HCSGD entry for JUN

1. General information

Official gene symbolJUN
Entrez ID3725
Gene full namejun proto-oncogene
Other gene symbolsAP-1 AP1 c-Jun
Links to Entrez GeneLinks to Entrez Gene

2. Neighbors in the network

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3. Gene ontology annotation

GO ID

GO term

Evidence

Category

GO:0000228Nuclear chromosomeTAScellular_component
GO:0000980RNA polymerase II distal enhancer sequence-specific DNA bindingIDAmolecular_function
GO:0001077RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcriptionIEAmolecular_function
GO:0001102RNA polymerase II activating transcription factor bindingIPImolecular_function
GO:0001190RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcriptionICmolecular_function
GO:0001525AngiogenesisIEAbiological_process
GO:0001774Microglial cell activationIEAbiological_process
GO:0001836Release of cytochrome c from mitochondriaIEAbiological_process
GO:0001889Liver developmentIEAbiological_process
GO:0001938Positive regulation of endothelial cell proliferationIEAbiological_process
GO:0002224Toll-like receptor signaling pathwayTASbiological_process
GO:0002755MyD88-dependent toll-like receptor signaling pathwayTASbiological_process
GO:0002756MyD88-independent toll-like receptor signaling pathwayTASbiological_process
GO:0003151Outflow tract morphogenesisIEAbiological_process
GO:0003677DNA bindingTASmolecular_function
GO:0003690Double-stranded DNA bindingIEAmolecular_function
GO:0003700Sequence-specific DNA binding transcription factor activityIDAmolecular_function
GO:0003705RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activityIC IDAmolecular_function
GO:0003713Transcription coactivator activityIDAmolecular_function
GO:0005100Rho GTPase activator activityIDAmolecular_function
GO:0005515Protein bindingIPImolecular_function
GO:0005654NucleoplasmTAScellular_component
GO:0005667Transcription factor complexIEAcellular_component
GO:0005719Nuclear euchromatinIDAcellular_component
GO:0005829CytosolIEAcellular_component
GO:0007179Transforming growth factor beta receptor signaling pathwayIDAbiological_process
GO:0007184SMAD protein import into nucleusIDAbiological_process
GO:0007568AgingIEAbiological_process
GO:0007612LearningIEAbiological_process
GO:0007623Circadian rhythmIEAbiological_process
GO:0008134Transcription factor bindingIPImolecular_function
GO:0008285Negative regulation of cell proliferationIEAbiological_process
GO:0009314Response to radiationIEAbiological_process
GO:0009612Response to mechanical stimulusIEAbiological_process
GO:0017053Transcriptional repressor complexIEAcellular_component
GO:0030224Monocyte differentiationIEAbiological_process
GO:0031103Axon regenerationIEAbiological_process
GO:0031953Negative regulation of protein autophosphorylationIEAbiological_process
GO:0032320Positive regulation of Ras GTPase activityIDAbiological_process
GO:0032321Positive regulation of Rho GTPase activityIDAbiological_process
GO:0032496Response to lipopolysaccharideIEAbiological_process
