source stringlengths 32 209 | text stringlengths 18 1.5k |
|---|---|
https://en.wikipedia.org/wiki/GGA3 | ADP-ribosylation factor-binding protein GGA3 is a protein that in humans is encoded by the GGA3 gene.
This gene encodes a member of the Golgi-localized, gamma adaptin ear-containing, ARF-binding (GGA) family. This family includes ubiquitous coat proteins that regulate the trafficking of proteins between the trans-Golgi network and the lysosome. These proteins share an amino-terminal VHS domain which mediates sorting of the mannose 6-phosphate receptors at the trans-Golgi network. They also contain a carboxy-terminal region with homology to the ear domain of gamma-adaptins. Alternative splicing of this gene results in two transcript variants.
Interactions
GGA3 has been shown to interact with ARF1 and ARF3.
References
Further reading |
https://en.wikipedia.org/wiki/TPH2 | Tryptophan hydroxylase 2 (TPH2) is an isozyme of tryptophan hydroxylase found in vertebrates. In humans, TPH2 is primarily expressed in the serotonergic neurons of the brain, with the highest expression in the raphe nucleus of the midbrain. Until the discovery of TPH2 in 2003, serotonin levels in the central nervous system were believed to be regulated by serotonin synthesis in peripheral tissues, in which tryptophan hydroxylase is the dominant form.
Function
Tryptophan hydroxylase (TPH; EC 1.14.16.4) is the rate-limiting enzyme in the synthesis of serotonin (5-hydroxytryptamine, or 5HT). 5HT is causally involved in numerous central nervous activities, and it has several functions in peripheral tissues, including the maintenance of vascular tone and gut motility.[supplied by OMIM]
Disabling this enzyme with drugs (especially p-chlorophenylalanine aka PCPA and Fenclonine) has allowed researchers to investigate the effects of very low serotonin levels on humans and others animals, and by extension, gain insights into the functions of serotonin systems more broadly (such as hypersexuality in rodents as well as increased aggression and hypersexuality cats following PCPA administration). In rat brain, administration of a single PCPA injection resulted in the lowest level of serotonin production occurring on day 2 and returning to control values on day 7. Drugs such as MDMA and methamphetamine have been shown to lower levels of this enzyme which may result in periods of low ser |
https://en.wikipedia.org/wiki/Annexin%20A6 | Annexin A6 is a protein that in humans is encoded by the ANXA6 gene.
Function
Annexin VI belongs to a family of calcium-dependent membrane and phospholipid binding proteins. Although their functions are still not clearly defined, several members of the annexin family have been implicated in membrane-related events along exocytotic and endocytotic pathways. The annexin VI gene is approximately 60 kbp long and contains 26 exons. It encodes a protein of about 68 kDa that consists of eight 68-amino acid repeats separated by linking sequences of variable lengths. It is highly similar to human annexins I and II sequences, each of which contain four such repeats. Exon 21 of annexin VI is alternatively spliced, giving rise to two isoforms that differ by a 6-amino acid insertion at the start of the seventh repeat. Annexin VI has been implicated in mediating the endosome aggregation and vesicle fusion in secreting epithelia during exocytosis.
Model organisms
Model organisms have been used in the study of ANXA6 function. A conditional knockout mouse line, called Anxa6tm1a(EUCOMM)Wtsi was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists — at the Wellcome Trust Sanger Institute.
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty six tests were carried out on mutant mice and one sig |
https://en.wikipedia.org/wiki/ARAF | Serine/threonine-protein kinase A-Raf or simply A-Raf is an enzyme that in humans is encoded by the ARAF gene. A-Raf is a member of the Raf kinase family of serine/threonine-specific protein kinases.
Compared to the other members of this family (Raf-1 and B-Raf), very little is known about A-Raf. It seems to share many of the properties of the other isoforms, but its biological functions are not as thoroughly researched. All three Raf proteins are involved in the MAPK signaling pathway.
There are several ways A-Raf is different from the other Raf kinases. A-Raf is the only steroid hormone-regulated Raf isoform. In addition, the A-Raf protein has amino acid substitutions in a negatively charged region upstream of the kinase domain (N-region). This could be responsible for its low basal activity.
Like Raf-1 and B-Raf, A-Raf activates MEK proteins which causes the activation of ERK and ultimately leads to cell cycle progression and cell proliferation. All three Raf proteins are located in the cytosol in their inactive state when bound to 14-3-3. In the presence of active Ras, they translocate to the plasma membrane. Among the Ras kinase family, A-Raf has the lowest kinase activity towards MEK proteins in the Raf kinase family. Thus, it is possible that A-Raf has other functions outside the MAPK pathway or that it helps the other Raf kinases activate the MAPK pathway. In addition to phosphorylating MEK, A-Raf also inhibits MST2, a tumor suppressor and proapoptotic kinase |
https://en.wikipedia.org/wiki/Glucose-6-phosphate%20exchanger%20SLC37A4 | Glucose-6-phosphate exchanger SLC37A4, also known as glucose-6-phosphate translocase, is an enzyme that in humans is encoded by the SLC37A4 gene.
It consists of three subunits, each of which are vital components of the multi-enzyme Glucose-6-Phosphatase Complex (G6Pase). This important enzyme complex is located within the membrane of the endoplasmic reticulum, and catalyzes the terminal reactions in both glycogenolysis and gluconeogenesis. The G6Pase complex is most abundant in liver tissue, but also present in kidney cells, small intestine, pancreatic islets and at a lower concentration in the gallbladder. The G6Pase complex is highly involved in the regulation of homeostasis and blood glucose levels. Within this framework of glucose regulation, the translocase components are responsible for transporting the substrates and products across the endoplasmic reticulum membrane, resulting in the release of free glucose into the bloodstream.
Structure
Glucose-6-phosphate translocase is a transmembrane protein providing a selective channel between the endoplasmic reticulum lumen and the cytosol. The enzyme is made up of three separate transporting subunits referred to as G6PT1 (subunit 1), G6PT2 (subunit 2) and G6PT3 (subunit 3). While the hydrolyzing component of the G6Pase complex is located on the side of the membrane on which it acts, namely facing the lumen, the translocases are all integral membrane proteins in order to perform their function as cross-membrane transporters |
https://en.wikipedia.org/wiki/GPX4 | Glutathione peroxidase 4, also known as GPX4, is an enzyme that in humans is encoded by the GPX4 gene. GPX4 is a phospholipid hydroperoxidase that protects cells against membrane lipid peroxidation.
Function
The antioxidant enzyme glutathione peroxidase 4 (GPX4) belongs to the family of glutathione peroxidases, which consists of 8 known mammalian isoenzymes (GPX1–8). GPX4 catalyzes the reduction of hydrogen peroxide, organic hydroperoxides, and lipid peroxides at the expense of reduced glutathione and functions in the protection of cells against oxidative stress. The oxidized form of glutathione (glutathione disulfide), which is generated during the reduction of hydroperoxides by GPX4, is recycled by glutathione reductase and NADPH/H+. GPX4 differs from the other GPX family members in terms of its monomeric structure, a less restricted dependence on glutathione as reducing substrate, and the ability to reduce lipid-hydroperoxides inside biological membranes.
Inactivation of GPX4 leads to an accumulation of lipid peroxides, resulting in ferroptotic cell death. Mutations in GPX4 cause spondylometaphyseal dysplasia.
Structure
Mammalian GPX1, GPX2, GPX3, and GPX4 (this protein) have been shown to be selenium-containing enzymes, whereas GPX6 is a selenoprotein in humans with cysteine-containing homologues in rodents. In selenoproteins, the amino acid selenocysteine is inserted in the nascent polypeptide chain during the process of translational recoding of the UGA stop cod |
https://en.wikipedia.org/wiki/IRF2 | Interferon regulatory factor 2 is a protein that in humans is encoded by the IRF2 gene.
Function
IRF2 encodes interferon regulatory factor 2, a member of the interferon regulatory transcription factor (IRF) family. IRF2 competitively inhibits the IRF1-mediated transcriptional activation of interferons alpha and beta, and presumably other genes that employ IRF1 for transcription activation. However, IRF2 also functions as a transcriptional activator of histone H4.
See also
IRF1
Interferon regulatory factors
Interactions
IRF2 has been shown to interact with BRD7, EP300 and PCAF.
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/MMP10 | Stromelysin-2 also known as matrix metalloproteinase-10 (MMP-10) or transin-2 is an enzyme that in humans is encoded by the MMP10 gene.
Function
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades proteoglycans and fibronectin. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.
Clinical significance
MMP10 has been linked to cancer stem cell vitality and metastasis.
MMP10 is a potential prognostic biomarker for oral cancer.
References
Further reading
External links
The MEROPS online database for peptidases and their inhibitors: M10.006
Matrix metalloproteinases
EC 3.4.24 |
https://en.wikipedia.org/wiki/NFYB | Nuclear transcription factor Y subunit beta is a protein that in humans is encoded by the NFYB gene.
Function
The protein encoded by this gene is one subunit of a trimeric complex, forming a highly conserved transcription factor that binds with high specificity to CCAAT motifs in the promoter regions in a variety of genes. This gene product, subunit B, forms a tight dimer with the C subunit, a prerequisite for subunit A association. The resulting trimer binds to DNA with high specificity and affinity. Subunits B and C each contain a histone-like motif. Observation of the histone nature of these subunits is supported by two types of evidence; protein sequence alignments and experiments with mutants.
Interactions
NFYB has been shown to interact with:
CEBPZ,
CNTN2,
Myc, and
TBP
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/PAWR | PRKC apoptosis WT1 regulator protein, or Prostate apoptosis response-4, is a tumor-suppressor protein coded for in the human by the PAWR gene, that induces apoptosis in cancer cells, but not in normal cells.
Function
The tumor suppressor WT1 represses and activates transcription. The protein encoded by this gene is a WT1-interacting protein that itself functions as a transcriptional repressor. It contains a putative leucine zipper domain which interacts with the zinc finger DNA binding domain of WT1. This protein is specifically upregulated during apoptosis of prostate cells.
The active domain of the Par-4 protein has been found to confer cancer resistance in transgenic mice without compromising normal viability or aging, and may have therapeutic significance.
Interactions
PAWR has been shown to interact with:
Protein AATF,
DAPK3,
Protein kinase Mζ,
SLC5A1,
THAP1, and
WT1.
References
Further reading |
https://en.wikipedia.org/wiki/PPIB | Peptidyl-prolyl cis-trans isomerase B is an enzyme that is encoded by the PPIB gene. As a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family, this protein catalyzes the cis-trans isomerization of proline imidic peptide bonds, which allows it to regulate protein folding of type I collagen. Generally, PPIases are found in all eubacteria and eukaryotes, as well as in a few archaebacteria, and thus are highly conserved.
Structure
Like other cyclophilins, PPIB forms a β-barrel structure with a hydrophobic core. This β-barrel is composed of eight anti-parallel β-strands and capped by two α-helices at the top and bottom. In addition, the β-turns and loops in the strands contribute to the flexibility of the barrel. In particular, PPIB is a 21 kDa protein which contains a C-terminal ER retention motif that directs the protein to the ER organelle, while its N-terminal extension attaches it to its substrates.
Function
PPIB is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds and regulate protein folding and maturation. Proline is the only amino acid known to exist in both the cis and trans isomerization rate in vivo, and is often the rate-limiting step in protein refolding. The PPIase family is further divided into three structurally distinct subfamilies: cyclophilin (CyP), FK506-binding protein (FKBP), and parvulin (Pvn). While each family demonstrates PPIase activity, t |
https://en.wikipedia.org/wiki/Auxiliary%20electrode | In electrochemistry, the auxiliary electrode, often also called the counter electrode, is an electrode used in a three-electrode electrochemical cell for voltammetric analysis or other reactions in which an electric current is expected to flow. The auxiliary electrode is distinct from the reference electrode, which establishes the electrical potential against which other potentials may be measured, and the working electrode, at which the cell reaction takes place.
In a two-electrode system, either a known current or potential is applied between the working and auxiliary electrodes and the other variable may be measured. The auxiliary electrode functions as a cathode whenever the working electrode is operating as an anode and vice versa. The auxiliary electrode often has a surface area much larger than that of the working electrode to ensure that the half-reaction occurring at the auxiliary electrode can occur fast enough so as not to limit the process at the working electrode.
When a three-electrode cell is used to perform electroanalytical chemistry, the auxiliary electrode, along with the working electrode, provides a circuit over which current is either applied or measured. Here, the potential of the auxiliary electrode is usually not measured and is adjusted so as to balance the reaction occurring at the working electrode. This configuration allows the potential of the working electrode to be measured against a known reference electrode without compromising the stabili |
https://en.wikipedia.org/wiki/David%20Hibbett | David Hibbett is an associate professor in biology at Clark University. He is considered one of today's leading researchers "in the analysis of fungal relationships through DNA analysis." At Clark he concentrates his lab work in evolutionary biology and ecology of Fungi.
