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IRF1, IFN regulatory factor 1, is a member of the IFN regulatory transcription factor (IRF) family which regulates gene expression critical to immune response, hematopoiesis and proliferation. IRF-1 is a transcriptional activator for IFN-A, IFN-B, and IFN-G stimulated genes. IRF1 is also a tumor suppressor transcription factor inducing apoptosis of tumorigenic cell lines.

Members of the Interferon regulatory factor (IRF) family regulate gene expression critical to immune response, hemopoiesis, and proliferation. IRF-3 is a member of the IRF family, and is distinct from other family members. Its transcriptional activity is regulated solely by posttranslational modifications. It plays a crucial role in activation of innate immunity and inflammation in response to viral infection. IRF-3 mediates interferon-stimulated response element (isre) promoter activation. Functions as a molecular switch for antiviral activity. Dsrna generated during the course of an viral infection leads to IRF3 phosphorylation on the c-terminal serine/threonine cluster. This induces a conformational change, leading to its dimerization, nuclear localization and association with creb binding protein (crebbp) to form dsrna-activated factor 1 (draf1), a complex which activates the transcription of genes under the control of isre. The complex binds to the ie and prdiii regions on the ifn

IRF5 belongs to the interferon regulatory factor (IRF) family, which is a group of transcription factors with diverse roles, including virus-mediated activation of interferon, and modulation of cell growth, differentiation, apoptosis, and immune system activity. Members of the IRF family are characterized by a conserved N-terminal DNA-binding domain containing tryptophan (W) repeats.

IRF7 belongs to the interferon regulatory transcription factor (IRF) family. IRF7 plays a role in the transcriptional activation of virus-inducible cellular genes, including interferon beta chain genes. Inducible expression of IRF7 is largely restricted to lymphoid tissue.

Immunity-related GTPase family M protein (IRGM) is essential for clearance of severe protozoan and bacterial infections. IRGM belongs to the p47 immunity-related GTPase family. IRGM serves in innate immune response possibly via regulation of autophagy. IRGM regulates proinflammatory cytokine production and inhibit endotoxemia upon infection and also has a part in macrophages adhesion and motility. Polymorphisms which modify the natural expression of the IRGM gene are associated with a susceptibility to Crohn's disease and tuberculosis.

Iron-sulfur cluster assembly enzyme (ISCU) belongs to the nifU family. Iron-sulfur (Fe-S) clusters are required for several mitochondrial enzymes and other subcellular compartment proteins. ISCU interacts with ISCS (a cysteine desulfurase) to sequester inorganic sulfur for Fe-S cluster assembly. The ISCU-ISCS protein complex localizes in both mitochondria and cytosol, implying that Fe-S cluster assembly occurs in multiple subcellular compartments in mammalian cells.

ISG15 ubiquitin-like Modifier is conjugated to the intracellular target proteins after IFN-alpha or IFN-beta stimulation. ISG15 enzymatic pathway is partially distinct from that of ubiquitin, differing in substrate specificity and interaction with ligating enzymes. ISG15 conjugation pathway uses a dedicated E1 enzyme, but seems to converge with the ub conjugation pathway at the level of a specific E2 enzyme. ISG15 protein targets include STAT1, SERPINA 3G/SPI2A, JAK1, MAPK3/ERK1, PLCG1, EIF2AK2/PKR, MX1/MXA, and RIG-1. Deconjugated by USP18/UBP43 shows specific chemotactic activity towards neutrophils and activates them to induce release of eosinophil chemotactic factors. ISG15 serves as a trans-acting binding factor directing the association of ligated target proteins to intermediate filaments. ISG15 plays a role in autocrine, paracrine and endocrine mechanisms, as in cell-to-cell signaling, possibly partly by inducing ifn-gamma secretion by monocytes and macrophages. ISG15 displays a

