Full text data of JUND
JUND
[Confidence: low (only semi-automatic identification from reviews)]
Transcription factor jun-D
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Transcription factor jun-D
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P17535
ID JUND_HUMAN Reviewed; 347 AA.
AC P17535; Q53EK9;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-MAY-2009, sequence version 3.
DT 22-JAN-2014, entry version 133.
DE RecName: Full=Transcription factor jun-D;
GN Name=JUND;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1903194;
RA Berger I., Shaul Y.;
RT "Structure and function of human jun-D.";
RL Oncogene 6:561-566(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-20.
RG NIEHS SNPs program;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 45-347.
RX PubMed=2112242; DOI=10.1093/nar/18.10.3047;
RA Nomura N., Ide M., Sasamoto S., Matsui M., Date T., Ishizaki R.;
RT "Isolation of human cDNA clones of jun-related genes, jun-B and jun-
RT D.";
RL Nucleic Acids Res. 18:3047-3048(1990).
RN [6]
RP FUNCTION, AND INTERACTION WITH MEN1.
RX PubMed=9989505; DOI=10.1016/S0092-8674(00)80967-8;
RA Agarwal S.K., Guru S.C., Heppner C., Erdos M.R., Collins R.M.,
RA Park S.Y., Saggar S., Chandrasekharappa S.C., Collins F.S.,
RA Spiegel A.M., Marx S.J., Burns A.L.;
RT "Menin interacts with the AP1 transcription factor JunD and represses
RT JunD-activated transcription.";
RL Cell 96:143-152(1999).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251; SER-255 AND
RP SER-259, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255 AND SER-259, AND
RP MASS SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255 AND SER-259, AND
RP MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
CC -!- FUNCTION: Transcription factor binding AP-1 sites.
CC -!- SUBUNIT: Binds DNA as a dimer (By similarity). Interacts with
CC MEN1; this interaction represses transcriptional activation.
CC -!- INTERACTION:
CC P61158:ACTR3; NbExp=2; IntAct=EBI-2682803, EBI-351428;
CC P01100:FOS; NbExp=3; IntAct=EBI-2682803, EBI-852851;
CC Q00987:MDM2; NbExp=3; IntAct=EBI-2682803, EBI-389668;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the bZIP family. Jun subfamily.
CC -!- SIMILARITY: Contains 1 bZIP (basic-leucine zipper) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA40010.1; Type=Frameshift; Positions=Several;
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/tnfrsf1b/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/JUNDID179.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X56681; CAA40010.1; ALT_FRAME; mRNA.
DR EMBL; EF044249; ABJ53425.1; -; Genomic_DNA.
DR EMBL; AK223630; BAD97350.1; -; mRNA.
DR EMBL; CH471106; EAW84684.1; -; Genomic_DNA.
DR EMBL; X51346; CAA35739.1; -; mRNA.
DR PIR; A43815; A43815.
DR PIR; S10184; TVHUJD.
DR RefSeq; NP_005345.3; NM_005354.4.
DR UniGene; Hs.2780; -.
DR PDB; 3U86; X-ray; 2.84 A; B=27-39.
DR PDBsum; 3U86; -.
DR ProteinModelPortal; P17535; -.
DR SMR; P17535; 273-324.
DR DIP; DIP-1053N; -.
DR IntAct; P17535; 8.
DR MINT; MINT-260192; -.
DR STRING; 9606.ENSP00000252818; -.
DR PhosphoSite; P17535; -.
DR DMDM; 229462969; -.
DR PaxDb; P17535; -.
DR PRIDE; P17535; -.
DR Ensembl; ENST00000252818; ENSP00000252818; ENSG00000130522.
DR GeneID; 3727; -.
DR KEGG; hsa:3727; -.
DR UCSC; uc002nip.2; human.
DR CTD; 3727; -.
DR GeneCards; GC19M018391; -.
DR H-InvDB; HIX0040163; -.
DR HGNC; HGNC:6206; JUND.
DR HPA; CAB005268; -.
DR MIM; 165162; gene.
DR neXtProt; NX_P17535; -.
DR PharmGKB; PA30008; -.
DR eggNOG; NOG283376; -.
DR HOGENOM; HOG000006648; -.
DR HOVERGEN; HBG001722; -.
DR InParanoid; P17535; -.
DR KO; K04449; -.
DR OMA; QFLYPKV; -.
DR OrthoDB; EOG75MVXV; -.
