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https://en.wikipedia.org/wiki/S100A8 | S100 calcium-binding protein A8 (S100A8) is a protein that in humans is encoded by the S100A8 gene. It is also known as calgranulin A.
The proteins S100A8 and S100A9 form a heterodimer called calprotectin.
The protein encoded by this gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100 genes include at least 13 members which are located as a cluster on chromosome 1q21. This protein may function in the inhibition of casein kinase and as a cytokine. Altered expression of this protein is associated with the disease cystic fibrosis and post COVID-19 condition.
References
Further reading
S100 proteins |
https://en.wikipedia.org/wiki/POU%20domain | POU (pronounced 'pow') is a family of eukaryotic transcription factors that have well-conserved homeodomains. The Pou domain is a bipartite DNA binding domain found in these proteins.
Etymology
The acronym POU is derived from the names of three transcription
factors:
the Pituitary-specific Pit-1
the Octamer transcription factor proteins Oct-1 and Oct-2 (octamer sequence is ATGCAAAT)
the neural Unc-86 transcription factor from Caenorhabditis elegans.
Diversity
POU domain genes have been described in organisms as divergent as
Caenorhabditis elegans, Drosophila, Xenopus,
zebrafish and human but have not been yet identified in plants
and fungi.
Comparisons of POU domain genes across the animals suggests that the family can be divided into six major classes (POU1-POU6). Pit-1 is part of the POU1 class, Oct-1 and Oct-2 are members of POU2, while Unc-86 is a member of POU4. The six classes diverged early in animal evolution: POU1, POU3, POU4, and POU6 classes evolved before the last common ancestor of sponges and eumetazoans, POU2 evolved in the Bilatera, and POU5 appears to be unique to vertebrates.
There is a surprisingly high degree of amino acid sequence conservation
(37%-42%) of POU homeodomains to the transcriptional regulator comS, the competence protein from the gram positive prokaryote Bacillus subtilis. Akin to the way that POU homeodomain
regulators lead to tissue differentiation in metazoans, this
transcription factor is critical for differentiation of a |
https://en.wikipedia.org/wiki/Markit | Markit was a British financial information and services company with over 4,000 employees, founded in 2003 as an independent source of credit derivative pricing. The company provides independent data, trade processing of derivatives, foreign exchange and loans, customised technology platforms and managed services. The company aims to enhance transparency, reduce financial risk and improve operational efficiency. Its client base includes institutional participants in the financial marketplace. On 12 July 2016, Markit and IHS Inc. merged in an all-stock merger of equals to form IHS Markit. IHS Markit later merged with S&P Global on 28 February 2022.
Background
Markit was founded in 2003 by Canadian Lance Uggla in St Albans, outside London, as Mark-it Partners to provide daily credit default swap (CDS) pricing.
Markit's credit derivative data sales rose during the subprime mortgage crisis in 2007 and later years.
In September 2009, Markit and Depository Trust & Clearing Corporation (DTCC) launched MarkitSERV, a joint venture to provide over-the-counter (OTC) derivative trade processing.
On 5 May 2014 Markit Ltd., a company registered in Bermuda, filed for an initial public offering (IPO), to be listed on the NASDAQ Global Select Market under the symbol MRKT. The stock began trading on 19 June 2014 with an initial pricing of $24 per share.
Company performance
By 2009 Markit had "1,000 institutions as clients - including investment banks, hedge funds, asset managers, central |
https://en.wikipedia.org/wiki/List%20of%20FC%20Barcelona%20records%20and%20statistics | Futbol Club Barcelona is a professional association football club based in Barcelona, Catalonia, Spain. Founded by a group of Swiss, German, English and Catalan footballers led by Joan Gamper, the club has become a symbol of Catalan culture and Catalanism, hence the motto "Més que un club" (More than a club). The official Barça anthem is the "Cant del Barça", written by Jaume Picas and Josep Maria Espinàs. Unlike many other football clubs, the socis, who are the members and supporters of the club, own and operate Barcelona. It is the world's fourth richest football club in terms of revenue, with an annual turnover of €582.1 million in the 2020–21 season.
Barcelona played its first friendly match on 8 December 1899 against the English colony in Barcelona in the old velodrome in Bonanova. Initially, Barcelona played against other local clubs in various Catalan tournaments. In 1929, the club became one of the founding members of La Liga, Spain's first national league, and has since achieved the distinction of being one of only three clubs to have never been relegated, along with Real Madrid and Athletic Bilbao. Barcelona is also the only European club to have played continental football every season since 1955. They hold a long-standing rivalry with Real Madrid, with matches between the two teams referred to as "El Clásico" (El Clàssic in Catalan). Matches against city rivals Espanyol are known as the "Derbi barceloní".
Barcelona has amassed various records in regional, domest |
https://en.wikipedia.org/wiki/Enthalpy%E2%80%93entropy%20compensation | In thermodynamics, enthalpy–entropy compensation is a specific example of the compensation effect. The compensation effect refers to the behavior of a series of closely related chemical reactions (e.g., reactants in different solvents or reactants differing only in a single substituent), which exhibit a linear relationship between one of the following kinetic or thermodynamic parameters for describing the reactions:
Between the logarithm of the pre-exponential factors (or prefactors) and the activation energies where the series of closely related reactions are indicated by the index , are the preexponential factors, are the activation energies, is the gas constant, and are constants.
Between enthalpies and entropies of activation (enthalpy–entropy compensation) where are the enthalpies of activation and are the entropies of activation.
Between the enthalpy and entropy changes of a series of similar reactions (enthalpy–entropy compensation) where are the enthalpy changes and are the entropy changes.
When the activation energy is varied in the first instance, we may observe a related change in pre-exponential factors. An increase in tends to compensate for an increase in , which is why we call this phenomenon a compensation effect. Similarly, for the second and third instances, in accordance with the Gibbs free energy equation, with which we derive the listed equations, scales proportionately with . The enthalpy and entropy compensate for each other because of th |
https://en.wikipedia.org/wiki/RHO%20protein%20GDP%20dissociation%20inhibitor | RHO protein GDP dissociation inhibitor of Rho proteins (rho GDI) regulates GDP/GTP exchange. The protein plays an important role in the activation of the oxygen superoxide-generating NADPH oxidase of phagocytes. This process requires the interaction of membrane-associated cytochrome b559 with 3 cytosolic components: p47-phox, p67-phox and a heterodimer of the small G-protein p21Rac1 and rho GDI. The association of p21rac and GDI inhibits dissociation of GDP from p21rac, thereby maintaining it in an inactive form. The proteins are attached via a lipid tail on p21rac that binds to the hydrophobic region of GDI. Dissociation of these proteins might be mediated by the release of lipids (e.g., arachidonate and phosphatidate) from membranes through the action of phospholipases. The lipids may then compete with the lipid tail on p21rac for the hydrophobic pocket on GDI.
Human proteins containing this domain
ARHGDIA; ARHGDIB; ARHGDIG;
References
Protein domains
Peripheral membrane proteins |
https://en.wikipedia.org/wiki/John%20LeKay | John LeKay (born 1 June 1961) is an English conceptual and installation artist and sculptor, who lives in New York City. In 1993, he began to make skulls covered in crystal: he has accused Damien Hirst of copying this and other ideas. He publishes the web site, heyokamagazine.
Life and work
John LeKay was born in London. He was educated at Isleworth Polytechnic, London in 1977. He moved to New York in 1991. Instead of higher art education, he travelled with a circus and worked at Pinewood Studios.
1983–1986, he created an installation, Non Terrestrial Black Bird of Paradise, consisting of a taxidermied crow, chairs, chicken wire, glasses and photos: this was exhibited at the Bronx Museum.
Inspired by the early work of Francis Bacon and the painting of a slaughtered ox by Rembrandt, he made a “meat series”, 1986–87. An example of this is the 1987 sculpture, This is my Body this is my Blood, consisting of a cut open decapitated lamb carcass, nailed to a piece of plywood. His 1987 sculpture, Wind pipe, was a double bed with a varnished sewer pipe on it.
In 1990, he held his first solo exhibition, at the Paula Allen Gallery, New York. Exhibits included a sensory deprivation tank, and also a large tape recorder, whose microphone was placed inside a sound-proofed acrylic glass box in order to record the sound of silence. Another sculpture subtitled Vanishing Object, was a cross made out of closet freshener, which slowly evaporated in a tall acrylic glass vitrine. Roberta |
https://en.wikipedia.org/wiki/Cation%20channel%20superfamily | The transmembrane cation channel superfamily was defined in InterPro and Pfam as the family of tetrameric ion channels. These include the sodium, potassium, calcium, ryanodine receptor, HCN, CNG, CatSper, and TRP channels. This large group of ion channels apparently includes families , , , and of the TCDB transporter classification.
They are described as minimally having two transmembrane helices flanking a loop which determines the ion selectivity of the channel pore. Many eukaryotic channels have four additional transmembrane helices (TM) (), related to or vestigial of voltage gating. The proteins with only two transmembrane helices () are most commonly found in bacteria. This also includes the 2-TM inward-rectifier potassium channels () found primarily in eukaryotes. There are commonly additional regulatory domains which serve to regulate ion conduction and channel gating. The pores may also be homotetramers or heterotetramers; where heterotetramers may be encoded as distinct genes or as multiple pore domains within a single polypeptide. The HVCN1 and Putative tyrosine-protein phosphatase proteins do not contain an expected ion conduction pore domain, but rather have homology only to the voltage sensor domain of voltage gated ion channels.
Human channels with 6 TM helices
Cation
Transient receptor potential
Canonical
TRPC1; TRPC3; TRPC4; TRPC5; TRPC6; TRPC7
Melastatin
TRPM1; TRPM2; TRPM3; TRPM4; TRPM5; TRPM6; TRPM7; TRPM8
Vanilloid
TRPV1; TRPV2; TRPV3; TR |
https://en.wikipedia.org/wiki/Imaginary%20Landscape%20No.%201 | Imaginary Landscape No. 1 is a composition for records of constant and variable frequency, large chinese cymbal and string piano by American composer John Cage and the first in the series of Imaginary Landscapes. It was composed in 1939.
Composition
John Cage wrote this composition while he was living in Seattle, earning money by making music for dancers, such as Music for an Aquatic Ballet. Having studied for some time with Arnold Schoenberg in the past drew him closer to serial organization into his studies regarding temporal structure. In Seattle, he had the chance to experiment with the different possibilities of the prepared piano, which allowed him to create new percussive sonorities without having to use several instruments and performers. At this time, Henry Cowell, a pioneer in advanced avant-garde techniques for the piano (such as plucking the strings from the inside, using clusters, etc.), was his mentor. However, even though percussion was fairly established in the 30s (Ionisation, considered a historical breakthrough work, was composed in 1930), electric equipment used in musical performance was rare and largely unexplored.
Cage was working in a radio studio when he started working on this piece, which was meant to be a short piece of music as part of the accompaniment to a performance of Jean Cocteau's Les mariés de la tour Eiffel. The piece was never meant to be performed on-site but was rather meant to be either recorded or broadcast. However, as most mate |
https://en.wikipedia.org/wiki/GRAM%20domain | The GRAM domain is found in glucosyltransferases, myotubularins and other membrane-associated proteins. The structure of the GRAM domain is similar to that found in PH domains.
Proteins containing GRAM domains are found in all eukaryotes and bacteria, but not archaea. Various GRAM domains can bind proteins or lipids.
Human proteins containing this domain
GRAMD1A; GRAMD1B; GRAMD1C; GRAMD2A; GRAMD2B; GRAMD4; MTM1; MTMR1; MTMR2; NCOA7; NSMAF; OXR1; SBF1; SBF2; TBC1D8; TBC1D8B; TBC1D9; TBC1D9B; WBP2; WBP2NL; dJ439F8.1;
References
Protein domains
Protein families
Peripheral membrane proteins |
https://en.wikipedia.org/wiki/Ch%C3%A2teau%20La%20Tour%20Blanche | Château La Tour Blanche, or La Tour-Blanche, is a sweet white wine ranked as Premier Cru Classé (French, “First Growth”) in the original Bordeaux Wine Official Classification of 1855. Belonging to the Sauternes appellation in Gironde, in the region of Graves, the winery is located in the commune of Bommes.
Uniquely among classed growth wineries, the estate is the property of the French state, and the site of the La Tour Blanche School of Viticulture and Oenology.
History
Records date the estate's origins to the 18th century, and connect them to Jean Saint-Marc du Latourblanche, treasurer-general to Louis XIV. Following the French Revolution, the estate was owned by Pierre Pécherie, but a later owner, the German Frederic Focke raised the reputation of the winery, and was for a period credited with bringing the tradition of sweet white wine to Sauternes from his Rhine origins. After the rewarding outcome of the 1855 Classification and Focke's death, the estate was eventually acquired by Daniel "Osiris" Iffla who among several patriotic acts, testamented La Tour Blanche to the State upon his death in 1907, on the condition it would become an agricultural college. From 1911, the La Tour Blanche School of Viticulture and Oenology has been responsible for education and training of wine industry professionals, as well as running La Tour Blanche as a classed winery.
Production
The estate contains 65 hectares with grape varieties of 83% Sémillon, 12% Sauvignon blanc and 5% Muscade |
https://en.wikipedia.org/wiki/Ch%C3%A2teau%20Carbonnieux | Château Carbonnieux is a Bordeaux wine estate located in the Pessac-Léognan region of the Graves. The estate was one of the first estates included in the Graves wine classification and is known for its red and white wine production.
Chateau Carbonnieux has two Graves classifications for both its red and white wines. These are Grand Cru Classé and Grand Vin de Graves. The red wines are the Bordeaux blend of Cabernet Sauvignon, Merlot and Cabernet Franc. Petit Verdot is used for structure for the Grand Vin but not for the Grand Cru Classé. The white wine is a blend of Sauvignon Blanc and Semillon.
