source stringlengths 32 209 | text stringlengths 18 1.5k |
|---|---|
https://en.wikipedia.org/wiki/MAP2K3 | Dual specificity mitogen-activated protein kinase kinase 3 is an enzyme that in humans is encoded by the MAP2K3 gene.
The protein encoded by this gene is a dual specificity protein kinase that belongs to the MAP kinase kinase family. This kinase is activated by mitogenic and environmental stress, and participates in the MAP kinase-mediated signaling cascade. It phosphorylates and thus activates MAPK14/p38-MAPK. This kinase can be activated by insulin, and is necessary for the expression of glucose transporter. Expression of RAS oncogene is found to result in the accumulation of the active form of this kinase, which thus leads to the constitutive activation of MAPK14, and confers oncogenic transformation of primary cells. The inhibition of this kinase is involved in the pathogenesis of Yersinia pseudotuberculosis. Multiple alternatively spliced transcript variants that encode distinct isoforms have been reported for this gene.
Interactions
MAP2K3 has been shown to interact with TAOK2 and PLCB2.
References
Further reading
EC 2.7.12 |
https://en.wikipedia.org/wiki/NOX1 | NADPH oxidase 1 is an enzyme that in humans is encoded by the NOX1 gene.
NOX1 is a homolog of the catalytic subunit of the superoxide-generating NADPH oxidase of phagocytes, gp91phox. Two transcript variants encoding different isoforms have been found for this gene.
References
Further reading |
https://en.wikipedia.org/wiki/HIPK2 | Homeodomain-interacting protein kinase 2 is an enzyme that in humans is encoded by the HIPK2 gene. HIPK2 can be categorized as a Serine/Threonine Protein kinase, specifically one that interacts with homeodomain transcription factors. It belongs to a family of protein kinases known as the DYRK kinases. Within this family HIPK2 belongs to a group of homeodomain-interacting protein kinases (HIPKs), including HIPK1 and HIPK3. HIPK2 can be found in a wide variety of species and its functions in gene expression and apoptosis are regulated by several different mechanisms.
Discovery
HIPK2 was discovered concurrently with HIPKs 1 and 3 in 1998. The HIPKs were discovered during an experiment that tried to identify genes that when expressed, yielded products that interacted with transcription factors related to the NK homeodomain . HIPKs were discovered using a technique called Two-hybrid screening. Two-hybrid screening is in conjunction with cDNA cloning, in which embryonic mouse cDNA libraries were used with mouse homeoprotein Nkx-1.2 to find genes involved with homeodomain transcription factors. The researchers found two clones that were similar in protein sequence, demonstrated a strong interaction with the homeoprotein, and an active site characteristic of protein kinases. These characteristics led to the name "HIPK". In 2000, the location of the HIPK2 gene was discovered to be on the long arm of Chromosome 7 (human) in the human genome. In mice, HIPK2 was discovered to be on Ch |
https://en.wikipedia.org/wiki/PTK2B | Protein tyrosine kinase 2 beta is an enzyme that in humans is encoded by the PTK2B gene.
Function
This gene encodes a cytoplasmic protein tyrosine kinase that is involved in calcium-induced regulation of ion channels and activation of the MAP kinase signaling pathway. The encoded protein may represent an important signaling intermediate between neuropeptide-activated receptors or neurotransmitters that increase calcium flux and the downstream signals that regulate neuronal activity.
The encoded protein undergoes rapid tyrosine phosphorylation and activation in response to increases in the intracellular calcium concentration
, nicotinic acetylcholine receptor activation, membrane depolarization, or protein kinase C activation. In addition, SOCE-induced Pyk2 activation mediates disassembly of endothelial adherens junctions, via tyrosine (Y1981-residue) phosphorylation of VE-PTP.
This protein has been shown to bind a CRK-associated substrate, a nephrocystin, a GTPase regulator associated with FAK, and the SH2 domain of GRB2.
The encoded protein is a member of the FAK subfamily of protein tyrosine kinases but lacks significant sequence similarity to kinases from other subfamilies. Four transcript variants encoding two different isoforms have been found for this gene.
Interactions
PTK2B has been shown to interact with:
BCAR1,
Cbl gene,
DDEF2,
DLG3,
DLG4,
Ewing sarcoma breakpoint region 1,
FYN,
GRIN2A,
Gelsolin,
NPHP1,
PITPNM1,
PTPN11,
PTPN6,
P |
https://en.wikipedia.org/wiki/Lloyd%20R.%20Welch | Lloyd Richard Welch (born September 28, 1927) is an American information theorist and applied mathematician, and co-inventor of the Baum–Welch algorithm and the Berlekamp–Welch algorithm, also known as the Welch–Berlekamp algorithm.
Welch received his B.S. in mathematics from the University of Illinois, 1951, and Ph.D. in mathematics from the California Institute of Technology, 1958, under advisor Frederic Bohnenblust. He worked at the Jet Propulsion Laboratory 1956–1959, Institute for Defense Analyses in Princeton, 1959–1965, and University of Southern California, 1965–1999. He was elected a member of the National Academy of Engineering in 1979 for "contributions to an understanding of possibilities, limitations, and design of communications coding for reliability, security, and synchronization". He is also an IEEE Fellow, and received the 2003 Claude E. Shannon Award.
References
University of Southern California faculty web page
National Academy of Engineering
Caltech thesis
AMS genealogy
American information theorists
Members of the United States National Academy of Engineering
Possibly living people
1927 births
University of Illinois alumni
California Institute of Technology alumni
University of Southern California faculty |
https://en.wikipedia.org/wiki/Membership%20statistics%20of%20the%20Church%20of%20Jesus%20Christ%20of%20Latter-day%20Saints | The Church of Jesus Christ of Latter-day Saints (LDS Church) releases membership, congregational, and related information on a regular basis. The latest membership information LDS Church releases includes a count of membership, stakes, wards, branches, missions, temples, and family history centers for the worldwide church and for individual countries and territories where the church is recognized. The latest information released was as of December 31, 2022.
At the end of 2022, the LDS Church had 31,330 congregations and a reported membership of 17,002,461.
Membership defined
The LDS Church defines membership as a count of living individuals who:
have been baptized and confirmed.
are under age nine and have been blessed but not baptized.
are not accountable because of intellectual disabilities, regardless of age.
are unblessed children under age eight when:
two member parents request it; or
one member parent requests it and the nonmember parent gives permission.
After baptism, blessing, or parental request stated above, membership must be recorded and maintained by the church to have and keep membership.
Membership considerations
In 2005, Peggy Fletcher Stack, longtime religion columnist for The Salt Lake Tribune, estimated that about one-third of the reported LDS membership was "active" (i.e., regularly attending church services and participating in other expected meetings and obligations). In 2005, this would have amounted to approximately 4 million active member |
https://en.wikipedia.org/wiki/The%20Daily%20Observer | The Daily Observer is a newspaper published in Bakau in Banjul, the Gambia.
The paper, Gambia's first daily newspaper, was founded by Mae Gene and Kenneth Best in 1990. Kenneth Best had previously managed another paper called the Daily Observer in Liberia, until the First Liberian Civil War caused him to relocate with his family to the Gambia. In October 1994, following Yahya Jammeh's military coup, Best was expelled from Gambia, although the newspaper was allowed to continue. It was eventually shutdown by tax authorities on 23 August 2017 for non-compliance of its tax obligations.
In the early 1990s, the paper ran its History Corner on its weekend supplement (the Weekend Observer). The Gambian statesman and historian Alieu Ebrima Cham Joof "pioneered" this column (the History Corner) in 1993 before asking the paper's resident journalist Hassoum Ceesay to take over the column. Ceesay took over it in 1996.
Some of the topics covered during the tenure of Cham Joof included:
History Corner with Alhaji A. E Cham Joof, Diamond Jubilee of Scouting in The Gambia, Senegambian Scouting Joint Committee Senegalo/Gambian Katibougou old Scouts (Weekend Observer, 29–31 March 1995. p. 9 (Gambia))
History Corner with Alhaji A. E Cham Joof, The History of the Banjul Mosque, (Weekend Observer, 5–7 May 1995)
Ebrima Manneh case
In July 2006, Observer reporter Ebrima Manneh was reportedly arrested by state security after attempting to republish a BBC report criticizing Jammeh shortly before a |
https://en.wikipedia.org/wiki/ABCG2 | ATP-binding cassette super-family G member 2 is a protein that in humans is encoded by the ABCG2 gene. ABCG2 has also been designated as CDw338 (cluster of differentiation w338). ABCG2 is a translocation protein used to actively pump drugs and other compounds against their concentration gradient using the bonding and hydrolysis of ATP as the energy source.
ABCG2 forms into a homodimer to assume its active transport conformation. The dimer weighs approximately 144 kDa. The expression of this transport protein is highly conserved throughout the animal kingdom, pointing to its importance.
Substrate binding with compounds occurs in the large central cavity. ABCG2 can bind to a broad range of compounds but binds strongest to flat, polycyclic chemicals with lots of hydrophobic character.
Function
The membrane-associated protein encoded by this gene is included in the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intra-cellular membranes. The active transport of chemicals requires a source of energy to catalyze the conformational changes the protein undergoes. The nucleotide-binding domains (NBDs) found towards the N-terminus allow binding to ATP molecules. The NBD and the transmembrane domain (TMD) are the most conserved region of the transporter in various animal groups, highlighting the importance of these regions for overall protein function. Additionally, many ABC transporters have conserved NBD regions s |
https://en.wikipedia.org/wiki/MRX | MRX may refer to:
The ABCG2 gene
MRX complex, DNA damage repair complex in yeast
The Magnetic Reconnection eXperiment led by DoE's Princeton Plasma Physics Laboratory
Mahshahr Airport, Iran, by IATA airport code
Philips HeartStart MRx cardiac monitor/defibrillator
Proposed pressurized water reactor for ship propulsion developed by the Japan Atomic Energy Research Institute (JAERI)
ម៉ែ រុំ |
https://en.wikipedia.org/wiki/ASIX | ASIX Electronics Corp. () is a fabless semiconductor supplier with a focus on networking, communication, and connectivity applications. ASIX Electronics specializes in Ethernet-centric silicon products such as non-PCI Ethernet controller, USB 2.0 to LAN controller, and network SoC for embedded networking applications.
Corporate history
ASIX was founded in May 1995 in Hsinchu Science Park, Taiwan. In 2002, ASIX announced its first USB to MII chip. In June 2007, electronicstalk.com featured the AX11005BF, billed as the industry smallest single-chip embedded Ethernet MCU. Electronicstalk.com describes powering embedded systems in a machine to machine world (M2M) in reference to the AX110xx family of chips.
ASIX Electronics introduced the industry's first:
USB 3.0 to Gigabit Ethernet controller
Non-PCI/USB 2.0 Gigabit Ethernet controller
Single chip microcontroller with TCP/IP, 10/100 Mbit Fast Ethernet MAC/PHY, and flash
Industry smallest single chip embedded Ethernet MCU
Asix Electronics saw its revenues jump 59.3% sequentially to NT$31.5 million (US$957,000) in December 2006 on shipments of USB-to-Ethernet controller ICs for Nintendo's Wii consoles, according to market sources.
ASIX is listed as a vendor in the 2007 EDN Microprocessor Directory.
ASIX Electronics Corp:To acquire 100 pct stake in ZYWYN CORPORATION with amount of $8 million.
Products
The current offerings are as follows:
Non-PCI/PCMCIA embedded Ethernet
High-speed USB-to-LAN
Embedded network SoC
|
https://en.wikipedia.org/wiki/O-6-methylguanine-DNA%20methyltransferase | O6-alkylguanine DNA alkyltransferase (also known as AGT, MGMT or AGAT) is a protein that in humans is encoded by the O6-methylguanine DNA methyltransferase (MGMT) gene.
O6-methylguanine DNA methyltransferase is crucial for genome stability. It repairs the naturally occurring mutagenic DNA lesion O6-methylguanine back to guanine and prevents mismatch and errors during DNA replication and transcription. Accordingly, loss of MGMT increases the carcinogenic risk in mice after exposure to alkylating agents.
The two bacterial isozymes are Ada and Ogt.
Function and mechanism
Although alkylating mutagens preferentially modify the guanine base at the N7 position, O6-alkyl-guanine is a major carcinogenic lesion in DNA. This DNA adduct is removed by the repair protein O6-alkylguanine DNA alkyltransferase through an SN2 mechanism. This protein is not a true enzyme since it removes the alkyl group from the lesion in a stoichiometric reaction and the active enzyme is not regenerated after it is alkylated (referred to as a suicide enzyme). The methyl-acceptor residue in the protein is a cysteine.