He spent 1991 as a Science and Technology Agency of Japan Post-doctoral Fellow at the Tottori Mycological Institute in Tottori, Japan. A year later Hibbett taught microbiology at Framingham State College for the spring semester. From 1993 to 1999, Hibbett was a postdoctoral researcher and then a research associate in the laboratory of Michael Donoghue in the Harvard University Herbaria.
He received his Bachelor of Arts from the Botany Department of University of Massachusetts Amherst and his Ph.D. from the Botany Department of Duke University.
In 2007, Hibbett led the publication of a comprehensive, phylogenetically based classification scheme for the Kingdom Fungi with a long list of international taxonomic specialists, which has remained the standard framework for the higher classification of these organisms. His most cited paper (as of 4 January 2021) with 1755 citations is Reconstructing the early evolution of Fungi using a six-gene phylogeny.
References
Clark University faculty
Duke University alumni
University of Massachusetts Amherst College of Natural Sciences alumni
Harvard University staff
Living people
Year of birth missing (living people) |
https://en.wikipedia.org/wiki/RBBP7 | Histone-binding protein RBBP7 is a protein that in humans is encoded by the RBBP7 gene.
Function
This protein is a ubiquitously expressed nuclear protein and belongs to a highly conserved subfamily of WD-repeat proteins. It is found among several proteins that binds directly to retinoblastoma protein, which regulates cell proliferation. The encoded protein is found in many histone deacetylase complexes, including mSin3 co-repressor complex. It is also present in protein complexes involved in chromatin assembly. This protein can interact with BRCA1 tumor-suppressor gene and may have a role in the regulation of cell proliferation and differentiation.
Model organisms
Model organisms have been used in the study of RBBP7 function. A conditional knockout mouse line, called Rbbp7tm1a(EUCOMM)Wtsi was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty one tests were carried out on mutant mice and one significant abnormality was observed: hemizygous mutant males had decreased CD4-positive and CD8-positive T cell numbers.
Interactions
RBBP7 has been shown to interact with:
BRCA1,
GATAD2B,
HDAC1,
MTA2,
Retinoblastoma protein,
SAP30, and
SIN3A.
References
Further reading
Genes |
https://en.wikipedia.org/wiki/SAA2 | Serum amyloid A protein is a protein that in humans is encoded by the SAA2 gene.
References
Further reading |
https://en.wikipedia.org/wiki/Ataxin-2 | Ataxin-2 is a protein that in humans is encoded by the ATXN2 gene. Mutations in ATXN2 cause spinocerebellar ataxia type 2 (SCA2).
Protein structure
Ataxin-2 contains the following protein domains:
Two LSm domains, which likely allow it to bind RNA
A PAM2 motif, predicted to associate with the poly(A)-binding protein
A polyglutamine tract in some species (located near the amino terminal in primates and between the LSm domains in insects)
A potential transcript variant, missing an internal coding exon, has been described; however, its full-length nature is not certain.
Species, tissue, and subcellular distribution
ATXN2 is conserved across eukaryotes. Most vertebrates have two orthologs of the gene (called ATXN2 and ATXN2L in humans), with the exception of birds which only have one. Plant species have two to six ATXN2 orthologs.
ATXN2 is ubiquitously expressed in different tissues. Within individual cells, it localizes to the Golgi apparatus and stress granules.
Function
Ataxin-2 is involved in regulating mRNA translation through its interactions with the poly(A)-binding protein. It is also involved in the formation of stress granules and P-bodies, which also play roles in RNA regulation.
Clinical significance
Spinocerebellar ataxia type 2 (SCA2)
The polyglutamine tract in human ataxin-2 is unstable and can expand as it is transmitted across generations. Normal alleles usually have 22 or 23 repeats, but can contain up to 31 repeats. Longer expansions can cause sp |
https://en.wikipedia.org/wiki/Sodium%E2%80%93hydrogen%20antiporter%203 | Sodium–hydrogen antiporter 3 also known as sodium–hydrogen exchanger 3 (NHE3) or solute carrier family 9 member 3 (SLC9A3) is a protein that in humans is encoded by the SLC9A3 gene.
SLC9A3 is a sodium–hydrogen antiporter. It is found on the apical side of the epithelial cells of the proximal tubule of the nephron of the kidney, in the apical membrane of enterocytes of the intestine, as well as the basolateral side of both duodenal and pancreatic cells responsible for the release of HCO−3 into the duodenal lumen. It is primarily responsible for maintaining the balance of sodium. It is also indirectly linked to buffering of blood pH. The NHE3 antiporter imports one sodium ion into the cytosol of a tubule cell as it ejects one hydrogen ion from the cell into the lumen of the proximal tubule. The sodium within the tubule cell may then be retained by the body rather than excreted in the urine. The NHE3 antiporter indirectly contributes to blood buffering capacity because hydrogen ions that are ejected are the products of the carbonic anhydrase enzyme, which also makes bicarbonate.
Regulation
Protein kinase C stimulates NHE3, while protein kinase A inhibits it.
There is a specific protein functioning as an NHE3 regulator, Sodium-hydrogen antiporter 3 regulator 1.
Inhibitors
Tenapanor
Stimulators
Insulin stimulates NHE3 and thereby proximal tubule sodium absorption.
Interactions
Sodium–hydrogen antiporter 3 has been shown to interact with CHP.
References
Furt |
https://en.wikipedia.org/wiki/Small%20nuclear%20ribonucleoprotein%20D1 | Small nuclear ribonucleoprotein Sm D1 is a protein that in humans is encoded by the SNRPD1 gene.
Function
This gene encodes a small nuclear ribonucleoprotein that belongs to the SNRNP core protein family. The protein may act as a charged protein scaffold to promote SNRNP assembly or strengthen SNRNP-SNRNP interactions through nonspecific electrostatic contacts with RNA.
Interactions
Small nuclear ribonucleoprotein D1 has been shown to interact with:
CDC5L,
CLNS1A,
DDX20,
SMN1, and
Small nuclear ribonucleoprotein D2
References
Further reading |
https://en.wikipedia.org/wiki/ADCYAP1R1 | Pituitary adenylate cyclase-activating polypeptide type I receptor also known as PAC1, is a protein that in humans is encoded by the ADCYAP1R1 gene. This receptor binds pituitary adenylate cyclase activating peptide.
Function
PAC1 is a membrane-associated protein and shares significant homology with members of the G-protein coupled class B glucagon/secretin receptor family. This receptor mediates diverse biological actions of adenylate cyclase activating polypeptide 1 and is positively coupled to adenylate cyclase. Alternative splicing of two exons of this gene generates four major splice variants, but their full-length nature has not been determined. PAC1 is expressed in the adrenal medulla, pancreatic acini, uterus, myenteric plexus and brain. It is also expressed in the trigeminal, otic and superior cervical ganglia (prejunctional) and cerebral arteries (postjunctional).
References
Further reading
External links |
https://en.wikipedia.org/wiki/CLDN4 | Claudin 4, also known as CLDN4, is a protein which in humans is encoded by the CLDN4 gene. It belongs to the group of claudins.
This gene encodes an integral membrane protein, which belongs to the claudin family. The protein is a component of tight junction strands and may play a role in internal organ development and function during pre- and postnatal life. This gene is deleted in Williams-Beuren syndrome, a neurodevelopmental disorder affecting multiple systems.
Claudin 4 can also be used as a marker for distinguishing malignant mesothelioma from lung cancer and uterine serous carcinoma. As a pancreatic cancer marker in cell-blocks of effusion specimens, it has also been found to have a superior performance to BerEp4 staining.
References
External links
Further reading |
https://en.wikipedia.org/wiki/Somatostatin%20receptor%205 | Somatostatin receptor type 5 is a protein that in humans is encoded by the SSTR5 gene.
Somatostatin acts at many sites to inhibit the release of many hormones and other secretory proteins. The biological effects of somatostatin are probably mediated by a family of G protein-coupled receptors that are expressed in a tissue-specific manner. SSTR5 is a member of the superfamily of receptors having seven transmembrane segments.
See also
Somatostatin receptor
References
Further reading
External links
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Sieve%20estimator | In statistics, sieve estimators are a class of non-parametric estimators which use progressively more complex models to estimate an unknown high-dimensional function as more data becomes available, with the aim of asymptotically reducing error towards zero as the amount of data increases. This method is generally attributed to Ulf Grenander.
Method of sieves in positron emission tomography
Sieve estimators have been used extensively for estimating density functions in high-dimensional spaces such as in Positron emission tomography (PET). The first exploitation of Sieves in PET for solving the maximum-likelihood image reconstruction problem was by Donald Snyder and Michael Miller, where they stabilized the time-of-flight PET problem originally solved by Shepp and Vardi.
Shepp and Vardi's introduction of Maximum-likelihood estimators in emission tomography exploited the use of the Expectation-Maximization algorithm, which as it ascended towards the maximum-likelihood estimator developed a series of artifacts associated to the fact that the underlying emission density was of too high a dimension for any fixed sample size of Poisson measured counts. Grenander's method of sieves was used to stabilize the estimator, so that for any fixed sample size a resolution could be set which was consistent for the number of counts. As the observe PET imaging time would go to infinity, the dimension of the sieve would increase as well in such a manner that the density was appropriate for ea |
https://en.wikipedia.org/wiki/Oncogenic%20retroviridae%20protein | Oncogenic retroviridae proteins are retroviral proteins that have the ability to transform cells. They can induce sarcomas, leukaemias, lymphomas, and mammary carcinomas. These include the gag-onc fusion protein, rex, tax, v-fms, ras, v-myc, v-src, v-akt, v-cbl, v-crk, v-maf, v-abl, v-erbA, v-erbB, v-fos, v-mos, v-myb, v-raf, v-rel, and v-sis. The "v" prefix indicates viral genes which once originated as similarly named genes of the host species, but have since been altered through independent evolution as retroviral components. Not all retroviral proteins are oncogenic. The phrase was introduced as a MeSH term in 1990, under which over 6000 primary scientific publications are indexed.
See also
Oncogenic
References
Proteins |
https://en.wikipedia.org/wiki/5-HT4%20receptor | {{DISPLAYTITLE:5-HT4 receptor}}
5-Hydroxytryptamine receptor 4 is a protein that in humans is encoded by the HTR4 gene.
Function
This gene is a member of the family of human serotonin receptors, which are G protein-coupled receptors that stimulate cAMP production in response to serotonin (5-hydroxytryptamine). The gene product is a glycosylated transmembrane protein that functions in both the peripheral and central nervous system to modulate the release of various neurotransmitters. Multiple transcript variants encoding proteins with distinct C-terminal sequences have been described, but the full-length nature of some transcript variants has not been determined.
Location
The receptor is located in the alimentary tract, urinary bladder, heart and adrenal gland as well as the central nervous system (CNS).
In the CNS the receptor appears in the putamen, caudate nucleus, nucleus accumbens, globus pallidus, and substantia nigra, and to a lesser extent in the neocortex, raphe, pontine nuclei, and some areas of the thalamus.
It has not been found in the cerebellum.
Isoforms
Internalization is isoform-specific.
Ligands
Several drugs that act as 5-HT4 selective agonists have recently been introduced into use in both scientific research and clinical medicine. Some drugs that act as 5-HT4 agonists are also active as 5-HT3 antagonists, such as mosapride, metoclopramide, renzapride, and zacopride, and so these compounds cannot be considered highly selective. Research in this area |
https://en.wikipedia.org/wiki/Siuslaw%20National%20Forest | The Siuslaw National Forest ( ) is a national forest in western Oregon in the United States. Established in 1908, the Siuslaw is made up of a wide variety of ecosystems, ranging from coastal forests to sand dunes.
Geography
The Siuslaw National Forest encompasses more than along the central Oregon Coast between Coos Bay and Tillamook, and in some places extends east from the ocean, beyond the crest of the Oregon Coast Range, almost reaching the Willamette Valley. The forest lies primarily in Lane County (39% of the forest) and Lincoln County (27% of the forest); the rest in descending order of land area are Tillamook, Douglas, Yamhill, Benton, Coos, and Polk counties. It includes the Sand Lake Recreation Area and the Oregon Dunes National Recreation Area. The Forest Supervisor's office is located in Corvallis, and the Siuslaw is broken up into two ranger districts—the Hebo Ranger District, with approximately , and the Central Coast Ranger District, with approximately .