Historically, Chateau Carbonnieux was better known for its white wines than its reds.
Wines
In addition to the main wines, Carbonnieux produces two second wines: La Croix de Carbonnieux, made from the same plots as the grand vin; and Château Tour Léognan, made from young vines.
References
External links
Bordeaux wine producers |
https://en.wikipedia.org/wiki/Ch%C3%A2teau%20de%20Rayne-Vigneau | Château de Rayne-Vigneau is a sweet white wine ranked as Premier Cru Classé (French, “First Growth”) in the original Bordeaux Wine Official Classification of 1855. Belonging to the Sauternes appellation in Gironde, in the region of Graves, the winery is located in Bommes. It has been owned by Crédit Agricole since 2004.
The castle, its park with its facilities are the subject of a classification as historic monuments by decree of 19 April 2004.
In 2015, the estate is bought by the group Trésor du Patrimoine.
References
Bordeaux wine producers
Monuments historiques of Gironde |
https://en.wikipedia.org/wiki/Ch%C3%A2teau%20Suduiraut | Château Suduiraut, formerly Cru du Roy and Château de Suduiraut, is a sweet white wine ranked as Premier Cru Classé (French, “First Growth”) in the original Bordeaux Wine Official Classification of 1855. Belonging to the Sauternes appellation in Gironde, in the region of Graves, the winery is located in Preignac, adjacent to Château d'Yquem.
See also
Château Raymond-Lafon
References
External links
Château Suduiraut official site
Bordeaux wine producers |
https://en.wikipedia.org/wiki/Ch%C3%A2teau%20Guiraud | Château Guiraud is a sweet white wine ranked as Premier Cru Classé (French, “First Growth”) in the original Bordeaux Wine Official Classification of 1855. Belonging to the Sauternes appellation in Gironde, in the region of Graves, the winery is located in the commune of Sauternes. The estate vine plantings consist of 65% Semillon and 35% Sauvignon Blanc. The vines are on average 35–40 years old.
References
External links
Château Guiraud official site
Bordeaux wine producers |
https://en.wikipedia.org/wiki/Ch%C3%A2teau%20Rieussec | Château Rieussec is a sweet white wine ranked as Premier Cru Classé (French, “First Growth”) in the original Bordeaux Wine Official Classification of 1855. Belonging to the Sauternes appellation in Gironde, in the region of Graves, the winery is located in the commune of Fargues.
History
The Rieussec estate was the property of the monks of Carmes de Langon in the 18th century. Following the French revolution, church property was confiscated by the state and auctioned off. In about 1790, Rieussec was bought in this fashion by a Mr. Marheilhac, who at this time was also the owner of Château La Louvière in Léognan. The owner at the time of the 1855 classification, when Rieussec was classified a first growth, was a Mr. Mayne. After that, Rieussec had a long succession of owners: Charles Crepin bought in around 1870, Paul Defolie in 1892, Mr. Edgar Bannel a well known banker of Bordeaux in 1907, the Gasqueton family (also owners of Château Calon-Ségur in Saint Estèphe), the American P. F. Berry (brother-in-law of the Vicomte de Bouzet) during the war, Mr. Balaresque in 1957 and Albert Vuillier in 1971.
In 1984, Rieussec was bought by Domaines Barons de Rothschild, the owners of Château Lafite Rothschild. The Rothschilds invested in a new cellar in 1989, and strove to increase quality by better selection of the grapes, which also led to reduced production in the 1990s. In the 1993 vintage, one of three difficult Bordeaux vintages in a row, no Château Rieussec grand vin was produc |
https://en.wikipedia.org/wiki/Endonuclease/Exonuclease/phosphatase%20family | Endonuclease/Exonuclease/phosphatase family is a structural domain found in the large family of proteins including magnesium dependent endonucleases and many phosphatases involved in intracellular signaling.
Examples
AP endonuclease proteins ,
DNase I proteins ,
Synaptojanin, an inositol-1,4,5-trisphosphate phosphatase
Sphingomyelinase
Nocturnin, an NADPH 2' phosphatase
Subfamilies
Inositol polyphosphate related phosphatase
Human proteins containing this domain
2'-PDE; 2-PDE; ANGEL1; ANGEL2; APEX1; APEX2; CCRN4L; CNOT6;
CNOT6L; DNASE1; DNASE1L1; DNASE1L2; DNASE1L3; INPP5A; INPP5B; INPP5D;
INPP5E; INPPL1; KIAA1706; OCRL; PIB5PA; SKIP; SMPD2; SMPD3;
SYNJ1; SYNJ2; TTRAP; Nocturnin;
Notes
References
Protein domains
Peripheral membrane proteins
EC 3.1.3 |
https://en.wikipedia.org/wiki/Ch%C3%A2teau%20Doisy-Dubroca | Château Doisy-Dubroca is a sweet white wine, ranked as Second Cru Classé (French, “Second Growth”), in the original Bordeaux Wine Official Classification of 1855. Belonging to the Sauternes appellation in Gironde, in the region of Graves, the winery is located in the commune of Barsac, Gironde.
Notes and references
External links
Château Doisy Daëne official site
Bordeaux wine producers |
https://en.wikipedia.org/wiki/Ch%C3%A2teau%20Doisy-V%C3%A9drines | Château Doisy-Védrines is a sweet white wine ranked as Second Cru Classé (French, “Second Growth”) in the original Bordeaux Wine Official Classification of 1855. Belonging to the Sauternes appellation in Gironde, in the region of Graves, the winery is located in the commune of Barsac.
References
External links
Doisy-Védrines official site
Bordeaux wine producers |
https://en.wikipedia.org/wiki/Ch%C3%A2teau%20d%27Arche | Château d'Arche is a sweet white wine ranked as Second Cru Classé (French, “Second Growth”) in the original Bordeaux Wine Official Classification of 1855. Belonging to the Sauternes appellation in Gironde, in the region of Graves, the winery is located in the commune of Sauternes.
History
One of three estates within the Sauternes commune that was rated second growth in the Classification of 1855, situated on a favourable ridge location, Château d'Arche is named for the Comte d'Arche, owner of the estate from 1733 to 1789. Under Comte d'Arche the estate held a high reputation, and its placement in the 1855 classification's second tier is considered due to the divisions of the estate that followed the French Revolution, and the subsequent drop in quality from the level of the 1780s.
In 1981 the property was leased by INAO president Pierre Perromat, who sought to make improvements to the standard of production. With the arrival of Perromat, production of the formerly widely known second wine d'Arche-Lafaurie ceased, bearing the name of former share-owner Lafaurie of Château Lafaurie-Peyraguey.
In 2009, d'Arche began a campaign of bottling wine in a 100ml test-tube shaped bottle, in an effort to target young drinkers in nightclubs.
Production
The vineyards measure , with a grape variety distribution of 90% Sémillon, 10% Sauvignon blanc.
The estate produces the second wine, Prieuré d'Arche, a choice reserve wine, Chateau d'Arche Lafaurie, as well as dry white and red bottling |
https://en.wikipedia.org/wiki/Ch%C3%A2teau%20Broustet | Château Broustet is a sweet white wine ranked as Second Cru Classé (French, "Second Growth") in the original Bordeaux Wine Official Classification of 1855. Belonging to the Sauternes appellation in Gironde, in the region of Graves, the winery is located in the commune of Barsac.
References
External links
Château Broustet official site
Bordeaux wine producers |
https://en.wikipedia.org/wiki/Ch%C3%A2teau%20Nairac | Château Nairac is a sweet white wine ranked as Second Cru Classé (French, “Second Growth”) in the original Bordeaux Wine Official Classification of 1855. Belonging to the Sauternes appellation in Gironde, in the region of Graves, the winery is located in the commune of Barsac.
Further reading
Bordeaux wine producers |
https://en.wikipedia.org/wiki/Ch%C3%A2teau%20Caillou | Château Caillou is a sweet white wine ranked as Second Cru Classé (French, "Second Growth") in the original Bordeaux Wine Official Classification of 1855. Belonging to the Sauternes appellation in Gironde, in the region of Graves, the winery is located in the commune of Barsac.
References
External links
Château Caillou official site
Bordeaux wine producers |
https://en.wikipedia.org/wiki/Ch%C3%A2teau%20Suau | Château Suau is a sweet white wine ranked as Second Cru Classé (French, “Second Growth”) in the original Bordeaux Wine Official Classification of 1855. Belonging to the Sauternes appellation in Gironde, in the region of Graves, the winery is located in the commune of Barsac.
Not to be confused with Château Suau (Capian) located in the commune of Capian.
References
Bordeaux wine producers |
https://en.wikipedia.org/wiki/Ch%C3%A2teau%20de%20Malle | Château de Malle is a sweet white wine ranked as Second Cru Classé (French, "Second Growth") in the original Bordeaux Wine Official Classification of 1855. Belonging to the Sauternes appellation in Gironde, in the region of Graves, the winery is located in the commune of Sauternes. The gardens of the chateau are classified among the Notable Gardens of France by the Committee of Parks and Gardens of the French Ministry of Culture.
History
The estate has, over the centuries, known numerous trials and tribulations. Both good and bad fortune. The Château was not inhabited regularly for practically two generations. In the early fifties Pierre de Bournazel took over the property inherited from his uncle and godfather, Pierre de Lur-Saluces. He was a man possessed by a love of the land and of stone and he decided to re-instil life into the buildings and vineyards which undeniably were in a state of considerable neglect. He rebuilt the fermentation cellar, studied estate management, followed a course in oenology and together, with the help of his wife, made it a point of honour to re-establish the initial shape and form of the rooms of the Château whilst retaining their original appearance.
In 1956 he replanted the entire vineyard which had been destroyed by frost. Pierre de Bournazel became, as time went by, a major figure in the viticultural world of Bordeaux.
He became the president of the Classified Growth Association of Sauternes and Barsac and in 1959 created the “Commanderie |
https://en.wikipedia.org/wiki/Ch%C3%A2teau%20Romer | Château Romer is a sweet white wine ranked as Second Cru Classé (French, “Second Growth”) in the original Bordeaux Wine Official Classification of 1855. Belonging to the Sauternes appellation in Gironde, in the region of Graves, the estate is located in the commune of Fargues de Langon.
History
The wine estate was probably founded already in the 17th century by the Montalier family, and shares its early history with that of Château Romer du Hayot. In the year 1800, Ferdinand Auguste de Lur-Saluces married a descendant of the founders, Marie Thérèse Gabrielle de Montalier, which for a time made the estate part of the wine empire of the Lur-Saluces family. In 1824, their daughter Louise Alexandrine married Count Anne Auguste Jacques de la Myre-Mory. In 1855, the year of the classification of Bordeaux wine, the estate was named Château Romer, and was classified as a second growth.
In 1881, due to inheritance, the estate was divided in several smaller lots that were passed down to members of the Myre-Mory family. However, the different lots were managed together by one of the inheritors, Comtesse Beaurepaire-Louvagny. In 1911, about of the estate was sold by Myre-Mory to Roger Farges, and this land forms the basis of the current Château Romer which stayed in the Farges family for the next century. Th remaining to were sold in 1937 to Xavier Dauglade and Madame du Hayot, forming Château Romer du Hayot.
Later, the Farges family did not put much emphasis on winemaking. From 19 |
https://en.wikipedia.org/wiki/Saposin%20protein%20domain | The saposin domains refers to two evolutionally-conserved protein domains found in saposin and related proteins (SAPLIP). Saposins are small lysosomal proteins that serve as activators of various lysosomal lipid-degrading enzymes. They probably act by isolating the lipid substrate from the membrane surroundings, thus making it more accessible to the soluble degradative enzymes. All mammalian saposins are synthesized as a single precursor molecule (prosaposin) which contains four Saposin-B domains, yielding the active saposins after proteolytic cleavage, and two Saposin-A domains that are removed in the activation reaction.
The Saposin-B domains also occur in other proteins, most of them playing a role in interacting with membranes.
Classification
The saposin (SapB1-SapB2) domains are found in a wide range of proteins. Each half-domain encodes two alpha helices in the SapB domain for a total of four.
The mamallian prosaposin (domain organization below) is a prototypic family member. It also includes the N- and C-terminal SapA domains, both of which are proteolyticly cleaved as the proprotein matures. Four connected pairs of SapB1-SapB2 domains are released, sequentially named Saposin-A through D. Some closely related proteins, such as PSAPL1 and SFTPB, share the architecture and the cleaving mechanism in whole or in part. While Prosaposin and PSAPL1 act in lysosomal lipid degradation, SFTPB is released into the pulmonary surfactant, playing a role in rearranging lipids.
H |
https://en.wikipedia.org/wiki/Ch%C3%A2teau%20Lamothe | Château Lamothe is a sweet white wine ranked as Second Cru Classé (French, “Second Growth”) in the original Bordeaux Wine Official Classification of 1855. Belonging to the Sauternes appellation in Gironde, in the region of Graves, the winery is located in the commune of Sauternes.
References
Bordeaux wine producers |
https://en.wikipedia.org/wiki/Major%20facilitator%20superfamily | The major facilitator superfamily (MFS) is a superfamily of membrane transport proteins that facilitate movement of small solutes across cell membranes in response to chemiosmotic gradients.
Function
The major facilitator superfamily (MFS) are membrane proteins which are expressed ubiquitously in all kingdoms of life for the import or export of target substrates. The MFS family was originally believed to function primarily in the uptake of sugars but subsequent studies revealed that drugs, metabolites, oligosaccharides, amino acids and oxyanions were all transported by MFS family members. These proteins energetically drive transport utilizing the electrochemical gradient of the target substrate (uniporter), or act as a cotransporter where transport is coupled to the movement of a second substrate.