Demethylation of 6-O-methylguanosine to Guanosine
Clinical significance
In patients with glioblastoma, a severe type of brain tumor, the cancer medicine temozolomide is more effective in those with a methylation of the gene's promoter. Overall, MGMT methylation is associated with prolonged patient survival in clinical prediction models. For testing of the MGMT promoter methylation status in th |
https://en.wikipedia.org/wiki/ABCC1 | Multidrug resistance-associated protein 1 (MRP1) is a protein that in humans is encoded by the ABCC1 gene.
Function
The protein encoded by this gene is a member of the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra-and intra-cellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This full transporter is a member of the MRP subfamily which is involved in multi-drug resistance. This protein functions as a multispecific organic anion transporter, with oxidized glutathione, cysteinyl leukotrienes, and activated aflatoxin B1 as substrates. This protein also transports glucuronides and sulfate conjugates of steroid hormones and bile salts. Alternative splicing by exon deletion results in several splice variants but maintains the original open reading frame in all forms.
Structure
ABCC1 is a 190 kDa protein that contains two membrane-spanning domains of hydrophobic nature and two nucleotide binding domains. Each membrane-spanning domain is made up of six α-helices. In addition, the protein also contains a third membrane-spanning domain that sets it apart from other transporters within the ATP-binding cassette family of transporters. The two nucleotide binding domains have a functional asymmetry that plays a significant role in the ability of ATP to power the transporter. The first nucleotide binding domain, which is delegated NBD1, is responsible for t |
https://en.wikipedia.org/wiki/CFLAR | CASP8 and FADD-like apoptosis regulator is a protein that in humans is encoded by the CFLAR gene. Also called c-FLIP (FLICE-like inhibitory protein).
References
Further reading
External links |
https://en.wikipedia.org/wiki/HRX | HRX may refer to:
Zinc finger protein HRX, or simply HRX, an enzyme
Hypo Real Estate (stock ticker symbol: HRX), a German company
hrx, the ISO 639 language code of the Hunsrik language. |
https://en.wikipedia.org/wiki/RETN | RETN may refer to:
RETN (ISP), a Tier 2 ISP in Europe headquartered in London
Resistin, a protein encoded by RETN gene. |
https://en.wikipedia.org/wiki/Cyclin%20E1 | G1/S-specific cyclin-E1 is a protein that in humans is encoded by the CCNE1 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. Different cyclins exhibit distinct expression and degradation patterns which contribute to the temporal coordination of each mitotic event. This cyclin forms a complex with and functions as a regulatory subunit of CDK2, whose activity is required for cell cycle G1/S transition. This protein accumulates at the G1-S phase boundary and is degraded as cells progress through S phase. Overexpression of this gene has been observed in many tumors, which results in chromosome instability, and thus may contribute to tumorigenesis. This protein was found to associate with, and be involved in, the phosphorylation of NPAT protein (nuclear protein mapped to the ATM locus), which participates in cell-cycle regulated histone gene expression and plays a critical role in promoting cell-cycle progression in the absence of pRB. Two alternatively spliced transcript variants of this gene, which encode distinct isoforms, have been described. Two additional splice variants were reported but detailed nucleotide sequence information is not yet available.
Interactions
Cyclin E1 has been shown to interact with:
CDC25A,
CDKN1B,
CUL3
Cdk1,
Cyclin-dependent kinase 2,
HERC5,
P21,
|
https://en.wikipedia.org/wiki/NR4A | NR4A (nuclear receptor subfamily 4A) is a family of orphan nuclear receptors which act as transcription factors in neuron development and maintenance. In 2006, it was shown that members of the NR4A family were implicated in the control of skeletal muscle metabolism.
Three members have been identified in humans:
Nuclear receptor 4A1 (),
Nuclear receptor 4A2 (), and
Nuclear receptor 4A3 ().
References
Intracellular receptors
Transcription factors |
https://en.wikipedia.org/wiki/Goodbye%20Priscilla%20%28Bye%20Bye%20Baby%20Blue%29 | "Goodbye Priscilla (Bye Bye Baby Blue)" is a song written by Deanna Summers, David Saxton and Ben Shaw. It was published by Silicon Music, BMI in 1977 and first recorded by Gene Summers that same year. The song was initially released by Tear Drop Records as a one-sided, promotional, single and later re-issued with "World Of Illusion" as the flip side (#TD 3405).
"Goodbye Priscilla" was written as a tribute to Elvis and Priscilla Presley. The "Goodbye Priscilla" 45 is now a much-sought-after collectible and has been issued on several Elvis "tribute" compilation albums and CDs. When "Goodbye Priscilla (Bye Bye Baby Blue)" was first released there was a controversy about which Priscilla it was written for: Priscilla Presley, or Priscilla Davis, wife of T. Cullen Davis and central figure in the T. Cullen Davis murder trials. In his book Blood Will Tell: The Murder Trials Of Cullen Davis author Gary Cartwright credited the song (page 199) as referring to Priscilla Davis.
References
Discography references
Gene Summers discography from Rockin' Country Style, United States
Gene Summers discography from Rocky Productions, France
Gene Summers discography from Wangdangdula Finland
Gene Summers session data from Tapio's Fin-A-Billy, Finland
Sources
"Blood Will Tell: The Murder Trials Of T. Cullen Davis" by Gary Cartwright (published by Pocket Books USA 1978/1980)
Liner notes "The Ultimate School Of Rock & Roll" 1997 United States
Article and sessionography in issue 15 (1977) of New |
https://en.wikipedia.org/wiki/MHC%20class%20I%20polypeptide%E2%80%93related%20sequence%20A | MHC class I polypeptide–related sequence A (MICA) is a highly polymorphic cell surface glycoprotein encoded by the MICA gene located within MHC locus. MICA is related to MHC class I and it has similar domain structure, however, it is not associated with β2-microglobulin nor binds peptides as conventional MHC class I molecules do. MICA rather functions as a stress-induced ligand (as a danger signal) for integral membrane protein receptor NKG2D ("natural-killer group 2, member D"). MICA is broadly recognized by NK cells, γδ T cells, and CD8+ αβ T cells which carry NKG2D receptor on their cell surface and which are activated via this interaction.
Structure
The MICA gene is highly polymorphic in humans with more than 50 defined alleles. It is located on chromosome 6 and the protein is expressed in two isoforms formed by alternative splicing: MICA1 and MICA2 which is lacking exon 3. MICA contains external α1α2α3 domain, transmembrane segment and C-terminal cytoplasmic tail. It binds in a form of monomer to a KLRK1/NKG2D homodimer.
There are no orthologs of the MICA in mice species.
Expression
Expression of MICA can be upregulated by heat shock or by exposure of the cells to DNA damaging conditions (for example ionizing radiation, chromatin-modifying interventions and inhibitors of DNA replication). The expression can be as well affected by some infectious agents such as human cytomegalovirus (HCMV), human adenovirus 5, M. tuberculosis, diarrheagenic E.coli, or human papilloma |
https://en.wikipedia.org/wiki/TOP1 | DNA topoisomerase 1 is an enzyme that in humans is encoded by the TOP1 gene. It is a DNA topoisomerase, an enzyme that catalyzes the transient breaking and rejoining of a single strand of DNA.
Function
This gene encodes a DNA topoisomerase, an enzyme that controls and alters the topologic states of DNA during transcription. This enzyme catalyzes the transient breaking and rejoining of a single strand of DNA which lets the broken strand rotate around the intact strand, thus altering the topology of DNA. This gene is localized to chromosome 20 and has pseudogenes which reside on chromosomes 1 and 22.
Mechanism
As reviewed by Champoux, the type IB topoisomerases, including TOP1, form a covalent intermediate in which the active site tyrosine becomes attached to the 3' phosphate end of the cleaved strand rather than the 5' phosphate end.
The eukaryotic topoisomerases I were found to nick the DNA with a preference for a sequence of nucleotides that extends from positions -4 to -1 from the nick. The preferred nucleotides in the strand to be cut are 5'-(A/T)(G/C)(A/T)T-3' with the enzyme covalently attached to the -1 T residue, though sometimes a C residue is found at the -1 position.
The TOP1 protein of humans has been subdivided into four regions. The N-terminal 214 amino acids are dispensable for relaxation of supercoiling activity in vitro and there are four nuclear localization signals and sites for interaction with other cellular proteins within the N-terminal domain. |
https://en.wikipedia.org/wiki/SMN1 | Survival of motor neuron 1 (SMN1), also known as component of gems 1 or GEMIN1, is a gene that encodes the SMN protein in humans.
Gene
SMN1 is the telomeric copy of the gene encoding the SMN protein; the centromeric copy is termed SMN2. SMN1 and SMN2 are part of a 500 kbp inverted duplication on chromosome 5q13. This duplicated region contains at least four genes and repetitive elements which make it prone to rearrangements and deletions. The repetitiveness and complexity of the sequence have also caused difficulty in determining the organization of this genomic region. SMN1 and SMN2 are nearly identical and encode the same protein. The critical sequence difference between the two is a single nucleotide in exon 7 which is thought to be an exon splice enhancer. It is thought that gene conversion events may involve the two genes, leading to varying copy numbers of each gene.
Clinical significance
Mutations in SMN1 are associated with spinal muscular atrophy. Mutations in SMN2 alone do not lead to disease, although mutations in both SMN1 and SMN2 result in embryonic death.
References
Further reading
External links
Spinal muscular atrophy |
https://en.wikipedia.org/wiki/SMNC | SMNC may refer to:
Super Monday Night Combat, a 2012 third-person shooter video game
Survival of motor neuron centromeric, a gene involved in the assembly of snRNPs |
https://en.wikipedia.org/wiki/Cancer%20in%20cats | Cancer in cats is the leading cause of death among cats. It is caused by uncontrolled cell growth, and affects a wide range of cell types and organs in the body. Feline cancer initially manifests as a lump or bump on any parts of the body. It rapidly grows in the affected cell; attaches itself to the tissue under the skin in that area; and, depending on the tumour, it can spread to other parts of the body. Although cancer accounts for approximately 32% of deaths in cats over ten years old, it can be successfully treated if diagnosed early.
While the causes of cancer in cats are unknown, feline leukemia virus is suspected to be a prime contributor. Other factors suspected to increase rates of feline cancer include toxins from the environment, passive smoking, excessive grooming, or licking parts of the body that have been in contact with an environmental toxin.
Cancer can be detected at an early stage by observing certain signs and symptoms. Common diagnostic methods include physical examination, x-rays, ultrasounds, cytology, blood tests, urine tests, and nuclear scans. Depending on the type of cancer and its level of progress, surgery, radiation, chemotherapy, or immunotherapy may be used to treat the cancer. Although research into causes and treatment of feline cancers has been slow, there have been advances in radiation therapy, as well as newer and improved chemotherapy procedures.
Signs and symptoms
Cancer in cats can occur in any location or body system, and most sy |
https://en.wikipedia.org/wiki/DAPK1 | Death-associated protein kinase 1 is an enzyme that in humans is encoded by the DAPK1 gene.
Function
Death-associated protein kinase 1 is a positive mediator of gamma-interferon induced programmed cell death. DAPK1 encodes a structurally unique 160-kD calmodulin dependent serine-threonine kinase that carries 8 ankyrin repeats and 2 putative P-loop consensus sites. It is a tumor suppressor candidate.
In melanocytic cells DAPK1 gene expression may be regulated by MITF.
As a drug target
Depletion of DAPK1 results in inhibition of tumor cell count and volume growth in cellular and animal models of triple receptor-negative breast cancer, from individuals with p53-mutant cancers. This has not been demonstrated in actual patients.
References
Further reading
EC 2.7.11 |
https://en.wikipedia.org/wiki/S1PR1 | Sphingosine-1-phosphate receptor 1 (S1P receptor 1 or S1PR1), also known as endothelial differentiation gene 1 (EDG1) is a protein that in humans is encoded by the S1PR1 gene. S1PR1 is a G-protein-coupled receptor which binds the bioactive signaling molecule sphingosine 1-phosphate (S1P). S1PR1 belongs to a sphingosine-1-phosphate receptor subfamily comprising five members (S1PR1-5). S1PR1 was originally identified as an abundant transcript in endothelial cells and it has an important role in regulating endothelial cell cytoskeletal structure, migration, capillary-like network formation and vascular maturation. In addition, S1PR1 signaling is important in the regulation of lymphocyte maturation, migration and trafficking.
