JUN_BOVIN
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 03-AUG-2022, entry version 136.
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. Heterodimer with FOS
CC (By similarity). Heterodimer with FOSB (By similarity). Component of an
CC AP-1 transcription factor complex composed of JUN-FOS heterodimers (By
CC similarity). As part of the AP-1 transcription factor complex, forms
CC heterodimers with FOSB, thereby binding to the AP-1 consensus sequence
CC and stimulating transcription (By similarity). Interacts with FOS and
CC FOSB (By similarity). The ATF7/JUN heterodimer is essential for ATF7
CC transactivation activity. Interacts with DSIPI; the interaction
CC inhibits the binding of active AP1 to its target DNA. Interacts with
CC HIVEP3 and MYBBP1A. Interacts with SP1, SPIB and TCF20. Interacts with
CC COPS5; the interaction leads indirectly to its phosphorylation.
CC Component of the SMAD3/SMAD4/JUN/FOS/complex which forms at the AP1
CC promoter site. The SMAD3/SMAD4 heterodimer acts synergistically with
CC the JUN/FOS heterodimer to activate transcription in response to TGF-
CC beta. Interacts (via its basic DNA binding and leucine zipper domains)
CC with SMAD3 (via an N-terminal domain); the interaction is required for
CC TGF-beta-mediated transactivation of the SMAD3/SMAD4/JUN/FOS/complex.
CC Component of an AP-1 transcription factor complex (By similarity). As
CC part of the AP-1 transcription factor complex, forms heterodimers with
CC FOSB, thereby binding to the AP-1 consensus sequence and stimulating
CC transcription (By similarity). Interacts with methylated RNF187. Binds
CC to HIPK3. Interacts (when phosphorylated) with FBXW7. Found in a
CC complex with PRR7 and FBXW7. Interacts with PRR7 and FBXW7; the
CC interaction inhibits ubiquitination-mediated JUN degradation promoting
CC its phosphorylation and transcriptional activity. Interacts with RBM39
CC (By similarity). Interacts with PAGE4 (By similarity).
CC {ECO:0000250|UniProtKB:P05412, ECO:0000250|UniProtKB:P05627,
CC 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 PRIDE; O77627; -.
DR eggNOG; KOG0837; Eukaryota.
DR InParanoid; O77627; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
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 InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR015558; C_Jun/v-Jun.
DR InterPro; IPR005643; JNK.
DR InterPro; IPR002112; Leuzip_Jun.
DR InterPro; IPR008917; TF_DNA-bd_sf.
DR PANTHER; PTHR11462:SF8; PTHR11462:SF8; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR Pfam; PF03957; Jun; 1.
DR PRINTS; PR00043; LEUZIPPRJUN.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF47454; SSF47454; 1.
DR SUPFAM; SSF57959; SSF57959; 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
