query: what protein does the hfe gene code for

pos: HFE (gene) HFE (gene) Human hemochromatosis protein also known as the HFE protein is a protein which in humans is encoded by the "HFE" gene. The "HFE" gene is located on short arm of chromosome 6 at location 6p21.3. Unusually, the official gene symbol ("HFE" for "H"igh Iron "Fe") is not an abbreviation of the official name (hemochromatosis). Protein encoded by this gene is a membrane protein that is similar to MHC class I-type proteins and associates with beta-2 microglobulin (beta2M). It is thought that this protein functions to regulate circulating iron uptake by regulating the interaction of the transferrin receptor with

pos: HFE (gene) HFE (gene) Human hemochromatosis protein also known as the HFE protein is a protein which in humans is encoded by the "HFE" gene. The "HFE" gene is located on short arm of chromosome 6 at location 6p21.3. Unusually, the official gene symbol ("HFE" for "H"igh Iron "Fe") is not an abbreviation of the official name (hemochromatosis). Protein encoded by this gene is a membrane protein that is similar to MHC class I-type proteins and associates with beta-2 microglobulin (beta2M). It is thought that this protein functions to regulate circulating iron uptake by regulating the interaction of the transferrin receptor with

pos: HFE (gene) "HFE" was well conserved across the species, numerous nucleotide differences were found between rhinoceros and human or mouse, some of which changed deduced amino acids. Only one allele, p.S88T in the black rhinoceros, was a candidate that might adversely affect HFE function. p.S88T occurs in a highly conserved region involved in the interaction of HFE and TfR1. HFE (gene) Human hemochromatosis protein also known as the HFE protein is a protein which in humans is encoded by the "HFE" gene. The "HFE" gene is located on short arm of chromosome 6 at location 6p21.3. Unusually, the official gene symbol ("HFE"

pos: HFE (gene) hemochromatosis phenotypes, often in compound heterozygosity with "HFE" C282Y. Other mutations are either synonymous or their effect on iron phenotypes, if any, has not been demonstrated. The HFE protein interacts with the transferrin receptor TFRC. Its primary mode of action is the regulation of the iron storage hormone hepcidin. It is possible to delete part or all of a gene of interest in mice (or other experimental animals) as a means of studying function of the gene and its protein. Such mice are called “knockouts” with respect to the deleted gene. "Hfe" is the mouse equivalent of the human hemochromatosis

pos: William S. Sly mouse models of several CA deficiencies. With collaborators, he identified other human diseases attributed to mutations in the genes encoding CA IV, CA VA, and CA XII. Dr. Sly has also done research on hereditary hemochromatosis, collaborating on studies leading to the cloning of the HFE gene and identification of the product it encodes. He also showed that the HFE gene knockout in the mouse produces iron storage resembling human hemochromatosis. Dr. Sly also contributed to resolution of a famous forensic case involving a “missing murder”. He and his colleague James Shoemaker provided evidence that a woman convicted for poisoning

neg: HFE (gene) gene "HFE". The protein encoded by "Hfe" is Hfe. Mice homozygous (two abnormal gene copies) for a targeted knockout of all six transcribed "Hfe" exons are designated "Hfe"−/−. Iron-related traits of "Hfe"−/− mice, including increased iron absorption and hepatic iron loading, are inherited in an autosomal recessive pattern. Thus, the "Hfe"−/− mouse model simulates important genetic and physiologic abnormalities of "HFE" hemochromatosis. Other knockout mice were created to delete the second and third "Hfe" exons (corresponding to α1 and α2 domains of Hfe). Mice homozygous for this deletion also had increased duodenal iron absorption, elevated plasma iron and transferrin saturation

neg: HFE (gene) transferrin. The "HFE" gene contains 7 exons spanning 12 kb. The full-length transcript represents 6 exons. HFE protein is composed of 343 amino acids. There are several components, in sequence: a signal peptide (initial part of the protein), an extracellular transferrin receptor-binding region (α1 and α2), a portion that resembles immunoglobulin molecules (α3), a transmembrane region that anchors the protein in the cell membrane, and a short cytoplasmic tail. HFE expression is subjected to alternative splicing. The predominant HFE full-length transcript has ~4.2 kb. Alternative HFE splicing variants may serve as iron regulatory mechanisms in specific cells or tissues. HFE

neg: HFE hereditary haemochromatosis a lesser role. The regulation of dietary iron absorption is complex and our understanding is incomplete. One of the better characterized genes responsible for hereditary haemochromatosis is HFE on chromosome 6, which codes for a protein that participates in the regulation of iron absorption. The HFE gene has two common mutations, C282Y and H63D. The C282Y allele is a transition point mutation from guanine to adenine at nucleotide 845 in the HFE gene, resulting in a missense mutation that replaces the cysteine residue at position 282 with a tyrosine amino acid. Heterozygotes for either allele do not manifest clinical iron

neg: HFE hereditary haemochromatosis disease. Penetrance differs between populations. Since the regulation of iron metabolism is still poorly understood, a clear model of how haemochromatosis operates is still not available. A working model describes the defect in the HFE gene, where a mutation puts the intestinal absorption of iron into overdrive. Normally, HFE facilitates the binding of transferrin, which is iron's carrier protein in the blood. Transferrin levels are typically elevated at times of iron depletion (low ferritin stimulates the release of transferrin from the liver). When transferrin is high, HFE works to increase the intestinal release of iron into the blood. When HFE

neg: Iron overload diagnosis of haemochromatosis in asymptomatic individuals with blood tests showing increased iron stores, or for predictive testing of individuals with a family history of haemochromatosis. The alleles evaluated by HFE gene analysis are evident in ~80% of patients with haemochromatosis; a negative report for HFE gene does not rule out haemochromatosis. First degree relatives of those with primary haemochromatosis should be screened to determine if they are a carrier or if they could develop the disease. This can allow preventive measures to be taken. Screening the general population is not recommended. Liver biopsy is the removal of small sample in

neg: HFE hereditary haemochromatosis greater than 62% is suggestive of homozygosity for mutations in the HFE gene. Serum Ferritin: Ferritin, a protein synthesized by the liver is the primary form of iron storage within cells and tissues. Measuring ferritin provides another crude estimate of whole body iron stores though many conditions, particularly inflammation (but also chronic alcohol consumption, non-alcoholic fatty liver disease and others), can elevate serum ferritin - which can account for up to 90% of cases where elevated levels are observed. Normal values for males are 12–300 ng/ml (nanograms per millilitre) and for female, 12–150 ng/ml. Serum ferritin in excess of 1000

neg: HFE (gene) levels, and iron overload, mainly in hepatocytes. Mice have also been created that are homozygous for a missense mutation in "Hfe" (C282Y). These mice correspond to persons with hemochromatosis who are homozygous for "HFE" C282Y. These mice develop iron loading that is less severe than that of "Hfe"−/− mice. Black rhinoceroses ("Diceros bicornis") develop iron overload. To determine whether the "HFE" gene of black rhinoceroses has undergone mutation as an adaptive mechanism to improve iron absorption from iron-poor diets, Beutler et al. sequenced the entire "HFE" coding region of four species of rhinoceros (two browsing and two grazing species). Although