Structure
S1PR1 like the other members of the GPCR family is composed of seven-transmembrane helices arranged in a structurally conserved bundle. As well as the other GPCRs, in the extracellular region S1PR1 is composed of three loops: ECL1 between helices II and III, ECL2 between helices IV and V and ECL3 between helices VI and VII. Compared to the other members of the family, S1PR1 has some specific features. The N-terminal of the protein folds as a helical cap above the top of the receptor and therefore it limits the access of the ligands to the amphipathic binding pocket. This marked amphipathicity is indeed in agreement with the zwitterionic nature of S1P. In addition, helices ECL1 and ECL2 pack tightly against the N-terminal helix, further occludi |
https://en.wikipedia.org/wiki/YWHAG | 14-3-3 protein gamma is a protein that in humans is encoded by the YWHAG gene.
This gene product belongs to the 14-3-3 protein family which mediate signal transduction by binding to phosphoserine-containing proteins. This highly conserved protein family is found in both plants and mammals, and this protein is 100% identical to the rat ortholog. It is induced by growth factors in human vascular smooth muscle cells, and is also highly expressed in skeletal and heart muscles, suggesting an important role for this protein in muscle tissue. It has been shown to interact with RAF1 and protein kinase C, proteins involved in various signal transduction pathways.
Interactions
YWHAG has been shown to interact with C-Raf, EPB41L3, KIF1C and Stratifin.
References
Further reading
External links
14-3-3 proteins |
https://en.wikipedia.org/wiki/TRIM28 | Tripartite motif-containing 28 (TRIM28), also known as transcriptional intermediary factor 1β (TIF1β) and KAP1 (KRAB-associated protein-1), is a protein that in humans is encoded by the TRIM28 gene.
Function
The protein encoded by this gene mediates transcriptional control by interaction with the Krüppel-associated box repression domain found in many transcription factors. The protein localizes to the nucleus and is thought to associate with specific chromatin regions. The protein is a member of the tripartite motif family. This tripartite motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region.
KAP1 is a ubiquitously expressed protein involved in many critical functions including: transcriptional regulation, cellular differentiation and proliferation, DNA damage repair, viral suppression, and apoptosis. Its functionality is dependent upon post-translational modifications. Sumoylated TRIM28 can assemble epigenetic machinery for gene silencing, while phosphorylated TRIM28 is involved in DNA repair.
Cellular differentiation and proliferation
Studies have shown that deletion of KAP1 in mice before gastrulation results in death (implicating it as a necessary protein for proliferation) while deletion in adult mice results in increased anxiety and stress-induced alterations in learning and memory. KAP1 has been shown to participate in the maintenance of pluripotency of embryonic stem cells and to promote and inhibit cell |
https://en.wikipedia.org/wiki/SPRY2 | Sprouty homolog 2 (Drosophila), also known as SPRY2, is a protein which in humans is encoded by the SPRY2 gene.
Function
This gene encodes a protein belonging to the sprouty family. The encoded protein contains a carboxyl-terminal cysteine-rich domain essential for the inhibitory activity on receptor tyrosine kinase signaling proteins and is required for growth factor stimulated translocation of the protein to membrane ruffles. In primary dermal endothelial cells this gene is transiently upregulated in response to fibroblast growth factor two. This protein is indirectly involved in the non-cell autonomous inhibitory effect on fibroblast growth factor two signaling. The protein interacts with Cas-Br-M (murine) ectropic retroviral transforming sequence, and can function as a bimodal regulator of epidermal growth factor receptor/mitogen-activated protein kinase signaling. This protein may play a role in alveoli branching during lung development as shown by a similar mouse protein.
SPRY2 is a negative feedback regulator of multiple receptor tyrosine kinases (RTKs) including receptors for fibroblast growth factor (FGF), epidermal growth factor (EGF), and hepatocyte growth factor (HGF). Antagonization of growth factor mediated pathways, cell migration, and cellular differentiation occurs through the ERK pathway. Spry2 can also enhance EGFR signaling by sequestering CBL. Spry gene expression has been reported silenced or repressed in cancer of the breast, liver, lung, prostat |
https://en.wikipedia.org/wiki/PINK1 | PTEN-induced kinase 1 (PINK1) is a mitochondrial serine/threonine-protein kinase encoded by the PINK1 gene.
It is thought to protect cells from stress-induced mitochondrial dysfunction. PINK1 activity causes the parkin protein to bind to depolarized mitochondria to induce autophagy of those mitochondria. PINK1 is processed by healthy mitochondria and released to trigger neuron differentiation. Mutations in this gene cause one form of autosomal recessive early-onset Parkinson's disease.
Structure
PINK1 is synthesized as a 63000 Da protein which is often cleaved by PARL, between the 103-Alanine and the 104-Phenylalanine residues, into a 53000 Da fragment. PINK1 contains an N-terminal mitochondrial localization sequence, a putative transmembrane sequence, a Ser/Thr kinase domain, and a C-terminal regulatory sequence. The protein has been found to localize to the outer membrane of mitochondria, but can also be found throughout the cytosol. Experiments suggest the Ser/Thr kinase domain faces outward toward the cytosol, indicating a possible point of interaction with parkin.
The structure of PINK1 has been solved and shows how the protein binds and phosphorylates its substrate ubiquitin.
Function
PINK1 is intimately involved with mitochondrial quality control by identifying damaged mitochondria and targeting specific mitochondria for degradation. Healthy mitochondria maintain a membrane potential that can be used to import PINK1 into the inner membrane where it is cleaved by |
https://en.wikipedia.org/wiki/BUB1 | Mitotic checkpoint serine/threonine-protein kinase BUB1 also known as BUB1 (budding uninhibited by benzimidazoles 1) is an enzyme that in humans is encoded by the BUB1 gene.
Bub1 is a serine/threonine protein kinase first identified in genetic screens of Saccharomyces cerevisiae. The protein is bound to kinetochores and plays a key role in the establishment of the mitotic spindle checkpoint and chromosome congression. The mitotic checkpoint kinase is evolutionarily conserved in organisms as diverse as Saccharomyces cerevisiae and humans. Loss-of-function mutations or absence of Bub1 has been reported to result in aneuploidy, chromosomal instability (CIN) and premature senescence.
Structure
Bub1p comprises a conserved N-terminal region, a central non-conserved region and a C-terminal serine/threonine kinase domain. The N-terminal region mediates binding of Hs-BUB1 to the mitotic kinetochore protein blinkin (a protein also commonly referred to as AF15q14). The latter interaction is essential for kinetochore localization of Bub1 and its function in cell cycle arrest induced by spindle assembly checkpoint (SAC) activation. The crystal structure of human Bub1 revealed the presence of a N-terminal tetratricopeptide repeat (TPR) domain and a C-terminal kinase domain (residues 784–1085), adopting a canonical kinase fold with two lobes. The ATP binding and the catalytic sites are located at the interface of the two lobes. The N-terminal extension contains three β-strands and an |
https://en.wikipedia.org/wiki/FHL2 | Four and a half LIM domains protein 2 also known as FHL-2 is a protein that in humans is encoded by the FHL2 gene. LIM proteins contain a highly conserved double zinc finger motif called the LIM domain.
Function
FHL-2 is thought to have a role in the assembly of extracellular membranes and may function as a link between presenilin-2 and an intracellular signaling pathway.
Family
The Four-and-a-half LIM (FHL)-only protein subfamily is one of the members of the LIM-only protein family. Protein members within the group might be originated from a common ancestor and share a high degree of similarity in their amino acid sequence. These proteins are defined by the presence of the four and a half cysteine-rich LIM homeodomain with the half-domain always located in its N-terminus. The name LIM was derived from the first letter of the transcription factors LIN-11, ISL-1 and MEC-3, from which the domain was originally characterized. No direct interactions between LIM domain and DNA have been reported. Instead, extensive evidence points towards the functional role of FHL2 in supporting protein-protein interactions of LIM-containing proteins and its binding partners. Thus far, five members have been categorized into the FHL subfamily, which are FHL1, FHL2, FHL3, FHL4 and activator of CREM in testis (ACT) in human. FHL1, FHL2 and FHL3 are predominantly expressed in muscle, while FHL4 and FHL5 are expressed exclusively in testis.
Gene
FHL2 is the best studied member within the sub |
https://en.wikipedia.org/wiki/Interleukin-7%20receptor | The interleukin-7 receptor is a protein found on the surface of cells. It is made up of two different smaller protein chains - i.e. it is a heterodimer, and consists of two subunits, interleukin-7 receptor-α (CD127) and common-γ chain receptor (CD132). The common-γ chain receptors is shared with various cytokines, including interleukin-2, -4, -9, and -15. Interleukin-7 receptor is expressed on various cell types, including naive and memory T cells and many others.
Function
Interleukin-7 receptor has been shown to play a critical role in the development of immune cells called lymphocytes - specifically in a process known as V(D)J recombination. This protein is also found to control the accessibility of a region of the genome that contains the T-cell receptor gamma gene, by STAT5 and histone acetylation . Knockout studies in mice suggest that blocking apoptosis is an essential function of this protein during differentiation and activation of T lymphocytes. Functional defects in this protein may be associated with the pathogenesis of severe combined immunodeficiency (SCID).
Diseases
Several diseases are associated with Interleukin-7 receptor including T-cell acute lymphoblastic leukaemia, multiple sclerosis, rheumatoid arthritis and juvenile idiopathic arthritis.
See also
Cluster of differentiation
References
External links
Type I cytokine receptors |
https://en.wikipedia.org/wiki/ILF3 | Interleukin enhancer-binding factor 3 is a protein that in humans is encoded by the ILF3 gene.
Function
Nuclear factor of activated T-cells (NFAT) is a transcription factor required for T-cell expression of interleukin 2. NFAT binds to a sequence in the IL2 enhancer known as the antigen receptor response element 2. In addition, NFAT can bind RNA and is an essential component for encapsidation and protein priming of hepatitis B viral polymerase. NFAT is a heterodimer of 45 kDa and 90 kDa proteins, the larger of which is the product of this gene. The encoded protein, which is primarily localized to ribosomes, probably regulates transcription at the level of mRNA elongation. At least three transcript variants encoding three different isoforms have been found for this gene.
Interactions
ILF3 has been shown to interact with:
DNA-PKcs,
FUS,
PRMT1
Protein kinase R, and
XPO5.
C5orf36
Small NF90/ILF3-associated RNAs (snaR) (~120 nucleotides long) and are known to interact with ILF3 double-stranded RNA-binding motifs. snaR-A is abundant in human testis and has been shown to associate with ribosomes in HeLa cells. snaR-A is present in human and gorilla but not in chimpanzee. Other snaR RNAs are found in African Great Apes (including chimpanzee and bonobo).
ILF2 and ILF3 have been identified as autoantigens in mice with induced lupus, in canine systemic rheumatic autoimmune disease, and as a rare finding in humans with autoimmune disease.
References
Further reading
|
https://en.wikipedia.org/wiki/LIMK1 | LIM domain kinase 1 is an enzyme that in humans is encoded by the LIMK1 gene.
Function
There are approximately 40 known eukaryotic LIM proteins, so named for the LIM domains they contain. LIM domains are highly conserved cysteine-rich structures containing 2 zinc fingers. Although zinc fingers usually function by binding to DNA or RNA, the LIM motif probably mediates protein-protein interactions. LIM kinase-1 and LIM kinase-2 belong to a small subfamily with a unique combination of 2 N-terminal LIM motifs, a central PDZ domain, and a C-terminal protein kinase domain. LIMK1 is likely to be a component of an intracellular signaling pathway and may be involved in brain development.
Clinical significance
LIMK1 hemizygosity is implicated in the impaired visuospatial constructive cognition of Williams syndrome.
Interactions
LIMK1 has been shown to interact with:
CFL1,
CDKN1C,
NRG1,
PAK1,
PAK4, and
YWHAZ.
References
Further reading
External links
LIMK1 Info with links in the Cell Migration Gateway |
https://en.wikipedia.org/wiki/PSMA4 | Proteasome subunit alpha type-4 also known as macropain subunit C9, proteasome component C9, and 20S proteasome subunit alpha-3 is a protein that in humans is encoded by the PSMA4 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.
Structure
Protein expression
The PSMA4 gene encodes a member of the peptidase T1A family, that is a 20S core alpha subunit. The gene has 9 exons and locates at chromosome band 15q25.1. The human protein proteasome subunit alpha type-4 is 29.5 kDa in size and composed of 261 amino acids. The calculated theoretical pI of this protein is 6.97.
