JUN_MOUSE
ID JUN_MOUSE Reviewed; 334 AA.
AC P05627;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 3.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Transcription factor Jun {ECO:0000305};
DE AltName: Full=AH119;
DE AltName: Full=Activator protein 1;
DE Short=AP1;
DE AltName: Full=Proto-oncogene c-Jun;
DE AltName: Full=Transcription factor AP-1 subunit Jun {ECO:0000305};
DE AltName: Full=V-jun avian sarcoma virus 17 oncogene homolog;
DE Short=Jun A;
GN Name=Jun;
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].
RX PubMed=3136397; DOI=10.1038/334535a0;
RA Ryseck R.-P., Hirai S., Yaniv M., Bravo R.;
RT "Transcriptional activation of c-jun during the G0/G1 transition in mouse
RT fibroblasts.";
RL Nature 334:535-537(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2457172; DOI=10.1038/334629a0;
RA Lamph W.W., Wamsley P., Sassone-Corsi P., Verma I.M.;
RT "Induction of proto-oncogene JUN/AP-1 by serum and TPA.";
RL Nature 334:629-631(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3186736; DOI=10.1073/pnas.85.22.8464;
RA Ryder K., Nathans D.;
RT "Induction of protooncogene c-jun by serum growth factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:8464-8467(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 [5]
RP FUNCTION, IDENTIFICATION IN AN AP-1 COMPLEX, SUBUNIT, AND INTERACTION WITH
RP FOSB.
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 [6]
RP INTERACTION WITH MYBBP1A.
RX PubMed=9447996; DOI=10.1128/mcb.18.2.989;
RA Tavner F.J., Simpson R., Tashiro S., Favier D., Jenkins N.A., Gilbert D.J.,
RA Copeland N.G., Macmillan E.M., Lutwyche J., Keough R.A., Ishii S.,
RA Gonda T.J.;
RT "Molecular cloning reveals that the p160 Myb-binding protein is a novel,
RT predominantly nucleolar protein which may play a role in transactivation by
RT Myb.";
RL Mol. Cell. Biol. 18:989-1002(1998).
RN [7]
RP INTERACTION WITH DSIPI.
RX PubMed=11397794; DOI=10.1074/jbc.m101522200;
RA Mittelstadt P.R., Ashwell J.D.;
RT "Inhibition of AP-1 by the glucocorticoid-inducible protein GILZ.";
RL J. Biol. Chem. 276:29603-29610(2001).
RN [8]
RP INTERACTION WITH RBM39.
RX PubMed=11704680; DOI=10.1074/jbc.m110417200;
RA Jung D.-J., Na S.-Y., Na D.S., Lee J.W.;
RT "Molecular cloning and characterization of CAPER, a novel coactivator of
RT activating protein-1 and estrogen receptors.";
RL J. Biol. Chem. 277:1229-1234(2002).
RN [9]
RP INTERACTION WITH HIVEP3, AND FUNCTION.
RX PubMed=14707112; DOI=10.1084/jem.20030421;
RA Oukka M., Wein M.N., Glimcher L.H.;
RT "Schnurri-3 (KRC) interacts with c-Jun to regulate the IL-2 gene in T
RT cells.";
RL J. Exp. Med. 199:15-24(2004).
RN [10]
RP FUNCTION, AND PHOSPHORYLATION BY HIPK3.
RX PubMed=17210646; DOI=10.1128/mcb.02253-06;
RA Lan H.-C., Li H.-J., Lin G., Lai P.-Y., Chung B.-C.;
RT "Cyclic AMP stimulates SF-1-dependent CYP11A1 expression through
RT homeodomain-interacting protein kinase 3-mediated Jun N-terminal kinase and
RT c-Jun phosphorylation.";
RL Mol. Cell. Biol. 27:2027-2036(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-63; THR-242 AND
RP SER-246, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP INTERACTION WITH RNF187.
RX PubMed=20852630; DOI=10.1038/ncb2098;
RA Davies C.C., Chakraborty A., Cipriani F., Haigh K., Haigh J.J., Behrens A.;
RT "Identification of a co-activator that links growth factor signalling to c-
RT Jun/AP-1 activation.";
RL Nat. Cell Biol. 12:963-972(2010).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-56, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [15]
RP INTERACTION WITH PRR7.
RX PubMed=27458189; DOI=10.15252/embj.201593070;
RA Kravchick D.O., Karpova A., Hrdinka M., Lopez-Rojas J., Iacobas S.,
RA Carbonell A.U., Iacobas D.A., Kreutz M.R., Jordan B.A.;
RT "Synaptonuclear messenger PRR7 inhibits c-Jun ubiquitination and regulates
RT NMDA-mediated excitotoxicity.";
RL EMBO J. 35:1923-1934(2016).
RN [16]
RP INTERACTION WITH FOS; FOSB; FOSL1 AND FOSL2.
