JUNB_RAT
ID JUNB_RAT Reviewed; 344 AA.
AC P24898; Q6P733;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Transcription factor JunB {ECO:0000305};
DE AltName: Full=Transcription factor AP-1 subunit JunB {ECO:0000305};
GN Name=Junb; Synonyms=Jun-b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Fischer; TISSUE=Liver;
RX PubMed=1542584; DOI=10.1093/nar/20.4.914;
RA Kawakami Z., Kitabayashi I., Matsuoka T., Gachelin G., Yokoyama K.;
RT "Conserved structural motifs among mammalian junB genes.";
RL Nucleic Acids Res. 20:914-914(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-252 AND SER-256, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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'. Heterodimerizes with proteins of the FOS family to
CC form an AP-1 transcription complex, thereby enhancing its DNA binding
CC activity to an AP-1 consensus sequence and its transcriptional activity
CC (By similarity). {ECO:0000250|UniProtKB:P09450}.
CC -!- SUBUNIT: Binds DNA as a homodimer or as a heterodimer with another
CC member of the Jun/Fos family. Component of an AP-1 transcription factor
CC complex (By similarity). As part of the AP-1 transcription factor
CC complex, forms heterodimers with FOSB, thereby binding to the AP-1
CC consensus sequence and stimulating transcription (By similarity).
CC Interacts with NFE2 (via its WW domains). {ECO:0000250,
CC ECO:0000250|UniProtKB:P09450}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- INDUCTION: By growth factors.
CC -!- PTM: Ubiquitinated by ITCH, leading to its degradation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bZIP family. Jun subfamily. {ECO:0000305}.
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DR EMBL; X54686; CAA38500.1; -; Genomic_DNA.
DR EMBL; BC061862; AAH61862.1; -; mRNA.
DR PIR; S21063; S21063.
DR RefSeq; NP_068608.2; NM_021836.2.
DR AlphaFoldDB; P24898; -.
DR SMR; P24898; -.
DR BioGRID; 246672; 1.
DR CORUM; P24898; -.
DR STRING; 10116.ENSRNOP00000061729; -.
DR iPTMnet; P24898; -.
DR PhosphoSitePlus; P24898; -.
DR PaxDb; P24898; -.
DR GeneID; 24517; -.
DR KEGG; rno:24517; -.
DR CTD; 3726; -.
DR RGD; 2944; Junb.
DR eggNOG; KOG0837; Eukaryota.
DR InParanoid; P24898; -.
DR OrthoDB; 1090460at2759; -.
DR PhylomeDB; P24898; -.
DR PRO; PR:P24898; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR GO; GO:0035976; C:transcription factor AP-1 complex; ISO:RGD.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0071277; P:cellular response to calcium ion; ISO:RGD.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IEP:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR GO; GO:0046697; P:decidualization; ISO:RGD.
DR GO; GO:0060136; P:embryonic process involved in female pregnancy; ISO:RGD.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0060716; P:labyrinthine layer blood vessel development; ISO:RGD.
DR GO; GO:0001649; P:osteoblast differentiation; ISO:RGD.
DR GO; GO:0033687; P:osteoblast proliferation; ISO:RGD.
DR GO; GO:0030316; P:osteoclast differentiation; ISO:RGD.
DR GO; GO:0045597; P:positive regulation of cell differentiation; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:RGD.
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:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0072724; P:response to 4-nitroquinoline N-oxide; IEP:RGD.
DR GO; GO:0051591; P:response to cAMP; IEP:RGD.
DR GO; GO:0051412; P:response to corticosterone; IEP:RGD.
DR GO; GO:0034097; P:response to cytokine; IEP:RGD.
DR GO; GO:0009416; P:response to light stimulus; IEP:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR GO; GO:0032570; P:response to progesterone; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:RGD.
DR GO; GO:0001829; P:trophectodermal cell differentiation; ISO:RGD.
DR GO; GO:0001570; P:vasculogenesis; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..344
FT /note="Transcription factor JunB"
FT /id="PRO_0000076440"
FT DOMAIN 265..328
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 51..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..292
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 293..321
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 237
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09450"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17275"
FT MOD_RES 252
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17275"
FT CROSSLNK 237
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P17275"
FT CROSSLNK 237
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P17275"
FT CROSSLNK 340
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17275"
FT CONFLICT 8
FT /note="P -> A (in Ref. 1; CAA38500)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="H -> Q (in Ref. 1; CAA38500)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="A -> T (in Ref. 2; AAH61862)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 35765 MW; 6F52D4FECC32E234 CRC64;
MCTKMEQPFY HDDSYAAAGY GRSPGSLSLH DYKLLKPTLA LNLADPYRGL KGPGARGPGP
EGSGAGSYFS GQGSDTGASL KLASTELERL IVPNSNGVIT TTPTPPGQYF YPRGGGSGGG
TGGGVTEEQE GFADGFVKAL DDLHKMNHVT PPNVSLGASG GPQAGPGGVY AGPEPPPVYT
NLSSYSPASA PSGGSGTAVG TGSSYPTATI SYLPHAPPFA GGHPAQLGLS RGASAFKEEP
QTVPEARSRD ATPPVSPINM EDQERIKVER KRLRNRLAAT KCRKRKLERI ARLEDKVKTL
KAENAGLSSA AGLLREQVAQ LKQKVMTHVS NGCQLLLGVK GHAF