Complex assembly
The proteasome is a multicatalytic proteinase complex with a highly ordered 20S core structure. This barrel-shaped core structure is composed of 4 axially stacked rings of 28 non-identical subunits: the two end rings are each formed by 7 alpha subunits, and the two central rings are each formed by 7 beta subunits. Three beta subunits (beta1, beta2, and beta5) each contains a proteolytic active site and has distinct substrate preferences. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway.
Function
Crystal structures of isolated 20S proteasome complex demonstrate that the two rings of beta subuni |
https://en.wikipedia.org/wiki/PSMB1 | Proteasome subunit beta type-1 also known as 20S proteasome subunit beta-6 (based on systematic nomenclature) is a protein that in humans is encoded by the PSMB1 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-1, along with other beta subunits, assemble into two heptameric rings and subsequently a proteolytic chamber for substrate degradation. The eukaryotic proteasome recognized degradable proteins, including damaged proteins for protein quality control purpose or key regulatory protein components for dynamic biological processes. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides.
Structure
Gene
The gene PSMB1 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 tightly linked to the TBP (TATA-binding protein) gene in human and in mouse, and is transcribed in the opposite orientation in both species. The gene has 6 exons and locates at chromosome band 6q27.
Protein
The human protein proteasome subunit beta type-1 is 26.5 kDa in size and composed of 241 amino acids. The calculated theoretical pI of this protein is 8.27.
Complex assembly
The proteasome is a multicatalytic proteinase complex with a highly orde |
https://en.wikipedia.org/wiki/RAB6A | Ras-related protein Rab-6A is a protein that in humans is encoded by the RAB6A gene located in the eleventh chromosome. Its main function is the regulation of protein transport from the Golgi complex to the endoplasmic reticulum and the exocytosis along with the microtubules.
Interactions
RAB6A has been shown to interact with:
BICD1,
DCTN1
ERC1, and
KIF20A.
References
Further reading |
https://en.wikipedia.org/wiki/RGS2 | Regulator of G-protein signaling 2 is a protein that in humans is encoded by the RGS2 gene. It is part of a larger family of RGS proteins that control signalling through G-protein coupled receptors (GPCR).
Function
RGS2 is thought to have protective effects against myocardial hypertrophy as well as atrial arrhythmias. Increased stimulation of Gs coupled β1-adrenergic receptors and Gq coupled α1-adrenergic receptors in the heart can result in cardiac hypertrophy. In the case of Gq protein coupled receptor (GqPCR) mediated hypertrophy, Gαq will activate the intracellular affectors phospholipase Cβ and rho guanine nucleotide exchange factor to stimulate cell processes which lead to cardiomyocyte hypertrophy. RGS2 functions as a GTPase Activating Protein (GAP) which acts to increase the natural GTPase activity of the Gα subunit. By increasing the GTPase activity of the Gα subunit, RGS2 promotes GTP hydrolysis back to GDP, thus converting the Gα subunit back to its inactive state and reducing its signalling ability. Both GsPCR and GqPCR activation can contribute to cardiac hypertrophy via activation of MAP Kinases as well. RGS2 has been shown to decrease phosphorylation of those MAP kinases and therefore decrease their activation in response to Gαs signalling.
In the case of GsPCR mediated hypertrophy, the main mechanism by which signalling contributes to hypertrophy is through the Gβγ subunit; Gαs signalling by itself is not sufficient. Nevertheless, RGS2 has been shown to |
https://en.wikipedia.org/wiki/SUV39H1 | Histone-lysine N-methyltransferase SUV39H1 is an enzyme that in humans is encoded by the SUV39H1 gene.
Function
This gene is a member of the suppressor of variegation 3-9 homolog family and encodes a protein with a chromodomain and a C-terminal SET domain. This nuclear protein moves to the centromeres during mitosis and functions as a histone methyltransferase, methylating Lys-9 of histone H3. Overall, it plays a vital role in heterochromatin organization, chromosome segregation, and mitotic progression.
In mouse embryonic stem cells, Suv39h1 expression is repressed by OCT4 protein through the induction of an antisense long non-coding RNA.
Interactions
SUV39H1 has been shown to interact with:
CBX1,
CBX5,
DNMT3A,
HDAC1,
HDAC3,
HDAC9,
Histone deacetylase 2,
MBD1,
RUNX1,
Retinoblastoma protein, and
SBF1.
PIN1
References
Further reading |
https://en.wikipedia.org/wiki/CAMK2B | Calcium/calmodulin-dependent protein kinase type II beta chain is an enzyme that in humans is encoded by the CAMK2B gene.
Function
The enzyme belongs to the serine/threonine protein kinase family and to the Ca2+/calmodulin-dependent protein kinase subfamily. Calcium signalling is crucial for several aspects of plasticity at glutamatergic synapses. In mammalian cells, the enzyme is composed of four different chains: alpha, beta, gamma, and delta. The product of this gene is a beta chain. It is possible that distinct isoforms of this chain have different cellular localizations and interact differently with calmodulin. Eight transcript variants encoding eight distinct isoforms have been identified for this gene.
Interactions
CAMK2B has been shown to interact with Actinin alpha 4.
References
Further reading
External links
EC 2.7.11 |
https://en.wikipedia.org/wiki/CD3G | T-cell surface glycoprotein CD3 gamma chain is a protein that in humans is encoded by the CD3G gene.
T cell antigen receptor (TCR) is associated on the T cell surface with a complex of protein called CD3. CD3G (gamma chain) is one of the four peptides (gamma, delta, epsilon and zeta) that form CD3. Defects in CD3G are associated with T cell immunodeficiency.
See also
CD3 (immunology)
Cluster of differentiation
References
Further reading
External links
Clusters of differentiation |
https://en.wikipedia.org/wiki/CDC6 | Cell division control protein 6 homolog is a protein that in humans is encoded by the CDC6 gene.
The protein encoded by this gene is highly similar to Saccharomyces cerevisiae Cdc6, a protein essential for the initiation of DNA replication. This protein functions as a regulator at the early steps of DNA replication. It localizes in the cell nucleus during cell cycle phase G1, but translocates to the cytoplasm at the start of S phase. The subcellular translocation of this protein during the cell cycle is regulated through its phosphorylation by cyclin-dependent kinases. Transcription of this protein was reported to be regulated in response to mitogenic signals through a transcriptional control mechanism involving E2F proteins.
Interactions
CDC6 has been shown to interact with ORC1L, ORC2L, Cyclin A2, PPP2R3B, MCM3, PPP2R3A, MCM7 and PSKH1.
See also
Cdc6, the family of orthologs in eukaryotes
References
Further reading
External links |
https://en.wikipedia.org/wiki/DAB2 | Disabled homolog 2 is a protein that in humans is encoded by the DAB2 gene.
Function
DAB2 mRNA is expressed in normal ovarian epithelial cells but is down-regulated or absent from ovarian carcinoma cell lines. The 770-amino acid predicted protein has an overall 83% identity with the mouse p96 protein, a putative mitogen-responsive phosphoprotein; homology is strongest in the amino-terminal end of the protein in a region corresponding to the phosphotyrosine interaction domain. The down-regulation of DAB2 may play an important role in ovarian carcinogenesis. This gene was initially named DOC2 (for Differentially expressed in Ovarian Cancer) and is distinct from the DOC2A and DOC2B genes (for double C2-like domains, alpha and beta).
Interactions
DAB2 has been shown to interact with:
C-src tyrosine kinase,
Cdk1,
DAB2IP,
DVL2,
DVL3,
LRP2,
MYO6,
Mothers against decapentaplegic homolog 2,
Mothers against decapentaplegic homolog 3
PIN1, and
Src.
References
Further reading |
https://en.wikipedia.org/wiki/FCER1A | Fc fragment of IgE, high affinity I, receptor for; alpha polypeptide, also known as FCER1A, is a protein which in humans is encoded by the FCER1A gene.
Function
The high affinity IgE receptor plays a central role in allergic disease, coupling allergen and mast cell to initiate the inflammatory and immediate hypersensitivity responses that are characteristic of disorders such as hay fever and asthma. The allergic response occurs when 2 or more IgE receptors are crosslinked via IgE molecules that in turn are bound to an allergen (antigen) molecule. A perturbation occurs that brings about the release of histamine and proteases from the granules in the cytoplasm of the mast cell and leads to the synthesis of prostaglandins and leukotrienes—potent effectors of the hypersensitivity response. The IgE receptor consists of 3 subunits: alpha (this protein), beta, and gamma; only the alpha subunit is glycosylated.
References
Further reading
Fc receptors |
https://en.wikipedia.org/wiki/Gamma-aminobutyric%20acid%20receptor%20subunit%20gamma-2 | Gamma-aminobutyric acid receptor subunit gamma-2 is a protein that in humans is encoded by the GABRG2 gene.
Function
Gamma-aminobutyric acid (GABA), the major inhibitory neurotransmitter in the brain, mediates neuronal inhibition by binding to GABA receptors. The type A GABA receptors are pentameric chloride channels assembled from among many genetic variants of GABA(A) subunits. This gene encodes the gamma 2 subunit of GABA(A) receptor. Mutations in this gene have been associated with epilepsy and febrile seizures. Alternative splicing of this gene results in transcript variants encoding different isoforms.
Interactions
GABRG2 has been shown to interact with GABARAP and Dopamine receptor D5.
See also
GABAA receptor
References
Further reading
Ion channels |
https://en.wikipedia.org/wiki/GATA2 | GATA2 or GATA-binding factor 2 is a transcription factor, i.e. a nuclear protein which regulates the expression of genes. It regulates many genes that are critical for the embryonic development, self-renewal, maintenance, and functionality of blood-forming, lympathic system-forming, and other tissue-forming stem cells. GATA2 is encoded by the GATA2 gene, a gene which often suffers germline and somatic mutations which lead to a wide range of familial and sporadic diseases, respectively. The gene and its product are targets for the treatment of these diseases.
Inactivating mutations of the GATA2 gene cause a reduction in the cellular levels of GATA2 and the development of a wide range of familial hematological, immunological, lymphatic, and/or other disorders that are grouped together into a common disease termed GATA2 deficiency. Less commonly, these disorders are associated with non-familial (i.e. sporadic or acquired) GATA inactivating mutations. GATA2 deficiency often begins with seemingly benign abnormalities but if untreated progresses to life-threatening opportunistic infections, virus-induced cancers, lung failure, the myelodysplastic syndrome (i.e. MDS), and/or acute myeloid leukemia, principally acute myeloid leukemia (AML), less commonly chronic myelomonocytic leukemia (CMML), and rarely a lymphoid leukemia.
Overexpression of the GATA2 transcription factor that is not due to mutations in the GATA2 gene appears to be a secondary factor that promotes the aggressiven |
https://en.wikipedia.org/wiki/XBP1 | X-box binding protein 1, also known as XBP1, is a protein which in humans is encoded by the XBP1 gene. The XBP1 gene is located on chromosome 22 while a closely related pseudogene has been identified and localized to chromosome 5. The XBP1 protein is a transcription factor that regulates the expression of genes important to the proper functioning of the immune system and in the cellular stress response.
Discovery
The X-box binding protein 1 (XBP1) is a transcription factor containing a bZIP domain. It was first identified by its ability to bind to the Xbox, a conserved transcriptional element in the promoter of the human leukocyte antigen (HLA) DR alpha.
Function
MHC class II gene regulation
The expression of this protein is required for the transcription of a subset of class II major histocompatibility genes. Furthermore, XBP1 heterodimerizes with other bZIP transcription factors such as c-fos.
XBP1 expression is controlled by the cytokine IL-4 and the antibody IGHM. XBP1 in turn controls the expression of IL-6 which promotes plasma cell growth and of immunoglobulins in B lymphocytes.
Plasma cell differentiation
XBP1 is also essential for differentiation of plasma cells (a type of antibody secreting immune cell). This differentiation requires not only the expression of XBP1 but the expression of the spliced isoform of XBP1s. XBP1 regulates plasma cell differentiation independent of its known functions in the endoplasmic reticulum stress response (see below). |
https://en.wikipedia.org/wiki/SNAP23 | Synaptosomal-associated protein 23 is a protein that in humans is encoded by the SNAP23 gene. Two alternative transcript variants encoding different protein isoforms have been described for this gene.
Function
Specificity of vesicular transport is regulated, in part, by the interaction of a vesicle-associated membrane protein termed synaptobrevin/VAMP with a target compartment membrane protein termed syntaxin. These proteins, together with SNAP25 (synaptosome-associated protein of 25 kDa), form a complex which serves as a binding site for the general membrane fusion machinery. Synaptobrevin/VAMP and syntaxin are believed to be involved in vesicular transport in most, if not all cells, while SNAP25 is present almost exclusively in the brain, suggesting that a ubiquitously expressed homolog of SNAP25 exists to facilitate transport vesicle/target membrane fusion in other tissues.
