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Influenza A and B are the two types of influenza viruses that cause epidemic human disease. Influenza type C infections cause a mild respiratory illness and are not thought to cause epidemics. Influenza A viruses are further categorized into subtypes on the basis of two surface antigens: hemagglutinin (H) and neuraminidase (N). Strains are also described by geographic origin, strain number and year of isolation.

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HOXB4 is a homeodomain-containing transcription factor with diverse roles in embryonic development and the regulation of adult stem cells. It promotes proliferation of hematopoietic stem cells and can both activate and repress apoptosis.

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The complement pathway is an important host defense system that contributes to both innate and acquired immunity. There are three pathways of complement activation: the classical pathway, lectin pathway and alternative pathway. Complement protein Factor I is a key serine protease that modulates the complement cascade by regulating the levels of C3 convertases. It circulates in plasma as a heavily N-glycosylated heterodimer made up of two disulfide linked chains, each carrying three N-linked oligosaccharide chains that may have both structural and functional roles in the interactions with the natural substrate and the cofactor during catalysis. Factor I is a serine protease with a high degree of specificity for C3b and C4b. It requires protein cofactors for cleavage of these complement proteins; Factor H, CR1 or MCP are required for C3b cleavage, and C4bp or CR1 are required for C4b cleavage.

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Arylalkylamine N-acetyltransferase belongs to the superfamily of acetyltransferases. It is the penultimate enzyme in melatonin synthesis and controls the night/day rhythm in melatonin production in the vertebrate pineal gland. Melatonin is essential for seasonal reproduction, modulates the function of the circadian clock in the suprachiasmatic nucleus, and influences activity and sleep. This enzyme is rapidly inactivated when animals are exposed to light at night. This protein is 80% identical to sheep and rat AA-NAT. Arylalkylamine N-acetyltransferase may contribute a multifactorial genetic diseases such as altered behavior in sleep/wake cycle.

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Transcription factor essential for hepatocyte growth, the differentiation of plasma cells, the immunoglobulin secretion, and the unfolded protein response (UPR). Acts during endoplasmic reticulum stress (ER) by activating unfolded protein response (UPR) target genes via direct binding to the UPR element (UPRE). Binds DNA preferably to the CRE-like element 5'-GATGACGTG[TG]N(3)[AT]T-3', and also to some TPA response elements (TRE). Binds to the HLA DR-alpha promoter. Binds to the Tax-responsive element (TRE) of HTLV-I.

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KIF7 is a 1,343 amino acid protein expressed in embryonic stem cells, melanotic melanoma and Jurkat T-cells. KIF7 is a member of the KIF27 subfamily of the kinesin-like protein family and contains one kinesin-motor domain. It is suggested that KIF7 may participate in the Hedgehog (Hh) signaling pathway by regulating the proteolysis and stability of GLI transcription factors. Hedgehog (Hh) signaling plays a critical role in embryonic development.

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The Ras-related superfamily of guanine nucleotide binding proteins includes the R-Ras, Rap, Ral/Rec and Rho/Rab subfamilies. Increasing data suggests an important role for Rab proteins in either endocytosis or in biosynthetic protein transport. The process of transporting newly synthesized proteins from the endoplasmic reticulum to various stacks of the Golgi complex and to secretory vesicles involves the movement of carrier vesicles and requires Rab protein function. Rab proteins are also an integral part of endocytic pathways. Rab 23, also known as HSPC137, is a 237 amino acid member of the Rab family of proteins and localizes to the cytoplasmic side of the cell membrane. Rab 23 is believed to play a role in intracellular protein transportation and signal transduction mediated by small GTPases. Mutations in the gene encoding Rab 23 may result in Carpenter syndrome, also known as ACPS2 (acrocephalopolysyndactyly type 2), a condition characterized by obesity, cardiac defects, polysyndactyly and craniosynostosis.