DR PhylomeDB; P17535; -.
DR SignaLink; P17535; -.
DR ChiTaRS; JUND; human.
DR GeneWiki; JunD; -.
DR GenomeRNAi; 3727; -.
DR NextBio; 14591; -.
DR PRO; PR:P17535; -.
DR Bgee; P17535; -.
DR CleanEx; HS_JUND; -.
DR Genevestigator; P17535; -.
DR GO; GO:0000785; C:chromatin; TAS:ProtInc.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043234; C:protein complex; IEA:Ensembl.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:Ensembl.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:Ensembl.
DR GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0071277; P:cellular response to calcium ion; IEA:Ensembl.
DR GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR GO; GO:0002076; P:osteoblast development; IEA:Ensembl.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
DR GO; GO:0009416; P:response to light stimulus; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0043434; P:response to peptide hormone stimulus; IEA:Ensembl.
DR GO; GO:0006366; P:transcription from RNA polymerase II promoter; IEA:Ensembl.
DR Gene3D; 1.10.880.10; -; 1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR005643; JNK.
DR InterPro; IPR002112; Leuzip_Jun.
DR InterPro; IPR008917; TF_DNA-bd.
DR Pfam; PF00170; bZIP_1; 1.
DR Pfam; PF03957; Jun; 1.
DR PRINTS; PR00043; LEUZIPPRJUN.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF47454; SSF47454; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Complete proteome; DNA-binding; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1 347 Transcription factor jun-D.
FT /FTId=PRO_0000076442.
FT DOMAIN 268 331 bZIP.
FT REGION 268 295 Basic motif (By similarity).
FT REGION 296 324 Leucine-zipper (By similarity).
FT COMPBIAS 158 166 Poly-Ala.
FT MOD_RES 251 251 Phosphoserine.
FT MOD_RES 255 255 Phosphoserine.
FT MOD_RES 259 259 Phosphoserine.
FT VARIANT 20 20 G -> V (in dbSNP:rs41478151).
FT /FTId=VAR_055247.
FT CONFLICT 24 24 S -> T (in Ref. 1; CAA40010).
FT CONFLICT 157 157 A -> R (in Ref. 1; CAA40010).
SQ SEQUENCE 347 AA; 35174 MW; FE85A1AA2B5B9597 CRC64;
METPFYGDEA LSGLGGGASG SGGSFASPGR LFPGAPPTAA AGSMMKKDAL TLSLSEQVAA
ALKPAAAPPP TPLRADGAPS AAPPDGLLAS PDLGLLKLAS PELERLIIQS NGLVTTTPTS
SQFLYPKVAA SEEQEFAEGF VKALEDLHKQ NQLGAGAAAA AAAAAAGGPS GTATGSAPPG
ELAPAAAAPE APVYANLSSY AGGAGGAGGA ATVAFAAEPV PFPPPPPPGA LGPPRLAALK
DEPQTVPDVP SFGESPPLSP IDMDTQERIK AERKRLRNRI AASKCRKRKL ERISRLEEKV
KTLKSQNTEL ASTASLLREQ VAQLKQKVLS HVNSGCQLLP QHQVPAY
//
ID JUND_HUMAN Reviewed; 347 AA.
AC P17535; Q53EK9;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-MAY-2009, sequence version 3.
DT 22-JAN-2014, entry version 133.
DE RecName: Full=Transcription factor jun-D;
GN Name=JUND;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1903194;
RA Berger I., Shaul Y.;
RT "Structure and function of human jun-D.";
RL Oncogene 6:561-566(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-20.
RG NIEHS SNPs program;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 45-347.
RX PubMed=2112242; DOI=10.1093/nar/18.10.3047;
RA Nomura N., Ide M., Sasamoto S., Matsui M., Date T., Ishizaki R.;
RT "Isolation of human cDNA clones of jun-related genes, jun-B and jun-
RT D.";
RL Nucleic Acids Res. 18:3047-3048(1990).
RN [6]
RP FUNCTION, AND INTERACTION WITH MEN1.
RX PubMed=9989505; DOI=10.1016/S0092-8674(00)80967-8;
RA Agarwal S.K., Guru S.C., Heppner C., Erdos M.R., Collins R.M.,
RA Park S.Y., Saggar S., Chandrasekharappa S.C., Collins F.S.,
RA Spiegel A.M., Marx S.J., Burns A.L.;
RT "Menin interacts with the AP1 transcription factor JunD and represses
RT JunD-activated transcription.";
RL Cell 96:143-152(1999).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251; SER-255 AND
RP SER-259, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255 AND SER-259, AND
RP MASS SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255 AND SER-259, AND
RP MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
CC -!- FUNCTION: Transcription factor binding AP-1 sites.
