ID   JDP2_HUMAN              Reviewed;         163 AA.
AC   Q8WYK2; J3KN58; O95430; Q9UIE4;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 172.
DE   RecName: Full=Jun dimerization protein 2;
GN   Name=JDP2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
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 GENOMIC DNA].
RX   PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA   Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA   Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA   Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA   Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA   Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA   Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA   Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA   Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA   Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA   Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA   Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA   Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA   Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon;
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   [5]
RP   FUNCTION.
RX   PubMed=12903123; DOI=10.1093/nass/2.1.97;
RA   Jin C., Li H., Ugai H., Murata T., Yokoyama K.K.;
RT   "Transcriptional regulation of the c-jun gene by AP-1 repressor protein
RT   JDP2 during the differentiation of F9 cells.";
RL   Nucleic Acids Res. Suppl. 2:97-98(2002).
RN   [6]
RP   FUNCTION.
RX   PubMed=16518400; DOI=10.1038/nsmb1063;
RA   Jin C., Kato K., Chimura T., Yamasaki T., Nakade K., Murata T., Li H.,
RA   Pan J., Zhao M., Sun K., Chiu R., Ito T., Nagata K., Horikoshi M.,
RA   Yokoyama K.K.;
RT   "Regulation of histone acetylation and nucleosome assembly by transcription
RT   factor JDP2.";
RL   Nat. Struct. Mol. Biol. 13:331-338(2006).
RN   [7]
RP   FUNCTION.
RX   PubMed=16026868; DOI=10.1016/j.bbamcr.2005.06.008;
RA   Lerdrup M., Holmberg C., Dietrich N., Shaulian E., Herdegen T.,
RA   Jaeaettelae M., Kallunki T.;
RT   "Depletion of the AP-1 repressor JDP2 induces cell death similar to
RT   apoptosis.";
RL   Biochim. Biophys. Acta 1745:29-37(2005).
RN   [8]
RP   PHOSPHORYLATION AT THR-148 BY MAPK8, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
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).
RN   [9]
RP   UBIQUITINATION, AND INTERACTION WITH IRF2BP1.
RX   PubMed=18671972; DOI=10.1016/j.febslet.2008.07.033;
RA   Kimura M.;
RT   "IRF2-binding protein-1 is a JDP2 ubiquitin ligase and an inhibitor of
RT   ATF2-dependent transcription.";
RL   FEBS Lett. 582:2833-2837(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-148, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [11]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-65, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [12]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-65, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA   Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "System-wide analysis of SUMOylation dynamics in response to replication
RT   stress reveals novel small ubiquitin-like modified target proteins and
RT   acceptor lysines relevant for genome stability.";
RL   Mol. Cell. Proteomics 14:1419-1434(2015).
RN   [13]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-65, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
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. {ECO:0000269|PubMed:12707301,
CC       ECO:0000269|PubMed:12903123, ECO:0000269|PubMed:16026868,
CC       ECO:0000269|PubMed:16518400}.
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 heterodimer
CC       (By similarity). Interacts with IRF2BP1. {ECO:0000250,
CC       ECO:0000269|PubMed:18671972}.
CC   -!- INTERACTION:
CC       Q8WYK2; P18848: ATF4; NbExp=3; IntAct=EBI-1248415, EBI-492498;
CC       Q8WYK2; Q02930-3: CREB5; NbExp=3; IntAct=EBI-1248415, EBI-10192698;
CC       Q8WYK2; P35638: DDIT3; NbExp=3; IntAct=EBI-1248415, EBI-742651;
CC       Q8WYK2; Q8IU81: IRF2BP1; NbExp=4; IntAct=EBI-1248415, EBI-6115514;
CC       Q8WYK2; P17275: JUNB; NbExp=3; IntAct=EBI-1248415, EBI-748062;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8WYK2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8WYK2-2; Sequence=VSP_047128;
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:18307971}.
CC   -!- PTM: Polyubiquitinated; probably by IRF2BP1.
CC       {ECO:0000269|PubMed:18671972}.
CC   -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily. {ECO:0000305}.
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DR   EMBL; AB077880; BAB83896.1; -; mRNA.
DR   EMBL; AF111167; AAC98313.1; -; Genomic_DNA.
DR   EMBL; AC009363; AAF21148.1; -; Genomic_DNA.
DR   EMBL; CH471061; EAW81231.1; -; Genomic_DNA.
DR   EMBL; BC051303; AAH51303.1; -; mRNA.
DR   CCDS; CCDS45139.1; -. [Q8WYK2-2]
DR   CCDS; CCDS9842.1; -. [Q8WYK2-1]
DR   RefSeq; NP_001128519.1; NM_001135047.1. [Q8WYK2-1]
DR   RefSeq; NP_001128520.1; NM_001135048.1. [Q8WYK2-1]
DR   RefSeq; NP_001128521.1; NM_001135049.1. [Q8WYK2-2]
DR   RefSeq; NP_569736.1; NM_130469.3. [Q8WYK2-1]
DR   RefSeq; XP_005267389.1; XM_005267332.4. [Q8WYK2-1]
DR   RefSeq; XP_016876461.1; XM_017020972.1.
DR   RefSeq; XP_016876462.1; XM_017020973.1. [Q8WYK2-1]
DR   RefSeq; XP_016876463.1; XM_017020974.1.
DR   RefSeq; XP_016876464.1; XM_017020975.1.
DR   AlphaFoldDB; Q8WYK2; -.
