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Transcription factor AP-1 (Activator protein 1) (AP1) (Proto-oncogene c-Jun) (V-jun avian sarcoma virus 17 oncogene homolog) (p39)

 JUN_HUMAN               Reviewed;         331 AA.
P05412; Q6FHM7; Q96G93;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 2.
30-AUG-2017, entry version 225.
RecName: Full=Transcription factor AP-1;
AltName: Full=Activator protein 1;
Short=AP1;
AltName: Full=Proto-oncogene c-Jun;
AltName: Full=V-jun avian sarcoma virus 17 oncogene homolog;
AltName: Full=p39;
Name=JUN;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3194415; DOI=10.1073/pnas.85.23.9148;
Hattori K., Angel P., le Beau M.M., Karin M.;
"Structure and chromosomal localization of the functional intronless
human JUN protooncogene.";
Proc. Natl. Acad. Sci. U.S.A. 85:9148-9152(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=2825349; DOI=10.1126/science.2825349;
Bohmann D., Bos T.J., Admon A., Nishimura T., Vogt P.K., Tjian R.;
"Human proto-oncogene c-jun encodes a DNA binding protein with
structural and functional properties of transcription factor AP-1.";
Science 238:1386-1392(1987).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=B-cell, Ovary, Testis, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PHOSPHORYLATION AT THR-239; SER-243 AND SER-249 BY GSK3B.
PubMed=1846781; DOI=10.1016/0092-8674(91)90241-P;
Boyle W.J., Smeal T., Defize L.H., Angel P., Woodgett J.R., Karin M.,
Hunter T.;
"Activation of protein kinase C decreases phosphorylation of c-Jun at
sites that negatively regulate its DNA-binding activity.";
Cell 64:573-584(1991).
[9]
PHOSPHORYLATION AT SER-249.
PubMed=8464713; DOI=10.1093/nar/21.5.1289;
Bannister A.J., Gottlieb T.M., Kouzarides T., Jackson S.P.;
"c-Jun is phosphorylated by the DNA-dependent protein kinase in vitro;
definition of the minimal kinase recognition motif.";
Nucleic Acids Res. 21:1289-1295(1993).
[10]
PHOSPHORYLATION BY CAMK4.
PubMed=8855261; DOI=10.1073/pnas.93.20.10803;
Enslen H., Tokumitsu H., Stork P.J., Davis R.J., Soderling T.R.;
"Regulation of mitogen-activated protein kinases by a
calcium/calmodulin-dependent protein kinase cascade.";
Proc. Natl. Acad. Sci. U.S.A. 93:10803-10808(1996).
[11]
INTERACTION WITH TCF20.
PubMed=8663478; DOI=10.1074/jbc.271.30.18231;
Kirstein M., Sanz L., Moscat J., Diaz-Meco M.T., Saus J.;
"Cross-talk between different enhancer elements during mitogenic
induction of the human stromelysin-1 gene.";
J. Biol. Chem. 271:18231-18236(1996).
[12]
INTERACTION WITH COPS5.
PubMed=8837781; DOI=10.1038/383453a0;
Claret F.-X., Hibi M., Dhut S., Toda T., Karin M.;
"A new group of conserved coactivators that increase the specificity
of AP-1 transcription factors.";
Nature 383:453-457(1996).
[13]
IDENTIFICATION AS A COMPONENT OF THE SMAD3/SMAD4/JUN/FOS COMPLEX, AND
INTERACTION WITH SMAD3.
PubMed=9732876; DOI=10.1038/29814;
Zhang Y., Feng X.H., Derynck R.;
"Smad3 and Smad4 cooperate with c-Jun/c-Fos to mediate TGF-beta-
induced transcription.";
Nature 394:909-913(1998).
[14]
INTERACTION WITH SPIB.
PubMed=10196196; DOI=10.1074/jbc.274.16.11115;
Rao S., Matsumura A., Yoon J., Simon M.C.;
"SPI-B activates transcription via a unique proline, serine, and
threonine domain and exhibits DNA binding affinity differences from
PU.1.";
J. Biol. Chem. 274:11115-11124(1999).
[15]
INTERACTION WITH ATF7, AND MUTAGENESIS OF SER-63 AND SER-73.