The forest contains Marys Peak, the highest point in the Oregon Coast Range at . Numerous aquatic habitats are found in the forest: marine shore, rivers and streams—, including the Alsea, Nestucca, Siuslaw, and Umpqua rivers—and 30 lakes. The terrestrial environment can be regarded as two major vegetation zones, one near the coast dominated by Sitka spruce (Picea sitchensis), and the other dominated by western hemlock (Tsuga heterophylla) and Douglas fir (Pseudotsuga menziesii). Western hemlock often gr |
https://en.wikipedia.org/wiki/John%20Renshaw%20Carson | John Renshaw Carson (June 28, 1886 – October 31, 1940) was an American transmission theorist for early communications systems. He invented single-sideband modulation and developed the Carson bandwidth rule for estimating frequency modulation (FM) bandwidth. In 2013 Carson was inducted into the Electronic Design Hall of Fame for his contributions to communications.
Biography
Carson was born in Pittsburgh, Pennsylvania, and together with his twin brother Joseph attended Princeton University, graduating in 1907 with a Bachelor of Science degree. John attended the Massachusetts Institute of Technology 1907–1908, before returning to Princeton to receive his electrical engineering degree in 1909 and a Master of Science degree in 1912. From 1912 to 1914 Carson was an instructor in Electrical Engineering and Physics at Princeton, but in 1913 was offered a position at American Telephone & Telegraph (AT&T), and in 1914 left the university.
At AT&T, Carson was involved in early radio telephone experiments. In 1915 he invented single-sideband modulation to transmit multiple telephone calls simultaneously on a single electrical circuit, and was responsible for installing the first such system between Pittsburgh and Baltimore. In 1922 he published a mathematical treatment of frequency modulation (FM), which introduced the Carson bandwidth rule. In his 1922 paper, Carson presented a negative opinion of narrowband FM, which occurs when the maximum frequency swing is made narrower than t |
https://en.wikipedia.org/wiki/Manifold%20%28fluid%20mechanics%29 | A manifold is a wider and/or larger pipe or channel, into which smaller pipes or channels lead, or a pipe fitting or similar device that connects multiple inputs or outputs for fluids.
Manifolds
Engineering
Types of manifolds in engineering include:
Exhaust manifold
An engine part that collects the exhaust gases from multiple cylinders into one pipe. Also known as headers.
Hydraulic manifold
A component used to regulate fluid flow in a hydraulic system, thus controlling the transfer of power between actuators and pumps
Inlet manifold (or "intake manifold")
An engine part that supplies the air or fuel/air mixture to the cylinders
Scuba manifold
In a scuba set, connects two or more diving cylinders
Vacuum gas manifold
An apparatus used in chemistry to manipulate gases
Also, many dredge pipe pieces.
Biology
In biology manifolds are found in:
Cardiovascular system (blood vessel manifolds, etc.)
Lymphatic system
Respiratory system
Other fields
Manifolds are used in:
HVAC
Pipe organ
Plumbing
References
Fluid mechanics |
https://en.wikipedia.org/wiki/Wall%20stress%20relaxation | The plant cell wall is made up of hydrated polymetric material, allowing it to have viscoelastic properties. The primary cell wall of a plant consists of cellulose fibers, hemicellulose, and xyloglucans. This load bearing network is also surrounded by pectins and glycoproteins.
Wall stress relaxation is an important factor in cell wall expansion. Wall stress (measured in force per unit area) is created in response to the plant cell's turgor pressure. Turgor pressure creates tension in the cell walls of plants, fungi, and bacteria, as it opposes the pressure of the cell's primary cell wall; this also allows for stretching of the cell wall. The stretching of the cell wall, or the reduction of stress, occurs as a result of cell expansion and rearrangement. Cell expansion is crucial for the reshaping and rearranging of plant cells. Expansion is the result of "creep", or selective wall loosening, which is driven by turgor pressure. During this "creep", cellulose microfibers move relative to each other creating an irreversible extension
Cell expansion
Cell expansion begins with the selective loosening of the cell wall, reducing the plant cell's turgor pressure and water potential. This allows for the influx of water, leading to cell enlargement. This enlargement is made possible by the sliding of polymers, increasing the cell wall's surface area.
In most plants, cell expansion is anisotropic. Previous experiments have confirmed that the cellulose microfibril orientation in the |
https://en.wikipedia.org/wiki/Walter%20Guyton%20Cady | Walter Guyton Cady (December 10, 1874 – December 9, 1974) was a noted American physicist and electrical engineer. He was a pioneer in piezoelectricity, and in 1921 developed the first quartz crystal oscillator.
Cady was born in Providence, Rhode Island, graduated from Brown University in 1895, and studied 1897-1900 at the University of Berlin, receiving his Ph.D. in Physics in 1900. (From 1895 to 1897 he was also instructor in mathematics at Brown.) He was a Magnetic Observer from 1900 to 1902 with the Coast and Geodetic Survey, and from 1902 to 1946 he was a professor of physics at Wesleyan University, where his principal interests included electrical discharges in gases, piezoelectricity, ultrasound, piezoelectric resonators and oscillators, and crystal devices.
Before World War I, Cady investigated arc discharges and radio detectors, but during the war became interested in crystals as he worked with General Electric Company's Research Laboratory, Columbia University, and the Naval Experimental Station in New London, Connecticut, on using high-frequency sound generated by piezoelectricity to detect submarines. His early experiments employed Rochelle salt crystals as transducers. After noticing that a quartz crystal connected to a variable-frequency electronic oscillator would vibrate strongly at a very specific frequency, but that at other frequencies it would not vibrate at all, he had the insight to apply crystal oscillators to radio frequency applications.
In 1921 Cad |
https://en.wikipedia.org/wiki/Debra%20Bernhardt | Debra Bernhardt (née Searles) (born 1965) is an Australian theoretical chemist. She is best known for her contributions towards understanding the fluctuation theorem. This theorem shows the second law of thermodynamics and the zeroth law of thermodynamics can be derived mathematically rather than postulated as laws of nature.
Personal profile
Bernhardt has previously worked as an associate professor in the Faculty of Science at Griffith University. During her time at Griffith University, she became the founding director of the Queensland Micro- and Nanotechnology Centre. She received her PhD from the University of Newcastle for her work on quantum chemistry. In 2012, Bernhardt joined the University of Queensland as a professor in a joint appointment between the School of Chemistry and Molecular Biosciences and the Australian Institute of Bioengineering and Nanotechnology.
In 2019 Bernhardt was elected to a Fellowship of the Australian Academy of Science. She is also a Fellow of the Royal Australian Chemical Institute. In the past, Bernhardt has also held research positions at the University of Basel in Switzerland and Australian National University.
Research interests
Bernhardt's research interests are in the study of liquids under equilibrium and nonequilibrium conditions, development of the theory of nonequilibrium fluids and use of simulations to assist in understanding experimental results. Current research projects include: the study of nonequilibrium liquids via sta |
https://en.wikipedia.org/wiki/Pisit%20Charnsnoh | Pisit Charnsnoh, from Trang Province, Thailand, cofounded the Yadfon Association in 1985. He was awarded the Goldman Environmental Prize in 2002, for his efforts on protecting the coastal ecosystems of Thailand. Charnsnoh is on the board of the international Seattle-based Mangrove Action Project, and is affiliated with the Industrial Shrimp Action Network.
References
Pisit Charnsnoh
Living people
Year of birth missing (living people)
Goldman Environmental Prize awardees |
https://en.wikipedia.org/wiki/UCSC%20Malaria%20Genome%20Browser | UCSC Malaria Genome Browser is a bioinformatic research tool to study the malaria genome, developed by Hughes Undergraduate Research Laboratory together with the laboratory of Prof. Manuel Ares Jr. at the University of California, Santa Cruz.
The web interface and database structure is based on the UCSC Genome Browser. UCSC Malaria Genome Browser brings together on a single screen the full DNA sequences of several species of the malaria parasite (Plasmodium sp.), alongside experimental results and previously discovered genes collected from the literature. The program allows users to search through 14 chromosomes of the malaria parasite's genome, enter their own sequence data and notes, and compare findings across species. The Malaria Genome Browser also supports text and sequence based searches that provide quick, precise access to any region of specific interest in the malaria genome. This site contains the reference genome sequence and working draft assembly for Plasmodium falciparum from PlasmoDb, the Plasmodium genome database build 5.0.
References
External links
UCSC Malaria Genome Browser
UCSC Genome Browser for human, vertebrate, invertebrate and other species
Ares lab page
UCSC Genome Browser tutorials
Genome databases
Malaria |
https://en.wikipedia.org/wiki/GGSE | GGSE may refer to:
Gravity-gradient stabilization, a method of stabilizing artificial satellites
GGSE-1, a technology satellite launched by the US military in 1964
Gevirtz Graduate School of Education, University of California at Santa Barbara
See also
GSE (disambiguation) |
https://en.wikipedia.org/wiki/TYROBP | TYRO protein tyrosine kinase-binding protein is an adapter protein that in humans is encoded by the TYROBP gene.
Function
This gene encodes a transmembrane signaling polypeptide which contains an immunoreceptor tyrosine-based activation motif (ITAM) in its cytoplasmic domain. The encoded protein may associate with the killer cell immunoglobulin-like receptor (KIR) family of membrane glycoproteins and may act as an activating signal transduction element. This protein may bind zeta-chain associated protein kinase 70 kDa (ZAP-70) and spleen tyrosine kinase (SYK) and play a role in signal transduction, bone modeling, brain myelination, and inflammation. Mutations within this gene have been associated with polycystic lipomembranous osteodysplasia with sclerosing leukoencephalopathy (PLOSL), also known as Nasu-Hakola disease. Its putative receptor, triggering receptor expressed on myeloid cells 2 (TREM2), also causes PLOSL. Two alternative transcript variants encoding distinct isoforms have been identified for this gene. Other alternative splice variants have been described, but their full-length nature has not been determined.
Interactions
TYROBP has been shown to interact with SIRPB1.
Clinical significance
Pathological mutations of the TYROBP gene cause polycystic lipomembranous osteodysplasia with sclerosing leukoencephalopathy 1, a condition presenting as early-onset dementia.
References
External links
GeneReviews/NIH/NCBI/UW entry on Polycystic Lipomembranous Osteo |
https://en.wikipedia.org/wiki/NCOA4 | Nuclear receptor coactivator 4, also known as Androgen Receptor Activator (ARA70), is a protein that in humans is encoded by the NCOA4 gene. It plays an important role in ferritinophagy, acting as a cargo receptor, binding to the ferritin heavy chain and latching on to ATG8 on the surface of the autophagosome.
Interactions
NCOA4 has been shown to interact with:
Androgen receptor, and
Peroxisome proliferator-activated receptor gamma
Ferritin
ATG8
See also
Transcription coregulator
References
Further reading
External links
Gene expression
Transcription coregulators |
https://en.wikipedia.org/wiki/FRS2 | Fibroblast growth factor receptor substrate 2 is a protein that in humans is encoded by the FRS2 gene.
FRS2 is an 80 kDa membrane-anchored signal transducing adaptor protein (STAP) that links specific activated Receptor Tyrosine Kinases (RTKs) to multiple downstream signaling pathways, most notably the MAPK/ERK, PI3K/AKT/mTOR and PLCγ pathways. It is overexpressed and amplified in several cancer types, including prostate cancer.
Interactions
FRS2 has been shown to interact with:
CBL
FGFR1
GRB2
PRKCI
PTPN11
SOS1
TrkA
ALK
References
Further reading |
https://en.wikipedia.org/wiki/GABARAP | Gamma-aminobutyric acid receptor-associated protein is a protein that in humans is encoded by the GABARAP gene.
Function
Gamma-aminobutyric acid A receptors [GABA(A) receptors] are ligand-gated chloride channels that mediate inhibitory neurotransmission. This gene encodes GABA(A) receptor-associated protein, which is highly positively charged in its N-terminus and shares sequence similarity with light chain-3 of microtubule-associated proteins 1A and 1B. This protein clusters neurotransmitter receptors by mediating interaction with the cytoskeleton.
Moreover, GABARAP has an important function in autophagosome mediated autophagy, since it is crucial for autophagosome formation and sequestration of cytosolic cargo into double-membrane vesicles, leading to subsequent degradation after fusion with lysosomes. In addition, GABARAP can mediate selective autophagy because it binds to so-called autophagic receptors (e.g. p62, NBr1), which bind and recruit specific cargo.
Interactions
GABARAP has been shown to interact with TFRC, ULK1 and GABRG2. A bound structure for GABARAP to GABRG2 consistent with experimental observations has been computationally derived.
References
Further reading |
https://en.wikipedia.org/wiki/AP1G1 | AP-1 complex subunit gamma-1 is a protein that in humans is encoded by the AP1G1 gene.
Function
Adaptins are important components of clathrin-coated vesicles transporting ligand-receptor complexes from the plasma membrane or from the trans-Golgi network to lysosomes. The adaptin family of proteins is composed of four classes of molecules named alpha, beta-, beta prime- and gamma- adaptins. Adaptins, together with medium and small subunits, form a heterotetrameric complex called an adaptor, whose role is to promote the formation of clathrin-coated pits and vesicles. The protein encoded by this gene is a gamma-adaptin protein and it belongs to the adaptor complexes large subunits family. Two transcript variants encoding different isoforms have been found for this gene.