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Glut4 is a twelve pass transmembrane protein (12TM) whose carboxy-terminus may dictate its cellular localization. Aberrant Glut4 expression has been suggested to contribute to such maladies as obesity and diabetes. Glut4 null mice have shown that while functional Glut4 protein is not required for maintaining normal glucose levels, it is necessary for sustained growth, normal cellular glucose, fat metabolism and prolonged longevity. TUG (ASPL in humans) regulates the trafficking of glucose via Glut4. Full-length TUG forms a complex with Glut4 and in 3T3-L1 adipocytes and this complex is present in unstimulated cells and is disassembled by insulin. TUG acts by trapping endocytosed Glut4 and tethering it intracellularly. Insulin mobilizes this pool of retained Glut4 by releasing the tether.

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G proteins are composed of 3 units, alpha, beta and gamma and are involved in the modulation and transduction of various transmembrane signalling systems. There are families of related genes for each subunit. GNB3 encodes a beta subunit. Beta subunits are required for GTPase activity, for replacement of GDP by GTP, regulate alpha subunits and for G protein-effector interactions. A single-nucleotide polymorphism (C825T) in this gene is associated with essential hypertension and obesity and is also associated with the occurrence of the splice variant GNB3-s, which appears to have increased activity.

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Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of CP110 during G2 phase, thereby acting as an inhibitor of centrosome reduplication.

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Transcription factor involved in regulating gene activity following the primary growth factor response. Binds to the DNA sequence 5'-TGA[CG]TCA-3'.

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The protein encoded by this gene belongs to the membrane-associated guanylate kinase (MAGUK) family, a class of proteins that functions as molecular scaffolds for the assembly of multiprotein complexes at specialized regions of the plasma membrane. This protein is also a member of the CARD protein family, which is defined by carrying a characteristic caspase-associated recruitment domain (CARD). This protein shares a similar domain structure with CARD11 protein. The CARD domains of both proteins have been shown to specifically interact with BCL10, a protein known to function as a positive regulator of cell apoptosis and NF-kappaB activation. When expressed in cells, this protein activated NF-kappaB and induced the phosphorylation of BCL10. Two alternatively spliced variants of this gene encoding distinct isoforms have been reported.

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Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 60S subunit. The protein belongs to the L15E family of ribosomal proteins. It is located in the cytoplasm. This gene shares sequence similarity with the yeast ribosomal protein YL10 gene. Although this gene has been referred to as RPL10, its official symbol is RPL15. This gene has been shown to be overexpressed in some esophageal tumors compared to normal matched tissues. Alternate splicing results in multiple transcript variants. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.

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This gene encodes a transcriptional repressor that interacts with several members of the BCL2 family of proteins. Overexpression of this protein induces apoptosis, which can be suppressed by co-expression of BCL2 proteins. The protein localizes to dot-like structures throughout the nucleus, and redistributes to a zone near the nuclear envelope in cells undergoing apoptosis. Multiple transcript variants encoding different isoforms have been found for this gene.

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Making up nearly 6% of the human genome, chromosome 6 contains around 1200 genes within 170 million base pairs of sequence. Deletion of a portion of the q arm of chromosome 6 is associated with early onset intestinal cancer suggesting the presence of a cancer susceptibility locus. Porphyria cutanea tarda is associated with chromosome 6 through the HFE gene which, when mutated, predisposes an individual to developing this porphyria. Notably, the PARK2 gene, which is associated with Parkinson's disease, and the genes encoding the major histocompatiblity complex proteins, which are key molecular components of the immune system and determine predisposition to rheumatic diseases, are also located on chromosome 6. Stickler syndrome, 21-hydroxylase deficiency and maple syrup urine disease are also associated with genes on chromosome 6. A bipolar disorder susceptibility locus has been identified on the q arm of chromosome 6. The C6orf154 gene product has been provisionally designated C6orf154 pending further characterisation.

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E3 ubiquitin-protein ligase that promotes the degradation of insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln repeat expanded HTT and poly-Ala repeat expanded ARX. Mediates PAX6 ubiquitination leading to proteasomal degradation, thereby modulating cortical neurogenesis. May also inhibit PAX6 transcriptional activity, possibly in part by preventing the binding of PAX6 to its consensus sequences. May contribute to the regulation of the intracellular level of HN (humanin) or HN-containing proteins through the proteasomal degradation pathway. Mediates MED15 ubiquitination leading to proteasomal degradation. May contribute to the innate restriction of retroviruses. Upon overexpression, reduces HIV-1 and murine leukemia virus infectivity, by suppressing viral gene expression. Antiviral activity depends on a functional E3 ubiquitin-protein ligase domain. May regulate TRIM5 turnover via the proteasome pathway, thus counteracting the TRIM5-mediated cross-species restriction of retroviral infection at early stages of the retroviral life cycle.