Fold
The basic fold of the MFS transporter is built around 12, or in some cases, 14 transmembrane helices (TMH), with two 6- (or 7- ) helix bundles formed by the N and C terminal homologous domains of the transporter which are connected by an extended cytoplasmic loop. The two halves of the protein pack against each other in a clam-shell fashion, sealing via interactions at the ends of the transmembrane helices and extracellular loops. This forms a large aqueous cavity at the center of the membrane, which is alternatively open to the cytoplasm or periplasm/extracellular space. Lining this aqueous cavity are the amino-acids which bind the substrates and define transporter specifi |
https://en.wikipedia.org/wiki/Stannin | Stannins are small proteins that consist of a single transmembrane helix, an unstructured linker domain, and a cytoplasmic domain. The transmembrane region contains a conserved cysteine residue (Cys32) that, together with Cys34 found in the stannin unstructured linker domain, constitutes the putative trimethyltin-binding site, close to the lipid/solvent interface.
The unstructured protein region connects two adjacent helical domains. It contains a conserved CXC metal-binding motif and a putative 14-3-3-zeta binding domain. Upon coordinating dimethytin, considerable structural or dynamic changes in the flexible loop region of SNN may take place, recruiting other binding partners such as 14-3-3-zeta, and thereby initiating the apoptotic cascade.
The cytoplasmic domain forms a distorted helix that is partially absorbed into the plane of the lipid bilayer. It interacts with the surface of the lipid bilayer, and contributes to the initiation of the apoptotic cascade on binding of the unstructured linker domain to dimethyltin.
Human proteins containing this domain
SNN;
References
Protein domains
Single-pass transmembrane proteins |
https://en.wikipedia.org/wiki/%C3%82nderson%20Lima%20%28footballer%2C%20born%201973%29 | Ânderson Lima Veiga (born March 18, 1973), or simply Ânderson Lima, is a Brazilian football midfielder. He is well known as being a free-kick specialist in Brazil.
Club statistics
Honours
Brazil
South American Under-17 Championship: 1988
South American Under-20 Championship: 1991
Santos
Torneio Rio-São Paulo: 1997
Copa Conmebol: 1998
Grêmio
Copa do Brasil: 2001
Campeonato Gaúcho: 2001
São Caetano
Campeonato Paulista: 2004
Coritiba
Campeonato Brasileiro Série B: 2007
References
External links
1973 births
Living people
Brazilian men's footballers
Brazilian expatriate men's footballers
Expatriate men's footballers in Japan
Campeonato Brasileiro Série A players
Campeonato Brasileiro Série B players
J1 League players
São Paulo state football team players
Clube Atlético Juventus players
Guarani FC players
Santos FC players
São Paulo FC players
Grêmio Foot-Ball Porto Alegrense players
Associação Desportiva São Caetano players
Albirex Niigata players
Coritiba Foot Ball Club players
Operário Futebol Clube (MS) players
Clube Atlético Bragantino players
Associação Chapecoense de Futebol players
Brazil men's youth international footballers
Men's association football midfielders
Footballers from São Paulo |
https://en.wikipedia.org/wiki/Nucleoside-specific%20porin | Nucleoside-specific porin (the tsx gene of Escherichia coli) is an outer membrane protein, Tsx, which constitutes the receptor for colicin K and Bacteriophage T6, and functions as a substrate-specific channel for nucleosides and deoxy-nucleosides.<ref
name="PUB00006257"></ref> The protein contains 294 amino acids, the first 22 of which are characteristic of a bacterial signal sequence peptide. Tsx shows no significant similarities to general bacterial porins.
References
Protein domains
Protein families
Outer membrane proteins |
https://en.wikipedia.org/wiki/Griffithsin | Griffithsin is a protein isolated from the red algae Griffithsia. It has a 121-amino acid sequence which exhibits a Jacalin-like lectin fold. Several structures of this protein have been solved by X-ray crystallography and deposited in the PDB. It has been shown in vitro to be a highly potent HIV entry inhibitor. It is currently being investigated as a potential microbicide for use in the prevention of the transmission of HIV.
Griffithsin shows a broad spectrum ability to bind to the glycoproteins of other viruses, such as the coronavirus. Griffithsin's three identical carbohydrate binding sites bind to oligosaccharides present on some envelopes of viral glycoproteins. This was demonstrated by in vitro and in vivo studies. For instance, it was shown that griffithsin binds to the SARS-CoV spike glycoprotein to inhibit entry of the SARS virus and thus inhibit infection. A 2014 study showed griffithsin to also possess useful antiviral activity against Ebolavirus.
As reported in March 2009, Kenneth Palmer and coworkers modified the tobacco mosaic virus to incorporate the griffithsin gene and infected more than 9,300 tobacco plants. They were able to extract enough griffithsin to produce about 100,000 HIV microbicide doses from the leaves.
References
Eukaryote proteins
Entry inhibitors |
https://en.wikipedia.org/wiki/Protein%20diet | Protein diet may refer to:
High-protein diet
Low-protein diet |
https://en.wikipedia.org/wiki/5-Hydroxyeicosatetraenoic%20acid | 5-Hydroxyeicosatetraenoic acid (5-HETE, 5(S)-HETE, or 5S-HETE) is an eicosanoid, i.e. a metabolite of arachidonic acid. It is produced by diverse cell types in humans and other animal species. These cells may then metabolize the formed 5(S)-HETE to 5-oxo-eicosatetraenoic acid (5-oxo-ETE), 5(S),15(S)-dihydroxyeicosatetraenoic acid (5(S),15(S)-diHETE), or 5-oxo-15-hydroxyeicosatetraenoic acid (5-oxo-15(S)-HETE).
5(S)-HETE, 5-oxo-ETE, 5(S),15(S)-diHETE, and 5-oxo-15(S)-HETE, while differing in potencies, share a common mechanism for activating cells and a common set of activities. They are therefore a family of structurally related metabolites. Animal studies and a limited set of human studies suggest that this family of metabolites serve as hormone-like autocrine and paracrine signalling agents that contribute to the up-regulation of acute inflammatory and allergic responses. In this capacity, these metabolites may be members of the innate immune system.
In vitro studies suggest that 5(S)-HETE and/or other of its family members may also be active in promoting the growth of certain types of cancers, in simulating bone reabsorption, in signaling for the secretion of aldosterone and progesterone, in triggering parturition, and in contributing to other responses in animals and humans. However, the roles of 5(S)-HETE family members in these responses as well as in inflammation and allergy are unproven and will require much further study.
Among the 5(S)-HETE family members, 5(S)-H |
https://en.wikipedia.org/wiki/China%20Girl%20%281942%20film%29 | China Girl is a 1942 drama film which follows the exploits of an American newsreel photographer in China and Burma against the backdrop of World War II. The film stars Gene Tierney, George Montgomery, Lynn Bari and Victor McLaglen, and was directed by Henry Hathaway. It is also known as A Yank In China, Burma Road and Over The Burma Road.
Plot summary
In Luzhou, China, news cameraman Johnny Williams (George Montgomery) is taken into custody by the Japanese military. He is offered $20,000 to take pictures of the Burma Road, a vital link for Allied supply that had been built to support the Chinese war effort. He isn't interested.
Johnny is put back into his cell, together with a Canadian, "Major" Bull Weed (Victor McLaglen), who claims to be serving as a Chinese irregular. His confederate, 'Captain' Fifi (Lynn Bari), smuggles a gun in during a faked tempestuous farewell, and the two men escape.
They rendezvous with Fifi, who says she saw a plane nearby at an abandoned airfield. Johnny, an ex-barnstormer expert at flying biplanes, pilots them all through a hail of Burmese anti-aircraft fire to safety in Mandalay. Upon their arrival, he bumps into his old pal, Captain Shorty Maguire (Myron McCormick), a mercenary pilot with the U.S. staffed "Flying Tigers" defending China against the Japanese.
Johnny is asked to join up, but again declines to take sides. He discovers that instead of grabbing his confiscated press credentials while fleeing Luchow, the document he picked up is |
https://en.wikipedia.org/wiki/Vocal%20resonation | Vocal resonance may be defined as "the process by which the basic product of phonation is enhanced in timbre and/or intensity by the air-filled cavities through which it passes on its way to the outside air." Throughout the vocal literature, various terms related to resonation are used, including: amplification, filtering, enrichment, enlargement, improvement, intensification, and prolongation. Acoustic authorities would question many of these terms from a strictly scientific perspective. However, the main point to be drawn from these terms by a singer or speaker is that the result of resonation is to make a better sound, or at least suitable to a certain esthetical and practical domain.
Human resonating chambers
The voice, like all acoustic instruments such as the guitar, trumpet, piano, or violin, has its own special chambers for resonating the tone. Once the tone is produced by the vibrating vocal cords, it vibrates in and through the open resonating ducts and chambers. Since the vocal tract is often associated with different regions of the body, different resonance chambers might be referred to as: chest, mouth, nose/"mask", or head.
In more symbolic/perceptual way, rather than physical, the various terms applied can represent vocal "colors" in a continuous scale: from dark (chest) resonance to bright (head-nasal) resonance. We may call this spectrum a resonance track. In the lower range, the chest/dark color predominates; in the middle range, the mouth-nasal resonance |
https://en.wikipedia.org/wiki/Ch%C3%A2teau%20Romer%20du%20Hayot | Château Romer du Hayot is a sweet white wine ranked as Second Cru Classé (French, “Second Growth”) in the original Bordeaux Wine Official Classification of 1855. Belonging to the Sauternes appellation in Gironde, in the region of Graves, the winery is located in the commune of Sauternes.
History
The wine estate was probably founded already in the 17th century by the Montalier family, and shares its early history with that of Château Romer. In the year 1800, Ferdinand Auguste de Lur-Saluces married a descendant of the founders, Marie Thérèse Gabrielle de Montalier, which for a time made the estate part of the wine empire of the Lur-Saluces family. In 1824, their daughter Louise Alexandrine married Count Anne Auguste Jacques de la Myre-Mory. In 1855, the year of the classification of Bordeaux wine, the estate was named Château Romer, and was classified as a second growth.
In 1881, due to inheritance, the estate was divided into several smaller lots that were passed down to members of the Myre-Mory family. However, the different lots were managed together by one of the inheritors, Comtesse Beaurepaire-Louvagny. In 1937, the majority of the former Château Romer vineyards, compromising to , were sold to Xavier Dauglade and Madame du Hayot, forming Château Romer du Hayot. The part of the original estate that has remained under the Château Romer name, about , had been sold by Myre-Mory to Roger Farges in 1911.
The original estate buildings were torn down in the 1970s, when the E |
https://en.wikipedia.org/wiki/Ch%C3%A2teau%20Lamothe-Guignard | Château Lamothe-Guignard is a sweet white wine ranked as Second Cru Classé (French, “Second Growth”) in the original Bordeaux Wine Official Classification of 1855. Belonging to the Sauternes appellation in Gironde, in the region of Graves, the winery is located in the commune of Sauternes.
References
Bordeaux wine producers |
https://en.wikipedia.org/wiki/Urea%20transporter | A urea transporter is a membrane transport protein, transporting urea. Humans and other mammals have two types of urea transport proteins, UT-A and UT-B. The UT-A proteins are important for renal urea handling and are produced by alternative splicing of the SLC14A2 gene. Urea transport in the kidney is regulated by vasopressin.
The structure of a urea transport family protein from Desulfovibrio vulgaris was determined by x-ray crystallography. The structure has a pathway through the membrane that is similar to that of ion channel proteins, accounting for the ability of urea transport proteins to move up to one million urea molecules per second across the membrane.
Urea transporters can be inhibited by the action of urea analogues like thiourea and glycosides like phloretin. Their inhibition results in increased diuresis due to urea induced osmosis in the collecting ducts of the kidney.
Types
In mammals, there are two urea transporter genes: UT-A (SLC14A2) and UT-B (SLC14A1). Multiple protein isoforms derived from each gene are produced by alternative splicing and alternative promoters.
UT-A1
Urea transporter A1 transports urea across the apical membrane into the intracellular space of luminal cells in the inner medullary collecting duct of the kidneys. UT-1 is activated by ADH, but is a passive transporter. It reabsorbs up to 70% of the original filtered load of urea.
UT-A2
Urea Transporter 2 transports urea across the apical membrane into the luminal space of |
https://en.wikipedia.org/wiki/June%20Storey | Mary June Storey (April 20, 1918 – December 18, 1991) was a Canadian-born American film actress who appeared in 45 films during the 1930s and 1940s. She was leading lady to cowboy singer Gene Autry in 10 films.
Early years
Storey was born on April 20, 1918, in Toronto, Ontario, Canada. Her father, William Storey, was a forest ranger; her mother was Lareta Storey. Her acting interests were evident early when, as a little girl, she put on shows in her family's backyard.
Her family moved to Tyler Lake, Connecticut, when she was five years old. She had a sister, Maxine, who became a "noted motion picture magazine feature writer."
After living in Connecticut and Long Island, New York, in 1930, her family moved to Southern California, where she attended Laguna Beach High School. She gained acting experience with the Laguna Beach Little Theater. Her first appearance on film was an uncredited role as a coed in Student Tour (1933).
Film
Pretty in her youth, Storey caught the attention of Fox Film Corporation when she auditioned with them to star in films. After being hired as a contract player by Fox, Storey studied acting with Florence Enright and took dancing lessons from Rita Hayworth's father, Eduardo Cansino. Storey, like Hayworth and other young actors, participated in a "training school" operated by Fox. The school used one-act plays to develop the actors' talents.
In 1934, Storey made her first film appearance in Student Tour. In June 1935, Storey signed a seven-year con |
https://en.wikipedia.org/wiki/Extensor%20digitorum%20reflex | The extensor digitorum reflex is tested as part of the neurological examination to assess the sensory and motor pathways within the C6 and C7 spinal nerves. It is also known as Braunecker-Effenberg reflex, or BER.
