SPRY2
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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 C-terminus, carboxyl-terminal cysteine-rich protein domain, domain essential for the inhibitory activity on receptor tyrosine kinase signaling proteins and is required for growth factor stimulated Protein translocation, translocation of the protein to membrane ruffles. In primary dermal endothelial cells this gene is transiently upregulated in response to basic fibroblast growth factor, 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 r ...
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SPR Domain
In molecular biology the SPR domain is a protein domain found in the Sprouty (Spry) and Spread (Sprouty related EVH1 domain) proteins. These have been identified as Enzyme inhibitor, inhibitors of the Ras/mitogen-activated protein kinase (MAPK) cascade, a pathway crucial for developmental processes initiated by gene activation, activation of various receptor tyrosine kinases. These proteins share a conserved, C-terminal cysteine-rich region, the SPR Domain (biology), domain. This domain has been defined as a novel cytosol to Cell membrane, membrane Chromosomal translocation, translocation domain. It has been found to be a PtdIns(4,5)P2-binding domain that targets the proteins to a cell (biology), cellular localization that maximizes their inhibitory potential. It also mediates homodimer formation of these proteins. The SPR domain can occur in association with the WH1 domain (see ) (located in the N-terminus) in the Spread proteins. Examples Human genes encoding protein containi ...
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SPRY1
Protein sprouty homolog 1 is a protein that in humans is encoded by the ''SPRY1'' gene. See also *Neurofibromin 1 *SPRED1 Sprouty-related, EVH1 domain-containing protein 1 (Spread-1) is a protein that in humans is encoded by the ''SPRED1'' gene located on chromosome 15q13.2 and has seven coding exons. Function SPRED-1 is a member of the Sprouty family of proteins ... References Further reading * * * * * * * * * * External links * * SPR domain Human proteins {{gene-4-stub ...
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SPRED1 Gene
Sprouty-related, EVH1 domain-containing protein 1 (Spread-1) is a protein that in humans is encoded by the ''SPRED1'' gene located on chromosome 15q13.2 and has seven coding exons. Function SPRED-1 is a member of the Sprouty family of proteins and is phosphorylated by tyrosine kinase in response to several growth factors. The encoded protein can act as a homodimer or as a heterodimer with SPRED2 to regulate activation of the MAP kinase cascade. Clinical associations Defects in this gene are a cause of neurofibromatosis type 1-like syndrome (NFLS). Mutations in this gene are associated with * Legius syndrome. * * Childhood leukemia Mutations The following mutations have been observed: * An exon 3 c.46C>T mutation leading to p.Arg16Stop. This mutation may result in a truncated nonfunctional protein. Blast cells analysis displayed the same abnormality as germline mutation with one mutated allele (no somatic SPRED1 single-point mutation or loss of heterozygosity was found). ...
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Cbl Gene
''Cbl'' (named after Casitas B-lineage Lymphoma) is a mammalian gene encoding the protein CBL which is an E3 ubiquitin-protein ligase involved in cell signalling and protein ubiquitination. Mutations to this gene have been implicated in a number of human cancers, particularly acute myeloid leukaemia. Discovery In 1989 a virally encoded portion of the chromosomal mouse ''Cbl'' gene was the first member of the Cbl family to be discovered and was named ''v-Cbl'' to distinguish it from normal mouse ''c-Cbl''. The virus used in the experiment was a mouse-tropic strain of Murine leukemia virus isolated from the brain of a mouse captured at Lake Casitas, California known as ''Cas-Br-M'', and was found to have excised approximately a third of the original ''c-Cbl'' gene from a mouse into which it was injected. Sequencing revealed that the portion carried by the retrovirus encoded a ''tyrosine kinase binding domain'', and that this was the oncogenic form as retroviruses carrying ful ...
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CBL (gene)
''Cbl'' (named after Casitas B-lineage Lymphoma) is a mammalian gene encoding the protein CBL which is an E3 ubiquitin-protein ligase involved in cell signalling and protein ubiquitination. Mutations to this gene have been implicated in a number of human cancers, particularly acute myeloid leukaemia. Discovery In 1989 a virally encoded portion of the chromosomal mouse ''Cbl'' gene was the first member of the Cbl family to be discovered and was named ''v-Cbl'' to distinguish it from normal mouse ''c-Cbl''. The virus used in the experiment was a mouse-tropic strain of Murine leukemia virus isolated from the brain of a mouse captured at Lake Casitas, California known as ''Cas-Br-M'', and was found to have excised approximately a third of the original ''c-Cbl'' gene from a mouse into which it was injected. Sequencing revealed that the portion carried by the retrovirus encoded a ''tyrosine kinase binding domain'', and that this was the oncogenic form as retroviruses carrying ful ...