PubMed=10376527; DOI=10.1038/sj.onc.1202723;
De Graeve F., Bahr A., Sabapathy K.T., Hauss C., Wagner E.F.,
Kedinger C., Chatton B.;
"Role of the ATFa/JNK2 complex in Jun activation.";
Oncogene 18:3491-3500(1999).
[16]
INTERACTION WITH SMAD3 IN THE SMAD3/SMAD4/JUN/FOS COMPLEX,
DNA-BINDING, FUNCTION, AND MUTAGENESIS OF ARG-272.
PubMed=10995748; DOI=10.1074/jbc.M004731200;
Qing J., Zhang Y., Derynck R.;
"Structural and functional characterization of the transforming growth
factor-beta -induced Smad3/c-Jun transcriptional cooperativity.";
J. Biol. Chem. 275:38802-38812(2000).
[17]
ACETYLATION AT LYS-271 BY EP300.
PubMed=11689449; DOI=10.1093/emboj/20.21.6095;
Vries R.G., Prudenziati M., Zwartjes C., Verlaan M., Kalkhoven E.,
Zantema A.;
"A specific lysine in c-Jun is required for transcriptional repression
by E1A and is acetylated by p300.";
EMBO J. 20:6095-6103(2001).
[18]
INTERACTION WITH BATF3.
PubMed=12087103; DOI=10.1074/jbc.M205048200;
Bower K.E., Zeller R.W., Wachsman W., Martinez T., McGuire K.L.;
"Correlation of transcriptional repression by p21(SNFT) with changes
in DNA.NF-AT complex interactions.";
J. Biol. Chem. 277:34967-34977(2002).
[19]
INTERACTION WITH BATF3.
PubMed=15467742; DOI=10.1038/sj.onc.1208109;
Bower K.E., Fritz J.M., McGuire K.L.;
"Transcriptional repression of MMP-1 by p21SNFT and reduced in vitro
invasiveness of hepatocarcinoma cells.";
Oncogene 23:8805-8814(2004).
[20]
PHOSPHORYLATION AT SER-63; SER-73; THR-91 AND THR-93, UBIQUITINATION,
INTERACTION WITH FBXW7, AND MUTAGENESIS OF SER-63; SER-73; THR-91 AND
THR-93.
PubMed=14739463; DOI=10.1126/science.1092880;
Nateri A.S., Riera-Sans L., Da Costa C., Behrens A.;
"The ubiquitin ligase SCFFbw7 antagonizes apoptotic JNK signaling.";
Science 303:1374-1378(2004).
[21]
FUNCTION, AND PHOSPHORYLATION BY HIPK3.
PubMed=17210646; DOI=10.1128/MCB.02253-06;
Lan H.-C., Li H.-J., Lin G., Lai P.-Y., Chung B.-C.;
"Cyclic AMP stimulates SF-1-dependent CYP11A1 expression through
homeodomain-interacting protein kinase 3-mediated Jun N-terminal
kinase and c-Jun phosphorylation.";
Mol. Cell. Biol. 27:2027-2036(2007).
[22]
INTERACTION WITH SP1.
PubMed=16478997; DOI=10.1128/MCB.26.5.1770-1785.2006;
Hung J.J., Wang Y.T., Chang W.C.;
"Sp1 deacetylation induced by phorbol ester recruits p300 to activate
12(S)-lipoxygenase gene transcription.";
Mol. Cell. Biol. 26:1770-1785(2006).
[23]
PHOSPHORYLATION AT SER-63 AND SER-73.
PubMed=17804415; DOI=10.1074/jbc.M702791200;
Wang L., Dai W., Lu L.;
"Stress-induced c-Jun activation mediated by Polo-like kinase 3 in
corneal epithelial cells.";
J. Biol. Chem. 282:32121-32127(2007).
[24]
PHOSPHORYLATION AT SER-63 AND SER-73.
PubMed=18650425; DOI=10.1074/jbc.M801326200;
Wang L., Gao J., Dai W., Lu L.;
"Activation of Polo-like kinase 3 by hypoxic stresses.";
J. Biol. Chem. 283:25928-25935(2008).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-63; THR-239 AND
SER-243, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63 AND SER-243, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[28]
INTERACTION WITH RNF187.