neg: Iron overload on the HFE gene, and 1% having the condition. This has been recognised in several alternative names such as "Celtic curse", "Irish illness", "British gene", and "Scottish sickness". Although it was known most of the 20th century that most cases of haemochromatosis were inherited, they were incorrectly assumed to depend on a single gene. The overwhelming majority depend on mutations of the HFE gene discovered in 1996, but since then others have been discovered and sometimes are grouped together as "non-classical hereditary haemochromatosis", "non-HFE related hereditary haemochromatosis", or "non-HFE haemochromatosis". Most types of hereditary haemochromatosis have autosomal recessive inheritance, while

neg: Complementary DNA complements (T, A, C and G, respectively). To obtain eukaryotic cDNA whose introns have been removed: Complementary DNA is often used in gene cloning or as gene probes or in the creation of a cDNA library. When scientists transfer a gene from one cell into another cell in order to express the new genetic material as a protein in the recipient cell, the cDNA will be added to the recipient (rather than the entire gene), because the DNA for an entire gene may include DNA that does not code for the protein or that interrupts the coding sequence of the

neg: NLK NLK Serine/threonine protein kinase NLK is an enzyme that in humans is encoded by the "NLK" gene. Its name is an abbreviation for "Nemo-Like Kinase", Nemo (nmo) being the "Drosophila" ortholog of the mammalian NLK gene. This enzyme is a member of the Mitogen-activated protein kinase (MAPK) family, although not explicitly designated as such (it does not even have a numbered MAPK code). It is a highly divergent, atypical member of the MAPK group, lacking most features so characteristic of most mitogen-activated protein kinases (e.g. it does not have the dual phosphorylation motifs of typical MAPKs, and is not phosphorylated

neg: NLK by any known MAP2 kinases). Its activation mechanism and downstream targets are still not well characterized. NLK Serine/threonine protein kinase NLK is an enzyme that in humans is encoded by the "NLK" gene. Its name is an abbreviation for "Nemo-Like Kinase", Nemo (nmo) being the "Drosophila" ortholog of the mammalian NLK gene. This enzyme is a member of the Mitogen-activated protein kinase (MAPK) family, although not explicitly designated as such (it does not even have a numbered MAPK code). It is a highly divergent, atypical member of the MAPK group, lacking most features so characteristic of most mitogen-activated protein kinases

neg: Transferrin receptor 1 studies in the therapy of two incurable orphan oncohematological diseases: the adult T cell leukemia (ATLL) caused by HTLV-1 and the Mantle cell lymphoma (MCL). TfR1 has been shown to interact with GABARAP and HFE. Transferrin receptor 1 Transferrin receptor protein 1 (TfR1), also known as Cluster of Differentiation 71 (CD71), is a protein that in humans is encoded by the "TFRC" gene. TfR1 is required for iron import from transferrin into cells by endocytosis. TfR1 is a transmembrane glycoprotein composed of two disulfide-linked monomers joined by two disulfide bonds. Each monomer binds one holo-transferrin molecule creating an iron-Tf-TfR complex

neg: HFE hereditary haemochromatosis overload but may display an increased iron uptake. Mutations of the HFE gene account for 90% of the cases of non-transfusional iron overload. This gene is closely linked to the HLA-A3 locus. Homozygosity for the C282Y mutation is the most common genotype responsible for clinical iron accumulation, though heterozygosity for C282Y/H63D mutations, so-called compound heterozygotes, results in clinically evident iron overload. There is considerable debate regarding the penetrance—the probability of clinical expression of the trait given the genotype— for clinical disease in homozygotes. Most, if not all, males homozygous for HFE C282Y will show manifestations of liver dysfunction such as

neg: Iron overload of hemochromatosis following the discovery of the HFE gene which helped lead to the population screenings and estimates that are still being used today. Historically, the term "haemochromatosis" (spelled "hemochromatosis" in American English) was initially used to refer to what is now more specifically called haemochromatosis type 1 (or HFE-related hereditary haemochromatosis). Currently, haemochromatosis (without further specification) is mostly defined as iron overload with a hereditary or primary cause, or originating from a metabolic disorder. However, the term is currently also used more broadly to refer to any form of iron overload, thus requiring specification of the cause, for example,

neg: HFE hereditary haemochromatosis At that time when dietary iron may have been scarcer than today, the presence of the mutant allele may have provided an evolutionary or natural selection reproductive advantage by maintaining higher iron levels in the blood. The term "haemochromatosis" is used by different sources in many different ways. It is often used to imply an association with the HFE gene. For many years, HFE was the only known gene associated with haemochromatosis, and the term "hereditary haemochromatosis" was used to describe haemochromatosis type 1. However, it is now known that there are many different genetic associations with this condition. The

neg: Gene step, but are not translated into protein. The process of producing a biologically functional molecule of either RNA or protein is called gene expression, and the resulting molecule is called a gene product. The nucleotide sequence of a gene's DNA specifies the amino acid sequence of a protein through the genetic code. Sets of three nucleotides, known as codons, each correspond to a specific amino acid. The principle that three sequential bases of DNA code for each amino acid was demonstrated in 1961 using frameshift mutations in the rIIB gene of bacteriophage T4 (see Crick, Brenner et al. experiment). Additionally,

neg: Iron overload of the liver and had bronzed skin color. The term hemochromatosis was first used by German pathologist named Friedrich Daniel von Recklinghausen in 1890 when he introduced an accumulation of iron in body tissue. In 1935 J.H. Sheldon, a British physician, described the pathophysiology mechanism linked to iron metabolism for the first time. In 1996 Felder and colleagues identified the hemochromatosis gene, HFE gene. Felder found that the HFE gene has two main mutations, C282Y and H63D, which were the main cause of hereditary hemochromatosis. The next year the CDC and the National Human Genome Research Institute sponsored an examination

neg: Iron overload "hereditary haemochromatosis". Hereditary haemochromatosis is an autosomal recessive disorder with estimated prevalence in the population of 1 in 200 among patients with European ancestry, with lower incidence in other ethnic groups. The gene responsible for hereditary haemochromatosis (known as HFE gene) is located on chromosome 6; the majority of hereditary haemochromatosis patients have mutations in this HFE gene. Hereditary haemochromatosis is characterized by an accelerated rate of intestinal iron absorption and progressive iron deposition in various tissues. This typically begins to be expressed in the third to fifth decades of life, but may occur in children. The most common presentation

neg: Phage group Laboratory in Cambridge to perform genetic experiments that demonstrated the basic nature of the genetic code for proteins. These experiments, carried out with mutants of the rIIB gene of phage T4, showed, that for a gene that encodes a protein, three sequential bases of the gene’s DNA specify each successive amino acid of the protein. Thus the genetic code is a triplet code, where each triplet (called a codon) specifies a particular amino acid. They also obtained evidence that the codons do not overlap with each other in the DNA sequence encoding a protein, and that such a sequence is

neg: Sarcosine dehydrogenase mitochondria (See figure 4 for pathway). Even so, the biological significance of sarcosine dehydrogenase beyond sarcosine metabolism is not entirely known. In a study of hereditary hemochromatosis using both wild type and HFE (gene) deficient mice fed with 2 percent carbonyl iron supplemented diet, sarcosine dehydrogenase was shown to be down-regulated in HFE deficient mice, but role sarcosine dehydrogenase in iron metabolism is unknown from the experiment conducted. Sarcosinemia is an autosomal recessive disease caused by a mutation of the sarcosine dehydrogenase gene in the 9q33-q34 gene locus. This leads to a compromised sarcosine metabolism and causes the build-up of

