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Protein

Jun dimerization protein 2

Gene

JDP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Molecular functioni

  1. chromatin binding Source: Ensembl
  2. double-stranded DNA binding Source: Ensembl
  3. sequence-specific DNA binding Source: InterPro
  4. sequence-specific DNA binding transcription factor activity Source: InterPro

GO - Biological processi

  1. negative regulation of fat cell differentiation Source: Ensembl
  2. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  3. positive regulation of histone deacetylation Source: Ensembl
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Jun dimerization protein 2
Gene namesi
Name:JDP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:17546. JDP2.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. nucleoplasm Source: HPA
  2. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162392499.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 163163Jun dimerization protein 2PRO_0000331130Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei148 – 1481Phosphothreonine; by MAPK81 Publication

Post-translational modificationi

Phosphorylation of Thr-148 by MAPK8 in response to different stress conditions such as, UV irradiation, oxidatives stress and anisomycin treatments.1 Publication
Polyubiquitinated; probably by IRF2BP1.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ8WYK2.
PaxDbiQ8WYK2.
PRIDEiQ8WYK2.

PTM databases

PhosphoSiteiQ8WYK2.

Expressioni

Gene expression databases

BgeeiQ8WYK2.
CleanExiHS_JDP2.
ExpressionAtlasiQ8WYK2. baseline and differential.
GenevestigatoriQ8WYK2.

Organism-specific databases

HPAiHPA051651.
HPA059511.

Interactioni

Subunit structurei

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 (By similarity). Interacts with IRF2BP1.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
IRF2BP1Q8IU814EBI-1248415,EBI-6115514

Protein-protein interaction databases

BioGridi125807. 15 interactions.
IntActiQ8WYK2. 12 interactions.
MINTiMINT-189454.
STRINGi9606.ENSP00000267569.

Structurei

3D structure databases

ProteinModelPortaliQ8WYK2.
SMRiQ8WYK2. Positions 73-135.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini72 – 13564bZIPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni74 – 9623Basic motifPROSITE-ProRule annotationAdd
BLAST
Regioni100 – 12829Leucine-zipperPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the bZIP family. ATF subfamily.Curated
Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG280450.
GeneTreeiENSGT00730000110847.
HOGENOMiHOG000034126.
HOVERGENiHBG057870.
InParanoidiQ8WYK2.
KOiK09033.
OMAiKKERTEY.
OrthoDBiEOG70S777.
PhylomeDBiQ8WYK2.
TreeFamiTF326301.

Family and domain databases

InterProiIPR000837. AP-1.
IPR004827. bZIP.
IPR029819. JDP2.
[Graphical view]
PANTHERiPTHR23351. PTHR23351. 1 hit.
PTHR23351:SF10. PTHR23351:SF10. 1 hit.
PfamiPF00170. bZIP_1. 1 hit.
[Graphical view]
PRINTSiPR00042. LEUZIPPRFOS.
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8WYK2-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MMPGQIPDPS VTTGSLPGLG PLTGLPSSAL TVEELKYADI RNLGAMIAPL
60 70 80 90 100
HFLEVKLGKR PQPVKSELDE EEERRKRRRE KNKVAAARCR NKKKERTEFL
110 120 130 140 150
QRESERLELM NAELKTQIEE LKQERQQLIL MLNRHRPTCI VRTDSVKTPE
160
SEGNPLLEQL EKK
Length:163
Mass (Da):18,704
Last modified:March 1, 2002 - v1
Checksum:i29C576AF2C574BA8
GO
Isoform 2 (identifier: Q8WYK2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MVAGWPATPPAM

Note: Gene prediction based on EST data.

Show »
Length:174
Mass (Da):19,783
Checksum:i4E073AA3A46F0B7C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti13 – 131T → A.
Corresponds to variant rs3625 [ dbSNP | Ensembl ].
VAR_042738

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MVAGWPATPPAM in isoform 2. CuratedVSP_047128

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB077880 mRNA. Translation: BAB83896.1.
AF111167 Genomic DNA. Translation: AAC98313.1.
AC009363 Genomic DNA. Translation: AAF21148.1.
CH471061 Genomic DNA. Translation: EAW81231.1.
BC051303 mRNA. Translation: AAH51303.1.
CCDSiCCDS45139.1. [Q8WYK2-2]
CCDS9842.1. [Q8WYK2-1]
RefSeqiNP_001128519.1. NM_001135047.1. [Q8WYK2-1]
NP_001128520.1. NM_001135048.1. [Q8WYK2-1]
NP_001128521.1. NM_001135049.1. [Q8WYK2-2]
NP_569736.1. NM_130469.3. [Q8WYK2-1]
XP_005267389.1. XM_005267332.2. [Q8WYK2-1]
XP_006720095.1. XM_006720032.1. [Q8WYK2-2]
UniGeneiHs.196482.