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).
CC -!- FUNCTION: Transcription factor that recognizes and binds to the AP-1
CC consensus motif 5'-TGA[GC]TCA-3' (PubMed:14707112). Heterodimerizes
CC with proteins of the FOS family to form an AP-1 transcription factor
CC complex, thereby enhancing its DNA binding activity to the AP-1
CC consensus sequence 5'-TGA[GC]TCA-3' and enhancing its transcriptional
CC activity (PubMed:2498083). Together with FOSB, plays a role in
CC activation-induced cell death of T cells by binding to the AP-1
CC promoter site of FASLG/CD95L, and inducing its transcription in
CC response to activation of the TCR/CD3 signaling pathway (By
CC similarity). Promotes activity of NR5A1 when phosphorylated by HIPK3
CC leading to increased steroidogenic gene expression upon cAMP signaling
CC pathway stimulation (PubMed:17210646). Involved in activated KRAS-
CC mediated transcriptional activation of USP28 (By similarity). Binds to
CC the USP28 promoter (By similarity). {ECO:0000250|UniProtKB:P05412,
CC ECO:0000269|PubMed:14707112, ECO:0000269|PubMed:17210646,
CC ECO:0000269|PubMed:2498083}.
CC -!- SUBUNIT: Heterodimer with either BATF3 or ATF7 (By similarity).
CC Heterodimer with FOS (PubMed:29272704). Heterodimer with FOSB isoform 1
CC and 2 (PubMed:29272704). Component of an AP-1 transcription factor
CC complex composed of JUN-FOS heterodimers (PubMed:2498083). As part of
CC the AP-1 transcription factor complex, forms heterodimers with FOSB,
CC thereby binding to the AP-1 consensus sequence and stimulating
CC transcription (PubMed:2498083). The ATF7/JUN heterodimer is essential
CC for ATF7 transactivation activity. Interacts with SP1, SPIB and TCF20.
CC Interacts with COPS5; the interaction leads indirectly to its
CC phosphorylation. Component of the SMAD3/SMAD4/JUN/FOS/complex which
CC forms at the AP1 promoter site. The SMAD3/SMAD4 heterodimer acts
CC synergistically with the JUN/FOS heterodimer to activate transcription
CC in response to TGF-beta (By similarity). Interacts (via its basic DNA
CC binding and leucine zipper domains) with SMAD3 (via an N-terminal
CC domain); the interaction is required for TGF-beta-mediated
CC transactivation of the SMAD3/SMAD4/JUN/FOS/complex (By similarity).
CC Interacts with DSIPI; the interaction inhibits the binding of active
CC AP1 to its target DNA (PubMed:11397794). Interacts with HIVEP3 and
CC MYBBP1A (PubMed:9447996, PubMed:14707112). Interacts with methylated
CC RNF187 (PubMed:20852630). Binds to HIPK3. Interacts (when
CC phosphorylated) with FBXW7 (By similarity). Interacts with PRR7
CC (PubMed:27458189). Found in a complex with PRR7 and FBXW7 (By
CC similarity). Interacts with PRR7 and FBXW7; the interaction inhibits
CC ubiquitination-mediated JUN degradation promoting its phosphorylation
CC and transcriptional activity (By similarity). Interacts with RBM39
CC (PubMed:11704680). Interacts with PAGE4 (By similarity). Interacts with
CC FOSL1 and FOSL2 (PubMed:29272704). {ECO:0000250|UniProtKB:P05412,
CC ECO:0000250|UniProtKB:P17325, ECO:0000269|PubMed:11397794,
CC ECO:0000269|PubMed:11704680, ECO:0000269|PubMed:14707112,
CC ECO:0000269|PubMed:20852630, ECO:0000269|PubMed:2498083,
CC ECO:0000269|PubMed:27458189, ECO:0000269|PubMed:29272704,
CC ECO:0000269|PubMed:9447996}.
CC -!- INTERACTION:
CC P05627; Q64261: Cdk6; NbExp=2; IntAct=EBI-764369, EBI-847380;
CC P05627; Q91Y86: Mapk8; NbExp=2; IntAct=EBI-764369, EBI-298784;
CC P05627; P03372: ESR1; Xeno; NbExp=6; IntAct=EBI-764369, EBI-78473;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P05412}.
CC -!- PTM: Phosphorylated by CaMK4 and PRKDC; phosphorylation enhances the
CC transcriptional activity. Phosphorylated by HIPK3. Phosphorylated by
CC DYRK2 at Ser-246; this primes the protein for subsequent
CC phosphorylation by GSK3B at Thr-242. Phosphorylated at Thr-242, Ser-246
CC and Ser-252 by GSK3B; phosphorylation reduces its ability to bind DNA.