PubMed=20852630; DOI=10.1038/ncb2098;
Davies C.C., Chakraborty A., Cipriani F., Haigh K., Haigh J.J.,
Behrens A.;
"Identification of a co-activator that links growth factor signalling
to c-Jun/AP-1 activation.";
Nat. Cell Biol. 12:963-972(2010).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[30]
PHOSPHORYLATION AT THR-2; THR-8; THR-89; THR-93 AND THR-286, AND
MUTAGENESIS OF THR-2; THR-8; THR-89; THR-93 AND THR-286.
PubMed=21177766; DOI=10.1093/carcin/bgq271;
Li T., Zhang J., Zhu F., Wen W., Zykova T., Li X., Liu K., Peng C.,
Ma W., Shi G., Dong Z., Bode A.M., Dong Z.;
"P21-activated protein kinase (PAK2)-mediated c-Jun phosphorylation at
5 threonine sites promotes cell transformation.";
Carcinogenesis 32:659-666(2011).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58 AND SER-63, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[32]
PHOSPHORYLATION AT SER-243, AND MUTAGENESIS OF SER-243.
PubMed=22307329; DOI=10.1172/JCI60818;
Taira N., Mimoto R., Kurata M., Yamaguchi T., Kitagawa M., Miki Y.,
Yoshida K.;
"DYRK2 priming phosphorylation of c-Jun and c-Myc modulates cell cycle
progression in human cancer cells.";
J. Clin. Invest. 122:859-872(2012).
[33]
INTERACTION WITH RNF187.
PubMed=23624934; DOI=10.1038/emboj.2013.98;
Davies C.C., Chakraborty A., Diefenbacher M.E., Skehel M., Behrens A.;
"Arginine methylation of the c-Jun coactivator RACO-1 is required for
c-Jun/AP-1 activation.";
EMBO J. 32:1556-1567(2013).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63 AND SER-243, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[35]
FUNCTION, AND DNA-BINDING.
PubMed=24623306; DOI=10.7554/eLife.02313;
Serra R.W., Fang M., Park S.M., Hutchinson L., Green M.R.;
"A KRAS-directed transcriptional silencing pathway that mediates the
CpG island methylator phenotype.";
Elife 3:E02313-E02313(2014).
[36]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-35; LYS-50; LYS-56; LYS-70
AND LYS-226, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[37]
X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 257-313 OF COMPLEX WITH FOS.
PubMed=7816143; DOI=10.1038/373257a0;
Glover J.N., Harrison S.C.;
"Crystal structure of the heterodimeric bZIP transcription factor c-
Fos-c-Jun bound to DNA.";
Nature 373:257-261(1995).
[38]
STRUCTURE BY NMR OF 276-314.
PubMed=8662824; DOI=10.1074/jbc.271.23.13663;
Junius F.K., O'Donoghue S.I., Nilges M., Weiss A.S., King G.F.;
"High resolution NMR solution structure of the leucine zipper domain
of the c-Jun homodimer.";
J. Biol. Chem. 271:13663-13667(1996).
-!- FUNCTION: Transcription factor that recognizes and binds to the
enhancer heptamer motif 5'-TGA[CG]TCA-3'. Promotes activity of
NR5A1 when phosphorylated by HIPK3 leading to increased
steroidogenic gene expression upon cAMP signaling pathway
stimulation. Involved in activated KRAS-mediated transcriptional
activation of USP28 in colorectal cancer (CRC) cells
(PubMed:24623306). Binds to the USP28 promoter in colorectal
cancer (CRC) cells (PubMed:24623306).
{ECO:0000269|PubMed:10995748, ECO:0000269|PubMed:17210646,
ECO:0000269|PubMed:24623306}.