ISG15 ubiquitin-like Modifier is conjugated to the intracellular target proteins after IFN-alpha or IFN-beta stimulation. ISG15 enzymatic pathway is partially distinct from that of ubiquitin, differing in substrate specificity and interaction with ligating enzymes. ISG15 conjugation pathway uses a dedicated E1 enzyme, but seems to converge with the ub conjugation pathway at the level of a specific E2 enzyme. ISG15 protein targets include STAT1, SERPINA 3G/SPI2A, JAK1, MAPK3/ERK1, PLCG1, EIF2AK2/PKR, MX1/MXA, and RIG-1. Deconjugated by USP18/UBP43 shows specific chemotactic activity towards neutrophils and activates them to induce release of eosinophil chemotactic factors. ISG15 serves as a trans-acting binding factor directing the association of ligated target proteins to intermediate filaments. ISG15 plays a role in autocrine, paracrine and endocrine mechanisms, as in cell-to-cell signaling, possibly partly by inducing ifn-gamma secretion by monocytes and macrophages. ISG15 displays antiviral activity during viral infections. ISG15 in response to IFN-TAU secreted by the conceptus, ligates to and regulate proteins involved in the release of prostaglandin F2-alpha and thus prevent lysis of the corpus luteum and maintain the pregnancy. ISG15 shares several common properties with other ubiquitin-like molecules, but its activity is strongly regulated by precise signaling pathways that have a role in innate immunity.

Isochorismatase Domain Containing 2, also known as ISOC2, is a part of the isochorismatase family. SOC2 is localized in mitochondrion, cytoplasm, and nucleus. ISOC2 which interacts with CDKN2A is localizes to the nucleus in the attendance of CDKN2A.

Integrins are heterodimeric proteins consist of alpha and beta subunits. There are more than 18 alpha and 8 beta subunits discovered in mammals. Integrin family members are membrane receptors that participates in cell adhesion and recognition in a variety of processes including embryogenesis, hemostasis, tissue repair, immune response and metastatic diffusion of tumor cells. ITGB1 encodes a beta subunit.

Integrins are heterodimeric proteins consist of alpha and beta subunits. There are more than 18 alpha and 8 beta subunits discovered in mammals. Integrin family members are membrane receptors that participates in cell adhesion and recognition in a variety of processes including embryogenesis, hemostasis, tissue repair, immune response and metastatic diffusion of tumor cells. ITGB1 encodes a beta subunit.

Integrins are heterodimeric proteins consist of alpha and beta subunits. There are more than 18 alpha and 8 beta subunits discovered in mammals. Integrin family members are membrane receptors that participates in cell adhesion and recognition in a variety of processes including embryogenesis, hemostasis, tissue repair, immune response and metastatic diffusion of tumor cells. ITGB1 encodes a beta subunit.

Nicotinamide riboside kinase 2 (ITGB1BP3) is a member of the uridine kinase family and NRK subfamily. ITGB1BP3 catalyzes the phosphorylation of nicotinic acid riboside and nicotinamide riboside to create nicotinic acid mononucleotide and nicotinamide mononucleotide. ITGB1BP3 reduces laminin matrix deposition and cell adhesion to laminin, but not to fibronectin. ITGB1BP3 is involved in the regulation of PXN at the protein level and of PXN tyrosine phosphorylation. ITGB1BP3 also has a role in the regulation of terminal myogenesis.

Integrin Beta 3 Binding Protein (ITGB3BP1) is a broadly expressed protein which contains a DD1 or RepD1 domain and an LXXLL motif. ITGB3BP1 functions as a nuclear receptor coactivator while induced by estrogen. ITGB3BP1 is also relates with the CENP-A-CAD complex that is engaged in mitotic progression, the assembly of kinetochore proteins and chromosome segregation. ITGB3BP1 behave s as a transcriptional corepressor via its interaction with the NFKB1 NF-kappa-B subunit by interfering with the transactivation domain of NFKB1.

ITGB4 (integrin beta-4 isoform 1) belongs to the Integrin beta family. ITGB4 forms noncovalent heterodimers with Integrin alpha 6 and takes part in the formation of epithelial hemidesmosomes. ITGB4 has a vital structural role in the hemidesmosome of epithelial cells and is needed for the regulation of keratinocyte motility & polarity. ITGB4 leans towards the association with alpha 6 subunit and is expected to take a key role in the biology of invasive carcinoma.

