0000269|PubMed:28981703, ECO:0000269|PubMed:32542236}.
CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:D3ZLB7}.
CC -!- PTM: [Isoform 11]: Phosphorylated at Ser-27 by CSNK2A1; phosphorylation
CC increases protein stability and transactivation potential.
CC {ECO:0000250|UniProtKB:P13346}.
CC -!- SIMILARITY: Belongs to the bZIP family. Fos subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/fosb/";
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DR EMBL; L49169; AAB53946.1; -; mRNA.
DR EMBL; EU178109; ABW34730.1; -; mRNA.
DR EMBL; EU178110; ABW34731.1; -; mRNA.
DR EMBL; EU178111; ABW34732.1; -; mRNA.
DR EMBL; EU178112; ABW34733.1; -; mRNA.
DR EMBL; EU178113; ABW34734.1; -; mRNA.
DR EMBL; EU178114; ABW34735.1; -; mRNA.
DR EMBL; EU178115; ABW34736.1; -; mRNA.
DR EMBL; EU178116; ABW34737.1; -; mRNA.
DR EMBL; AY898963; AAW65374.1; -; Genomic_DNA.
DR EMBL; AK292720; BAF85409.1; -; mRNA.
DR EMBL; AC138128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471126; EAW57351.1; -; Genomic_DNA.
DR EMBL; BC036724; AAH36724.1; -; mRNA.
DR EMBL; BC040197; AAH40197.1; -; mRNA.
DR CCDS; CCDS12664.1; -. [P53539-1]
DR CCDS; CCDS46113.1; -. [P53539-2]
DR PIR; I53043; I53043.
DR RefSeq; NP_001107643.1; NM_001114171.1. [P53539-2]
DR RefSeq; NP_006723.2; NM_006732.2. [P53539-1]
DR PDB; 5VPA; X-ray; 2.83 A; A=153-219.
DR PDB; 5VPB; X-ray; 2.69 A; A/C=153-219.
DR PDB; 5VPC; X-ray; 2.50 A; A/C=153-219.
DR PDB; 5VPD; X-ray; 2.79 A; A/C=153-219.
DR PDB; 5VPE; X-ray; 2.05 A; A/C=153-219.
DR PDB; 5VPF; X-ray; 2.69 A; A/C=153-219.
DR PDB; 6UCI; X-ray; 2.09 A; A/B/C/D=153-219.
DR PDB; 6UCL; X-ray; 2.21 A; A=153-219.
DR PDB; 6UCM; X-ray; 2.42 A; A/B/C=153-219.
DR PDBsum; 5VPA; -.
DR PDBsum; 5VPB; -.
DR PDBsum; 5VPC; -.
DR PDBsum; 5VPD; -.
DR PDBsum; 5VPE; -.
DR PDBsum; 5VPF; -.
DR PDBsum; 6UCI; -.
DR PDBsum; 6UCL; -.
DR PDBsum; 6UCM; -.
DR AlphaFoldDB; P53539; -.
DR SMR; P53539; -.
DR BioGRID; 108637; 42.
DR CORUM; P53539; -.
DR DIP; DIP-60013N; -.
DR IntAct; P53539; 28.
DR MINT; P53539; -.
DR STRING; 9606.ENSP00000245919; -.
DR BindingDB; P53539; -.
DR ChEMBL; CHEMBL4630821; -.
DR GlyGen; P53539; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P53539; -.
DR PhosphoSitePlus; P53539; -.
DR BioMuta; FOSB; -.
DR DMDM; 1706888; -.
DR CPTAC; CPTAC-1760; -.
DR EPD; P53539; -.
DR MassIVE; P53539; -.
DR MaxQB; P53539; -.
DR PaxDb; P53539; -.
DR PeptideAtlas; P53539; -.
DR PRIDE; P53539; -.
DR ProteomicsDB; 17421; -.
DR ProteomicsDB; 20551; -.
DR ProteomicsDB; 56584; -. [P53539-1]
DR Antibodypedia; 4139; 564 antibodies from 39 providers.
DR DNASU; 2354; -.
DR Ensembl; ENST00000353609.8; ENSP00000245919.3; ENSG00000125740.14. [P53539-1]
DR Ensembl; ENST00000417353.6; ENSP00000407207.1; ENSG00000125740.14. [P53539-2]
DR Ensembl; ENST00000443841.6; ENSP00000414177.1; ENSG00000125740.14. [P53539-8]
DR Ensembl; ENST00000585836.5; ENSP00000467497.1; ENSG00000125740.14. [P53539-5]
DR Ensembl; ENST00000586615.5; ENSP00000468207.1; ENSG00000125740.14. [P53539-10]
DR Ensembl; ENST00000591858.5; ENSP00000466530.1; ENSG00000125740.14. [P53539-3]
DR Ensembl; ENST00000592436.5; ENSP00000465552.1; ENSG00000125740.14. [P53539-11]
DR Ensembl; ENST00000615753.4; ENSP00000485018.1; ENSG00000125740.14. [P53539-4]
DR GeneID; 2354; -.