-!- SUBUNIT: Heterodimer with either FOS or BATF3 or ATF7. The
ATF7/JUN heterodimer is essential for ATF7 transactivation
activity. Interacts with DSIPI; the interaction inhibits the
binding of active AP1 to its target DNA (By similarity). Interacts
with HIVEP3 and MYBBP1A (By similarity). Interacts with SP1, SPIB
and TCF20. Interacts with COPS5; the interaction leads indirectly
to its phosphorylation. Component of the
SMAD3/SMAD4/JUN/FOS/complex which forms at the AP1 promoter site.
The SMAD3/SMAD4 heterodimer acts synergistically with the JUN/FOS
heterodimer to activate transcription in response to TGF-beta.
Interacts (via its basic DNA binding and leucine zipper domains)
with SMAD3 (via an N-terminal domain); the interaction is required
for TGF-beta-mediated transactivation of the
SMAD3/SMAD4/JUN/FOS/complex. Interacts with methylated RNF187.
Binds to HIPK3. Interacts (when phosphorylated) with FBXW7
(PubMed:14739463). {ECO:0000250, ECO:0000269|PubMed:10196196,
ECO:0000269|PubMed:10376527, ECO:0000269|PubMed:10995748,
ECO:0000269|PubMed:12087103, ECO:0000269|PubMed:14739463,
ECO:0000269|PubMed:15467742, ECO:0000269|PubMed:16478997,
ECO:0000269|PubMed:20852630, ECO:0000269|PubMed:23624934,
ECO:0000269|PubMed:8663478, ECO:0000269|PubMed:8837781,
ECO:0000269|PubMed:9732876}.
-!- INTERACTION:
Self; NbExp=5; IntAct=EBI-852823, EBI-852823;
Q06481:APLP2; NbExp=3; IntAct=EBI-852823, EBI-79306;
P05067:APP; NbExp=2; IntAct=EBI-852823, EBI-77613;
P18846:ATF1; NbExp=2; IntAct=EBI-852823, EBI-852794;
P15336:ATF2; NbExp=14; IntAct=EBI-852823, EBI-1170906;
P18847:ATF3; NbExp=7; IntAct=EBI-852823, EBI-712767;
P18848:ATF4; NbExp=2; IntAct=EBI-852823, EBI-492498;
P17544:ATF7; NbExp=6; IntAct=EBI-852823, EBI-765623;
Q16520:BATF; NbExp=2; IntAct=EBI-852823, EBI-749503;
Q9NR55:BATF3; NbExp=4; IntAct=EBI-852823, EBI-10312707;
Q8IWZ6:BBS7; NbExp=3; IntAct=EBI-852823, EBI-1806001;
Q99966:CITED1; NbExp=2; IntAct=EBI-852823, EBI-2624951;
O43889:CREB3; NbExp=4; IntAct=EBI-852823, EBI-625002;
P14921:ETS1; NbExp=3; IntAct=EBI-852823, EBI-913209;
P01100:FOS; NbExp=32; IntAct=EBI-852823, EBI-852851;
P15407:FOSL1; NbExp=7; IntAct=EBI-852823, EBI-744510;
P15408:FOSL2; NbExp=9; IntAct=EBI-852823, EBI-3893419;
Q9HD26:GOPC; NbExp=3; IntAct=EBI-852823, EBI-349832;
P0C746:HBZ (xeno); NbExp=3; IntAct=EBI-852823, EBI-10890294;
P07900:HSP90AA1; NbExp=4; IntAct=EBI-852823, EBI-296047;
P11142:HSPA8; NbExp=3; IntAct=EBI-852823, EBI-351896;
Q8WQG9:jnk-1 (xeno); NbExp=3; IntAct=EBI-852823, EBI-321822;
P52292:KPNA2; NbExp=4; IntAct=EBI-852823, EBI-349938;
P53779:MAPK10; NbExp=2; IntAct=EBI-852823, EBI-713543;
P45983:MAPK8; NbExp=4; IntAct=EBI-852823, EBI-286483;
P45983-1:MAPK8; NbExp=2; IntAct=EBI-852823, EBI-288687;
Q9UPY8:MAPRE3; NbExp=3; IntAct=EBI-852823, EBI-726739;
P56671:Maz (xeno); NbExp=2; IntAct=EBI-852823, EBI-1809712;
Q00987:MDM2; NbExp=3; IntAct=EBI-852823, EBI-389668;
Q9DGW5:MDV005 (xeno); NbExp=3; IntAct=EBI-852823, EBI-10889526;
P07197:NEFM; NbExp=2; IntAct=EBI-852823, EBI-1105035;
O95644:NFATC1; NbExp=5; IntAct=EBI-852823, EBI-6907210;
Q13469-2:NFATC2; NbExp=6; IntAct=EBI-852823, EBI-10087113;
P48634:PRRC2A; NbExp=2; IntAct=EBI-852823, EBI-347545;
Q15796:SMAD2; NbExp=3; IntAct=EBI-852823, EBI-1040141;
Q9NRL3:STRN4; NbExp=3; IntAct=EBI-852823, EBI-717245;
Q71U36:TUBA1A; NbExp=3; IntAct=EBI-852823, EBI-302552;
P07437:TUBB; NbExp=3; IntAct=EBI-852823, EBI-350864;
Q99986:VRK1; NbExp=5; IntAct=EBI-852823, EBI-1769146;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- PTM: Ubiquitinated by the SCF(FBXW7), leading to its degradation.
