Jun
entrez
16476
canonical
uniprot
P05627
canonical
ensembl
ENSMUSG00000052684
resolver
ensp
ENSMUSP00000102711
resolver
enst
ENSMUST00000107094
resolver
genesymbol
Jun
resolver
uniprot
Q52L79
resolver
uniprot_entry
JUN_MOUSE
resolver
uniprot_entry
Q52L79_MOUSE
resolver
amino_acid_sequence
MTAKMETTFYDDALNASFLQSESGAYGYSNPKILKQSMTLNLADPVGSLKPHLRAKNSDLLTSPDVGLLKLASPELERLIIQSSNGHITTTPTPTQFLCPKNVTDEQEGFAEGFVRALAELHSQNTLPSVTSAAQPVSGAGMVAPAVASVAGAGGGGGYSASLHSEPPVYANLSNFNPGALSSGGGAPSYGAAGLAFPSQPQQQQQPPQPPHHLPQQIPVQHPRLQALKEEPQTVPEMPGETPPLSPIDMESQERIKAERKRMRNRIAASKCRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNHVNSGCQLMLTQQLQTF
uniprot
proteins
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). {ECO:0000250|UniProtKB:P05412, ECO:0000269|PubMed:14707112, ECO:0000269|PubMed:17210646, ECO:0000269|PubMed:2498083}.
uniprot
proteins
mass_dalton
35944
uniprot
proteins
post_translational_modification
PTM: 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). {ECO:0000250|UniProtKB:P05412}.; PTM: Ubiquitinated by the SCF(FBXW7), leading to its degradation. Ubiquitination takes place following phosphorylation, that promotes interaction with FBXW7. {ECO:0000250|UniProtKB:P05412}.; PTM: Acetylated at Lys-271 by EP300. {ECO:0000250|UniProtKB:P05412}.
uniprot
proteins
protein_family
BZIP family
uniprot
proteins
protein_family
Jun subfamily
uniprot
proteins
pubmed
11397794
uniprot
proteins
pubmed
11704680
uniprot
proteins
pubmed
14707112
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17210646
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
20852630
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
2457172
uniprot
proteins
pubmed
2498083
uniprot
proteins
pubmed
27458189
uniprot
proteins
pubmed
29272704
uniprot
proteins
pubmed
3136397
uniprot
proteins
pubmed
3186736
uniprot
proteins
pubmed
9447996
uniprot
proteins
sequence_length
334
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P05412}.
uniprot
proteins