JUND_MOUSE
ID JUND_MOUSE Reviewed; 341 AA.
AC P15066;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Transcription factor JunD {ECO:0000305};
DE AltName: Full=Transcription factor AP-1 subunit JunD {ECO:0000305};
GN Name=Jund; Synonyms=Jun-d, Jund1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2493644; DOI=10.1073/pnas.86.5.1500;
RA Ryder K., Lanahan A., Perez-Albuerne E., Nathans D.;
RT "jun-D: a third member of the jun gene family.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:1500-1503(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2504580; DOI=10.1002/j.1460-2075.1989.tb03525.x;
RA Hirai S., Ryseck R.P., Mechta F., Bravo R., Yaniv M.;
RT "Characterization of junD: a new member of the jun proto-oncogene family.";
RL EMBO J. 8:1433-1439(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2104845; DOI=10.1016/s0021-9258(19)40053-7;
RA Li L., Hu J.-S., Olson E.N.;
RT "Different members of the jun proto-oncogene family exhibit distinct
RT patterns of expression in response to type beta transforming growth
RT factor.";
RL J. Biol. Chem. 265:1556-1562(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 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., Park S.Y.,
RA Saggar S., Chandrasekharappa S.C., Collins F.S., Spiegel A.M., Marx S.J.,
RA Burns A.L.;
RT "Menin interacts with the AP1 transcription factor JunD and represses JunD-
RT activated transcription.";
RL Cell 96:143-152(1999).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249 AND SER-253, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Transcription factor binding AP-1 sites (By similarity).
CC Heterodimerizes with proteins of the FOS family to form an AP-1
CC transcription factor complex, thereby enhancing its DNA binding
CC activity to an AP-1 consensus sequence 3'-TGA[GC]TCA-5' and enhancing
CC its transcriptional activity (By similarity).
CC {ECO:0000250|UniProtKB:P17535}.
CC -!- SUBUNIT: Heterodimer; binds DNA as a heterodimer (By similarity).
CC Component of an AP-1 transcription factor complex composed of JUN-FOS
CC heterodimers (By similarity). As part of the AP-1 transcription factor
CC complex, forms heterodimers with FOS proteins, thereby binding to the
CC AP-1 consensus sequence and stimulating transcription (By similarity).
CC Forms heterodimers with FOSB; thereby binding to the AP-1 consensus
CC sequence (By similarity). Interacts (via MBM motif) with MEN1; this
CC interaction represses transcriptional activation (PubMed:9989505).
CC Interacts with MAPK10; this interaction is inhibited in the presence of
CC MEN1 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P13346,
CC ECO:0000250|UniProtKB:P17535, ECO:0000269|PubMed:9989505}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Brain and kidney.
CC -!- DOMAIN: Binds DNA via bZIP domain; DNA-binding is under control of
CC cellular redox homeostasis (in vitro) (By similarity). To enable DNA
CC binding, the bZIP domain must undergo a conformational rearrangement
CC which requires the reduction of the interchain disulfide bond between
CC FosB and JunD (in vitro) (By similarity).
CC {ECO:0000250|UniProtKB:P17535}.
CC -!- PTM: Phosphorylated by MAP kinases MAPK8 and MAPK10; phosphorylation is
CC inhibited in the presence of MEN1. {ECO:0000250|UniProtKB:P17535}.
CC -!- SIMILARITY: Belongs to the bZIP family. Jun subfamily. {ECO:0000305}.
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DR EMBL; J04509; AAA39344.1; -; Genomic_DNA.
DR EMBL; X15358; CAA33418.1; -; mRNA.
DR EMBL; J05205; AAA39345.1; -; mRNA.
DR EMBL; BC010572; AAH10572.1; -; mRNA.
DR CCDS; CCDS40375.1; -.
DR PIR; A32158; TVMSJD.
DR RefSeq; NP_034722.1; NM_010592.5.
DR AlphaFoldDB; P15066; -.
DR SMR; P15066; -.
DR BioGRID; 200873; 6.
DR ComplexPortal; CPX-628; Menin-JUND transcription inhibition complex.
DR ELM; P15066; -.
DR IntAct; P15066; 2.
DR STRING; 10090.ENSMUSP00000092901; -.
DR iPTMnet; P15066; -.
DR PhosphoSitePlus; P15066; -.
DR EPD; P15066; -.
DR jPOST; P15066; -.
