ID JUN_HUMAN Reviewed; 331 AA. AC P05412; Q6FHM7; Q96G93; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 2. DT 27-MAR-2024, entry version 269. DE RecName: Full=Transcription factor Jun {ECO:0000305}; 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 AltName: Full=p39; GN Name=JUN; 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=3194415; DOI=10.1073/pnas.85.23.9148; RA Hattori K., Angel P., le Beau M.M., Karin M.; RT "Structure and chromosomal localization of the functional intronless human RT JUN protooncogene."; RL Proc. Natl. Acad. Sci. U.S.A. 85:9148-9152(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RX PubMed=2825349; DOI=10.1126/science.2825349; RA Bohmann D., Bos T.J., Admon A., Nishimura T., Vogt P.K., Tjian R.; RT "Human proto-oncogene c-jun encodes a DNA binding protein with structural RT and functional properties of transcription factor AP-1."; RL Science 238:1386-1392(1987). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NIEHS SNPs program; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=B-cell, Ovary, Testis, and Uterus; 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 [8] RP PHOSPHORYLATION AT THR-239; SER-243 AND SER-249 BY GSK3B. RX PubMed=1846781; DOI=10.1016/0092-8674(91)90241-p; RA Boyle W.J., Smeal T., Defize L.H., Angel P., Woodgett J.R., Karin M., RA Hunter T.; RT "Activation of protein kinase C decreases phosphorylation of c-Jun at sites RT that negatively regulate its DNA-binding activity."; RL Cell 64:573-584(1991). RN [9] RP PHOSPHORYLATION AT SER-249. RX PubMed=8464713; DOI=10.1093/nar/21.5.1289; RA Bannister A.J., Gottlieb T.M., Kouzarides T., Jackson S.P.; RT "c-Jun is phosphorylated by the DNA-dependent protein kinase in vitro; RT definition of the minimal kinase recognition motif."; RL Nucleic Acids Res. 21:1289-1295(1993). RN [10] RP PHOSPHORYLATION BY CAMK4. RX PubMed=8855261; DOI=10.1073/pnas.93.20.10803; RA Enslen H., Tokumitsu H., Stork P.J., Davis R.J., Soderling T.R.; RT "Regulation of mitogen-activated protein kinases by a calcium/calmodulin- RT dependent protein kinase cascade."; RL Proc. Natl. Acad. Sci. U.S.A. 93:10803-10808(1996). RN [11] RP INTERACTION WITH TCF20. RX PubMed=8663478; DOI=10.1074/jbc.271.30.18231; RA Kirstein M., Sanz L., Moscat J., Diaz-Meco M.T., Saus J.; RT "Cross-talk between different enhancer elements during mitogenic induction RT of the human stromelysin-1 gene."; RL J. Biol. Chem. 271:18231-18236(1996). RN [12] RP INTERACTION WITH COPS5. RX PubMed=8837781; DOI=10.1038/383453a0; RA Claret F.-X., Hibi M., Dhut S., Toda T., Karin M.; RT "A new group of conserved coactivators that increase the specificity of AP- RT 1 transcription factors."; RL Nature 383:453-457(1996). RN [13] RP IDENTIFICATION AS A COMPONENT OF THE SMAD3/SMAD4/JUN/FOS COMPLEX, AND RP INTERACTION WITH SMAD3. RX PubMed=9732876; DOI=10.1038/29814; RA Zhang Y., Feng X.H., Derynck R.; RT "Smad3 and Smad4 cooperate with c-Jun/c-Fos to mediate TGF-beta-induced RT transcription."; RL Nature 394:909-913(1998). RN [14] RP INTERACTION WITH SPIB. RX PubMed=10196196; DOI=10.1074/jbc.274.16.11115; RA Rao S., Matsumura A., Yoon J., Simon M.C.; RT "SPI-B activates transcription via a unique proline, serine, and threonine RT domain and exhibits DNA binding affinity differences from PU.1."; RL J. Biol. Chem. 274:11115-11124(1999). RN [15] RP INTERACTION WITH ATF7, AND MUTAGENESIS OF SER-63 AND SER-73. RX PubMed=10376527; DOI=10.1038/sj.onc.1202723; RA De Graeve F., Bahr A., Sabapathy K.T., Hauss C., Wagner E.F., Kedinger C., RA Chatton B.; RT "Role of the ATFa/JNK2 complex in Jun activation."; RL Oncogene 18:3491-3500(1999). RN [16] RP INTERACTION WITH SMAD3 IN THE SMAD3/SMAD4/JUN/FOS COMPLEX, DNA-BINDING, RP FUNCTION, AND MUTAGENESIS OF ARG-272. RX PubMed=10995748; DOI=10.1074/jbc.m004731200; RA Qing J., Zhang Y., Derynck R.; RT "Structural and functional characterization of the transforming growth RT factor-beta -induced Smad3/c-Jun transcriptional cooperativity."; RL J. Biol. Chem. 275:38802-38812(2000). RN [17] RP ACETYLATION AT LYS-271 BY EP300. RX PubMed=11689449; DOI=10.1093/emboj/20.21.6095; RA Vries R.G., Prudenziati M., Zwartjes C., Verlaan M., Kalkhoven E., RA Zantema A.; RT "A specific lysine in c-Jun is required for transcriptional repression by RT E1A and is acetylated by p300."; RL EMBO J. 20:6095-6103(2001). RN [18] RP INTERACTION WITH BATF3. RX PubMed=12087103; DOI=10.1074/jbc.m205048200; RA Bower K.E., Zeller R.W., Wachsman W., Martinez T., McGuire K.L.; RT "Correlation of transcriptional repression by p21(SNFT) with changes in RT DNA.NF-AT complex interactions."; RL J. Biol. Chem. 277:34967-34977(2002). RN [19] RP FUNCTION, AND MUTAGENESIS OF 6-GLU--GLY-194. 