DR   SMR; Q8WYK2; -.
DR   BioGRID; 125807; 23.
DR   ComplexPortal; CPX-6419; bZIP transcription factor complex, ATF2-JDP2.
DR   IntAct; Q8WYK2; 16.
DR   MINT; Q8WYK2; -.
DR   STRING; 9606.ENSP00000267569; -.
DR   DrugBank; DB00852; Pseudoephedrine.
DR   iPTMnet; Q8WYK2; -.
DR   PhosphoSitePlus; Q8WYK2; -.
DR   BioMuta; JDP2; -.
DR   DMDM; 74751626; -.
DR   EPD; Q8WYK2; -.
DR   jPOST; Q8WYK2; -.
DR   MassIVE; Q8WYK2; -.
DR   MaxQB; Q8WYK2; -.
DR   PaxDb; 9606-ENSP00000267569; -.
DR   PeptideAtlas; Q8WYK2; -.
DR   ProteomicsDB; 75164; -. [Q8WYK2-1]
DR   Antibodypedia; 25829; 152 antibodies from 23 providers.
DR   DNASU; 122953; -.
DR   Ensembl; ENST00000267569.5; ENSP00000267569.5; ENSG00000140044.13. [Q8WYK2-2]
DR   Ensembl; ENST00000419727.6; ENSP00000415558.2; ENSG00000140044.13. [Q8WYK2-1]
DR   Ensembl; ENST00000435893.6; ENSP00000399587.2; ENSG00000140044.13. [Q8WYK2-1]
DR   Ensembl; ENST00000437176.5; ENSP00000409787.1; ENSG00000140044.13. [Q8WYK2-1]
DR   Ensembl; ENST00000651602.1; ENSP00000498745.1; ENSG00000140044.13. [Q8WYK2-1]
DR   GeneID; 122953; -.
DR   KEGG; hsa:122953; -.
DR   MANE-Select; ENST00000651602.1; ENSP00000498745.1; NM_001135048.2; NP_001128520.1.
DR   UCSC; uc001xrq.4; human. [Q8WYK2-1]
DR   AGR; HGNC:17546; -.
DR   CTD; 122953; -.
DR   DisGeNET; 122953; -.
DR   GeneCards; JDP2; -.
DR   HGNC; HGNC:17546; JDP2.
DR   HPA; ENSG00000140044; Low tissue specificity.
DR   MIM; 608657; gene.
DR   neXtProt; NX_Q8WYK2; -.
DR   OpenTargets; ENSG00000140044; -.
DR   PharmGKB; PA162392499; -.
DR   VEuPathDB; HostDB:ENSG00000140044; -.
DR   eggNOG; KOG1414; Eukaryota.
DR   GeneTree; ENSGT00940000155693; -.
DR   HOGENOM; CLU_088612_0_1_1; -.
DR   InParanoid; Q8WYK2; -.
DR   OMA; FKVGLMQ; -.
DR   OrthoDB; 5360790at2759; -.
DR   PhylomeDB; Q8WYK2; -.
DR   TreeFam; TF326301; -.
DR   PathwayCommons; Q8WYK2; -.
DR   SignaLink; Q8WYK2; -.
DR   SIGNOR; Q8WYK2; -.
DR   BioGRID-ORCS; 122953; 20 hits in 1185 CRISPR screens.
DR   ChiTaRS; JDP2; human.
DR   GeneWiki; JDP2_(gene); -.
DR   GeneWiki; Jun_dimerization_protein; -.
DR   GenomeRNAi; 122953; -.
DR   Pharos; Q8WYK2; Tbio.
DR   PRO; PR:Q8WYK2; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q8WYK2; Protein.
DR   Bgee; ENSG00000140044; Expressed in synovial joint and 174 other cell types or tissues.
DR   ExpressionAtlas; Q8WYK2; baseline and differential.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:0005634; C:nucleus; EXP:ComplexPortal.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; EXP:ComplexPortal.
DR   GO; GO:0035497; F:cAMP response element binding; IEA:Ensembl.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:ARUK-UCL.
DR   GO; GO:0140713; F:histone chaperone activity; IEA:Ensembl.
DR   GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR   GO; GO:0043522; F:leucine zipper domain binding; IEA:Ensembl.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR   GO; GO:0006338; P:chromatin remodeling; IEA:Ensembl.
DR   GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0045599; P:negative regulation of fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; Q8WYK2; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; DNA-binding; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Reference proteome; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN           1..163
FT                   /note="Jun dimerization protein 2"
FT                   /id="PRO_0000331130"
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          58..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        58..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:18307971,
FT                   ECO:0007744|PubMed:23186163"
FT   CROSSLNK        65
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         1
FT                   /note="M -> MVAGWPATPPAM (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_047128"
FT   VARIANT         13
FT                   /note="T -> A (in dbSNP:rs3625)"
FT                   /id="VAR_042738"
SQ   SEQUENCE   163 AA;  18704 MW;  29C576AF2C574BA8 CRC64;
     MMPGQIPDPS VTTGSLPGLG PLTGLPSSAL TVEELKYADI RNLGAMIAPL HFLEVKLGKR
     PQPVKSELDE EEERRKRRRE KNKVAAARCR NKKKERTEFL QRESERLELM NAELKTQIEE
     LKQERQQLIL MLNRHRPTCI VRTDSVKTPE SEGNPLLEQL EKK
//