JUNB

Protein-coding gene in the species Homo sapiens
JUNB
Identifiers
AliasesJUNB, AP-1, JunB proto-oncogene, AP-1 transcription factor subunit
External IDsOMIM: 165161 MGI: 96647 HomoloGene: 7390 GeneCards: JUNB
Gene location (Human)
Chromosome 19 (human)
Chr.Chromosome 19 (human)[1]
Chromosome 19 (human)
Genomic location for JUNB
Genomic location for JUNB
Band19p13.13Start12,791,486 bp[1]
End12,793,315 bp[1]
Gene location (Mouse)
Chromosome 8 (mouse)
Chr.Chromosome 8 (mouse)[2]
Chromosome 8 (mouse)
Genomic location for JUNB
Genomic location for JUNB
Band8 C3|8 41.41 cMStart85,701,113 bp[2]
End85,705,347 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • gastric mucosa

  • left uterine tube

  • monocyte

  • vena cava

  • saphenous vein

  • nipple

  • trachea

  • ascending aorta

  • skin of abdomen

  • anterior pituitary
Top expressed in
  • lip

  • superior surface of tongue

  • spermatid

  • spermatocyte

  • corneal stroma

  • visual cortex

  • esophagus

  • superior frontal gyrus

  • islet of Langerhans

  • duodenum
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • DNA binding
  • RNA polymerase II transcription regulatory region sequence-specific DNA binding
  • transcription corepressor activity
  • DNA-binding transcription factor activity
  • transcription coactivator activity
  • DNA-binding transcription activator activity, RNA polymerase II-specific
  • transcription factor binding
  • RNA polymerase II cis-regulatory region sequence-specific DNA binding
  • protein binding
  • DNA-binding transcription factor activity, RNA polymerase II-specific
Cellular component
  • nucleoplasm
  • chromatin
  • nucleus
  • transcription factor AP-1 complex
  • transcription regulator complex
Biological process
  • cellular response to calcium ion
  • regulation of transcription, DNA-templated
  • regulation of transcription by RNA polymerase II
  • regulation of cell death
  • osteoclast differentiation
  • labyrinthine layer blood vessel development
  • in utero embryonic development
  • negative regulation of transcription by RNA polymerase II
  • transcription by RNA polymerase II
  • regulation of cell cycle
  • vasculogenesis
  • embryonic process involved in female pregnancy
  • response to lipopolysaccharide
  • decidualization
  • regulation of cell population proliferation
  • trophectodermal cell differentiation
  • osteoblast differentiation
  • positive regulation of cell differentiation
  • response to radiation
  • osteoblast proliferation
  • cellular process
  • response to cAMP
  • response to mechanical stimulus
  • transcription, DNA-templated
  • cellular response to hormone stimulus
  • response to cytokine
  • positive regulation of transcription by RNA polymerase II
  • cytokine-mediated signaling pathway
  • response to organic substance
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

3726

16477

Ensembl

ENSG00000171223

ENSMUSG00000052837

UniProt

P17275

P09450

RefSeq (mRNA)

NM_002229

NM_008416

RefSeq (protein)

NP_002220

NP_032442

Location (UCSC)Chr 19: 12.79 – 12.79 MbChr 8: 85.7 – 85.71 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Transcription factor jun-B is a protein that, in humans, is encoded by the JUNB gene.[5][6] Transcription factor jun-B is a transcription factor involved in regulating gene activity following the primary growth factor response. It binds to the DNA sequence 5'-TGA[CG]TCA-3'.

Interactions

JUNB has been shown to interact with

See also

  • AP-1 (transcription factor)

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000171223 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000052837 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Schütte J, Viallet J, Nau M, Segal S, Fedorko J, Minna J (Feb 1990). "jun-B inhibits and c-fos stimulates the transforming and trans-activating activities of c-jun". Cell. 59 (6): 987–997. doi:10.1016/0092-8674(89)90755-1. PMID 2513129.
  6. ^ "Entrez Gene: JUNB jun B proto-oncogene".
  7. ^ Hu YF, Li R (Jun 2002). "JunB potentiates function of BRCA1 activation domain 1 (AD1) through a coiled-coil-mediated interaction". Genes Dev. 16 (12): 1509–17. doi:10.1101/gad.995502. PMC 186344. PMID 12080089.
  8. ^ Liberati NT, Datto MB, Frederick JP, Shen X, Wong C, Rougier-Chapman EM, Wang XF (Apr 1999). "Smads bind directly to the Jun family of AP-1 transcription factors". Proc. Natl. Acad. Sci. U.S.A. 96 (9): 4844–9. Bibcode:1999PNAS...96.4844L. doi:10.1073/pnas.96.9.4844. PMC 21779. PMID 10220381.