GO:0034097Response to cytokineIEAbiological_process
GO:0034134Toll-like receptor 2 signaling pathwayTASbiological_process
GO:0034138Toll-like receptor 3 signaling pathwayTASbiological_process
GO:0034142Toll-like receptor 4 signaling pathwayTASbiological_process
GO:0034146Toll-like receptor 5 signaling pathwayTASbiological_process
GO:0034162Toll-like receptor 9 signaling pathwayTASbiological_process
GO:0034166Toll-like receptor 10 signaling pathwayTASbiological_process
GO:0035026Leading edge cell differentiationIEAbiological_process
GO:0035497CAMP response element bindingIDAmolecular_function
GO:0035666TRIF-dependent toll-like receptor signaling pathwayTASbiological_process
GO:0038095Fc-epsilon receptor signaling pathwayTASbiological_process
GO:0038123Toll-like receptor TLR1:TLR2 signaling pathwayTASbiological_process
GO:0038124Toll-like receptor TLR6:TLR2 signaling pathwayTASbiological_process
GO:0042493Response to drugIEAbiological_process
GO:0042542Response to hydrogen peroxideIEAbiological_process
GO:0043085Positive regulation of catalytic activityIDAbiological_process
GO:0043392Negative regulation of DNA bindingIDAbiological_process
GO:0043524Negative regulation of neuron apoptotic processIEAbiological_process
GO:0043525Positive regulation of neuron apoptotic processIEAbiological_process
GO:0043547Positive regulation of GTPase activityIDAbiological_process
GO:0043922Negative regulation by host of viral transcriptionIDAbiological_process
GO:0043923Positive regulation by host of viral transcriptionIDAbiological_process
GO:0044212Transcription regulatory region DNA bindingIDAmolecular_function
GO:0045087Innate immune responseTASbiological_process
GO:0045657Positive regulation of monocyte differentiationIEAbiological_process
GO:0045740Positive regulation of DNA replicationIEAbiological_process
GO:0045892Negative regulation of transcription, DNA-templatedIDAbiological_process
GO:0045893Positive regulation of transcription, DNA-templatedIDAbiological_process
GO:0045944Positive regulation of transcription from RNA polymerase II promoterIC IDAbiological_process
GO:0048146Positive regulation of fibroblast proliferationIEAbiological_process
GO:0048661Positive regulation of smooth muscle cell proliferationIEAbiological_process
GO:0050790Regulation of catalytic activityIDAbiological_process
GO:0051090Regulation of sequence-specific DNA binding transcription factor activityTASbiological_process
GO:0051365Cellular response to potassium ion starvationIEAbiological_process
GO:0051403Stress-activated MAPK cascadeTASbiological_process
GO:0051591Response to cAMPIEAbiological_process
GO:0051726Regulation of cell cycleIEAbiological_process
GO:0051899Membrane depolarizationIEAbiological_process
GO:0060395SMAD protein signal transductionIDAbiological_process
GO:0070412R-SMAD bindingIPImolecular_function
GO:0071277Cellular response to calcium ionIEAbiological_process
GO:0071837HMG box domain bindingIEAmolecular_function
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4. Expression levels in datasets