ITPA enzyme catalyzes the pyrophosphohydrolysis of both ITP (inosine triphosphate) and dITP (deoxyinosine triphosphate) to IMP (inosine monophosphate) and diphosphate. IMP is exercised as a substrate for purine nucleotide pathways. IMP is phosphorylated to ITP, and ITPA mediates the concentration of ITP in the cell by changing ITP back to IMP. Defects in ITPA result in ITPA deficiency which is thought to be inherited and is characterized by an over-accumulation of ITP in erythocytes, leukocytes and fibroblasts.

Inositol-tetrakisphosphate 1-kinase (ITPK1) is a 414 amino acid monomer which is a member of the ITPK1 family and exists as 2 alternatively spliced isoforms. ITPK1 highest levels are found in the brain, followed by the heart, skeletal muscle, kidney, pancreas, liver, placenta and lung. ITPK1 is comprised of one ATP-grasp domain and has been shown to phosphorylate various inositol polyphosphates and modify TNFa induced apoptosis.

IVD is a mitochondrial matrix enzyme that is part of the cyl-CoA dehydrogenase family which catalyzes the third step in leucine catabolism. The genetic deficiency of IVD leads to a buildup of isovaleric acid, which is toxic to the central nervous system and results in isovaleric acidemia. IVD is a homotetrameric flavoenzyme which catalyzes the conversion of isovaleryl-CoA to 3-methylcrotonyl-CoA.

IYD is an enzyme that catalyzes the oxidative NADPH-dependent deiodination of both mono- and diiodotyrosine although acts more efficiently on monoiodotyrosine. The N-terminus of Iodotyrosine Deiodinase , also known as IYD, plays a role as a membrane anchor. IYD acts during the hydrolysis of thyroglobulin to liberate iodide, which then reenter the hormone-producing pathways.

Janus Kinase 2 (JAK2) is a protein tyrosine kinase which takes part in a specific subset of cytokine receptor signaling pathways such as cell growth, development, differentiation or histone modifications. JAK2 is linked with the prolactin receptor and is necessary for responses to gamma interferon. Mice which do not express an active protein for JAK2 show embryonic lethality associated with the absence of definitive erythropoiesis.

Janus Kinase 2 (JAK2) is a protein tyrosine kinase which takes part in a specific subset of cytokine receptor signaling pathways such as cell growth, development, differentiation or histone modifications. JAK2 is linked with the prolactin receptor and is necessary for responses to gamma IFN. Mice which do not express an active protein for JAK2 show embryonic lethality associated with the absence of definitive erythropoiesis.

Junctional Adhesion Molecule 2 (JAM2) is a member of the immunoglobulin superfamily, and the junctional adhesion molecule (JAM) family. JAM2 is a type I membrane protein which is localized at the tight junctions of both epithelial and endothelial cells. JAM2 functions as an adhesive ligand for interacting with various immune cell types, and may have a role in lymphocyte homing to secondary lymphoid organs.

Junctional Adhesion Molecule 2 (JAM2) is a member of the immunoglobulin superfamily, and the junctional adhesion molecule (JAM) family. JAM2 is a type I membrane protein which is localized at the tight junctions of both epithelial and endothelial cells. JAM2 functions as an adhesive ligand for interacting with various immune cell types, and may have a role in lymphocyte homing to secondary lymphoid organs.

Junctional Adhesion Molecule 2 (JAM2) is a member of the immunoglobulin superfamily, and the junctional adhesion molecule (JAM) family. JAM2 is a type I membrane protein which is localized at the tight junctions of both epithelial and endothelial cells. JAM2 functions as an adhesive ligand for interacting with various immune cell types, and may have a role in lymphocyte homing to secondary lymphoid organs.

