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Database: UniProt
Entry: O77627
LinkDB: O77627
Original site: O77627 
ID   JUN_BOVIN               Reviewed;         335 AA.
AC   O77627;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 145.
DE   RecName: Full=Transcription factor Jun {ECO:0000305};
DE   AltName: Full=Activator protein 1;
DE            Short=AP1;
DE   AltName: Full=Proto-oncogene c-Jun;
DE   AltName: Full=Transcription factor AP-1 subunit Jun {ECO:0000305};
DE   AltName: Full=V-jun avian sarcoma virus 17 oncogene homolog;
GN   Name=JUN;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19390049; DOI=10.1126/science.1169588;
RG   The bovine genome sequencing and analysis consortium;
RT   "The genome sequence of taurine cattle: a window to ruminant biology and
RT   evolution.";
RL   Science 324:522-528(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 6-110.
RC   TISSUE=Brain;
RA   Davis J.S., Fong H.W., Westfall S.W.;
RT   "Stimulation of c-fos and c-jun mRNA in bovine luteal cells.";
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcription factor that recognizes and binds to the AP-1
CC       consensus motif 5'-TGA[GC]TCA-3'. Heterodimerizes with proteins of the
CC       FOS family to form an AP-1 transcription complex, thereby enhancing its
CC       DNA binding activity to the AP-1 consensus sequence 5'-TGA[GC]TCA-3'
CC       and enhancing its transcriptional activity (By similarity). Together
CC       with FOSB, plays a role in activation-induced cell death of T cells by
CC       binding to the AP-1 promoter site of FASLG/CD95L, and inducing its
CC       transcription in response to activation of the TCR/CD3 signaling
CC       pathway (By similarity). Promotes activity of NR5A1 when phosphorylated
CC       by HIPK3 leading to increased steroidogenic gene expression upon cAMP
CC       signaling pathway stimulation. Involved in activated KRAS-mediated
CC       transcriptional activation of USP28. Binds to the USP28 promoter.
CC       {ECO:0000250|UniProtKB:P05412, ECO:0000250|UniProtKB:P05627}.
CC   -!- SUBUNIT: Heterodimer with either BATF3 or ATF7 (By similarity).
CC       Heterodimer with FOS (By similarity). Heterodimer with FOSB isoform 1
CC       and 2 (By similarity). Component of an AP-1 transcription factor
CC       complex composed of JUN-FOS heterodimers (By similarity). As part of
CC       the AP-1 transcription factor complex, forms heterodimers with FOSB,
CC       thereby binding to the AP-1 consensus sequence and stimulating
CC       transcription (By similarity). Interacts with FOS and FOSB isoform 1
CC       and 2 (By similarity). The ATF7/JUN heterodimer is essential for ATF7
CC       transactivation activity (By similarity). Interacts with TSC22D3 (via
CC       N-terminus); the interaction inhibits the binding of active AP1 to its
CC       target DNA (By similarity). Interacts with HIVEP3 and MYBBP1A (By
CC       similarity). Interacts with SP1, SPIB and TCF20. Interacts with COPS5;
CC       the interaction leads indirectly to its phosphorylation. Component of
CC       the SMAD3/SMAD4/JUN/FOS/complex which forms at the AP1 promoter site.
CC       The SMAD3/SMAD4 heterodimer acts synergistically with the JUN/FOS
CC       heterodimer to activate transcription in response to TGF-beta.
CC       Interacts (via its basic DNA binding and leucine zipper domains) with
CC       SMAD3 (via an N-terminal domain); the interaction is required for TGF-
CC       beta-mediated transactivation of the SMAD3/SMAD4/JUN/FOS/complex.
CC       Interacts with methylated RNF187. Binds to HIPK3. Interacts (when
CC       phosphorylated) with FBXW7. Found in a complex with PRR7 and FBXW7.