SNAP23 is structurally and functionally similar to SNAP25 and binds tightly to multiple syntaxins and synaptobrevins/VAMPs. It is an essential component of the high affinity receptor for the general membrane fusion machinery and is an important regulator of transport vesicle docking and fusion.
Clinical significance
In individuals with insulin resistance, SNAP23 is found to be translocated from the plasma membrane to the cytosol where it becomes associated with lipid droplets and is therefore unable to translocate GLUT-4 to the membrane, hindering glucose transport.
Interactions
SNAP23 has bee |
https://en.wikipedia.org/wiki/Cyclin%20A1 | Cyclin-A1 is a protein that in humans is encoded by the CCNA1 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 division cycle. Cyclins function as activating subunits of enzymatic complex together with cyclin-dependent kinases (CDKs). Different cyclins exhibit distinct expression and degradation patterns that contribute to the temporal coordination of cell cycle events. Cyclin A1 was shown to be expressed in testis and brain, as well as in several leukemic cell lines, and is thought to primarily function in the control of meiosis. This cyclin binds both Cdk1 and Cdk2 kinases, which give two distinct kinase activities, one appearing in S phase, the other in G2, and thus regulate separate functions in cell cycle. This cyclin was found to bind to important cell cycle regulators, such as Rb family proteins, transcription factor E2F1, and the Kip/Cip family of CDK-inhibitor proteins.
Interactions
Cyclin-A1 interacts with:
CDC20,
Cyclin-dependent kinase 2,
E2F1,
GNB2L1,
GPS2,
MYBL2, and
Retinoblastoma protein.
References
Further reading
Cell cycle regulators |
https://en.wikipedia.org/wiki/EBAG9 | Receptor-binding cancer antigen expressed on SiSo cells is a protein that in humans is encoded by the EBAG9 gene.
This gene was identified as an estrogen-responsive gene. Regulation of transcription by estrogen is mediated by estrogen receptor which binds to the estrogen-responsive element (ERE) found in the 5'-flanking region of this gene. The encoded protein is a tumor-associated antigen that is expressed at high frequency in a variety of cancers. Two transcript variants differing in the 5' UTR, but encoding the same protein, have been identified for this gene.
References
Further reading |
https://en.wikipedia.org/wiki/MAPK8IP1 | C-jun-amino-terminal kinase-interacting protein 1 is an enzyme that in humans is encoded by the MAPK8IP1 gene.
The protein encoded by this gene is a regulator of the pancreatic beta-cell function. It is highly similar to JIP-1, a mouse protein known to be a regulator of c-Jun amino-terminal kinase (Mapk8). This protein has been shown to prevent MAPK8 mediated activation of transcription factors, and decrease IL-1 beta and MAP kinase kinase 1 (MEKK1) induced apoptosis in pancreatic beta cells. This protein also functions as a DNA-binding transactivator of the glucose transporter GLUT2. RE1-silencing transcription factor (REST) is reported to repress the expression of this gene in insulin-secreting beta cells. This gene is found to be mutated in a type 2 diabetes family, and thus is thought to be a susceptibility gene for type 2 diabetes.
Interactions
MAPK8IP1 has been shown to interact with MAP3K10, DUSP16, Mitogen-activated protein kinase 9, MAPK8, LRP2, LRP1, MAP3K12, MAP2K7, MAPK8IP2 and MAP3K11.
References
Further reading |
https://en.wikipedia.org/wiki/ADAMTS4 | A disintegrin and metalloproteinase with thrombospondin motifs 4 is an enzyme that in humans is encoded by the ADAMTS4 gene.
This gene encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family. Members of the family share several distinct protein modules, including a propeptide region, a metalloproteinase domain, a disintegrin-like domain, and a thrombospondin type 1 (TS) motif. Individual members of this family differ in the number of C-terminal TS motifs, and some have unique C-terminal domains. The enzyme encoded by this gene lacks a C-terminal TS motif. It can degrade aggrecan, a major proteoglycan of cartilage, brevican, a brain-specific extracellular matrix protein, neurocan and versican. The cleavage of aggrecan and brevican suggests key roles of this enzyme in arthritic disease and in the central nervous system, potentially, in the progression of glioma.
Structure
ADAMTS4 is the shortest known ADAMTS, lacking the C-terminal domain and is the only non-glycosylated ADAMTS. It also only has one thrombospondin type 1 motif (TSR), whereas all the other ADAMTS have two or more TSRs. The TSR is important for binding of the enzyme to the extracellular matrix and hence its substrate specificity. Adjacent to the C-terminal TSR is a disintegrin-like domain, a cysteine-rich region
that stacks against the active-site of the enzyme when in its final folded tertiary structure.
Function
ADAMTS4 is capable of cleaving all the |
https://en.wikipedia.org/wiki/ISG15 | Interferon-stimulated gene 15 (ISG15) is a 17 kDA secreted protein that in humans is encoded by the ISG15 gene. ISG15 is induced by type I interferon (IFN) and serves many functions, acting both as an extracellular cytokine and an intracellular protein modifier. The precise functions are diverse and vary among species but include potentiation of Interferon gamma (IFN-II) production in lymphocytes, ubiquitin-like conjugation to newly-synthesized proteins and negative regulation of the IFN-I response.
Structure
The ISG15 gene consists of two exons and encodes for a 17 kDa polypeptide. The immature polypeptide is cleaved at its carboxy terminus, generating a mature 15 kDa product that terminates with a LRLRGG motif, as found in ubiquitin. The tertiary structure of ISG15 also resembles ubiquitin, despite only ~30% sequence identity. Specifically, this structure consists of two ubiquitin-like domains connected by a polypeptide ‘hinge.’ Of note, ISG15 shows substantial sequence variation among species, with homology as low as 30% between orthologs.
Function
After induction by type I interferon, ISG15 can be found in three forms, each with unique functions:
Extracellular cytokine
ISG15 is secreted from the cell and can be detected in supernatant or blood plasma. ISG15 binds the LFA-1 integrin receptor on NK- and T-cells to potentiate their production of IFN-II, which is essential for mycobacterial immunity.
Intracellular conjugate: ISGylation
In a ubiquitin-like fashion, ISG15 |
https://en.wikipedia.org/wiki/CDC37 | Hsp90 co-chaperone Cdc37 is a protein that in humans is encoded by the CDC37 gene. This protein is highly similar to Cdc 37, a cell division cycle control protein of Saccharomyces cerevisiae. This protein is a HSP90 Co-chaperone with specific function in cell signal transduction. It has been shown to form complex with Hsp90 and a variety of protein kinases including CDK4, CDK6, SRC, RAF1, MOK, as well as eIF-2 alpha kinases. It is thought to play a critical role in directing Hsp90 to its target kinases.
Interactions
CDC37 has been shown to interact with:
CDK4,
HSP90AA1
IKBKG,
IKK2, and
STK11.
Domain architecture
CDC37 consists of three structural domains. The N-terminal domain binds to protein kinases. The central domain is the Hsp90 chaperone (heat shock protein 90) binding domain. The function of the C-terminal domain is unclear.
References
Further reading
External links
Co-chaperones |
https://en.wikipedia.org/wiki/ATF1 | Cyclic AMP-dependent transcription factor ATF-1 is a protein that in humans is encoded by the ATF1 gene.
This gene encodes an activating transcription factor, which belongs to the ATF subfamily and bZIP (basic-region leucine zipper) family. It influences cellular physiologic processes by regulating the expression of downstream target genes, which are related to growth, survival, and other cellular activities. This protein is phosphorylated at serine 63 in its kinase-inducible domain by serine/threonine kinases, cAMP-dependent protein kinase A, calmodulin-dependent protein kinase I/II, mitogen- and stress-activated protein kinase and cyclin-dependent kinase 3 (cdk-3). Its phosphorylation enhances its transactivation and transcriptional activities, and enhances cell transformation.
Clinical significance
Fusion of this gene and FUS on chromosome 16 or EWSR1 on chromosome 22 induced by translocation generates chimeric proteins in angiomatoid fibrous histiocytoma and clear cell sarcoma. This gene has a pseudogene on chromosome 6.
See also
Activating transcription factor
Interactions
ATF1 has been shown to interact with:
BRCA1,
CSNK2A2,
CSNK2A1, and
EWS.
References
Further reading
External links
Transcription factors
Oncogenes |
https://en.wikipedia.org/wiki/HNRPU | Heterogeneous nuclear ribonucleoprotein U is a protein that in humans is encoded by the HNRNPU gene.
Function
This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins that form complexes with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene contains a RNA binding domain and scaffold-associated region (SAR)-specific bipartite DNA-binding domain. This protein is also thought to be involved in the packaging of hnRNA into large ribonucleoprotein complexes. During apoptosis, this protein is cleaved in a caspase-dependent way. Cleavage occurs at the SALD site, resulting in a loss of DNA-binding activity and a concomitant detachment of this protein from nuclear structural sites. But this cleavage does not affect the function of the encoded protein in RNA metabolism. At least two alternatively spliced transcript variants have been identified for this gene.
Interactions
HNRPU has been shown to interact with:
EP300,
GTF2F1,
Glucocorticoid receptor, and
NDN.
References
Further reading
Ribonucleoprot |
https://en.wikipedia.org/wiki/PBX1 | Pre-B-cell leukemia transcription factor 1 is a protein that in humans is encoded by the PBX1 gene. The homologous protein in Drosophila is known as extradenticle, and causes changes in embryonic development.
Function
Mice studies suggest PBX1 is involved in bone generation and skeletal patterning.
Interactions
PBX1 has been shown to interact with:
HOXB1,
HOXB7,
MEIS1, and
Prep1.
Fruit fly homolog
The Drosophila melangoster gene called extradenticle encodes a homeodomain protein that is 71% similar to the Pbx1 protein, and is considered homologous to PBX1. extradenticle is a homeodomain transcription factor expressed during embryogenesis and is related to morphological changes and development.
Reduced levels of extradenticle cause segmental transformations, without affecting the functionality or location of homeotic genes. Complete removal of extradenticle both maternally and zygotically leads to alterations from failure of non-extradenticle protein expression.
A monoclonal antibody study of the expression of extradenticle protein in embryonic development found that it is uniformly distributed, as well as excluded from cell nuclei, until gastrulation. During the germ band retraction stage of development, extradenticle protein begins to accumulate in the nuclei of cells in a specific pattern. Proximal areas of wing and leg imaginal discs have extradenticle present in the nucleus, while distal areas only have it in the cytoplasm.
References
Further reading
Ext |
https://en.wikipedia.org/wiki/Profilin%201 | Profilin-1 is a protein that in humans is encoded by the PFN1 gene.
Function
The protein encoded by this gene is a ubiquitous actin monomer-binding protein belonging to the profilin family. It is thought to regulate actin polymerization in response to extracellular signals. Deletion of this gene is associated with Miller-Dieker syndrome. Mutations in this gene may be a rare cause of amyotrophic lateral sclerosis, also called Lou Gehrig's disease.
Interactions
Profilin 1 has been shown to interact with:
FMNL1,
MLLT4
Vasodilator-stimulated phosphoprotein,
WASF1, and
WASL.
References
Further reading |
https://en.wikipedia.org/wiki/PSMB4 | Proteasome subunit beta type-4 also known as 20S proteasome subunit beta-7 (based on systematic nomenclature) is a protein that in humans is encoded by the PSMB4 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-2, along with other beta subunits, assemble into two heptameric rings and subsequently a proteolytic chamber for substrate degradation. The eukaryotic proteasome recognized degradable proteins, including damaged proteins for protein quality control purpose or key regulatory protein components for dynamic biological processes. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides.
Structure
Gene
This gene PSMB4 encodes a member of the proteasome B-type family, also known as the T1B family, that is a 20S core beta subunit. The gene has 7 exons and locates at chromosome band 1q21.
Protein
The human protein proteasome subunit beta type-2 is 23 kDa in size and composed of 219 amino acids. The calculated theoretical pI of this protein is 5.47.
Complex assembly
The proteasome is a multicatalytic proteinase complex with a highly ordered 20S core structure. This barrel-shaped core structure is composed of 4 axially stacked rings of 28 non-identical subunits: the two end rings are each |
https://en.wikipedia.org/wiki/PSMD10 | 26S proteasome non-ATPase regulatory subunit 10 or gankyrin is an enzyme that in humans is encoded by the PSMD10 gene. First isolated in 1998 by Tanaka et al.; Gankyrin is an oncoprotein that is a component of the 19S regulatory cap of the proteasome. Structurally, it contains a 33-amino acid ankyrin repeat that forms a series of alpha helices. It plays a key role in regulating the cell cycle via protein-protein interactions with the cyclin-dependent kinase CDK4. It also binds closely to the E3 ubiquitin ligase MDM2, which is a regulator of the degradation of p53 and retinoblastoma protein, both transcription factors involved in tumor suppression and found mutated in many cancers. Gankyrin also has an anti-apoptotic effect and is overexpressed in certain types of tumor cells such as hepatocellular carcinoma.