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 [20] RP INTERACTION WITH BATF3. RX PubMed=15467742; DOI=10.1038/sj.onc.1208109; RA Bower K.E., Fritz J.M., McGuire K.L.; RT "Transcriptional repression of MMP-1 by p21SNFT and reduced in vitro RT invasiveness of hepatocarcinoma cells."; RL Oncogene 23:8805-8814(2004). RN [21] RP PHOSPHORYLATION AT SER-63; SER-73; THR-91 AND THR-93, UBIQUITINATION, RP INTERACTION WITH FBXW7, AND MUTAGENESIS OF SER-63; SER-73; THR-91 AND RP THR-93. RX PubMed=14739463; DOI=10.1126/science.1092880; RA Nateri A.S., Riera-Sans L., Da Costa C., Behrens A.; RT "The ubiquitin ligase SCFFbw7 antagonizes apoptotic JNK signaling."; RL Science 303:1374-1378(2004). RN [22] 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 [23] RP INTERACTION WITH SP1. RX PubMed=16478997; DOI=10.1128/mcb.26.5.1770-1785.2006; RA Hung J.J., Wang Y.T., Chang W.C.; RT "Sp1 deacetylation induced by phorbol ester recruits p300 to activate RT 12(S)-lipoxygenase gene transcription."; RL Mol. Cell. Biol. 26:1770-1785(2006). RN [24] RP PHOSPHORYLATION AT SER-63 AND SER-73. RX PubMed=17804415; DOI=10.1074/jbc.m702791200; RA Wang L., Dai W., Lu L.; RT "Stress-induced c-Jun activation mediated by Polo-like kinase 3 in corneal RT epithelial cells."; RL J. Biol. Chem. 282:32121-32127(2007). RN [25] RP PHOSPHORYLATION AT SER-63 AND SER-73. RX PubMed=18650425; DOI=10.1074/jbc.m801326200; RA Wang L., Gao J., Dai W., Lu L.; RT "Activation of Polo-like kinase 3 by hypoxic stresses."; RL J. Biol. Chem. 283:25928-25935(2008). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-63; THR-239 AND RP SER-243, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [27] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [28] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63 AND SER-243, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [29] RP FUNCTION, AND DNA-BINDING. RX PubMed=22083952; DOI=10.1128/mcb.05504-11; RA Ji Z., Donaldson I.J., Liu J., Hayes A., Zeef L.A., Sharrocks A.D.; RT "The forkhead transcription factor FOXK2 promotes AP-1-mediated RT transcriptional regulation."; RL Mol. Cell. Biol. 32:385-398(2012). RN [30] 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 [31] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [32] RP PHOSPHORYLATION AT THR-2; THR-8; THR-89; THR-93 AND THR-286, AND RP MUTAGENESIS OF THR-2; THR-8; THR-89; THR-93 AND THR-286. RX PubMed=21177766; DOI=10.1093/carcin/bgq271; RA Li T., Zhang J., Zhu F., Wen W., Zykova T., Li X., Liu K., Peng C., Ma W., RA Shi G., Dong Z., Bode A.M., Dong Z.; RT "P21-activated protein kinase (PAK2)-mediated c-Jun phosphorylation at 5 RT threonine sites promotes cell transformation."; RL Carcinogenesis 32:659-666(2011). RN [33] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58 AND SER-63, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [34] RP PHOSPHORYLATION AT SER-243, AND MUTAGENESIS OF SER-243. RX PubMed=22307329; DOI=10.1172/jci60818; RA Taira N., Mimoto R., Kurata M., Yamaguchi T., Kitagawa M., Miki Y., RA Yoshida K.; RT "DYRK2 priming phosphorylation of c-Jun and c-Myc modulates cell cycle RT progression in human cancer cells."; RL J. Clin. Invest. 122:859-872(2012). RN [35] RP INTERACTION WITH RNF187. RX PubMed=23624934; DOI=10.1038/emboj.2013.98; RA Davies C.C., Chakraborty A., Diefenbacher M.E., Skehel M., Behrens A.; RT "Arginine methylation of the c-Jun coactivator RACO-1 is required for c- RT Jun/AP-1 activation."; RL EMBO J. 32:1556-1567(2013). RN [36] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63 AND SER-243, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [37] RP INTERACTION WITH PAGE4, AND TISSUE SPECIFICITY. RX PubMed=24559171; DOI=10.1021/bi500013w; RA Mooney S.M., Qiu R., Kim J.J., Sacho E.J., Rajagopalan K., Johng D., RA Shiraishi T., Kulkarni P., Weninger K.R.; RT "Cancer/testis antigen PAGE4, a regulator