JDP2_RAT
ID JDP2_RAT Reviewed; 163 AA.
AC Q78E65;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Jun dimerization protein 2;
GN Name=Jdp2; Synonyms=Jdp-2, Jundm2, Jundp2;
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 [MRNA], FUNCTION, INTERACTION WITH JUN; JUNB AND JUND,
RP AND DNA-BINDING.
RC TISSUE=Pituitary;
RX PubMed=9154808; DOI=10.1128/mcb.17.6.3094;
RA Aronheim A., Zandi E., Hennemann H., Elledge S.J., Karin M.;
RT "Isolation of an AP-1 repressor by a novel method for detecting protein-
RT protein interactions.";
RL Mol. Cell. Biol. 17:3094-3102(1997).
RN [2]
RP INTERACTION WITH CEBPG.
RX PubMed=9778531; DOI=10.1016/s0960-9822(98)70467-1;
RA Broder Y.C., Katz S., Aronheim A.;
RT "The ras recruitment system, a novel approach to the study of protein-
RT protein interactions.";
RL Curr. Biol. 8:1121-1124(1998).
CC -!- FUNCTION: Component of the AP-1 transcription factor that represses
CC transactivation mediated by the Jun family of proteins. Involved in a
CC variety of transcriptional responses associated with AP-1, such as UV-
CC induced apoptosis, cell differentiation, tumorigenesis and
CC antitumogeneris. Can also function as a repressor by recruiting histone
CC deacetylase 3/HDAC3 to the promoter region of JUN. May control
CC transcription via direct regulation of the modification of histones and
CC the assembly of chromatin (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:9154808}.
CC -!- SUBUNIT: Interacts with IRF2BP1 (By similarity). Forms homodimer or
CC heterodimer with JUN, JUNB, JUND, CEBPG and ATF2 thereby inhibiting
CC transactivation by JUN, ATF2 and CEBPG (By similarity). Binds multiple
CC DNA elements such as cAMP-response element (CRE) and TPA response
CC element (TRE) either as homodimer or heterodimer. {ECO:0000250,
CC ECO:0000269|PubMed:9154808, ECO:0000269|PubMed:9778531}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- PTM: Phosphorylation of Thr-148 by MAPK8 in response to different
CC stress conditions such as, UV irradiation, oxidatives stress and
CC anisomycin treatments. {ECO:0000250}.
CC -!- PTM: Polyubiquitinated; probably by IRF2BP1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily. {ECO:0000305}.
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DR EMBL; U53449; AAC02258.1; -; mRNA.
DR RefSeq; NP_446346.1; NM_053894.1.
DR AlphaFoldDB; Q78E65; -.
DR SMR; Q78E65; -.
DR BioGRID; 250557; 1.
DR STRING; 10116.ENSRNOP00000011339; -.
DR PhosphoSitePlus; Q78E65; -.
DR PaxDb; Q78E65; -.
DR GeneID; 116674; -.
DR KEGG; rno:116674; -.
DR UCSC; RGD:621611; rat.
DR CTD; 122953; -.
DR RGD; 621611; Jdp2.
DR eggNOG; KOG1414; Eukaryota.
DR HOGENOM; CLU_088612_0_1_1; -.
DR InParanoid; Q78E65; -.
DR OMA; XESERLE; -.
DR OrthoDB; 1457971at2759; -.
DR PhylomeDB; Q78E65; -.
DR TreeFam; TF326301; -.
DR PRO; PR:Q78E65; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000008224; Expressed in frontal cortex and 20 other tissues.
DR Genevisible; Q78E65; RN.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0035497; F:cAMP response element binding; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:RGD.
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; ISO:RGD.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD.
DR GO; GO:0043522; F:leucine zipper domain binding; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:RGD.
DR GO; GO:0031065; P:positive regulation of histone deacetylation; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR InterPro; IPR000837; AP-1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR029819; JDP2.
DR PANTHER; PTHR23351; PTHR23351; 1.
DR PANTHER; PTHR23351:SF10; PTHR23351:SF10; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR PRINTS; PR00042; LEUZIPPRFOS.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..163
FT /note="Jun dimerization protein 2"
FT /id="PRO_0000331132"
FT DOMAIN 72..135
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..96
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 100..128
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 59..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 148
FT /note="Phosphothreonine; by MAPK8"
FT /evidence="ECO:0000250|UniProtKB:Q8WYK2"
FT CROSSLNK 65
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8WYK2"
SQ SEQUENCE 163 AA; 18675 MW; A8AB65A7D20564F8 CRC64;
MMPGQIPDPS VTAGSLPGLG PLTGLPSSAL TTEELKYADI RNIGAMIAPL HFLEVKLGKR
PQPVKSELDE EEERRKRRRE KNKVAAARCR NKKKERTEFL QRESERLELM NAELKTQIEE
LKLERQQLIL MLNRHRPTCI VRTDSVRTPE SEGNPLLEQL DKK