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ErbB3 is a member of the epidermal growth factor receptor (EGFR) family of receptor tyrosine kinases. ErbB3 is a membrane-bound protein which has a neuregulin binding domain but not an active kinase domain. It can therefore bind this ligand but cannot convey a signal into the cell via protein phosphorylation. However it does form heterodimers with other EGF receptor family members which do have kinase activity. Heterodimerization leads to the activation of pathways which lead to cell proliferation or differentiation. Amplification of this gene and/or overexpression of its protein have been reported in numerous cancers including prostate, bladder and breast tumors. Alternate transcriptional splice variants encoding different isoforms have been characterized. Isoform 2 lacks the intermembrane region and is secreted outside the cell. This form acts to modulate the activity of the membrane-bound form. Additional splice variants have also been reported but they have not been thoroughly characterized. Defects in ERBB3 are the cause of lethal congenital contracture syndrome type 2 (LCCS2); also called Israeli Bedouin multiple contracture syndrome type A. LCCS2 is an autosomal recessive neurogenic form of a neonatally lethal arthrogryposis that is associated with atrophy of the anterior horn of the spinal cord.

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The brain-specific STEP (striatal enriched phosphatase) family of protein tyrosine phosphatases (PTPs) comprises both transmembrane and cytosolic protein members which are the products of alternative splicing. STEP family members are expressed in the dopaminoceptive neurons of the CNS, with highest expression in the basal ganglia and related structures. The STEP protein regulates the N-methyl-d-aspartate receptor (NMDAR) complex; STEP depresses both NMDAR single-channel activity and synaptic currents. The membrane-associated STEP61 isoform localizes in the postsynaptic densities (PSDs) of striatal neurons. STEP61 contains a single tyrosine phosphatase domain, two proline-rich domains and two transmembrane domains. The STEP61 protein associates with the Src family kinase member Fyn when Fyn is phosphorylated at Tyr-420 and not Tyr-431. Upon association, STEP61 dephosphorylates Tyr-420 residue and may thus regulate Fyn activity in PSDs. Isolated from mouse brain, the STEP20 isoform lacks the conserved tyrosine phosphatase domain. The human STEP gene maps to chromosome 11p15.2-p15.1.

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Protein kinases are enzymes that transfer a phosphate group from a phosphate donor onto an acceptor amino acid in a substrate protein. By this basic mechanism, protein kinases mediate most of the signal transduction in eukaryotic cells, regulating cellular metabolism, transcription, cell cycle progression, cytoskeletal rearrangement and cell movement, apoptosis, and differentiation. The protein kinase family is one of the largest families of proteins in eukaryotes, classified in 8 major groups based on sequence comparison of their tyrosine (PTK) or serine/threonine (STK) kinase catalytic domains. Epidermal Growth factor receptor (EGFR) is the prototype member of the type 1 receptor tyrosine kinases. EGFR overexpression in tumors indicates poor prognosis and is observed in tumors of the head and neck, brain, bladder, stomach, breast, lung, endometrium, cervix, vulva, ovary, esophagus, stomach and in squamous cell carcinoma.

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Component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the vertebrate brain. Functions also as histamine receptor and mediates cellular responses to histamine. Functions as receptor for diazepines and various anesthetics, such as pentobarbital; these are bound at a separate allosteric effector binding site. Functions as ligand-gated chloride channel (By similarity).

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ATG4A is a cysteine protease required for autophagy, which cleaves the C-terminal part of either MAP1LC3, GABARAPL2 or GABARAP, allowing the liberation of form I. A subpopulation of form I is subsequently converted to a smaller form (form II). Form II, with a revealed C-terminal glycine, is considered to be the phosphatidylethanolamine (PE)-conjugated form, and has the capacity for the binding to autophagosomes.

