P05627 · JUN_MOUSE
- ProteinTranscription factor Jun
- GeneJun
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids334 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Transcription factor that recognizes and binds to the AP-1 consensus motif 5'-TGA[GC]TCA-3' (PubMed:14707112).
Heterodimerizes with proteins of the FOS family to form an AP-1 transcription factor complex, thereby enhancing its DNA binding activity to the AP-1 consensus sequence 5'-TGA[GC]TCA-3' and enhancing its transcriptional activity (PubMed:2498083).
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 (By similarity).
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 (By similarity).
Binds to the USP28 promoter (By similarity).
Heterodimerizes with proteins of the FOS family to form an AP-1 transcription factor complex, thereby enhancing its DNA binding activity to the AP-1 consensus sequence 5'-TGA[GC]TCA-3' and enhancing its transcriptional activity (PubMed:2498083).
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 (By similarity).
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 (By similarity).
Binds to the USP28 promoter (By similarity).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 275 | Necessary for synergistic transcriptional activity with SMAD3 | ||||
Sequence: R |
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTranscription factor Jun
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP05627
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 18 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000076430 | 1-334 | Transcription factor Jun | |||
Sequence: MTAKMETTFYDDALNASFLQSESGAYGYSNPKILKQSMTLNLADPVGSLKPHLRAKNSDLLTSPDVGLLKLASPELERLIIQSSNGHITTTPTPTQFLCPKNVTDEQEGFAEGFVRALAELHSQNTLPSVTSAAQPVSGAGMVAPAVASVAGAGGGGGYSASLHSEPPVYANLSNFNPGALSSGGGAPSYGAAGLAFPSQPQQQQQPPQPPHHLPQQIPVQHPRLQALKEEPQTVPEMPGETPPLSPIDMESQERIKAERKRMRNRIAASKCRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNHVNSGCQLMLTQQLQTF | ||||||
Modified residue | 2 | Phosphothreonine; by PAK2 | ||||
Sequence: T | ||||||
Modified residue | 8 | Phosphothreonine; by PAK2 | ||||
Sequence: T | ||||||
Cross-link | 35 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 50 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 56 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Cross-link | 56 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | ||||||
Modified residue | 58 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 63 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 70 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 73 | Phosphoserine; by MAPK8 and PLK3 | ||||
Sequence: S | ||||||
Modified residue | 89 | Phosphothreonine; by PAK2 | ||||
Sequence: T | ||||||
Modified residue | 91 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 93 | Phosphothreonine; by PAK2 | ||||
Sequence: T | ||||||
Cross-link | 229 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 242 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 246 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 252 | Phosphoserine; by GSK3-beta | ||||
Sequence: S | ||||||
Modified residue | 274 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 289 | Phosphothreonine; by PAK2 | ||||
Sequence: T |
Post-translational modification
Phosphorylated by CaMK4 and PRKDC; phosphorylation enhances the transcriptional activity. Phosphorylated by HIPK3. Phosphorylated by DYRK2 at Ser-246; this primes the protein for subsequent phosphorylation by GSK3B at Thr-242. Phosphorylated at Thr-242, Ser-246 and Ser-252 by GSK3B; phosphorylation reduces its ability to bind DNA. Phosphorylated by PAK2 at Thr-2, Thr-8, Thr-89, Thr-93 and Thr-289 thereby promoting JUN-mediated cell proliferation and transformation. Phosphorylated by PLK3 following hypoxia or UV irradiation, leading to increase DNA-binding activity (By similarity).
Phosphorylated by VRK1 (By similarity).
Phosphorylated by VRK1 (By similarity).
Ubiquitinated by the SCF(FBXW7), leading to its degradation. Ubiquitination takes place following phosphorylation, that promotes interaction with FBXW7.
Acetylated at Lys-271 by EP300.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Heterodimer with either BATF3 or ATF7 (By similarity).
Heterodimer with FOS (PubMed:29272704).
Heterodimer with FOSB isoform 1 and 2 (PubMed:29272704).
Component of an AP-1 transcription factor complex composed of JUN-FOS heterodimers (PubMed:2498083).
As part of the AP-1 transcription factor complex, forms heterodimers with FOSB, thereby binding to the AP-1 consensus sequence and stimulating transcription (PubMed:2498083).
The ATF7/JUN heterodimer is essential for ATF7 transactivation activity. 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 (By similarity).
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 (By similarity).
Interacts with TSC22D3 (via N-terminus); the interaction inhibits the binding of active AP1 to its target DNA (PubMed:11397794).
Interacts with HIVEP3 and MYBBP1A (PubMed:14707112, PubMed:9447996).
