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   27-MAR-2024, entry version 172.
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.ENSMUSP00000136823; -.
DR   iPTMnet; P97875; -.
DR   PhosphoSitePlus; P97875; -.
DR   MaxQB; P97875; -.
DR   PaxDb; 10090-ENSMUSP00000059724; -.
DR   PeptideAtlas; P97875; -.
DR   ProteomicsDB; 269234; -.
DR   Antibodypedia; 25829; 152 antibodies from 23 providers.
DR   DNASU; 81703; -.
DR   Ensembl; ENSMUST00000050687.14; ENSMUSP00000059724.7; ENSMUSG00000034271.17.
DR   Ensembl; ENSMUST00000171754.3; ENSMUSP00000129985.3; ENSMUSG00000034271.17.
DR   Ensembl; ENSMUST00000177587.9; ENSMUSP00000136823.2; ENSMUSG00000034271.17.
DR   GeneID; 81703; -.
DR   KEGG; mmu:81703; -.
DR   UCSC; uc007ohb.1; mouse.
DR   AGR; MGI:1932093; -.
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; FKVGLMQ; -.
DR   OrthoDB; 5360790at2759; -.
DR   PhylomeDB; P97875; -.
DR   TreeFam; TF326301; -.
DR   BioGRID-ORCS; 81703; 3 hits in 79 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 276 other cell types or tissues.
DR   ExpressionAtlas; P97875; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO: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:0140713; F:histone chaperone activity; IGI:MGI.
DR   GO; GO:0042826; F:histone deacetylase binding; IPI: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:0006338; P:chromatin remodeling; IGI: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:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR   Gene3D; 1.20.5.170; -; 1.
DR   InterPro; IPR000837; AP-1.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   PANTHER; PTHR23351; FOS TRANSCRIPTION FACTOR-RELATED; 1.
DR   PANTHER; PTHR23351:SF10; JUN DIMERIZATION PROTEIN 2; 1.
DR   Pfam; PF00170; bZIP_1; 1.
DR   PRINTS; PR00042; LEUZIPPRFOS.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; Leucine zipper domain; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
DR   Genevisible; P97875; MM.
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
//