Interactions
AP1G1 has been shown to interact with:
AP1B1,
AP1GBP1,
AP1M1,
AP1S1,
NECAP2,
RABEP1, and
Synaptophysin.
References
Further reading
External links
Proteins |
https://en.wikipedia.org/wiki/DLG2 | Disks large homolog 2 (DLG2) also known as channel-associated protein of synapse-110 (chapsyn-110) or postsynaptic density protein 93 (PSD-93) is a protein that in humans is encoded by the DLG2 gene.
Function
Chapsyn-110/PSD-93 a member of the membrane-associated guanylate kinase (MAGUK) family. The protein forms a heterodimer with a related family member that may interact at postsynaptic sites to form a multimeric scaffold for the clustering of receptors, ion channels, and associated signaling proteins. Alternatively spliced transcript variants encoding distinct isoforms have been described but their full-length nature has yet to be completely determined.
Model organisms
Model organisms have been used in the study of DLG2 function. A knockout mouse line, called Dlg2tm1Dsb was generated. Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty four tests were carried out on homozygous mutant mice and five significant abnormalities were observed. Both sexes had atypical indirect calorimetry and DEXA parameters. Females also had decreased body weight, decreased circulating HDL cholesterol levels, and increased susceptibility to bacterial infection.
Interactions
DLG2 has been shown to interact with GRIN2B, KCNJ12.
References
Further reading
Genes mutated in mice |
https://en.wikipedia.org/wiki/F13B | Coagulation factor XIII B chain is a protein that in humans is encoded by the F13B gene.
This gene encodes coagulation factor XIII B subunit. Coagulation factor XIII is the last zymogen to become activated in the blood coagulation cascade. Plasma factor XIII is a heterotetramer composed of 2 A subunits and 2 B subunits. The A subunits have catalytic function, and the B subunits do not have enzymatic activity and may serve as a plasma carrier molecules. Platelet factor XIII is composed of just 2 A subunits, which are identical to those of plasma origin. Upon activation by the cleavage of the activation peptide by thrombin and in the presence of calcium ion, the plasma factor XIII dissociates its B subunits and yields the same active enzyme, factor XIIIa, as platelet factor XIII. This enzyme acts as a transglutaminase to catalyze the formation of gamma-glutamyl-epsilon-lysine crosslinking between fibrin molecules, thus stabilizing the fibrin clot. Factor XIII deficiency is classified into two categories: type I deficiency, characterized by the lack of both the A and B subunits; and type II deficiency, characterized by the lack of the A subunit alone. These defects can result in a lifelong bleeding tendency, defective wound healing, and habitual abortion.
Interactions
F13B has been shown to interact with Coagulation factor XIII, A1 polypeptide.
References
Further reading |
https://en.wikipedia.org/wiki/GAS6 | Growth arrest – specific 6, also known as GAS6, is a human gene coding for the GAS6 protein. It is similar to the Protein S with the same domain organization and 43% amino acid identity. It was originally found as a gene upregulated by growth arrested fibroblasts.
Function
Gas6 is a gamma-carboxyglutamic acid (Gla) domain-containing protein thought to be involved in the stimulation of cell proliferation.
Interactions
Gas6 has been shown to interact with AXL receptor tyrosine kinase, MerTK and TYRO3.
The presence of Gla needs a vitamin K-dependent enzymatic reaction that carboxylates the gamma carbon of certain glutamic residues of the protein during its production in the endoplasmic reticulum. The action of vitamin K is essential on GAS6 function.
References
Further reading |
https://en.wikipedia.org/wiki/HK1 | Hexokinase-1 (HK1) is an enzyme that in humans is encoded by the HK1 gene on chromosome 10. Hexokinases phosphorylate glucose to produce glucose-6-phosphate (G6P), the first step in most glucose metabolism pathways. This gene encodes a ubiquitous form of hexokinase which localizes to the outer membrane of mitochondria. Mutations in this gene have been associated with hemolytic anemia due to hexokinase deficiency. Alternative splicing of this gene results in five transcript variants which encode different isoforms, some of which are tissue-specific. Each isoform has a distinct N-terminus; the remainder of the protein is identical among all the isoforms. A sixth transcript variant has been described, but due to the presence of several stop codons, it is not thought to encode a protein. [provided by RefSeq, Apr 2009]
Structure
HK1 is one of four highly homologous hexokinase isoforms in mammalian cells.
Gene
The HK1 gene spans approximately 131 kb and consists of 25 exons. Alternative splicing of its 5’ exons produces different transcripts in different cell types: exons 1-5 and exon 8 (exons T1-6) are testis-specific exons; exon 6, located approximately 15 kb downstream of the testis-specific exons, is the erythroid-specific exon (exon R); and exon 7, located approximately 2.85 kb downstream of exon R, is the first 5’ exon for the ubiquitously expressed HK1 isoform. Moreover, exon 7 encodes the porin-binding domain (PBD) conserved in mammalian HK1 genes. Meanwhile, the rema |
https://en.wikipedia.org/wiki/HSD3B1 | HSD3B1 is a human gene that encodes for a 3beta-hydroxysteroid dehydrogenase/delta(5)-delta(4)isomerase type I or hydroxy-delta-5-steroid dehydrogenase, 3 beta- and steroid delta-isomerase 1. While it can carry out the same function as HSD3B2, it localizes primarily to different tissues, such as the placenta and nonsteroidogenic tissues. Its requirement for the production of progesterone by the placenta, which has a vital role in pregnancy, may be one reason why no disease based on mutations in this gene has been identified to date, besides prostate cancer.
Clinical significance
The 1245C allele encodes for a missense and hyperactive enzyme that increases extragonadal androgen synthesis and is associated with poorer outcomes after androgen deprivation therapy in prostate cancer.
References
Further reading |
https://en.wikipedia.org/wiki/Bradykinin%20receptor%20B1 | Bradykinin receptor B1 (B1) is a G-protein coupled receptor encoded by the BDKRB1 gene in humans. Its principal ligand is bradykinin, a 9 amino acid peptide generated in pathophysiologic conditions such as inflammation, trauma, burns, shock, and allergy. The B1 receptor is one of two of G protein-coupled receptors that have been found which bind bradykinin and mediate responses to these pathophysiologic conditions.
B1 protein is synthesized de novo following tissue injury and receptor binding leads to an increase in the cytosolic calcium ion concentration, ultimately resulting in chronic and acute inflammatory responses.
Classical agonist of this receptor includes bradykinin1-8 (bradykinin with the first 8 amino acid) and antagonist includes [Leu8]-bradykinin1-8.
Antagonists
LF22-0542
See also
Bradykinin receptor
References
External links
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/LCP1 | Plastin-2 is a protein that in humans is encoded by the LCP1 gene.
Function
Plastins are a family of actin-binding proteins that are conserved throughout eukaryote evolution and expressed in most tissues of higher eukaryotes. In humans, two ubiquitous plastin isoforms (L and T) have been identified. Plastin 1 (otherwise known as fimbrin) is a third distinct plastin isoform which is specifically expressed at high levels in the small intestine. The L isoform is expressed only in hemopoietic cell lineages, while the T isoform has been found in all other normal cells of solid tissues that have replicative potential (fibroblasts, endothelial cells, epithelial cells, melanocytes, etc.). However, L-plastin has been found in many types of malignant human cells of non-hemopoietic origin suggesting that its expression is induced accompanying tumorigenesis in solid tissues.
References
Further reading
EF-hand-containing proteins |
https://en.wikipedia.org/wiki/LMO2 | LIM domain only 2 (rhombotin-like 1), also known as LMO2, RBTNL1, RBTN2, RHOM2, LIM Domain Only Protein 2, TTG2, and T-Cell Translocation Protein 2, is a protein which in humans is encoded by the LMO2 gene.
Function
LMO2 encodes a cysteine-rich, two LIM domain protein that is required for yolk sac erythropoiesis. The LMO2 protein has a central and crucial role in hematopoietic development and is highly conserved.
Clinical significance
Aberrant LMO2 expression is a significant feature of T cell acute lymphoblastic leukaemia with multiple described mechanisms of activation. The LMO2 transcription start site is located approximately 25 kb downstream from the 11p13 T-cell translocation cluster (11p13 ttc), where a number of T-cell acute lymphoblastic leukemia-specific translocations occur. An upstream noncoding DNA element is also the site of recurrent mutations in T cell acute lymphoblastic leukaemia, leading the recruitment of the transcription factor MYB and significant H3K27ac enrichment and thus the formation of an aberrant enhancer which up-regulates the expression of LMO2 Furthermore, recurrent and somatically acquired mutations of LMO2 intron 1 lead to its over-expression in both adult and paediatric T cell acute lymphoblastic leukaemia. These mutations introduce new transcription factor binding sites for MYB, ETS1 and RUNX1 allowing for the formation of an aberrant promoter which drives LMO2 expression.
Interactions
LMO2 has been shown to interact with:
GATA1 |
https://en.wikipedia.org/wiki/MAP3K3 | Mitogen-activated protein kinase kinase kinase 3 is an enzyme that in humans is encoded by the MAP3K3 gene, which is located on the long arm of chromosome 17 (17q23.3).
Function
This gene product is a 626-amino acid polypeptide that is 96.5% identical to mouse MEKK3. Its catalytic domain is closely related to those of several other kinases, including mouse MEKK2, tobacco NPK, and yeast STE11. Northern blot analysis revealed a 4.6-kb transcript that appears to be ubiquitously expressed.
MAP3Ks are involved in regulating cell fate in response to external stimuli. MAP3K3 directly regulates the stress-activated protein kinase (SAPK) and extracellular signal-regulated protein kinase (ERK) pathways by activating SEK and MEK1/2 respectively. In cotransfection assays, it enhanced transcription from a nuclear factor kappa-B (NF-κB)-dependent reporter gene, consistent with a role in the SAPK pathway. Alternatively spliced transcript variants encoding distinct isoforms have been observed. MEKK3 regulates the p38, JNK and ERK1/2 pathways.
Interactions
MAP3K3 has been shown to interact with [SQSTM1/p62],:
BRCA1, AKT.
GAB1,
MAP2K5, and
YWHAE.
MAP3K3 in cancer
Two SNPs in the MAP3K3 gene were found as candidates for association with colon and rectal cancers.
MEKK3 is highly expressed in 4 ovarian cancer cell lines (OVCA429, Hey, DOV13, and SKOv3). This expression level is significantly higher in those cancer cells when compared to normal cells. MEKK3 expression levels are c |
https://en.wikipedia.org/wiki/Melanotransferrin | Melanotransferrin is a protein that in humans is encoded by the MFI2 gene. MFI2 has also recently been designated CD228 (cluster of differentiation 228).
The protein encoded by this gene is a cell-surface glycoprotein found on melanoma cells. The protein shares sequence similarity and iron-binding properties with members of the transferrin superfamily. The importance of the iron binding function has not yet been identified. This gene resides in the same region of chromosome 3 as members of the transferrin superfamily. Alternative splicing results in two transcript variants. It is part of neural crest tissue, often present in melanotic neuroectodermal tumor of infancy.
References
Further reading
External links
Clusters of differentiation
Human proteins |
https://en.wikipedia.org/wiki/Unconventional%20myosin-VI | Unconventional myosin-VI, is a protein that in humans is coded for by MYO6. Unconventional myosin-VI is a myosin molecular motor involved in intracellular vesicle and organelle transport.
Structure
Human myosin-VI contains a N-terminal myosin head domain (residues 59–759), two coiled coil motifs (residues 902–984 and 986–1009 respectively), and a C-terminal myosin VI cargo binding domain (residues 1177–1267).
Function
Unconventional myosin-VI is unique because it travels in the opposite direction of other myosins, towards the negative end of actin filaments. Myosin-VI follows the same structure as other myosin but with two unique "inserts" allowing for its diversified properties. One insert is called the "reverse gear" and is responsible for its movement towards the negative end of actin filaments. The reverse gear is located on the neck region of the myosin and acts as a reorienting device for the lever arm to move backwards after myosin movement. The second insert assists in regulating ATP enzyme activity located in the motor head domain.
There are 3 amino acid binding sites essential for myosin-VI's interactions, Arg-Arg-Leu and Trp-Trp-Tyr in the tail region and Met-Ile-Sec in the helix. The Arg-Arg-Leu amino acid segment (abbreviated RRL) takes part in ubiquitin interactions while Trp-Trp-Tyr (abbreviated WWY) assists in interactions with DAB2. Myosin-VI's Met-Ile-Sec bonding interactions are limited to the myosin-VI long isoform but interact with clathrin in endoc |
https://en.wikipedia.org/wiki/NFKBIB | NF-kappa-B inhibitor beta is a protein that in humans is encoded by the NFKBIB gene.
