RhoGEF Domain
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RhoGEF Domain
RhoGEF domain describes two distinct structural domains with guanine nucleotide exchange factor (GEF) activity to regulate small GTPases in the Rho family. Rho small GTPases are inactive when bound to GDP but active when bound to GTP; RhoGEF domains in proteins are able to promote GDP release and GTP binding to activate specific Rho family members, including RhoA, Rac1 and Cdc42. The largest class of RhoGEFs is composed of proteins containing the " Dbl-homology" (DH) domain, which almost always is found together with a pleckstrin-homology (PH) domain to form a combined DH/PH domain structure. A distinct class of RhoGEFs is those proteins containing the DOCK/CZH/DHR-2 domain. This structure has no sequence similarity with DBL-homology domains. Human proteins containing DH/PH RhoGEF domain ABR; AKAP13/ARHGEF13/Lbc; ALS2; ALS2CL; ARHGEF1/p115-RhoGEF; ARHGEF10; ARHGEF10L; ARHGEF11/PDZ-RhoGEF.; ARHGEF12/LARG; ARHGEF15; ARHGEF16; ARHGEF17; ARHGEF18; ...
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Structural Domain
In molecular biology, a protein domain is a region of a protein's polypeptide chain that is self-stabilizing and that folds independently from the rest. Each domain forms a compact folded three-dimensional structure. Many proteins consist of several domains, and a domain may appear in a variety of different proteins. Molecular evolution uses domains as building blocks and these may be recombined in different arrangements to create proteins with different functions. In general, domains vary in length from between about 50 amino acids up to 250 amino acids in length. The shortest domains, such as zinc fingers, are stabilized by metal ions or disulfide bridges. Domains often form functional units, such as the calcium-binding EF hand domain of calmodulin. Because they are independently stable, domains can be "swapped" by genetic engineering between one protein and another to make chimeric proteins. Background The concept of the domain was first proposed in 1973 by Wetlaufer after ...
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ARHGEF10
The human ARHGEF10 gene encodes the protein Rho guanine nucleotide exchange factor 10. Rho GTPases play a fundamental role in numerous cellular processes that are initiated by extracellular stimuli that work through G protein G proteins, also known as guanine nucleotide-binding proteins, are a family of proteins that act as molecular switches inside cells, and are involved in transmitting signals from a variety of stimuli outside a cell to its interior. Their a ... coupled receptors. The encoded protein may form a complex with G proteins and stimulate Rho-dependent signals. References External links * Further reading

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ARHGEF3
Rho guanine nucleotide exchange factor (GEF) 3, also known as ARHGEF3, is a human gene. Function Rho GTPases play a fundamental role in numerous cellular processes that are initiated by extracellular stimuli that work through G protein-coupled receptors. The encoded protein may form complex with G proteins and stimulate Rho-dependent signals. This protein is similar to the NET1A protein. Interactions ARHGEF3 has been shown to interact with RHOA Transforming protein RhoA, also known as Ras homolog family member A (RhoA), is a small GTPase protein in the Rho family of GTPases that in humans is encoded by the ''RHOA'' gene. While the effects of RhoA activity are not all well known, it is ... and RHOB. References External links * Further reading

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ARHGEF2
Rho guanine nucleotide exchange factor 2 is a protein that in humans is encoded by the ''ARHGEF2'' gene. Function Rho GTPases play a fundamental role in numerous cellular processes that are initiated by extracellular stimuli that work through G protein-coupled receptors. The encoded protein may form complex with G proteins and stimulate rho-dependent signals. Interactions ARHGEF2 has been shown to interact with PAK1 Serine/threonine-protein kinase PAK 1 is an enzyme that in humans is encoded by the ''PAK1'' gene. PAK1 is one of six members of the PAK family of serine/threonine kinases which are broadly divided into group I (PAK1, PAK2 and PAK3) and group II .... References External links * Further reading

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