CC -!- SUBUNIT: Binds DNA as a dimer (By similarity). Interacts with
CC MEN1; this interaction represses transcriptional activation.
CC -!- INTERACTION:
CC P61158:ACTR3; NbExp=2; IntAct=EBI-2682803, EBI-351428;
CC P01100:FOS; NbExp=3; IntAct=EBI-2682803, EBI-852851;
CC Q00987:MDM2; NbExp=3; IntAct=EBI-2682803, EBI-389668;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the bZIP family. Jun subfamily.
CC -!- SIMILARITY: Contains 1 bZIP (basic-leucine zipper) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA40010.1; Type=Frameshift; Positions=Several;
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/tnfrsf1b/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/JUNDID179.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X56681; CAA40010.1; ALT_FRAME; mRNA.
DR EMBL; EF044249; ABJ53425.1; -; Genomic_DNA.
DR EMBL; AK223630; BAD97350.1; -; mRNA.
DR EMBL; CH471106; EAW84684.1; -; Genomic_DNA.
DR EMBL; X51346; CAA35739.1; -; mRNA.
DR PIR; A43815; A43815.
DR PIR; S10184; TVHUJD.
DR RefSeq; NP_005345.3; NM_005354.4.
DR UniGene; Hs.2780; -.
DR PDB; 3U86; X-ray; 2.84 A; B=27-39.
DR PDBsum; 3U86; -.
DR ProteinModelPortal; P17535; -.
DR SMR; P17535; 273-324.
DR DIP; DIP-1053N; -.
DR IntAct; P17535; 8.
DR MINT; MINT-260192; -.
DR STRING; 9606.ENSP00000252818; -.
DR PhosphoSite; P17535; -.
DR DMDM; 229462969; -.
DR PaxDb; P17535; -.
DR PRIDE; P17535; -.
DR Ensembl; ENST00000252818; ENSP00000252818; ENSG00000130522.
DR GeneID; 3727; -.
DR KEGG; hsa:3727; -.
DR UCSC; uc002nip.2; human.
DR CTD; 3727; -.
DR GeneCards; GC19M018391; -.
DR H-InvDB; HIX0040163; -.
DR HGNC; HGNC:6206; JUND.
DR HPA; CAB005268; -.
DR MIM; 165162; gene.
DR neXtProt; NX_P17535; -.
DR PharmGKB; PA30008; -.
DR eggNOG; NOG283376; -.
DR HOGENOM; HOG000006648; -.
DR HOVERGEN; HBG001722; -.
DR InParanoid; P17535; -.
DR KO; K04449; -.
DR OMA; QFLYPKV; -.
DR OrthoDB; EOG75MVXV; -.
DR PhylomeDB; P17535; -.
DR SignaLink; P17535; -.
DR ChiTaRS; JUND; human.
DR GeneWiki; JunD; -.
DR GenomeRNAi; 3727; -.
DR NextBio; 14591; -.
DR PRO; PR:P17535; -.
DR Bgee; P17535; -.
DR CleanEx; HS_JUND; -.
DR Genevestigator; P17535; -.
DR GO; GO:0000785; C:chromatin; TAS:ProtInc.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043234; C:protein complex; IEA:Ensembl.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:Ensembl.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:Ensembl.
DR GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0071277; P:cellular response to calcium ion; IEA:Ensembl.
DR GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR GO; GO:0002076; P:osteoblast development; IEA:Ensembl.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
DR GO; GO:0009416; P:response to light stimulus; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0043434; P:response to peptide hormone stimulus; IEA:Ensembl.
DR GO; GO:0006366; P:transcription from RNA polymerase II promoter; IEA:Ensembl.
DR Gene3D; 1.10.880.10; -; 1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR005643; JNK.
DR InterPro; IPR002112; Leuzip_Jun.
DR InterPro; IPR008917; TF_DNA-bd.
DR Pfam; PF00170; bZIP_1; 1.
DR Pfam; PF03957; Jun; 1.
DR PRINTS; PR00043; LEUZIPPRJUN.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF47454; SSF47454; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Complete proteome; DNA-binding; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1 347 Transcription factor jun-D.