Function
NFKB1 (MIM 164011) or NFKB2 (MIM 164012) is bound to REL (MIM 164910), RELA (MIM 164014), or RELB (MIM 604758) to form the NFKB complex. The NFKB complex is inhibited by I-kappa-B proteins (NFKBIA, MIM 164008, or NFKBIB), which inactivate NF-kappa-B by trapping it in the cytoplasm. Phosphorylation of serine residues on the I-kappa-B proteins by kinases (IKBKA, MIM 600664 or IKBKB, MIM 603258) marks them for destruction via the ubiquitination pathway, thereby allowing activation of the NF-kappa-B complex. Activated NFKB complex translocates into the nucleus and binds DNA at kappa-B-binding motifs such as 5-prime GGGRNNYYCC 3-prime or 5-prime HGGARNYYCC 3-prime (where H is A, C, or T; R is an A or G purine; and Y is a C or T pyrimidine).[supplied by OMIM]
Interactions
NFKBIB has been shown to interact with:
IKK2,
RELA, and
Retinoid X receptor alpha.
References
Further reading |
https://en.wikipedia.org/wiki/NKX3-1 | Homeobox protein Nkx-3.1, also known as NKX3-1, NKX3, BAPX2, NKX3A and NKX3.1 is a protein that in humans is encoded by the NKX3-1 gene located on chromosome 8p. NKX3-1 is a prostatic tumor suppressor gene.
NKX3-1 is an androgen-regulated, prostate-specific homeobox gene whose expression is predominantly localized to prostate epithelium. It acts as a transcription factor that has critical function in prostate development and tumor suppression. It is a negative regulator of epithelial cell growth in prostate tissue. The NKX3-1 homeobox protein is encoded by the NKX3-1 gene.
Function
The homeodomain-containing transcription factor NKX3A is a putative prostate tumor suppressor that is expressed in a largely prostate-specific and androgen-regulated manner. Loss of NKX3A protein expression is a common finding in human prostate carcinomas and prostatic intraepithelial neoplasia.
Gene
In humans, the NKX3-1 gene is located on chromosome 8p21.2 with 4 exons. The 8p chromosome is a region that is frequently reported to undergo a loss of heterozygosity (LOH) associated with tissue dedifferentiation and loss of androgen responsiveness during the progression of prostate cancer. LOH has been reported to be observed in 12-89% of high-grade prostatic intraepithelial neoplasia (PIN) and 35-86% of prostatic adenocarcinomas. The frequency of loss of heterozygosity on chromosome 8p is seen to increase with advanced prostate cancer grade and stage.
Structure
NKX3-1 contains two exons |
https://en.wikipedia.org/wiki/PPP2CB | Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform is an enzyme that in humans is encoded by the PPP2CB gene.
Function
This gene encodes the phosphatase 2A catalytic subunit. Protein phosphatase 2A is one of the four major Ser/Thr phosphatases, and it is implicated in the negative control of cell growth and division. It consists of a common heteromeric core enzyme, which is composed of a catalytic subunit and a constant regulatory subunit, that associates with a variety of regulatory subunits. This gene encodes a beta isoform of the catalytic subunit. Two transcript variants encoding the same protein have been identified for this gene.
Interactions
PPP2CB has been shown to interact with TLX1, PPP2R1B and PPP2R1A.
See also
PPP2CA
References
Further reading |
https://en.wikipedia.org/wiki/PPP2R5A | Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform is an enzyme that in humans is encoded by the PPP2R5A gene.
Function
The product of this gene belongs to the phosphatase 2A regulatory subunit B family. Protein phosphatase 2A is one of the four major Ser/Thr phosphatases, and it is implicated in the negative control of cell growth and division. It consists of a common heteromeric core enzyme, which is composed of a catalytic subunit and a constant regulatory subunit, that associates with a variety of regulatory subunits. The B regulatory subunit might modulate substrate selectivity and catalytic activity. This gene encodes an alpha isoform of the regulatory subunit B56 subfamily.
Interactions
PPP2R5A has been shown to interact with:
AXIN1,
CTLA-4,
PPP2CA,
PPP2R1A,
PPP2R1B, and
PPP2R5C
References
Further reading |
https://en.wikipedia.org/wiki/RAD23B | UV excision repair protein RAD23 homolog B is a protein that in humans is encoded by the RAD23B gene.
Function
The protein encoded by this gene is one of two human homologs of Saccharomyces cerevisiae Rad23, a protein involved in nucleotide excision repair (NER). This protein was found to be a component of the protein complex that specifically complements the NER defect of xeroderma pigmentosum group C (XP-c) cell extracts in vitro. This protein was also shown to interact with, and elevate the nucleotide excision activity of 3-methyladenine-DNA glycosylase (MPG), which suggested a role in DNA damage recognition in base excision repair. This protein contains an N-terminal ubiquitin-like domain, which was reported to interact with 26S proteasome, and thus this protein may be involved in the ubiquitin mediated proteolytic pathway in cells.
Role in DNA repair
The complex of XPC-RAD23B is the initial damage recognition factor in global genomic nucleotide excision repair (GG-NER). XPC-RAD23B recognizes a wide variety of lesions that thermodynamically destabilize DNA duplexes, including UV-induced photoproducts (cyclopyrimidine dimers and 6-4 photoproducts ), adducts formed by environmental mutagens such as benzo[a]pyrene or various aromatic amines, certain oxidative endogenous lesions such as cyclopurines and adducts formed by cancer chemotherapeutic drugs such as cisplatin. The presence of XPC-RAD23B is required for assembly of the other core NER factors and progression throu |
https://en.wikipedia.org/wiki/Intersectin%201 | Intersectin-1 is a protein that, in humans, is encoded by the ITSN1 gene.
Function
The protein encoded by this gene is a cytoplasmic membrane-associated protein that indirectly coordinates endocytic membrane traffic with the actin assembly machinery. In addition, the encoded protein may regulate the formation of clathrin-coated vesicles and could be involved in synaptic vesicle recycling. This protein has been shown to interact with dynamin, CDC42, SNAP23, SNAP25, SPIN90, EPS15, EPN1, EPN2, and STN2. Multiple transcript variants encoding different isoforms have been found for this gene, but the full-length nature of only two of them have been characterized so far.
Interactions
ITSN1 has been shown to interact with:
CDC42,
SCAMP1
SNAP-25, and
SOS1.
References
Further reading
EH-domain-containing proteins |
https://en.wikipedia.org/wiki/SRD5A1 | 3-Oxo-5α-steroid 4-dehydrogenase 1 is an enzyme that in humans is encoded by the SRD5A1 gene. It is one of three forms of steroid 5α-reductase.
Steroid 5α-reductase (EC 1.3.99.5) catalyzes, among other reactions, the conversion of testosterone into the more potent androgen, 5α-dihydrotestosterone (DHT). The SRD5A1, SRD5A2, and SRD5A3 genes in humans all encode 5α-reductase isozymes.
Function
The 3-oxo-5α-steroid 4-dehydrogenase 1 enzyme is involved in bile acid biosynthesis, androgen and estrogen metabolism. For instance, the enzyme catalyzes the conversion of testosterone into the more potent androgen, 5α-dihydrotestosterone. It can also catalyze the conversion of progesterone, corticosterone or other steroids, to its corresponding 5α-3-oxo-steroids. This chemical reaction is called 5α-reduction, i.e. the reduction of the Δ5-4 double bond in steroids by catalyzing direct hydride transfer from NADPH to the carbon 5 position of the steroid substrate.
Regulation
ETV4 family members bind to ETS DNA-binding sites and both regulate their own expression and the transcription of a subset of genes that are dependent upon testicular luminal fluid factors, including Ggt_pr4, SRD5A1, and Gpx5.
Six-month dietary vitamin E deficiency in rats resulted in a twofold increase in the mRNA level of SRD5A1 gene and a twofold decrease in the mRNA level of GCLM gene but is not directly mediated by changes in promoter DNA methylation.
Insulin increases the expression of 5α-reductase type 1 |
https://en.wikipedia.org/wiki/Artemis%20%28protein%29 | Artemis is a protein that in humans is encoded by the DCLRE1C (DNA cross-link repair 1C) gene.
Function
Artemis is a nuclear protein that is involved in V(D)J recombination and DNA repair. The protein has endonuclease activity on 5' and 3' overhangs and hairpins when complexed with PRKDC.
Immune response
Artemis plays an essential role in V(D)J recombination, the process by which B cell antibody genes and T cell receptor genes are assembled from individual V (variable), D (diversity), and J (joining) segments. For example, in joining a V segment to a D segment, the RAG (recombination activating gene) nuclease cuts both DNA strands adjacent to a V segment and adjacent to a D segment. The intervening DNA between the V and D segments is ligated to form a circular DNA molecule that is lost from the chromosome. At each of the two remaining ends, called the coding ends, the two strands of DNA are joined to form a hairpin structure. Artemis nuclease, in a complex with the DNA-dependent protein kinase (DNA‑PK), binds to these DNA ends and makes a single cut near the tip of the hairpin. The exposed 3' termini are subject to deletion and addition of nucleotides by a variety of exonucleases and DNA polymerases, before the V and D segments are ligated to restore the integrity of the chromosome. The exact site of cleavage of the hairpin by Artemis is variable, and this variability, combined with random nucleotide deletion and addition, confers extreme diversity upon the resul |
https://en.wikipedia.org/wiki/Carbonic%20anhydrase%20III%2C%20muscle%20specific | Carbonic anhydrase 3 is an enzyme that in humans is encoded by the CA3 gene.
Carbonic anhydrase III (CAIII) is a member of a multigene family (at least six separate genes are known) that encode carbonic anhydrase isozymes. These carbonic anhydrases are a class of metalloenzymes that catalyze the reversible hydration of carbon dioxide and are differentially expressed in a number of cell types. The expression of the CA3 gene is strictly tissue-specific and present at high levels in skeletal muscle and much lower levels in cardiac and smooth muscle. CA3 is insufficient in muscles of Myasthenia Gravis patients. A proportion of carriers of Duchenne muscle dystrophy have a higher CA3 level than normal. Autoantibodies to CA3 have been found to be significantly higher in patients with rheumatoid arthritis, systemic lupus erythematosus, and type 1 diabetes. The gene spans 10.3 kb and contains seven exons and six introns.
References
Further reading
External links |
https://en.wikipedia.org/wiki/CEBPD | CCAAT/enhancer-binding protein delta is a protein that in humans is encoded by the CEBPD gene.
Function
The protein encoded by this intronless gene is a bZIP transcription factor which can bind as a homodimer to certain DNA regulatory regions. It can also form heterodimers with the related protein CEBP-alpha. The encoded protein is important in the regulation of genes involved in immune and inflammatory responses, and may be involved in the regulation of genes associated with activation and/or differentiation of macrophages.
Functions
CEBPD is involved in regulation of apoptosis and cell proliferation. It probably acts as tumor suppressor.
One study in mice showed that CEBPD prevents development of tubular injury and tubulointerstitial fibrogenesis during the progression of chronic obstructive nephropathy.
Function of CEBPD gene can be effectively examined by siRNA knockdown based on an independent validation.
Interactions
CEBPD has been shown to interact with Mothers against decapentaplegic homolog 3.
See also
Ccaat-enhancer-binding proteins
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/EGR2 | Early growth response protein 2 is a protein that in humans is encoded by the EGR2 gene. EGR2 (also termed Krox20) is a transcription regulatory factor, containing three zinc finger DNA-binding sites, and is highly expressed in a population of migrating neural crest cells. It is later expressed in the neural crest derived cells of the cranial ganglion. The protein encoded by Krox20 contains two cys2his2-type zinc fingers. Krox20 gene expression is restricted to the early hindbrain development. It is evolutionarily conserved in vertebrates, humans, mice, chicks, and zebra fish. In addition, the amino acid sequence and most aspects of the embryonic gene pattern is conserved among vertebrates, further implicating its role in hindbrain development. When the Krox20 is deleted in mice, the protein coding ability of the Krox20 gene (including the DNA-binding domain of the zinc finger) is diminished. These mice are unable to survive after birth and exhibit major hindbrain defects. These defects include but are not limited to defects in formation of cranial sensory ganglia, partial fusion of the trigeminal nerve (V) with the facial (VII) and auditory (VII) nerves, the proximal nerve roots coming off of these ganglia were disorganized and intertwined among one another as they entered the brainstem, and there was fusion of the glossopharyngeal (IX) nerve complex.
Function
The early growth response protein 2 is a transcription factor with three tandem C2H2-type zinc fingers. Mutatio |
https://en.wikipedia.org/wiki/F2RL2 | Protease activated receptor 3 (PAR-3) also known as coagulation factor II receptor-like 2 (F2RL2) and thrombin receptor-like 2, is a protein that in humans is encoded by the F2RL2 gene.