neg: Point mutation GUG, which encodes the amino acid valine rather than glutamic acid. The protein may also exhibit a "gain of function" or become activated, such is the case with the mutation changing a valine to glutamic acid in the braf gene; this leads to an activation of the RAF protein which causes unlimited proliferative signalling in cancer cells. These are both examples of a non-conservative (missense) mutation. Silent mutations code for the same amino acid (a "synonymous substitution"). A silent mutation does not affect the functioning of the protein. A single nucleotide can change, but the new codon specifies the same

neg: Porphyria cutanea tarda is usually reduced by 50% in all tissues in people with the inherited form of the condition. Nongenetic factors such as alcohol abuse, excess iron, and others listed above can increase the demand for heme and the enzymes required to make heme. The combination of this increased demand and reduced activity of uroporphyrinogen decarboxylase disrupts heme production and allows byproducts of the process to accumulate in the body, triggering the signs and symptoms of porphyria cutanea tarda. The "HFE" gene makes a protein that helps cells regulate the absorption of iron from the digestive tract and into the cells of

neg: Beta-2 microglobulin I molecules, but also with class I-like molecules such as CD1 and Qa. An additional function is association with the HFE protein, together regulating the expression of hepcidin in the liver which targets the iron transporter ferroportin on the cytoplasmic membrane of enterocytes and macrophages for degradation resulting in increased iron uptake from food and decreased iron release from recycled red blood cells in the MPS (mononuclear phagocyte system) respectively. Loss of this function causes iron excess and hemochromatosis. Mice models deficient for the β microglobulin gene have been engineered. These mice demonstrate that β microglobulin is necessary for cell

neg: Suppressor mutation deleted triplet does not disturb the reading frame and the genetic code is in fact a triplet. Intergenic (also known as extragenic) suppression relieves the effects of a mutation in one gene by a mutation somewhere else within the genome. The second mutation is not on the same gene as the original mutation. Intergenic suppression is useful for identifying and studying interactions between molecules, such as proteins. For example, a mutation which disrupts the complementary interaction between protein molecules may be compensated for by a second mutation elsewhere in the genome that restores or provides a suitable alternative interaction between

neg: Gene expression profiling that the experimental treatment regulates cholesterol, because the treatment seems to selectively regulate genes associated with cholesterol. While this may be true, there are a number of reasons why making this a firm conclusion based on enrichment alone represents an unwarranted leap of faith. One previously mentioned issue has to do with the observation that gene regulation may have no direct impact on protein regulation: even if the proteins coded for by these genes do nothing other than make cholesterol, showing that their mRNA is altered does not directly tell us what is happening at the protein level. It is

neg: Transmembrane protein 134 The gene does have three isoforms; a, b, and c. The protein is encoded by TMEM134 gene and is 195 amino acids in length. The protein contains two transmembrane domains but does not contain a signal peptide. This suggests that there is an internal signal peptide upstream of the translated portion of the protein. The protein is overall considering normal with its amino acid content but does have two regions of high hydrophobicity, which occur during the transmembrane regions of the protein. This gives the protein an isoelectric point of 6.08. The overall weight of the protein is 21.6 kilodaltons,

neg: DSCR1 DSCR1 Down syndrome critical region gene 1, also known as DSCR1, is a protein that in humans is encoded by the "DSCR1" gene. RCAN1 is a gene that in humans encodes the protein DSCR1. DSCR1 in human is located at the centromeric border of the DSCR and encodes an inhibitor of calcineurin/ NFAT (nuclear factor activated T cells) signalling. DSCR1 genomic sequence of total 45 kb contain 7 exons and 6 introns , different cDNA analysis yield first four exons are alternative and code for two isoforms of 197 amino acids, and one isoform code for 171 amino acids which

neg: PAK5 four exons are for 5’-UTR and remaining 8 exons for protein coding(Gene from review). Alternative exon splicing of the PAK5 gene generates three transcripts, and one of the transcript encodes a 719 amino acids long protein(Gene from review). The exon splicing of the murine PAK5 gene generates three transcripts, two of which code an identical 719 amino acids long polypeptide while the 2.0-kb transcript is a non-coding RNA with retained intron. Similar to PAK4, PAK5 consists of a kinase, a CDC42/Rac1 interactive binding (CRIB) motif. The protein encoded by this gene is a member of the PAK family of Ser/Thr

neg: HES1 HES1 Transcription factor HES1 (hairy and enhancer of split-1) is a protein that is encoded by the "Hes1" gene, and is the mammalian homolog of the hairy gene in "Drosophila." HES1 is one of the seven members of the Hes gene family (HES1-7). Hes genes code nuclear proteins that suppress transcription. This protein belongs to the basic helix-loop-helix (bHLH) family of transcription factors. It is a transcriptional repressor of genes that require a bHLH protein for their transcription. The protein has a particular type of basic domain that contains a helix interrupting protein that binds to the N-box promoter region

neg: Structural gene Structural gene A structural gene is a gene that codes for any RNA or protein product other than a regulatory factor (i.e. regulatory protein). A term derived from the "lac" operon, structural genes are typically viewed as those containing sequences of DNA corresponding to the amino acids of a protein that will be produced, as long as said protein does not function to regulate gene expression. Structural gene products include enzymes and structural proteins. Also encoded by structural genes are non-coding RNAs, such as rRNAs and tRNAs (but excluding any regulatory miRNAs and siRNAs). In prokaryotes, structural genes of related

neg: EGFL7 EGFL7 EGF-like domain-containing protein 7 is a protein that in humans is encoded by the "EGFL7" gene. Intron 7 of EGFL7 hosts the miR-126 microRNA gene. Epidermal Growth Factor like domain 7 (Egfl7) also known as Vascular Endothelial-statin (VE-statin) codes for a gene mostly expressed in endothelial cells. The "egfl7" gene is located on chromosomes 9 and 2 in human and mouse, respectively, and is structured in 11 exons and introns, including intron-1a and 1b which are alternatively transcribed from two different promoters. These transcripts vary only in the first exon and code for the same protein which is initiated

neg: C19orf44 (gene) found to interact with various proteins from the two-hybrid screening method. Interactions with Hsp90 co-chaperone (CDC37), and spermatid associated protein (SPERT) have been found. C19orf44 (gene) Chromosome 19 open reading frame 44 is a protein that in humans is encoded by the C19orf44 gene. The entire gene is 25,416 base pairs in length, and has an unprocessed mRNA that is 3,446 nucleotides in length. It contains 10 exons that code for a 657 amino acid protein. There are 7 splice variants that exist for C19orf44. C19orf44 is located on the nineteenth chromosome on 19p13.11. C19orf44 has a molecular weight of

neg: BACH1 and transcription is repressed. Multiple alternatively spliced transcript variants have been identified for this gene. Some exons of this gene overlap with some exons from the C21orf41 gene, which is transcribed in an opposite orientation to this gene but does not seem to encode a protein. BACH1 Transcription regulator protein BACH1 is a protein that in humans is encoded by the "BACH1" gene. This gene encodes a transcription factor that belongs to the cap'n'collar type of basic region leucine zipper factor family (CNC-bZip). The encoded protein contains broad complex, tramtrack, bric-a-brac/poxvirus and zinc finger (BTB/POZ) domains, which is atypical of