FT /FTId=PRO_0000076442.
FT DOMAIN 268 331 bZIP.
FT REGION 268 295 Basic motif (By similarity).
FT REGION 296 324 Leucine-zipper (By similarity).
FT COMPBIAS 158 166 Poly-Ala.
FT MOD_RES 251 251 Phosphoserine.
FT MOD_RES 255 255 Phosphoserine.
FT MOD_RES 259 259 Phosphoserine.
FT VARIANT 20 20 G -> V (in dbSNP:rs41478151).
FT /FTId=VAR_055247.
FT CONFLICT 24 24 S -> T (in Ref. 1; CAA40010).
FT CONFLICT 157 157 A -> R (in Ref. 1; CAA40010).
SQ SEQUENCE 347 AA; 35174 MW; FE85A1AA2B5B9597 CRC64;
METPFYGDEA LSGLGGGASG SGGSFASPGR LFPGAPPTAA AGSMMKKDAL TLSLSEQVAA
ALKPAAAPPP TPLRADGAPS AAPPDGLLAS PDLGLLKLAS PELERLIIQS NGLVTTTPTS
SQFLYPKVAA SEEQEFAEGF VKALEDLHKQ NQLGAGAAAA AAAAAAGGPS GTATGSAPPG
ELAPAAAAPE APVYANLSSY AGGAGGAGGA ATVAFAAEPV PFPPPPPPGA LGPPRLAALK
DEPQTVPDVP SFGESPPLSP IDMDTQERIK AERKRLRNRI AASKCRKRKL ERISRLEEKV
KTLKSQNTEL ASTASLLREQ VAQLKQKVLS HVNSGCQLLP QHQVPAY
//
MIM
165162
*RECORD*
*FIELD* NO
165162
*FIELD* TI
*165162 ONCOGENE JUN-D; JUND
*FIELD* TX
GENE FUNCTION
JUND is the most broadly expressed member of the JUN family and the AP1
read moretranscription factor complex (see 165160). Weitzman et al. (2000) found
that primary fibroblasts lacking murine Jund displayed p53
(191170)-dependent growth arrest, upregulated p19(ARF) (see 600160)
expression, and premature senescence. In contrast, immortalized cell
lines lacking Jund showed increased proliferation and higher cyclin D1
(CCND1; 168461) levels. These properties were reminiscent of the effects
of oncogenic RAS (190020) expression on primary and established cell
cultures. Furthermore, Jund -/- fibroblasts exhibited increased
p53-dependent apoptosis upon ultraviolet irradiation and were sensitive
to the cytotoxic effects of tumor necrosis factor-alpha (TNF; 191160).
The antiapoptotic role of JUND was confirmed using an in vivo model of
TNF-mediated hepatitis. The authors proposed that JUND protects cells
from senescence, or apoptotic responses to stress stimuli, by acting as
a modulator of the signaling pathways that link RAS to p53.
Gerald et al. (2004) found that mouse Jund reduced tumor angiogenesis by
limiting Ras-mediated production of reactive oxygen species. Using
Jund-deficient cells, they showed that Jund regulates genes involved in
antioxidant defense, H2O2 production, and angiogenesis. Accumulation of
H2O2 in Jund -/- cells decreased the availability of Fe(II) and reduced
the activity of HIF-prolyl hydroxylases (see 606424) that target
hypoxia-inducible factor (HIF) alpha subunits (e.g., HIF1A; 603348) for
degradation. Subsequently, HIF-alpha proteins accumulated and enhanced
transcription of Vegfa (192240), a potent proangiogenic factor. Gerald
et al. (2004) concluded that their findings reveal the mechanism by
which JUND protects cells from oxidative stress and exerts an
antiangiogenic effect.
Behmoaras et al. (2008) demonstrated by combined congenic, linkage, and
microarray studies that the activator protein-1 (AP-1) transcription
factor JunD is a major determinant of macrophage activity and is
associated with glomerulonephritis susceptibility. Introgression of the
rat crescentic glomerulonephritis locus Crgn2 from the nonsusceptible
Lewis strain onto the Wistar Kyoto rat background led to significant
reductions in crescent formation, macrophage infiltration, Fc
receptor-mediated macrophage activation, and cytokine production.