Ubiquitination takes place following phosphorylation, that
promotes interaction with FBXW7. {ECO:0000269|PubMed:14739463}.
-!- PTM: Phosphorylated by CaMK4 and PRKDC; phosphorylation enhances
the transcriptional activity. Phosphorylated by HIPK3.
Phosphorylated by DYRK2 at Ser-243; this primes the protein for
subsequent phosphorylation by GSK3B at Thr-239. Phosphorylated at
Thr-239, Ser-243 and Ser-249 by GSK3B; phosphorylation reduces its
ability to bind DNA. Phosphorylated by PAK2 at Thr-2, Thr-8, Thr-
89, Thr-93 and Thr-286 thereby promoting JUN-mediated cell
proliferation and transformation. Phosphorylated by PLK3 following
hypoxia or UV irradiation, leading to increase DNA-binding
activity. {ECO:0000269|PubMed:14739463,
ECO:0000269|PubMed:17210646, ECO:0000269|PubMed:17804415,
ECO:0000269|PubMed:1846781, ECO:0000269|PubMed:18650425,
ECO:0000269|PubMed:21177766, ECO:0000269|PubMed:22307329,
ECO:0000269|PubMed:8464713, ECO:0000269|PubMed:8855261}.
-!- PTM: Acetylated at Lys-271 by EP300.
{ECO:0000269|PubMed:11689449}.
-!- SIMILARITY: Belongs to the bZIP family. Jun subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/JUNID151.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/jun/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; J04111; AAA59197.1; -; Genomic_DNA.
EMBL; CR541724; CAG46525.1; -; mRNA.
EMBL; BT019759; AAV38564.1; -; mRNA.
EMBL; AY217548; AAO22993.1; -; Genomic_DNA.
EMBL; AL136985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC002646; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC006175; AAH06175.1; -; mRNA.
EMBL; BC009874; AAH09874.2; -; mRNA.
EMBL; BC068522; AAH68522.1; -; mRNA.
CCDS; CCDS610.1; -.
PIR; A31264; TVHUJN.
RefSeq; NP_002219.1; NM_002228.3.
UniGene; Hs.696684; -.
PDB; 1A02; X-ray; 2.70 A; J=253-308.
PDB; 1FOS; X-ray; 3.05 A; F/H=254-315.
PDB; 1JNM; X-ray; 2.20 A; A/B=254-315.
PDB; 1JUN; NMR; -; A/B=276-314.
PDB; 1S9K; X-ray; 3.10 A; E=257-308.
PDB; 1T2K; X-ray; 3.00 A; C=254-314.
PDB; 5T01; X-ray; 1.89 A; A/B=254-315.
PDBsum; 1A02; -.
PDBsum; 1FOS; -.
PDBsum; 1JNM; -.
PDBsum; 1JUN; -.
PDBsum; 1S9K; -.
PDBsum; 1T2K; -.
PDBsum; 5T01; -.
ProteinModelPortal; P05412; -.
SMR; P05412; -.
BioGrid; 109928; 234.
DIP; DIP-5961N; -.