neg: Zinc finger protein 804A Zinc finger protein 804A Zinc finger protein 804A is a protein that in humans is encoded by the "ZNF804A" gene. The human gene maps to chromosome 2 q32.1 and consists of 4 exons that code for a protein of 1210 amino acids (137 kDa). Little is known about the characteristics and function of the encoded protein. However, the protein sequence codes for a domain characteristic of a classical CH-type zinc finger near the N-terminal end. ZNF804A binds to the N-terminus of ATXN1. The tertiary structure of the CH finger consists of a beta hairpin folded against an alpha helix. The

neg: Hydrofluoroether the EPA does not regulate its use due to its short atmospheric lifetime and zero ozone depletion potential compared to alternative chemicals. Industrial uses are many and varied: Although 3M first developed HFEs, other manufacturers have begun producing them. Hydrofluoroether A Hydrofluoroether (HFE) is a complex organic solvent. As a non-ozone-depleting chemical, it was developed originally as a replacement for CFCs, HFCs, HCFCs, and PFCs HFE does not occur naturally. It is colorless, odorless, tasteless, low toxicity, low viscosity, and liquid at room temperature. It is visually indistinguishable from water at room temperature. The vapor-point of HFE varies by chemistry

neg: Alternatives to evolution by natural selection 1969 paper by Jack Lester King and Thomas H. Jukes, provocatively but misleadingly titled "Non-Darwinian Evolution". It provided a wide variety of evidence including protein sequence comparisons, studies of the Treffers mutator gene in "E. coli", analysis of the genetic code, and comparative immunology, to argue that most protein evolution is due to neutral mutations and genetic drift. According to Kimura, the theory applies only for evolution at the molecular level, while phenotypic evolution is controlled by natural selection, so the neutral theory does not constitute a true alternative. The various alternatives to Darwinian evolution by natural selection were not

neg: Equalization payments sources and operated at the same level of efficiency. Currently the funds distributed to achieve HFE are the revenues raised from the Goods and Services Tax (GST), currently about AUD 50 bn a year. The distribution of GST required to achieve HFE is decided by the Federal Treasurer each year, on the basis of advice provided by the Commonwealth Grants Commission (CGC). Achieving HFE does not mean that the states are directed how to raise revenue or how to spend their funds. GST revenue grants from the Commonwealth are unencumbered and available for any purpose. Accordingly, HFE equalises fiscal capacity,

neg: HES1 syndrome, a hallmark of which is mutations in "Jagged1". Therefore, Hes-Notch interactions also play a role in digestive organ development. HES1 Transcription factor HES1 (hairy and enhancer of split-1) is a protein that is encoded by the "Hes1" gene, and is the mammalian homolog of the hairy gene in "Drosophila." HES1 is one of the seven members of the Hes gene family (HES1-7). Hes genes code nuclear proteins that suppress transcription. This protein belongs to the basic helix-loop-helix (bHLH) family of transcription factors. It is a transcriptional repressor of genes that require a bHLH protein for their transcription. The protein

neg: SH3BGRL3 SH3BGRL3 SH3 domain-binding glutamic acid-rich-like protein 3 is a protein that in humans is encoded by the "SH3BGRL3" gene. The 10.5kDa protein SH3 binding glutamic acid-rich protein-like 3 has an isoelectric point of 5.0. SH3 binding glutamic acid-rich (SH3BGR) gene is located to human chromosome 21. Two homologous genes, SH3BGRL and SH3BGRL3 are located to chromosome Xq13.3 and 1p34.3-35, respectively and code for small proteins similar to the N-terminal region of the SH3BGR protein. SH3BGRL3 protein shows a significant similarity to glutaredoxin 1 of "E. coli", and all the three proteins are predicted to belong to thioredoxin-like protein family. Glutaredoxins

neg: Regulator gene of RNA, as in the case of genes encoding microRNAs. An example of a regulator gene is a gene that codes for a repressor protein that inhibits the activity of an operator gene (a gene which binds repressor proteins thus inhibiting the translation of RNA to protein via RNA polymerase). In prokaryotes, regulator genes often code for repressor proteins. Repressor proteins bind to operators or promoters, preventing RNA polymerase from transcribing RNA. They are usually constantly expressed so the cell always has a supply of repressor molecules on hand. Inducers cause repressor proteins to change shape or otherwise become unable

neg: HFE (gene) North American non-Hispanic whites are 6-7%. C282Y exists as a polymorphism only in Western European white and derivative populations, although C282Y may have arisen independently in non-whites outside Europe. "HFE" H63D is cosmopolitan but occurs with greatest frequency in whites of European descent. Allele frequencies of H63D in ethnically diverse western European populations are 10-29%. and in North American non-Hispanic whites are 14-15%. At least 42 mutations involving "HFE" introns and exons have been discovered, most of them in persons with hemochromatosis or their family members. Most of these mutations are rare. Many of the mutations cause or probably cause

neg: HFE (gene) is prominent in small intestinal absorptive cells, gastric epithelial cells, tissue macrophages, and blood monocytes and granulocytes, and the syncytiotrophoblast, an iron transport tissue in the placenta. The iron storage disorder hereditary hemochromatosis (HHC) is an autosomal recessive genetic disorder that usually results from defects in this gene. The mutation or polymorphism most commonly associated with hemochromatosis is p. C282Y. About 1/200 of people of Northern European origin have two copies of this variant; they, particularly males, are at high risk of developing hemochromatosis. Allele frequencies of "HFE" C282Y in ethnically diverse western European white populations are 5-14% and in

neg: Cotesia congregata range in size from 5,000 to 40,000 base pairs. Of the 30, 29 circles code for at least one protein product. The genome is composed of 66% A-T residues. The top gene products are: The rest of the protein products have no known homologs and their function is not known. Much of what has been discovered makes it difficult to place the virus in a phylogenetic niche, and lends support to the theory that the virus was assembled, rather than evolved. The most closely related viruses are the nudiviruses and their baculovirus relatives, although this relatedness goes back approximately 75

neg: Bromodomain-containing protein 3 Bromodomain-containing protein 3 Bromodomain-containing protein 3 (BRD3) also known as RING3-like protein (RING3L) is a protein that in humans is encoded by the BRD3 gene. This gene was identified based on its homology to the gene encoding the RING3 (BRD2) protein, a serine/threonine kinase. The gene localizes to 9q34, a region which contains several major histocompatibility complex (MHC) genes. BRD3 is a member of the Bromodomain and Extra-Terminal motif (BET) protein family. Like other BET family members it contains two tandem homologous bromodomains and an "Extra-Terminal" motif. BRD3, similar to BRD2, does not have a long C-terminal domain as BET

neg: Gene expression profiling which protein each gene product makes and what function this protein performs. Gene annotation provides functional and other information, for example the location of each gene within a particular chromosome. Some functional annotations are more reliable than others; some are absent. Gene annotation databases change regularly, and various databases refer to the same protein by different names, reflecting a changing understanding of protein function. Use of standardized gene nomenclature helps address the naming aspect of the problem, but exact matching of transcripts to genes remains an important consideration. Having identified some set of regulated genes, the next step in expression

