This gene is a classical cadherin from the cadherin superfamily. The encoded protein is a calcium dependent cell-cell adhesion glycoprotein comprised of five extracellular cadherin repeats, a transmembrane region and a highly conserved cytoplasmic tail. Mutations in this gene are correlated with gastric, breast, colorectal, thyroid and ovarian cancer. Loss of function is thought to contribute to progression in cancer by increasing proliferation, invasion, and/or metastasis. The ectodomain of this protein mediates bacterial adhesion to mammalian cells and the cytoplasmic domain is required for internalization. Identified transcript variants arise from mutation at consensus splice sites.
Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells.
This gene encodes a member of the hydratase/isomerase superfamily. The gene product shows high sequence similarity to enoyl-coenzyme A (CoA) hydratases of several species, particularly within a conserved domain characteristic of these proteins. The encoded protein, which contains a C-terminal peroxisomal targeting sequence, localizes to the peroxisome. The rat ortholog, which localizes to the matrix of both the peroxisome and mitochondria, can isomerize 3-trans,5-cis-dienoyl-CoA to 2-trans,4-trans-dienoyl-CoA, indicating that it is a delta3,5-delta2,1-dienoyl-CoA isomerase. This enzyme functions in the auxiliary step of the fatty acid beta-oxidation pathway. Expression of the rat gene is induced by peroxisome proliferators.
Antibodies against EEA1 are found in sera from patients with subacute cutaneous lupus erythematosus and other autoimmune diseases.,domain:The FYVE-type zinc finger domain mediates interactions with phosphatidylinositol 3-phosphate.,Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate and participates in endosomal trafficking.,similarity:Contains 1 C2H2-type zinc finger.,similarity:Contains 1 FYVE-type zinc finger.,subunit:Homodimer. Binds STX6. Binds RAB5A, RAB5B, RAB5C and RAB22A that have been activated by GTP-binding.
The polycomb group (PcG) proteins contribute to the maintenance of cell identity, stem cell self-renewal, cell cycle regulation and oncogenesis by maintaining the silenced state of genes that promote cell lineage specification, cell death and cell-cycle arrest. PcG proteins exist in two complexes that cooperate to maintain long-term gene silencing through epigenetic chromatin modifications. The first complex, EED-EZH2, is recruited to genes by DNA-binding transcription factors and methylates histone H3 on Lys27. Methylation of Lys27 facilitates the recruitment of the second complex, PRC1, which ubiquitinylates histone H2A on Lys119. Embryonic ectoderm development protein (EED) is a component of the PRC2 complex, which together with Ezh2 and SUZ12 is absolutely required for histone methyl-transferase activity. EED, SUZ12 and EZH2 are overexpressed in various types of cancer, including tumors of the colon, breast, prostate and ovary.
eEF1A, also named elongation factor Tu (EF-Tu), is one of the eukaryotic elongation factors (eEFs), that function in translation. eEF1A binds GTP and interacts with amino acyl-tRNAs to promote the recruitment of amino acyl-tRNAs to the A-site of the ribosome. After GTP hydrolysis, GDP-eEF1A leaves the ribosome and is later converted back to the GTP-eEF1A by eEF1B. eEF1A is phosphorylated under certain conditions, indicating that its activity is regulated at the post-translational level.
This gene encodes an isoform of the alpha subunit of the elongation factor-1 complex, which is responsible for the enzymatic delivery of aminoacyl tRNAs to the ribosome. This isoform (alpha 2) is expressed in brain, heart and skeletal muscle, and the other isoform (alpha 1) is expressed in brain, placenta, lung, liver, kidney, and pancreas. This gene may be critical in the development of ovarian cancer.
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