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Details on Person UniProt:P05412 JUN
| Class:Id | ReferenceGeneProduct:50080 |
|---|---|
| _chainChangeLog | chain:1-331 added on Fri February 6 2015 |
| _displayName | UniProt:P05412 JUN |
| _timestamp | 2024-11-03 19:51:47 |
| chain | chain:1-331 |
| checksum | 0695E23AC4D33561 |
| comment | FUNCTION Transcription factor that recognizes and binds to the AP-1 consensus motif 5'-TGA[GC]TCA-3' (PubMed:10995748, PubMed:22083952). Heterodimerizes with proteins of the FOS family to form an AP-1 transcription complex, thereby enhancing its DNA binding activity to the AP-1 consensus sequence 5'-TGA[GC]TCA-3' and enhancing its transcriptional activity (By similarity). Together with FOSB, plays a role in activation-induced cell death of T cells by binding to the AP-1 promoter site of FASLG/CD95L, and inducing its transcription in response to activation of the TCR/CD3 signaling pathway (PubMed:12618758). Promotes activity of NR5A1 when phosphorylated by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation (PubMed:17210646). 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).FUNCTION (Microbial infection) Upon Epstein-Barr virus (EBV) infection, binds to viral BZLF1 Z promoter and activates viral BZLF1 expression.SUBUNIT Heterodimer with either BATF3 or ATF7 (PubMed:10376527, PubMed:12087103, PubMed:15467742). Heterodimer with FOS (By similarity). Heterodimer with FOSB isoform 1 and 2 (By similarity). Component of an AP-1 transcription factor complex composed of JUN-FOS heterodimers (By similarity). As part of the AP-1 transcription factor complex, forms heterodimers with FOSB, thereby binding to the AP-1 consensus sequence and stimulating transcription (By similarity). Interacts with FOS and FOSB isoform 1 and 2 (By similarity). The ATF7/JUN heterodimer is essential for ATF7 transactivation activity (PubMed:10376527). Interacts with TSC22D3 (via N-terminus); 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 (PubMed:10196196, PubMed:16478997, PubMed:8663478). Interacts with COPS5; the interaction leads indirectly to its phosphorylation (PubMed:8837781). Component of the SMAD3/SMAD4/JUN/FOS/complex which forms at the AP1 promoter site (PubMed:10995748). The SMAD3/SMAD4 heterodimer acts synergistically with the JUN/FOS heterodimer to activate transcription in response to TGF-beta (PubMed:9732876). 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 (PubMed:10995748). Interacts with methylated RNF187 (PubMed:20852630, PubMed:23624934). Binds to HIPK3. Interacts (when phosphorylated) with FBXW7 (PubMed:14739463). Found in a complex with PRR7 and FBXW7 (PubMed:27458189). Interacts with PRR7 and FBXW7; the interaction inhibits ubiquitination-mediated JUN degradation promoting its phosphorylation and transcriptional activity (PubMed:27458189). Interacts with RBM39 (By similarity). Interacts with PAGE4 (PubMed:24263171, PubMed:24559171, PubMed:26242913). Interacts with ARK2N and CSNK2B; the interaction with ARK2N is mediated by CSNK2B (PubMed:31341047).INTERACTION Expressed in the developing and adult prostate and prostate cancer cells.PTM Ubiquitinated by the SCF(FBXW7), leading to its degradation (PubMed:14739463, PubMed:27458189). Ubiquitination takes place following phosphorylation, that promotes interaction with FBXW7 (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. Phosphorylated by VRK1 (PubMed:31527692).PTM Acetylated at Lys-271 by EP300.SIMILARITY Belongs to the bZIP family. Jun subfamily. |
| description | recommendedName: fullName evidence="34"Transcription factor Jun alternativeName: Activator protein 1 shortName: AP1 alternativeName: Proto-oncogene c-Jun alternativeName: fullName evidence="34"Transcription factor AP-1 subunit Jun alternativeName: V-jun avian sarcoma virus 17 oncogene homolog alternativeName: p39 |
| geneName | JUN |
| identifier | P05412 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Acetylation Activator Direct protein sequencing DNA-binding Isopeptide bond Nucleus Phosphoprotein Proteomics identification Proto-oncogene Reference proteome Transcription Transcription regulation Ubl conjugation |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9841277] Weiser, Joel [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 |
| name | JUN |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8994286] ENSEMBL:ENSG00000177606 JUN [Homo sapiens] |
| secondaryIdentifier | JUN_HUMAN Q6FHM7 Q96G93 |
| sequenceLength | 331 |
| species | [Species:48887] Homo sapiens |
| (referenceEntity) | [EntityWithAccessionedSequence:168158] p-S63-JUN [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:168194] JUN [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:450237] p-S63,S73-JUN [nucleoplasm] [Homo sapiens] [EntityWithAccessionedSequence:450250] JUN [nucleoplasm] [Homo sapiens] [EntityWithAccessionedSequence:3261181] monoSUMO1-K226,254-JUN [nucleoplasm] [Homo sapiens] [EntityWithAccessionedSequence:8868682] p-S63,S73-JUN [cytosol] [Homo sapiens] |
| (referenceSequence) | [ModifiedResidue:168361] O-phospho-L-serine at 63 [ModifiedResidue:168397] phosphorylated residue at unknown position [ModifiedResidue:450265] O-phospho-L-serine at 73 [GroupModifiedResidue:3261172] sumoylated lysine (monoSUMO1 [nucleoplasm]) at 226 [GroupModifiedResidue:3261173] sumoylated lysine (monoSUMO1 [nucleoplasm]) at 254 |
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No pathways have been reviewed or authored by UniProt:P05412 JUN (50080)