neg: Inclusion bodies a recombinant gene in a prokaryote risks the formation of the inactive aggregates of protein known as inclusion bodies. While the cDNA may properly code for a translatable mRNA, the protein that results will emerge in a foreign microenvironment. This often has fatal effects, especially if the intent of cloning is to produce a biologically active protein. For example, eukaryotic systems for carbohydrate modification and membrane transport are not found in prokaryotes. The internal microenvironment of a prokaryotic cell (pH, osmolarity) may differ from that of the original source of the gene. Mechanisms for folding a protein may also be

neg: DSCR1 of RCAN1 expression by H2O2 increases of the half-life of the protein. DSCR1 Down syndrome critical region gene 1, also known as DSCR1, is a protein that in humans is encoded by the "DSCR1" gene. RCAN1 is a gene that in humans encodes the protein DSCR1. DSCR1 in human is located at the centromeric border of the DSCR and encodes an inhibitor of calcineurin/ NFAT (nuclear factor activated T cells) signalling. DSCR1 genomic sequence of total 45 kb contain 7 exons and 6 introns , different cDNA analysis yield first four exons are alternative and code for two isoforms of

neg: GADV-protein world hypothesis GNC-SNS primitive gene code hypothesis (GNC hypothesis) also formulated by him. In the GNC hypothesis, the origin of the present standard genetic code is considered to be the GNC genetic code that includes the codons GGC, GCC, GAC, GUC, respectively coding glycine, alanine, aspartic acid, and valine; it also follows the SNS primitive genetic code that codes ten amino acids, where N denotes arbitrary four RNA bases and S denotes guanine (G) and cytosine (C). The GADV hypothesis proposes these mechanisms: GADV-protein world hypothesis GADV-protein world is a hypothetical stage of abiogenesis. GADV stands for the one letter codes of

neg: C19orf44 (gene) C19orf44 (gene) Chromosome 19 open reading frame 44 is a protein that in humans is encoded by the C19orf44 gene. The entire gene is 25,416 base pairs in length, and has an unprocessed mRNA that is 3,446 nucleotides in length. It contains 10 exons that code for a 657 amino acid protein. There are 7 splice variants that exist for C19orf44. C19orf44 is located on the nineteenth chromosome on 19p13.11. C19orf44 has a molecular weight of 71,343 Da, and an isoelectric point of 5.52. The amino acid sequence for C19orf44 was found to be serine rich using tools on EMBL-EBI.

neg: Protein isoform the protein level can manifest in the deletion of whole domains or shorter loops, usually located on the surface of the protein. One single gene has the ability to produce multiple proteins that differ both in structure and composition; this process is regulated by the alternative splicing of mRNA, though it is not clear to what extent such a process affects the diversity of the human proteome, as the abundance of mRNA transcript isoforms does not necessarily correlate with the abundance of protein isoforms. The specificity of translated isoforms is derived by the protein's structure/function, as well as the cell

neg: Artificial gene synthesis these genes offers a means to improve gene expression in many cases. Rewriting the open reading frame is possible because of the degeneracy of the genetic code. Thus it is possible to change up to about a third of the nucleotides in an open reading frame and still produce the same protein. The available number of alternate designs possible for a given protein is astronomical. For a typical protein sequence of 300 amino acids there are over 10 codon combinations that will encode an identical protein. Using optimization methods such as replacing rarely used codons with more common codons sometimes

neg: SCN1A (gene) families which code for the voltage-gated sodium transmembrane proteins Na1.1. Within the family of genes which code for other portions of voltage-gated sodium channels, the SCN1A mutations were the first identified, since mutations to this gene caused epilepsy and febrile seizures. Indeed, the SCN1A gene is one of the most commonly mutated genes in the human genome associated with epilepsy, which has given it the title of a ‘super culprit gene’. There are 900 distinct mutations reported for the SCN1A gene, approximately half of the reported mutations are truncations which result in no protein. The remaining half of mutations are

neg: ANP32C PP32 and the protein encoded by this gene. This gene does not contain introns. ANP32C Acidic leucine-rich nuclear phosphoprotein 32 family member C is a protein that in humans is encoded by the "ANP32C" gene. Phosphoprotein 32 (PP32) is a tumor suppressor that can inhibit several types of cancers, including prostate and breast cancers. The protein encoded by this gene is one of at least two proteins that are similar in amino acid sequence to PP32 and are part of the same acidic nuclear phosphoprotein gene family. However, unlike PP32, the encoded protein is tumorigenic. The tumor suppressor function of

neg: DMC1 (gene) the absence of Rad51 strand exchange activity, Dmc1 appears to be able to repair all meiotic DNA breaks, and this absence does not affect meiotic crossing over rates. DMC1 (gene) Meiotic recombination protein DMC1/LIM15 homolog is a protein that in humans is encoded by the "DMC1" gene. Meiotic recombination protein Dmc1 is a homolog of the bacterial strand exchange protein RecA. Dmc1 plays the central role in homologous recombination in meiosis by assembling at the sites of programmed DNA double strand breaks and carrying out a search for allelic DNA sequences located on homologous chromatids. The name "Dmc" stands for

neg: C17orf98 C17orf98 C17orf98 is a protein which in humans is coded by the gene c17orf98. The protein is derived from "Homo sapiens" chromosome 17. The C17orf98 gene consists of a 6,302 base sequence. Its mRNA has three exons and no alternative splice sites. The protein has 154 amino acids, with no abnormal amino acid levels. C17orf98 has a domain of unknown function (DUF4542) and is 17.6kDa in weight. C17orf98 does not belong to any other families nor does it have any isoforms. The protein has orthologs with high percent similarity in mammals and reptiles. The protein has additional distantly related orthologs

neg: PAK6 protein coding RNAs to code four proteins of 681 and 636 amino acids while remaining PAK6 transcripts are non-coding RNAs. There are five transcripts in murine PAK6 gene, of which two transcripts are protein coding and other two non-coding RNAs(Gene from review). Following the general structural organization of the group II PAKs, PAK6 also contains a kinase, and a GTPase interacting domain. This gene encodes a protein that shares a high degree of sequence similarity with p21-activated kinase (PAK) family members. The proteins of this family are Rac/Cdc42-associated Ste20-like Ser/Thr protein kinases, characterized by a highly conserved amino-terminal Cdc42/Rac interactive

neg: ASPM (gene) sometime in the last 15000 years, and it seems to have swept through much of the European and Middle-Eastern population. Although the new allele is evidently beneficial, researchers do not know what it does. The mouse gene, "Aspm", is expressed in the primary sites of prenatal cerebral cortical neurogenesis. The difference between "Aspm" and ASPM is a single, large insertion coding for so-called IQ domains. Studies in mice also suggest a role of the expressed Aspm gene product in mitotic spindle regulation. The function is conserved, the "C. elegans" protein ASPM-1 was shown to be localized to spindle asters, where

neg: Gap gene thus defines the anterior boundary of the knirps gene. Due to more efficient inhibition of the knirps gene by hunchback, knirps is expressed more posterially in the embryo compared to Krüppel. Tailless protein inhibits knirps gene expression in the posterior part of the embryo, allowing the knirps protein to be expressed only in the central part of the embryo (but more posterior compared to Krüppel). This is due to the ability of both hunchback and tailless to bind to the enhancer regions of knirps. The gap genes code for transcription factors that regulate the expression of pair-rule genes and homeotic

neg: Trans-acting the intermediary protein or RNA that it encodes. Cis-acting elements, on the other hand, do not code for protein or RNA. Both the trans-acting gene and the protein/RNA that it encodes are said to "act in trans" on the target gene. Trans-acting In the field of molecular biology, trans-acting (trans-regulatory, trans-regulation), in general, means "acting from a different molecule" ("i.e.", intermolecular). It may be considered the opposite of cis-acting (cis-regulatory, cis-regulation), which, in general, means "acting from the same molecule" ("i.e.", intramolecular). In the context of transcription regulation, a trans-acting element is usually a DNA sequence that contains a gene.

