JUN_PIG
ID JUN_PIG Reviewed; 331 AA.
AC P56432;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 25-MAY-2022, entry version 141.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary anterior lobe;
RX PubMed=8793856; DOI=10.1016/0303-7207(96)03798-7;
RA Chung H.-O., Kato T., Kato Y.;
RT "Molecular cloning of c-jun and c-fos cDNAs from porcine anterior pituitary
RT and their involvement in gonadotropin-releasing hormone stimulation.";
RL Mol. Cell. Endocrinol. 119:75-82(1996).
RN [2]
RP ERRATUM OF PUBMED:8793856.
RX PubMed=8898353; DOI=10.1016/0303-7207(96)03902-0;
RA Chung H.-O., Kato T., Kato Y.;
RL Mol. Cell. Endocrinol. 122:113-114(1996).
CC -!- FUNCTION: Transcription factor that recognizes and binds to the AP-1
CC consensus motif 5'-TGA[GC]TCA-3' (By similarity). Heterodimerizes with
CC proteins of the FOS family to form an AP-1 transcription complex,
CC thereby enhancing its DNA binding activity to the AP-1 consensus
CC sequence 5'-TGA[GC]TCA-3' and enhancing its transcriptional activity
CC (By similarity). Together with FOSB, plays a role in activation-induced
CC cell death of T cells by binding to the AP-1 promoter site of
CC FASLG/CD95L, and inducing its transcription in response to activation
CC of the TCR/CD3 signaling pathway (By similarity). Promotes activity of
CC NR5A1 when phosphorylated by HIPK3 leading to increased steroidogenic
CC gene expression upon cAMP signaling pathway stimulation (By
CC similarity). Involved in activated KRAS-mediated transcriptional
CC activation of USP28. Binds to the USP28 promoter (By similarity).
CC Interacts with FOSB to form an AP-1 transcription complex, thereby
CC enhancing its DNA binding activity to an AP-1 consensus sequence and
CC its transcriptional activity (By similarity). Together with FOSB, plays
CC a role in activation-induced cell death of T cells by binding to the
CC AP-1 site of FASLG/CD95L, and activating its transcription in T cells
CC upon stimulation by TCR/CD3 (By similarity).
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-243; this primes the protein for subsequent
CC phosphorylation by GSK3B at Thr-239. Phosphorylated at Thr-239, Ser-243
CC and Ser-249 by GSK3B; phosphorylation reduces its ability to bind DNA.
CC Phosphorylated by PAK2 at Thr-2, Thr-8, Thr-89, Thr-93 and Thr-286
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-271 by EP300. {ECO:0000250|UniProtKB:P05412}.
CC -!- SIMILARITY: Belongs to the bZIP family. Jun subfamily. {ECO:0000305}.
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DR EMBL; S83515; AAB50808.1; -; mRNA.
DR RefSeq; NP_999045.1; NM_213880.1.
DR AlphaFoldDB; P56432; -.
DR SMR; P56432; -.
DR STRING; 9823.ENSSSCP00000030489; -.
DR iPTMnet; P56432; -.
DR PRIDE; P56432; -.
DR GeneID; 396913; -.
DR KEGG; ssc:396913; -.
DR CTD; 3725; -.
DR eggNOG; KOG0837; Eukaryota.
DR InParanoid; P56432; -.
DR OrthoDB; 1090460at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005634; C:nucleus; IDA:AgBase.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IMP:AgBase.
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:0071222; P:cellular response to lipopolysaccharide; IDA:AgBase.
DR GO; GO:0006955; P:immune response; IDA:AgBase.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IMP:AgBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:AgBase.
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..331
FT /note="Transcription factor Jun"
FT /id="PRO_0000076431"
FT DOMAIN 252..315
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 150..223
FT /note="Interaction with PAGE4"
FT /evidence="ECO:0000250|UniProtKB:P05412"
FT REGION 192..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..279
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 280..308
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
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 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 239
FT /note="Phosphothreonine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:P05412"
FT MOD_RES 243
FT /note="Phosphoserine; by DYRK2 and GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:P05412"
FT MOD_RES 249
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:P05412"
FT MOD_RES 271
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05412"
FT MOD_RES 286
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 70
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05412"
FT CROSSLNK 226
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05412"
SQ SEQUENCE 331 AA; 35629 MW; 0B45EAD5911340EB CRC64;
MTAKMETTFY DDALNASFLQ SESGAYGYSN PKILKQSMTL NLADPVGNLK PHLRAQDSDL
LTSPDVGLLK LASPELERLI IQSSNGHITT TPTPTQFLCP KNVTDEQEGF AEGFVRALAE
LHSQNTLPSV TSAAQPVSGA GLVAPAVASV AGGSGSGGFS ASLHSEPPVY ANLSNFNPGA
LSSGGGAPSY GAAGLAFPAQ PQQQQQQPPQ PPHHLPVQHP RLQALKEEPQ TVPEMPGETP
PLSPIDMESQ ERIKAERKRM RNRIAASKCR KRKLERIARL EEKVKTLKAQ NSELASTANM
LREQVAQLKQ KVMNHVNSGC QLMLTQQLQT F