CC       Interacts with PRR7 and FBXW7; the interaction inhibits ubiquitination-
CC       mediated JUN degradation promoting its phosphorylation and
CC       transcriptional activity (By similarity). Interacts with RBM39 (By
CC       similarity). Interacts with PAGE4 (By similarity). Interacts with ARK2N
CC       and CSNK2B; the interaction with ARK2N is mediated by CSNK2B (By
CC       similarity). {ECO:0000250|UniProtKB:P05412,
CC       ECO:0000250|UniProtKB:P05627, ECO:0000250|UniProtKB:P17325}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P05412}.
CC   -!- PTM: Phosphorylated by CaMK4 and PRKDC; phosphorylation enhances the
CC       transcriptional activity. Phosphorylated by HIPK3. Phosphorylated by
CC       DYRK2 at Ser-247; this primes the protein for subsequent
CC       phosphorylation by GSK3B at Thr-243. Phosphorylated at Thr-243, Ser-247
CC       and Ser-253 by GSK3B; phosphorylation reduces its ability to bind DNA.
CC       Phosphorylated by PAK2 at Thr-2, Thr-8, Thr-89, Thr-93 and Thr-290
CC       thereby promoting JUN-mediated cell proliferation and transformation.
CC       Phosphorylated by PLK3 following hypoxia or UV irradiation, leading to
CC       increase DNA-binding activity (By similarity).
CC       {ECO:0000250|UniProtKB:P05412}.
CC   -!- PTM: Ubiquitinated by the SCF(FBXW7), leading to its degradation.
CC       Ubiquitination takes place following phosphorylation, that promotes
CC       interaction with FBXW7. {ECO:0000250|UniProtKB:P05412}.
CC   -!- PTM: Acetylated at Lys-275 by EP300. {ECO:0000250|UniProtKB:P05412}.
CC   -!- SIMILARITY: Belongs to the bZIP family. Jun subfamily. {ECO:0000305}.
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DR   EMBL; AF069514; AAC21576.1; -; mRNA.
DR   AlphaFoldDB; O77627; -.
DR   BMRB; O77627; -.
DR   SMR; O77627; -.
DR   DIP; DIP-61529N; -.
DR   IntAct; O77627; 1.
DR   STRING; 9913.ENSBTAP00000005279; -.
DR   iPTMnet; O77627; -.
DR   PaxDb; 9913-ENSBTAP00000005279; -.
DR   eggNOG; KOG0837; Eukaryota.
DR   InParanoid; O77627; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0000791; C:euchromatin; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0035976; C:transcription factor AP-1 complex; IEA:Ensembl.
DR   GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR   GO; GO:0035497; F:cAMP response element binding; IEA:Ensembl.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR   GO; GO:0140296; F:general transcription initiation factor binding; IEA:Ensembl.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0070412; F:R-SMAD binding; IEA:Ensembl.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl.
DR   GO; GO:0034614; P:cellular response to reactive oxygen species; IEA:Ensembl.
DR   GO; GO:0043922; P:negative regulation by host of viral transcription; IEA:Ensembl.
DR   GO; GO:0043923; P:positive regulation by host of viral transcription; IEA:Ensembl.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:2000144; P:positive regulation of DNA-templated transcription initiation; IEA:Ensembl.
DR   GO; GO:1902895; P:positive regulation of miRNA transcription; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR   GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0019046; P:release from viral latency; IEA:Ensembl.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:Ensembl.
DR   GO; GO:0060395; P:SMAD protein signal transduction; IEA:Ensembl.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR   CDD; cd14696; bZIP_Jun; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   InterPro; IPR005643; JNK.
DR   InterPro; IPR002112; Leuzip_Jun.
DR   InterPro; IPR008917; TF_DNA-bd_sf.
DR   PANTHER; PTHR11462; JUN TRANSCRIPTION FACTOR-RELATED; 1.
DR   PANTHER; PTHR11462:SF8; TRANSCRIPTION FACTOR JUN; 1.
