Annotation inferences using phylogenetic trees
Combined Automated Annotation using Multiple IEA Methods
A gene encoding a family with sequence similarity 84, member A (FAM84A) enhanced migration of human colon cancer cells.
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FAM84A was frequently upregulated in colorectal cancer, while its expression was not detected across the surveyed normal tissues except testis.
"Using genome-wide cDNA microarray analysis, we identified a number of genes whose expression was up-regulated frequently in colorectal cancer. One of these was a gene termed FAM84A that was not expressed in any of the 23 normal tissues examined except the testis."
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Immunocytochemistry placed FAM84A at a peripheral subcellular membrane region specifically away from contacts with neighboring cells.
"Although immuno-cytochemical staining revealed localization of FAM84A protein in the subcellular membrane region, the staining was limited to the region lacking attachment with neighboring cells."
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Exogenous FAM84A increased motility in mouse NIH3T3 cells, and Ser38 phosphorylation was associated with cell morphology.
"In addition, we found that exogenous FAM84A expression increased cell motility in NIH3T3 cells, and that phosphorylation of serine 38 of FAM84A was associated with morphology of cells."
Nuclear receptor CAR-regulated expression of the FAM84A gene during the development of mouse liver tumors.
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In a phenobarbital-promoted mouse liver tumor model, Fam84a induction depended on CAR and protein was detected cytoplasmically during tumor development.
"Western blotting demonstated that FAM84A protein expression increased in mouse liver after PB treatment; however, the FAM84A protein in liver and liver tumors was not phosphorylated at the serine 38 residue, which has been reported to correlate with morphological changes in cells. Immunohistochemistry analysis revealed the cytoplasmic localization of FAM84A protein and its expression during tumor development in normal tissues (especially in hepatocytes around the central vein), eosinophilic foci, adenomas and carcinomas."
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Mouse FAM84A overexpression increased migration in HepG2 but not detectably in Huh7 cells, demonstrating a strong cell-context boundary.
"The migration rates in cells over-expressing FAM84A were significantly higher (P<0.01) than in control cells (187±20.9 and 120±17.3, respectively, Fig. 7B). We also used Huh7 cells for the migration experiment, but a clear difference was not observed (data not shown). These data indicate that FAM84A plays an important role in acceleration of cell migration, but this depends on the cell type."
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Ser38 phosphorylation was not detected in the mouse liver/cancer contexts, limiting generalization of the earlier morphology-associated phosphosite.
"However, we did not detect serine 38 phosphorylation in over-expressed FAM84A protein in cancer cells, or induced FAM84A protein in mouse liver by PB treatment, neither in the FAM84A protein expressed in liver tumors."
A reference map of the human binary protein interactome.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
The direct miR-874-3p-target FAM84A promotes tumor development in papillary thyroid cancer.
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Knockdown of FAM84A reduced migration and invasion in two human papillary thyroid cancer cell lines.
"Collectively, these results indicated that knockdown of FAM84A significantly suppressed the migration and invasion ability of PTC cells in vitro."
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FAM84A appeared mainly cytoplasmic in papillary thyroid cancer cells, while knockdown reduced nuclear beta-catenin.
"Immunofluorescence analysis indicated that FAM84A was mainly located in cytoplasm, β‐catenin was located both in cytoplasm and in nuclei, and that downregulation of FAM84A inhibited expression of nuclear β‐catenin."
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Reporter and binding assays supported direct regulation of the FAM84A 3' UTR by miR-874-3p in papillary thyroid cancer cells.
"Then, the dual‐luciferase reporter assay showed that overexpression of miR‐874‐3p significantly reduced the relative luciferase activity of the wild‐type FAM84A (Fig. 6E,F)."
Binding Affinity Determines Substrate Specificity and Enables Discovery of Substrates for N-Myristoyltransferases.
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Chemical-proteomic labeling identified LRATD1, its paralog LRATD2, and ERICH5 as candidate human NMT1/2 substrates.
"However, three proteins LRATD1 (LRAT domain-containing 1, also called FAM84A or neurological sensory protein 1 NSE1), LRATD2 (FAM84B/NSE2), and ERICH5 (glutamate-rich protein 5) demonstrated clear fluorescence signals in the Alk12 treated samples compared to the control without Alk12 treatment, and the signals were hydroxylamine-resistant, suggesting that they are potentially N-myristoylated."
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NMT inhibition and loss of labeling in Gly2-to-Ala mutants confirmed LRATD1 and LRATD2 separately as NMT1/2 substrates.
"Alk12 labeling signals decreased with the treatment of NMT inhibitor in LRATD1, LRATD2, and ERICH5 and were completely removed in G2A mutants, confirming LRATD1, LRATD2, and ERICH5 as substrates of NMT1/2 (Figure 4C)."