Testing
The test is performed by tapping the extensor digitorum muscle while the fingers are light or half flexed. A sudden contraction of the musculus extensor digitorum and extension of the fingers indicate a normal reflex.
Absence of reflex
An absence of reflex can be an indicator for radiculopathy within the C6 and C7 or neuropathy within the deep branch of the radial nerve.
References
External links
Extensor-Digitorum-Reflex
Applying the Extensor Digitorum Reflex to Neurological Examination
Reflexes |
https://en.wikipedia.org/wiki/Rick%20Durrett | Richard Timothy Durrett is an American mathematician known for his research and
books on mathematical probability theory, stochastic processes and their
application to mathematical ecology and population genetics.
Education and career
He received his BS and MS at Emory University in 1972 and 1973 and his Ph.D. at Stanford University in 1976 under advisor Donald
Iglehart. From 1976 to 1985 he taught at UCLA. From 1985 until 2010 was on the faculty at Cornell University, where his students included Claudia Neuhauser. Since 2010, Durrett has been a professor at Duke University.
He was elected to the United States National Academy of Sciences in 2007. In 2012 he became a fellow of the American Mathematical Society.
Durrett is the founder of the Cornell Probability Summer Schools.
Selected publications
Books
Durrett, R. Probability. Theory and examples. Wadsworth & Brooks/Cole, Pacific Grove, CA (1991). 453 pp. ; 4th edition, 2010
Durrett, R. Probability models for DNA sequence evolution. Springer-Verlag, New York (2002). 240 pp. ; 2nd edition, 2008
Durrett, R. Stochastic Calculus: A Practical Introduction. CRC Press (1996). 341 pp.
Durrett, R. Random Graph Dynamics. Cambridge University Press (2006). 222 pp.
Papers
(This article has over 1100 citations.)
References
External links
Personal Home Page at Duke University.
Cornell Probability Summer Schools.
20th-century American mathematicians
21st-century American mathematicians
Fellows of the American Mathem |
https://en.wikipedia.org/wiki/Binding%20immunoglobulin%20protein | Binding immunoglobulin protein (BiPS) also known as 78 kDa glucose-regulated protein (GRP-78) or heat shock 70 kDa protein 5 (HSPA5) is a protein that in humans is encoded by the HSPA5 gene.
BiP is a HSP70 molecular chaperone located in the lumen of the endoplasmic reticulum (ER) that binds newly synthesized proteins as they are translocated into the ER, and maintains them in a state competent for subsequent folding and oligomerization. BiP is also an essential component of the translocation machinery and plays a role in retrograde transport across the ER membrane of aberrant proteins destined for degradation by the proteasome. BiP is an abundant protein under all growth conditions, but its synthesis is markedly induced under conditions that lead to the accumulation of unfolded polypeptides in the ER.
Structure
BiP contains two functional domains: a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The NBD binds and hydrolyzes ATP, and the SBD binds polypeptides.
The NBD consists of two large globular subdomains (I and II), each further divided into two small subdomains (A and B). The subdomains are separated by a cleft where the nucleotide, one Mg2+, and two K+ ions bind and connect all four domains (IA, IB, IIA, IIB). The SBD is divided into two subdomains: SBDβ and SBDα. SBDβ serves as a binding pocket for client proteins or peptide and SBDα serves as a helical lid to cover the binding pocket. An inter-domain linker connects NBD and SBD, favoring t |
https://en.wikipedia.org/wiki/Outer%20membrane%20protein%20OpcA | Outer membrane adhesin OpcA protein family consists of several Neisseria species specific outer membrane proteins. Neisseria meningitidis causes meningococcal meningitis and sepsis. Opc (formerly called 5C) is one of the major outer membrane proteins and has been shown to play an important role in meningococcal adhesion and invasion of epithelial and endothelial cells, mediating attachment to host cells by binding proteoglycan cell-surface receptors.
OpcA forms a 10-stranded beta-barrel with five highly mobile extracellular loops that protrude above the surface of the membrane. These extracellular loops combine to form a crevice in the external surface that is lined by positively charged residues, which is predicted to be a binding site for proteoglycan polysaccharides involved in pathogenesis. Conformational changes in the extracellular loops modulate the surface of OpcA, which could affect the proteoglycan binding site. These conformational changes could also lead to pore opening.
References
Protein domains
Protein families
Outer membrane proteins |
https://en.wikipedia.org/wiki/Outer%20membrane%20protein%20G | Outer membrane protein G (OmpG) is a porin, a channel proteins in the outer membrane of Gram-negative bacteria.
Escherichia coli OmpG forms a 14-stranded beta-barrel and in contrast to most porins, appears to function as a monomer. The central pore of OmpG is wider than other E. coli porins and it is speculated that it may form a non-specific channel for the transport of larger oligosaccharides.
References
Protein domains
Protein families
Outer membrane proteins |
https://en.wikipedia.org/wiki/Coupon%20collector%27s%20problem | In probability theory, the coupon collector's problem describes "collect all coupons and win" contests. It asks the following question: If each box of a brand of cereals contains a coupon, and there are n different types of coupons, what is the probability that more than t boxes need to be bought to collect all n coupons? An alternative statement is: Given n coupons, how many coupons do you expect you need to draw with replacement before having drawn each coupon at least once? The mathematical analysis of the problem reveals that the expected number of trials needed grows as . For example, when n = 50 it takes about 225 trials on average to collect all 50 coupons.
Solution
Calculating the expectation
Let time T be the number of draws needed to collect all n coupons, and let ti be the time to collect the i-th coupon after i − 1 coupons have been collected. Then . Think of T and ti as random variables. Observe that the probability of collecting a coupon is . Therefore, has geometric distribution with expectation . By the linearity of expectations we have:
Here Hn is the n-th harmonic number. Using the asymptotics of the harmonic numbers, we obtain:
where is the Euler–Mascheroni constant.
Using the Markov inequality to bound the desired probability:
The above can be modified slightly to handle the case when we've already collected some of the coupons. Let k be the number of coupons already collected, then:
And when then we get the original result.
Calculating the var |
https://en.wikipedia.org/wiki/Germanium%20iodides | Germanium iodides are inorganic compound with the formula GeIx. Two such compounds exist: germanium(II) iodide, , and germanium(IV) iodide .
Germanium(II) iodide is an orange-yellow crystalline solid which decomposes on melting. Its specific density is 5.37 and it can be sublimed at 240 °C in a vacuum. It can be prepared by reducing germanium(IV) iodide with aqueous hypophosphorous acid in the presence of hydroiodic acid. It is oxidised by a solution of potassium iodide in hydrochloric acid to germanium(IV) iodide. It reacts with acetylene at 140 °C to form an analogue of cyclohexa-1,4-diene in which the methylene groups, , are replaced with diiodogermylene groups, .
Germanium(IV) iodide is an orange-red crystalline solid with melting point 144 °C and boiling point 440 °C (with decomposition). Its specific density is 4.32. It is soluble in non-polar solvents like carbon disulfide, chloroform or benzene, but hydrolyses readily.
References
Germanium compounds
Iodides
Metal halides |
https://en.wikipedia.org/wiki/Z%284430%29 | Z(4430) is a mesonic resonance discovered by the Belle experiment. It has a mass of . The resonant nature of the peak has been confirmed by the LHCb experiment with a significance of at least 13.9 σ. The particle is charged and is thought to have a quark content of , making it a tetraquark candidate. It has the spin-parity quantum numbers JP = 1+.
The particle joins the X(3872), Zc(3900) and Y(4140) as exotic hadron candidates observed by multiple experiments, although it is the first to be confirmed as a resonance.
See also
XYZ particle
References
External links
Major harvest of four-leaf clover
Mesons
2014 in science
Subatomic particles with spin 1 |
https://en.wikipedia.org/wiki/APAF1 | Apoptotic protease activating factor 1, also known as APAF1, is a human homolog of C. elegans CED-4 gene.
Function
The protein was identified in the laboratory of Xiaodong Wang as an activator of caspase-3 in the presence of cytochromeC and dATP. This gene encodes a cytoplasmic protein that forms one of the central hubs in the apoptosis regulatory network. This protein contains (from the N terminal) a caspase recruitment domain (CARD), an ATPase domain (NB-ARC), few short helical domains and then several copies of the WD40 repeat domain. Upon binding cytochrome c and dATP, this protein forms an oligomeric apoptosome. The apoptosome binds and cleaves Procaspase-9 protein, releasing its mature, activated form. The precise mechanism for this reaction is still debated though work published by Guy Salvesen suggests that the apoptosome may induce caspase-9 dimerization and subsequent autocatalysis. Activated caspase-9 stimulates the subsequent caspase cascade that commits the cell to apoptosis.
Alternative splicing results in several transcript variants encoding different isoforms.
Structure
APAF1 contains a CARD domain with a Greek key motif composed of six helices, a Rossman fold nucleotide binding domains, a short helical motif and a winged-helix domain.
Interactions
APAF1 has been shown to interact with:
APIP,
BCL2-like 1
Caspase-9,
HSPA4, and
NLRP1.
References
External links
Further reading
Programmed cell death
Ap |
https://en.wikipedia.org/wiki/CEACAM1 | Carcinoembryonic antigen-related cell adhesion molecule 1 (biliary glycoprotein) (CEACAM1) also known as CD66a (Cluster of Differentiation 66a), is a human glycoprotein, and a member of the carcinoembryonic antigen (CEA) gene family.
Function
This gene encodes a member of the carcinoembryonic antigen (CEA) gene family, which belongs to the immunoglobulin superfamily. Two subgroups of the CEA family, the CEA cell adhesion molecules and the pregnancy-specific glycoproteins, are located within a 1.2 Mb cluster on the long arm of chromosome 19. Eleven pseudogenes of the CEA cell adhesion molecule subgroup are also found in the cluster. The encoded protein was originally described in bile ducts of liver as biliary glycoprotein. Subsequently, it was found to be a cell–cell adhesion molecule detected on leukocytes, epithelia, and endothelia. The encoded protein mediates cell adhesion via homophilic as well as heterophilic binding to other proteins of the subgroup. Multiple cellular activities have been attributed to the encoded protein, including roles in the differentiation and arrangement of tissue three-dimensional structure, angiogenesis, apoptosis, tumor suppression, metastasis, and the modulation of innate and adaptive immune responses. Multiple transcript variants encoding different isoforms have been reported, but the full-length nature of only two has been determined.
In melanocytic cells CEACAM1 gene expression may be regulated by MITF.
Interactions
CEACAM1 has been |
https://en.wikipedia.org/wiki/CD81 | CD81 molecule, also known as CD81 (Cluster of Differentiation 81), is a protein which in humans is encoded by the CD81 gene. It is also known as 26 kDa cell surface protein, TAPA-1 (Target of the Antiproliferative Antibody 1), and Tetraspanin-28 (Tspan-28).
Gene
The gene is located on the plus strand of the short arm of chromosome 11 (11p15.5). It is 20,103 bases in length and encodes a protein of 236 amino acids (predicted molecular weight 25.809 kDa).
The protein does not appear to be post translationally modified and has four transmembrane domains. Both the N-terminus and C-terminus lie on the intracellular side of the membrane.
The gene is expressed in hemopoietic, endothelial, and epithelial cells. It is absent from erythrocytes, platelets, and neutrophils.
Function
The protein encoded by this gene is a member of the transmembrane 4 superfamily, also known as the tetraspanin family. Most of these members are cell-surface proteins that are characterized by the presence of four hydrophobic domains. The proteins mediate signal transduction events that play a role in the regulation of cell development, activation, growth and motility. This encoded protein is a cell surface glycoprotein that is known to complex with integrins. This protein appears to promote muscle cell fusion and support myotube maintenance. Also it may be involved in signal transduction. This gene is localized in the tumor-suppressor gene region and thus it is a candidate gene for malignancies.
Th |
https://en.wikipedia.org/wiki/Activating%20transcription%20factor%202 | Activating transcription factor 2, also known as ATF2, is a protein that, in humans, is encoded by the ATF2 gene.
Function
This gene encodes a transcription factor that is a member of the leucine zipper family of DNA-binding proteins. This protein binds to the cAMP-responsive element (CRE), an octameric palindrome. The protein forms a homodimer or heterodimer with c-Jun. The protein is also a histone acetyltransferase (HAT) that specifically acetylates histones H2B and H4 in vitro; thus, it may represent a class of sequence-specific factors that activate transcription by direct effects on chromatin components. Additional transcript variants have been identified but their biological validity has not been determined.
The gene atf2 is located at human chromosome 2q32. The protein ATF-2 has 505 amino acids. Studies in mice indicate a role for ATF-2 in the development of nervous system and the skeleton. ATF-2 is normally activated in response to signals that converge on stress-activated protein kinases p38 and JNK. ATF-2 phosphorylation in response to treatment of cells with tumor promoter phorbol ester has been demonstrated.
Several studies implicate abnormal activation of ATF-2 in growth and progression of mammalian skin tumors. ATF-2 may mediate oncogenesis caused by mutant Ras protein and regulate maintenance of the aggressive cancer phenotype of some types of epithelial cells.
ATF2 has also been shown to be phosphorylated at its C-terminal (serine 472 and 480 in mouse; s |
https://en.wikipedia.org/wiki/Cathepsin%20D | Cathepsin D is a protein that in humans is encoded by the CTSD gene. This gene encodes a lysosomal aspartyl protease composed of a protein dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. Cathepsin D is an aspartic endo-protease that is ubiquitously distributed in lysosomes. The main function of cathepsin D is to degrade proteins and activate precursors of bioactive proteins in pre-lysosomal compartments. This proteinase, which is a member of the peptidase A1 family, has a specificity similar to but narrower than that of pepsin A. Transcription of the CTSD gene is initiated from several sites, including one that is a start site for an estrogen-regulated transcript. Mutations in this gene are involved in the pathogenesis of several diseases, including breast cancer and possibly Alzheimer disease. Homozygous deletion of the CTSD gene leads to early lethality in the postnatal phase. Deficiency of CTSD gene has been reported an underlying cause of neuronal ceroid lipofuscinosis (NCL).
