JUNB_BOVIN
ID JUNB_BOVIN Reviewed; 347 AA.
AC Q0VBZ5;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Transcription factor JunB {ECO:0000305};
DE AltName: Full=Transcription factor AP-1 subunit JunB {ECO:0000305};
GN Name=JUNB;
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 MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcription factor involved in regulating gene activity
CC following the primary growth factor response. Binds to the DNA sequence
CC 5'-TGA[GC]TCA-3' (By similarity). Heterodimerizes with proteins of the
CC FOS family to form an AP-1 transcription complex, thereby enhancing its
CC DNA binding activity to an AP-1 consensus sequence and its
CC transcriptional activity (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P09450}.
CC -!- SUBUNIT: Binds DNA as a homodimer or as a heterodimer with another
CC member of the Jun/Fos family (By similarity). Component of an AP-1
CC 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 ITCH (via
CC its WW domains) (By similarity). {ECO:0000250|UniProtKB:P09450,
CC ECO:0000250|UniProtKB:P17275}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC -!- PTM: Ubiquitinated by ITCH, leading to its degradation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bZIP family. Jun subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC120428; AAI20429.1; -; mRNA.
DR RefSeq; NP_001069124.1; NM_001075656.1.
DR AlphaFoldDB; Q0VBZ5; -.
DR SMR; Q0VBZ5; -.
DR STRING; 9913.ENSBTAP00000015987; -.
DR PaxDb; Q0VBZ5; -.
DR PRIDE; Q0VBZ5; -.
DR Ensembl; ENSBTAT00000015987; ENSBTAP00000015987; ENSBTAG00000012046.
DR GeneID; 514246; -.
DR KEGG; bta:514246; -.
DR CTD; 3726; -.
DR VEuPathDB; HostDB:ENSBTAG00000012046; -.
DR VGNC; VGNC:30387; JUNB.
DR eggNOG; KOG0837; Eukaryota.
DR GeneTree; ENSGT00940000161195; -.
DR HOGENOM; CLU_057007_0_0_1; -.
DR InParanoid; Q0VBZ5; -.
DR OMA; MNHMPPP; -.
DR OrthoDB; 1090460at2759; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000012046; Expressed in ureter and 104 other tissues.
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: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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0071277; P:cellular response to calcium ion; IEA:Ensembl.
DR GO; GO:0046697; P:decidualization; IEA:Ensembl.
DR GO; GO:0060136; P:embryonic process involved in female pregnancy; IEA:Ensembl.
DR GO; GO:0060716; P:labyrinthine layer blood vessel development; IEA:Ensembl.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0033687; P:osteoblast proliferation; IEA:Ensembl.
DR GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0002158; P:osteoclast proliferation; IEA:Ensembl.
DR GO; GO:0045597; P:positive regulation of cell differentiation; 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:0001829; P:trophectodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR005643; JNK.
DR InterPro; IPR029822; JunB.
DR InterPro; IPR002112; Leuzip_Jun.
DR InterPro; IPR008917; TF_DNA-bd_sf.
DR PANTHER; PTHR11462:SF37; PTHR11462:SF37; 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; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..347
FT /note="Transcription factor JunB"
FT /id="PRO_0000285212"
FT DOMAIN 268..331
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 50..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..295
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 296..324
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT MOD_RES 102
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P17275"
FT MOD_RES 104
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P17275"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17275"
FT MOD_RES 240
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09450"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17275"
FT MOD_RES 255
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P17275"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17275"
FT CROSSLNK 4
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17275"
FT CROSSLNK 33
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17275"
FT CROSSLNK 36
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17275"
FT CROSSLNK 81
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17275"
FT CROSSLNK 141
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17275"
FT CROSSLNK 240
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P17275"
FT CROSSLNK 240
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P17275"
FT CROSSLNK 343
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17275"
SQ SEQUENCE 347 AA; 35929 MW; 8635054623B08A0B CRC64;
MCTKMEQPFY HDDSYAAAGY GRTPGGLSLH DYKLLKPSLA LNLSDPYRNL KAPGARGPGP
EGNGGGSYFS SQGSDTGASL KLASSELERL IVPNSNGVIT TTPTPPGQYF YPRGGGSGGG
AGGAGGGVTE EQEGFADGFV KALDDLHKMN HVTPPNVSLG ASGGPPAGPG GVYAGPEPPP
VYTNLSSYSP ASAPSGGAGA AVGTGSSYPT ATISYLPHAP PFAGGHPAQL GLGRGASAFK
EEPQTVPEAR SRDATPPVSP INMEDQERIK VERKRLRNRL AATKCRKRKL ERIARLEDKV
KTLKAENAGL SSTAGLLREQ VAQLKQKVMT HVSNGCQLLL GVKGHAF
