JUNB_MOUSE
ID JUNB_MOUSE Reviewed; 344 AA.
AC P09450; Q8C2G9;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Transcription factor JunB {ECO:0000305};
DE AltName: Full=MyD21;
DE AltName: Full=Transcription factor AP-1 subunit JunB {ECO:0000305};
GN Name=Junb; Synonyms=Jun-b;
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 [MRNA].
RX PubMed=3422745; DOI=10.1073/pnas.85.5.1487;
RA Ryder K., Lau L.F., Nathans D.;
RT "A gene activated by growth factors is related to the oncogene v-jun.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:1487-1491(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ;
RX PubMed=8530030; DOI=10.1006/geno.1995.1135;
RA Phinney D.G., Tseng S.W., Ryder K.;
RT "Complex genetic organization of junB: multiple blocks of flanking
RT evolutionarily conserved sequence at the murine and human junB loci.";
RL Genomics 28:228-234(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-30.
RX PubMed=1690380;
RA Lord K.A., Hoffman-Liebermann B., Liebermann D.A.;
RT "Complexity of the immediate early response of myeloid cells to terminal
RT differentiation and growth arrest includes ICAM-1, Jun-B and histone
RT variants.";
RL Oncogene 5:387-396(1990).
RN [6]
RP FUNCTION, IDENTIFICATION IN AN AP-1 COMPLEX, SUBUNIT, AND INTERACTION WITH
RP FOSB.
RX PubMed=2498083; DOI=10.1002/j.1460-2075.1989.tb03441.x;
RA Zerial M., Toschi L., Ryseck R.-P., Schuermann M., Mueller R., Bravo R.;
RT "The product of a novel growth factor activated gene, fos B, interacts with
RT JUN proteins enhancing their DNA binding activity.";
RL EMBO J. 8:805-813(1989).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248; THR-252 AND SER-256, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, and Spleen;
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).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-237, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Transcription factor involved in regulating gene activity
CC following the primary growth factor response. Binds to the DNA sequence
CC 5'-TGA[GC]TCA-3'. Heterodimerizes with proteins of the FOS family to
CC form an AP-1 transcription complex, thereby enhancing its DNA binding
CC activity to an AP-1 consensus sequence 5'-TGA[GC]TCA-3' and enhancing
CC its transcriptional activity (PubMed:2498083).
CC {ECO:0000269|PubMed:2498083}.
CC -!- SUBUNIT: Binds DNA as a homodimer or as a heterodimer with another
CC member of the Jun/Fos family (By similarity). Component of an AP-1
CC transcription factor complex composed of JUN-FOS heterodimers
CC (PubMed:2498083). As part of the AP-1 transcription factor complex,
CC forms heterodimers with FOSB, thereby binding to the AP-1 consensus
CC sequence and stimulating transcription (PubMed:2498083). Interacts with
CC NFE2 (via its WW domains) (By similarity).
CC {ECO:0000250|UniProtKB:P17275, ECO:0000269|PubMed:2498083}.
CC -!- INTERACTION:
CC P09450; Q9DGW5: MDV005; Xeno; NbExp=2; IntAct=EBI-5347760, EBI-10889526;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- INDUCTION: By growth factors.
CC -!- PTM: Ubiquitinated by ITCH, leading to its degradation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bZIP family. Jun subfamily. {ECO:0000305}.
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; J03236; AAA39343.1; -; mRNA.
DR EMBL; U20735; AAA74916.1; -; Genomic_DNA.
DR EMBL; AK088643; BAC40473.1; -; mRNA.
DR EMBL; BC003790; AAH03790.1; -; mRNA.
DR EMBL; X54332; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS22488.1; -.
DR PIR; A28963; TVMSJB.
DR RefSeq; NP_032442.1; NM_008416.3.
DR AlphaFoldDB; P09450; -.
DR SMR; P09450; -.
DR BioGRID; 200872; 106.
DR CORUM; P09450; -.
DR DIP; DIP-1069N; -.
DR ELM; P09450; -.
DR IntAct; P09450; 105.
DR STRING; 10090.ENSMUSP00000064680; -.
DR iPTMnet; P09450; -.
DR PhosphoSitePlus; P09450; -.
DR EPD; P09450; -.
DR jPOST; P09450; -.
DR PaxDb; P09450; -.
