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Jun dimerization protein 2

 JDP2_MOUSE              Reviewed;         163 AA.
P97875;
29-APR-2008, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 2.
20-JUN-2018, entry version 141.
RecName: Full=Jun dimerization protein 2;
Name=Jdp2; Synonyms=Jundm2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
PubMed=12707301; DOI=10.1084/jem.20021321;
Kawaida R., Ohtsuka T., Okutsu J., Takahashi T., Kadono Y., Oda H.,
Hikita A., Nakamura K., Tanaka S., Furukawa H.;
"Jun dimerization protein 2 (JDP2), a member of the AP-1 family of
transcription factor, mediates osteoclast differentiation induced by
RANKL.";
J. Exp. Med. 197:1029-1035(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
TISSUE SPECIFICITY, INTERACTION WITH ATF2, AND DNA-BINDING.
PubMed=11231009; DOI=10.1016/S0014-5793(00)02387-5;
Jin C., Ugai H., Song J., Murata T., Nili F., Sun K., Horikoshi M.,
Yokoyama K.K.;
"Identification of mouse Jun dimerization protein 2 as a novel
repressor of ATF-2.";
FEBS Lett. 489:34-41(2001).
[4]
INTERACTION WITH ATF2, PHOSPHORYLATION AT THR-148 BY MAPK8, AND
MUTAGENESIS OF THR-148.
PubMed=11602244; DOI=10.1016/S0014-5793(01)02907-6;
Katz S., Heinrich R., Aronheim A.;
"The AP-1 repressor, JDP2, is a bona fide substrate for the c-Jun N-
terminal kinase.";
FEBS Lett. 506:196-200(2001).
[5]
FUNCTION.
PubMed=14627710; DOI=10.1074/jbc.M307608200;
Heinrich R., Livne E., Ben-Izhak O., Aronheim A.;
"The c-Jun dimerization protein 2 inhibits cell transformation and
acts as a tumor suppressor gene.";
J. Biol. Chem. 279:5708-5715(2004).
[6]
INTERACTION WITH ATF2, PHOSPHORYLATION AT THR-148 BY MAPK8/JNK1, AND
MUTAGENESIS OF THR-148.
PubMed=18307971; DOI=10.1016/j.ab.2008.01.038;
Murata T., Shinozuka Y., Obata Y., Yokoyama K.K.;
"Phosphorylation of two eukaryotic transcription factors, Jun
dimerization protein 2 and activation transcription factor 2, in
Escherichia coli by Jun N-terminal kinase 1.";
Anal. Biochem. 376:115-121(2008).
-!- FUNCTION: Component of the AP-1 transcription factor that
represses transactivation mediated by the Jun family of proteins.
Involved in a variety of transcriptional responses associated with
AP-1, such as UV-induced apoptosis, cell differentiation,
tumorigenesis and antitumogeneris. Can also function as a
repressor by recruiting histone deacetylase 3/HDAC3 to the
promoter region of JUN. May control transcription via direct
regulation of the modification of histones and the assembly of
chromatin (By similarity). {ECO:0000250,
ECO:0000269|PubMed:12707301, ECO:0000269|PubMed:14627710}.
-!- SUBUNIT: Forms a homodimer or heterodimer with JUN, JUNB, JUND,
CEBPG and ATF2 thereby inhibiting transactivation by JUN, ATF2 and
CEBPG (By similarity). Binds multiple DNA elements such as cAMP-
response element (CRE) and TPA response element (TRE) either as
homodimer or heterodimer. Interacts with IRF2BP1 (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed in all adult tissues
tested as well in embryos. {ECO:0000269|PubMed:11231009}.
-!- PTM: Phosphorylation of Thr-148 by MAPK8 in response to different
stress conditions such as, UV irradiation, oxidatives stress and
anisomycin treatments. {ECO:0000269|PubMed:11602244,
ECO:0000269|PubMed:18307971}.
-!- PTM: Polyubiquitinated; probably by IRF2BP1. {ECO:0000250}.