Genome annotation databases

EnsembliENST00000267569; ENSP00000267569; ENSG00000140044. [Q8WYK2-2]
ENST00000419727; ENSP00000415558; ENSG00000140044. [Q8WYK2-1]
ENST00000435893; ENSP00000399587; ENSG00000140044. [Q8WYK2-1]
ENST00000437176; ENSP00000409787; ENSG00000140044. [Q8WYK2-1]
GeneIDi122953.
KEGGihsa:122953.
UCSCiuc010asj.3. human. [Q8WYK2-1]

Polymorphism databases

DMDMi74751626.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB077880 mRNA. Translation: BAB83896.1.
AF111167 Genomic DNA. Translation: AAC98313.1.
AC009363 Genomic DNA. Translation: AAF21148.1.
CH471061 Genomic DNA. Translation: EAW81231.1.
BC051303 mRNA. Translation: AAH51303.1.
CCDSiCCDS45139.1. [Q8WYK2-2]
CCDS9842.1. [Q8WYK2-1]
RefSeqiNP_001128519.1. NM_001135047.1. [Q8WYK2-1]
NP_001128520.1. NM_001135048.1. [Q8WYK2-1]
NP_001128521.1. NM_001135049.1. [Q8WYK2-2]
NP_569736.1. NM_130469.3. [Q8WYK2-1]
XP_005267389.1. XM_005267332.2. [Q8WYK2-1]
XP_006720095.1. XM_006720032.1. [Q8WYK2-2]
UniGeneiHs.196482.

3D structure databases

ProteinModelPortaliQ8WYK2.
SMRiQ8WYK2. Positions 73-135.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125807. 15 interactions.
IntActiQ8WYK2. 12 interactions.
MINTiMINT-189454.
STRINGi9606.ENSP00000267569.

Chemistry

DrugBankiDB00852. Pseudoephedrine.

PTM databases

PhosphoSiteiQ8WYK2.

Polymorphism databases

DMDMi74751626.

Proteomic databases

MaxQBiQ8WYK2.
PaxDbiQ8WYK2.
PRIDEiQ8WYK2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000267569; ENSP00000267569; ENSG00000140044. [Q8WYK2-2]
ENST00000419727; ENSP00000415558; ENSG00000140044. [Q8WYK2-1]
ENST00000435893; ENSP00000399587; ENSG00000140044. [Q8WYK2-1]
ENST00000437176; ENSP00000409787; ENSG00000140044. [Q8WYK2-1]
GeneIDi122953.
KEGGihsa:122953.
UCSCiuc010asj.3. human. [Q8WYK2-1]

Organism-specific databases

CTDi122953.
GeneCardsiGC14P075894.
H-InvDBHIX0026627.
HGNCiHGNC:17546. JDP2.
HPAiHPA051651.
HPA059511.
MIMi608657. gene.
neXtProtiNX_Q8WYK2.
PharmGKBiPA162392499.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG280450.
GeneTreeiENSGT00730000110847.
HOGENOMiHOG000034126.
HOVERGENiHBG057870.
InParanoidiQ8WYK2.
KOiK09033.
OMAiKKERTEY.
OrthoDBiEOG70S777.
PhylomeDBiQ8WYK2.
TreeFamiTF326301.

Miscellaneous databases

GeneWikiiJDP2_(gene).
Jun_dimerization_protein.
GenomeRNAii122953.
NextBioi35534825.
PROiQ8WYK2.
SOURCEiSearch...

Gene expression databases

BgeeiQ8WYK2.
CleanExiHS_JDP2.
ExpressionAtlasiQ8WYK2. baseline and differential.
GenevestigatoriQ8WYK2.

Family and domain databases

InterProiIPR000837. AP-1.
IPR004827. bZIP.
IPR029819. JDP2.
[Graphical view]
PANTHERiPTHR23351. PTHR23351. 1 hit.
PTHR23351:SF10. PTHR23351:SF10. 1 hit.
PfamiPF00170. bZIP_1. 1 hit.
[Graphical view]
PRINTSiPR00042. LEUZIPPRFOS.
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Jun dimerization protein 2 (JDP2), a member of the AP-1 family of transcription factor, mediates osteoclast differentiation induced by RANKL."
    Kawaida R., Ohtsuka T., Okutsu J., Takahashi T., Kadono Y., Oda H., Hikita A., Nakamura K., Tanaka S., Furukawa H.
    J. Exp. Med. 197:1029-1035(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  2. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon.
  5. "Transcriptional regulation of the c-jun gene by AP-1 repressor protein JDP2 during the differentiation of F9 cells."
    Jin C., Li H., Ugai H., Murata T., Yokoyama K.K.
    Nucleic Acids Res. Suppl. 2:97-98(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Regulation of histone acetylation and nucleosome assembly by transcription factor JDP2."
    Jin C., Kato K., Chimura T., Yamasaki T., Nakade K., Murata T., Li H., Pan J., Zhao M., Sun K., Chiu R., Ito T., Nagata K., Horikoshi M., Yokoyama K.K.
    Nat. Struct. Mol. Biol. 13:331-338(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Depletion of the AP-1 repressor JDP2 induces cell death similar to apoptosis."
    Lerdrup M., Holmberg C., Dietrich N., Shaulian E., Herdegen T., Jaeaettelae M., Kallunki T.
    Biochim. Biophys. Acta 1745:29-37(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Phosphorylation of two eukaryotic transcription factors, Jun dimerization protein 2 and activation transcription factor 2, in Escherichia coli by Jun N-terminal kinase 1."
    Murata T., Shinozuka Y., Obata Y., Yokoyama K.K.
    Anal. Biochem. 376:115-121(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-148 BY MAPK8, IDENTIFICATION BY MASS SPECTROMETRY.
  9. "IRF2-binding protein-1 is a JDP2 ubiquitin ligase and an inhibitor of ATF2-dependent transcription."
    Kimura M.
    FEBS Lett. 582:2833-2837(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, INTERACTION WITH IRF2BP1.

Entry informationi

Entry nameiJDP2_HUMAN
AccessioniPrimary (citable) accession number: Q8WYK2
Secondary accession number(s): J3KN58, O95430, Q9UIE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: March 1, 2002
Last modified: February 4, 2015
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.