Function
The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasom |
https://en.wikipedia.org/wiki/S100A7 | S100 calcium-binding protein A7 (S100A7), also known as psoriasin, is a protein that in humans is encoded by the S100A7 gene.
Function
S100A7 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 differs from the other S100 proteins of known structure in its lack of calcium binding ability in one EF-hand at the N-terminus. The protein functions as a prominent antimicrobial peptide mainly against E. coli.
S100A7 also displays antimicrobial properties. It is secreted by epithelial cells of the skin and is a key antimicrobial protein against Escherichia coli by disrupting their cell membranes. This is the reason that in countries with poor sanitation, human skin is exposed to E. coli strains from faecal matter but it does not usually result in an infection.
S100A7 is highly homologous to S100A7A (koebnerisin) but distinct in expression, tissue distribution and function.
Clinical significance
This protein is markedly over-expressed in the skin lesions of psoriatic patients, but is excluded as a candidate gene for familial psoriasis susceptibility. The expression of psoriasin is induced in skin wounds through activation of the epidermal g |
https://en.wikipedia.org/wiki/COPB1 | Coatomer subunit beta is a protein that in humans is encoded by the COPB1 gene.
See also
COPI coatomer, a protein complex
References
Further reading
External links
PDBe-KB provides an overview of all the structure information available in the PDB for Mouse Coatomer subunit beta |
https://en.wikipedia.org/wiki/ETS2 | Protein C-ETS2 is a protein that in humans is encoded by the ETS2 gene. The protein encoded by this gene belongs to the ETS family of transcription factors.
Interactions
ETS2 has been shown to interact with:
C-jun,
Cyclin-dependent kinase 10,
ERG,
myb, and
ZMYND11.
References
Further reading
External links
Drosophila pointed - The Interactive Fly
Transcription factors |
https://en.wikipedia.org/wiki/GDI1 | Rab GDP dissociation inhibitor alpha is a protein that in humans is encoded by the GDI1 gene.
Function
GDP dissociation inhibitors are proteins that regulate the GDP-GTP exchange reaction of members of the rab family, small GTP-binding proteins of the ras superfamily, that are involved in vesicular trafficking of molecules between cellular organelles. GDIs slow the rate of dissociation of GDP from rab proteins and release GDP from membrane-bound rabs. GDI1 is expressed primarily in neural and sensory tissues. Mutations in GDI1 have been linked to X-linked nonspecific mental retardation.
Rab GTPases cycles between the cytosolic compartment, where it is bound to a protein called GDI (GDP Dissociation Inhibitor), and the membrane, where it interacts with a receptor, a nucleotide exchange factor, a GAP (GTPase Activating Protein) and probably other factors that link it to the appropriate SNARE. GDI is non-specific with respect to the rab it binds. However, the exchanger, receptor and GAP, are rab specific.
Interactions
GDI1 has been shown to interact with CDC42.
References
Further reading |
https://en.wikipedia.org/wiki/TPSAB1 | Tryptase alpha-1 and tryptase beta-1 are enzymes that in humans are encoded by the same TPSAB1 gene. Beta tryptases appear to be the main isoenzymes expressed in mast cells; whereas in basophils, alpha tryptases predominate.
Function
Tryptases comprise a family of trypsin-like serine proteases, the peptidase family S1. Tryptases are enzymatically active only as heparin-stabilized tetramers, and they are resistant to all known endogenous proteinase inhibitors. Several tryptase genes are clustered on chromosome 16p13.3. These genes are characterized by several distinct features. They have a highly conserved 3' UTR and contain tandem repeat sequences at the 5' flank and 3' UTR which are thought to play a role in regulation of the mRNA stability. These genes have an intron immediately upstream of the initiator Met codon, which separates the site of transcription initiation from protein coding sequence. This feature is characteristic of tryptases but is unusual in other genes. The alleles of this gene exhibit an unusual amount of sequence variation, such that the alleles were once thought to represent two separate genes, alpha and beta 1.Tryptases have been implicated as mediators in the pathogenesis of asthma and other allergic and inflammatory disorders.
References
Further reading
EC 3.4.21 |
https://en.wikipedia.org/wiki/CASK | Peripheral plasma membrane protein CASK is a protein that in humans is encoded by the CASK gene. This gene is also known by several other names: CMG 2 (CAMGUK protein 2), calcium/calmodulin-dependent serine protein kinase 3 and membrane-associated guanylate kinase 2. CASK gene mutations are the cause of XL-ID with or without nystagmus and MICPCH, an X-linked neurological disorder.
Gene
This gene is located on the short arm of the X chromosome (Xp11.4). It is 404,253 bases in length and lies on the Crick (minus) strand. The encoded protein has 926 amino acids with a predicted molecular weight of 105,123 Daltons.
Function
This protein is a multidomain scaffolding protein with a role in synaptic transmembrane protein anchoring and ion channel trafficking. It interacts with the transcription factor TBR1 and binds to several cell-surface proteins including neurexins and syndecans.
Clinical importance
This gene has been implicated in X-linked mental retardation, including specifically mental retardation and microcephaly with pontine and cerebellar hypoplasia. The role of CASK in disease is primarily associated with a loss of function (under expression) of the CASK gene as a result of a deletion, missense or splice mutation. It appears that mutations in the gene lead to diminished amounts of the protein being coded. As a result, CASK is unable to form complexes with other proteins leading to a cascade of events. Research has shown there is significant down-regulation of the |
https://en.wikipedia.org/wiki/CLDN1 | Claudin-1 is a protein that in humans is encoded by the CLDN1 gene. It belongs to the group of claudins.
Function
Tight junctions represent one mode of cell-to-cell adhesion in epithelial or endothelial cell sheets, forming continuous seals around cells and serving as a physical barrier to prevent solutes and water from passing freely through the paracellular space. These junctions are composed of sets of continuous networking strands in the outwardly facing cytoplasmic leaflet, with complementary grooves in the inwardly facing extracytoplasmic leaflet. The protein encoded by this gene, a member of the claudin family, is an integral membrane protein and a component of tight junction strands. Loss of function mutations result in neonatal ichthyosis-sclerosing cholangitis syndrome.
Interactions
CLDN1 has been shown to interact with CLDN5 and CLDN3.
References
External links
Further reading |
https://en.wikipedia.org/wiki/NEDD4L | Neural precursor cell expressed developmentally downregulated gene 4-like (NEDD4L) or NEDD4-2 is an enzyme (ubiquitin ligase) of the NEDD4 family.
In human the protein is encoded by the NEDD4L gene. In mouse the protein is commonly known as NEDD4-2 and the gene Nedd4-2.
NEDD4-2 has been shown to ubiquitinate and therefore down regulate the epithelial sodium channel (ENaC) in the collecting ducts of the kidneys, therefore opposing the actions of aldosterone and increasing salt excretion. In Liddle's Syndrome NEDD4 is unable to bind to the ENaC and lead to salt retention and hypertension occur.
NEDD4L belongs to the NEDD4 family of E3 HECT domain ubiquitin ligases. It is the closest homologue of NEDD4, the prototypic member of the family and probably arose as a result of gene duplication. While NEDD4 orthologues are present in all eukaryotes, NEDD4L proteins are limited to vertebrates. NEDD4L proteins are known to be involved in regulating many membrane proteins via ubiquitination and endocytosis.
NEDD4L protein is expressed widely. The primary targets of NEDD4-2 include the epithelial sodium channel (ENaC), the Na+-Cl- co-transporter (NCC), and the voltage gated sodium channels (Navs), although additional targets are predicted from in vitro studies. NEDD4-2 gene in mice is essential for animal survival and the polymorphisms in NEDD4L are associated with human hypertension.
Protein architecture
The NEDD4-2 protein consists of an amino-terminal Ca2+-phospholipid binding d |
https://en.wikipedia.org/wiki/PD-L1 | Programmed death-ligand 1 (PD-L1) also known as cluster of differentiation 274 (CD274) or B7 homolog 1 (B7-H1) is a protein that in humans is encoded by the CD274 gene.
Programmed death-ligand 1 (PD-L1) is a 40kDa type 1 transmembrane protein that has been speculated to play a major role in suppressing the adaptive arm of immune systems during particular events such as pregnancy, tissue allografts, autoimmune disease and other disease states such as hepatitis. Normally the adaptive immune system reacts to antigens that are associated with immune system activation by exogenous or endogenous danger signals. In turn, clonal expansion of antigen-specific CD8+ T cells and/or CD4+ helper cells is propagated. The binding of PD-L1 to the inhibitory checkpoint molecule PD-1 transmits an inhibitory signal based on interaction with phosphatases (SHP-1 or SHP-2) via Immunoreceptor Tyrosine-Based Switch Motif (ITSM). This reduces the proliferation of antigen-specific T-cells in lymph nodes, while simultaneously reducing apoptosis in regulatory T cells (anti-inflammatory, suppressive T cells) – further mediated by a lower regulation of the gene Bcl-2.
History
PD-L1 also known as B7-H1 was characterized at the Mayo Clinic in 1999 as an immune regulatory molecule. At that time, it was concluded that B7-H1 helps tumor cells evade anti-tumor immunity. In 2003, B7-H1 was shown to be expressed on myeloid cells as checkpoint protein and was proposed as potential target in cancer immunotherapy |
https://en.wikipedia.org/wiki/Stand-In | Stand-In is a 1937 American screwball comedy directed by Tay Garnett and starring Leslie Howard, Joan Blondell and Humphrey Bogart. The film's screenplay was written by Gene Towne and C. Graham Baker from a story by Clarence Budington Kelland. It was produced by independent producer Walter Wanger, and released by United Artists. The film is set in Hollywood and satirizes the film industry during the classical Hollywood era.
Plot
During the Great Depression, Fowler Pettypacker, a Wall Street banker, is debating whether or not to accept an offer from Ivor Nassau to buy "Colossal Pictures," a fictional film studio on Poverty Row. The studio has not been turning a profit, but financial analyst Atterbury Dodd advises against selling. He stakes his reputation on his mathematical calculations that show Colossal should turn a profit. The bank sends Dodd to Hollywood as the new head of the studio.
Colossal's star actress, Thelma Cheri, eccentric foreign director Koslofski, and press agent Tom Potts are conspiring with Nassau to sabotage the studio. They are deliberately running up costs on producer Douglas Quintain's jungle feature, Sex and Satan so that the film flops and the studio goes bankrupt.
In Hollywood, Dodd meets Lester Plum, a cheerful former child star currently working as a stand-in for Cheri. Lester teaches Dodd about the business of filmmaking and eventually becomes his secretary. Under Lester's tutelage, Dodd comes to see that the workers are more than just numbers |
https://en.wikipedia.org/wiki/Capsomere | The capsomere is a subunit of the capsid, an outer covering of protein that protects the genetic material of a virus. Capsomeres self-assemble to form the capsid.
Subunits called protomers aggregate to form capsomeres. Various arrangements of capsomeres are: 1) Icosahedral, 2) Helical, and 3) Complex.
1) Icosahedral- An icosahedron is a polyhedron with 12 vertices and 20 faces. Two types of capsomeres constitute the icosahedral capsid: pentagonal (pentons) at the vertices and hexagonal (hexons) at the faces. There are always twelve pentons, but the number of hexons varies among virus groups. In electron micrographs, capsomeres are recognized as regularly spaced rings with a central hole.
2) Helical- The protomers are not grouped in capsomeres, but are bound to each other so as to form a ribbon-like structure. This structure folds into a helix because the protomers are thicker at one end than at the other. The diameter of the helical capsid is determined by characteristics of its protomers, while its length is determined by the length of the nucleic acid it encloses.
3) Complex- e.g., that exhibited by poxvirus and rhabdovirus. This group comprises all those viruses which do not fit into either of the above two groups.
When the viral particle has entered a host cell, the host cellular enzymes digest the capsid and its constituent capsomeres, thereby exposing the naked genetic material (DNA/RNA) of the virus, which subsequently enters the replication cycle.