JAM3 belongs to the junctional adhesion molecule protein family and functions as a receptor for another member of this family. JAM3 plays a part in cell-cell adhesion. The soluble form of JAM3 is a mediator of angiogenesis. JAM3 is a counter-receptor for ITGAM, mediating leukocyte-platelet interactions and is involved in the regulation of transepithelial migration of polymorphonuclear neutrophils (PMN). A mutation in an intron of the JAM3 gene is linked with hemorrhagic destruction of the brain, subependymal calcification, and congenital cataracts.

JAZF zinc finger 1 (JAZF1) is a nuclear protein with 3 C2H2-type zinc fingers, which functions as a transcriptional repressor. Chromosomal anomalies involving the JAZF1 are linked with endometrial stromal tumors. Alternatively spliced variants which encode different protein isoforms have been described; though, not all variants have been fully characterized.

Jun dimerization protein 2 (JDP2) is a component of the AP-1 transcription factor which inhibits transactivation mediated by the Jun family of proteins. JDP2 is involved in various transcriptional responses associated with AP-1 such as UV-induced apoptosis, cell differentiation, tumorigenesis and antitumogeneris. In addition, JDP2 can act as a repressor by recruiting histone deacetylase 3/HDAC3 to the promoter region of JUN. JDP2 controls transcription via direct regulation of the modification of histones and the assembly of chromatin.

Japanese encephalitis previously known as Japanese B encephalitis is a virus from the family Flaviviridae. it is closely related to the West Nile virus and St. Louis encephalitis virus. Positive sense single stranded RNA genome is packaged in the capsid, formed by the capsid protein. The outer envelope is formed by envelope (E) protein and is the protective antigen. It aids in entry of the virus to the inside of the cell. The genome also encodes several nonstructural proteins also (NS1,NS2a,NS2b,NS3,N4a,NS4b,NS5). NS1 is produced as secretory form also. NS3 is a putative helicase, and NS5 is the viral polymerase. It has been noted that the Japanese encephalitis virus (JEV) infects the lumen of the endoplasmic reticulum (ER) and rapidly accumulates substantial amounts of viral proteins for the JEV. Japanese Encephalitis is diagnosed by detection of antibodies in serum and CSF (cerebrospinal fluid) by IgM capture ELISA.

Jumonji Domain Containing 6, also known as JMJD6 performs as a lysyl-hydroxylase which catalyzes 5-hydroxylation on specific lysine residues of target proteins for instance U2AF2/U2AF65 and LUC7L2, as a regulator of RNA splicing by mediating 5-hydroxylation of U2AF2/U2AF65, affecting the pre-mRNA splicing activity of U2AF2/U2AF65. Additionally to peptidyl-lysine 5-dioxygenase activity, JMJD6 performs as an RNA hydroxylase, as proposed by its ability to bind single strand RNA. Furthermore, it acts as an arginine demethylase which demethylates histone H3 at 'Arg-2' (H3R2me) as well as histone H4 at 'Arg-3' (H4R3me), thus taking a part in histone code.

JmjC domain-containing protein 7 (JMJD7) is a member of the JMJD family. JMJD7 encodes highly conserved proteins with a JmjC domain, which are part of the cupin metalloenzyme superfamily. JMJD7 was first thought to be an alternatively spliced isoform of PLA2G4B. It is derived from JMJD7 which is located upstream of PLA2G4B. Most tissues also express read-through transcripts from JMJD7 into the downstream PLA2G4B gene, some of which may encode fusion proteins combining the N-terminus of JMJD7 with PLA2G4B protein.

JUN N-terminal Kinase 2is a member of the MAP kinase family. MAP kinases act as an integration point for multiple biochemical signals, and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation and development. This kinase targets specific transcription factors, and thus mediates immediate-early gene expression in response to various cell stimuli. It is most closely related to MAPK8, both of which are involved in UV radiation induced apoptosis, thought to be related to the cytochrome c-mediated cell death pathway. This gene and MAPK8 are also known as c-Jun N-terminal kinases. This kinase blocks the ubiquitination of tumor suppressor p53, and thus it increases the stability of p53 in nonstressed cells. Studies of this gene's mouse counterpart suggest a key role in T-cell differentiation. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.