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NMDA receptor subtype of glutamate-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine. This protein plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. It mediates neuronal functions in glutamate neurotransmission. Is involved in the cell surface targeting of NMDA receptors (By similarity).

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Key transcriptional regulator of type I interferon (IFN)-dependent immune responses which plays a critical role in the innate immune response against DNA and RNA viruses. Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters. Acts as a more potent activator of the IFN-beta (IFNB) gene than the IFN-alpha (IFNA) gene and plays a critical role in both the early and late phases of the IFNA/B gene induction. Found in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, is phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization and association with CREB binding protein (CREBBP) to form dsRNA-activated factor 1 (DRAF1), a complex which activates the transcription of the type I IFN and ISG genes. Can activate distinct gene expression programs in macrophages and can induce significant apoptosis in primary macrophages.

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Regulator of sister chromatid cohesion in mitosis stabilizing cohesin complex association with chromatin. May antagonize the action of WAPAL which stimulates cohesin dissociation from chromatin. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. Required for efficient DNA double-stranded break repair.

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Necessary for sperm flagellar function. Plays a role in motile ciliogenesis. May help to recruit STK36 to the cilium or apical surface of the cell to initiate subsequent steps of construction of the central pair apparatus of motile cilia (By similarity).

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Functions as a dosage-dependent inducer in mitotic control. Tyrosine protein phosphatase required for progression of the cell cycle. When phosphorylated, highly effective in activating G2 cells into prophase. Directly dephosphorylates CDK1 and activates its kinase activity.

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MIB1 is a 1006 amino acid E3 ubiquitin ligase that activates the Notch ligand, Delta. MIB1 ubiquinates Delta by binding to its intracellular domain, leading to the endocytosis and eventual degradation of the Delta receptor, which, paradoxically, results in the up-regulation of receptor activity and enhances Notch signaling. MIB1 also interacts with DAPK, a protein that plays an important role in the regulation of apoptosis. Ubiquination of DAPK leads to inhibition of caspase-dependent apoptosis, therefore it is likely that overexpression of MIB1 can lead to tumor growth. Although it seems to be widely expressed at low levels, MIB1 is expressed at highest concentrations in the CNS and ovary. Both DAPK and MIB1 are overexpressed in epileptic brain tissue, suggesting that they probably cooperate as regulators of neuronal death in epilepsy.

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LGI4, also known as leucine-rich glioma-inactivated protein 4, is a 537 amino acid secreted glycosylated protein that is widely expressed, with highest levels found within the nervous system. Interestingly, siRNA knockdown studies of LGI4 expression in Schwann cells have been shown to result in the inhibition of myelination, thus suggesting that LGI4 is an essential component of myelin formation and axon segregation. LGI4 shares significant homology with its other family members, LGI1, LGI2 and LGI3. Significantly, mutations in the gene encoding LGI1 have been linked to human temporal lobe epilepsy and, given the sequence similarity of LGI4, it is likely that it also may be implicated in the pathology of seizures. LGI4 is localized subcellularly to the Golgi, ER and vesicles. There are two isoforms of LGI4 that are produced as a result of alternative splicing events.

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This gene encodes a member of the Ced-4 family of apoptosis proteins. Ced-family members contain a caspase recruitment domain (CARD) and are known to be key mediators of programmed cell death. The encoded protein contains a distinct N-terminal pyrin-like motif, which is possibly involved in protein-protein interactions. This protein interacts strongly with caspase 2 and weakly with caspase 9. Overexpression of this gene was demonstrated to induce apoptosis in cells. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found for this gene, but the biological validity of some variants has not been determined. [provided by RefSeq, Jul 2008].

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This gene is a member of the Ets family of transcription factors and of the ternary complex factor (TCF) subfamily. Proteins of the TCF subfamily form a ternary complex by binding to the the serum response factor and the serum response element in the promoter of the c-fos proto-oncogene. The protein encoded by this gene is a nuclear target for the ras-raf-MAPK signaling cascade. This gene produces multiple isoforms by using alternative translational start codons and by alternative splicing. Related pseudogenes have been identified on chromosomes 7 and 14. [provided by RefSeq, Mar 2012].