Haplotype analysis restricted the Crgn2 linkage interval to a 430-kb
interval containing Jund, which is markedly overexpressed in Wistar
Kyoto macrophages and glomeruli. JunD knockdown in rat and human primary
macrophages led to significantly reduced macrophage activity and
cytokine secretion, indicating conservation of JunD function in
macrophage activation in rats and human and suggesting in vivo
inhibition of JunD as a possible therapeutic strategy for diseases
characterized by inflammation and macrophage activation.
GENE STRUCTURE
Sullivan et al. (1999) found that the JUND gene contains no introns.
MAPPING
By fluorescence in situ hybridization, Trask et al. (1993) assigned the
JUND gene to 19p13.1-p12. Sullivan et al. (1999) determined that the
JUND gene is located about 27 kb proximal to PDE4C (600128).
BIOCHEMICAL FEATURES
- Crystal Structure
Huang et al. (2012) reported the crystal structures of human menin
(613733) in its free form and in complexes with MLL1 (159555) or with
JUND, or with an MLL1-LEDGF (603620) heterodimer. These structures show
that menin contains a deep pocket that binds short peptides of MLL1 or
JUND in the same manner, but that it can have opposite effects on
transcription. The menin-JUND interaction blocks JUN N-terminal
kinase-mediated JUND phosphorylation and suppresses JUND-induced
transcription. In contrast, menin promotes gene transcription by binding
the transcription activator MLL1 through the peptide pocket while still
interacting with the chromatin-anchoring protein LEDGF at a distinct
surface formed by both menin and MLL1.
ANIMAL MODEL
Using Jund knockout mice and an experimental model of chronic renal
injury (75% nephron reduction), Pillebout et al. (2003) demonstrated
that Jund was not required for the initial compensatory growth phase but
was essential to inhibit a second wave of cell proliferation and to halt
the development of renal lesions. They also showed that the effects of
Jund inactivation involve upregulation of the paracrine mitogen
transforming growth factor-alpha (TGFA; 190170), and suggested that JUND
is part of a regulatory network that controls proliferation to prevent
pathologic progression in chronic renal diseases.
*FIELD* RF
1. Behmoaras, J.; Bhangal, G.; Smith, J.; McDonald, K.; Mutch, B.;
Lai, P. C.; Domin, J.; Game, L.; Salama, A.; Foxwell, B. M.; Pusey,
C. D.; Cook, H. T.; Aitman, T. J.: Jund is a determinant of macrophage
activation and is associated with glomerulonephritis susceptibility. Nature
Genet. 40: 553-559, 2008.
2. Gerald, D.; Berra, E.; Frapart, Y. M.; Chan, D. A.; Giaccia, A.
J.; Mansuy, D.; Pouyssegur, J.; Yaniv, M.; Mechta-Grigoriou, F.:
JunD reduces tumor angiogenesis by protecting cells from oxidative
stress. Cell 118: 781-794, 2004.
3. Huang, J.; Gurung, B.; Wan, B.; Matkar, S.; Veniaminova, N. A.;
Wan, K.; Merchant, J. L.; Hua, X.; Lei, M.: The same pocket in menin
binds both MLL and JUND but has opposite effects on transcription. Nature 482:
542-546, 2012.
4. Pillebout, E.; Weitzman, J. B.; Burtin, M.; Martino, C.; Federici,
P.; Yaniv, M.; Friedlander, G.; Terzi, F.: JunD protects against
chronic kidney disease by regulating paracrine mitogens. J. Clin.
Invest. 112: 843-852, 2003.
5. Sullivan, M.; Olsen, A. S.; Houslay, M. D.: Genomic organisation
of the human cyclic AMP-specific phosphodiesterase PDE4C gene and
its chromosomal localisation to 19p13.1, between RAB3A and JUND. Cell.
Signal. 11: 735-742, 1999.
6. Trask, B.; Fertitta, A.; Christensen, M.; Youngblom, J.; Bergmann,
A.; Copeland, A.; de Jong, P.; Mohrenweiser, H.; Olsen, A.; Carrano,
A.; Tynan, K.: Fluorescence in situ hybridization mapping of human
chromosome 19: cytogenetic band location of 540 cosmids and 70 genes
or DNA markers. Genomics 15: 133-145, 1993.
7. Weitzman, J. B.; Fiette, L.; Matsuo, K.; Yaniv, M.: JunD protects
cells from p53-dependent senescence and apoptosis. Molec. Cell 6:
1109-1119, 2000.