Further reading

  • Hsu JC, Bravo R, Taub R (1992). "Interactions among LRF-1, JunB, c-Jun, and c-Fos define a regulatory program in the G1 phase of liver regeneration". Mol. Cell. Biol. 12 (10): 4654–65. doi:10.1128/MCB.12.10.4654. PMC 360392. PMID 1406655.
  • Zafarullah M, Martel-Pelletier J, Cloutier JM, Gedamu L, Pelletier JP (1992). "Expression of c-fos, c-jun, jun-B, metallothionein and metalloproteinase genes in human chondrocyte". FEBS Lett. 306 (2–3): 169–172. doi:10.1016/0014-5793(92)80992-P. PMID 1633872. S2CID 43460076.
  • Mollinedo F, Vaquerizo MJ, Naranjo JR (1991). "Expression of c-jun, jun B and jun D proto-oncogenes in human peripheral-blood granulocytes". Biochem. J. 273(Pt 2) (2): 477–9. doi:10.1042/bj2730477. PMC 1149869. PMID 1899335.
  • Nomura N, Ide M, Sasamoto S, Matsui M, Date T, Ishizaki R (1990). "Isolation of human cDNA clones of jun-related genes, jun-B and jun-D". Nucleic Acids Res. 18 (10): 3047–3048. doi:10.1093/nar/18.10.3047. PMC 330838. PMID 2112242.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–174. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Trask B, Fertitta A, Christensen M, Youngblom J, Bergmann A, Copeland A, de Jong P, Mohrenweiser H, Olsen A, Carrano A (1993). "Fluorescence in situ hybridization mapping of human chromosome 19: cytogenetic band location of 540 cosmids and 70 genes or DNA markers". Genomics. 15 (1): 133–145. doi:10.1006/geno.1993.1021. PMID 8432525.
  • Phinney DG, Tseng SW, Ryder K (1996). "Complex genetic organization of junB: multiple blocks of flanking evolutionarily conserved sequence at the murine and human junB loci". Genomics. 28 (2): 228–234. doi:10.1006/geno.1995.1135. PMID 8530030.
  • Dorsey MJ, Tae HJ, Sollenberger KG, Mascarenhas NT, Johansen LM, Taparowsky EJ (1996). "B-ATF: a novel human bZIP protein that associates with members of the AP-1 transcription factor family". Oncogene. 11 (11): 2255–65. PMID 8570175.
  • Neyns B, Vermeij J, Bourgain C, Vandamme B, Amfo K, Lissens W, DeSutter P, Hooghe-Peters E, DeGrève J (1996). "Expression of the jun family of genes in human ovarian cancer and normal ovarian surface epithelium". Oncogene. 12 (6): 1247–57. PMID 8649827.
  • Mendelson KG, Contois LR, Tevosian SG, Davis RJ, Paulson KE (1996). "Independent regulation of JNK/p38 mitogen-activated protein kinases by metabolic oxidative stress in the liver". Proc. Natl. Acad. Sci. U.S.A. 93 (23): 12908–12913. Bibcode:1996PNAS...9312908M. doi:10.1073/pnas.93.23.12908. PMC 24019. PMID 8917518.
  • Aronheim A, Zandi E, Hennemann H, Elledge SJ, Karin M (1997). "Isolation of an AP-1 repressor by a novel method for detecting protein-protein interactions". Mol. Cell. Biol. 17 (6): 3094–102. doi:10.1128/mcb.17.6.3094. PMC 232162. PMID 9154808.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–156. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Fuchs SY, Xie B, Adler V, Fried VA, Davis RJ, Ronai Z (1998). "c-Jun NH2-terminal kinases target the ubiquitination of their associated transcription factors". J. Biol. Chem. 272 (51): 32163–32168. doi:10.1074/jbc.272.51.32163. PMID 9405416.
  • Venugopal R, Jaiswal AK (1999). "Nrf2 and Nrf1 in association with Jun proteins regulate antioxidant response element-mediated expression and coordinated induction of genes encoding detoxifying enzymes". Oncogene. 17 (24): 3145–3156. doi:10.1038/sj.onc.1202237. PMID 9872330.
  • Li B, Tournier C, Davis RJ, Flavell RA (1999). "Regulation of IL-4 expression by the transcription factor JunB during T helper cell differentiation". EMBO J. 18 (2): 420–432. doi:10.1093/emboj/18.2.420. PMC 1171136. PMID 9889198.
  • Liberati NT, Datto MB, Frederick JP, Shen X, Wong C, Rougier-Chapman EM, Wang XF (1999). "Smads bind directly to the Jun family of AP-1 transcription factors". Proc. Natl. Acad. Sci. U.S.A. 96 (9): 4844–4849. Bibcode:1999PNAS...96.4844L. doi:10.1073/pnas.96.9.4844. PMC 21779. PMID 10220381.
  • Chen P, Flory E, Avots A, Jordan BW, Kirchhoff F, Ludwig S, Rapp UR (2000). "Transactivation of naturally occurring HIV-1 long terminal repeats by the JNK signaling pathway. The most frequent naturally occurring length polymorphism sequence introduces a novel binding site for AP-1 factors". J. Biol. Chem. 275 (27): 20382–20390. doi:10.1074/jbc.M001149200. PMID 10764760.
  • Echlin DR, Tae HJ, Mitin N, Taparowsky EJ (2000). "B-ATF functions as a negative regulator of AP-1 mediated transcription and blocks cellular transformation by Ras and Fos". Oncogene. 19 (14): 1752–1763. doi:10.1038/sj.onc.1203491. PMID 10777209.
  • Verrecchia F, Pessah M, Atfi A, Mauviel A (2000). "Tumor necrosis factor-alpha inhibits transforming growth factor-beta /Smad signaling in human dermal fibroblasts via AP-1 activation". J. Biol. Chem. 275 (39): 30226–30231. doi:10.1074/jbc.M005310200. PMID 10903323.
  • Singh K, Camera E, Krug L, Basu A, Pandey RK, Munir S, Wlaschek M, Kochanek S, Schorpp-Kistner M, Picardo M, Angel P, Niemann C, Maity P, Scharffetter-Kochanek K (2018). "JunB defines functional and structural integrity of the epidermo-pilosebaceous unit in the skin". Nature. 9 (1): 3425. Bibcode:2018NatCo...9.3425S. doi:10.1038/s41467-018-05726-z. PMC 6109099. PMID 30143626.

