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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
 
 
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