The capsomere |
https://en.wikipedia.org/wiki/Ch%C3%A2teau%20Filhot | Château Filhot, archaically named Maison Noble de Verdoulet, is a winery rated Deuxième cru classé (French, “Second Growth”) in the Bordeaux Wine Official Classification of 1855, from the Sauternes appellation in Gironde. Considered by some unjustly omitted from the Premier cru classification, Filhot produces a drier wine than Château d'Yquem, with an unusually high alcohol content for a Sauternes.
History
The vineyard dating from the 1630s, the château was founded by Romain de Filhot in 1709. Following the French revolution, the estate was taken over by
Romain-Bertrand de Lur-Saluces who added the estate of Pinaud du Rey and had the château redesigned to its English appearance in 1840. During the period when then American ambassador to France Thomas Jefferson ranked the wine directly behind Yquem, Filhot enjoyed a greater reputation than today, and the two wines were comparably priced.
In 1935, Comtesse Durieu de Lacarelle (the sister of the Marquis de Lur-Saluces, proprietor of Château d'Yquem) bought the estate, which was subsequently modernised by her son, Louis Durieu de Lacarelle, during the 1970s. The estate is currently run by the Vaucelles family.
Production
The vineyard area extends from a 350 hectares estate with the grape varieties of 60% Sémillon, 36% Sauvignon blanc and 4% Muscadelle. Their annual production is an average of 6500 cases. The second wine is called Chateau Pineau du Rey.
References
External links
Château Filhot official site
Bordeaux wi |
https://en.wikipedia.org/wiki/STK6 | STK6 may refer to:
Aurora A kinase, an enzyme
Myosin-heavy-chain kinase, an enzyme |
https://en.wikipedia.org/wiki/Malgrange%E2%80%93Ehrenpreis%20theorem | In mathematics, the Malgrange–Ehrenpreis theorem states that every non-zero linear differential operator with constant coefficients has a Green's function. It was first proved independently by and
.
This means that the differential equation
where P is a polynomial in several variables and δ is the Dirac delta function, has a distributional solution u. It can be used to show that
has a solution for any compactly supported distribution f. The solution is not unique in general.
The analogue for differential operators whose coefficients are polynomials (rather than constants) is false: see Lewy's example.
Proofs
The original proofs of Malgrange and Ehrenpreis were non-constructive as they used the Hahn–Banach theorem. Since then several constructive proofs have been found.
There is a very short proof using the Fourier transform and the Bernstein–Sato polynomial, as follows. By taking Fourier transforms the Malgrange–Ehrenpreis theorem is equivalent to the fact that every non-zero polynomial P has a distributional inverse. By replacing P by the product with its complex conjugate, one can also assume that P is non-negative. For non-negative polynomials P the existence of a distributional inverse follows from the existence of the Bernstein–Sato polynomial, which implies that Ps can be analytically continued as a meromorphic distribution-valued function of the complex variable s; the constant term of the Laurent expansion of Ps at s = −1 is then a distributional inverse of P. |
https://en.wikipedia.org/wiki/SubAntarctic%20Foundation%20for%20Ecosystems%20Research | The SubAntarctic Foundation for Ecosystems Research (aka SAFER), founded in 1996 by New Zealand-based zoologist Dr. Peter Carey, is working on several habitat restoration projects on four small islands that SAFER owns in the western Falkland Islands. The islands (Bense, Little Bense, Cliff, and Bradley Islet) are in various states of modification from such human activities as grazing, widespread fire, and introduced species.
SAFER is conducting fauna and flora inventories, studying the ecology of introduced rodents (Norway rat and house mouse) and examining the behaviour and ecology of various resident bird species. In addition, the soil erosion and deposition that resulted from a fire in 1985 is being monitored, with a view to replanting in the future. Eradication of invasive species is also a key part of SAFER's plans to restore the islands to prime wildlife habitat.
These projects are coordinated by SAFER's Director, Peter Carey. SAFER is registered in the United States as a non-profit 501(c)(3) organisation.
References
External links
SAFER homepage
Organizations established in 1996
Ecology organizations
Environment of the Falkland Islands
Foundations based in New Zealand
Subantarctic
Conservation and environmental foundations |
https://en.wikipedia.org/wiki/Paul%20Kline | Paul Kline (1937 – 25 September 1999) was a British psychologist noted for his contribution to psychometrics.
Career
Kline was originally educated in classics, in education, and in statistics: he studied at the University of Reading, University College Swansea, the University of Aberdeen and the University of Manchester. When he first joined the University of Exeter, it was as a staff member in the university's then Institute of Education. However, in 1969 he joined the Department of Psychology as a Lecturer, rising eventually to become the university's first Professor of Psychometrics.
Research
Kline was interested in depth psychology, especially theories of Sigmund Freud, the founder of psychoanalysis. He was also an expert in psychometrics and carried out extensive research in the statistical analysis of personality and intelligence.
In his 1972 book Fact and Fantasy in Freudian Theory, widely translated, he brought these two interests together, examining the objective evidence for various ideas of Freudian theory, finding that some, but not all, were supported by the evidence. He also wrote introductory books to psychometrics, for example An easy guide to factor analysis (1994). He was a prolific author, writing or editing at least 14 books, and over 150 scientific papers are listed under his name in Web of Science.
Among colleagues, Kline had a reputation as an opinionated controversialist who remained a genial and supportive colleague; he was revered by students |
https://en.wikipedia.org/wiki/CALR | CALR may refer to:
Calreticulin, a protein that in humans is encoded by the CALR gene.
Chief Albert Luthuli Regiment, an infantry regiment of the South African Army
Computer-assisted legal research, a mode of legal research
Centre for Applied Language Research at the University of Southampton
Advisory Commission on Religious Freedom, part of the Spanish Ministry of Justice |
https://en.wikipedia.org/wiki/L-amino-acid%20oxidase | In enzymology, an L-amino acid oxidase (LAAO) () is an enzyme that catalyzes the chemical reaction.
an L-amino acid + H2O + O2 a 2-oxo acid + NH3 + H2O2
The enzyme was first described in 1944 by A. Zeller and A. Maritz. Not only are LAAOs quite variable in terms of molecular mass, they also vary widely regarding stability. In a similar vein, this enzyme performs in a myriad of biological activities including apoptosis-induction, edema-induction, hemorrhaging, and inhibition or induction of platelet aggregation.
As suggested by the name of the family, LAAOs are flavoenzymes which function to catalyze the stereospecific oxidative deamination of an L-amino acid. The three substrates of the enzymatic reaction are an L-amino acid, water, and oxygen, whereas the three products are the corresponding α-keto acid (2-oxo acid), ammonia, and hydrogen peroxide. One example of the enzyme in action occurs with the conversion L-alanine into pyruvic acid (2-oxopropanoic acid), as shown in Figure 1.
Abundance
Snake Venom
Although LAAOs are present in a variety of eukaryotic and prokaryotic organisms, snake venom is a particularly rich source of the enzyme and the LAAOs are proposed to supply toxic effects upon envenomation. LAAOs that have been purified from the venoms of various snake species have proven to be the best suitors for examining this novel family of enzymes. It has been determined in most cases concerning the snake families, such as Viperidae, Crotalidae, and Elapidae, that |
https://en.wikipedia.org/wiki/L-aspartate%20oxidase | In enzymology, a L-aspartate oxidase () is an enzyme that catalyzes the chemical reaction
L-aspartate + H2O + O2 oxaloacetate + NH3 + H2O2
The 3 substrates of this enzyme are L-aspartate, H2O, and O2, whereas its 3 products are oxaloacetate, NH3, and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is L-aspartate:oxygen oxidoreductase (deaminating). This enzyme participates in alanine and aspartate metabolism and nicotinate and nicotinamide metabolism. It employs one cofactor, FAD.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 1.4.3
Flavoproteins
Enzymes of known structure |
https://en.wikipedia.org/wiki/Leghemoglobin%20reductase | In enzymology, a leghemoglobin reductase () is an enzyme that catalyzes the chemical reaction
NAD(P)H + H+ + 2 ferrileghemoglobin NAD(P)+ + 2 ferroleghemoglobin
In other words, a leghemoglobin (or phytoglobin in general) with a Fe3+ is reduced to one with the ferrous ion, Fe2+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with a heme protein as acceptor. The systematic name of this enzyme class is NAD(P)H:ferrileghemoglobin oxidoreductase. This enzyme is also called ferric leghemoglobin reductase.
Role in legume nodules
Leghemoglobin (Lb) is a heme-containing protein that reversibly binds and transports O2 into the N2-fixing nodules of leguminous plants. In order to function as an O2-carrier Lb must be in the ferrous oxidation state (Lb2+). Oxygenated Lb2+ (Lb2+O2) readily autoxidizes to ferric Lb (Lb3+) generating O2− in the presence of trace amounts of transition metals, chelators and toxic metabolites (such as nitrite, superoxide radical and peroxides), however Lb2+ is the predominant form in nodules. Therefore, mechanisms exist in vivo for maintaining Lb in the functional ferrous status.
History
Burris and Hass were the first to propose that reduced pyridine nucleotides might function as reductants of Lb3+ in leguminous root nodules and in 1969 Appleby reported that Lb3+ was reduced to Lb2+ by a suspension of bacteroids. In 1982 Kretovich and collaborators purified an enzyme from lupine nodules which catalyzed |
https://en.wikipedia.org/wiki/L-erythro-3%2C5-diaminohexanoate%20dehydrogenase | In enzymology, a L-erythro-3,5-diaminohexanoate dehydrogenase () is an enzyme that catalyzes the chemical reaction
L-erythro-3,5-diaminohexanoate + H2O + NAD+ (S)-5-amino-3-oxohexanoate + NH3 + NADH + H+
The 3 substrates of this enzyme are L-erythro-3,5-diaminohexanoate, H2O, and NAD+, whereas its 4 products are (S)-5-amino-3-oxohexanoate, NH3, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-erythro-3,5-diaminohexanoate:NAD+ oxidoreductase (deaminating). This enzyme is also called L-3,5-diaminohexanoate dehydrogenase. This enzyme participates in lysine degradation.
References
EC 1.4.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Leucine%20dehydrogenase | In enzymology, a leucine dehydrogenase () is an enzyme that catalyzes the chemical reaction
L-leucine + H2O + NAD+ 4-methyl-2-oxopentanoate + NH3 + NADH + H+
The 3 substrates of this enzyme are L-leucine, H2O, and NAD+, whereas its 4 products are 4-methyl-2-oxopentanoate, NH3, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-leucine:NAD+ oxidoreductase (deaminating). Other names in common use include L-leucine dehydrogenase, L-leucine:NAD+ oxidoreductase, deaminating, and LeuDH. This enzyme participates in valine, leucine and isoleucine degradation and valine, leucine and isoleucine biosynthesis.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.4.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/L-glutamate%20oxidase | In enzymology, a L-glutamate oxidase () is an enzyme that catalyzes the chemical reaction
L-glutamate + O2 + H2O 2-oxoglutarate + NH3 + H2O2
The 3 substrates of this enzyme are L-glutamate, O2, and H2O, whereas its 3 products are 2-oxoglutarate, NH3, and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is L-glutamate:oxygen oxidoreductase (deaminating). Other names in common use include glutamate (acceptor) dehydrogenase, glutamate oxidase, glutamic acid oxidase, glutamic dehydrogenase (acceptor), and L-glutamic acid oxidase. It employs one cofactor, FAD.
References
EC 1.4.3
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Gallium%20manganese%20arsenide | Gallium manganese arsenide, chemical formula is a magnetic semiconductor. It is based on the world's second most commonly used semiconductor, gallium arsenide, (chemical formula ), and readily compatible with existing semiconductor technologies. Differently from other dilute magnetic semiconductors, such as the majority of those based on II-VI semiconductors, it is not paramagnetic
but ferromagnetic, and hence exhibits hysteretic magnetization behavior. This memory effect is of importance for the creation of persistent devices. In , the manganese atoms provide a magnetic moment, and each also acts as an acceptor, making it a p-type material. The presence of carriers allows the material to be used for spin-polarized currents. In contrast, many other ferromagnetic magnetic semiconductors are strongly insulating
and so do not possess free carriers. is therefore a candidate as a spintronic material.