Structure
Gene
The CTSD gene is located at chromosome 11.
Protein
The catalytic sites of cathepsin D include two critical aspartic residues (amino acid 33 and 231) located on the 14 kDa and 34kDa chains. The ultimate form of mature cathepsin D is composed of 337 amino acid residues, 196 amino acid residues in the heavy chain and 141 in the light chain. These two chains are linked by the hydrophobic effect.
Function
The optimum pH for cathepsin D |
https://en.wikipedia.org/wiki/Cathepsin%20L1 | Cathepsin L1 is a protein that in humans is encoded by the CTSL1 gene. The protein is a cysteine cathepsin, a lysosomal cysteine protease that plays a major role in intracellular protein catabolism.
Function
Cathepsin L1 is a member of the Peptidase C1 (cathepsin) MEROPS family, which plays an important role in diverse processes including normal lysosome mediated protein turnover, antigen and proprotein processing, and apoptosis. Its substrates include collagen and elastin, as well as alpha-1 protease inhibitor, a major controlling element of neutrophil elastase activity. The encoded protein has been implicated in several pathologic processes, including myofibril necrosis in myopathies and in myocardial ischemia, and in the renal tubular response to proteinuria. This protein, which is a member of the peptidase C1 family, is a dimer composed of disulfide-linked heavy and light chains, both produced from a single protein precursor. At least two transcript variants encoding the same protein have been found for this gene.
Viral entry
Cleavage of the SARS-CoV-2 S2 spike protein required for viral entry into cells can be accomplished by proteases TMPRSS2 located on the cell membrane, or by cathepsins (primarily cathepsin L) in endolysosomes. Hydroxychloroquine inhibits the action of cathepsin L in endolysosomes, but because cathepsin L cleavage is minor compared to TMPRSS2 cleavage, hydroxychloroquine does little to inhibit SARS-CoV-2 infection.
Inflammation
Although Cathepsin |
https://en.wikipedia.org/wiki/GRIN1 | Glutamate [NMDA] receptor subunit zeta-1 is a protein that in humans is encoded by the GRIN1 gene.
The protein encoded by this gene is a critical subunit of N-methyl-D-aspartate receptors, members of the glutamate receptor channel superfamily which are heteromeric protein complexes with multiple subunits arranged to form a ligand-gated ion channel. These subunits play a key role in the plasticity of synapses, which is believed to underlie memory and learning. The gene consists of 21 exons and is alternatively spliced, producing transcript variants differing in the C-terminus. The sequence of exon 5 is identical in vertebrates, with exon 5 splicing demonstrated in human, mouse and rat. Cell-specific factors are thought to control expression of different isoforms, possibly contributing to the functional diversity of the subunits.
See also
NMDA receptor
References
Further reading
Ionotropic glutamate receptors
Ion channels |
https://en.wikipedia.org/wiki/Interferon%20alpha-1 | Interferon alpha-1 is a protein that in humans is encoded by the IFNA1 gene.
Leukocyte interferon is produced predominantly by B lymphocytes. Immune interferon (IFN-gamma; MIM 147570) is produced by mitogen- or antigen-stimulated T lymphocytes.[supplied by OMIM]
The type I interferon gene family
The interferons (IFN)s are a family of cytokines with potent antiviral, antiproliferative and immunomodulatory properties. IFNs were originally discovered as molecules that could reduce the ability of a normal virus to infect cells, a process called viral 'interference'.
IFNs have been classified into two major types of IFNs, type I and type II, based on their interactions to a specific cell surface receptor.
In recent years, a novel class of cytokines with IFN-like activities has been described and designated as type III IFNs (IFN-λ1-3). In humans, there are 13 different IFN-alpha genes, designated as IFN-α1, -α2, - α4, - α5, - α6, - α7, - α8, - α10, - α13, - α14, - α16, - α17 and - α21, and one each of the IFN beta (IFNB), IFN-Epsilon, IFN-Kappa and IFN-Omega genes. The human IFNA gene family shares 70-80% amino acid sequence homology, and about 35% identity with IFNB. The high degree of amino-acid sequence similarity within the IFNA genes suggests a common ancestor gene. It seems likely that the IFNA gene cluster has been generated by gene conversion or recent duplication events.
There are 12 functional human IFNA gene products. All of these IFN-α proteins exhibit high ho |
https://en.wikipedia.org/wiki/IFNB1 | Interferon beta is a protein that in humans is encoded by the IFNB1 gene. The natural and recombinant protein forms have antiviral, antibacterial, and anticancer properties.
Interferon beta 1a (tradenames: Avonex and Rebif) and Interferon beta 1b (tradenames: Betaseron/Betaferon) are used as drugs.
References
Further reading |
https://en.wikipedia.org/wiki/IGFBP1 | Insulin-like growth factor-binding protein 1 (IBP-1) also known as placental protein 12 (PP12) is a protein that in humans is encoded by the IGFBP1 gene.
Function
This gene is a member of the Insulin-like growth factor-binding protein (IGFBP) family and encodes a protein with an IGFBP domain and a type-I thyroglobulin domain. The protein binds both insulin-like growth factors (IGFs) I and II and circulates in the plasma. Binding of this protein prolongs the half-life of the IGFs and alters their interaction with cell surface receptors. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
References
Further reading |
https://en.wikipedia.org/wiki/Integrin%20beta%204 | Integrin, beta 4 (ITGB4) also known as CD104 (Cluster of Differentiation 104), is a human gene.
Function
Integrins are heterodimers composed of alpha and beta subunits, that are noncovalently associated transmembrane glycoprotein receptors. Different combinations of alpha and beta polypeptides form complexes that vary in their ligand-binding specificities. Integrins mediate cell-matrix or cell-cell adhesion, and transduced signals that regulate gene expression and cell growth. This gene encodes the integrin beta 4 subunit, a receptor for the laminins. This subunit tends to associate with alpha 6 subunit and is likely to play a pivotal role in the biology of invasive carcinoma. Mutations in this gene are associated with epidermolysis bullosa with pyloric atresia. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.
Interactions
ITGB4 has been shown to interact with Collagen, type XVII, alpha 1, EIF6 and Erbin.
See also
Cluster of differentiation
List of target antigens in pemphigoid
References
Further reading
External links
GeneReviews/NCBI/NIH/UW entry on Epidermolysis Bullosa with Pyloric Atresia
ITGB4 Info with links in the Cell Migration Gateway
Clusters of differentiation
Integrins |
https://en.wikipedia.org/wiki/RPS6KA3 | protein S6 kinase, 90kDa, polypeptide 3, also s RPS6KA3, is an enzyme that in humans is encoded by the RPS6KA3 gene.
Function
This gene encodes a member of the RSK (ribosomal S6 kinase) family of serine/threonine kinases. This kinase contains 2 non-identical kinase catalytic domains and phosphorylates various substrates, including members of the mitogen-activated kinase (MAPK) signalling pathway. The activity of this protein has been implicated in controlling cell growth and differentiation.
Clinical significance
Mutations in this gene have been associated with Coffin–Lowry syndrome (CLS).
Interactions
RPS6KA3 has been shown to interact with CREB-binding protein, MAPK1 and PEA15.
References
Further reading
External links
GeneReviews/NCBI/NIH/UW entry on Coffin–Lowry syndrome
EC 2.7.11 |
https://en.wikipedia.org/wiki/P70-S6%20Kinase%201 | Ribosomal protein S6 kinase beta-1 (S6K1), also known as p70S6 kinase (p70S6K, p70-S6K), is an enzyme (specifically, a protein kinase) that in humans is encoded by the RPS6KB1 gene. It is a serine/threonine kinase that acts downstream of PIP3 and phosphoinositide-dependent kinase-1 in the PI3 kinase pathway. As the name suggests, its target substrate is the S6 ribosomal protein. Phosphorylation of S6 induces protein synthesis at the ribosome.
The phosphorylation of p70S6K at threonine 389 has been used as a hallmark of activation by mTOR and correlated with autophagy inhibition in various situations. However, several recent studies suggest that the activity of p70S6K plays a more positive role in the increase of autophagy.
Function
This gene encodes a member of the S6K family of serine/threonine kinases, which phosphorylate several residues of the S6 ribosomal protein. The kinase activity of this protein leads to an increase in protein synthesis and cell proliferation. Amplification of the region of DNA encoding this gene and overexpression of this kinase are seen in some breast cancer cell lines. Alternate translational start sites have been described and alternate transcriptional splice variants have been observed but have not been thoroughly characterized.
mTOR
The p70S6 kinase is a downstream target of mTOR (mammalian target of rapamycin) signaling, specifically mTORC1, an mTOR-containing complex characterized by the inclusion of Raptor rather than Rictor (mTORC2). |
https://en.wikipedia.org/wiki/S100A9 | S100 calcium-binding protein A9 (S100A9) also known as migration inhibitory factor-related protein 14 (MRP14) or calgranulin B is a protein that in humans is encoded by the S100A9 gene.
The proteins S100A8 and S100A9 form a heterodimer called calprotectin.
Function
S100A9 is a member of the S100 family of proteins containing 2 EF hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100 genes include at least 13 members which are located as a cluster on chromosome 1q21. This protein may function in the inhibition of casein kinase.
MRP14 complexes with MRP-8 (S100A8), another member of the S100 family of calcium-modulated proteins; together, MRP8 and MRP14 regulate myeloid cell function by binding to Toll-like receptor 4 (TLR4) and the receptor for advanced glycation end products.
Intracellular S100A9 alters mitochondrial homeostasis within neutrophils. As a result, neutrophils lacking S100A9 produce higher levels of mitochondrial superoxide and undergo elevated levels of suicidal NETosis in response to bacterial pathogens. Furthermore, S100A9-deficient mice are protected from systemic Staphylococcus aureus infections with lower bacterial burdens in the heart, which suggests an organ-specific function for S100A9.
Clinical significance
Altered expression of the S100A9 protein is associated wi |
https://en.wikipedia.org/wiki/Spectrin%2C%20alpha%201 | Spectrin alpha chain, erythrocyte is a protein that in humans is encoded by the SPTA1 gene.
Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is a tetramer made up of alpha-beta dimers linked in a head-to-head arrangement. This gene is one member of a family of alpha-spectrin genes. The encoded protein is primarily composed of 22 spectrin repeats which are involved in dimer formation. It forms weaker tetramer interactions than non-erythrocytic alpha spectrin, which may increase the plasma membrane elasticity and deformability of red blood cells. Mutations in this gene result in a variety of hereditary red blood cell disorders, including elliptocytosis type 2, pyropoikilocytosis, and spherocytic hemolytic anemia.
Interactions
Spectrin, alpha 1 has been shown to interact with Abl gene.
References
Further reading
EF-hand-containing proteins |
https://en.wikipedia.org/wiki/TGFBI | Transforming growth factor, beta-induced, 68kDa, also known as TGFBI (initially called BIGH3, BIG-H3), is a protein which in humans is encoded by the TGFBI gene, locus 5q31.
Function
This gene encodes an RGD-containing protein that binds to type I, II and IV collagens. The RGD motif is found in many extracellular matrix proteins modulating cell adhesion and serves as a ligand recognition sequence for several integrins. This protein plays a role in cell-collagen interactions and may be involved in endochondrial bone formation in cartilage. The protein is induced by transforming growth factor-beta and acts to inhibit cell adhesion.
Clinical significance
Mutations of the gene cause several forms of corneal dystrophies.
References
Further reading
Extracellular matrix proteins |
https://en.wikipedia.org/wiki/ACTC1 | ACTC1 encodes cardiac muscle alpha actin. This isoform differs from the alpha actin that is expressed in skeletal muscle, ACTA1. Alpha cardiac actin is the major protein of the thin filament in cardiac sarcomeres, which are responsible for muscle contraction and generation of force to support the pump function of the heart.
Structure
Cardiac alpha actin is a 42.0 kDa protein composed of 377 amino acids. Cardiac alpha actin is a filamentous protein extending from a complex mesh with cardiac alpha-actinin (ACTN2) at Z-lines towards the center of the sarcomere. Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to four others. The atomic structure of monomeric actin was solved by Kabsch et al., and closely thereafter this same group published the structure of the actin filament. Actins are highly conserved proteins; the alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. Cardiac (ACTC1) and skeletal (ACTA1) alpha actins differ by only four amino acids (Asp4Glu, Glu5Asp, Leu301Met, Ser360Thr; cardiac/skeletal). The actin monomer has two asymmetric domains; the larger inner domain comprised by sub-domains 3 and 4, and the smaller outer domain by sub-domains 1 and 2. Both the amino and carboxy-termini lie in sub-domain 1 of the outer domain.
Function
Actin is a dynamic structure that can adapt two states of flexibility, with the greatest dif |
https://en.wikipedia.org/wiki/Alpha-1-microglobulin/bikunin%20precursor | Protein AMBP is a protein that in humans is encoded by the AMBP gene.
Interactions
Alpha-1-microglobulin/bikunin precursor has been shown to interact with CD79A.
See also
Inter-alpha-trypsin inhibitor
Alpha-1-microglobulin
References
Further reading
External links
The MEROPS online database for peptidases and their inhibitors: LI02-001
Precursor proteins
Lipocalins |
https://en.wikipedia.org/wiki/Colony%20stimulating%20factor%201%20receptor | Colony stimulating factor 1 receptor (CSF1R), also known as macrophage colony-stimulating factor receptor (M-CSFR), and CD115 (Cluster of Differentiation 115), is a cell-surface protein encoded by the human CSF1R gene (known also as c-FMS). CSF1R is a receptor that can be activated by two ligands: colony stimulating factor 1 (CSF-1) and interleukin-34 (IL-34). CSF1R is highly expressed in myeloid cells, and CSF1R signaling is necessary for the survival, proliferation, and differentiation of many myeloid cell types in vivo and in vitro. CSF1R signaling is involved in many diseases and is targeted in therapies for cancer, neurodegeneration, and inflammatory bone diseases.