ELM; P05412; -.
IntAct; P05412; 1376.
MINT; MINT-105756; -.
STRING; 9606.ENSP00000360266; -.
BindingDB; P05412; -.
ChEMBL; CHEMBL4977; -.
DrugBank; DB01169; Arsenic trioxide.
DrugBank; DB01029; Irbesartan.
DrugBank; DB05785; LGD-1550.
DrugBank; DB00852; Pseudoephedrine.
DrugBank; DB00570; Vinblastine.
iPTMnet; P05412; -.
PhosphoSitePlus; P05412; -.
BioMuta; JUN; -.
DMDM; 135298; -.
EPD; P05412; -.
MaxQB; P05412; -.
PaxDb; P05412; -.
PeptideAtlas; P05412; -.
PRIDE; P05412; -.
DNASU; 3725; -.
Ensembl; ENST00000371222; ENSP00000360266; ENSG00000177606.
GeneID; 3725; -.
KEGG; hsa:3725; -.
UCSC; uc001cze.4; human.
CTD; 3725; -.
DisGeNET; 3725; -.
GeneCards; JUN; -.
H-InvDB; HIX0000635; -.
HGNC; HGNC:6204; JUN.
HPA; CAB003801; -.
HPA; CAB007780; -.
HPA; HPA059474; -.
MIM; 165160; gene.
neXtProt; NX_P05412; -.
OpenTargets; ENSG00000177606; -.
PharmGKB; PA30006; -.
eggNOG; KOG0837; Eukaryota.
eggNOG; ENOG410XRWH; LUCA.
GeneTree; ENSGT00390000009929; -.
HOGENOM; HOG000006648; -.
HOVERGEN; HBG001722; -.
InParanoid; P05412; -.
KO; K04448; -.
OMA; KDHVAQL; -.
OrthoDB; EOG091G0N0L; -.
PhylomeDB; P05412; -.
TreeFam; TF323952; -.
Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
Reactome; R-HSA-450341; Activation of the AP-1 family of transcription factors.
Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
Reactome; R-HSA-8862803; Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models.
SignaLink; P05412; -.
SIGNOR; P05412; -.
ChiTaRS; JUN; human.
EvolutionaryTrace; P05412; -.
GeneWiki; C-jun; -.
GenomeRNAi; 3725; -.
PRO; PR:P05412; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000177606; -.
CleanEx; HS_JUN; -.
Genevisible; P05412; HS.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0000228; C:nuclear chromosome; TAS:ProtInc.
GO; GO:0005719; C:nuclear euchromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
GO; GO:0035976; C:transcription factor AP-1 complex; IDA:CAFA.
GO; GO:0017053; C:transcriptional repressor complex; IEA:Ensembl.
GO; GO:0035497; F:cAMP response element binding; IDA:BHF-UCL.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
GO; GO:0071837; F:HMG box domain binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046982; F:protein heterodimerization activity; IDA:CAFA.
GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
GO; GO:0070412; F:R-SMAD binding; IPI:BHF-UCL.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; IPI:CAFA.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IC:ParkinsonsUK-UCL.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0000982; F:transcription factor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IMP:BHF-UCL.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; IDA:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0008134; F:transcription factor binding; IPI:BHF-UCL.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IEA:Ensembl.
GO; GO:0001190; F:transcriptional activator activity, RNA polymerase II transcription factor binding; IC:BHF-UCL.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
GO; GO:0031103; P:axon regeneration; IEA:Ensembl.
GO; GO:0071276; P:cellular response to cadmium ion; IMP:CAFA.
GO; GO:0071277; P:cellular response to calcium ion; IEA:Ensembl.
GO; GO:0032870; P:cellular response to hormone stimulus; IBA:GO_Central.
GO; GO:0051365; P:cellular response to potassium ion starvation; IEA:Ensembl.
GO; GO:0034614; P:cellular response to reactive oxygen species; IMP:CAFA.
GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
GO; GO:0061029; P:eyelid development in camera-type eye; IEA:Ensembl.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0035026; P:leading edge cell differentiation; IEA:Ensembl.
GO; GO:0007612; P:learning; IEA:Ensembl.