  • Meta-analysis result

p-value upp-value downFDR upFDR down
0.01906306750.46556986060.33652515091.0000000000

  • Individual experiment result
    ( "-" represent NA in the specific microarray platform )

Data sourceUp or downLog fold change
GSE11954Down-0.0008256744
GSE13712_SHEARUp0.7208044301
GSE13712_STATICUp0.6552964935
GSE19018Down-0.3227193388
GSE19899_A1Up0.7872152596
GSE19899_A2Up0.4102989824
PubMed_21979375_A1Up1.0626368118
PubMed_21979375_A2Up0.5265359149
GSE35957Up0.1418683586
GSE36640Down-0.2512815236
GSE54402Up0.2637571402
GSE9593Up0.1897745913
GSE43922Up0.3504350993
GSE24585Down-1.1018367898
GSE37065Up0.1652378868
GSE28863_A1Down-0.0441959953
GSE28863_A2Up0.4079855711
GSE28863_A3Down-0.4451947901
GSE28863_A4Down-0.0912751982
GSE48662Up0.3954886152

5. Regulation relationships with compounds/drugs/microRNAs

  • Compounds

Compound

Target

Confidence score

Uniprot

CHEMBL248370CHEMBL49779P05412
CHEMBL245535CHEMBL49779P05412
CHEMBL392613CHEMBL49779P05412
CHEMBL424872CHEMBL49779P05412
CHEMBL246545CHEMBL49779P05412
CHEMBL246544CHEMBL49779P05412
CHEMBL248176CHEMBL49779P05412
CHEMBL245732CHEMBL49779P05412
CHEMBL250474CHEMBL49779P05412
CHEMBL246543CHEMBL49779P05412
CHEMBL392615CHEMBL49779P05412
CHEMBL245724CHEMBL49779P05412
CHEMBL245335CHEMBL49779P05412
CHEMBL398325CHEMBL49779P05412
CHEMBL393659CHEMBL49779P05412
CHEMBL245725CHEMBL49779P05412
CHEMBL392614CHEMBL49779P05412
CHEMBL245334CHEMBL49779P05412
CHEMBL393861CHEMBL49779P05412
CHEMBL245935CHEMBL49779P05412
CHEMBL399454CHEMBL49779P05412
CHEMBL245534CHEMBL49779P05412
CHEMBL245936CHEMBL49779P05412
CHEMBL391794CHEMBL49779P05412
CHEMBL245733CHEMBL49779P05412
CHEMBL250854CHEMBL49779P05412
CHEMBL245336CHEMBL49779P05412
CHEMBL397531CHEMBL49779P05412
CHEMBL1767254CHEMBL49779P05412
CHEMBL261237CHEMBL49778P05412
CHEMBL515276CHEMBL49778P05412
CHEMBL1765575CHEMBL49778P05412
CHEMBL1761567CHEMBL49778P05412
CHEMBL1761584CHEMBL49778P05412
CHEMBL485904CHEMBL49778P05412
CHEMBL1761565CHEMBL49778P05412
CHEMBL1761583CHEMBL49778P05412
CHEMBL1093503CHEMBL49778P05412
CHEMBL128708CHEMBL49778P05412
CHEMBL1242520CHEMBL49778P05412
CHEMBL1761582CHEMBL49778P05412
CHEMBL1761554CHEMBL49778P05412
CHEMBL1761575CHEMBL49778P05412
CHEMBL1765574CHEMBL49778P05412
CHEMBL1761577CHEMBL49778P05412
CHEMBL564009CHEMBL49778P05412
CHEMBL1761566CHEMBL49778P05412
CHEMBL340779CHEMBL49778P05412
CHEMBL1761579CHEMBL49778P05412
CHEMBL423150CHEMBL49778P05412
CHEMBL131006CHEMBL49778P05412
CHEMBL458347CHEMBL49778P05412
CHEMBL340410CHEMBL49778P05412
CHEMBL337656CHEMBL49778P05412
CHEMBL1761568CHEMBL49778P05412
CHEMBL1761555CHEMBL49778P05412
CHEMBL1241534CHEMBL49778P05412
CHEMBL262514CHEMBL49778P05412
CHEMBL1761564CHEMBL49778P05412
CHEMBL485904CHEMBL49778P05412
CHEMBL128599CHEMBL49778P05412
CHEMBL487336CHEMBL49778P05412
CHEMBL339462CHEMBL49778P05412
CHEMBL1242519CHEMBL49778P05412
CHEMBL1242070CHEMBL49778P05412
CHEMBL132495CHEMBL49778P05412
CHEMBL474718CHEMBL49778P05412
CHEMBL487194CHEMBL49778P05412
CHEMBL458347CHEMBL49778P05412
CHEMBL1761562CHEMBL49778P05412
CHEMBL1761581CHEMBL49778P05412
CHEMBL1761569CHEMBL49778P05412
CHEMBL338934CHEMBL49778P05412
CHEMBL1761578CHEMBL49778P05412
CHEMBL1807644CHEMBL49778P05412
CHEMBL487336CHEMBL49778P05412
CHEMBL1761576CHEMBL49778P05412
CHEMBL1761572CHEMBL49778P05412
CHEMBL421280CHEMBL49778P05412
CHEMBL336546CHEMBL49778P05412
CHEMBL1761570CHEMBL49778P05412
CHEMBL1761563CHEMBL49778P05412
CHEMBL1761561CHEMBL49778P05412
CHEMBL186393CHEMBL49777P05412
CHEMBL186600CHEMBL49777P05412
CHEMBL199325CHEMBL49774P05412
CHEMBL371446CHEMBL49774P05412
CHEMBL200061CHEMBL49774P05412
CHEMBL426477CHEMBL49774P05412
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  • Drugs