DR PeptideAtlas; P09450; -.
DR PRIDE; P09450; -.
DR ProteomicsDB; 269036; -.
DR Antibodypedia; 3847; 925 antibodies from 45 providers.
DR DNASU; 16477; -.
DR Ensembl; ENSMUST00000064922; ENSMUSP00000064680; ENSMUSG00000052837.
DR GeneID; 16477; -.
DR KEGG; mmu:16477; -.
DR UCSC; uc009mop.1; mouse.
DR CTD; 3726; -.
DR MGI; MGI:96647; Junb.
DR VEuPathDB; HostDB:ENSMUSG00000052837; -.
DR eggNOG; KOG0837; Eukaryota.
DR GeneTree; ENSGT00940000161195; -.
DR HOGENOM; CLU_057007_0_0_1; -.
DR InParanoid; P09450; -.
DR OMA; PTPAHYL; -.
DR OrthoDB; 1090460at2759; -.
DR PhylomeDB; P09450; -.
DR BioGRID-ORCS; 16477; 6 hits in 76 CRISPR screens.
DR ChiTaRS; Junb; mouse.
DR PRO; PR:P09450; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P09450; protein.
DR Bgee; ENSMUSG00000052837; Expressed in granulocyte and 150 other tissues.
DR ExpressionAtlas; P09450; baseline and differential.
DR Genevisible; P09450; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; 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:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP: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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IMP:NTNU_SB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:MGI.
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:0030154; P:cell differentiation; IDA:MGI.
DR GO; GO:0071277; P:cellular response to calcium ion; IDA:MGI.
DR GO; GO:0046697; P:decidualization; IMP:MGI.
DR GO; GO:0060136; P:embryonic process involved in female pregnancy; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0060716; P:labyrinthine layer blood vessel development; IMP:MGI.
DR GO; GO:0001649; P:osteoblast differentiation; IMP:MGI.
DR GO; GO:0033687; P:osteoblast proliferation; IMP:MGI.
DR GO; GO:0030316; P:osteoclast differentiation; IMP:MGI.
DR GO; GO:0002158; P:osteoclast proliferation; IMP:MGI.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:NTNU_SB.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:MGI.
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; IDA:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0001829; P:trophectodermal cell differentiation; IDA:MGI.
DR GO; GO:0001570; P:vasculogenesis; IMP:MGI.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR005643; JNK.
DR InterPro; IPR029822; JunB.
DR InterPro; IPR002112; Leuzip_Jun.
DR InterPro; IPR008917; TF_DNA-bd_sf.
DR PANTHER; PTHR11462:SF37; PTHR11462:SF37; 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 Acetylation; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..344
FT /note="Transcription factor JunB"
FT /id="PRO_0000076439"
FT DOMAIN 265..328
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 51..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..292
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 293..321
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT MOD_RES 102
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P17275"
FT MOD_RES 104
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P17275"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17275"
FT MOD_RES 237
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 252
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CROSSLNK 4
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17275"
FT CROSSLNK 33
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17275"
FT CROSSLNK 36
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17275"
FT CROSSLNK 81
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17275"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17275"
FT CROSSLNK 237
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P17275"
FT CROSSLNK 237
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P17275"
FT CROSSLNK 340
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17275"
FT CONFLICT 53
FT /note="P -> S (in Ref. 3; BAC40473)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="G -> R (in Ref. 2; AAA74916)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 35765 MW; 6F52D4FECC32E234 CRC64;
MCTKMEQPFY HDDSYAAAGY GRSPGSLSLH DYKLLKPTLA LNLADPYRGL KGPGARGPGP
EGSGAGSYFS GQGSDTGASL KLASTELERL IVPNSNGVIT TTPTPPGQYF YPRGGGSGGG
TGGGVTEEQE GFADGFVKAL DDLHKMNHVT PPNVSLGASG GPQAGPGGVY AGPEPPPVYT
NLSSYSPASA PSGGSGTAVG TGSSYPTATI SYLPHAPPFA GGHPAQLGLS RGASAFKEEP
QTVPEARSRD ATPPVSPINM EDQERIKVER KRLRNRLAAT KCRKRKLERI ARLEDKVKTL
KAENAGLSSA AGLLREQVAQ LKQKVMTHVS NGCQLLLGVK GHAF