GO; GO:0001889; P:liver development; IEA:Ensembl.
GO; GO:0051899; P:membrane depolarization; IEA:Ensembl.
GO; GO:0001774; P:microglial cell activation; IEA:Ensembl.
GO; GO:0030224; P:monocyte differentiation; IEA:Ensembl.
GO; GO:0043922; P:negative regulation by host of viral transcription; IDA:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0043392; P:negative regulation of DNA binding; IDA:UniProtKB.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0031953; P:negative regulation of protein autophosphorylation; IEA:Ensembl.
GO; GO:1990441; P:negative regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; IMP:ParkinsonsUK-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0003151; P:outflow tract morphogenesis; IEA:Ensembl.
GO; GO:0043923; P:positive regulation by host of viral transcription; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:CAFA.
GO; GO:0045597; P:positive regulation of cell differentiation; IBA:GO_Central.
GO; GO:0045740; P:positive regulation of DNA replication; IEA:Ensembl.
GO; GO:2000144; P:positive regulation of DNA-templated transcription, initiation; IDA:CACAO.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl.
GO; GO:0010634; P:positive regulation of epithelial cell migration; IEA:Ensembl.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
GO; GO:0045657; P:positive regulation of monocyte differentiation; IEA:Ensembl.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0007265; P:Ras protein signal transduction; IDA:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0051090; P:regulation of sequence-specific DNA binding transcription factor activity; TAS:Reactome.
GO; GO:0001836; P:release of cytochrome c from mitochondria; IEA:Ensembl.
GO; GO:0051591; P:response to cAMP; IBA:GO_Central.
GO; GO:0034097; P:response to cytokine; IBA:GO_Central.
GO; GO:0042493; P:response to drug; IBA:GO_Central.
GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IBA:GO_Central.
GO; GO:0009612; P:response to mechanical stimulus; IBA:GO_Central.
GO; GO:0035994; P:response to muscle stretch; IEA:Ensembl.
GO; GO:0009314; P:response to radiation; IBA:GO_Central.
GO; GO:0007184; P:SMAD protein import into nucleus; IDA:BHF-UCL.
GO; GO:0060395; P:SMAD protein signal transduction; IDA:BHF-UCL.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL.
InterPro; IPR004827; bZIP.
InterPro; IPR015558; C_Jun/v-Jun.
InterPro; IPR005643; JNK.
InterPro; IPR002112; Leuzip_Jun.
InterPro; IPR008917; TF_DNA-bd.
PANTHER; PTHR11462:SF43; PTHR11462:SF43; 1.
Pfam; PF00170; bZIP_1; 1.
Pfam; PF03957; Jun; 1.
PRINTS; PR00043; LEUZIPPRJUN.
SMART; SM00338; BRLZ; 1.
SUPFAM; SSF47454; SSF47454; 1.
PROSITE; PS50217; BZIP; 1.
PROSITE; PS00036; BZIP_BASIC; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Complete proteome;
Direct protein sequencing; DNA-binding; Isopeptide bond; Nucleus;
Phosphoprotein; Polymorphism; Proto-oncogene; Reference proteome;
Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 331 Transcription factor AP-1.
/FTId=PRO_0000076429.
DOMAIN 252 315 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 252 279 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 280 308 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
SITE 272 272 Necessary for synergistic transcriptional
activity with SMAD3.
MOD_RES 2 2 Phosphothreonine; by PAK2.
{ECO:0000269|PubMed:21177766}.
MOD_RES 8 8 Phosphothreonine; by PAK2.
{ECO:0000269|PubMed:21177766}.
MOD_RES 56 56 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P05627}.
MOD_RES 58 58 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 63 63 Phosphoserine; by MAPK8 and PLK3.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:14739463,
ECO:0000269|PubMed:17804415,
ECO:0000269|PubMed:18650425}.
MOD_RES 73 73 Phosphoserine; by MAPK8 and PLK3.
{ECO:0000269|PubMed:14739463,
ECO:0000269|PubMed:17804415,
ECO:0000269|PubMed:18650425}.
MOD_RES 89 89 Phosphothreonine; by PAK2.