*FIELD* CN
Ada Hamosh - updated: 3/13/2012
Ada Hamosh - updated: 7/29/2008
Stylianos E. Antonarakis - updated: 3/10/2005
Marla J. F. O'Neill - updated: 5/7/2004
Stylianos E. Antonarakis - updated: 12/14/2000
Victor A. McKusick - updated: 12/7/1999
*FIELD* CD
Victor A. McKusick: 9/9/1990
*FIELD* ED
alopez: 03/14/2012
terry: 3/13/2012
alopez: 7/31/2008
terry: 7/29/2008
wwang: 11/5/2007
mgross: 3/10/2005
carol: 1/4/2005
carol: 5/12/2004
terry: 5/7/2004
mgross: 12/14/2000
mcapotos: 12/10/1999
terry: 12/7/1999
carol: 2/11/1993
supermim: 3/16/1992
carol: 11/20/1990
carol: 9/9/1990
*RECORD*
*FIELD* NO
165162
*FIELD* TI
*165162 ONCOGENE JUN-D; JUND
*FIELD* TX
GENE FUNCTION
JUND is the most broadly expressed member of the JUN family and the AP1
read moretranscription factor complex (see 165160). Weitzman et al. (2000) found
that primary fibroblasts lacking murine Jund displayed p53
(191170)-dependent growth arrest, upregulated p19(ARF) (see 600160)
expression, and premature senescence. In contrast, immortalized cell
lines lacking Jund showed increased proliferation and higher cyclin D1
(CCND1; 168461) levels. These properties were reminiscent of the effects
of oncogenic RAS (190020) expression on primary and established cell
cultures. Furthermore, Jund -/- fibroblasts exhibited increased
p53-dependent apoptosis upon ultraviolet irradiation and were sensitive
to the cytotoxic effects of tumor necrosis factor-alpha (TNF; 191160).
The antiapoptotic role of JUND was confirmed using an in vivo model of
TNF-mediated hepatitis. The authors proposed that JUND protects cells
from senescence, or apoptotic responses to stress stimuli, by acting as
a modulator of the signaling pathways that link RAS to p53.
Gerald et al. (2004) found that mouse Jund reduced tumor angiogenesis by
limiting Ras-mediated production of reactive oxygen species. Using
Jund-deficient cells, they showed that Jund regulates genes involved in
antioxidant defense, H2O2 production, and angiogenesis. Accumulation of
H2O2 in Jund -/- cells decreased the availability of Fe(II) and reduced
the activity of HIF-prolyl hydroxylases (see 606424) that target
hypoxia-inducible factor (HIF) alpha subunits (e.g., HIF1A; 603348) for
degradation. Subsequently, HIF-alpha proteins accumulated and enhanced
transcription of Vegfa (192240), a potent proangiogenic factor. Gerald
et al. (2004) concluded that their findings reveal the mechanism by
which JUND protects cells from oxidative stress and exerts an
antiangiogenic effect.
Behmoaras et al. (2008) demonstrated by combined congenic, linkage, and
microarray studies that the activator protein-1 (AP-1) transcription
factor JunD is a major determinant of macrophage activity and is
associated with glomerulonephritis susceptibility. Introgression of the
rat crescentic glomerulonephritis locus Crgn2 from the nonsusceptible
Lewis strain onto the Wistar Kyoto rat background led to significant
reductions in crescent formation, macrophage infiltration, Fc
receptor-mediated macrophage activation, and cytokine production.
Haplotype analysis restricted the Crgn2 linkage interval to a 430-kb
interval containing Jund, which is markedly overexpressed in Wistar
Kyoto macrophages and glomeruli. JunD knockdown in rat and human primary
macrophages led to significantly reduced macrophage activity and
cytokine secretion, indicating conservation of JunD function in
macrophage activation in rats and human and suggesting in vivo
inhibition of JunD as a possible therapeutic strategy for diseases
characterized by inflammation and macrophage activation.
GENE STRUCTURE
Sullivan et al. (1999) found that the JUND gene contains no introns.
MAPPING
By fluorescence in situ hybridization, Trask et al. (1993) assigned the
JUND gene to 19p13.1-p12. Sullivan et al. (1999) determined that the
JUND gene is located about 27 kb proximal to PDE4C (600128).