of c-Jun transactivation, is RT phosphorylated by homeodomain-interacting protein kinase 1, a component of RT the stress-response pathway."; RL Biochemistry 53:1670-1679(2014). RN [38] RP INTERACTION WITH PAGE4, AND TISSUE SPECIFICITY. RX PubMed=24263171; DOI=10.1016/j.bbadis.2013.11.014; RA Rajagopalan K., Qiu R., Mooney S.M., Rao S., Shiraishi T., Sacho E., RA Huang H., Shapiro E., Weninger K.R., Kulkarni P.; RT "The Stress-response protein prostate-associated gene 4, interacts with c- RT Jun and potentiates its transactivation."; RL Biochim. Biophys. Acta 1842:154-163(2014). RN [39] RP FUNCTION, AND DNA-BINDING. RX PubMed=24623306; DOI=10.7554/elife.02313; RA Serra R.W., Fang M., Park S.M., Hutchinson L., Green M.R.; RT "A KRAS-directed transcriptional silencing pathway that mediates the CpG RT island methylator phenotype."; RL Elife 3:E02313-E02313(2014). RN [40] RP INTERACTION WITH PAGE4. RX PubMed=26242913; DOI=10.1074/jbc.m115.658583; RA He Y., Chen Y., Mooney S.M., Rajagopalan K., Bhargava A., Sacho E., RA Weninger K., Bryan P.N., Kulkarni P., Orban J.; RT "Phosphorylation-induced conformational ensemble switching in an RT intrinsically disordered cancer/testis antigen."; RL J. Biol. Chem. 290:25090-25102(2015). RN [41] RP IDENTIFICATION IN COMPLEX WITH PRR7 AND FBXW7, INTERACTION WITH PRR7 AND RP FBXW7, AND UBIQUITINATION. 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 [42] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-35; LYS-50; LYS-56; LYS-70 AND RP LYS-226, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [43] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH ARK2C AND CSNK2B. RX PubMed=31341047; DOI=10.1128/jvi.00989-19; RA Siddiqi U.Z., Vaidya A.S., Li X., Marcon E., Tsao S.W., Greenblatt J., RA Frappier L.; RT "Identification of ARKL1 as a Negative Regulator of Epstein-Barr Virus RT Reactivation."; RL J. Virol. 93:0-0(2019). RN [44] RP X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 257-313 OF COMPLEX WITH FOS. RX PubMed=7816143; DOI=10.1038/373257a0; RA Glover J.N., Harrison S.C.; RT "Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c- RT Jun bound to DNA."; RL Nature 373:257-261(1995). RN [45] RP STRUCTURE BY NMR OF 276-314. RX PubMed=8662824; DOI=10.1074/jbc.271.23.13663; RA Junius F.K., O'Donoghue S.I., Nilges M., Weiss A.S., King G.F.; RT "High resolution NMR solution structure of the leucine zipper domain of the RT c-Jun homodimer."; RL J. Biol. Chem. 271:13663-13667(1996). CC -!- FUNCTION: Transcription factor that recognizes and binds to the AP-1 CC consensus motif 5'-TGA[GC]TCA-3' (PubMed:10995748, PubMed:22083952). CC Heterodimerizes with proteins of the FOS family to form an AP-1 CC transcription complex, thereby enhancing its DNA binding activity to CC the AP-1 consensus sequence 5'-TGA[GC]TCA-3' and enhancing its CC transcriptional activity (By similarity). Together with FOSB, plays a CC role in 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 CC (PubMed:12618758). Promotes activity of NR5A1 when phosphorylated by CC HIPK3 leading to increased steroidogenic gene expression upon cAMP CC signaling pathway stimulation (PubMed:17210646). Involved in activated CC KRAS-mediated transcriptional activation of USP28 in colorectal cancer CC (CRC) cells (PubMed:24623306). Binds to the USP28 promoter in CC colorectal cancer (CRC) cells (PubMed:24623306). CC {ECO:0000250|UniProtKB:P05627, ECO:0000269|PubMed:10995748, CC ECO:0000269|PubMed:12618758, ECO:0000269|PubMed:17210646, CC ECO:0000269|PubMed:22083952, ECO:0000269|PubMed:24623306}. CC -!- FUNCTION: (Microbial infection) Upon Epstein-Barr virus (EBV) CC infection, binds to viral BZLF1 Z promoter and activates viral BZLF1 CC expression. {ECO:0000269|PubMed:31341047}. CC -!