Josephin-1 (JOSD1) has minimal protease activity towards poly-ubiquitin chains (in vitro). JOSD1 functions as a deubiquitinating enzyme. Ubiquitin-binding sites in the Josephin domain are a factor in ubiquitin chain binding and cleavage.

JSRP1 takes part in excitation-contraction connection at the sarcoplasmic reticulum. JSRP1 is able to cooperate with CACNA1S, CACNB1 and calsequestrin to assist in regulating calcium influx and efflux in skeletal muscle.

Jumping Translocation Breakpoint (JTB) takes part in the regulation of cell proliferation and is essential for cytokinesis during mitosis. JTB inhibits apoptosis induced by TGFB1 and increases AURKB activity. JTB is also a part of the chromosomal passenger complex (CPC) which is a key regulator of mitosis.

Kidney associated antigen 1 (KAAG1) is expressed in testis and kidney, and, at lower levels, in urinary bladder and liver. KAAG1 is expressed by numerous tumors of various histologic origin, including melanomas, sarcomas and colorectal carcinomas.

Lysyl-tRNA synthetase (KARS) is a member of the class-II aminoacyl-tRNA synthetase family. KARS exists as both mitochondrial and cytoplasmic isoforms produced by alternative splicing, and believed to have a role in autoimmune diseases, such as polymyositis or dermatomyositis. The KARS protein functions to catalyze the aminoacylation of tRNAs by their corresponding amino acids, so linking amino acids with tRNA-contained nucleotide triplets.

KAT2A (GCN5L2 or GCN5) is a histone acetyltransferase (HAT), which functions mainly as a transcriptional activator. GCN5L2 may be one of the enzymes involved in acetylation in vivo. GCN5 is expressed primarily in the embryo and newborn and is crucial for normal embryonic development. Hence, KAT2A appears to be significant for differentiation of embryonic-derived preadipocytes. GCN5 also functions as a repressor of NF-kappa-B by promoting ubiquitination of the NF-kappa-B subunit RELA in a HAT-independent manner. Loss of GCN5L2 leads to a high occurrence of apoptosis in the KAT2A mutants, which begins before the onset of morphological abnormality.

General control of amino acid synthesis protein 5 like 2 (KAT2A) is a member of the GCN5 family. KAT2A functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Acetylation of histones gives a specific tag for epigenetic transcription activation. KAT2A interacts with Ku70, TAF9, transcription initiation protein SPT3 homolog, TADA2L, Ku80 and DDB1.

KCNIP3 belongs to a family of voltage-gated potassium (Kv) channel-interacting proteins, which belong to the recoverin branch of the EF-hand superfamily. KCNIP family members are small calcium binding proteins containing EF-hand-like domains. KCNIP3 also functions as a calcium-regulated transcriptional repressor, and interacts with presenilins. Mutations in the presenilin genes are implicated in Alzheimer's disease.

The KCNMB3 belongs to a family of 4 auxiliary beta subunits found in the mammalian genome, which associate with Slo1 alpha subunits and regulate BK channel function. In humans, the KCNMB3 gene is comprised of 4 N-terminal alternative exons which produce 4 functionally distinct beta3 subunits, beta3a-d. Three variants, beta3a-c, display kinetically distinct inactivation behaviors.

Potassium Channel Tetramerisation Domain Containing 11 (KCTD11) is a 232 amino acid regulator of neuronal differentiation which induces growth arrest, apoptosis and the expression of p27 (cyclin-dependent kinase inhibitor). KCTD11 is expressed most highly in cerebellum. KCTD11 functions as an antagonist of the Hedgehog pathway and activator of the caspase cascade and among its related super-pathways are Melatonin Signaling and Activation of cAMP-Dependent PKA.