Interacts with methylated RNF187 (PubMed:20852630).
Binds to HIPK3. Interacts (when phosphorylated) with FBXW7 (By similarity).
Interacts with PRR7 (PubMed:27458189).
Found in a complex with PRR7 and FBXW7 (By similarity).
Interacts with PRR7 and FBXW7; the interaction inhibits ubiquitination-mediated JUN degradation promoting its phosphorylation and transcriptional activity (By similarity).
Interacts with RBM39 (PubMed:11704680).
Interacts with PAGE4 (By similarity).
Interacts with FOSL1 and FOSL2 (PubMed:29272704).
Interacts with ARK2N and CSNK2B; the interaction with ARK2N is mediated by CSNK2B (By similarity).
Heterodimer with FOS (PubMed:29272704).
Heterodimer with FOSB isoform 1 and 2 (PubMed:29272704).
Component of an AP-1 transcription factor complex composed of JUN-FOS heterodimers (PubMed:2498083).
As part of the AP-1 transcription factor complex, forms heterodimers with FOSB, thereby binding to the AP-1 consensus sequence and stimulating transcription (PubMed:2498083).
The ATF7/JUN heterodimer is essential for ATF7 transactivation activity. 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 (By similarity).
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 (By similarity).
Interacts with TSC22D3 (via N-terminus); the interaction inhibits the binding of active AP1 to its target DNA (PubMed:11397794).
Interacts with HIVEP3 and MYBBP1A (PubMed:14707112, PubMed:9447996).
Interacts with methylated RNF187 (PubMed:20852630).
Binds to HIPK3. Interacts (when phosphorylated) with FBXW7 (By similarity).
Interacts with PRR7 (PubMed:27458189).
Found in a complex with PRR7 and FBXW7 (By similarity).
Interacts with PRR7 and FBXW7; the interaction inhibits ubiquitination-mediated JUN degradation promoting its phosphorylation and transcriptional activity (By similarity).
Interacts with RBM39 (PubMed:11704680).
Interacts with PAGE4 (By similarity).
Interacts with FOSL1 and FOSL2 (PubMed:29272704).
Interacts with ARK2N and CSNK2B; the interaction with ARK2N is mediated by CSNK2B (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P05627 | Cdk6 Q64261 | 2 | EBI-764369, EBI-847380 | |
XENO | P05627 | ESR1 P03372 | 6 | EBI-764369, EBI-78473 | |
BINARY | P05627 | Mapk8 Q91Y86 | 2 | EBI-764369, EBI-298784 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 150-226 | Interaction with PAGE4 | ||||
Sequence: VAGAGGGGGYSASLHSEPPVYANLSNFNPGALSSGGGAPSYGAAGLAFPSQPQQQQQPPQPPHHLPQQIPVQHPRLQ | ||||||
Region | 191-217 | Disordered | ||||
Sequence: GAAGLAFPSQPQQQQQPPQPPHHLPQQ | ||||||
Compositional bias | 203-217 | Pro residues | ||||
Sequence: QQQQPPQPPHHLPQQ | ||||||
Region | 255-282 | Basic motif | ||||
Sequence: RIKAERKRMRNRIAASKCRKRKLERIAR | ||||||
Domain | 255-318 | bZIP | ||||
Sequence: RIKAERKRMRNRIAASKCRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNH | ||||||
Region | 283-311 | Leucine-zipper | ||||
Sequence: LEEKVKTLKAQNSELASTANMLREQVAQL |
Sequence similarities
Belongs to the bZIP family. Jun subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length334
- Mass (Da)35,944
- Last updated1989-10-01 v3
- Checksum2BE0E4025B8B1CA3
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0AA74KT59 | A0AA74KT59_MOUSE | Jun | 356 |
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 183 | in Ref. 1; CAA31252 | ||||
Sequence: S → C | ||||||
Compositional bias | 203-217 | Pro residues | ||||
Sequence: QQQQPPQPPHHLPQQ |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X12761 EMBL· GenBank· DDBJ | CAA31252.1 EMBL· GenBank· DDBJ | mRNA | ||
X12740 EMBL· GenBank· DDBJ | CAA31236.1 EMBL· GenBank· DDBJ | mRNA | ||
J04115 EMBL· GenBank· DDBJ | AAA37419.1 EMBL· GenBank· DDBJ | mRNA | ||
BC002081 EMBL· GenBank· DDBJ | AAH02081.1 EMBL· GenBank· DDBJ | mRNA | ||
BC021888 EMBL· GenBank· DDBJ | AAH21888.1 EMBL· GenBank· DDBJ | mRNA |