ID   JUND_HUMAN              Reviewed;         347 AA.
AC   P17535; Q53EK9;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 3.
DT   09-DEC-2015, entry version 151.
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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       {ECO:0000269|PubMed:9989505}.
CC   -!- SUBUNIT: Binds DNA as a dimer (By similarity). Interacts with
CC       MEN1; this interaction represses transcriptional activation.
CC       {ECO:0000250, ECO:0000269|PubMed:9989505}.
CC   -!- INTERACTION:
CC       Q9DGW5:- (xeno); NbExp=2; IntAct=EBI-2682803, EBI-10889526;
CC       P61158:ACTR3; NbExp=2; IntAct=EBI-2682803, EBI-351428;
CC       P10275:AR; NbExp=2; IntAct=EBI-2682803, EBI-608057;
CC       P15336:ATF2; NbExp=2; IntAct=EBI-2682803, EBI-1170906;
CC       P18847:ATF3; NbExp=2; IntAct=EBI-2682803, EBI-712767;
CC       P17544:ATF7; NbExp=2; IntAct=EBI-2682803, EBI-765623;
CC       Q16520:BATF; NbExp=2; IntAct=EBI-2682803, EBI-749503;
CC       Q9NR55:BATF3; NbExp=2; IntAct=EBI-2682803, EBI-10312707;
CC       P01100:FOS; NbExp=7; IntAct=EBI-2682803, EBI-852851;
CC       P15408:FOSL2; NbExp=3; IntAct=EBI-2682803, EBI-3893419;
CC       P0C746:HBZ (xeno); NbExp=2; IntAct=EBI-2682803, EBI-10890294;
CC       Q00987:MDM2; NbExp=3; IntAct=EBI-2682803, EBI-389668;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the bZIP family. Jun subfamily.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 bZIP (basic-leucine zipper) domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA40010.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
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 https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) 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   CCDS; CCDS32959.1; -.
DR   PIR; A43815; A43815.
DR   PIR; S10184; TVHUJD.
DR   RefSeq; NP_001273897.1; NM_001286968.1.
DR   RefSeq; NP_005345.3; NM_005354.5.
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   BioGrid; 109930; 36.
DR   DIP; DIP-1053N; -.
DR   IntAct; P17535; 19.
DR   MINT; MINT-260192; -.
DR   STRING; 9606.ENSP00000252818; -.
DR   PhosphoSite; P17535; -.
DR   DMDM; 229462969; -.
DR   MaxQB; P17535; -.
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; JUND; -.
DR   H-InvDB; HIX0040163; -.
DR   HGNC; HGNC:6206; JUND.
DR   HPA; CAB005268; -.
DR   HPA; HPA063029; -.
DR   MIM; 165162; gene.
DR   neXtProt; NX_P17535; -.
DR   PharmGKB; PA30008; -.
DR   eggNOG; KOG0837; Eukaryota.
DR   eggNOG; ENOG410XRWH; LUCA.
DR   GeneTree; ENSGT00390000009929; -.
DR   HOGENOM; HOG000006648; -.
DR   HOVERGEN; HBG001722; -.
DR   InParanoid; P17535; -.
DR   KO; K04449; -.
DR   OMA; APVYANL; -.
DR   OrthoDB; EOG75MVXV; -.
DR   PhylomeDB; P17535; -.
DR   TreeFam; TF323952; -.
DR   SignaLink; P17535; -.
DR   ChiTaRS; JUND; human.
DR   GeneWiki; JunD; -.
DR   GenomeRNAi; 3727; -.
DR   NextBio; 14591; -.
DR   PRO; PR:P17535; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   Bgee; P17535; -.
DR   CleanEx; HS_JUND; -.
DR   ExpressionAtlas; P17535; baseline and differential.
DR   Genevisible; P17535; HS.
DR   GO; GO:0000785; C:chromatin; TAS:ProtInc.
DR   GO; GO:0000790; C:nuclear chromatin; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:HPA.
DR   GO; GO:0032993; C:protein-DNA complex; IEA:Ensembl.
DR   GO; GO:0005667; C:transcription factor complex; IBA:GO_Central.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR   GO; GO:0008134; F:transcription factor binding; IBA:GO_Central.
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:0032870; P:cellular response to hormone stimulus; IBA:GO_Central.
DR   GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IBA:GO_Central.
DR   GO; GO:0002076; P:osteoblast development; IEA:Ensembl.
DR   GO; GO:0045597; P:positive regulation of cell differentiation; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR   GO; GO:0010941; P:regulation of cell death; IBA:GO_Central.
DR   GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
DR   GO; GO:0051591; P:response to cAMP; IBA:GO_Central.
DR   GO; GO:0034097; P:response to cytokine; IBA:GO_Central.
DR   GO; GO:0042493; P:response to drug; IBA:GO_Central.
DR   GO; GO:0009416; P:response to light stimulus; IEA:Ensembl.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IBA:GO_Central.
DR   GO; GO:0009612; P:response to mechanical stimulus; IBA:GO_Central.
DR   GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
DR   GO; GO:0009314; P:response to radiation; IBA:GO_Central.
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; IPR029823; JunD.
DR   InterPro; IPR002112; Leuzip_Jun.
DR   InterPro; IPR008917; TF_DNA-bd.
DR   PANTHER; PTHR11462:SF7; PTHR11462:SF7; 2.
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. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00978}.
FT   REGION      268    295       Basic motif. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00978}.
FT   REGION      296    324       Leucine-zipper. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00978}.
FT   COMPBIAS    158    166       Poly-Ala.
FT   MOD_RES     251    251       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     255    255       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19369195,
FT                                ECO:0000244|PubMed:19690332}.
FT   MOD_RES     259    259       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19369195,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231}.
FT   VARIANT      20     20       G -> V (in dbSNP:rs41478151).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_055247.
FT   CONFLICT     24     24       S -> T (in Ref. 1; CAA40010).
FT                                {ECO:0000305}.
FT   CONFLICT    157    157       A -> R (in Ref. 1; CAA40010).
FT                                {ECO:0000305}.
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
//