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MAPK/ERK Pathway
The MAPK/ERK pathway (also known as the Ras-Raf-MEK-ERK pathway) is a chain of proteins in the cell that communicates a signal from a receptor on the surface of the cell to the DNA in the nucleus of the cell. The signal starts when a signaling molecule binds to the receptor on the cell surface and ends when the DNA in the nucleus expresses a protein and produces some change in the cell, such as cell division. The pathway includes many proteins, such as mitogen-activated protein kinases (MAPKs), originally called extracellular signal-regulated kinases (ERKs), which communicate by adding phosphate groups to a neighboring protein ( phosphorylating it), thereby acting as an "on" or "off" switch. When one of the proteins in the pathway is mutated, it can become stuck in the "on" or "off" position, a necessary step in the development of many cancers. In fact, components of the MAPK/ERK pathway were first discovered in cancer cells, and drugs that reverse the "on" or "off" switch are ...
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Neurofibromin 1
Neurofibromin 1 (''NF1'') is a gene in humans that is located on chromosome 17. ''NF1'' codes for neurofibromin, a GTPase-activating protein that negatively regulates RAS/MAPK pathway activity by accelerating the hydrolysis of Ras-bound GTP. ''NF1'' has a high mutation rate and mutations in ''NF1'' can alter cellular growth control, and neural development, resulting in neurofibromatosis type 1 (NF1, also known as von Recklinghausen syndrome). Symptoms of NF1 include disfiguring cutaneous neurofibromas (CNF), café au lait pigment spots, plexiform neurofibromas (PN), skeletal defects, optic nerve gliomas, life-threatening malignant peripheral nerve sheath tumors (MPNST), pheochromocytoma, attention deficits, learning deficits and other cognitive disabilities. Gene ''NF1'' was cloned in 1990 and its gene product neurofibromin was identified in 1992. Neurofibromin, a GTPase-activating protein, primarily regulates the protein Ras. ''NF1'' is located on the long arm of chromosom ...
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Homodimers
In biochemistry, a protein dimer is a macromolecular complex formed by two protein monomers, or single proteins, which are usually non-covalently bound. Many macromolecules, such as proteins or nucleic acids, form dimers. The word ''dimer'' has roots meaning "two parts", '' di-'' + '' -mer''. A protein dimer is a type of protein quaternary structure. A protein homodimer is formed by two identical proteins. A protein heterodimer is formed by two different proteins. Most protein dimers in biochemistry are not connected by covalent bonds. An example of a non-covalent heterodimer is the enzyme reverse transcriptase, which is composed of two different amino acid chains. An exception is dimers that are linked by disulfide bridges such as the homodimeric protein NEMO. Some proteins contain specialized domains to ensure dimerization (dimerization domains) and specificity. The G protein-coupled cannabinoid receptors have the ability to form both homo- and heterodimers with several typ ...
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Heterodimers
In biochemistry, a protein dimer is a macromolecular complex formed by two protein monomers, or single proteins, which are usually non-covalently bound. Many macromolecules, such as proteins or nucleic acids, form dimers. The word ''dimer'' has roots meaning "two parts", '' di-'' + ''-mer''. A protein dimer is a type of protein quaternary structure. A protein homodimer is formed by two identical proteins. A protein heterodimer is formed by two different proteins. Most protein dimers in biochemistry are not connected by covalent bonds. An example of a non-covalent heterodimer is the enzyme reverse transcriptase, which is composed of two different amino acid chains. An exception is dimers that are linked by disulfide bridges such as the homodimeric protein NEMO. Some proteins contain specialized domains to ensure dimerization (dimerization domains) and specificity. The G protein-coupled cannabinoid receptors have the ability to form both homo- and heterodimers with several ...
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Isoforms
A protein isoform, or "protein variant", is a member of a set of highly similar proteins that originate from a single gene or gene family and are the result of genetic differences. While many perform the same or similar biological roles, some isoforms have unique functions. A set of protein isoforms may be formed from alternative splicings, variable promoter usage, or other post-transcriptional modifications of a single gene; post-translational modifications are generally not considered. (For that, see Proteoforms.) Through RNA splicing mechanisms, mRNA has the ability to select different protein-coding segments ( exons) of a gene, or even different parts of exons from RNA to form different mRNA sequences. Each unique sequence produces a specific form of a protein. The discovery of isoforms could explain the discrepancy between the small number of protein coding regions genes revealed by the human genome project and the large diversity of proteins seen in an organism: different ...
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Microtubules
Microtubules are polymers of tubulin that form part of the cytoskeleton and provide structure and shape to eukaryotic cells. Microtubules can be as long as 50 micrometres, as wide as 23 to 27  nm and have an inner diameter between 11 and 15 nm. They are formed by the polymerization of a dimer of two globular proteins, alpha and beta tubulin into protofilaments that can then associate laterally to form a hollow tube, the microtubule. The most common form of a microtubule consists of 13 protofilaments in the tubular arrangement. Microtubules play an important role in a number of cellular processes. They are involved in maintaining the structure of the cell and, together with microfilaments and intermediate filaments, they form the cytoskeleton. They also make up the internal structure of cilia and flagella. They provide platforms for intracellular transport and are involved in a variety of cellular processes, including the movement of secretory vesicles, organell ...
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