neg: DNMT3L DNMT3L DNA (cytosine-5)-methyltransferase 3-like is an enzyme that in humans is encoded by the "DNMT3L" gene. CpG methylation is an epigenetic modification that is important for embryonic development, imprinting, and X-chromosome inactivation. Studies in mice have demonstrated that DNA methylation is required for mammalian development. This gene encodes a nuclear protein with similarity to DNA methyltransferases. This protein is not thought to function as a DNA methyltransferase as it does not contain the amino acid residues necessary for methyltransferase activity. However, this protein does stimulate de novo methylation by DNA cytosine methyltransferase 3 alpha and it is thought to be

neg: Penetrance as well as genetic cofactors and epigenetic regulation of expression: A consensus definition of what constitutes the presence of a phenotype is essential for determining the penetrance of an allele. For hereditary hemochromatosis, a disease caused by excess intestinal iron absorption, the degree of penetrance has been a subject of controversy for many years and illustrates the challenges facing investigators seeking a quantitative measure of penetrance. Individuals who are homozygotes for the C282Y allele of the HFE gene are at risk for developing lethal concentrations of iron, particularly in the liver. Typically patients develop clinical disease in late-middle age. Determining

neg: Gene expression profiling with a disease, and relationships with drugs or toxins. The Molecular Signatures Database and the Comparative Toxicogenomics Database are examples of resources to categorize genes in numerous ways. Regulated genes are categorized in terms of what they are and what they do, important relationships between genes may emerge. For example, we might see evidence that a certain gene creates a protein to make an enzyme that activates a protein to turn on a second gene on our list. This second gene may be a transcription factor that regulates yet another gene from our list. Observing these links we may begin

neg: CRYM CRYM Mu-crystallin homolog also known as NADP-regulated thyroid-hormone-binding protein (THBP) is a protein that in humans is encoded by the "CRYM" gene. Multiple alternatively spliced transcript variants have been found for this gene. Crystallins are separated into two classes: taxon-specific and ubiquitous. The former class is also called phylogenetically-restricted crystallins. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. This gene encodes a taxon-specific crystallin protein that binds NADPH and has sequence similarity to bacterial ornithine cyclodeaminases. The encoded protein does not perform a structural role in lens

neg: Point accepted mutation a gene, an exon, then this will change the codon specifying a particular amino acid in the protein produced by that gene. Despite the redundancy in the genetic code, there is a possibility that this mutation will then change the amino acid that is produced during translation, and as a consequence the structure of the protein will be changed. The functionality of a protein is highly dependent on its structure. Changing a single amino acid in a protein may reduce its ability to carry out this function, or the mutation may even change the function that the protein carries out.

neg: Hydrofluoroether Hydrofluoroether A Hydrofluoroether (HFE) is a complex organic solvent. As a non-ozone-depleting chemical, it was developed originally as a replacement for CFCs, HFCs, HCFCs, and PFCs HFE does not occur naturally. It is colorless, odorless, tasteless, low toxicity, low viscosity, and liquid at room temperature. It is visually indistinguishable from water at room temperature. The vapor-point of HFE varies by chemistry from 50C to nearly 100C. Due to its high molecular weight, it remains in the atmosphere for less than two weeks, being absorbed into the ground rather than remaining dissolved in the atmosphere. Although it is a greenhouse gas,

neg: PTEN (gene) have identified more than 70 mutations in the "PTEN" gene in people with Cowden syndrome. These mutations can be changes in a small number of base pairs or, in some cases, deletions of a large number of base pairs. Most of these mutations cause the "PTEN" gene to make a protein that does not function properly or does not work at all. The defective protein is unable to stop cell division or signal abnormal cells to die, which can lead to tumor growth, particularly in the breast, thyroid, or uterus. Mutations in the "PTEN" gene cause several other disorders that,

neg: Angiopoietin-related protein 1 mitogen in vitro. Angiopoietin-related protein 1 Angiopoietin-related protein 1 also known as angiopoietin-3 (ANG-3) is a protein that in humans is encoded by the ANGPTL1 gene. Angiopoietins are members of the vascular endothelial growth factor family and the only known growth factors largely specific for vascular endothelium. Angiopoietin-1, angiopoietin-2, and angiopoietin-4 participate in the formation of blood vessels. The protein encoded by this gene is another member of the angiopoietin family that is widely expressed in adult tissues with mRNA levels highest in highly vascularized tissues. This protein was found to be a secretory protein that does not act as

neg: Angiopoietin-related protein 1 Angiopoietin-related protein 1 Angiopoietin-related protein 1 also known as angiopoietin-3 (ANG-3) is a protein that in humans is encoded by the ANGPTL1 gene. Angiopoietins are members of the vascular endothelial growth factor family and the only known growth factors largely specific for vascular endothelium. Angiopoietin-1, angiopoietin-2, and angiopoietin-4 participate in the formation of blood vessels. The protein encoded by this gene is another member of the angiopoietin family that is widely expressed in adult tissues with mRNA levels highest in highly vascularized tissues. This protein was found to be a secretory protein that does not act as an endothelial cell

neg: Visna-maedi virus a similar manner as the HIV Rev protein. Rev binds as a multimer to the Rev Response Element (RRE) which has a stem-loop secondary structure. The function of the auxiliary gene "vif" is not fully known. The "vif" gene product, a 29 kDa protein, induces a weak immune response in animals. Deletion experiments have demonstrated that the "vif" gene is essential for infectivity. Though it does not produce severe immunodeficiency, visna shares many characteristics with human immunodeficiency virus, including the establishment of persistent infection with chronic active lymphoproliferation; however, visna virus does not infect T-lymphocytes. The relationship of visna and

neg: Non-Darwinian Evolution (paper) Non-Darwinian Evolution (paper) "Non-Darwinian Evolution" is a scientific paper written by Jack Lester King and Thomas H. Jukes and published in 1969. It is credited, along with Motoo Kimura's 1968 paper "Evolutionary Rate at the Molecular Level", with proposing what became known as the neutral theory of molecular evolution. The paper brings together a wide variety of evidence, ranging from protein sequence comparisons to studies of the Treffers mutator gene in "E. coli" to analysis of the genetic code to comparative immunology, to argue that most protein evolution is due to neutral mutations and genetic drift. It was published in

