TSC22D3

TSC22 domain family, member 3

PDB rendering based on 1dip.

Available structures
PDB	1dip

Identifiers

Symbols

TSC22D3; DIP; DKFZp313A1123; DSIPI; GILZ; TSC-22R; hDIP

External IDs

OMIM: 300506 MGI: 1196284 HomoloGene: 104035 GeneCards: TSC22D3 Gene

Gene Ontology
Molecular function	• sequence-specific DNA binding transcription factor activity • MyoD binding
Cellular component	• nucleus • cytoplasm
Biological process	• transcription, DNA-dependent • regulation of transcription, DNA-dependent • anti-apoptosis • response to osmotic stress • negative regulation of skeletal muscle tissue development
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr X:
106.96 – 107.02 Mb

Chr X:
137.07 – 137.14 Mb

PubMed search

[1]

[2]

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

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

^ Vogel P, Magert HJ, Cieslak A, Adermann K, Forssmann WG (Jan 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.
^ ^a ^b "Entrez Gene: TSC22D3 TSC22 domain family, member 3". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1831.
^ Ayroldi, Emira; Zollo Ornella, Macchiarulo Antonio, Di Marco Barbara, Marchetti Cristina, Riccardi Carlo (Nov. 2002). "Glucocorticoid-Induced Leucine Zipper Inhibits the Raf-Extracellular Signal-Regulated Kinase Pathway by Binding to Raf-1". Mol. Cell. Biol. (United States) 22 (22): 7929–41. doi:10.1128/MCB.22.22.7929-7941.2002. ISSN 0270-7306. PMC 134721. PMID 12391160. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=134721.
^ ^a ^b 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 (United States) 98 (3): 743–53. doi:10.1182/blood.V98.3.743. ISSN 0006-4971. PMID 11468175.

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.
Yu W, Andersson B, Worley KC et al. (1997). "Large-Scale Concatenation cDNA Sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139146.
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.GR1547R. PMC 311072. PMID 11230166. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=311072.
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. doi:10.1182/blood.V98.3.743. 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. doi:10.1128/MCB.22.22.7929-7941.2002. PMC 134721. PMID 12391160. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=134721.
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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
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. PMC 1319161. PMID 12671681. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1319161.
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. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
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). "Hyperhomocysteinemia: DNA hypomethylation and endothelial degeneration". Blood 110 (1): 211–9. doi:10.1182/blood-2006-10-052506. PMC 2077304. PMID 17356131. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2077304.

PDB gallery

1dip: THE SOLUTION STRUCTURE OF PORCINE DELTA-SLEEP-INDUCING PEPTIDE IMMUNOREACTIVE PEPTIDE, NMR, 10 STRUCTURES

TSC22D3

Interactions

References

Further reading