DR   Pfam; PF00170; bZIP_1; 1.
DR   Pfam; PF03957; Jun; 1.
DR   PRINTS; PR00043; LEUZIPPRJUN.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF47454; A DNA-binding domain in eukaryotic transcription factors; 1.
DR   SUPFAM; SSF57959; Leucine zipper domain; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Activator; DNA-binding; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Proto-oncogene; Reference proteome; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN           1..335
FT                   /note="Transcription factor Jun"
FT                   /id="PRO_0000076428"
FT   DOMAIN          256..319
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          150..227
FT                   /note="Interaction with PAGE4"
FT                   /evidence="ECO:0000250|UniProtKB:P05412"
FT   REGION          184..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          256..283
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          284..312
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   COMPBIAS        204..218
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            272
FT                   /note="Necessary for synergistic transcriptional activity
FT                   with SMAD3"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="Phosphothreonine; by PAK2"
FT                   /evidence="ECO:0000250|UniProtKB:P05412"
FT   MOD_RES         8
FT                   /note="Phosphothreonine; by PAK2"
FT                   /evidence="ECO:0000250|UniProtKB:P05412"
FT   MOD_RES         56
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P05627"
FT   MOD_RES         58
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P05412"
FT   MOD_RES         63
FT                   /note="Phosphoserine; by MAPK8 and PLK3"
FT                   /evidence="ECO:0000250|UniProtKB:P05412"
FT   MOD_RES         73
FT                   /note="Phosphoserine; by MAPK8 and PLK3"
FT                   /evidence="ECO:0000250|UniProtKB:P05412"
FT   MOD_RES         89
FT                   /note="Phosphothreonine; by PAK2"
FT                   /evidence="ECO:0000250|UniProtKB:P05412"
FT   MOD_RES         91
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P05412"
FT   MOD_RES         93
FT                   /note="Phosphothreonine; by PAK2"
FT                   /evidence="ECO:0000250|UniProtKB:P05412"
FT   MOD_RES         243
FT                   /note="Phosphothreonine; by GSK3-beta"
FT                   /evidence="ECO:0000250|UniProtKB:P05412"
FT   MOD_RES         247
FT                   /note="Phosphoserine; by DYRK2 and GSK3-beta"
FT                   /evidence="ECO:0000250|UniProtKB:P05412"
FT   MOD_RES         253
FT                   /note="Phosphoserine; by GSK3-beta"
FT                   /evidence="ECO:0000250|UniProtKB:P05412"
FT   MOD_RES         275
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P05412"
FT   MOD_RES         290
FT                   /note="Phosphothreonine; by PAK2"
FT                   /evidence="ECO:0000250|UniProtKB:P05412"
FT   CROSSLNK        35
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P05412"
FT   CROSSLNK        50
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P05412"
FT   CROSSLNK        56
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P05412"
FT   CROSSLNK        70
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P05412"
FT   CROSSLNK        230
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P05412"
SQ   SEQUENCE   335 AA;  36084 MW;  435557862BFEA254 CRC64;
     MTAKMETTFY DDALNASFLQ SESGAYGYSN PKILKQSMTL NLADPVGSLK PHLRAKNSDL
     LTSPDVGLLK LASPELERLI IQSSNGHITT TPTPTQFLCP KNVTDEQEGF AEGFVRALAE
     LHSQNTLPSV TSAAQPVSGA GLVAPAVASV AGGSGSGGFS ASLHSEPPVY ANLSNFNPGS
     LSSGGGAPSY GAAGLAFPAQ PQQQQQQPPQ PPHHLPQQIP VQHPRLQALK EEPQTVPEMP
     GETPPLSPID MESQERIKAE RKRMRNRIAA SKCRKRKLER IARLEEKVKT LKAQNSELAS
     TANMLREQVA QLKQKVMNHV NSGCQLMLTQ QLQTF
//
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