TSC22D3

TSC22 domain family, member 3
PDB rendering based on 1dip.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1dip​
Identifiers
Symbols	TSC22D3 ; DIP; DSIPI; GILZ; TSC-22R; hDIP
External IDs	OMIM: 300506 MGI: 1196284 HomoloGene: 104035 GeneCards: TSC22D3 Gene
Gene ontology Molecular function • transcription factor activity, sequence-specific DNA binding • protein binding • MRF binding Cellular component • nucleus • cytosol Biological process • negative regulation of transcription from RNA polymerase II promoter • regulation of transcription, DNA-templated • response to osmotic stress • ion transmembrane transport • negative regulation of skeletal muscle tissue development • transmembrane transport • negative regulation of activation-induced cell death of T cells Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	1831	14605
Ensembl	ENSG00000157514	ENSMUSG00000031431
UniProt	Q99576	Q9Z2S7
RefSeq (mRNA)	NM_001015881	NM_001077364
RefSeq (protein)	NP_001015881	NP_001070832
Location (UCSC)	Chr X: 107.71 – 107.78 Mb	Chr X: 140.54 – 140.6 Mb
PubMed search

TSC22 domain family protein 3 is a protein that in humans is encoded by the TSC22D3 gene.^[1][2]

Function

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.^[2]

Interactions

TSC22D3 has been shown to interact with C-Raf,^[3] NFKB2^[4] and NFKB1.^[4]

References

1. Vogel P, Mägert HJ, Cieslak A, Adermann K, Forssmann WG (Dec 1996). "hDIP--a potential transcriptional regulator related to murine TSC-22 and Drosophila shortsighted (shs)--is expressed in a large number of human tissues". Biochimica Et Biophysica Acta 1309 (3): 200–4. doi:10.1016/s0167-4781(96)00177-7. PMID 8982256.
2. "Entrez Gene: TSC22D3 TSC22 domain family, member 3".
3. Ayroldi E, Zollo O, Macchiarulo A, Di Marco B, Marchetti C, Riccardi C (Nov 2002). "Glucocorticoid-induced leucine zipper inhibits the Raf-extracellular signal-regulated kinase pathway by binding to Raf-1". Molecular and Cellular Biology 22 (22): 7929–41. doi:10.1128/MCB.22.22.7929-7941.2002. PMC 134721. PMID 12391160.
4. Ayroldi E, Migliorati G, Bruscoli S, Marchetti C, Zollo O, Cannarile L, D'Adamio F, Riccardi C (Aug 2001). "Modulation of T-cell activation by the glucocorticoid-induced leucine zipper factor via inhibition of nuclear factor kappaB". Blood 98 (3): 743–53. doi:10.1182/blood.V98.3.743. PMID 11468175.

Further reading

• Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (Apr 1996). "A "double adaptor" method for improved shotgun library construction". Analytical Biochemistry 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
• Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA (Apr 1997). "Large-scale concatenation cDNA sequencing". Genome Research 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
• Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Böcher M, Blöcker H, Bauersachs S, Blum H, Lauber J, Düsterhöft A, Beyer A, Köhrer K, Strack N, Mewes HW, Ottenwälder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A (Mar 2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Research 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
• Cannarile L, Zollo O, D'Adamio F, Ayroldi E, Marchetti C, Tabilio A, Bruscoli S, Riccardi C (Feb 2001). "Cloning, chromosomal assignment and tissue distribution of human GILZ, a glucocorticoid hormone-induced gene". Cell Death and Differentiation 8 (2): 201–3. doi:10.1038/sj/cdd/4400798. PMID 11313722.
• Mittelstadt PR, Ashwell JD (Aug 2001). "Inhibition of AP-1 by the glucocorticoid-inducible protein GILZ". The Journal of Biological Chemistry 276 (31): 29603–10. doi:10.1074/jbc.M101522200. PMID 11397794.
• Ayroldi E, Migliorati G, Bruscoli S, Marchetti C, Zollo O, Cannarile L, D'Adamio F, Riccardi C (Aug 2001). "Modulation of T-cell activation by the glucocorticoid-induced leucine zipper factor via inhibition of nuclear factor kappaB". Blood 98 (3): 743–53. doi:10.1182/blood.V98.3.743. PMID 11468175.
• Ayroldi E, Zollo O, Macchiarulo A, Di Marco B, Marchetti C, Riccardi C (Nov 2002). "Glucocorticoid-induced leucine zipper inhibits the Raf-extracellular signal-regulated kinase pathway by binding to Raf-1". Molecular and Cellular Biology 22 (22): 7929–41. doi:10.1128/MCB.22.22.7929-7941.2002. PMC 134721. PMID 12391160.
• Berrebi D, Bruscoli S, Cohen N, Foussat A, Migliorati G, Bouchet-Delbos L, Maillot MC, Portier A, Couderc J, Galanaud P, Peuchmaur M, Riccardi C, Emilie D (Jan 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.
• Shi X, Shi W, Li Q, Song B, Wan M, Bai S, Cao X (Apr 2003). "A glucocorticoid-induced leucine-zipper protein, GILZ, inhibits adipogenesis of mesenchymal cells". EMBO Reports 4 (4): 374–80. doi:10.1038/sj.embor.embor805. PMC 1319161. PMID 12671681.
• Asselin-Labat ML, David M, Biola-Vidamment A, Lecoeuche D, Zennaro MC, Bertoglio J, Pallardy M (Jul 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.
• Asselin-Labat ML, Biola-Vidamment A, Kerbrat S, Lombès M, Bertoglio J, Pallardy M (Jul 2005). "FoxO3 mediates antagonistic effects of glucocorticoids and interleukin-2 on glucocorticoid-induced leucine zipper expression". Molecular Endocrinology 19 (7): 1752–64. doi:10.1210/me.2004-0206. PMID 15705665.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 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, Vandewalle A, Pearce D (Dec 2005). "A novel role for glucocorticoid-induced leucine zipper protein in epithelial sodium channel-mediated sodium transport". The Journal of Biological Chemistry 280 (48): 39970–81. doi:10.1074/jbc.M508658200. PMID 16216878.
• Hamdi H, Godot V, Maillot MC, Prejean MV, Cohen N, Krzysiek R, Lemoine FM, Zou W, Emilie D (Jul 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. PMC 2077304. PMID 17356131.