DR MaxQB; P15066; -.
DR PaxDb; P15066; -.
DR PeptideAtlas; P15066; -.
DR PRIDE; P15066; -.
DR ProteomicsDB; 269429; -.
DR Antibodypedia; 3936; 662 antibodies from 41 providers.
DR DNASU; 16478; -.
DR Ensembl; ENSMUST00000095267; ENSMUSP00000092901; ENSMUSG00000071076.
DR GeneID; 16478; -.
DR KEGG; mmu:16478; -.
DR UCSC; uc009mbe.2; mouse.
DR CTD; 3727; -.
DR MGI; MGI:96648; Jund.
DR VEuPathDB; HostDB:ENSMUSG00000071076; -.
DR eggNOG; KOG0837; Eukaryota.
DR GeneTree; ENSGT00940000162806; -.
DR HOGENOM; CLU_057007_0_0_1; -.
DR InParanoid; P15066; -.
DR OMA; CAQTNSM; -.
DR OrthoDB; 1090460at2759; -.
DR PhylomeDB; P15066; -.
DR TreeFam; TF323952; -.
DR BioGRID-ORCS; 16478; 7 hits in 61 CRISPR screens.
DR ChiTaRS; Jund; mouse.
DR PRO; PR:P15066; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P15066; protein.
DR Bgee; ENSMUSG00000071076; Expressed in granulocyte and 81 other tissues.
DR Genevisible; P15066; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0032993; C:protein-DNA complex; ISO:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0035976; C:transcription factor AP-1 complex; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0017053; C:transcription repressor complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0016922; F:nuclear receptor binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0001221; F:transcription coregulator binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0071277; P:cellular response to calcium ion; IDA:MGI.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0002076; P:osteoblast development; IGI:MGI.
DR GO; GO:0043032; P:positive regulation of macrophage activation; ISO:MGI.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IGI:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ParkinsonsUK-UCL.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
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; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISO:MGI.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR005643; JNK.
DR InterPro; IPR029823; JunD.
DR InterPro; IPR002112; Leuzip_Jun.
DR InterPro; IPR008917; TF_DNA-bd_sf.
DR PANTHER; PTHR11462:SF7; PTHR11462:SF7; 1.
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 SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..341
FT /note="Transcription factor JunD"
FT /id="PRO_0000076443"
FT DOMAIN 262..325
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 18..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..289
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 290..318
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT MOTIF 35..47
FT /note="Menin-binding motif (MBM)"
FT /evidence="ECO:0000250|UniProtKB:P17535"
FT MOTIF 51..60
FT /note="MAP kinase docking motif; essential for its
FT phosphorylation"
FT /evidence="ECO:0000250|UniProtKB:P17535"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17535"
FT MOD_RES 100
FT /note="Phosphoserine; by MAPK8"
FT /evidence="ECO:0000250|UniProtKB:P17535"
FT MOD_RES 117
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P17535"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17535"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT DISULFID 279
FT /note="Interchain (with C-172 in FOSB)"
FT /evidence="ECO:0000250|UniProtKB:P17535"
FT CONFLICT 5
FT /note="F -> L (in Ref. 3; AAA39345)"
FT /evidence="ECO:0000305"
FT CONFLICT 61..62
FT /note="EQ -> DE (in Ref. 3; AAA39345)"
FT /evidence="ECO:0000305"
FT CONFLICT 317..318
FT /note="QL -> HV (in Ref. 3; AAA39345)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 341 AA; 34905 MW; 2727392F6B65188D CRC64;
METPFYGEEA LSGLAAGASS VAGATGAPGG GGFAPPGRAF PGAPPTSSML KKDALTLSLA
EQGAAGLKPG SATAPSALRP DGAPDGLLAS PDLGLLKLAS PELERLIIQS NGLVTTTPTS
TQFLYPKVAA SEEQEFAEGF VKALEDLHKQ SQLGAATAAT SGAPAPPAPA DLAATPGATE
TPVYANLSSF AGGAGPPGGA ATVAFAAEPV PFPPPPGALG PPPPPHPPRL AALKDEPQTV
PDVPSFGDSP PLSPIDMDTQ ERIKAERKRL RNRIAASKCR KRKLERISRL EEKVKTLKSQ
NTELASTASL LREQVAQLKQ KVLSHVNSGC QLLPQHQVPA Y