Gene
In the human genome, the CSF1R gene is located on chromosome 5 (5q32), and in mice the Csf1r gene is located on chromosome 18 (18D). CSF1R is 60.002 kilobases (kbs) in length. Hematopoietic stem cells express CSF1R at low levels, but CSF1R is highly expressed in more differentiated myeloid cell types such as monocytes, macrophages, osteoclasts, myeloid dendritic cells, microglia, and Paneth cells. CSF1R expression is controlled by two alternative promoters that are active in specific tissue types. Exon 1 of CSF1R is specifically transcribed in trophoblastic cells whereas exon 2 is specifically transcribed in macrophages. Activation of CSF1R transcription is regulated by several transcription factors including Ets and PU.1. Macrophage expression of the CSF1R gene is regulated by the promoter upstream of |
https://en.wikipedia.org/wiki/DNA%20damage-inducible%20transcript%203 | DNA damage-inducible transcript 3, also known as C/EBP homologous protein (CHOP), is a pro-apoptotic transcription factor that is encoded by the DDIT3 gene. It is a member of the CCAAT/enhancer-binding protein (C/EBP) family of DNA-binding transcription factors. The protein functions as a dominant-negative inhibitor by forming heterodimers with other C/EBP members, preventing their DNA binding activity. The protein is implicated in adipogenesis and erythropoiesis and has an important role in the cell's stress response.
Structure
C/EBP proteins are known to have a conserved C-terminal structure, basic leucine zipper domain(bZIP), that is necessary for the formation of DNA-binding capable homodimers or heterodimers with other proteins or members of the C/EBP protein family. CHOP is a relatively small (29kDa) protein that differs from most C/EBP proteins in several amino acid substitutions, which impacts its DNA-binding ability.
Regulation and function
Due to a variety of upstream and downstream regulatory interactions, CHOP plays an important role in ER stress-induced apoptosis caused by a variety of stimuli such as pathogenic microbial or viral infections, amino acid starvation, mitochondrial stress, neurological diseases, and neoplastic diseases.
Under normal physiological conditions, CHOP is ubiquitously present at very low levels. However, under overwhelming ER stress conditions, the expression of CHOP rises sharply along with the activation of apoptotic pathways i |
https://en.wikipedia.org/wiki/EIF2S1 | Eukaryotic translation initiation factor 2 subunit 1 (eIF2α) is a protein that in humans is encoded by the EIF2S1 gene.
Function
The protein encoded by this gene is the alpha (α) subunit of the translation initiation factor eIF2 protein complex which catalyzes an early regulated step of protein synthesis initiation, promoting the binding of the initiator tRNA (Met-tRNAiMet) to 40S ribosomal subunits. Binding occurs as a ternary complex of methionyl-tRNA, eIF2, and GTP. eIF2 is composed of 3 nonidentical subunits, alpha (α, 36 kD, this article), beta (β, 38 kD), and gamma (γ, 52 kD). The rate of formation of the ternary complex is modulated by the phosphorylation state of eIF2α. Phosphorylation of eIF2α by EIF-2 kinases plays a key role in regulating the integrated stress response.
Clinical significance
After reperfusion following brain ischemia, there is inhibition of neuron protein synthesis due to phosphorylation of eIF2α. There is colocalization between phosphorylated eIF2α and cytosolic cytochrome c, which is released from mitochondria in apoptosis. Phosphorylated Eif2-alpha appeared before cytochrome c release, suggesting that phosphorylation of eIF2α triggers cytochrome c release during apoptotic cell death.
Mice heterozygous for the S51A mutation become obese and diabetic on a high-fat diet. Glucose intolerance resulted from reduced insulin secretion, defective transport of proinsulin, and a reduced number of insulin granules in beta cells. Hence proper functioni |
https://en.wikipedia.org/wiki/RNA-binding%20protein%20EWS | RNA-binding protein EWS is a protein that in humans is encoded by the EWSR1 gene on human chromosome 22, specifically 22q12.2. It is one of 3 proteins in the FET protein family.
Clinical significance
The q22.2 region of chromosome 22 encodes the N-terminal transactivation domain of the EWS protein and that region may become joined to one of several other chromosomes which encode various transcription factors; see EWS/FLI and OMIM-133450. The expression of a chimeric protein with the EWS transactivation domain fused to the DNA binding region of a transcription factor generates a powerful oncogenic protein causing Ewing sarcoma and other members of the Ewing family of tumors. These translocations can occur due to chromoplexy, a burst of complex chromosomal rearrangements seen in cancer cells. The normal EWS gene encodes an RNA binding protein closely related to FUS (gene) and TAF15, all of which have been associated to amyotrophic lateral sclerosis.
Interactions
The EWS protein has been shown to interact with:
ATF1,
BARD1,
ERG,
POU4F1,
PTK2B
SF1,
SNRPC, and
ZNF165.
References
Further reading
External links
Ewing sarcoma breakpoint region 1 on the Atlas of Genetics and Oncology
Oncogenes |
https://en.wikipedia.org/wiki/FGF7 | Keratinocyte growth factor is a protein that in humans is encoded by the FGF7 gene.
Function
The protein encoded by this gene is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein is a potent epithelial cell-specific growth factor, whose mitogenic activity is predominantly exhibited in keratinocytes but not in fibroblasts and endothelial cells. Studies of mouse and rat homologs of this gene implicated roles in morphogenesis of epithelium, reepithelialization of wounds, hair development and early lung organogenesis.
Interactions
FGF7 has been shown to interact with Perlecan.
References
Further reading |
https://en.wikipedia.org/wiki/P4HB | Protein disulfide-isomerase, also known as the beta-subunit of prolyl 4-hydroxylase (P4HB), is an enzyme that in humans encoded by the P4HB gene. The human P4HB gene is localized in chromosome 17q25. Unlike other prolyl 4-hydroxylase family proteins, this protein is multifunctional and acts as an oxidoreductase for disulfide formation, breakage, and isomerization. The activity of P4HB is tightly regulated. Both dimer dissociation and substrate binding are likely to enhance its enzymatic activity during the catalysis process.
Structure
P4HB has four thioredoxin domains (a, b, b’, and a’), with two CGHC active sites in the a and a’ domains. In both the reduced and oxidized state, these domains are arranged as a horseshoe shape. In reduced P4HB, domains a, b, and b' are in the same plane, while domain a' twists out at a ~45° angle. When oxidized, the four domains stay in the same plane, and the distance between the active sites is larger than that in the reduced state. The oxidized form also exposes more hydrophobic areas and possesses a larger cleft to facilitate substrate binding. P4HB has been shown to dimerize in vivo via noncatalytic bb' domains. Formation of dimer blocks substrate-binding site and inhibits P4HB's activity.
Function
This gene encodes the beta subunit of prolyl 4-hydroxylase, a highly abundant multifunctional enzyme that belongs to the protein disulfide isomerase family. When present as a tetramer consisting of two alpha and two beta subunits, this enzy |
https://en.wikipedia.org/wiki/PLA2G4A | Cytosolic phospholipase A2 is an enzyme that in humans is encoded by the PLA2G4A gene.
Function
This gene encodes a member of the cytosolic phospholipase A2 group IV family. The enzyme catalyzes the hydrolysis of membrane phospholipids to release arachidonic acid which is subsequently metabolized into eicosanoids. Eicosanoids, including prostaglandins and leukotrienes, are lipid-based cellular hormones that regulate hemodynamics, inflammatory responses, and other intracellular pathways. The hydrolysis reaction also produces lysophospholipids that are converted into platelet-activating factor. The enzyme is activated by increased intracellular Ca2+ levels and phosphorylation, resulting in its translocation from the cytosol and nucleus to perinuclear membrane vesicles.
Interactions
PLA2G4A has been shown to interact with HTATIP.
Clinical significance
Mutations in this gene have been associated with multifocal stenosing ulceration of the small intestine.
References
Further reading
EC 3.1.1 |
https://en.wikipedia.org/wiki/PRKCI | Protein kinase C iota type is an enzyme that in humans is encoded by the PRKCI gene.
Function
This gene encodes a member of the protein kinase C (PKC) family of serine/threonine protein kinases. The PKC family comprises at least eight members, which are differentially expressed and are involved in a wide variety of cellular processes. This protein kinase is calcium-independent and phospholipid-dependent. It is not activated by phorbol esters or diacylglycerol. This kinase can be recruited to vesicle tubular clusters (VTCs) by direct interaction with the small GTPase RAB2, where this kinase phosphorylates glyceraldehyde-3-phosphate dehydrogenase (GAPD/GAPDH) and plays a role in microtubule dynamics in the early secretory pathway. This kinase is found to be necessary for BCL-ABL-mediated resistance to drug-induced apoptosis and therefore protects leukemia cells against drug-induced apoptosis. There is a single exon pseudogene mapped on chromosome X.
Interactions
PRKCI has been shown to interact with:
Centaurin, alpha 1,
FRS2,
Glyceraldehyde 3-phosphate dehydrogenase,
PARD3,
Phosphoinositide-dependent kinase-1,
SMG1 (gene),
Sequestosome 1,
KRAS.
Vimentin
References
Further reading
EC 2.7.11 |
https://en.wikipedia.org/wiki/Protein%20kinase%20D1 | Serine/threonine-protein kinase D1 is an enzyme that in humans is encoded by the PRKD1 gene.
Function
Members of the protein kinase D (PKD) family function in many extracellular receptor-mediated signal transduction pathways. The PRKCM gene encodes a cytosolic serine-threonine kinase that binds to the trans-Golgi network and regulates the fission of transport carriers specifically destined to the cell surface.[supplied by OMIM]
Interactions
Protein kinase D1 has been shown to interact with:
Bruton's tyrosine kinase,
C1QBP,
Centaurin, alpha 1,
Metallothionein 2A, and
YWHAQ.
References
Further reading
EC 2.7.11 |
https://en.wikipedia.org/wiki/PSMB8 | Proteasome subunit beta type-8 as known as 20S proteasome subunit beta-5i is a protein that in humans is encoded by the PSMB8 gene.
This protein is one of the 17 essential subunits (alpha subunits 1–7, constitutive beta subunits 1–7, and inducible subunits including beta1i, beta2i, beta5i) that contributes to the complete assembly of 20S proteasome complex. In particular, proteasome subunit beta type-5, along with other beta subunits, assemble into two heptameric rings and subsequently a proteolytic chamber for substrate degradation. This protein contains "Chymotrypsin-like" activity and is capable of cleaving after large hydrophobic residues of peptide. The eukaryotic proteasome recognized degradable proteins, including damaged proteins for protein quality control purpose or key regulatory protein components for dynamic biological processes. The constitutive subunit beta1, beta2, and beta 5 (systematic nomenclature) can be replaced by their inducible counterparts beta1i, 2i, and 5i when cells are under the treatment of interferon-γ. The resulting proteasome complex becomes the so-called immunoproteasome. An essential function of the modified proteasome complex, the immunoproteasome, is the processing of numerous MHC class-I restricted T cell epitopes.
Structure
Gene
This gene encodes a member of the proteasome B-type family, also known as the T1B family, that is a 20S core beta subunit. This gene is located in the class II region of the MHC (major histocompatibility comp |
https://en.wikipedia.org/wiki/PTCH1 | Protein patched homolog 1 is a protein that is the member of the patched family and in humans is encoded by the PTCH1 gene.
Function
PTCH1 is a member of the patched gene family and is the receptor for sonic hedgehog, a secreted molecule implicated in the formation of embryonic structures and in tumorigenesis. This gene functions as a tumor suppressor. The PTCH1 gene product, is a transmembrane protein that suppresses the release of another protein called smoothened, and when sonic hedgehog binds PTCH1, smoothened is released and signals cell proliferation.
Clinical significance
Mutations of this gene have been associated with nevoid basal cell carcinoma syndrome (AKA Gorlin's Syndrome), esophageal squamous cell carcinoma, trichoepitheliomas, transitional cell carcinomas of the bladder, as well as holoprosencephaly. Alternative splicing results in multiple transcript variants encoding different isoforms. Additional splice variants have been described, but their full length sequences and biological validity cannot be determined currently.
Mutations in PTCH1 cause Gorlin syndrome and mutations have also been found in holoprosencephaly patients. Some of these patients present cleft lip and palate among the holoprosencephaly features, and missense variants in PTCH1 were also found in a sequencing screening of nonsyndromic cleft lip and palate patients. In addition association between SNPs in or near PTCH1 have been found to be associated with nonsyndromic cleft lip and pa |
https://en.wikipedia.org/wiki/BTRC%20%28gene%29 | F-box/WD repeat-containing protein 1A (FBXW1A) also known as βTrCP1 or Fbxw1 or hsSlimb or pIkappaBalpha-E3 receptor subunit is a protein that in humans is encoded by the BTRC (beta-transducin repeat containing) gene.
This gene encodes a member of the F-box protein family which is characterized by an approximately 40 residue structural motif, the F-box. The F-box proteins constitute one of the four subunits of ubiquitin protein ligase complex called SCFs (Skp1-Cul1-F-box protein), which often, but not always, recognize substrates in a phosphorylation-dependent manner. F-box proteins are divided into 3 classes:
Fbxws containing WD40 repeats,
Fbxls containing leucine-rich repeats,
and Fbxos containing either "other" protein–protein interaction modules or no recognizable motifs.
