JDP2_HUMAN
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 03-AUG-2022, entry version 163.
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. [Q8WYK2-2]
DR RefSeq; XP_016876462.1; XM_017020973.1. [Q8WYK2-1]
DR RefSeq; XP_016876463.1; XM_017020974.1. [Q8WYK2-1]
DR RefSeq; XP_016876464.1; XM_017020975.1. [Q8WYK2-1]
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; Q8WYK2; -.
DR PeptideAtlas; Q8WYK2; -.
DR PRIDE; Q8WYK2; -.
DR ProteomicsDB; 75164; -. [Q8WYK2-1]
DR Antibodypedia; 25829; 124 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 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; XESERLE; -.
DR OrthoDB; 1457971at2759; -.
DR PhylomeDB; Q8WYK2; -.
DR TreeFam; TF326301; -.
DR PathwayCommons; Q8WYK2; -.
DR SignaLink; Q8WYK2; -.
DR SIGNOR; Q8WYK2; -.
DR BioGRID-ORCS; 122953; 18 hits in 1104 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 173 other tissues.
DR ExpressionAtlas; Q8WYK2; baseline and differential.
DR Genevisible; Q8WYK2; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IC: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: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: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:0031065; P:positive regulation of histone deacetylation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 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