Growth
Like other magnetic semiconductors, is formed by doping a standard semiconductor with magnetic elements. This is done using the growth technique molecular beam epitaxy, whereby crystal structures can be grown with atom layer precision. In the manganese substitute into gallium sites in the GaAs crystal and provide a magnetic moment. Because manganese has a low solubility in GaAs, incorporating a sufficiently high concentration for ferromagnetism to be achieved proves challenging. In standard molecular beam epitaxy growth, to ensure that a good structural quality is obtaine |
https://en.wikipedia.org/wiki/L-lysine%206-oxidase | In enzymology, a L-lysine 6-oxidase () is an enzyme that catalyzes the chemical reaction
L-lysine + O2 + H2O 2-aminoadipate 6-semialdehyde + H2O2 + NH3
The 3 substrates of this enzyme are L-lysine, O2, and H2O, whereas its 3 products are 2-aminoadipate 6-semialdehyde, H2O2, and NH3.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is L-lysine:oxygen 6-oxidoreductase (deaminating). Other names in common use include L-lysine-epsilon-oxidase, Lod, LodA, and marinocine.
References
EC 1.4.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/L-lysine%20oxidase | In enzymology, a L-lysine oxidase () is an enzyme that catalyzes the chemical reaction
L-lysine + O2 + H2O 6-amino-2-oxohexanoate + NH3 + H2O2
The 3 substrates of this enzyme are L-lysine, O2, and H2O, whereas its 3 products are 6-amino-2-oxohexanoate, NH3, and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is L-lysine:oxygen 2-oxidoreductase (deaminating). Other names in common use include L-lysine alpha-oxidase, and L-lysyl-alpha-oxidase. This enzyme participates in lysine degradation.
References
EC 1.4.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/L-methionine%20%28R%29-S-oxide%20reductase | In enzymology, a L-methionine (R)-S-oxide reductase () is an enzyme that catalyzes the chemical reaction
L-methionine + thioredoxin disulfide + H2O L-methionine (R)-S-oxide + thioredoxin
The 3 substrates of this enzyme are L-methionine, thioredoxin disulfide, and H2O, whereas its two products are L-methionine (R)-S-oxide and thioredoxin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The systematic name of this enzyme class is L-methionine:thioredoxin-disulfide S-oxidoreductase [L-methionine (R)-S-oxide-forming]. Other names in common use include fRMsr, FRMsr, free met-R-(o) reductase, and free-methionine (R)-S-oxide reductase. This enzyme participates in methionine metabolism.
References
EC 1.8.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/L-methionine%20%28S%29-S-oxide%20reductase | In enzymology, a L-methionine (S)-S-oxide reductase () is an enzyme that catalyzes the chemical reaction
L-methionine + thioredoxin disulfide + H2O L-methionine (S)-S-oxide + thioredoxin
The 3 substrates of this enzyme are L-methionine, thioredoxin disulfide, and H2O, whereas its two products are L-methionine (S)-S-oxide and thioredoxin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The systematic name of this enzyme class is L-methionine:thioredoxin-disulfide S-oxidoreductase. Other names in common use include fSMsr, methyl sulfoxide reductase I and II, acetylmethionine sulfoxide reductase, methionine sulfoxide reductase, L-methionine:oxidized-thioredoxin S-oxidoreductase, methionine-S-oxide reductase, and free-methionine (S)-S-oxide reductase. This enzyme participates in methionine metabolism.
References
EC 1.8.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/L-pipecolate%20dehydrogenase | In enzymology, a L-pipecolate dehydrogenase () is an enzyme that catalyzes the chemical reaction
L-pipecolate + acceptor 2,3,4,5-tetrahydropyridine-2-carboxylate + reduced acceptor
Thus, the two substrates of this enzyme are L-pipecolate and acceptor, whereas its two products are 2,3,4,5-tetrahydropyridine-2-carboxylate and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with other acceptors. The systematic name of this enzyme class is L-pipecolate:acceptor 1,6-oxidoreductase. This enzyme is also called L-pipecolate:(acceptor) 1,6-oxidoreductase. This enzyme participates in lysine degradation.
References
EC 1.5.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/L-pipecolate%20oxidase | In enzymology, a L-pipecolate oxidase () is an enzyme that catalyzes the chemical reaction
L-pipecolate + O2 2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
Thus, the two substrates of this enzyme are L-pipecolate and O2, whereas its two products are 2,3,4,5-tetrahydropyridine-2-carboxylate and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with oxygen as acceptor. The systematic name of this enzyme class is L-pipecolate:oxygen 1,6-oxidoreductase. Other names in common use include pipecolate oxidase, and L-pipecolic acid oxidase. This enzyme participates in lysine degradation.
References
EC 1.5.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Lysine%20dehydrogenase | In enzymology, a lysine dehydrogenase () is an enzyme that catalyzes the chemical reaction
L-lysine + NAD+ 1,2-didehydropiperidine-2-carboxylate + NH3 + NADH + H+
Thus, the two substrates of this enzyme are L-lysine and NAD+, whereas its 4 products are 1,2-didehydropiperidine-2-carboxylate, NH3, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-lysine:NAD+ oxidoreductase (deaminating, cyclizing).
References
EC 1.4.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Methanethiol%20oxidase | In enzymology, a methanethiol oxidase () is an enzyme that catalyzes the chemical reaction
methanethiol + O2 + H2O formaldehyde + hydrogen sulfide + H2O2
The 3 substrates of this enzyme are methanethiol, O2, and H2O, whereas its 3 products are formaldehyde, hydrogen sulfide, and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with oxygen as acceptor. The systematic name of this enzyme class is methanethiol:oxygen oxidoreductase. Other names in common use include methylmercaptan oxidase, methyl mercaptan oxidase, (MM)-oxidase, and MT-oxidase.
References
EC 1.8.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Methylenetetrahydrofolate%20dehydrogenase%20%28NAD%2B%29 | In enzymology, a methylenetetrahydrofolate dehydrogenase (NAD+) () is an enzyme that catalyzes a chemical reaction.
5,10-methylenetetrahydrofolate + NAD+ 5,10-methenyltetrahydrofolate + NADH + H+
Thus, the two substrates of this enzyme are 5,10-methylenetetrahydrofolate and NAD+, whereas its 3 products are 5,10-methenyltetrahydrofolate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 5,10-methylenetetrahydrofolate:NAD+ oxidoreductase. This enzyme is also called methylenetetrahydrofolate dehydrogenase (NAD+). This enzyme participates in one carbon pool by folate.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 1.5.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Methylenetetrahydrofolate%20dehydrogenase%20%28NADP%2B%29 | In enzymology, a methylenetetrahydrofolate dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
5,10-methylenetetrahydrofolate + NADP+ 5,10-methenyltetrahydrofolate + NADPH + H+
Thus, the two substrates of this enzyme are 5,10-methylenetetrahydrofolate and NADP+, whereas its 3 products are 5,10-methenyltetrahydrofolate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. This enzyme participates in glyoxylate and dicarboxylate metabolism and one carbon pool by folate.
Structural studies
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , and .
Clinical significance
Mutations of the MTHFD1 gene may disrupt the activity of the enzyme and cause methylenetetrahydrofolate dehydrogenase 1 deficiency, also known as combined immunodeficiency and megaloblastic anemia with or without hyperhomocysteinemia (CIMAH).
Alternative names
The systematic name of this enzyme class is 5,10-methylenetetrahydrofolate:NADP+ oxidoreductase. Other names in common use include N5,N10-methylenetetrahydrofolate dehydrogenase, 5,10-methylenetetrahydrofolate:NADP oxidoreductase, 5,10-methylenetetrahydrofolate dehydrogenase, methylenetetrahydrofolate dehydrogenase, and methylenetetrahydrofolate dehydrogenase (NADP).
References
EC 1.5.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Methylenetetrahydrofolate%20reductase%20%28ferredoxin%29 | In enzymology, a methylenetetrahydrofolate reductase (ferredoxin) () is an enzyme that catalyzes the chemical reaction
5-methyltetrahydrofolate + 2 oxidized ferredoxin 5,10-methylenetetrahydrofolate + 2 reduced ferredoxin + 2 H+
Thus, the two substrates of this enzyme are 5-methyltetrahydrofolate and oxidized ferredoxin, whereas its 3 products are 5,10-methylenetetrahydrofolate, reduced ferredoxin, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is 5-methyltetrahydrofolate:ferredoxin oxidoreductase. This enzyme is also called 5,10-methylenetetrahydrofolate reductase. This enzyme participates in one carbon pool by folate.
References
EC 1.5.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Methylenetetrahydromethanopterin%20dehydrogenase | In enzymology, a methylenetetrahydromethanopterin dehydrogenase () is an enzyme that catalyzes the chemical reaction
5,10-methylenetetrahydromethanopterin + coenzyme F420 5,10-methenyltetrahydromethanopterin + reduced coenzyme F420
Thus, the two substrates of this enzyme are 5,10-methylenetetrahydromethanopterin and coenzyme F420, whereas its two products are 5,10-methenyltetrahydromethanopterin and reduced coenzyme F420.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with other acceptors. The systematic name of this enzyme class is 5,10-methylenetetrahydromethanopterin:coenzyme-F420 oxidoreductase. Other names in common use include N5,N10-methylenetetrahydromethanopterin dehydrogenase, and 5,10-methylenetetrahydromethanopterin dehydrogenase. This enzyme participates in folate biosynthesis.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 1.5.98
Enzymes of known structure |
https://en.wikipedia.org/wiki/Methylglutamate%20dehydrogenase | In enzymology, a methylglutamate dehydrogenase () is an enzyme that catalyzes the chemical reaction
N-methyl-L-glutamate + acceptor + H2O L-glutamate + formaldehyde + reduced acceptor
The 3 substrates of this enzyme are N-methyl-L-glutamate, acceptor, and H2O, whereas its 3 products are L-glutamate, formaldehyde, and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with other acceptors. The systematic name of this enzyme class is N-methyl-L-glutamate:acceptor oxidoreductase (demethylating). Other names in common use include N-methylglutamate dehydrogenase, and N-methyl-L-glutamate:(acceptor) oxidoreductase (demethylating). This enzyme participates in methane metabolism.
References
EC 1.5.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Monodehydroascorbate%20reductase%20%28NADH%29 | In enzymology, a monodehydroascorbate reductase (MDAR) () is an enzyme that catalyzes the chemical reaction
NADH + H+ + 2 monodehydroascorbate NAD+ + 2 ascorbate
The 3 substrates of this enzyme are NADH, H+, and monodehydroascorbate, whereas its two products are NAD+ and ascorbate.
This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH, with a quinone or similar compound as an acceptor. The systematic name of this enzyme class is NADH: monodehydroascorbate oxidoreductase. Other names in common use include NADH: semidehydroascorbic acid oxidoreductase, MDHA, semidehydroascorbate reductase, AFR, AFR-reductase, ascorbic free radical reductase, ascorbate free radical reductase, SOR, MDAsA reductase (NADPH), SDA reductase, NADH: ascorbate radical oxidoreductase, NADH-semidehydroascorbate oxidoreductase, ascorbate free-radical reductase, NADH: AFR oxidoreductase, and monodehydroascorbate reductase (NADH2). This enzyme participates in ascorbate and aldarate metabolism.
In plants, the monodehydroascorbate reductase (MDAR) is an enzymatic component of the glutathione-ascorbate cycle that is one of the major antioxidant systems of plant cells for the protection against the damages produced by reactive oxygen species (ROS). The MDAR activity has been described in several cell compartments, such as chloroplasts, cytosol, mitochondria, glyoxysomes, and leaf peroxisomes.
References
EC 1.6.5
NADPH-dependent enzymes
NADH-dependent enzymes |
https://en.wikipedia.org/wiki/Mycothione%20reductase | In enzymology, a mycothione reductase () is an enzyme that catalyzes the chemical reaction
mycothione + NAD(P)H + H + 2 mycothiol + NADP+
in M. tuberculosis and other actinomycetes.
The 2 substrates of this enzyme are mycothiol and NADPH, whereas 2 molecules of mycothione and NADP+ are formed as products.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is mycothiol:NAD(P)+ oxidoreductase. This enzyme is also called mycothiol-disulfide reductase.
References
EC 1.8.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N5-%28carboxyethyl%29ornithine%20synthase | In enzymology, a N5-(carboxyethyl)ornithine synthase () is an enzyme that catalyzes the chemical reaction
N5-(L-1-carboxyethyl)-L-ornithine + NADP+ + H2O L-ornithine + pyruvate + NADPH + H+
The 3 substrates of this enzyme are N5-(L-1-carboxyethyl)-L-ornithine, NADP+, and H2O, whereas its 4 products are L-ornithine, pyruvate, NADPH, and H+.
Nomenclature
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is N5-(L-1-carboxyethyl)-L-ornithine:NADP+ oxidoreductase (L-ornithine-forming). Other names in common use include 5-N-(L-1-carboxyethyl)-L-ornithine:NADP+ oxidoreductase, and (L-ornithine-forming).
References
EC 1.5.1
NADPH-dependent enzymes
Enzymes of unknown structure |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.