neg: Laurence H. Kedes spanned over four decades. Among his scientific achievements was the first isolation of a protein-coding gene from an animal cell, and he was the first to determine the DNA sequence of a protein coding animal gene. His initial research focused on understanding the chromosomal arrangement, sequences, and regulation of the multi-gene family encoding histone proteins, which later proved to play a central role in controlling overall gene expression, including the formation of eu- and heterochromatin (see "histone code"). The second phase of his research delved into the study of the regulation of actin genes, another multi-gene family. During this period,

neg: HEXA levels and removed the toxic cell buildup by using a non-replicated Herpes simplex vector to code for the missing gene. [10] HEXA Hexosaminidase A (alpha polypeptide), also known as HEXA, is an enzyme that in humans is encoded by the "HEXA" gene, located on the 15th chromosome. Hexosaminidase A and the cofactor G activator protein catalyze the degradation of the G gangliosides and other molecules containing terminal N-acetyl hexosamines. Hexosaminidase A is a heterodimer composed of an alpha subunit (this protein) and a beta subunit. The alpha subunit polypeptide is encoded by the "HEXA" gene while the beta subunit is

neg: H3K4me3 of the least abundant histone modifications; however, it is highly enriched at active promoters near transcription start sites (TSS) and positively correlated with transcription. H3K4me3 is used as a histone code or histone mark in epigenetic studies (usually identified through chromatin immunoprecipitation) to identify active gene promoters. H3K4me3 promotes gene activation through the action of the NURF complex, a protein complex that acts through the PHD finger protein motif to remodel chromatin. This makes the DNA in the chromatin accessible for transcription factors, allowing the genes to be transcribed and expressed in the cell. Regulation of gene expression through H3K4me3

neg: STK35L1 endothelial cells. STK35L1 STK35L1 is a protein that in humans is encoded by the STK35 (serine/threonine kinase 35) gene. It is a member of the NKF4 (New Kinase Family 4) Ser/Thr kinases (STK) family and classified in group "Other" in the human kinome. Previously, STK35L1 was named as Clik1 (CLP36 Interacting Kinase 1) based on a study that showed an association of STK35 with CLP36 after overexpression of both proteins in osteosarcoma cells. Clik1 gene described by Vallenius "et al." code for a protein of 501 amino acids. Later, Goyal "et al." found that coding sequence of the STK35 gene

neg: STK35L1 STK35L1 STK35L1 is a protein that in humans is encoded by the STK35 (serine/threonine kinase 35) gene. It is a member of the NKF4 (New Kinase Family 4) Ser/Thr kinases (STK) family and classified in group "Other" in the human kinome. Previously, STK35L1 was named as Clik1 (CLP36 Interacting Kinase 1) based on a study that showed an association of STK35 with CLP36 after overexpression of both proteins in osteosarcoma cells. Clik1 gene described by Vallenius "et al." code for a protein of 501 amino acids. Later, Goyal "et al." found that coding sequence of the STK35 gene is incomplete.

neg: LACTB LACTB Serine beta-lactamase-like protein LACTB, mitochondrial is an enzyme that in humans is encoded by the "LACTB" gene. This gene encodes a 54 kDa protein sharing significant sequence similarity to serine proteases of the penicillin binding protein and beta-lactamase superfamily occurring in bacteria. The "LACTB" gene is located at chromosome 15q22.1, consisting of 8 exons. Alternative splicing results in multiple transcript variants encoding different protein isoforms. LACTB shares sequence similarity to the beta-lactamase/penicillin-binding protein family of serine proteases that are involved in bacterial cell wall metabolism. The N-terminal 97 amino acid segment of LACTB does not form part of the

neg: ATF4 eIF2-TC, which means the ribosome does not acquire one in time to translate uORF2. Instead "ATF4" is translated. ATF4 Activating transcription factor 4 (tax-responsive enhancer element B67), also known as ATF4, is a protein that in humans is encoded by the "ATF4" gene. This gene encodes a transcription factor that was originally identified as a widely expressed mammalian DNA binding protein that could bind a tax-responsive enhancer element in the LTR of HTLV-1. The encoded protein was also isolated and characterized as the cAMP-response element binding protein 2 (CREB-2). The protein encoded by this gene belongs to a family of

neg: Human mortality from H5N1 is characterized by a single amino acid change at position 92. By changing the amino acid from glutamic acid to aspartic acid, researchers were able to abrogate the effect of the H5N1 NS1. This single amino acid change in the NS1 gene greatly increased the pathogenicity of the H5N1 influenza virus. This is one genetic factor in why H5N1 is so deadly. Polymerase encoding gene segments are also implicated in why H5N1 is so deadly. PA genes code for the PA protein, which is a critical component of the viral polymerase. The PB1 gene codes for the PB1 protein and

neg: WormBase the 3-letter species code prepended, like Cre-acl-5, Cbr-acl-5, Cbn-acl-5. A gene can be a Pseudogene, or can express one or more non-coding RNA genes (ncRNA) or protein-coding sequences (CDS). Pseudogenes are genes that do not produce a reasonable, functional transcript. They may be pseudogenes of coding genes or of non-coding RNA and may be whole or fragments of a gene and may or may not express a transcript. The boundary between what is considered a "reasonable" coding transcript is sometimes subjective as, in the absence of other evidence, the use of weak splice sites or short exons can often produce

neg: TMEM106A TMEM106A TMEM106A is a gene that encodes the transmembrane protein 106A (TMEM106A) in "Homo sapiens". It is located at 17q21.31 on the plus strand next to cancer-related genes "NBR1" and "BRCA1". The "TMEM106A" gene contains a domain of unknown function, DUF1356. The TMEM106A protein has a molecular weight of 28.9 kdal. It has 262 amino acids, 240 of which are in the domain of function. The protein has a transmembrane region. There is evidence for a secondary transmembrane region in humans but this region is not conserved in related orthologs. The protein does not contain a peptide signal protein. The

neg: Chronic myelogenous leukemia fused with the ABL gene on chromosome 9. This abnormal "fusion" gene generates a protein of p210 or sometimes p185 weight (p210 is short for 210 kDa protein, a shorthand used for characterizing proteins based solely on size). Because abl carries a domain that can add phosphate groups to tyrosine residues (a tyrosine kinase), the "bcr-abl" fusion gene product is also a tyrosine kinase. The fused BCR-ABL protein interacts with the interleukin 3beta(c) receptor subunit. The BCR-ABL transcript is continuously active and does not require activation by other cellular messaging proteins. In turn, BCR-ABL activates a cascade of proteins that

neg: PAK1 neurological disorders. The human PAK1 gene is 153-kb long and consists of 23 exons, six exons for 5’-UTR and 17 exons for protein coding (Gene from review). Alternative splicing of six exons generates 20 transcripts from 308-bp to 3.7-kb long; however, only 12 spliced transcripts have open reading frames and are predicted to code ten proteins and two polypeptides. The remaining 8 transcripts range are for non-coding long RNAs from 308-bp to 863-bp long. Unlike the human PAK1, murine PAK1 gene generates five transcripts: three protein-coding from 508-bp to 3.0-kb long, and two transcripts of about 900-bp for non-coding RNAs.