DR KEGG; hsa:2354; -.
DR MANE-Select; ENST00000353609.8; ENSP00000245919.3; NM_006732.3; NP_006723.2.
DR UCSC; uc002pbx.5; human. [P53539-1]
DR CTD; 2354; -.
DR DisGeNET; 2354; -.
DR GeneCards; FOSB; -.
DR HGNC; HGNC:3797; FOSB.
DR HPA; ENSG00000125740; Low tissue specificity.
DR MIM; 164772; gene.
DR neXtProt; NX_P53539; -.
DR OpenTargets; ENSG00000125740; -.
DR PharmGKB; PA28213; -.
DR VEuPathDB; HostDB:ENSG00000125740; -.
DR eggNOG; KOG1414; Eukaryota.
DR GeneTree; ENSGT00940000160358; -.
DR HOGENOM; CLU_049742_4_0_1; -.
DR InParanoid; P53539; -.
DR OMA; QGMMQEV; -.
DR PhylomeDB; P53539; -.
DR TreeFam; TF326301; -.
DR PathwayCommons; P53539; -.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-HSA-9031628; NGF-stimulated transcription.
DR SignaLink; P53539; -.
DR SIGNOR; P53539; -.
DR BioGRID-ORCS; 2354; 11 hits in 1093 CRISPR screens.
DR ChiTaRS; FOSB; human.
DR GeneWiki; FOSB; -.
DR GenomeRNAi; 2354; -.
DR Pharos; P53539; Tbio.
DR PRO; PR:P53539; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P53539; protein.
DR Bgee; ENSG00000125740; Expressed in mucosa of stomach and 167 other tissues.
DR ExpressionAtlas; P53539; baseline and differential.
DR Genevisible; P53539; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0071277; P:cellular response to calcium ion; IEA:Ensembl.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IEA:Ensembl.
DR GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:ProtInc.
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; IEA:Ensembl.
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 3D-structure; Alternative splicing; Disulfide bond; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..338
FT /note="Protein FosB"
FT /id="PRO_0000076476"
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 79..191
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..132
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 172..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..269
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13346"
FT DISULFID 172
FT /note="Interchain (with C-285 in JUND)"
FT /evidence="ECO:0000269|PubMed:28981703,
FT ECO:0007744|PDB:5VPA, ECO:0007744|PDB:5VPB,
FT ECO:0007744|PDB:5VPC, ECO:0007744|PDB:5VPD"
FT VAR_SEQ 1..49
FT /note="Missing (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055562"
FT VAR_SEQ 42..80
FT /note="Missing (in isoform 3, isoform 5 and isoform 7)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_055563"
FT VAR_SEQ 43..185
FT /note="Missing (in isoform 8 and isoform 9)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_055564"
FT VAR_SEQ 150..185
FT /note="Missing (in isoform 2, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_046167"
FT VAR_SEQ 238..338
FT /note="Missing (in isoform 11)"
FT /id="VSP_061374"
FT VAR_SEQ 238..284
FT /note="Missing (in isoform 4, isoform 6, isoform 7 and
FT isoform 9)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_055565"
FT VARIANT 33
FT /note="G -> S (in dbSNP:rs28381241)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_022286"
FT CONFLICT 338
FT /note="L -> R (in Ref. 2; AAB53946 and 3; ABW34730/
FT ABW34731/ABW34732/ABW34733/ABW34734/ABW34735/ABW34736/
FT ABW34737)"
FT /evidence="ECO:0000305"
FT HELIX 157..217
FT /evidence="ECO:0007829|PDB:5VPE"
SQ SEQUENCE 338 AA; 35928 MW; DDFF827C5047850F CRC64;
MFQAFPGDYD SGSRCSSSPS AESQYLSSVD SFGSPPTAAA SQECAGLGEM PGSFVPTVTA
ITTSQDLQWL VQPTLISSMA QSQGQPLASQ PPVVDPYDMP GTSYSTPGMS GYSSGGASGS
GGPSTSGTTS GPGPARPARA RPRRPREETL TPEEEEKRRV RRERNKLAAA KCRNRRRELT
DRLQAETDQL EEEKAELESE IAELQKEKER LEFVLVAHKP GCKIPYEEGP GPGPLAEVRD
LPGSAPAKED GFSWLLPPPP PPPLPFQTSQ DAPPNLTASL FTHSEVQVLG DPFPVVNPSY
TSSFVLTCPE VSAFAGAQRT SGSDQPSDPL NSPSLLAL