CC Phosphorylated by PAK2 at Thr-2, Thr-8, Thr-89, Thr-93 and Thr-289
CC thereby promoting JUN-mediated cell proliferation and transformation.
CC Phosphorylated by PLK3 following hypoxia or UV irradiation, leading to
CC increase DNA-binding activity (By similarity).
CC {ECO:0000250|UniProtKB:P05412}.
CC -!- PTM: Ubiquitinated by the SCF(FBXW7), leading to its degradation.
CC Ubiquitination takes place following phosphorylation, that promotes
CC interaction with FBXW7. {ECO:0000250|UniProtKB:P05412}.
CC -!- PTM: Acetylated at Lys-271 by EP300. {ECO:0000250|UniProtKB:P05412}.
CC -!- SIMILARITY: Belongs to the bZIP family. Jun subfamily. {ECO:0000305}.
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DR EMBL; X12761; CAA31252.1; -; mRNA.
DR EMBL; X12740; CAA31236.1; -; mRNA.
DR EMBL; J04115; AAA37419.1; -; mRNA.
DR EMBL; BC002081; AAH02081.1; -; mRNA.
DR EMBL; BC021888; AAH21888.1; -; mRNA.
DR CCDS; CCDS18364.1; -.
DR PIR; A31345; TVMSJA.
DR RefSeq; NP_034721.1; NM_010591.2.
DR AlphaFoldDB; P05627; -.
DR BMRB; P05627; -.
DR SMR; P05627; -.
DR BioGRID; 200871; 42.
DR ComplexPortal; CPX-610; AP-1 transcription factor complex FOS-JUN-NFATC2.
DR ComplexPortal; CPX-611; bZIP transcription factor complex, Fos-Jun.
DR ComplexPortal; CPX-612; bZIP transcription factor complex, Jun-Jun.
DR DIP; DIP-1068N; -.
DR ELM; P05627; -.
DR IntAct; P05627; 10.
DR MINT; P05627; -.
DR STRING; 10090.ENSMUSP00000102711; -.
DR ChEMBL; CHEMBL5369; -.
DR iPTMnet; P05627; -.
DR PhosphoSitePlus; P05627; -.
DR EPD; P05627; -.
DR jPOST; P05627; -.
DR PaxDb; P05627; -.
DR PeptideAtlas; P05627; -.
DR PRIDE; P05627; -.
DR ProteomicsDB; 301703; -.
DR Antibodypedia; 3535; 3926 antibodies from 48 providers.
DR DNASU; 16476; -.
DR Ensembl; ENSMUST00000107094; ENSMUSP00000102711; ENSMUSG00000052684.
DR GeneID; 16476; -.
DR KEGG; mmu:16476; -.
DR UCSC; uc008tsq.2; mouse.
DR CTD; 3725; -.
DR MGI; MGI:96646; Jun.
DR VEuPathDB; HostDB:ENSMUSG00000052684; -.
DR eggNOG; KOG0837; Eukaryota.
DR GeneTree; ENSGT00940000162061; -.
DR HOGENOM; CLU_057007_0_0_1; -.
DR InParanoid; P05627; -.
DR OMA; HHQHMPA; -.
DR OrthoDB; 1090460at2759; -.
DR PhylomeDB; P05627; -.
DR TreeFam; TF323952; -.
DR Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
DR Reactome; R-MMU-450341; Activation of the AP-1 family of transcription factors.
DR Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
DR BioGRID-ORCS; 16476; 9 hits in 78 CRISPR screens.
DR ChiTaRS; Jun; mouse.
DR PRO; PR:P05627; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P05627; protein.
DR Bgee; ENSMUSG00000052684; Expressed in endoderm of midgut and 298 other tissues.
DR ExpressionAtlas; P05627; baseline and differential.
DR Genevisible; P05627; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000791; C:euchromatin; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0035976; C:transcription factor AP-1 complex; IPI:ComplexPortal.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0017053; C:transcription repressor complex; IPI:MGI.
DR GO; GO:0035497; F:cAMP response element binding; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0140296; F:general transcription initiation factor binding; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR GO; GO:0071837; F:HMG box domain binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0070412; F:R-SMAD binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
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:0000976; F:transcription cis-regulatory region binding; IDA:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; ISO:MGI.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0031103; P:axon regeneration; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; IGI:MGI.
DR GO; GO:0072740; P:cellular response to anisomycin; IDA:MGI.
DR GO; GO:0071276; P:cellular response to cadmium ion; ISO:MGI.
DR GO; GO:0071277; P:cellular response to calcium ion; IDA:MGI.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0051365; P:cellular response to potassium ion starvation; ISO:MGI.
DR GO; GO:1990646; P:cellular response to prolactin; IEA:Ensembl.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:MGI.
DR GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR GO; GO:0061029; P:eyelid development in camera-type eye; IMP:MGI.
DR GO; GO:0035026; P:leading edge cell differentiation; IMP:MGI.