Function
Coagulation factor II (thrombin) receptor-like 2 (F2RL2) is a member of the large family of 7-transmembrane receptors that couple to G proteins. F2RL2 is also a member of the protease-activated receptor family and activated by thrombin. F2RL2 is activated by proteolytic cleavage of its extracellular amino terminus. The new amino terminus functions as a tethered ligand and activates the receptor. F2RL2 is a cofactor for F2RL3 activation by thrombin. It mediates thrombin-triggered phosphoinositide hydrolysis and is expressed in a variety of tissues.
See also
Protease-activated receptor
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/SYT1 | Synaptotagmin-1 is a protein that in humans is encoded by the SYT1 gene.
Function
Synaptotagmins are integral membrane proteins of synaptic vesicles thought to serve as sensors for calcium ions (Ca2+) in the process of vesicular trafficking and exocytosis. Calcium ion binding to synaptotagmin I participates in triggering neurotransmitter release at the synapse. [Supplied by OMIM]
SYT1 is the master switch responsible for allowing the human brain to release neurotransmitters. SYT1 senses calcium ion concentrations as low as 10 ppm and subsequently signals the SNARE complex to open fusion pores.
Interactions
SYT1 has been shown to interact with SNAP-25, STX1A and S100A13.
Clinical Significance
Mutations in the SYT1 gene cause a rare neurodevelopmental disorder known as SYT1-associated neurodevelopmental disorder (or Baker-Gordon Syndrome).
References
Further reading |
https://en.wikipedia.org/wiki/TSPY1 | Testis-specific Y-encoded protein 1 is a protein that in humans is encoded by the TSPY1 gene.
The protein encoded by this gene is found only in testicular tissue and may be involved in spermatogenesis. Approximately 35 copies of this gene are present in humans, but only a single, nonfunctional orthologous gene is found in mice. Two transcript variants encoding different isoforms have been found for this gene. The protein is strongly overexpressed in gonadoblastoma.
See also
TSPYL1: TSPY1 like protein
References
Further reading |
https://en.wikipedia.org/wiki/Cyclin%20B2 | G2/mitotic-specific cyclin-B2 is a protein that in humans is encoded by the CCNB2 gene.
Function
Cyclin B2 is a member of the cyclin family, specifically the B-type cyclins. The B-type cyclins, B1 and B2, associate with p34cdc2 and are essential components of the cell cycle regulatory machinery. B1 and B2 differ in their subcellular localization. Cyclin B1 co-localizes with microtubules, whereas cyclin B2 is primarily associated with the Golgi region. Cyclin B2 also binds to transforming growth factor beta RII and thus cyclin B2/cdc2 may play a key role in transforming growth factor beta-mediated cell cycle control.
Interactions
Cyclin B2 has been shown to interact with TGF beta receptor 2.
See also
Cyclin B
References
Further reading
Cell cycle regulators |
https://en.wikipedia.org/wiki/Nucleoporin%20153 | Nucleoporin 153 (Nup153) is a protein which in humans is encoded by the NUP153 gene. It is an essential component of the basket of nuclear pore complexes (NPCs) in vertebrates, and required for the anchoring of NPCs. It also acts as the docking site of an importing karyopherin. On the cytoplasmic side of the NPC, Nup358 fulfills an analogous role.
Background
Nuclear pore complexes are extremely elaborate structures that mediate the regulated movement of macromolecules between the nucleus and cytoplasm. These complexes are composed of at least 100 different polypeptide subunits, many of which belong to the nucleoporin family. Nucleoporins are pore complex-specific glycoproteins characterized by cytoplasmically oriented O-linked N-acetylglucosamine residues and numerous repeats of the pentapeptide sequence XFXFG.
Structure
Nucleoporin 153 has a mass of 153 kDA (hence its name). It is filamentous and it contains three distinct domains: a N-terminal region within which a pore targeting domain has been identified, a central region containing multiple zinc finger motifs, and a C-terminal region containing multiple XFXFG repeats.
Interactions
NUP153 has been shown to interact with SENP2 and KPNB1.
References
Further reading
Nuclear pore complex |
https://en.wikipedia.org/wiki/WASF2 | Wiskott–Aldrich syndrome protein family member 2 is a protein that in humans is encoded by the WASF2 gene.
This gene encodes a member of the Wiskott–Aldrich syndrome protein family. The gene product is a protein that forms a multiprotein complex that links receptor kinases and actin. Binding to actin occurs through a C-terminal verprolin homology domain in all family members. The multiprotein complex serves to tranduce signals that involve changes in cell shape, motility or function. The published map location has been changed based on recent genomic sequence comparisons, which indicate that the expressed gene is located on chromosome 1, and a pseudogene may be located on chromosome X.
Interactions
WASF2 has been shown to interact with BAIAP2.
References
Further reading
External links |
https://en.wikipedia.org/wiki/CLEC4M | C-type lectin domain family 4 member M is a protein that in humans is encoded by the CLEC4M gene. CLEC4M has also been designated as CD299 (cluster of differentiation 299).
This gene encodes L-SIGN (liver/lymph node-specific intracellular adhesion molecules-3 grabbing non-integrin), a type II integral membrane protein that is 77% identical to CD209 antigen, an HIV gp120-binding protein. This protein, like CD209, efficiently binds both intercellular adhesion molecule 3 (ICAM3) and HIV-1 gp120, and enhances HIV-1 infection of T cells. This gene is mapped to 19p13.3, in a cluster with the CD209 and CD23/FCER2 genes. Multiple alternatively spliced transcript variants have been found for this gene, but the biological validity of some variants has not been determined.
References
Further reading
External links
Clusters of differentiation |
https://en.wikipedia.org/wiki/PTGES3 | Prostaglandin E synthase 3 (cytosolic) is an enzyme that in humans is encoded by the PTGES3 gene.
The protein encoded by this gene is also known as p23 which functions as a chaperone which is required for proper functioning of the glucocorticoid and other steroid receptors.
References
Further reading |
https://en.wikipedia.org/wiki/METAP2 | Methionine aminopeptidase 2 is an enzyme that in humans is encoded by the METAP2 gene.
Methionine aminopeptidase 2, a member of the dimetallohydrolase family, is a cytosolic metalloenzyme that catalyzes the hydrolytic removal of N-terminal methionine residues from nascent proteins.
peptide-methionine peptide + methionine
MetAP2 is found in all organisms and is especially important because of its critical role in tissue repair and protein degradation. Furthermore, MetAP2 is of particular interest because the enzyme plays a key role in angiogenesis, the growth of new blood vessels, which is necessary for the progression of diseases including solid tumor cancers and rheumatoid arthritis. MetAP2 is also the target of two groups of anti-angiogenic natural products, ovalicin and fumagillin, and their analogs such as beloranib.
Structure
In living organisms, the start codon that initiates protein synthesis codes for either methionine (eukaryotes) or formylmethionine (prokaryotes). In E. coli (prokaryote), an enzyme called formylmethionine deformylase can cleave the formyl group, leaving just the N-terminal methionine residue. For proteins with small, uncharged penultimate N-terminal residues, a methionine aminopeptidase can cleave the methionine residue.
The number of genes encoding for a methionine aminopeptidase varies between organisms. In E. coli, there is only one known MetAP, a 29,333 Da monomeric enzyme coded for by a gene consisting of 264 codons. The knockout of thi |
https://en.wikipedia.org/wiki/ATF6 | Activating transcription factor 6, also known as ATF6, is a protein that, in humans, is encoded by the ATF6 gene and is involved in the unfolded protein response.
Function
ATF6 is an endoplasmic reticulum (ER) stress-regulated transmembrane transcription factor that activates the transcription of ER molecules. Accumulation of misfolded proteins in the Endoplasmic Reticulum results in the proteolytic cleavage of ATF6. The cytosolic portion of ATF6 will move to the nucleus and act as a transcription factor to cause the transcription of ER chaperones.
See also
Activating transcription factor
Interactions
ATF6 has been shown to interact with YY1 and Serum response factor.
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/GABPA | GA-binding protein alpha chain is a protein that in humans is encoded by the GABPA gene.
Function
This gene encodes one of three GA-binding protein transcription factor subunits which functions as a DNA-binding subunit. Since this subunit shares identity with a subunit encoding the nuclear respiratory factor 2 gene, it is likely involved in activation of cytochrome c oxidase expression and nuclear control of mitochondrial function. This subunit also shares identity with a subunit constituting the transcription factor E4TF1, responsible for expression of the adenovirus E4 gene. Because of its chromosomal localization and ability to form heterodimers with other polypeptides, this gene may play a role in the Down syndrome phenotype.
Interactions
GABPA has been shown to interact with Host cell factor C1, Sp1 transcription factor and Sp3 transcription factor.
See also
ETS transcription factor family
GABPB2
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/GFRA1 | GDNF family receptor alpha-1 (GFRα1), also known as the GDNF receptor, is a protein that in humans is encoded by the GFRA1 gene.
Function
Glial cell line-derived neurotrophic factor (GDNF) and neurturin (NTN) are two structurally related, potent neurotrophic factors that play key roles in the control of neuron survival and differentiation. The protein encoded by this gene is a member of the GDNF receptor family. It is a glycosylphosphatidylinositol(GPI)-linked cell surface receptor for both GDNF and NTN, and mediates activation of the RET tyrosine kinase receptor. This gene is a candidate gene for Hirschsprung disease. Two alternatively spliced transcript variants encoding different isoforms have been described for this gene.
Interactions
GDNF family receptor alpha 1 has been shown to interact with GDNF and RET proto-oncogene.
See also
GFRα
References
Further reading
External links |
https://en.wikipedia.org/wiki/GM2A | GM2 ganglioside activator also known as GM2A is a protein which in humans is encoded by the GM2A gene.
Function
The protein encoded by this gene is a small glycolipid transport protein which acts as a substrate specific co-factor for the lysosomal enzyme β-hexosaminidase A. β-hexosaminidase A, together with GM2 ganglioside activator, catalyzes the degradation of the ganglioside GM2, and other molecules containing terminal N-acetyl hexosamines.
GM2A is a lipid transfer protein that stimulates the enzymatic processing of gangliosides, and also T-cell activation through lipid presentation. This protein binds molecules of ganglioside GM2, extracts them from membranes, and presents them to beta-hexosaminidase A for cleavage of N-acetyl-D-galactosamine and conversion to GM3.
It was identified as a member of ML domain family of proteins involved in innate immunity and lipid metabolism in the SMART database.
.
Regulation
In melanocytic cells GM2A gene expression may be regulated by MITF.
Clinical significance
Mutations in this gene, inherited in an autosomal recessive pattern, result in GM2-gangliosidosis, AB variant, a rare GM2 gangliosidosis that has symptoms and pathology identical with Tay–Sachs disease and Sandhoff disease.
GM2A mutations are rarely reported, and the cases that are observed often occur with consanguineous parents or in genetically isolated populations.
Because AB variant is so rarely diagnosed, even in infants, it is likely that most mutations of G |
https://en.wikipedia.org/wiki/HUS1 | Checkpoint protein HUS1 is a protein that in humans is encoded by the HUS1 gene.
Function
The protein encoded by this gene is a component of an evolutionarily conserved, genotoxin-activated checkpoint complex that is involved in the cell cycle arrest in response to DNA damage. This protein forms a heterotrimeric complex with checkpoint proteins RAD9 and RAD1. In response to DNA damage, the trimeric complex interacts with another protein complex consisting of checkpoint protein RAD17 and four small subunits of the replication factor C (RFC), which loads the combined complex onto the chromatin. The DNA damage induced chromatin binding has been shown to depend on the activation of the checkpoint kinase ATM, and is thought to be an early checkpoint signaling event.
In somatic cells
In somatic cells the RAD9-RAD1-HUS1 (9-1-1) complex responds to DNA damage by promoting DNA repair.
In meiosis
In flies, worms and yeast, the 9-1-1 complex is necessary for meiotic checkpoint function and efficient meiotic recombination. During mammalian meiosis 9-1-1 complexes promote synapsis of homologous chromosomes, double-strand break repair and cell cycle checkpoint signalling.
Interactions
HUS1 has been shown to interact with:
HDAC1,
PCNA,
RAD1 homolog
RAD17, and
RAD9A.
References
Further reading |
https://en.wikipedia.org/wiki/Interleukin%2010%20receptor%2C%20alpha%20subunit | Interleukin 10 receptor, alpha subunit is a subunit for the interleukin-10 receptor. IL10RA, is its human gene.
IL10RA has also been designated CDW210A (cluster of differentiation W210A).
Function
The protein encoded by this gene is a receptor for interleukin 10. This protein is structurally related to interferon receptors. It has been shown to mediate the immunosuppressive signal of interleukin 10, and thus inhibits the synthesis of proinflammatory cytokines. This receptor is reported to promote survival of progenitor myeloid cells through the insulin receptor substrate-2/PI 3-kinase/AKT pathway. Activation of this receptor leads to tyrosine phosphorylation of JAK1 and TYK2 kinases.