BIOCHEMICAL FEATURES
- Crystal Structure
Huang et al. (2012) reported the crystal structures of human menin
(613733) in its free form and in complexes with MLL1 (159555) or with
JUND, or with an MLL1-LEDGF (603620) heterodimer. These structures show
that menin contains a deep pocket that binds short peptides of MLL1 or
JUND in the same manner, but that it can have opposite effects on
transcription. The menin-JUND interaction blocks JUN N-terminal
kinase-mediated JUND phosphorylation and suppresses JUND-induced
transcription. In contrast, menin promotes gene transcription by binding
the transcription activator MLL1 through the peptide pocket while still
interacting with the chromatin-anchoring protein LEDGF at a distinct
surface formed by both menin and MLL1.
ANIMAL MODEL
Using Jund knockout mice and an experimental model of chronic renal
injury (75% nephron reduction), Pillebout et al. (2003) demonstrated
that Jund was not required for the initial compensatory growth phase but
was essential to inhibit a second wave of cell proliferation and to halt
the development of renal lesions. They also showed that the effects of
Jund inactivation involve upregulation of the paracrine mitogen
transforming growth factor-alpha (TGFA; 190170), and suggested that JUND
is part of a regulatory network that controls proliferation to prevent
pathologic progression in chronic renal diseases.
*FIELD* RF
1. Behmoaras, J.; Bhangal, G.; Smith, J.; McDonald, K.; Mutch, B.;
Lai, P. C.; Domin, J.; Game, L.; Salama, A.; Foxwell, B. M.; Pusey,
C. D.; Cook, H. T.; Aitman, T. J.: Jund is a determinant of macrophage
activation and is associated with glomerulonephritis susceptibility. Nature
Genet. 40: 553-559, 2008.
2. Gerald, D.; Berra, E.; Frapart, Y. M.; Chan, D. A.; Giaccia, A.
J.; Mansuy, D.; Pouyssegur, J.; Yaniv, M.; Mechta-Grigoriou, F.:
JunD reduces tumor angiogenesis by protecting cells from oxidative
stress. Cell 118: 781-794, 2004.
3. Huang, J.; Gurung, B.; Wan, B.; Matkar, S.; Veniaminova, N. A.;
Wan, K.; Merchant, J. L.; Hua, X.; Lei, M.: The same pocket in menin
binds both MLL and JUND but has opposite effects on transcription. Nature 482:
542-546, 2012.
4. Pillebout, E.; Weitzman, J. B.; Burtin, M.; Martino, C.; Federici,
P.; Yaniv, M.; Friedlander, G.; Terzi, F.: JunD protects against
chronic kidney disease by regulating paracrine mitogens. J. Clin.
Invest. 112: 843-852, 2003.
5. Sullivan, M.; Olsen, A. S.; Houslay, M. D.: Genomic organisation
of the human cyclic AMP-specific phosphodiesterase PDE4C gene and
its chromosomal localisation to 19p13.1, between RAB3A and JUND. Cell.
Signal. 11: 735-742, 1999.
6. Trask, B.; Fertitta, A.; Christensen, M.; Youngblom, J.; Bergmann,
A.; Copeland, A.; de Jong, P.; Mohrenweiser, H.; Olsen, A.; Carrano,
A.; Tynan, K.: Fluorescence in situ hybridization mapping of human
chromosome 19: cytogenetic band location of 540 cosmids and 70 genes
or DNA markers. Genomics 15: 133-145, 1993.
7. Weitzman, J. B.; Fiette, L.; Matsuo, K.; Yaniv, M.: JunD protects
cells from p53-dependent senescence and apoptosis. Molec. Cell 6:
1109-1119, 2000.
*FIELD* CN
Ada Hamosh - updated: 3/13/2012
Ada Hamosh - updated: 7/29/2008
Stylianos E. Antonarakis - updated: 3/10/2005
Marla J. F. O'Neill - updated: 5/7/2004
Stylianos E. Antonarakis - updated: 12/14/2000
Victor A. McKusick - updated: 12/7/1999
*FIELD* CD
Victor A. McKusick: 9/9/1990
*FIELD* ED
alopez: 03/14/2012
terry: 3/13/2012
alopez: 7/31/2008
terry: 7/29/2008
wwang: 11/5/2007
mgross: 3/10/2005
carol: 1/4/2005
carol: 5/12/2004
terry: 5/7/2004
mgross: 12/14/2000
mcapotos: 12/10/1999
terry: 12/7/1999
carol: 2/11/1993
supermim: 3/16/1992
carol: 11/20/1990
carol: 9/9/1990