JUN_HUMAN
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 03-AUG-2022, entry version 260.
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 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 [44]
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 -!- 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 DSIPI; the interaction inhibits the
CC binding of active AP1 to its target DNA (By similarity). Interacts with
CC HIVEP3 and MYBBP1A (By similarity). Interacts with SP1, SPIB and TCF20
CC (PubMed:10196196, PubMed:16478997, PubMed:8663478). Interacts with
CC COPS5; the interaction leads indirectly to its phosphorylation
CC (PubMed:8837781). Component of the SMAD3/SMAD4/JUN/FOS/complex which
CC forms at the AP1 promoter site (PubMed:10995748). The SMAD3/SMAD4
CC heterodimer acts synergistically with the JUN/FOS heterodimer to
CC activate transcription in response to TGF-beta (PubMed:9732876).
CC Interacts (via its basic DNA binding and leucine zipper domains) with
CC SMAD3 (via an N-terminal domain); the interaction is required for TGF-
CC beta-mediated transactivation of the SMAD3/SMAD4/JUN/FOS/complex
CC (PubMed:10995748). Interacts with methylated RNF187 (PubMed:20852630,
CC PubMed:23624934). Binds to HIPK3. Interacts (when phosphorylated) with
CC FBXW7 (PubMed:14739463). Found in a complex with PRR7 and FBXW7
CC (PubMed:27458189). Interacts with PRR7 and FBXW7; the interaction
CC inhibits ubiquitination-mediated JUN degradation promoting its
CC phosphorylation and transcriptional activity (PubMed:27458189).
CC Interacts with RBM39 (By similarity). Interacts with PAGE4
CC (PubMed:24263171, PubMed:24559171, PubMed:26242913).
CC {ECO:0000250|UniProtKB:P05627, ECO:0000250|UniProtKB:P17325,
CC ECO:0000269|PubMed:10196196, ECO:0000269|PubMed:10376527,
CC ECO:0000269|PubMed:10995748, ECO:0000269|PubMed:12087103,
CC ECO:0000269|PubMed:14739463, ECO:0000269|PubMed:15467742,
CC ECO:0000269|PubMed:16478997, ECO:0000269|PubMed:20852630,
CC ECO:0000269|PubMed:23624934, ECO:0000269|PubMed:24263171,
CC ECO:0000269|PubMed:24559171, ECO:0000269|PubMed:26242913,
CC ECO:0000269|PubMed:27458189, 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=18; 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; 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="http://atlasgeneticsoncology.org/Genes/JUNID151.html";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/jun/";
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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; 310.
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; 1411.
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 GlyGen; P05412; 6 sites, 2 O-linked glycans (6 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; P05412; -.
DR PeptideAtlas; P05412; -.
DR PRIDE; P05412; -.
DR ProteomicsDB; 51836; -.
DR Antibodypedia; 3535; 3926 antibodies from 48 providers.
DR CPTC; P05412; 6 antibodies.
DR DNASU; 3725; -.
DR Ensembl; ENST00000371222.4; ENSP00000360266.2; ENSG00000177606.8.
DR Ensembl; ENST00000678696.1; ENSP00000503132.1; ENSG00000177606.8.
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 CTD; 3725; -.
DR DisGeNET; 3725; -.
DR GeneCards; JUN; -.
DR HGNC; HGNC:6204; JUN.
DR HPA; ENSG00000177606; Low tissue specificity.
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; 1090460at2759; -.
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; 128 hits in 1113 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 206 other tissues.
DR Genevisible; P05412; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
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:0005886; C:plasma membrane; IDA:HPA.
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:0017053; C:transcription repressor complex; IEA:Ensembl.
DR GO; GO:0035497; F:cAMP response element binding; IDA:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
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:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0031103; P:axon regeneration; IEA:Ensembl.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0072740; P:cellular response to anisomycin; IEA:Ensembl.
DR GO; GO:0071276; P:cellular response to cadmium ion; IMP:CAFA.
DR GO; GO:0071277; P:cellular response to calcium ion; IEA:Ensembl.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IMP:CAFA.
DR GO; GO:0061029; P:eyelid development in camera-type eye; IEA:Ensembl.
DR GO; GO:0140467; P:integrated stress response signaling; IC:ComplexPortal.
DR GO; GO:0035026; P:leading edge cell differentiation; IEA:Ensembl.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0001774; P:microglial cell activation; IEA:Ensembl.
DR GO; GO:0030224; P:monocyte differentiation; IEA:Ensembl.
DR GO; GO:0043922; P:negative regulation by host of viral transcription; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0043392; P:negative regulation of DNA binding; IDA:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0031953; P:negative regulation of protein autophosphorylation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
DR GO; GO:1990441; P:negative regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; IMP:ParkinsonsUK-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0003151; P:outflow tract morphogenesis; IEA:Ensembl.
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:2000144; P:positive regulation of DNA-templated transcription, initiation; IDA:CACAO.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IEA:Ensembl.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
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:1901522; P:positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IMP:BHF-UCL.
DR GO; GO:0007265; P:Ras protein signal transduction; IDA:UniProtKB.
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:0035994; P:response to muscle stretch; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
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 IDEAL; IID00437; -.
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 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