neg: Gene desert the genome should play a role in protecting, regulating, or repairing the protein coding regions that determine the functions of life. Although there is still much to learn about the nooks and crannies of the immense (yet limited) human genome, with the aid of various new technologies and the synthesis of the full human genome, we may perhaps unravel a great collection of secrets in the approaching years about the marvels of our genetic code. Gene desert Gene deserts are regions of the genome that are devoid of protein-coding genes. Gene deserts constitute an estimated 25% of the entire genome,

neg: GAL4/UAS system and the UAS are very useful for studying gene expression in "Drosophila" as they are not normally present and their expression does not interfere with other processes in the cell. For example, GAL4/UAS-regulated transgenes in "Drosophila" have been used to alter glial expression to produce arrhythmic behavior in a known rhythmic circadian output called pigment dispersing factor (PDF). However, some research has indicated that over-expression of GAL4 in "Drosophila" can have side-effects, probably relating to immune and stress responses to what is essentially an alien protein. The GAL4-UAS system has also been employed to study gene expression in organisms besides

neg: Transmembrane protein 134 Transmembrane protein 134 Transmembrane protein 134 is a protein encoded by the "TMEM134" gene. TMEM134 does not have any other known aliases. There are two transmembrane domains and a domain of unknown function (DUF872). Evolutionary, the majority of the organisms that have this gene are primates and mammals, although there are some organisms dating back to "Drosphila" and "C. elegans". Through current research, there has not been any confirmed function of TMEM134. The gene is composed of 6 exons spanning from 67464348 to 67469277 kilo bases. It is located on chromosome 11q13.2, which is the minus strand of the chromosome.

neg: MYH16 gene H. Stedman. The date of the mutation has variously been estimated at about 2.4 million years ago or 5.3 million years ago. The MYH16 gene is present in dogs, but does not appear to be present in mice. MYH16 gene The MYH16 gene encodes a protein called myosin heavy chain 16 which is a muscle protein in mammals. At least in primates, it is a specialized muscle protein found only in the temporalis and masseter muscles of the jaw. Myosin heavy chain proteins are important in muscle contraction, and if they are missing, the muscles will be smaller. In non-human

neg: Protein Moreover, the number of proteins the genome encodes correlates well with the organism complexity. Eukaryotes, bacteria, archaea and viruses have on average 15145, 3200, 2358 and 42 proteins respectively coded in their genomes. Proteins are assembled from amino acids using information encoded in genes. Each protein has its own unique amino acid sequence that is specified by the nucleotide sequence of the gene encoding this protein. The genetic code is a set of three-nucleotide sets called codons and each three-nucleotide combination designates an amino acid, for example AUG (adenine-uracil-guanine) is the code for methionine. Because DNA contains four nucleotides, the

neg: Regulator gene to bind DNA, allowing RNA polymerase to continue transcription. Regulator genes can be located within an operon, adjacent to it, or far away from it. Other regulatory genes code for activator proteins. An activator binds to a site on the DNA molecule and causes an increase in transcription of a nearby gene. In prokaryotes, a well-known activator protein is the catabolite activator protein or CAP, involved in positive control of the lac operon. In the regulation of gene expression, studied in evolutionary developmental biology (evo-devo), both activators and repressors play important roles. Regulatory genes can also be described as positive

neg: ASIC5 ASIC5 ASIC5 gene is one of the five paralogous genes that encode proteins that form trimeric Acid-sensing ion channels (ASICs) in mammals. Aliases previously used for this gene include ACCN5 and BASIC. The protein encoded by this gene does not appear to be acid responsive. The cDNA coding for this protein was first characterized in 2000. The ASIC genes have splicing variants that encode different proteins that are called isoforms. These genes are mainly expressed in the central and peripheral nervous system. ASICs can form both homotrimeric (meaning composed of three identical subunits) and heterotrimeric channels. This gene encodes a

neg: Destrin and is thought to connect it as gelsolin segment-1 does. Furthermore, the binding of actin by destrin and cofilin is regulated negatively by phosphorylation. Destrin can also sever actin filaments. Destrin Destrin or DSTN (also known as actin depolymerizing factor or ADF) is a protein which in humans is encoded by the "DSTN" gene. Destrin is a component protein in microfilaments. The product of this gene belongs to the actin-binding proteins ADF (Actin-Depolymerizing Factor)/cofilin family. This family of proteins is responsible for enhancing the turnover rate of actin in vivo. This gene encodes the actin depolymerizing protein that severs actin

neg: Protein protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides, or sometimes oligopeptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residues in a protein is defined by the sequence of a gene, which is encoded in the genetic code. In general, the genetic code specifies 20 standard amino acids; however, in certain organisms the genetic code can include selenocysteine and—in certain archaea—pyrrolysine. Shortly after or even during synthesis, the residues in

neg: Major basic protein MBP does not bind either calcium or any of the other carbohydrates that this family recognize. Instead, MBP recognises heparan sulfate proteoglycans. Two crystallographic structures of MBP have been determined. Major basic protein has been shown to interact with Pregnancy-associated plasma protein A. arylsulfatase Major basic protein Eosinophil Major basic protein, often shortened to Major basic protein (MBP) (also called Proteoglycan 2(PRG2)) in humans is encoded by the "PRG2" gene. The protein encoded by this gene is the predominant constituent of the crystalline core of the eosinophil granule. High levels of the proform of this protein are also present in

neg: FKBP52 FKBP52 FK506-binding protein 4 is a protein that in humans is encoded by the "FKBP4" gene. The protein encoded by this gene is a member of the immunophilin protein family, which play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. This encoded protein is a cis-trans prolyl isomerase that binds to the immunosuppressants FK506 and rapamycin. It has high structural and functional similarity to FK506-binding protein 1A (FKBP1A), but unlike FKBP1A, this protein does not have immunosuppressant activity when complexed with FK506. It interacts with interferon regulatory factor-4 and plays an important role in immunoregulatory

neg: Gene cluster and divergence. These gene clusters include the Hox gene cluster, the human β-globin gene cluster, and four clustered human growth hormone (hGH)/chorionic somaomammotropin genes. Conserved gene clusters, such as Hox and the human β-globin gene cluster, may be formed as a result of the process of "gene duplication and divergence". A gene is duplicated during cell division, so that its descendants have two end-to-end copies of the gene where it had one copy, initially coding for the same protein or otherwise having the same function. In the course of subsequent evolution, they diverge, so that the products they code for

neg: Epigenetics of human development in the gene. Gene expression refers to the transcription of a gene but the RNA produced does not necessarily have to encode a protein product. Transcription may produce so called noncoding RNA products such as tRNA and regulatory RNA. Repression may refer to the decrease in transcription of a gene or inhibition of a protein. Proteins are often inhibited by binding the active site or causing a conformational change so that the active site can no longer bind. By making these alterations, proteins, like transcription factors, may bind DNA less or some protein may be inhibited so that it becomes

neg: FZD6 FZD6 Frizzled-6 is a protein that in humans is encoded by the "FZD6" gene. Members of the 'frizzled' gene family encode 7-transmembrane domain proteins that are receptors for WNT signaling proteins. The FZD6 protein contains a signal peptide, a cysteine-rich domain in the N-terminal extracellular region, and 7 transmembrane domains. However, unlike many other FZD family members, FDZ6 does not contain a C-terminal PDZ domain-binding motif. The FZD6 protein is believed to be the receptor for the WNT4 ligand. FZD6 has been shown to interact with Secreted frizzled-related protein 1. Model organisms have been used in the study of FXYD3