Interactions
Interleukin 10 receptor, alpha subunit has been shown to interact with:
Interleukin 10 and
Janus kinase 1.
References
Further reading
Clusters of differentiation
Type II cytokine receptors |
https://en.wikipedia.org/wiki/EIF3S6 | Eukaryotic translation initiation factor 3 subunit E (eIF3e) is a protein that in humans is encoded by the EIF3E gene.
Interactions
EIF3S6 has been shown to interact with:
BAT2,
COPS6
CSN3,
EIF3A, and
TRIM27.
See also
Eukaryotic initiation factor 3 (eIF3)
References
Further reading |
https://en.wikipedia.org/wiki/LIG1 | DNA ligase 1 is an enzyme that in humans is encoded by the LIG1 gene. DNA ligase I is the only known eukaryotic DNA ligase involved in both DNA replication and repair, making it the most studied of the ligases.
Discovery
It was known that DNA replication occurred through the breakage of the double DNA strand, but the enzyme responsible for ligating the strands back together, and mechanism of action, was unknown until Lehman, Gellert, Richardson, and Hurwitz laboratories, made significant contributions to the discovery of DNA ligase in 1967.
Recruitment and regulation
The LIG1 gene encodes a, 120kDa enzyme, 919 residues long, known as DNA ligase I. The DNA ligase I polypeptide contains an N-terminal replication factory-targeting sequence (RFTS), followed by a nuclear localization sequence (NLS), and three functional domains. The three domains consist of an N-terminal DNA binding domain (DBD), and catalytic nucleotidyltransferase (NTase), and C-terminal oligonucleotide / oligosaccharide binding (OB) domains. Although the N-terminus of the peptide has no catalytic activity it is needed for activity within the cells. The N-terminus of the protein contains a replication factory-targeting sequence that is used to recruit it to sites of DNA replication known as replication factories.
Activation and recruitment of DNA ligase I seem to be associated with posttranslational modifications. N-terminal domain is completed through phosphorylation of four serine residues on this doma |
https://en.wikipedia.org/wiki/MAGEA1 | Melanoma-associated antigen 1 is a protein that in humans is encoded by the MAGEA1 gene.
This gene is a member of the MAGEA gene family. The members of this family encode proteins with 50 to 80% sequence identity to each other. The promoters and first exons of the MAGEA genes show considerable variability, suggesting that the existence of this gene family enables the same function to be expressed under different transcriptional controls. The MAGEA genes are clustered at chromosomal location Xq28. They have been implicated in some hereditary disorders, such as dyskeratosis congenita.
References
Further reading
External links |
https://en.wikipedia.org/wiki/MCM4 | DNA replication licensing factor MCM4 is a protein that in humans is encoded by the MCM4 gene.
Function
The protein encoded by this gene is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein complex formed by MCM proteins is a key component of the pre-replication complex (pre-RC) and may be involved in the formation of replication forks and in the recruitment of other DNA replication related proteins. The MCM complex consisting of this protein and MCM2, 6 and 7 proteins possesses DNA helicase activity, and may act as a DNA unwinding enzyme. The phosphorylation of this protein by CDC2 kinase reduces the DNA helicase activity and chromatin binding of the MCM complex. This gene is mapped to a region on the chromosome 8 head-to-head next to the PRKDC/DNA-PK, a DNA-activated protein kinase involved in the repair of DNA double-strand breaks. Alternatively spliced transcript variants encoding the same protein have been reported.
See also
Mini Chromosome Maintenance
Interactions
MCM4 has been shown to interact with:
Cell division cycle 7-related protein kinase,
MCM2,
MCM6,
MCM7,
ORC1L,
ORC2L,
ORC3L,
ORC4L,
ORC5L,
ORC6L, and
Replication protein A1.
References
Further reading |
https://en.wikipedia.org/wiki/MT-ATP6 | MT-ATP6 (or ATP6) is a mitochondrial gene with the full name 'mitochondrially encoded ATP synthase membrane subunit 6' that encodes the ATP synthase Fo subunit 6 (or subunit/chain A). This subunit belongs to the Fo complex of the large, transmembrane F-type ATP synthase. This enzyme, which is also known as complex V, is responsible for the final step of oxidative phosphorylation in the electron transport chain. Specifically, one segment of ATP synthase allows positively charged ions, called protons, to flow across a specialized membrane inside mitochondria. Another segment of the enzyme uses the energy created by this proton flow to convert a molecule called adenosine diphosphate (ADP) to ATP. Mutations in the MT-ATP6 gene have been found in approximately 10 to 20 percent of people with Leigh syndrome.
Structure
The MT-ATP6 gene provides information for making a protein that is essential for normal mitochondrial function. The human MT-ATP6 gene, located in mitochondrial DNA, is 681 base pairs in length. An unusual feature of MT-ATP6 is the 46-nucleotide gene overlap of its first codons with the end of the MT-ATP8 gene. With respect to the MT-ATP6 reading frame (+3), the MT-ATP8 gene ends in the +1 reading frame with a TAG stop codon.
The MT-ATP6 protein weighs 24.8 kDa and is composed of 226 amino acids. The protein is a subunit of the F1Fo ATPase, also known as Complex V, which consists of 14 nuclear- and 2 mitochondrial-encoded subunits. As an A subunit, MT-ATP6 is cont |
https://en.wikipedia.org/wiki/RIG-I | RIG-I (retinoic acid-inducible gene I) is a cytosolic pattern recognition receptor (PRR) that can mediate induction of a type-I interferon (IFN1) response. RIG-I is an essential molecule in the innate immune system for recognizing cells that have been infected with a virus. These viruses can include West Nile virus, Japanese Encephalitis virus, influenza A, Sendai virus, flavivirus, and coronaviruses.
RIG-I is an ATP-dependent DExD/H box RNA helicase that is activated by immunostimulatory RNAs from viruses as well as RNAs of other origins. RIG-I recognizes short double-stranded RNA (dsRNA) in the cytosol with a blunt 5' end, 5' tri- or di-phosphate end or a 5' 7-methyl guanosine (m7G) cap (cap-0), but not RNA with a 5' m7G cap having a ribose 2′-O-methyl modification (cap-1). These are often generated during a viral infection but can also be host-derived. Once activated by the dsRNA, the N-terminus caspase activation and recruitment domains (CARDs) migrate and bind with CARDs attached to mitochondrial antiviral signaling protein (MAVS) to activate the signaling pathway for IFN1.
Type-I IFNs have three main functions: to limit the virus from spreading to nearby cells, promote an innate immune response, including inflammatory responses, and help activate the adaptive immune system. Other studies have shown that in different microenvironments, such as in cancerous cells, RIG-I has more functions other than viral recognition. RIG-I orthologs are found in mammals, geese, ducks, |
https://en.wikipedia.org/wiki/PA2G4 | Proliferation-associated protein 2G4 (PA2G4) also known as ErbB3-binding protein 1 (EBP1) is a protein that in humans is encoded by the PA2G4 gene.
Function
This gene encodes an RNA-binding protein that is involved in growth regulation. This protein is present in pre-ribosomal ribonucleoprotein complexes and may be involved in ribosome assembly and the regulation of intermediate and late steps of rRNA processing. This protein can interact with the cytoplasmic domain of the ErbB3 receptor and may contribute to transducing growth regulatory signals. This protein is also a transcriptional corepressor of androgen receptor-regulated genes and other cell cycle regulatory genes through its interactions with histone deacetylases. This protein has been implicated in growth inhibition and the induction of differentiation of human cancer cells. Paradoxically, the expression of EBP1 is decreased in prostate cancer, but increased in Acute Myelogneous Leukemia. Six pseudogenes, located on chromosomes 3, 6, 9, 18, 20 and X, have been identified.
Interactions
PA2G4 has been shown to interact with ERBB3, retinoblastoma protein, and androgen receptor.
References
Further reading |
https://en.wikipedia.org/wiki/PPP1CB | Serine/threonine-protein phosphatase PP1-beta catalytic subunit is an enzyme that in humans is encoded by the PPP1CB gene.
The protein encoded by this gene is one of the three catalytic subunits of protein phosphatase 1 (PP1). PP1 is a serine/threonine specific protein phosphatase known to be involved in the regulation of a variety of cellular processes, such as cell division, glycogen metabolism, muscle contractility, protein synthesis, and HIV-1 viral transcription. Mouse studies suggest that PP1 functions as a suppressor of learning and memory. Two alternatively spliced transcript variants encoding distinct isoforms have been observed.
Interactions
PPP1CB has been shown to interact with PPP1R15A, Nucleolin, SMARCB1 and PPP1R9B.
References
Further reading |
https://en.wikipedia.org/wiki/PPP2R2A | Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform is an enzyme regulator that in humans is encoded by the PPP2R2A gene.
Function
The product of this gene belongs to the phosphatase 2 regulatory subunit B family. Protein phosphatase 2 is one of the four major Ser/Thr phosphatases, and it is implicated in the negative control of cell growth and division. It consists of a common heteromeric core enzyme, which is composed of a catalytic subunit and a constant regulatory subunit, that associates with a variety of regulatory subunits. The B regulatory subunit might modulate substrate selectivity and catalytic activity. This gene encodes an alpha isoform of the regulatory subunit B55 subfamily.
Interactions
PPP2R2A has been shown to interact with:
P70-S6 Kinase 1,
PPP2CA,
PPP2R1A,
PPP2R1B,
TGF beta receptor 1, and
p107.
References
Further reading |
https://en.wikipedia.org/wiki/Syntenin-1 | Syntenin-1 is a protein that in humans is encoded by the SDCBP gene.
Function
The protein encoded by this gene was initially identified as a molecule linking syndecan-mediated signaling to the cytoskeleton. The syntenin protein contains tandemly repeated PDZ domains that bind the cytoplasmic, C-terminal domains of a variety of transmembrane proteins. This protein may also affect cytoskeletal-membrane organization, cell adhesion, protein trafficking, and the activation of transcription factors. The protein is primarily localized to membrane-associated adherens junctions and focal adhesions but is also found at the endoplasmic reticulum and nucleus. Alternative splicing results in multiple transcript variants encoding different isoforms.
Interactions
SDCBP has been shown to interact with:
EFNB1,
GRIK1,
GRIK2,
Interleukin 5 receptor alpha subunit,
Merlin,
RAB5A,
SOX4,
TRAF6,
ULK1. and
ERICH2
References
Further reading |
https://en.wikipedia.org/wiki/ST6GAL1 | Beta-galactoside alpha-2,6-sialyltransferase 1 is an enzyme that in humans is encoded by the ST6GAL1 gene.
The protein encoded by this gene is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. The encoded protein, which is normally found in the Golgi but which can be proteolytically processed to a soluble form, is involved in the generation of the cell-surface carbohydrate determinants and differentiation antigens HB-6, CDw75, and CD76. This protein is a member of glycosyltransferase family 29. Three transcript variants encoding two different isoforms have been found for this gene.
Transcripts of ST6GAL1 are found in mouse high endothelial cells of mesenteric lymph node and Peyer's patches, and it could be involved in the B cell homing to Peyer's patches.
References
Further reading |
https://en.wikipedia.org/wiki/STK4 | Serine/threonine-protein kinase 4 is an enzyme that in humans is encoded by the STK4 gene.
Function
The protein encoded by this gene is a cytoplasmic kinase that is structurally similar to the yeast Ste20p (sterile 20 protein) kinase, which acts upstream of the stress-induced mitogen-activated protein kinase (MAPK) cascade. The encoded protein can phosphorylate myelin basic protein and undergoes autophosphorylation. A caspase-cleaved fragment of the encoded protein has been shown to be capable of phosphorylating histone H2B. The particular phosphorylation catalyzed by this protein has been correlated with apoptosis, and it's possible that this protein induces the chromatin condensation observed in this process.
Interactions
STK4 has been shown to interact with PRKRIR.
STK4 has also been shown to prevent, through Yap1 coactivator modulation, haematological tumor cell apoptosis.
References
Further reading
EC 2.7.11 |
https://en.wikipedia.org/wiki/TAF6 | Transcription initiation factor TFIID subunit 6 is a protein that in humans is encoded by the TAF6 gene.
Function
Initiation of transcription by RNA polymerase II requires the activities of more than 70 polypeptides. The protein that coordinates these activities is transcription factor IID (TFIID), which binds to the core promoter to position the polymerase properly, serves as the scaffold for assembly of the remainder of the transcription complex, and acts as a channel for regulatory signals. TFIID is composed of the TATA-binding protein (TBP) and a group of evolutionarily conserved proteins known as TBP-associated factors or TAFs. TAFs may participate in basal transcription, serve as coactivators, function in promoter recognition or modify general transcription factors (GTFs) to facilitate complex assembly and transcription initiation. This gene encodes one of the smaller subunits of TFIID that binds weakly to TBP but strongly to TAF1, the largest subunit of TFIID. Four isoforms have been identified but complete transcripts have been determined for only three isoforms. One of the isoforms has been shown to preclude binding of one of the other TFIID subunits, thereby reducing transcription and initiating signals that trigger apoptosis.
