Reviewed, UniProtKB/Swiss-Prot Q8WYK2 (JDP2_HUMAN)

Names and origin

Protein names

Recommended name:
    Jun dimerization protein 2

Gene names

Name:

JDP2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	163 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

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. Ref.1 Ref.5 Ref.6 Ref.7
Subunit structure	Forms 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.
Subcellular location	Nucleus Probable.
Post-translational modification	Phosphorylation of Thr-148 by MAPK8 in response to different stress conditions such as, UV irradiation, oxidatives stress and anisomycin treatments.
Sequence similarities	Belongs to the bZIP family. ATF subfamily. Contains 1 bZIP domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Ligand	DNA-binding
Molecular function	Repressor
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein dimerization activity Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro transcription factor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PGR	P06401	1	EBI-1248415,EBI-78539

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 163	163	Jun dimerization protein 2		PRO_0000331130
Regions
	Domain	100 – 135	36	Leucine-zipper
	DNA binding	77 – 92	16	Basic motif
Amino acid modifications
	Modified residue	148	1	Phosphothreonine; by MAPK8 Ref.8
Natural variations
	Natural variant	13	1	T → A: dbSNP rs3625.		VAR_042738

Sequences

	Sequence		Length	Mass (Da)
	Q8WYK2-1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 29C576AF2C574BA8	FASTA	163	18,704
	10 20 30 40 50 60 MMPGQIPDPS VTTGSLPGLG PLTGLPSSAL TVEELKYADI RNLGAMIAPL HFLEVKLGKR 70 80 90 100 110 120 PQPVKSELDE EEERRKRRRE KNKVAAARCR NKKKERTEFL QRESERLELM NAELKTQIEE 130 140 150 160 LKQERQQLIL MLNRHRPTCI VRTDSVKTPE SEGNPLLEQL EKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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(2003) [PubMed: 12707301] [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(2003) [PubMed: 12508121] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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(2004) [PubMed: 15489334] [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(2002) [PubMed: 12903123] [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(2006) [PubMed: 16518400] [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(2005) [PubMed: 16026868] [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(2008) [PubMed: 18307971] [Abstract] Cited for: MASS SPECTROMETRY, PHOSPHORYLATION AT THR-148 BY MAPK8.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
IPI	IPI00913993.
RefSeq	NP_001128519.1. NP_001128520.1. NP_001128521.1. NP_569736.1.
UniGene	Hs.196482 Hs.699420
3D structure databases
HSSP	HSSP built from PDB template 1FOS based on UniProtKB P01100.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8WYK2. 1 interaction.
STRING	Q8WYK2.
PTM databases
PhosphoSite	Q8WYK2.
Proteomic databases
PRIDE	Q8WYK2.
Genome annotation databases
Ensembl	ENST00000267569; ENSP00000267569; ENSG00000140044; Homo sapiens. [Genome view] ENST00000413024; ENSP00000415655; ENSG00000140044; Homo sapiens. [Genome view] ENST00000419727; ENSP00000415558; ENSG00000140044; Homo sapiens. [Genome view] ENST00000435893; ENSP00000399587; ENSG00000140044; Homo sapiens. [Genome view] ENST00000437176; ENSP00000409787; ENSG00000140044; Homo sapiens. [Genome view]
GeneID	122953.
KEGG	hsa:122953.
UCSC	uc001xrq.1. human.
Organism-specific databases
CTD	122953.
GeneCards	GC14P074964.
HGNC	HGNC:17546. JDP2.
MIM	608657. gene.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q8WYK2.
HOVERGEN	Q8WYK2.
OMA	PESEANP.
Gene expression databases
ArrayExpress	Q8WYK2.
Bgee	Q8WYK2.
CleanEx	HS_JDP2.
Genevestigator	Q8WYK2.
Family and domain databases
InterPro	IPR011616. bZIP_1. IPR000837. Leuzip_Fos. IPR004827. TF_bZIP. [Graphical view]
Pfam	PF00170. bZIP_1. 1 hit. [Graphical view]
PRINTS	PR00042. LEUZIPPRFOS.
SMART	SM00338. BRLZ. 1 hit. [Graphical view]
PROSITE	PS50217. BZIP. 1 hit. PS00036. BZIP_BASIC. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	81038.
SOURCE	Search...

Entry information

Entry name

JDP2_HUMAN

Accession

Primary (citable) accession number: Q8WYK2
Secondary accession number(s): O95430, Q9UIE4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	March 1, 2002
Last modified:	November 3, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.