The protein encoded by this gene belongs to the Fbxw class as, in addition to an F-box, this protein contains multiple WD40 repeats. This protein is homologous to Xenopus βTrCP, yeast Met30, Neurospora Scon2 and Drosophila Slimb. In mammals, in addition to βTrCP1, a paralog protein (called βTrCP2 or FBXW11) also exists, but, so far, their functions appear redundant and indistinguishable.
Discovery
Human βTrCP (referred to both βTrCP1 and βTrCP2) was originally identified as a cellular ubiquitin ligase that is bound by the HIV-1 Vpu viral protein to eliminate cellular CD4 by connecting it to the proteolytic machinery. Subsequently, βTrCP was shown to regulate multiple cellular processes by mediati |
https://en.wikipedia.org/wiki/KAT5 | Histone acetyltransferase KAT5 is an enzyme that in humans is encoded by the KAT5 gene. It is also commonly identified as TIP60.
The protein encoded by this gene belongs to the MYST family of histone acetyl transferases (HATs) and was originally isolated as an HIV-1 TAT-interactive protein. HATs play important roles in regulating chromatin remodeling, transcription and other nuclear processes by acetylating histone and nonhistone proteins. This protein is a histone acetylase that has a role in DNA repair and apoptosis and is thought to play an important role in signal transduction. Alternative splicing of this gene results in multiple transcript variants.
Structure
The structure of KAT5 includes an acetyl CoA binding domain and a zinc finger in the MYST domain, and a CHROMO domain. Excess acetyl CoA is necessary for acetylation of histones. The zinc finger domain has been shown to aid in the acetylation process as well. The CHROMO domain aids in KAT5 ability to bind chromatin, which is important for DNA repair.
Function
KAT5 enzyme is known for acetylating histones in the nucleosome, which alters binding with DNA. Acetylation neutralizes the positive charge on histones, decreasing binding affinity of negatively charged DNA. This in turn decreases steric hindrance of DNA and increases interaction of transcription factors and other proteins. Three key functions of KAT5 are its ability to regulate transcription, DNA repair, and apoptosis.
Transcription
Transcription fact |
https://en.wikipedia.org/wiki/COP9%20constitutive%20photomorphogenic%20homolog%20subunit%205 | COP9 constitutive photomorphogenic homolog subunit 5 (Arabidopsis), also known as COPS5 or Csn5, is a gene conserved from humans to Saccharomyces cerevisiae.
Function
The protein encoded by this gene is one of the eight subunits of COP9 signalosome, a highly conserved protein complex that functions as an important regulator in multiple signaling pathways. The structure and function of COP9 signalosome is similar to that of the 19S regulatory particle of 26S proteasome. COP9 signalosome has been shown to interact with SCF-type E3 ubiquitin ligases and act as a positive regulator of E3 ubiquitin ligases. This protein is reported to be involved in the degradation of cyclin-dependent kinase inhibitor CDKN1B/p27Kip1. It is also known to be a coactivator that increases the specificity of JUN/AP1 transcription factors.
Interactions
COP9 constitutive photomorphogenic homolog subunit 5 has been shown to interact with Macrophage migration inhibitory factor, GFER, BCL3, Ubiquitin carboxy-terminal hydrolase L1, S100A7 and C-jun.
See also
COPS1
COPS2
COPS3
COPS4
COPS6
COPS7A
COPS7B
COPS8
References
External links
Further reading |
https://en.wikipedia.org/wiki/PTPN22 | Protein tyrosine phosphatase non-receptor type 22 (PTPN22) is a cytoplasmatic protein encoded by gene PTPN22 and a member of PEST family of protein tyrosine phosphatases. This protein is also called "PEST-domain Enriched Phosphatase" ("PEP") or "Lymphoid phosphatase" ("LYP"). The name LYP is used strictly for the human protein encoded by PTPN22, but the name PEP is used only for its mouse homolog. However, both proteins have similar biological functions and show 70% identity in amino acid sequence. PTPN22 functions as a negative regulator of T cell receptor (TCR) signaling, which maintains homeostasis of T cell compartment.
Gene
Gene PTPN22 is located on the p arm of the human chromosome 1. It is nearly 58 000 base pairs long and contains 21 exons. In the case of mouse genome, it is located on the q arm of the chromosome 3. It is nearly 55 700 base pairs long and contains 23 exons.
Structure
PTPN22 is composed from 807 amino acids, and it weighs 91,705 kDa. On its N terminus it possesses catalytic domain, which shows the highest level of conservation between human and mouse proteins. Other parts of PTPN22 are less conserved. After catalytic domain PTPN22 has approximately 300 amino acids long domain called "Interdomain". On the C terminus of PTPN22 there are 4 proline-rich motifs (P1 - P4), which can mediate interactions with other proteins. P1 motif is the most important among them, because it is crucial for binding of CSK kinase, and allele encoding PTPN22 with mutated P |
https://en.wikipedia.org/wiki/ABCA4 | ATP-binding cassette, sub-family A (ABC1), member 4, also known as ABCA4 or ABCR, is a protein which in humans is encoded by the ABCA4 gene.
ABCA4 is a member of the ATP-binding cassette transporter gene sub-family A (ABC1) found exclusively in multicellular eukaryotes. The gene was first cloned and characterized in 1997 as a gene that causes Stargardt disease, an autosomal recessive disease that causes macular degeneration. The ABCA4 gene transcribes a large retina-specific protein with two transmembrane domains (TMD), two glycosylated extracellular domains (ECD), and two nucleotide-binding domains (NBD). The ABCA4 protein is almost exclusively expressed in retina localizing in outer segment disk edges of rod photoreceptors.
Structure
Previously known as the photoreceptor rim protein RmP or ABCR, the recently proposed ABCA4 structure consists of two transmembrane domains (TMDs), two large glycosylated extracytosolic domains (ECD), and two internal nucleotide binding domains (NBDs). One TMD spans across membranes with six units of protein linked together to form a domain. The TMDs are usually not conserved across genomes due to its specificity and diversity in function as channels or ligand-binding controllers. However, NBDs are highly conserved across different genomes—an observation consistent with which it binds and hydrolyzes ATP. NBD binds adenosine triphosphate molecules (ATP) to utilize the high-energy inorganic phosphate to carry out change in conformation of the A |
https://en.wikipedia.org/wiki/Calpain-1%20catalytic%20subunit | Calpain-1 catalytic subunit (CANP 1) is a protein that in humans is encoded by the CAPN1 gene.
Function
The calpains, calcium-activated neutral proteases, are nonlysosomal, intracellular cysteine proteases. The mammalian calpains include ubiquitous, stomach-specific, and muscle-specific proteins. The ubiquitous enzymes consist of heterodimers with distinct large, catalytic subunits associated with a common small, regulatory subunit. This gene encodes the large subunit of the ubiquitous enzyme, calpain 1.
Interactions
CAPN1 has been shown to interact with PSEN2.
References
Further reading
External links
The MEROPS online database for peptidases and their inhibitors: C02.001
EF-hand-containing proteins |
https://en.wikipedia.org/wiki/RUNX1T1 | Protein CBFA2T1 is a protein that in humans is encoded by the RUNX1T1 gene.
Function
The protein encoded by this gene is a putative zinc finger transcription factor and oncoprotein. In acute myeloid leukemia, especially in the M2 subtype, the t(8;21)(q22;q22) translocation is one of the most frequent karyotypic abnormalities. The translocation produces a chimeric gene made up of the 5'-region of the RUNX1 gene fused to the 3'-region of this gene. The chimeric protein is thought to associate with the nuclear corepressor/histone deacetylase complex to block hematopoietic differentiation. Several transcript variants encoding multiple isoforms have been found for this gene.
Interactions
RUNX1T1 has been shown to interact with:
CBFA2T2,
CBFA2T3,
Calcitriol receptor
GFI1,
Nuclear receptor co-repressor 1,
Nuclear receptor co-repressor 2,
PRKAR2A, and
Zinc finger and BTB domain-containing protein 16.
References
Further reading
Transcription factors |
https://en.wikipedia.org/wiki/Cyclin%20H | Cyclin-H is a protein that in humans is encoded by the CCNH gene.
Function
The protein encoded by this gene belongs to the highly conserved cyclin family, whose members are characterized by a dramatic periodicity in protein abundance through the cell cycle. Cyclins function as regulators of CDK kinases. Different cyclins exhibit distinct expression and degradation patterns which contribute to the temporal coordination of each mitotic event. This cyclin forms a complex with CDK7 kinase and ring finger protein MAT1. The kinase complex is able to phosphorylate CDK2 and CDC2 kinases, thus functions as a CDK-activating kinase (CAK). This cyclin and its kinase partner are components of TFIIH, as well as RNA polymerase II protein complexes. They participate in two different transcriptional regulation processes, suggesting an important link between basal transcription control and the cell cycle machinery.
Interactions
Cyclin H has been shown to interact with P53, Cyclin-dependent kinase 7 and MNAT1.
References
Further reading |
https://en.wikipedia.org/wiki/CDKN2B | Cyclin-dependent kinase 4 inhibitor B also known as multiple tumor suppressor 2 (MTS-2) or p15INK4b is a protein that is encoded by the CDKN2B gene in humans.
Function
This gene lies adjacent to the tumor suppressor gene CDKN2A in a region that is frequently mutated, deleted, or disregulated in a wide variety of cancer. This gene encodes a cyclin-dependent kinase inhibitor, also known as p15Ink4b protein, which forms a complex with CDK4 or CDK6, and prevents the activation of the CDK kinases by cyclin D, thus the encoded protein functions as a cell growth regulator that inhibits cell cycle G1 progression. The expression of this gene was found to be dramatically induced by TGF beta, which suggested its role in the TGF beta induced growth inhibition. Two alternatively spliced transcripts of this gene encode proteins that share the N-terminal sequence but completely differ in the C-terminus.
Interactions
CDKN2B tumor suppressor gene product p15 has been shown to interact with cyclin-dependent kinase 4.
References
Further reading
External links |
https://en.wikipedia.org/wiki/Fanconi%20anemia%2C%20complementation%20group%20C | Fanconi anemia group C protein is a protein that in humans is encoded by the FANCC gene. This protein delays the onset of apoptosis and promotes homologous recombination repair of damaged DNA. Mutations in this gene result in Fanconi anemia, a human rare disorder characterized by cancer susceptibility and cellular sensitivity to DNA crosslinks and other damages.
Structure
Function
A nuclear complex containing FANCC protein (as well as FANCA, FANCF and FANCG) is essential for the activation of the FANCD2 protein to the mono-ubiquitinated isoform. In normal, non-mutant, cells FANCD2 is mono-ubiquinated in response to DNA damage. FANCC together with FANCE acts as the substrate adaptor for this reaction Activated FANCD2 protein co-localizes with BRCA1 (breast cancer susceptibility protein) at ionizing radiation-induced foci and in synaptonemal complexes of meiotic chromosomes. Activated FANCD2 protein may function prior to the initiation of meiotic recombination, perhaps to prepare chromosomes for synapsis, or to regulate subsequent recombination events.
FANCC(-/-) mutant male and female mice have compromised gametogenesis, leading to markedly impaired fertility, a characteristic of Fanconi anemia patients. Both male and female FANCC mutant mice have reduced numbers of germ cells.
Interactions
Fanconi anemia, complementation group C has been shown to interact with:
Cdk1,
FANCA,
FANCE,
FANCF,
GSTP1,
HSPA1A,
SPTAN1,
STAT1, and
ZBTB32.
References
Furt |
https://en.wikipedia.org/wiki/Vitamin%20D-binding%20protein | Vitamin D-binding protein (DBP), also/originally known as gc-globulin (group-specific component), is a protein that in humans is encoded by the GC gene. DBP is genetically the oldest member of the albuminoid family and appeared early in the evolution of vertebrates.
Structure
Human GC is a glycosylated alpha-globulin, ~58 kDa in size. Its 458 amino acids are coded for by 1690 nucleotides on chromosome 4 (4q11–q13). The primary structure contains 28 cysteine residues forming multiple disulfide bonds. GC contains 3 domains. Domain 1 is composed of 10 alpha helices, domain 2 of 9, and domain 3 of 4.
Function
Vitamin D-binding protein belongs to the albumin gene family, together with human serum albumin and alpha-fetoprotein. It is a multifunctional protein found in plasma, ascitic fluid, cerebrospinal fluid and on the surface of many cell types.
It is able to bind the various forms of vitamin D including ergocalciferol (vitamin D2) and cholecalciferol (vitamin D3), the 25-hydroxylated forms (calcifediol), and the active hormonal product, 1,25-dihydroxyvitamin D (calcitriol). The major proportion of vitamin D in blood is bound to this protein. It transports vitamin D metabolites between skin, liver and kidney, and then on to the various target tissues.
As Gc protein-derived macrophage activating factor it is a Macrophage Activating Factor (MAF) that has been tested for use as a cancer treatment that would activate macrophages against cancer cells.
Interactive pathway ma |
https://en.wikipedia.org/wiki/Myocyte-specific%20enhancer%20factor%202A | Myocyte-specific enhancer factor 2A is a protein that in humans is encoded by the MEF2A gene. MEF2A is a transcription factor in the Mef2 family. In humans it is located on chromosome 15q26. Certain mutations in MEF2A cause an autosomal dominant form of coronary artery disease and myocardial infarction.