- SUBUNIT: Heterodimer with either BATF3 or ATF7 (PubMed:10376527, CC PubMed:12087103, PubMed:15467742). Heterodimer with FOS (By CC similarity). Heterodimer with FOSB isoform 1 and 2 (By similarity). CC Component of an AP-1 transcription factor complex composed of JUN-FOS CC heterodimers (By similarity). As part of the AP-1 transcription factor CC complex, forms heterodimers with FOSB, thereby binding to the AP-1 CC consensus sequence and stimulating transcription (By similarity). CC Interacts with FOS and FOSB isoform 1 and 2 (By similarity). The CC ATF7/JUN heterodimer is essential for ATF7 transactivation activity CC (PubMed:10376527). Interacts with TSC22D3 (via N-terminus); the CC interaction inhibits the binding of active AP1 to its target DNA (By CC similarity). Interacts with HIVEP3 and MYBBP1A (By similarity). CC Interacts with SP1, SPIB and TCF20 (PubMed:10196196, PubMed:16478997, CC PubMed:8663478). Interacts with COPS5; the interaction leads indirectly CC to its phosphorylation (PubMed:8837781). Component of the CC SMAD3/SMAD4/JUN/FOS/complex which forms at the AP1 promoter site CC (PubMed:10995748). The SMAD3/SMAD4 heterodimer acts synergistically CC with the JUN/FOS heterodimer to activate transcription in response to CC TGF-beta (PubMed:9732876). Interacts (via its basic DNA binding and CC leucine zipper domains) with SMAD3 (via an N-terminal domain); the CC interaction is required for TGF-beta-mediated transactivation of the CC SMAD3/SMAD4/JUN/FOS/complex (PubMed:10995748). Interacts with CC methylated RNF187 (PubMed:20852630, PubMed:23624934). Binds to HIPK3. CC Interacts (when phosphorylated) with FBXW7 (PubMed:14739463). Found in CC a complex with PRR7 and FBXW7 (PubMed:27458189). Interacts with PRR7 CC and FBXW7; the interaction inhibits ubiquitination-mediated JUN CC degradation promoting its phosphorylation and transcriptional activity CC (PubMed:27458189). Interacts with RBM39 (By similarity). Interacts with CC PAGE4 (PubMed:24263171, PubMed:24559171, PubMed:26242913). Interacts CC with ARK2N and CSNK2B; the interaction with ARK2N is mediated by CSNK2B CC (PubMed:31341047). {ECO:0000250|UniProtKB:P05627, CC ECO:0000250|UniProtKB:P17325, ECO:0000269|PubMed:10196196, CC ECO:0000269|PubMed:10376527, ECO:0000269|PubMed:10995748, CC ECO:0000269|PubMed:12087103, ECO:0000269|PubMed:14739463, CC ECO:0000269|PubMed:15467742, ECO:0000269|PubMed:16478997, CC ECO:0000269|PubMed:20852630, ECO:0000269|PubMed:23624934, CC ECO:0000269|PubMed:24263171, ECO:0000269|PubMed:24559171, CC ECO:0000269|PubMed:26242913, ECO:0000269|PubMed:27458189, CC ECO:0000269|PubMed:31341047, ECO:0000269|PubMed:8663478, CC ECO:0000269|PubMed:8837781, ECO:0000269|PubMed:9732876}. CC -!- INTERACTION: CC P05412; P78563: ADARB1; NbExp=3; IntAct=EBI-852823, EBI-2967304; CC P05412; Q06481: APLP2; NbExp=3; IntAct=EBI-852823, EBI-79306; CC P05412; P05067: APP; NbExp=5; IntAct=EBI-852823, EBI-77613; CC P05412; P18846: ATF1; NbExp=2; IntAct=EBI-852823, EBI-852794; CC P05412; P15336: ATF2; NbExp=19; IntAct=EBI-852823, EBI-1170906; CC P05412; P18847: ATF3; NbExp=9; IntAct=EBI-852823, EBI-712767; CC P05412; P18848: ATF4; NbExp=4; IntAct=EBI-852823, EBI-492498; CC P05412; P17544: ATF7; NbExp=6; IntAct=EBI-852823, EBI-765623; CC P05412; Q16520: BATF; NbExp=4; IntAct=EBI-852823, EBI-749503; CC P05412; Q8N1L9: BATF2; NbExp=2; IntAct=EBI-852823, EBI-742695; CC P05412; Q8N1L9-1: BATF2; NbExp=3; IntAct=EBI-852823, EBI-15746052; CC P05412; Q9NR55: BATF3; NbExp=7; IntAct=EBI-852823, EBI-10312707; CC P05412; Q8IWZ6: BBS7; NbExp=3; IntAct=EBI-852823, EBI-1806001; CC P05412; Q99966: CITED1; NbExp=2; IntAct=EBI-852823, EBI-2624951; CC P05412; Q9UGL9: CRCT1; NbExp=3; IntAct=EBI-852823, EBI-713677; CC P05412; O43889: CREB3; NbExp=4; IntAct=EBI-852823, EBI-625002; CC P05412; P20042: EIF2S2; NbExp=4; IntAct=EBI-852823, EBI-711977; CC P05412; P14921: ETS1; NbExp=3; IntAct=EBI-852823, EBI-913209; CC P05412; P22607: FGFR3; NbExp=3; IntAct=EBI-852823, EBI-348399; CC P05412; P01100: FOS; NbExp=42; IntAct=EBI-852823, EBI-852851; CC P05412; P15407: FOSL1; NbExp=10; IntAct=EBI-852823, EBI-744510; CC P05412; P15408: FOSL2; NbExp=11; IntAct=EBI-852823, EBI-3893419; CC P05412; Q9UJY5: GGA1; NbExp=2; IntAct=EBI-852823, EBI-447141; CC P05412; Q9HD26: GOPC; NbExp=3; IntAct=EBI-852823, EBI-349832; CC P05412; P06396: GSN; NbExp=3; IntAct=EBI-852823, EBI-351506; CC P05412; P07900: HSP90AA1; NbExp=4; IntAct=EBI-852823, EBI-296047; CC P05412; P11142: HSPA8; NbExp=3; IntAct=EBI-852823, EBI-351896; CC P05412; P10809: HSPD1; NbExp=5; IntAct=EBI-852823, EBI-352528; CC P05412; P05412: JUN; NbExp=6; IntAct=EBI-852823, EBI-852823; CC P05412; P52292: KPNA2; NbExp=4; IntAct=EBI-852823, EBI-349938; CC P05412; P53779: MAPK10; NbExp=4; IntAct=EBI-852823, EBI-713543; CC P05412; P45983: MAPK8; NbExp=5; IntAct=EBI-852823, EBI-286483; CC