TSC22D3

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TSC22 domain family, member 3
File:PBB Protein TSC22D3 image.jpg
PDB rendering based on 1dip.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols TSC22D3 ; DIP; DKFZp313A1123; DSIPI; GILZ; TSC-22R; hDIP
External IDs Template:OMIM5 Template:MGI HomoloGene: 31215
RNA expression pattern
File:PBB GE TSC22D3 207001 x at tn.png
File:PBB GE TSC22D3 208763 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

TSC22 domain family, member 3, also known as TSC22D3, is a human gene.[1]

The protein encoded by this gene shares significant sequence identity with the murine TSC-22 and Drosophila shs, both of which are leucine zipper proteins, that function as transcriptional regulators. The expression of this gene is stimulated by glucocorticoids and interleukin 10, and it appears to play a key role in the anti-inflammatory and immunosuppressive effects of this steroid and chemokine. Transcript variants encoding different isoforms have been identified for this gene.[1]

References

  1. ↑ 1.0 1.1 "Entrez Gene: TSC22D3 TSC22 domain family, member 3".

Further reading

  • Andersson B, Wentland MA, Ricafrente JY; et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
  • Vogel P, Mägert HJ, Cieslak A; et al. (1997). "hDIP--a potential transcriptional regulator related to murine TSC-22 and Drosophila shortsighted (shs)--is expressed in a large number of human tissues". Biochim. Biophys. Acta. 1309 (3): 200–4. PMID 8982256.
  • Yu W, Andersson B, Worley KC; et al. (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. PMID 9110174.
  • Wiemann S, Weil B, Wellenreuther R; et al. (2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Res. 11 (3): 422–35. doi:10.1101/gr.154701. PMID 11230166.
  • Cannarile L, Zollo O, D'Adamio F; et al. (2001). "Cloning, chromosomal assignment and tissue distribution of human GILZ, a glucocorticoid hormone-induced gene". Cell Death Differ. 8 (2): 201–3. doi:10.1038/sj/cdd/4400798. PMID 11313722.
  • Mittelstadt PR, Ashwell JD (2001). "Inhibition of AP-1 by the glucocorticoid-inducible protein GILZ". J. Biol. Chem. 276 (31): 29603–10. doi:10.1074/jbc.M101522200. PMID 11397794.
  • Ayroldi E, Migliorati G, Bruscoli S; et al. (2001). "Modulation of T-cell activation by the glucocorticoid-induced leucine zipper factor via inhibition of nuclear factor kappaB". Blood. 98 (3): 743–53. PMID 11468175.
  • Ayroldi E, Zollo O, Macchiarulo A; et al. (2002). "Glucocorticoid-induced leucine zipper inhibits the Raf-extracellular signal-regulated kinase pathway by binding to Raf-1". Mol. Cell. Biol. 22 (22): 7929–41. PMID 12391160.
  • Berrebi D, Bruscoli S, Cohen N; et al. (2003). "Synthesis of glucocorticoid-induced leucine zipper (GILZ) by macrophages: an anti-inflammatory and immunosuppressive mechanism shared by glucocorticoids and IL-10". Blood. 101 (2): 729–38. doi:10.1182/blood-2002-02-0538. PMID 12393603.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Shi X, Shi W, Li Q; et al. (2003). "A glucocorticoid-induced leucine-zipper protein, GILZ, inhibits adipogenesis of mesenchymal cells". EMBO Rep. 4 (4): 374–80. doi:10.1038/sj.embor.embor805. PMID 12671681.
  • Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Asselin-Labat ML, David M, Biola-Vidamment A; et al. (2004). "GILZ, a new target for the transcription factor FoxO3, protects T lymphocytes from interleukin-2 withdrawal-induced apoptosis". Blood. 104 (1): 215–23. doi:10.1182/blood-2003-12-4295. PMID 15031210.
  • Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
  • Asselin-Labat ML, Biola-Vidamment A, Kerbrat S; et al. (2005). "FoxO3 mediates antagonistic effects of glucocorticoids and interleukin-2 on glucocorticoid-induced leucine zipper expression". Mol. Endocrinol. 19 (7): 1752–64. doi:10.1210/me.2004-0206. PMID 15705665.
  • Rual JF, Venkatesan K, Hao T; et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
  • Soundararajan R, Zhang TT, Wang J; et al. (2006). "A novel role for glucocorticoid-induced leucine zipper protein in epithelial sodium channel-mediated sodium transport". J. Biol. Chem. 280 (48): 39970–81. doi:10.1074/jbc.M508658200. PMID 16216878.
  • Hamdi H, Godot V, Maillot MC; et al. (2007). "Induction of antigen-specific regulatory T lymphocytes by human dendritic cells expressing the glucocorticoid-induced leucine zipper". Blood. 110 (1): 211–9. doi:10.1182/blood-2006-10-052506. PMID 17356131.

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