Thymidine kinase 1(TK1) belongs to the thymidine kinase family. It is located in the cytoplasm, and phosphorylated on Ser-13 in mitosis during post-translational modification. Two forms of this protein have been identified in animal cells, one in cytosol TK1 and one in mitochondria TK2. Thymidine kinases have a key function in the synthesis of DNA and thereby in cell division, as they are part of the unique reaction chain to introduce deoxythymidine into the DNA. Activity of the cytosolic enzyme is high in proliferating cells and peaks during the S-phase of the cell cycle, while it is very low in resting cells. TK1 acts as a homotetramer, and can transform thymidime to thymidine 5'-phosphate with the help of ATP
TL1A, also known as TNFSF15, is a cytokine that belongs to the tumor necrosis factor (TNF) ligand family. It is specifically expressed in endothelial cells. TL1A also can be detected in monocytes, placenta, lung, liver, kidney, skeletal muscle, pancreas, spleen, prostate, small intestine and colon. TL1A is a ligand for receptor TNFRSF25 and decoy receptor TNFRSF21/DR6. It mediates activation of NF-kappa-B. It also inhibits vascular endothelial growth and angiogenesis (in vitro). TL1A promotes activation of caspases and apoptosis. It is also found to inhibit endothelial cell proliferation, and thus may function as an angiogenesis inhibitor.
TL-1A belongs to the TNF superfamily of ligands. It is specially expressed in endothelial cells, and is detected in the placenta, lung, kidney skeletal muscle, pancreas, small intestine and colon. TL-1A inhibits endothelial cell proliferation and angiogenesis. It has been proved to promote NF-KB activation, caspase activity, and apoptosis in responding cell lines. TL-1Acan bind with TNFRSF25/DR3 receptor and a decoy receptor TNFRSF21/DR6.
Immunoglobulin superfamily member 11(IGSF11) are expressed on the plasma membrane in the tesis and brain. These IGSF proteins undergo final modifications during capacitation and/or the acrosome reaction. IGSF proteins share significant homology with endothelial cell-selective adhesion molecule and coxsackievirus and adenovirus receptor, which mediates cell attachment and homotypic intercellular interactions. In clinical, the IGSF11 has been reported to over expressed in colorectal cancers and hepatocellular carcinomas as well as intestinal-type gastric cancers compared to their corresponding non- cancerous tissues. The IGSF11 has also been found expressed abundantly in testis and ovary and the IGSF11 can be used as a candidate of cancer-testis antigen.
The protein encoded by this gene is a serine/threonine kinase that may be involved in the regulation of chromatin assembly. The encoded protein is only active when it is phosphorylated, and this phosphorylation is cell cycle-dependent, with the maximal activity of this protein coming during S phase. The catalytic activity of this protein is diminished by DNA damage and by blockage of DNA replication. Three transcript variants encoding different isoforms have been found for this gene.
Serine / threonine-protein kinase tousled-like 2; also known as PKU-alpha; Tousled-like kinase 2 and TLK2; is a nucleus protein which belongs to theprotein kinase superfamily and Ser/Thr protein kinase family. The tousled-like kinases are an evolutionarily conserved family of proteins implicated in DNA repair; DNA replication and mitosis in metazoans and plants. Their absence from the yeasts and other eukaryotic 'microbes' suggests a specific role for them in the development of multicellular organisms. Tousled-like kinase 2 / TLK2 is widely expressed. It is present in fetal placenta; liver; kidney; pancreas; heart and skeletal muscle. It is also found in adult cell lines. Tousled-like kinase 2 / TLK2 contains oneprotein kinase domain. Tousled-like kinase 2 / TLK2 is rapidly and transiently inhibited by phosphorylation following the generation of DNA double-stranded breaks during S-phase. This is cell cycle checkpoint and ATM-pathway dependent and appears to regulate processes involved in chromatin assembly.
TLR2, also known as CD282, is a member of the Toll-like receptor (TLR) family. TLRs are highly conserved from Drosophila to humans and share structural and functional similarities. They play a fundamental role in pathogen recognition and activation of innate immunity. They recognize pathogen-associated molecular patterns (PAMPs) that are expressed on infectious agents, and mediate the production of cytokines necessary for the development of effective immunity. The various TLRs exhibit different patterns of expression. TLR2 contains 14 LRR (leucine-rich) repeats and 1 TIR domain. TLR2 gene is expressed most abundantly in peripheral blood leukocytes, and mediates host response to Gram-positive bacteria and yeast via stimulation of NF-kappaB. CD282 cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. It also cooperates with TLR1 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. CD282 acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. It may also promote apoptosis in response to lipoproteins.
The protein encoded by this gene is a member of the Toll-like receptor (TLR) family which plays a fundamental role in pathogen recognition and activation of innate immunity. TLRs are highly conserved from Drosophila to humans and share structural and functional similarities. They recognize pathogen-associated molecular patterns (PAMPs) that are expressed on infectious agents, and mediate the production of cytokines necessary for the development of effective immunity. The various TLRs exhibit different patterns of expression. This gene is expressed most abundantly in peripheral blood leukocytes, and mediates host response to Gram-positive bacteria and yeast via stimulation of NF-kappaB.
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