P05412; P45983-1: MAPK8; NbExp=2; IntAct=EBI-852823, EBI-288687; CC P05412; Q9UPY8: MAPRE3; NbExp=3; IntAct=EBI-852823, EBI-726739; CC P05412; Q00987: MDM2; NbExp=3; IntAct=EBI-852823, EBI-389668; CC P05412; Q13330: MTA1; NbExp=4; IntAct=EBI-852823, EBI-714236; CC P05412; I6L9F6: NEFL; NbExp=3; IntAct=EBI-852823, EBI-10178578; CC P05412; P07197: NEFM; NbExp=2; IntAct=EBI-852823, EBI-1105035; CC P05412; O95644: NFATC1; NbExp=5; IntAct=EBI-852823, EBI-6907210; CC P05412; Q13469-2: NFATC2; NbExp=6; IntAct=EBI-852823, EBI-10087113; CC P05412; Q16236: NFE2L2; NbExp=2; IntAct=EBI-852823, EBI-2007911; CC P05412; O60829: PAGE4; NbExp=2; IntAct=EBI-852823, EBI-27085632; CC P05412; P27986-2: PIK3R1; NbExp=3; IntAct=EBI-852823, EBI-9090282; CC P05412; P48634: PRRC2A; NbExp=2; IntAct=EBI-852823, EBI-347545; CC P05412; P63000: RAC1; NbExp=5; IntAct=EBI-852823, EBI-413628; CC P05412; Q8WTV0: SCARB1; NbExp=3; IntAct=EBI-852823, EBI-78657; CC P05412; Q15796: SMAD2; NbExp=3; IntAct=EBI-852823, EBI-1040141; CC P05412; Q9NRL3: STRN4; NbExp=3; IntAct=EBI-852823, EBI-717245; CC P05412; P56279: TCL1A; NbExp=6; IntAct=EBI-852823, EBI-749995; CC P05412; Q71U36: TUBA1A; NbExp=3; IntAct=EBI-852823, EBI-302552; CC P05412; P07437: TUBB; NbExp=3; IntAct=EBI-852823, EBI-350864; CC P05412; Q13885: TUBB2A; NbExp=5; IntAct=EBI-852823, EBI-711595; CC P05412; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-852823, EBI-741480; CC P05412; Q99986: VRK1; NbExp=5; IntAct=EBI-852823, EBI-1769146; CC P05412; P0C746: HBZ; Xeno; NbExp=3; IntAct=EBI-852823, EBI-10890294; CC P05412; Q8WQG9: jnk-1; Xeno; NbExp=3; IntAct=EBI-852823, EBI-321822; CC P05412; P56671: Maz; Xeno; NbExp=2; IntAct=EBI-852823, EBI-1809712; CC P05412; Q9DGW5: MDV005; Xeno; NbExp=3; IntAct=EBI-852823, EBI-10889526; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- TISSUE SPECIFICITY: Expressed in the developing and adult prostate and CC prostate cancer cells. {ECO:0000269|PubMed:24263171, CC ECO:0000269|PubMed:24559171}. CC -!- PTM: Ubiquitinated by the SCF(FBXW7), leading to its degradation CC (PubMed:14739463, PubMed:27458189). Ubiquitination takes place CC following phosphorylation, that promotes interaction with FBXW7 CC (PubMed:14739463). {ECO:0000269|PubMed:14739463, CC ECO:0000269|PubMed:27458189}. CC -!- PTM: Phosphorylated by CaMK4 and PRKDC; phosphorylation enhances the CC transcriptional activity. Phosphorylated by HIPK3. Phosphorylated by CC DYRK2 at Ser-243; this primes the protein for subsequent CC phosphorylation by GSK3B at Thr-239. Phosphorylated at Thr-239, Ser-243 CC and Ser-249 by GSK3B; phosphorylation reduces its ability to bind DNA. CC Phosphorylated by PAK2 at Thr-2, Thr-8, Thr-89, Thr-93 and Thr-286 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. {ECO:0000269|PubMed:14739463, CC ECO:0000269|PubMed:17210646, ECO:0000269|PubMed:17804415, CC ECO:0000269|PubMed:1846781, ECO:0000269|PubMed:18650425, CC ECO:0000269|PubMed:21177766, ECO:0000269|PubMed:22307329, CC ECO:0000269|PubMed:8464713, ECO:0000269|PubMed:8855261}. CC -!- PTM: Acetylated at Lys-271 by EP300. {ECO:0000269|PubMed:11689449}. CC -!- SIMILARITY: Belongs to the bZIP family. Jun subfamily. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/151/JUN"; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/jun/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J04111; AAA59197.1; -; Genomic_DNA. DR EMBL; CR541724; CAG46525.1; -; mRNA. DR EMBL; BT019759; AAV38564.1; -; mRNA. DR EMBL; AY217548; AAO22993.1; -; Genomic_DNA. DR EMBL; AL136985; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC002646; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC006175; AAH06175.1; -; mRNA. DR EMBL; BC009874; AAH09874.2; -; mRNA. DR EMBL; BC068522; AAH68522.1; -; mRNA. DR CCDS; CCDS610.1; -. DR PIR; A31264; TVHUJN. DR RefSeq; NP_002219.1; NM_002228.3. DR PDB; 1A02; X-ray; 2.70 A; J=253-308. DR PDB; 1FOS; X-ray; 3.05 A; F/H=254-315. DR PDB; 1JNM; X-ray; 2.20 A; A/B=254-315. DR PDB; 1JUN; NMR; -; A/B=276-314. DR PDB; 1S9K; X-ray; 3.10 A; E=257-308. DR PDB; 1T2K; X-ray; 3.00 A; C=254-314. DR PDB; 5FV8; X-ray; 1.99 A; D/E=277-308. DR PDB; 5T01; X-ray; 1.89 A; A/B=254-315. DR PDB; 6Y3V; X-ray; 1.50 A; P=262-273. DR PDBsum; 1A02; -. DR PDBsum; 1FOS; -. DR PDBsum; 1JNM; -. DR PDBsum; 1JUN; -. DR PDBsum; 