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


  • v
  • t
  • e
(1) Basic domains
(1.1) Basic leucine zipper (bZIP)
(1.2) Basic helix-loop-helix (bHLH)
Group A
Group B
Group C
bHLH-PAS
Group D
Group E
Group F
bHLH-COE
(1.3) bHLH-ZIP
(1.4) NF-1
(1.5) RF-X
(1.6) Basic helix-span-helix (bHSH)
(2) Zinc finger DNA-binding domains
(2.1) Nuclear receptor (Cys4)
subfamily 1
subfamily 2
subfamily 3
subfamily 4
subfamily 5
subfamily 6
subfamily 0
(2.2) Other Cys4
(2.3) Cys2His2
(2.4) Cys6
(2.5) Alternating composition
(2.6) WRKY
(3) Helix-turn-helix domains
(3.1) Homeodomain
Antennapedia
ANTP class
protoHOX
Hox-like
metaHOX
NK-like
other
(3.2) Paired box
(3.3) Fork head / winged helix
(3.4) Heat shock factors
(3.5) Tryptophan clusters
(3.6) TEA domain
  • transcriptional enhancer factor
(4) β-Scaffold factors with minor groove contacts
(4.1) Rel homology region
(4.2) STAT
(4.3) p53-like
(4.4) MADS box
(4.6) TATA-binding proteins
(4.7) High-mobility group
(4.9) Grainyhead
(4.10) Cold-shock domain
(4.11) Runt
(0) Other transcription factors
(0.2) HMGI(Y)
(0.3) Pocket domain
(0.5) AP-2/EREBP-related factors
(0.6) Miscellaneous
see also transcription factor/coregulator deficiencies


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