JDP2_MOUSE
ID JDP2_MOUSE Reviewed; 163 AA.
AC P97875;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Jun dimerization protein 2;
GN Name=Jdp2; Synonyms=Jundm2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=12707301; DOI=10.1084/jem.20021321;
RA Kawaida R., Ohtsuka T., Okutsu J., Takahashi T., Kadono Y., Oda H.,
RA Hikita A., Nakamura K., Tanaka S., Furukawa H.;
RT "Jun dimerization protein 2 (JDP2), a member of the AP-1 family of
RT transcription factor, mediates osteoclast differentiation induced by
RT RANKL.";
RL J. Exp. Med. 197:1029-1035(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 TISSUE SPECIFICITY, INTERACTION WITH ATF2, AND DNA-BINDING.
RX PubMed=11231009; DOI=10.1016/s0014-5793(00)02387-5;
RA Jin C., Ugai H., Song J., Murata T., Nili F., Sun K., Horikoshi M.,
RA Yokoyama K.K.;
RT "Identification of mouse Jun dimerization protein 2 as a novel repressor of
RT ATF-2.";
RL FEBS Lett. 489:34-41(2001).
RN [4]
RP INTERACTION WITH ATF2, PHOSPHORYLATION AT THR-148 BY MAPK8, AND MUTAGENESIS
RP OF THR-148.
RX PubMed=11602244; DOI=10.1016/s0014-5793(01)02907-6;
RA Katz S., Heinrich R., Aronheim A.;
RT "The AP-1 repressor, JDP2, is a bona fide substrate for the c-Jun N-
RT terminal kinase.";
RL FEBS Lett. 506:196-200(2001).
RN [5]
RP FUNCTION.
RX PubMed=14627710; DOI=10.1074/jbc.m307608200;
RA Heinrich R., Livne E., Ben-Izhak O., Aronheim A.;
RT "The c-Jun dimerization protein 2 inhibits cell transformation and acts as
RT a tumor suppressor gene.";
RL J. Biol. Chem. 279:5708-5715(2004).
RN [6]
RP INTERACTION WITH ATF2, PHOSPHORYLATION AT THR-148 BY MAPK8/JNK1, AND
RP MUTAGENESIS OF THR-148.
RX PubMed=18307971; DOI=10.1016/j.ab.2008.01.038;
RA Murata T., Shinozuka Y., Obata Y., Yokoyama K.K.;
RT "Phosphorylation of two eukaryotic transcription factors, Jun dimerization
RT protein 2 and activation transcription factor 2, in Escherichia coli by Jun
RT N-terminal kinase 1.";
RL Anal. Biochem. 376:115-121(2008).
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:12707301, ECO:0000269|PubMed:14627710}.
CC -!- SUBUNIT: Forms a homodimer or heterodimer with JUN, JUNB, JUND, CEBPG
CC and ATF2 thereby inhibiting transactivation by JUN, ATF2 and CEBPG (By
CC similarity). Binds multiple DNA elements such as cAMP-response element
CC (CRE) and TPA response element (TRE) either as homodimer or
CC heterodimer. Interacts with IRF2BP1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in all adult tissues tested
CC as well in embryos. {ECO:0000269|PubMed:11231009}.
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:0000269|PubMed:11602244,
CC ECO:0000269|PubMed:18307971}.
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; AB077438; BAB83764.1; -; mRNA.
DR EMBL; BC019780; AAH19780.1; -; mRNA.
DR CCDS; CCDS26060.1; -.
DR RefSeq; NP_001191981.1; NM_001205052.1.
DR RefSeq; NP_001191982.1; NM_001205053.1.
DR RefSeq; NP_112149.2; NM_030887.2.
DR AlphaFoldDB; P97875; -.
DR SMR; P97875; -.
DR BioGRID; 219888; 14.
DR ELM; P97875; -.
DR IntAct; P97875; 9.
DR STRING; 10090.ENSMUSP00000059724; -.
DR iPTMnet; P97875; -.
DR PhosphoSitePlus; P97875; -.
DR MaxQB; P97875; -.
DR PaxDb; P97875; -.
DR PeptideAtlas; P97875; -.
DR PRIDE; P97875; -.
DR ProteomicsDB; 269234; -.
DR Antibodypedia; 25829; 124 antibodies from 23 providers.
DR DNASU; 81703; -.
DR Ensembl; ENSMUST00000050687; ENSMUSP00000059724; ENSMUSG00000034271.
DR Ensembl; ENSMUST00000171754; ENSMUSP00000129985; ENSMUSG00000034271.
DR Ensembl; ENSMUST00000177587; ENSMUSP00000136823; ENSMUSG00000034271.
DR GeneID; 81703; -.
DR KEGG; mmu:81703; -.
DR UCSC; uc007ohb.1; mouse.
DR CTD; 122953; -.
DR MGI; MGI:1932093; Jdp2.
DR VEuPathDB; HostDB:ENSMUSG00000034271; -.
DR eggNOG; KOG1414; Eukaryota.
DR GeneTree; ENSGT00940000155693; -.
DR HOGENOM; CLU_088612_0_1_1; -.
DR InParanoid; P97875; -.
DR OMA; XESERLE; -.
DR OrthoDB; 1457971at2759; -.
DR PhylomeDB; P97875; -.
DR TreeFam; TF326301; -.
DR BioGRID-ORCS; 81703; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Jdp2; mouse.
DR PRO; PR:P97875; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P97875; protein.
DR Bgee; ENSMUSG00000034271; Expressed in granulocyte and 275 other tissues.
DR ExpressionAtlas; P97875; baseline and differential.
DR Genevisible; P97875; MM.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0035497; F:cAMP response element binding; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI.
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; IDA:NTNU_SB.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0043522; F:leucine zipper domain binding; IPI:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0045444; P:fat cell differentiation; IDA:MGI.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0031065; P:positive regulation of histone deacetylation; IGI:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
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_0000331131"
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:0000269|PubMed:11602244,
FT ECO:0000269|PubMed:18307971"
FT CROSSLNK 65
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8WYK2"
FT MUTAGEN 148
FT /note="T->A: Blocks phosphorylation by MAPK8."
FT /evidence="ECO:0000269|PubMed:11602244,
FT ECO:0000269|PubMed:18307971"
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