1S9K; -. DR PDBsum; 1T2K; -. DR PDBsum; 5FV8; -. DR PDBsum; 5T01; -. DR PDBsum; 6Y3V; -. DR AlphaFoldDB; P05412; -. DR BMRB; P05412; -. DR SMR; P05412; -. DR BioGRID; 109928; 421. DR ComplexPortal; CPX-480; AP-1 transcription factor complex FOS-JUN-NFATC2. DR ComplexPortal; CPX-486; bZIP transcription factor complex, FOS-JUN. DR ComplexPortal; CPX-490; bZIP transcription factor complex, JUN-JUN. DR ComplexPortal; CPX-6420; bZIP transcription factor complex, ATF2-JUN. DR ComplexPortal; CPX-6474; bZIP transcription factor complex, ATF3-JUN. DR ComplexPortal; CPX-6562; bZIP transcription factor complex, ATF4-JUN. DR ComplexPortal; CPX-6786; bZIP transcription factor complex, ATF7-JUN. DR ComplexPortal; CPX-7005; bZIP transcription factor complex, BATF-JUN. DR ComplexPortal; CPX-7063; bZIP transcription factor complex, BATF2-JUN. DR ComplexPortal; CPX-7100; bZIP transcription factor complex, BATF3-JUN. DR CORUM; P05412; -. DR DIP; DIP-5961N; -. DR ELM; P05412; -. DR IntAct; P05412; 1410. DR MINT; P05412; -. DR STRING; 9606.ENSP00000360266; -. DR BindingDB; P05412; -. DR ChEMBL; CHEMBL4977; -. DR DrugBank; DB00210; Adapalene. DR DrugBank; DB01169; Arsenic trioxide. DR DrugBank; DB01029; Irbesartan. DR DrugBank; DB05785; LGD-1550. DR DrugBank; DB00852; Pseudoephedrine. DR DrugBank; DB00570; Vinblastine. DR GlyCosmos; P05412; 6 sites, 2 glycans. DR GlyGen; P05412; 8 sites, 2 O-linked glycans (8 sites). DR iPTMnet; P05412; -. DR PhosphoSitePlus; P05412; -. DR BioMuta; JUN; -. DR DMDM; 135298; -. DR CPTAC; CPTAC-1222; -. DR CPTAC; CPTAC-1324; -. DR CPTAC; CPTAC-3232; -. DR CPTAC; CPTAC-3233; -. DR CPTAC; CPTAC-807; -. DR CPTAC; CPTAC-927; -. DR EPD; P05412; -. DR jPOST; P05412; -. DR MassIVE; P05412; -. DR MaxQB; P05412; -. DR PaxDb; 9606-ENSP00000360266; -. DR PeptideAtlas; P05412; -. DR ProteomicsDB; 51836; -. DR Pumba; P05412; -. DR Antibodypedia; 3535; 4687 antibodies from 48 providers. DR CPTC; P05412; 6 antibodies. DR DNASU; 3725; -. DR Ensembl; ENST00000371222.4; ENSP00000360266.2; ENSG00000177606.9. DR Ensembl; ENST00000678696.1; ENSP00000503132.1; ENSG00000177606.9. DR GeneID; 3725; -. DR KEGG; hsa:3725; -. DR MANE-Select; ENST00000371222.4; ENSP00000360266.2; NM_002228.4; NP_002219.1. DR UCSC; uc001cze.4; human. DR AGR; HGNC:6204; -. DR CTD; 3725; -. DR DisGeNET; 3725; -. DR GeneCards; JUN; -. DR HGNC; HGNC:6204; JUN. DR HPA; ENSG00000177606; Low tissue specificity. DR MalaCards; JUN; -. DR MIM; 165160; gene. DR neXtProt; NX_P05412; -. DR OpenTargets; ENSG00000177606; -. DR PharmGKB; PA30006; -. DR VEuPathDB; HostDB:ENSG00000177606; -. DR eggNOG; KOG0837; Eukaryota. DR GeneTree; ENSGT00940000162061; -. DR HOGENOM; CLU_057007_0_0_1; -. DR InParanoid; P05412; -. DR OMA; HHQHMPA; -. DR OrthoDB; 4493275at2759; -. DR PhylomeDB; P05412; -. DR TreeFam; TF323952; -. DR PathwayCommons; P05412; -. DR Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation. DR Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence. DR Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP). DR Reactome; R-HSA-2871796; FCERI mediated MAPK activation. DR Reactome; R-HSA-450341; Activation of the AP-1 family of transcription factors. DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis. DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling. DR Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes. DR Reactome; R-HSA-8862803; Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models. DR Reactome; R-HSA-8943724; Regulation of PTEN gene transcription. DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression. DR Reactome; R-HSA-9673324; WNT5:FZD7-mediated leishmania damping. DR SignaLink; P05412; -. DR SIGNOR; P05412; -. DR BioGRID-ORCS; 3725; 147 hits in 1201 CRISPR screens. DR ChiTaRS; JUN; human. DR EvolutionaryTrace; P05412; -. DR GeneWiki; C-jun; -. DR GenomeRNAi; 3725; -. DR Pharos; P05412; Tchem. DR PRO; PR:P05412; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P05412; Protein. DR Bgee; ENSG00000177606; Expressed in vena cava and 207 other cell types or tissues. DR GO; GO:0000785; C:chromatin; IDA:UniProt. DR GO; GO:0000791; C:euchromatin; IDA:BHF-UCL. DR GO; GO:0000228; C:nuclear chromosome; TAS:ProtInc. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL. DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal. DR GO; GO:0035976; C:transcription factor AP-1 complex; IDA:CAFA. DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central. DR GO; GO:0035497; F:cAMP response element binding; 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; IDA:BHF-UCL. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:BHF-UCL. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:UniProtKB. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:ARUK-UCL. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0140296; F:general transcription initiation factor binding; IPI:UniProtKB. DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0070412; F:R-SMAD binding; IPI:BHF-UCL. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:BHF-UCL. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:CAFA. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB. DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; IPI:UniProtKB. DR GO; GO:0071276; P:cellular response to cadmium ion; IMP:CAFA. DR GO; GO:0034614; P:cellular response to reactive oxygen species; IMP:CAFA. DR GO; GO:0140467; P:integrated stress response signaling; NAS:ComplexPortal. DR GO; GO:0043922; P:negative regulation by host of viral transcription; IDA:UniProtKB. DR GO; GO:0043392; P:negative regulation of DNA binding; IDA:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ARUK-UCL. DR GO; GO:0043923; P:positive regulation by host of viral transcription; IDA:UniProtKB. DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:CAFA. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:2000144; P:positive regulation of DNA-templated transcription initiation; IDA:CACAO. DR GO; GO:1902895; P:positive regulation of miRNA transcription; IMP:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IMP:BHF-UCL. DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central. 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; IDA:ComplexPortal. DR GO; GO:0019046; P:release from viral latency; IDA:UniProt. DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:ParkinsonsUK-UCL. DR GO; GO:0060395; P:SMAD protein signal transduction; IDA:BHF-UCL. DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL. DR CDD; cd14696; bZIP_Jun; 1. DR Gene3D; 1.20.5.170; -; 1. DR IDEAL; IID00437; -. DR InterPro; IPR004827; bZIP. DR InterPro; IPR046347; bZIP_sf. DR InterPro; IPR005643; JNK. DR InterPro; IPR002112; Leuzip_Jun. DR InterPro; IPR008917; TF_DNA-bd_sf. DR PANTHER; PTHR11462; JUN TRANSCRIPTION FACTOR-RELATED; 1. DR PANTHER; PTHR11462:SF8; TRANSCRIPTION FACTOR JUN; 1. DR Pfam; PF00170; bZIP_1; 1. DR Pfam; PF03957; Jun; 1. DR PRINTS; PR00043; LEUZIPPRJUN. DR SMART; SM00338; BRLZ; 1. DR SUPFAM; SSF47454; A DNA-binding domain in eukaryotic transcription factors; 1. DR SUPFAM; SSF57959; Leucine zipper domain; 1. DR PROSITE; PS50217; BZIP; 1. DR PROSITE; PS00036; BZIP_BASIC; 1. DR Genevisible; P05412; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Direct protein sequencing; KW DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Proto-oncogene; KW Reference proteome; Transcription; Transcription regulation; KW Ubl conjugation. FT CHAIN 1..331 FT /note="Transcription factor Jun" FT /id="PRO_0000076429" FT DOMAIN 252..315 FT /note="bZIP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978" FT REGION 150..223 FT /note="Interaction with PAGE4" FT /evidence="ECO:0000269|PubMed:26242913" FT REGION 252..279 FT /note="Basic motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978" FT REGION 280..308 FT /note="Leucine-zipper" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978" FT SITE 272 FT /note="Necessary for synergistic transcriptional activity FT with SMAD3" FT MOD_RES 2 FT /note="Phosphothreonine; by PAK2" FT /evidence="ECO:0000269|PubMed:21177766" FT MOD_RES 8 FT /note="Phosphothreonine; by PAK2" FT /evidence="ECO:0000269|PubMed:21177766" FT MOD_RES 56 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05627" FT MOD_RES 58 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692" FT MOD_RES 63 FT /note="Phosphoserine; by MAPK8 and PLK3" FT /evidence="ECO:0000269|PubMed:14739463, FT ECO:0000269|PubMed:17804415, ECO:0000269|PubMed:18650425, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 73 FT /note="Phosphoserine; by MAPK8 and PLK3" FT /evidence="ECO:0000269|PubMed:14739463, FT