Function
The process of differentiation from mesodermal precursor cells to myoblasts has led to the discovery of a variety of tissue-specific factors that regulate muscle gene expression. The myogenic basic helix-loop-helix proteins, including myoD (MIM 159970), myogenin (MIM 159980), MYF5 (MIM 159990), and MRF4 (MIM 159991) are 1 class of identified factors. A second family of DNA binding regulatory proteins is the myocyte-specific enhancer factor-2 (MEF2) family. Each of these proteins binds to the MEF2 target DNA sequence present in the regulatory regions of many, if not all, muscle-specific genes. The MEF2 genes are members of the MADS gene family (named for the yeast mating type-specific transcription factor MCM1, the plant homeotic genes 'agamous' and 'deficiens' and the human serum response factor SRF (MIM 600589)), a family that also includes several homeotic genes and other transcription factors, all of which share a conserved DNA-binding domain.[supplied by OMIM]
Interactions
Myocyte-specific enhancer factor 2A has been shown to interact with:
ASCL1,
EP300,
HDAC4,
HDAC9,
Histone deacetylase 5,
MAPK14,
MEF2D,
Mothers against decapentaplegic hom |
https://en.wikipedia.org/wiki/Glycodelin | Glycodelin (GD) also known as human placental protein-14 (PP-14) progestogen-associated endometrial protein (PAEP) or pregnancy-associated endometrial alpha-2 globulin is a glycoprotein that inhibits cell immune function and plays an essential role in the pregnancy process. In humans is encoded by the PAEP gene.
Human endometrium synthesizes several proteins under the influence of progesterone. Of these proteins, glycodelin is of particular interest. It is synthesized by the endometrial glands in the luteal phase of menstrual cycle.
The temporal and spatial expression of GD in the female reproductive tract combined with its biological activities suggest that this glycoprotein probably plays an essential physiological role in the regulation of fertilization, implantation and maintenance of pregnancy.
Structure
Glycodelin is codified by 180 amino acid but it is thought that 18 of these are supposed signals peptides. The molecular weight of GD is 20,555, while its mature form is estimated to weigh 18,787. It is encoded by a 1-kilobase-pair mRNA that is expressed in human secretory endometrium and decidua but not in postmenopausal endometrium, placenta, liver, kidney, and adrenals.
The four cysteinyl residues (positions 66, 106, 119, and 160) responsible for intramolecular disulfide bridges in lactoglobulins are all conserved in GD. Southern blot analysis of human DNA suggested that GD gene sequences compass some 20 kilobase pairs of the human genomic DNA.
N-terminal amino |
https://en.wikipedia.org/wiki/PEDF | Pigment epithelium-derived factor (PEDF) also known as serpin F1 (SERPINF1), is a multifunctional secreted protein that has anti-angiogenic, anti-tumorigenic, and neurotrophic functions. Found in vertebrates, this 50 kDa protein is being researched as a therapeutic candidate for treatment of such conditions as choroidal neovascularization, heart disease, and cancer. In humans, pigment epithelium-derived factor is encoded by the SERPINF1 gene.
Discovery
Pigment epithelium-derived factor (PEDF) was originally discovered by Joyce Tombran-Tink and Lincoln Johnson in the late 1980s. This group was studying human retinal cell development by identifying secreted factors produced by the retinal pigmented epithelium (RPE), a layer of cells that supports the retina. Upon noticing RPE produced a factor that promoted the differentiation of primitive retinal cells into cells of a neuronal phenotype, they set out to determine the identity of the factor. They isolated proteins unique to RPE cells and tested the individual proteins for neurotrophic function, meaning promoting a neuronal phenotype. A neurotrophic protein around 50 kilodaltons (kDa) was identified and temporarily named RPE-54 before being officially termed pigment epithelium-derived factor.
Soon thereafter, the same laboratory sequenced the PEDF protein and compared it to a human fetal eye library. They found that PEDF was a previously uncharacterized protein and a member of the serpin (serine protease inhibitor) family.
|
https://en.wikipedia.org/wiki/Polycystin%202 | Polycystin-2 (PC2) is a protein that in humans is encoded by the PKD2 gene.
The gene PKD2 also known as TRPP2, encodes a member of the polycystin protein family, called TRPP, and contains multiple transmembrane domains, and cytoplasmic N- and C-termini. The protein may be an integral membrane protein involved in cell-cell/matrix interactions. TRPP2 may function in renal tubular development, morphology, and function, and may modulate intracellular calcium homeostasis and other signal transduction pathways. This protein interacts with polycystin 1 (TRPP1) to produce cation-permeable currents. It was discovered by Stefan Somlo at Yale University.
Clinical significance
Mutations in this gene have been associated with autosomal dominant polycystic kidney disease.
Interactions
Polycystin 2 has been shown to interact with the proteins TRPC1, PKD1 and TNNI3.
See also
HAX1
TRPP
References
Further reading
External links
GeneReviews/NIH/NCBI/UW entry on Polycystic Kidney Disease, Autosomal Dominant
EF-hand-containing proteins |
https://en.wikipedia.org/wiki/PSMC5 | 26S protease regulatory subunit 8, also known as 26S proteasome AAA-ATPase subunit Rpt6, is an enzyme that in humans is encoded by the PSMC5 gene. This protein is one of the 19 essential subunits of a complete assembled 19S proteasome complex Six 26S proteasome AAA-ATPase subunits (Rpt1, Rpt2, Rpt3, Rpt4, Rpt5, and Rpt6 (this protein)) together with four non-ATPase subunits (Rpn1, Rpn2, Rpn10, and Rpn13) form the base sub complex of 19S regulatory particle for proteasome complex.
Gene
The gene PSMC5 encodes one of the ATPase subunits, a member of the triple-A family of ATPases which have a chaperone-like activity. In addition to participation in proteasome functions, this subunit may participate in transcriptional regulation since it has been shown to interact with the thyroid hormone receptor and retinoid X receptor-alpha. The human PSMC5 gene has 13 exons and locates at chromosome band 17q23.3.
Protein
The human protein 26S protease regulatory subunit 8 is 45.6kDa in size and composed of 406 amino acids. The calculated theoretical pI of this protein is 8.23.
Complex assembly
26S proteasome complex is usually consisted of a 20S core particle (CP, or 20S proteasome) and one or two 19S regulatory particles (RP, or 19S proteasome) on either one side or both side of the barrel-shaped 20S. The CP and RPs pertain distinct structural characteristics and biological functions. In brief, 20S sub complex presents three types proteolytic activities, including caspase-like, tr |
https://en.wikipedia.org/wiki/RHCE%20%28gene%29 | Blood group Rh(CE) polypeptide is a protein that in humans is encoded by the RHCE gene. RHCE has also recently been designated CD240CE (cluster of differentiation 240CE).
The Rh blood group system is the second most clinically significant of the blood groups, second only to ABO. It is also the most polymorphic of the blood groups, with variations due to deletions, gene conversions, and missense mutations. The Rh blood group includes this gene which encodes both the RhC and RhE antigens on a single polypeptide and a second gene which encodes the RhD protein. The classification of Rh-positive and Rh-negative individuals is determined by the presence or absence of the highly immunogenic RhD protein on the surface of erythrocytes. Alternative splicing of this gene results in four transcript variants encoding four different isoforms.
A recent study in the population of the island of Sardinia shows the association of a noncoding variant in the RHCE gene (rs630337) with an increased erythrocyte sedimentation rate(ESR). This suggest a possible causal effect of this polymorphism on this inflammatory marker despite not found in coding region of the gene.
References
Further reading
External links
Clusters of differentiation |
https://en.wikipedia.org/wiki/SCNN1B | The SCNN1B gene encodes for the β subunit of the epithelial sodium channel ENaC in vertebrates. ENaC is assembled as a heterotrimer composed of three homologous subunits α, β, and γ or δ, β, and γ. The other ENAC subunits are encoded by SCNN1A, SCNN1G, and SCNN1D.
ENaC is expressed in epithelial cells and is different from the voltage-gated sodium channel that is involved in the generation of action potentials in neurons. The abbreviation for the genes encoding for voltage-gated sodium channel starts with three letters: SCN. In contrast to these sodium channels, ENaC is constitutively active and is not voltage-dependent. The second N in the abbreviation (SCNN1A) represents that these are NON-voltage-gated channels.
In most vertebrates, sodium ions are the major determinant of the osmolarity of the extracellular fluid. ENaC allows transfer of sodium ions across the epithelial cell membrane in so-called "tight-epithelia" that have low permeability. The flow of sodium ions across epithelia affects osmolarity of the extracellular fluid. Thus, ENaC plays a central role in the regulation of body fluid and electrolyte homeostasis and consequently affects blood pressure.
As ENaC is strongly inhibited by amiloride, it is also referred to as an "amiloride-sensitive sodium channel".
History
The first cDNA encoding the beta subunit of ENaC was cloned and sequenced by Canessa et al. from rat mRNA. A year later, two independent groups reported the cDNA sequences of the beta- and gamm |
https://en.wikipedia.org/wiki/SOX9 | Transcription factor SOX-9 is a protein that in humans is encoded by the SOX9 gene.
Function
SOX-9 recognizes the sequence CCTTGAG along with other members of the HMG-box class DNA-binding proteins. It is expressed by proliferating but not hypertrophic chondrocytes that is essential for differentiation of precursor cells into chondrocytes and, with steroidogenic factor 1, regulates transcription of the anti-Müllerian hormone (AMH) gene.
SOX-9 also plays a pivotal role in male sexual development; by working with Sf1, SOX-9 can produce AMH in Sertoli cells to inhibit the creation of a female reproductive system. It also interacts with a few other genes to promote the development of male sexual organs. The process starts when the transcription factor Testis determining factor (encoded by the sex-determining region SRY of the Y chromosome) activates SOX-9 activity by binding to an enhancer sequence upstream of the gene. Next, Sox9 activates FGF9 and forms feedforward loops with FGF9 and PGD2. These loops are important for producing SOX-9; without these loops, SOX-9 would run out and the development of a female would almost certainly ensue. Activation of FGF9 by SOX-9 starts vital processes in male development, such as the creation of testis cords and the multiplication of Sertoli cells. The association of SOX-9 and Dax1 actually creates Sertoli cells, another vital process in male development. In the brain development, its murine ortholog Sox-9 induces the expression of Wwp1 |
https://en.wikipedia.org/wiki/SPTAN1 | Alpha II-spectrin, also known as Spectrin alpha chain, brain is a protein that in humans is encoded by the SPTAN1 gene. Alpha II-spectrin is expressed in a variety of tissues, and is highly expressed in cardiac muscle at Z-disc structures, costameres and at the sarcolemma membrane. Mutations in alpha II-spectrin have been associated with early infantile epileptic encephalopathy-5, and alpha II-spectrin may be a valuable biomarker for Guillain–Barré syndrome and infantile congenital heart disease.
Structure
Alternate splicing of alpha II-spectrin has been documented and results in multiple transcript variants; specifically, cardiomyocytes have four identified alpha II-spectrin splice variants. As opposed to alpha I-spectrin that is principally found in erythrocytes, alpha II-spectrin is expressed in most tissues. In cardiac tissue, alpha II-spectrin is found in myocytes at Z-discs, costameres, and the sarcolemma membrane, and in cardiac fibroblasts along the surface of the cytoskeletal network. Alpha II-spectrin most commonly exists in a heterodimer with alpha II and beta II spectrin subunits; and dimers typically self-associate and heterotetramerize.
Function
The spectrins are a family of widely distributed cytoskeletal proteins which are involved in actin crosslinking, cell adhesion, intercellular communication and cell cycle regulation. Though a role in cardiac muscle is not well understood, it is likely that alpha II-spectrin is involved in organizing sub-sarcolemmal do |
https://en.wikipedia.org/wiki/Telomeric%20repeat-binding%20factor%201 | Telomeric repeat-binding factor 1 is a protein that in humans is encoded by the TERF1 gene.
Gene
The human TERF1 gene is located in the chromosome 8 at 73,921,097-73,960,357 bp. Two transcripts of this gene are alternatively spliced products. The TERF1 gene is also known as TRF, PIN2 (Proteinase Inhibitor 2), TRF1, t-TRF1 and h-TRF1-AS.
Protein
The protein structure contains a C-terminal Myb motif, a dimerization domain (TERF homology) near its N-terminus and an acidic N-terminus.
Subcellular distribution
The cellular distribution of this DNA binding protein features the nucleoplasm, chromosomes, a telomeric region, a nuclear telomere cap complex, the cytoplasm, the spindle, the nucleus and a nucleolus and a nuclear chromosome.
Function
TERF 1 gene encodes a telomere specific protein which is a component of the telomere's shelterin nucleoprotein complex. This protein is present at telomeres throughout the cell cycle and functions as an inhibitor of telomerase, acting in cis to limit the elongation of individual chromosome ends. It is known to protect telomeres in mammals from DNA mechanisms that are used for repair purposes and at the same time regulate the activity carried out by telomerase. The telomeric repeat binding factor 1 protein is present at telomeres, where the cells aging aspect is monitored, throughout the typical cell cycle process. The progressive loss of the telomeric ends of chromosomes is an important mechanism in the timing of human cellular agin |
https://en.wikipedia.org/wiki/Trefoil%20factor%201 | Trefoil factor 1 is a protein that in humans is encoded by the TFF1 gene (also called pS2 gene).
Function
Members of the trefoil family are characterized by having at least one copy of the trefoil motif, a 40-amino acid domain that contains three conserved disulfides. They are stable secretory proteins expressed in gastrointestinal mucosa. Their functions are not defined, but they may protect the mucosa from insults, stabilize the mucus layer, and affect healing of the epithelium. This gene, which is expressed in the gastric mucosa, has also been studied because of its expression in human tumors. This gene and two other related trefoil family member genes are found in a cluster on chromosome 21.
Glycan binding
All three human trefoil factors are lectins that interact specifically with the disaccharide GlcNAc-α-1,4-Gal. This disaccharide is an unusual glycotope that is only known to exist on the large, heavily glycosylated, mucins in the mucosa. By cross-linking mucins through the bivalent binding of this glycotope, the trefoil factors are then able to reversibly modulate the thickness and viscosity of the mucus.
In gastric carcinoma
TFF1 expression is frequently lost in gastric carcinoma, probably through mechanism of DNA methylation, and it is therefore considered as a tumor suppressor gene.
References
Further reading |
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