TIAF1

From Wikipedia, the free encyclopedia

TGFB1-induced anti-apoptotic factor 1

Identifiers

TIAF1; MAJN; MYO18A; MYSPDZ; SPR210

External IDs

Gene ontology
Molecular Function:	• nucleotide binding • molecular_function • motor activity • protein binding • ATP binding
Cellular Component:	• nucleus • cytoskeleton • myosin complex
Biological Process:	• apoptosis • anti-apoptosis • I-kappaB kinase/NF-kappaB cascade

Orthologs

Human

Mouse

Entrez

9220

n/a

Refseq

NM_004740 (mRNA)
NP_004731 (protein)

n/a (mRNA)
n/a (protein)

Pubmed search

[1]

n/a

TGFB1-induced anti-apoptotic factor 1, also known as TIAF1, is a human gene.^[1]

[edit] References

^ Entrez Gene: TIAF1 TGFB1-induced anti-apoptotic factor 1.

[edit] Further reading

Nagase T, Seki N, Ishikawa K, et al. (1997). "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 Res. 3 (5): 321–9, 341–54. PMID 9039502.
Chang NS, Mattison J, Cao H, et al. (1999). "Cloning and characterization of a novel transforming growth factor-beta1-induced TIAF1 protein that inhibits tumor necrosis factor cytotoxicity.". Biochem. Biophys. Res. Commun. 253 (3): 743–9. doi:10.1006/bbrc.1998.9846. PMID 9918798.
Ji H, Zhai Q, Zhu J, et al. (2000). "A novel protein MAJN binds to Jak3 and inhibits apoptosis induced by IL-2 deprival.". Biochem. Biophys. Res. Commun. 270 (1): 267–71. doi:10.1006/bbrc.2000.2413. PMID 10733938.
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.
Mori K, Furusawa T, Okubo T, et al. (2004). "Genome structure and differential expression of two isoforms of a novel PDZ-containing myosin (MysPDZ) (Myo18A).". J. Biochem. 133 (4): 405–13. PMID 12761286.
van der Leij J, van den Berg A, Albrecht EW, et al. (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.
Brajenovic M, Joberty G, Küster B, et al. (2004). "Comprehensive proteomic analysis of human Par protein complexes reveals an interconnected protein network.". J. Biol. Chem. 279 (13): 12804–11. doi:10.1074/jbc.M312171200. PMID 14676191.
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.
Bouwmeester T, Bauch A, Ruffner H, et al. (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway.". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216.
Schultz L, Khera S, Sleve D, et al. (2004). "TIAF1 and p53 functionally interact in mediating apoptosis and silencing of TIAF1 abolishes nuclear translocation of serine 15-phosphorylated p53.". DNA Cell Biol. 23 (1): 67–74. doi:10.1089/104454904322745943. PMID 14965474.
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.
Homma K, Kikuno RF, Nagase T, et al. (2004). "Alternative splice variants encoding unstable protein domains exist in the human brain.". J. Mol. Biol. 343 (5): 1207–20. doi:10.1016/j.jmb.2004.09.028. PMID 15491607.
Isogawa Y, Kon T, Inoue T, et al. (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, et al. (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.