KCTD15 protein is encoded in humans by the KCTD15 gene. KCTD15 is expressed at a high level in the brain and the hypothalamus. The potassium channel KCTD15 was identified as a genetic loci linked to higher than normal BMI in humans along with genes such as GNPDA2, MTCH2, FTO, and TMEM18. SNPs (Single nucleotide polymorphisms) in non-diabetic and diabetic patients showed that FTO was most strongly associated with obesity while MTCH2 and GNPDA2 were still notably associated with higher than normal BMI levels.

KCTD15 protein is encoded in humans by the KCTD15 gene. KCTD15 is expressed at a high level in the brain and the hypothalamus. The potassium channel KCTD15 was identified as a genetic loci linked to higher than normal BMI in humans along with genes such as GNPDA2, MTCH2, FTO, and TMEM18. SNPs (Single nucleotide polymorphisms) in non-diabetic and diabetic patients showed that FTO was most strongly associated with obesity while MTCH2 and GNPDA2 were still notably associated with higher than normal BMI levels.

KCTD15 protein is encoded in humans by the KCTD15 gene. KCTD15 is expressed at a high level in the brain and the hypothalamus. The potassium channel KCTD15 was identified as a genetic loci linked to higher than normal BMI in humans along with genes such as GNPDA2, MTCH2, FTO, and TMEM18. SNPs (Single nucleotide polymorphisms) in non-diabetic and diabetic patients showed that FTO was most strongly associated with obesity while MTCH2 and GNPDA2 were still notably associated with higher than normal BMI levels.

KCTD4 also known as Potassium Channel Tetramerisation Domain Containing 4 has an N-terminal homodimerization domain which contains multiple copies of kelch repeats and C2H2-type zinc fingers. Proteins which include BTB domains are consider being involved in transcriptional regulation through control of chromatin structure and function. In addition, KCTD4 is a 259 amino acid protein which contains one BTB domain, a possible role as a transcriptional regulator may be suggested.

BTB/POZ domain-containing protein KCTD5 (KCTD5), is a 234 amino acid protein which localizes mainly in the cytoplasm however translocates to the nucleus on interaction with REP proteins. The expression of KCTD5 is up regulated post-transcriptionally in peripheral blood lymphocytes stimulated via the T-cell receptor. KCTD5 interacts particularly with cullin3, attaches ubiquitinated proteins, and created oligomers through its BTB domain.

3-ketodihydrosphingosine reductase (KDSR) is a 332 amino acid multi-pass membrane protein which localizes to the ER and is a member of the short-chain dehydrogenases/reductases (SDR) family. KDSR is a secreted protein that is weakly expressed in hematopoietic tissue. Furthermore, KDSR catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS). The putative active site residues of KDSR are found on the cytosolic side of the endoplasmic reticulum membrane. Chromosomal rearrangement in the KDSR gene is a cause of follicular lymphoma, aka type II chronic lymphatic leukemia.

Kell blood group glycoprotein homolog or KEL, is an enzyme, part of the zinc endopeptidase of the neprilysin (NEP) group of proteins. KEL has a crucial part in the production of the potent bioactive ET-3, which also includes enzymes that are endothelin convertingenzymes (PEX, XCE, DINE &various NEP-like proteins). KEL uses a single disulfide bond to XK, a gated membranal transporter. The Kell antigen system that includes two proteins, is very crucial among blood group systems.

Ketohexokinase catalyzes the phosphorylation of fructose to produce fructose-1-phosphate, resulting in the utilization of ATP and creation of AMP. Ketohexokinase commences initial step in the metabolism of dietary fructose and is a significant regulator of hepatic glucose metabolism. Ketohexokinase is found in liver, renal cortex, and small intestine. Its deficiency causes the benign hereditary metabolic disorder essential fructosuria, leading to fructose being excreted in the urine. Ketohexokinase-dependent metabolism of fructose induces proinflammatory mediators in proximal tubular cells. ketohexokinase plays an unknown physiologic function that remains intact in essential fructosuria. Ketohexokinase expression is reduceed in human clear cell type of renal cell carcinoma.