ECO:0000269|PubMed:17804415, ECO:0000269|PubMed:18650425" FT MOD_RES 89 FT /note="Phosphothreonine; by PAK2" FT /evidence="ECO:0000269|PubMed:21177766" FT MOD_RES 91 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:14739463" FT MOD_RES 93 FT /note="Phosphothreonine; by PAK2" FT /evidence="ECO:0000269|PubMed:14739463, FT ECO:0000269|PubMed:21177766" FT MOD_RES 239 FT /note="Phosphothreonine; by GSK3-beta" FT /evidence="ECO:0000269|PubMed:1846781, FT ECO:0007744|PubMed:18669648" FT MOD_RES 243 FT /note="Phosphoserine; by DYRK2 and GSK3-beta" FT /evidence="ECO:0000269|PubMed:1846781, FT ECO:0000269|PubMed:22307329, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT MOD_RES 249 FT /note="Phosphoserine; by GSK3-beta" FT /evidence="ECO:0000269|PubMed:1846781, FT ECO:0000269|PubMed:8464713" FT MOD_RES 271 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:11689449" FT MOD_RES 286 FT /note="Phosphothreonine; by PAK2" FT /evidence="ECO:0000269|PubMed:21177766" FT CROSSLNK 35 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 50 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 56 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 70 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 226 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 297 FT /note="T -> M (in dbSNP:rs9989)" FT /id="VAR_012070" FT MUTAGEN 2 FT /note="T->A: Complete loss of PAK2-mediated FT phosphorylation; when associated with A-8; A-89; A-93; and FT A-286." FT /evidence="ECO:0000269|PubMed:21177766" FT MUTAGEN 6..194 FT /note="Missing: Abolishes activation of FASLG/CD95L FT transcription." FT /evidence="ECO:0000269|PubMed:12618758" FT MUTAGEN 8 FT /note="T->A: Complete loss of PAK2-mediated FT phosphorylation; when associated with A-2; A-89; A-93; and FT A-286." FT /evidence="ECO:0000269|PubMed:21177766" FT MUTAGEN 63 FT /note="S->A: Greatly reduced ATF7-mediated transcriptional FT activity; when associated with A-73. Abolishes interaction FT with FBXW7; when associated with A-73; A-91 and A-93." FT /evidence="ECO:0000269|PubMed:10376527, FT ECO:0000269|PubMed:14739463" FT MUTAGEN 73 FT /note="S->A: Greatly reduced ATF7-mediated transcriptional FT activity; when associated with A-63. Abolishes interaction FT with FBXW7; when associated with A-63; A-91 and A-93." FT /evidence="ECO:0000269|PubMed:10376527, FT ECO:0000269|PubMed:14739463" FT MUTAGEN 89 FT /note="T->A: Complete loss of PAK2-mediated FT phosphorylation; when associated with A-2; A-8; A-93; and FT A-286." FT /evidence="ECO:0000269|PubMed:21177766" FT MUTAGEN 91 FT /note="T->A: Abolishes interaction with FBXW7; when FT associated with A-63; A-73 and A-93." FT /evidence="ECO:0000269|PubMed:14739463" FT MUTAGEN 93 FT /note="T->A: Abolishes interaction with FBXW7; when FT associated with A-63; A-73 and A-91." FT /evidence="ECO:0000269|PubMed:14739463" FT MUTAGEN 93 FT /note="T->A: Complete loss of PAK2-mediated FT phosphorylation; when associated with A-2; A-8; A-89; and FT A-286." FT /evidence="ECO:0000269|PubMed:21177766" FT MUTAGEN 243 FT /note="S->A: Abolishes phosphorylation by DYRK2. Abolishes FT phosphorylation by GSK3B at Thr-239." FT /evidence="ECO:0000269|PubMed:22307329" FT MUTAGEN 272 FT /note="R->V: Abolishes the synergistic activity with SMAD3 FT to activate TGF-beta-mediated transcription." FT /evidence="ECO:0000269|PubMed:10995748" FT MUTAGEN 286 FT /note="T->A: Complete loss of PAK2-mediated FT phosphorylation; when associated with A-2; A-8; A-89; and FT A-93." FT /evidence="ECO:0000269|PubMed:21177766" FT CONFLICT 11 FT /note="D -> G (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 14 FT /note="L -> F (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 80 FT /note="I -> V (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 151 FT /note="A -> S (in Ref. 3; CAG46525)" FT /evidence="ECO:0000305" FT HELIX 255..310 FT /evidence="ECO:0007829|PDB:5T01" SQ SEQUENCE 331 AA; 35676 MW; 0695E23AC4D33561 CRC64; MTAKMETTFY DDALNASFLP SESGPYGYSN PKILKQSMTL NLADPVGSLK PHLRAKNSDL LTSPDVGLLK LASPELERLI IQSSNGHITT TPTPTQFLCP KNVTDEQEGF AEGFVRALAE LHSQNTLPSV TSAAQPVNGA GMVAPAVASV AGGSGSGGFS ASLHSEPPVY ANLSNFNPGA LSSGGGAPSY GAAGLAFPAQ PQQQQQPPHH LPQQMPVQHP RLQALKEEPQ TVPEMPGETP PLSPIDMESQ ERIKAERKRM RNRIAASKCR KRKLERIARL EEKVKTLKAQ NSELASTANM LREQVAQLKQ KVMNHVNSGC QLMLTQQLQT F //