{ECO:0000269|PubMed:21177766}.
MOD_RES 91 91 Phosphothreonine.
{ECO:0000269|PubMed:14739463}.
MOD_RES 93 93 Phosphothreonine; by PAK2.
{ECO:0000269|PubMed:14739463,
ECO:0000269|PubMed:21177766}.
MOD_RES 239 239 Phosphothreonine; by GSK3-beta.
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:1846781}.
MOD_RES 243 243 Phosphoserine; by DYRK2 and GSK3-beta.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:1846781,
ECO:0000269|PubMed:22307329}.
MOD_RES 249 249 Phosphoserine; by GSK3-beta.
{ECO:0000269|PubMed:1846781,
ECO:0000269|PubMed:8464713}.
MOD_RES 271 271 N6-acetyllysine.
{ECO:0000269|PubMed:11689449}.
MOD_RES 286 286 Phosphothreonine; by PAK2.
{ECO:0000269|PubMed:21177766}.
CROSSLNK 35 35 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 50 50 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 56 56 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 70 70 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 226 226 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 297 297 T -> M (in dbSNP:rs9989).
/FTId=VAR_012070.
MUTAGEN 2 2 T->A: Complete loss of PAK2-mediated
phosphorylation; when associated with A-
8; A-89; A-93; and A-286.
{ECO:0000269|PubMed:21177766}.
MUTAGEN 8 8 T->A: Complete loss of PAK2-mediated
phosphorylation; when associated with A-
2; A-89; A-93; and A-286.
{ECO:0000269|PubMed:21177766}.
MUTAGEN 63 63 S->A: Greatly reduced ATF7-mediated
transcriptional activity; when associated
with A-73. Abolishes interaction with
FBXW7; when associated with A-73; A-91
and A-93. {ECO:0000269|PubMed:10376527,
ECO:0000269|PubMed:14739463}.
MUTAGEN 73 73 S->A: Greatly reduced ATF7-mediated
transcriptional activity; when associated
with A-63. Abolishes interaction with
FBXW7; when associated with A-63; A-91
and A-93. {ECO:0000269|PubMed:10376527,
ECO:0000269|PubMed:14739463}.
MUTAGEN 89 89 T->A: Complete loss of PAK2-mediated
phosphorylation; when associated with A-
2; A-8; A-93; and A-286.
{ECO:0000269|PubMed:21177766}.
MUTAGEN 91 91 T->A: Abolishes interaction with FBXW7;
when associated with A-63; A-73 and A-93.
{ECO:0000269|PubMed:14739463}.
MUTAGEN 93 93 T->A: Abolishes interaction with FBXW7;
when associated with A-63; A-73 and A-91.
{ECO:0000269|PubMed:14739463}.
MUTAGEN 93 93 T->A: Complete loss of PAK2-mediated
phosphorylation; when associated with A-
2; A-8; A-89; and A-286.
{ECO:0000269|PubMed:21177766}.
MUTAGEN 243 243 S->A: Abolishes phosphorylation by DYRK2.
Abolishes phosphorylation by GSK3B at
Thr-239. {ECO:0000269|PubMed:22307329}.
MUTAGEN 272 272 R->V: Abolishes the synergistic activity
with SMAD3 to activate TGF-beta-mediated
transcription.
{ECO:0000269|PubMed:10995748}.
MUTAGEN 286 286 T->A: Complete loss of PAK2-mediated
phosphorylation; when associated with A-
2; A-8; A-89; and A-93.
{ECO:0000269|PubMed:21177766}.
CONFLICT 11 11 D -> G (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 14 14 L -> F (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 80 80 I -> V (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 151 151 A -> S (in Ref. 3; CAG46525).
{ECO:0000305}.
HELIX 255 310 {ECO:0000244|PDB:5T01}.
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


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GENTAUR France SARL
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Tel 01 43 25 01 50

Fax 01 43 25 01 60
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BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

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GENTAUR GmbH
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Support Karolina Elandt
Tel: 0035929830070
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San Jose, CA 95123
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Tel (408) 780-0908,
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Genprice Inc, Invoices and accounting
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GENTAUR Poland Sp. z o.o.


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