TIAF1

TIAF1
Identifiers
Aliases	TIAF1, MAJN, SPR210, TGFB1-induced anti-apoptotic factor 1
External IDs	OMIM: 609517; HomoloGene: 130531; GeneCards: TIAF1; OMA:TIAF1 - orthologs
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right lobe of liver gastrocnemius muscle Brodmann area 9 left ventricle nucleus accumbens putamen hypothalamus amygdala right coronary artery stromal cell of endometrium n/a More reference expression data BioGPS n/a
Gene ontology Molecular function molecular function Cellular component nucleus Biological process I-kappaB kinase/NF-kappaB signaling negative regulation of apoptotic process apoptotic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 9220 n/a Ensembl n/a n/a UniProt O95411 n/a RefSeq (mRNA) NM_004740 n/a RefSeq (protein) NP_004731 n/a Location (UCSC) n/a n/a PubMed search [1] n/a
Wikidata
View/Edit Human

TGFB1-induced anti-apoptotic factor 1 is a protein that in humans is encoded by the TIAF1 gene.^[2][3] Transforming growth factors (TGFs), like TGFB1, counteract the functions of tumor necrosis factors (TNFs), like TNF.^[2]

The TIAF1 protein has been shown to mimic TGFB1 functions such as the mediation of growth suppression of U937 cells, but also in the promotion of transforming growth of fibroblasts.^[4]

Human cells transfected with TIAF1 genes showed strong resistance to killing by the expression of intracellular TNF-receptor associated death domain proteins TRADD, FADD, and RIP (receptor interacting protein).^[2]

Interactions

TIAF1 has been shown to interact with p53^[4], Cip1/p21^[4], Smad proteins^[4], Janus kinase 3^[5] and TRIB3.^[6]

References

1. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
2. Chang NS, Mattison J, Cao H, Pratt N, Zhao Y, Lee C (December 1998). "Cloning and characterization of a novel transforming growth factor-beta1-induced TIAF1 protein that inhibits tumor necrosis factor cytotoxicity". Biochemical and Biophysical Research Communications. 253 (3): 743–9. doi:10.1006/bbrc.1998.9846. PMID 9918798.
3. "Entrez Gene: TIAF1 TGFB1-induced anti-apoptotic factor 1".^{[dead link]}
4. Khera, Smaira; Chang, Nan-Shan (2003). "TIAF1 Participates in the Transforming Growth Factor β1-Mediated Growth Regulation". Annals of the New York Academy of Sciences. 995 (1): 11–21. doi:10.1111/j.1749-6632.2003.tb03206.x. ISSN 1749-6632.
5. Ji H, Zhai Q, Zhu J, Yan M, Sun L, Liu X, Zheng Z (April 2000). "A novel protein MAJN binds to Jak3 and inhibits apoptosis induced by IL-2 deprival". Biochemical and Biophysical Research Communications. 270 (1): 267–71. doi:10.1006/bbrc.2000.2413. PMID 10733938.
6. Zhou Y, Li L, Liu Q, Xing G, Kuai X, Sun J, Yin X, Wang J, Zhang L, He F (May 2008). "E3 ubiquitin ligase SIAH1 mediates ubiquitination and degradation of TRB3". Cellular Signalling. 20 (5): 942–8. doi:10.1016/j.cellsig.2008.01.010. PMID 18276110.

Further reading

• Nagase T, Seki N, Ishikawa K, Ohira M, Kawarabayasi Y, Ohara O, Tanaka A, Kotani H, Miyajima N, Nomura N (October 1996). "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain". DNA Research. 3 (5): 321–9, 341–54. doi:10.1093/dnares/3.5.321. PMID 9039502.
• Ji H, Zhai Q, Zhu J, Yan M, Sun L, Liu X, Zheng Z (April 2000). "A novel protein MAJN binds to Jak3 and inhibits apoptosis induced by IL-2 deprival". Biochemical and Biophysical Research Communications. 270 (1): 267–71. doi:10.1006/bbrc.2000.2413. PMID 10733938.
• Mori K, Furusawa T, Okubo T, Inoue T, Ikawa S, Yanai N, Mori KJ, Obinata M (April 2003). "Genome structure and differential expression of two isoforms of a novel PDZ-containing myosin (MysPDZ) (Myo18A)". Journal of Biochemistry. 133 (4): 405–13. doi:10.1093/jb/mvg053. PMID 12761286.
• van der Leij J, van den Berg A, Albrecht EW, Blokzijl T, Roozendaal R, Gouw AS, de Jong KP, Stegeman CA, van Goor H, Chang NS, Poppema S (June 2003). "High expression of TIAF-1 in chronic kidney and liver allograft rejection and in activated T-helper cells". Transplantation. 75 (12): 2076–82. doi:10.1097/01.TP.0000069829.71088.88. PMID 12829915. S2CID 24178625.
• Brajenovic M, Joberty G, Küster B, Bouwmeester T, Drewes G (March 2004). "Comprehensive proteomic analysis of human Par protein complexes reveals an interconnected protein network". The Journal of Biological Chemistry. 279 (13): 12804–11. doi:10.1074/jbc.M312171200. PMID 14676191.
• Bouwmeester T, Bauch A, Ruffner H, Angrand PO, Bergamini G, Croughton K, Cruciat C, Eberhard D, Gagneur J, Ghidelli S, Hopf C, Huhse B, Mangano R, Michon AM, Schirle M, Schlegl J, Schwab M, Stein MA, Bauer A, Casari G, Drewes G, Gavin AC, Jackson DB, Joberty G, Neubauer G, Rick J, Kuster B, Superti-Furga G (February 2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nature Cell Biology. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216. S2CID 11683986.
• Schultz L, Khera S, Sleve D, Heath J, Chang NS (January 2004). "TIAF1 and p53 functionally interact in mediating apoptosis and silencing of TIAF1 abolishes nuclear translocation of serine 15-phosphorylated p53". DNA and Cell Biology. 23 (1): 67–74. doi:10.1089/104454904322745943. PMID 14965474.
• Homma K, Kikuno RF, Nagase T, Ohara O, Nishikawa K (November 2004). "Alternative splice variants encoding unstable protein domains exist in the human brain". Journal of Molecular Biology. 343 (5): 1207–20. doi:10.1016/j.jmb.2004.09.028. PMID 15491607.
• Isogawa Y, Kon T, Inoue T, Ohkura R, Yamakawa H, Ohara O, Sutoh K (April 2005). "The N-terminal domain of MYO18A has an ATP-insensitive actin-binding site". Biochemistry. 44 (16): 6190–6. doi:10.1021/bi0475931. PMID 15835906.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (November 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.