Interactions
TAF6 has been shown to interact with:
TAF5 and
TATA binding protein.
References
Further reading
External links |
https://en.wikipedia.org/wiki/TAF7 | Transcription initiation factor TFIID subunit 7 also known as TAFII55 is a protein that in humans is encoded by the TAF7 gene.
Function
The intronless gene for this transcription coactivator is located between the protocadherin beta and gamma gene clusters on chromosome 5. The protein encoded by this gene is a component of the TFIID protein complex, a complex which binds to the TATA box in class II promoters and recruits RNA polymerase II and other factors. This particular subunit interacts with the largest TFIID subunit, as well as multiple transcription activators. The protein is required for transcription by promoters targeted by RNA polymerase II.
The general transcription factor, TFIID, consists of the TATA-binding protein (TBP) associated with a series of TBP-associated factors (TAFs) that together participate in the assembly of the transcription preinitiation complex. TAFII55 binds to TAFII250 and inhibits its acetyltransferase activity. The exact role of TAFII55 is currently unknown but studies have shown that it interacts with the C-jun pathway. The conserved region is situated towards the N-terminal of the protein. This entry talks about the N-terminal domain.
Crystallographic studies have revealed a very significant hydrophobic pocket between TAF7 and TAF1, its main binding partner. Due to the incredible hydrophobicity of this interaction, it is unlikely that TAF1 would be able to fold properly without the presence of TAF7. Thus, it is possible that TAF7 is re |
https://en.wikipedia.org/wiki/POLK | DNA polymerase kappa is a DNA polymerase that in humans is encoded by the POLK gene. It is involved in translesion synthesis.
References
Further reading
External links
DNA repair
DNA-binding proteins |
https://en.wikipedia.org/wiki/CBFB | Core-binding factor subunit beta is a protein that in humans is encoded by the CBFB gene.
The protein encoded by this gene is the beta subunit of a heterodimeric core-binding transcription factor belonging to the PEBP2/CBF transcription factor family which master-regulates a host of genes specific to hematopoiesis (e.g., RUNX1) and osteogenesis (e.g., RUNX2). The beta subunit is a non-DNA binding regulatory subunit; it allosterically enhances DNA binding by the alpha subunit as the complex binds to the core site of various enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers and GM-CSF promoters. Alternative splicing generates two mRNA variants, each encoding a distinct carboxyl terminus. In some cases, a pericentric inversion of chromosome 16 [inv(16)(p13q22)] produces a chimeric transcript consisting of the N terminus of core-binding factor beta in a fusion with the C-terminal portion of the smooth muscle myosin heavy chain 11. This chromosomal rearrangement is associated with acute myeloid leukemia of the M4Eo subtype. Two transcript variants encoding different isoforms have been found for this gene.
Mutations in CBFB are implicated in cases of breast cancer.
Core binding factor acute myeloid leukaemia is a cancer related to genetic changes in the CBF gene. It is most commonly caused by an inversion of particular region of chromosome 16; however it can also be caused by translocation between copies of chromosome 16. |
https://en.wikipedia.org/wiki/Cholecystokinin%20A%20receptor | The Cholecystokinin A receptor is a human protein, also known as CCKAR or CCK1, with CCK1 now being the IUPHAR-recommended name.
Function
This gene encodes a G-protein coupled receptor that binds sulfated members of the cholecystokinin (CCK) family of peptide hormones. This receptor is a major physiologic mediator of pancreatic enzyme secretion and smooth muscle contraction of the gallbladder and stomach. In the central and peripheral nervous system this receptor regulates satiety and the release of beta-endorphin and dopamine.
The extracellular, N-terminal, domain of this protein adopts a tertiary structure consisting of a few helical turns and a disulfide-cross linked loop. It is required for interaction of the cholecystokinin A receptor with its corresponding hormonal ligand.
Selective Ligands
Agonists
Cholecystokinin
CCK-4
SR-146,131
A-71623 - modified tetrapeptide, potent and selective CCKA agonist, IC50 3.7nM, 1200x selectivity over CCKB, CAS# 130408-77-4
Antagonists
Proglumide
Lorglumide
Devazepide
Dexloxiglumide
Asperlicin
SR-27897
IQM-95333
JNJ-17156516
See also
Cholecystokinin receptor
Cholecystokinin antagonist
References
External links
Further reading
G protein-coupled receptors
Protein domains
Cholecystokinin receptors |
https://en.wikipedia.org/wiki/ENTPD1 | Ectonucleoside triphosphate diphosphohydrolase-1 (gene: ENTPD1; protein: NTPDase1) also known as CD39 (Cluster of Differentiation 39), is a typical cell surface enzyme with a catalytic site on the extracellular face.
Function
NTPDase1 is an ectonucleotidase that catalyse the hydrolysis of γ- and β-phosphate residues of triphospho- and diphosphonucleosides to the monophosphonucleoside derivative. NTPDase1 hydrolyzes P2 receptor ligands, namely ATP, ADP, UTP and UDP with similar efficacy. NTPDase1 can therefore affect P2 receptor activation and functions.
Clinical significance
ATP causes a pro-inflammatory environment, whereas degradation of ATP into adenosine by the CD39/CD73 pathway leads to an anti-inflammatory environment. CD39 converts ATP (or ADP) to adenosine monophosphate (AMP), which is converted into adenosine by CD73. A substantial portion of the immune suppressive and anti-inflammatory activity of regulatory T cells (Tregs) is due to the adenosine produced by the CD39/CD73 pathway, insofar as Tregs express CD39 and CD73.
Adenosine produced by the CD39/CD73 pathway can protect against ischemia-reperfusion injury. On the other hand, high expression and activity of CD39 and CD73 on cancer cells can prevent the immune system from inhibiting the progression of cancer.
Biallelic pathogenic variant in ENTPD1 causes autosomal recessive spastic paraplegia 64 (SPG64). SPG64 is a complex hereditary spastic paraplegia characterized by childhood onset progressive spastic |
https://en.wikipedia.org/wiki/Henrik%20Bundgaard | Henrik Bundgaard (born 20 March 1975) is a former Danish professional football goalkeeper.
External links
Danish Superliga player statistics at danskfodbold.com
1975 births
Living people
Danish men's footballers
Aabyhøj IF players
AC Horsens players
Aarhus Gymnastikforening players
Danish Superliga players
Brabrand IF players
Men's association football goalkeepers |
https://en.wikipedia.org/wiki/Transformation/transcription%20domain-associated%20protein | Transformation/transcription domain-associated protein, also known as TRRAP, is a protein that in humans is encoded by the TRRAP gene. TRRAP belongs to the phosphatidylinositol 3-kinase-related kinase protein family.
Function
TRRAP is an adaptor protein, which is found in various multiprotein chromatin complexes with histone acetyltransferase activity (HAT), which in turn is responsible for epigenetic transcription activation. TRRAP has a central role in MYC (c-Myc) transcription activation, and also participates in cell transformation by MYC. It is required for p53/TP53-, E2F1-, and E2F4-mediated transcription activation. It is also involved in transcription activation mediated by the adenovirus E1A, a viral oncoprotein that deregulates transcription of key genes.
TRRAP is also required for the mitotic checkpoint and normal cell cycle progression. The MRN complex (composed of MRE11, RAD50, and NBS1) is involved in the detection and repair of DNA double-strand breaks (DSBs). TRRAP associates with the MRN complex and when TRRAP is removed, the complex shows reduced cDNA end-joining activity. Hence, TRRAP may function as a link between DSB repair and chromatin remodeling.
Model organisms
Model organisms have been used in the study of TRRAP function. A conditional knockout mouse line, called Trraptm1a(EUCOMM)Wtsi was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of di |
https://en.wikipedia.org/wiki/NUMB%20%28gene%29 | Protein numb homolog is a protein that in humans is encoded by the NUMB gene. The protein encoded by this gene plays a role in the determination of cell fates during development. The encoded protein, whose degradation is induced in a proteasome-dependent manner by MDM2, is a membrane-bound protein that has been shown to associate with EPS15, LNX1, and NOTCH1. Four transcript variants encoding different isoforms have been found for this gene.
The protein Numb is coded for by the gene, NUMB, whose mechanism appears to be evolutionarily conserved. Numb has been extensively studied in both invertebrates and mammals, though its function is best understood in Drosophila. Numb plays a crucial role in asymmetrical cell division during development, allowing for differential cell fate specification in the central and peripheral nervous systems. During neurogenesis, Numb localizes to one side of the mother cell such that it is distributed selectively to one daughter cell. This asymmetric division allows a daughter cell containing Numb to acquire a different fate than the other daughter cell.
Gene
The numb gene protein product controls binary cell fate decisions in the peripheral and central nervous systems of both invertebrates and mammals during neurogenesis. During cell division, Numb is asymmetrically localized to one end of the progenitor cell and subsequently segregates to only one daughter cell where it intrinsically determines cell fate. Numb protein signaling plays a key rol |
https://en.wikipedia.org/wiki/Neuropilin%202 | Neuropilin 2 (NRP2) is a protein that in humans is encoded by the NRP2 gene.
This gene encodes a member of the neuropilin family of receptor proteins. NRP2 is expressed by a wide variety of cell types. The transmembrane protein has been reported to bind to SEMA3C, SEMA3F, VEGF-A, VEGF-C, VEGF-D, TGFβ, integrins and ANGPTL4 to promote downstream signaling pathways. Consequently, NRP2 is known to play a role in cardiovascular development, axon guidance, tumorigenesis, inflammation and cardiovascular disease. Multiple transcript variants encoding distinct isoforms have been identified for this gene.
References
Further reading |
https://en.wikipedia.org/wiki/IER3 | Radiation-inducible immediate-early gene IEX-1 is a protein that in humans is encoded by the IER3 gene.
This gene functions in the protection of cells from Fas- or tumor necrosis factor type alpha-induced apoptosis. Partially degraded and unspliced transcripts are found after virus infection in vitro, but these transcripts are not found in vivo and do not generate a valid protein.
References
Further reading |
https://en.wikipedia.org/wiki/DNAJA3 | DnaJ homolog subfamily A member 3, mitochondrial, also known as Tumorous imaginal disc 1 (TID1), is a protein that in humans is encoded by the DNAJA3 gene on chromosome 16. This protein belongs to the DNAJ/Hsp40 protein family, which is known for binding and activating Hsp70 chaperone proteins to perform protein folding, degradation, and complex assembly. As a mitochondrial protein, it is involved in maintaining membrane potential and mitochondrial DNA (mtDNA) integrity, as well as cellular processes such as cell movement, growth, and death. Furthermore, it is associated with a broad range of diseases, including neurodegenerative diseases, inflammatory diseases, and cancers.
Structure
As a member of the DNAJ/Hsp40 protein family, DNAJA3 contains a conserved DnaJ domain, which includes an HPD motif that interacts with Hsp70 to perform its cochaperone function. The DnaJ domain is composed of tetrahelical regions containing a tripeptide of histidine, proline and aspartic acid situated between two helices. In addition, this protein contains a glycine/phenylalanine (G/F) rich linker region and a central cysteine-rich region similar to a zinc finger repeat, both characteristic of type I DnaJ molecular chaperones. The mitochondrial targeting sequence at its N-terminal directs the localization of the protein to the mitochondrial matrix.
DNAJA3 possesses two alternatively spliced forms: a long isoform of 43 kDa and a short isoform of 40 kDa. The long isoform contains an additional |
https://en.wikipedia.org/wiki/Glycylpeptide%20N-tetradecanoyltransferase%202 | Glycylpeptide N-tetradecanoyltransferase 2 known also as N-myristoyltransferase, is an enzyme (EC: 2.3.1.97) that in humans is encoded by the NMT2 gene.
Function
N-myristoyltransferase (NMT) catalyzes the reaction of N-terminal myristoylation of many signaling proteins. It transfers myristic acid from myristoyl coenzyme A to the amino group of a protein's N-terminal glycine residue. Biochemical evidence indicates the presence of several distinct NMTs, varying in apparent molecular weight and /or subcellular distribution. The 496-amino acid of human NMT2 protein shares 77% and 96% sequence identity with human NMT1 and mouse Nmt2 comprise two distinct families of N-myristoyltransferases.
Interactions
NMT2 has been shown to interact with:
caspase 3
MARCKS
See also
N-myristoyltransferase 1
References
Further reading
External links
PDBe-KB provides an overview of all the structure information available in the PDB for Human Glycylpeptide N-tetradecanoyltransferase 2 (NMT2) |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.