Name

Drug

Accession number

VinblastineDB00570 APRD00708
IrbesartanDB01029 APRD00413
LGD-1550DB05785 -

  • MicroRNAs

  • mirTarBase

MiRNA_name

mirBase ID

miRTarBase ID

Experiment

Support type

References (Pubmed ID)

hsa-miR-16-5pMIMAT0000069MIRT000867MicroarrayFunctional MTI (Weak)18362358
hsa-miR-15a-5pMIMAT0000068MIRT000868MicroarrayFunctional MTI (Weak)18362358
hsa-miR-155-5pMIMAT0000646MIRT006208Luciferase reporter assay//qRT-PCR//Western blotFunctional MTI22508041
hsa-miR-30a-5pMIMAT0000087MIRT005128pSILAC//Proteomics;OtherFunctional MTI (Weak)18668040
hsa-miR-29c-3pMIMAT0000681MIRT020367SequencingFunctional MTI (Weak)20371350
hsa-miR-101-3pMIMAT0000099MIRT027318SequencingFunctional MTI (Weak)20371350
hsa-miR-26b-5pMIMAT0000083MIRT029641MicroarrayFunctional MTI (Weak)19088304
hsa-miR-342-3pMIMAT0000753MIRT043728CLASHFunctional MTI (Weak)23622248
hsa-miR-149-5pMIMAT0000450MIRT045693CLASHFunctional MTI (Weak)23622248
hsa-miR-93-5pMIMAT0000093MIRT048821CLASHFunctional MTI (Weak)23622248
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  • mirRecord

MicroRNA name

mirBase ID

Target site number

MiRNA mature ID

Test method inter

MiRNA regulation site

Reporter target site

Pubmed ID

hsa-miR-15a-5pMIMAT0000068NAhsa-miR-15a18362358
hsa-miR-16-5pMIMAT0000069NAhsa-miR-1618362358
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6. Text-mining results about the gene

Gene occurances in abstracts of cellular senescence-associated articles: 34 abstracts the gene occurs.