DR GO; GO:0007612; P:learning; ISO:MGI.
DR GO; GO:0001889; P:liver development; IMP:MGI.
DR GO; GO:0051899; P:membrane depolarization; ISO:MGI.
DR GO; GO:0001774; P:microglial cell activation; IMP:MGI.
DR GO; GO:0030224; P:monocyte differentiation; IMP:MGI.
DR GO; GO:0043922; P:negative regulation by host of viral transcription; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IGI:MGI.
DR GO; GO:0043392; P:negative regulation of DNA binding; ISO:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
DR GO; GO:0031953; P:negative regulation of protein autophosphorylation; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:1990441; P:negative regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0003151; P:outflow tract morphogenesis; IMP:MGI.
DR GO; GO:0043923; P:positive regulation by host of viral transcription; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0045740; P:positive regulation of DNA replication; ISO:MGI.
DR GO; GO:2000144; P:positive regulation of DNA-templated transcription, initiation; ISO:MGI.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:MGI.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:MGI.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:MGI.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:MGI.
DR GO; GO:0045657; P:positive regulation of monocyte differentiation; ISO:MGI.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:1901522; P:positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:MGI.
DR GO; GO:0001836; P:release of cytochrome c from mitochondria; ISO:MGI.
DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
DR GO; GO:0034097; P:response to cytokine; IEA:Ensembl.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0035994; P:response to muscle stretch; IDA:MGI.
DR GO; GO:0009314; P:response to radiation; ISO:MGI.
DR GO; GO:0048545; P:response to steroid hormone; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:MGI.
DR GO; GO:0060395; P:SMAD protein signal transduction; ISO:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006351; P:transcription, DNA-templated; ISO:MGI.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR015558; C_Jun/v-Jun.
DR InterPro; IPR005643; JNK.
DR InterPro; IPR002112; Leuzip_Jun.
DR InterPro; IPR008917; TF_DNA-bd_sf.
DR PANTHER; PTHR11462:SF8; PTHR11462:SF8; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR Pfam; PF03957; Jun; 1.
DR PRINTS; PR00043; LEUZIPPRJUN.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF47454; SSF47454; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Proto-oncogene; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..334
FT /note="Transcription factor Jun"
FT /id="PRO_0000076430"
FT DOMAIN 255..318
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 150..226
FT /note="Interaction with PAGE4"
FT /evidence="ECO:0000250|UniProtKB:P05412"
FT REGION 191..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..282
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 283..311
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 203..217
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 275
FT /note="Necessary for synergistic transcriptional activity
FT with SMAD3"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="Phosphothreonine; by PAK2"
FT /evidence="ECO:0000250|UniProtKB:P05412"
FT MOD_RES 8
FT /note="Phosphothreonine; by PAK2"
FT /evidence="ECO:0000250|UniProtKB:P05412"
FT MOD_RES 56
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 73
FT /note="Phosphoserine; by MAPK8 and PLK3"
FT /evidence="ECO:0000250|UniProtKB:P05412"
FT MOD_RES 89
FT /note="Phosphothreonine; by PAK2"
FT /evidence="ECO:0000250|UniProtKB:P05412"
FT MOD_RES 91
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P05412"
FT MOD_RES 93
FT /note="Phosphothreonine; by PAK2"
FT /evidence="ECO:0000250|UniProtKB:P05412"
FT MOD_RES 242
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 252
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:P05412"
FT MOD_RES 274
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05412"
FT MOD_RES 289
FT /note="Phosphothreonine; by PAK2"
FT /evidence="ECO:0000250|UniProtKB:P05412"
FT CROSSLNK 35
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05412"
FT CROSSLNK 50
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05412"
FT CROSSLNK 56
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P05412"
FT CROSSLNK 70
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05412"
FT CROSSLNK 229
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05412"
FT CONFLICT 183
FT /note="S -> C (in Ref. 1; CAA31252)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 334 AA; 35944 MW; 2BE0E4025B8B1CA3 CRC64;
MTAKMETTFY DDALNASFLQ SESGAYGYSN PKILKQSMTL NLADPVGSLK PHLRAKNSDL
LTSPDVGLLK LASPELERLI IQSSNGHITT TPTPTQFLCP KNVTDEQEGF AEGFVRALAE
LHSQNTLPSV TSAAQPVSGA GMVAPAVASV AGAGGGGGYS ASLHSEPPVY ANLSNFNPGA
LSSGGGAPSY GAAGLAFPSQ PQQQQQPPQP PHHLPQQIPV QHPRLQALKE EPQTVPEMPG
ETPPLSPIDM ESQERIKAER KRMRNRIAAS KCRKRKLERI ARLEEKVKTL KAQNSELAST
ANMLREQVAQ LKQKVMNHVN SGCQLMLTQQ LQTF