-!- SIMILARITY: Belongs to the bZIP family. ATF subfamily.
{ECO:0000305}.
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EMBL; AB077438; BAB83764.1; -; mRNA.
EMBL; BC019780; AAH19780.1; -; mRNA.
CCDS; CCDS26060.1; -.
RefSeq; NP_001191981.1; NM_001205052.1.
RefSeq; NP_001191982.1; NM_001205053.1.
RefSeq; NP_112149.2; NM_030887.2.
UniGene; Mm.103560; -.
ProteinModelPortal; P97875; -.
SMR; P97875; -.
BioGrid; 219888; 14.
ELM; P97875; -.
STRING; 10090.ENSMUSP00000059724; -.
iPTMnet; P97875; -.
PhosphoSitePlus; P97875; -.
MaxQB; P97875; -.
PaxDb; P97875; -.
PeptideAtlas; P97875; -.
PRIDE; P97875; -.
Ensembl; ENSMUST00000050687; ENSMUSP00000059724; ENSMUSG00000034271.
Ensembl; ENSMUST00000171754; ENSMUSP00000129985; ENSMUSG00000034271.
Ensembl; ENSMUST00000177587; ENSMUSP00000136823; ENSMUSG00000034271.
GeneID; 81703; -.
KEGG; mmu:81703; -.
UCSC; uc007ohb.1; mouse.
CTD; 122953; -.
MGI; MGI:1932093; Jdp2.
eggNOG; KOG1414; Eukaryota.
eggNOG; ENOG4111CH5; LUCA.
GeneTree; ENSGT00730000110847; -.
HOGENOM; HOG000034126; -.
HOVERGEN; HBG057870; -.
InParanoid; P97875; -.
KO; K09033; -.
OMA; XESERLE; -.
OrthoDB; EOG091G0M4N; -.
PhylomeDB; P97875; -.
TreeFam; TF326301; -.
PRO; PR:P97875; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000034271; -.
ExpressionAtlas; P97875; baseline and differential.
Genevisible; P97875; MM.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0003700; F:DNA binding transcription factor activity; ISO:MGI.
GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0045599; P:negative regulation of fat cell differentiation; IDA:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
GO; GO:0031065; P:positive regulation of histone deacetylation; IGI:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR000837; AP-1.
InterPro; IPR004827; bZIP.
InterPro; IPR029819; JDP2.
PANTHER; PTHR23351; PTHR23351; 1.
PANTHER; PTHR23351:SF10; PTHR23351:SF10; 1.
Pfam; PF00170; bZIP_1; 1.
PRINTS; PR00042; LEUZIPPRFOS.
SMART; SM00338; BRLZ; 1.
PROSITE; PS50217; BZIP; 1.
PROSITE; PS00036; BZIP_BASIC; 1.
1: Evidence at protein level;
Complete proteome; DNA-binding; Isopeptide bond; Nucleus;
Phosphoprotein; Reference proteome; Repressor; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 163 Jun dimerization protein 2.
/FTId=PRO_0000331131.
DOMAIN 72 135 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 74 96 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 100 128 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
MOD_RES 148 148 Phosphothreonine; by MAPK8.
{ECO:0000269|PubMed:11602244,
ECO:0000269|PubMed:18307971}.
CROSSLNK 65 65 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q8WYK2}.
MUTAGEN 148 148 T->A: Blocks phosphorylation by MAPK8.
{ECO:0000269|PubMed:11602244,
ECO:0000269|PubMed:18307971}.
SEQUENCE 163 AA; 18675 MW; A8AB65A7D20564F8 CRC64;
MMPGQIPDPS VTAGSLPGLG PLTGLPSSAL TTEELKYADI RNIGAMIAPL HFLEVKLGKR
PQPVKSELDE EEERRKRRRE KNKVAAARCR NKKKERTEFL QRESERLELM NAELKTQIEE
LKLERQQLIL MLNRHRPTCI VRTDSVRTPE SEGNPLLEQL DKK


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