PubMed ID of the article

Sentenece the gene occurs

27127888Only PLAU, JUN, and FOS were related to DNA damage, telomere dysfunction-induced aging markers, neutrophil function and IgA nephropathy
24984152In this study, we have shown that HKa induces EPC senescence via stimulation of c-Jun N-terminal kinases (JNK)-related pathway
21850009A146T mutants had weaker effects on downstream c-Jun N-terminal kinase signaling than did codon 12 or 13 mutants
21736542Jun dimerization protein 2 in oxygen restriction; control of senescence
21736542Transcription factor Jun dimerization protein 2 (JDP2) which binds directly to histones and DNA, inhibits the acetylation and methylation of core histones and of reconstituted nucleosomes that contain JDP2-recognition DNA sequences
21507983In normal CEF, the expression of a dominant negative mutant of c-Jun (TAM67) induced senescence
21507983The downregulation of c-Jun expression by short hairpin RNA (shRNA) induced senescence in normal and v-Src-transformed cells
21289643In this study we report that c-Jun was activated in human squamous cell carcinoma (SCC) and coexpression of c-Jun with oncogenic Ras was sufficient to transform primary human epidermal cells into malignancy in a regenerated human skin grafting model
21289643Conversely, the dominant-negative JunB mutant (DNJunB) promoted tumorigenesis, which is in contrast to the tumor-suppressor function of the corresponding c-Jun mutant
21289643These findings indicate that JunB and c-Jun differentially regulate cell growth and differentiation and induce opposite effects on epidermal neoplasia
21212468Zfra (zinc finger-like protein that regulates apoptosis) is a naturally occurring short peptide consisting of 31 amino acids, which regulates tumor necrosis factor (TNF)-mediated cell death by interacting with receptor adaptor protein TRADD (TNF receptorassociated death domain protein) and downstream JNK (c-Jun N-terminal kinase), NF-kappaB (Nuclear factor kappa B) and WWOX/WOX1 (WW domain-containing oxidoreductase)
21197464Jun dimerization protein 2 controls senescence and differentiation via regulating histone modification
21197464Transcription factor, Jun dimerization protein 2 (JDP2), binds directly to histones and DNAs and then inhibits the p300-mediated acetylation both of core histones and of reconstituted nucleosomes that contain JDP2 recognition DNA sequences
20959475BRAF(V600E) signaling through mitogen-activated protein kinase/extracellular signal-regulated kinase kinase resulted in increased reactive oxygen species levels and c-Jun NH(2) terminal kinase-mediated activation of FOXO4 via its phosphorylation on Thr(223), Ser(226), Thr(447), and Thr(451)
20950777Histone chaperone Jun dimerization protein 2 (JDP2): role in cellular senescence and aging
20950777Transcription factor Jun dimerization protein 2 (JDP2) binds directly to histones and DNA, and inhibits p300-mediated acetylation of core histones and reconstituted nucleosomes that contain JDP2-recognition DNA sequences
25961985Here, we summarize the molecular mechanisms that mediate cellular aging and introduce the Jun dimerization protein 2 (JDP2) as a factor that regulates replicative senescence by mediating dissociation of PRCs from the p16Ink4a/Arf locus
20354187The c-Jun NH2-terminal kinase 2 plays a dominant role in human epidermal neoplasia
20354187The c-Jun NH(2)-terminal kinase (JNK) signaling cascade has been implicated in a wide range of diseases, including cancer
20300111Jun and JunD-dependent functions in cell proliferation and stress response
20300111Jun is essential for fetal development, as fetuses lacking Jun die at mid-gestation with multiple cellular defects in liver and heart
20300111Embryos expressing JunD in place of Jun (Jun(d/d)) can develop to term with normal fetal livers, but display cardiac defects as observed in fetuses lacking Jun
20300111Thus, JunD cannot functionally replace Jun in regulating fibroblast proliferation
20300111These data show that Jun is of critical importance for cellular protection against oxidative stress in fetal livers and fibroblasts, and Jun-dependent cellular senescence can be restored by activation of the epidermal growth factor receptor pathway
18316603The stress-induced translocation of alternative reading frame (ARF) is JNK dependent and mediated by two activator proteins, c-Jun and JunB
18316603Thr(91) and Thr(93) of c-Jun are required for the translocation, but the transcriptional activity of c-Jun is dispensable
18316603Instead, c-Jun interacts with B23 in a dose-dependent manner
18316603Hence, we suggest that c-Jun translocates B23 and ARF from the nucleolus after JNK activation by means of protein interactions
18316603In senescent cells, JNK activity and c-Jun levels are reduced concomitantly with ARF nucleolar accumulation, and UV radiation does not cause the translocation of ARF
17339605Instead, the transcriptional activation of IFI16 gene by TSA treatment of LNCaP cells was dependent on transcriptional activation by c-Jun/activator protein-1 transcription factor
17126817Inducible overexpression of c-Jun in MCF7 cells causes resistance to vinblastine via inhibition of drug-induced apoptosis and senescence at a step subsequent to mitotic arrest
17126817Treatment of a wide variety of cells with the microtubule inhibitor vinblastine leads to a robust increase in c-Jun expression, JNK-mediated c-Jun phosphorylation, and activation of AP-1-dependent transcription
17126817However, the role of c-Jun induction in the response of cells to vinblastine remains obscure
17126817Vinblastine-induced cell death was not affected by TAM-67 expression whereas cells were protected by c-Jun overexpression
17126817Further investigation revealed that apoptotic and senescent cells were observed after vinblastine treatment and that both outcomes were strongly inhibited by c-Jun overexpression
17126817Although c-Jun expression inhibited cell death, it did not affect the ability of vinblastine to induce mitotic arrest
17126817These results indicate that c-Jun expression plays a protective role in the cellular response to vinblastine and operates post-mitotic block to inhibit drug-induced apoptosis and senescence
15780767Several proteasome-regulated proapoptotic proteins, including c-Jun (2
15520191Ceramide promotes apoptosis in lung cancer-derived A549 cells by a mechanism involving c-Jun NH2-terminal kinase
15520191Ceramide is known to potently activate a number of stress-regulated enzymes, including the c-Jun NH(2)-terminal kinase (JNK)
15520191To understand which JNK-mediated pathway may be involved, a number of JNK target proteins were examined, including the transcription factor, c-Jun, and the apoptotic regulatory proteins Bcl-X(L) and Bim
15520191A549 cells exhibited basal levels of phosphorylated c-Jun in nuclear fractions, revealing that active c-Jun is present in these cells
15520191Ceramide was found to inhibit c-Jun phosphorylation, suggesting that JNK-mediated phosphorylation of c-Jun is not likely involved in ceramide-induced apoptosis
15520191Ceramide-mediated changes in localization of JNK were consistent with the observed changes in phosphorylation status of c-Jun and Bim
15333603To investigate passage-dependent molecular events in endometrial cells, the c-jun and pp38 levels were examined
15333603Both c-jun and pp38 were significantly reduced with cellular aging and passages
15333603To understand the role of c-jun, endometrial stromal cells were treated with SP600125 which is a specific inhibitor of c-jun
15333603In addition, an immortalized endometrial cell line was established and shown to express activated c-jun, similiar to normal endometrial cells
15107616The c-Jun N-terminal kinase (JNK/SAPK) signaling cascade controls a spectrum of cellular processes, including cell growth, differentiation, transformation, and apoptosis
15107616We further explored other molecules involved in JNK pathway and found that both MKK4, another direct activator of JNK, and c-Jun, a direct substrate of JNK, have similar roles to MKK7
15039780Similarly, loss of c-Jun or expression of a c-JunAA mutant in which the JNK phosphorylation sites were replaced with alanine results in a G2/M cell-cycle block
12470828The accumulation of ROS in senescent cells may be related to the constitutive activation of Jun kinase
11781307Finally, we demonstrated that c-Jun expression overcame the suppression and resultant enhancement of p21 protein level in response to DNER
11480555Ceramide activates stress-activated protein kinases like c-jun N-terminal kinase (JNK) and thus affects transcription pathways involving c-jun
10982848Mitochondrial metabolism of pyruvate is demonstrated to activate the c-Jun N-terminal kinase (JNK)
10951233Transcription factor c-Jun, which is activated by stress-activated MAP kinases and promotes expression of connective-tissue-degrading matrix metalloproteinases, was elevated 2-fold in old skin compared with young skin
8853900However, serum-stimulated myotubes display a typical immediate-early response, including the up-regulation of c-fos, c-jun, c-myc, and ld-1
8934878These included c-fos, c-jun, Id-1, Id-2, E2F-1, and cdc2
7616677Senescent cells showed the strong transcriptional repressions of early serum responsive genes (c-fos, c-jun, c-myc), late responsive genes of transcription factor E2F1 and cyclin E
7908266DNA synthesis and Fos and Jun protein expression in mitotic and postmitotic WI-38 fibroblasts in vitro
7908266DNA synthesis of mitotic and postmitotic WI-38 cell populations may be regulated by the expression of Fos and Jun proteins
7908266The Fos level of MFs was higher by a factor of 15-24 and the Jun level of MFs by a factor of 4
79082665 times higher and the Jun level 1
7684831Likewise, expression of fra-1, c-jun and junB continued to be high in serum-stimulated senescent cells, while induction of fosB was reduced approximately fivefold
1426249There were no differences in c-jun expression and formation of other transcription factors (AP-2 and AP-3) between lymphocytes isolated from old and young mice
1297331We find that cyclin A and p34cdc2 expression is decreased by two- to four-fold in old fibroblasts, but that Fos expression and binding activity are reduced by as much as 95% in old, as opposed to young cells, despite equivalent amounts of p105Rb and Jun proteins being expressed
1560044In this study we have found that both c-jun and jun B, partners of c-fos in heterodimeric transactivating complexes, are equivalently expressed in young and senescent cells at both early (1-6 hr) and late (12 or 16 hr) time points following serum stimulation of quiescent cells
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