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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 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein 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 aft ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Homodimer
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 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
SPRY4
Protein sprouty homolog 4 is a protein that in humans is encoded by the ''SPRY4'' gene. Function SPRY4 is an inhibitor of the receptor-transduced mitogen-activated protein kinase (MAPK) signaling pathway. It is positioned upstream of RAS (see HRAS; MIM 190020) activation and impairs the formation of active GTP-RAS (Leeksma et al., 2002). Interactions SPRY4 has been shown to interact with TESK1. See also *MAPK signaling pathway *Ras subfamily Ras, from "Rat sarcoma virus", is a family of related proteins that are expressed in all animal cell lineages and organs. All Ras protein family members belong to a class of protein called small GTPase, and are involved in transmitting signals ... References Further reading * * * * * * External links PDBe-KBprovides an overview of all the structure information available in the PDB for Human Protein sprouty homolog 4 (SPRY4) SPR domain Human proteins {{gene-5-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
SPRY3
Protein sprouty homolog 3 is a protein that in humans is encoded by the ''SPRY3'' gene. The ''SPRY3'' gene is one of the genes found in the pseudoautosomal regions of the human sex chromosomes A sex chromosome (also referred to as an allosome, heterotypical chromosome, gonosome, heterochromosome, or idiochromosome) is a chromosome that differs from an ordinary autosome in form, size, and behavior. The human sex chromosomes, a typical ... (i.e. those 19 genes that are found on both the X and Y chromosome). It is located in the PAR2 region. References Further reading * * * * * * * * * External links * * SPR domain Human proteins {{gene-X-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
SPRED3
Sprouty-related, EVH1 domain-containing protein 3 also known as Spread-3 is a protein that in humans is encoded by the ''SPRED3'' gene. Spread-3 is a member of the Sprouty (see SPRY1/SPRED) family of proteins that regulate growth factor A growth factor is a naturally occurring substance capable of stimulating cell proliferation, wound healing, and occasionally cellular differentiation. Usually it is a secreted protein or a steroid hormone. Growth factors are important for regu ...-induced activation of the MAP kinase cascade. References Further reading * * * * EVH1 domain SPR domain {{gene-19-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
SPRED2
Sprouty-related, EVH1 domain-containing protein 2 is a protein that in humans is encoded by the ''SPRED2'' gene. Function SPRED2 is a member of the Sprouty (see SPRY1)/SPRED family of proteins that regulate growth factor-induced activation of the MAP kinase cascade (see MAPK1 Mitogen-activated protein kinase 1, (MAPK 1), also known as ERK2, is an enzyme that in humans is encoded by the ''MAPK1'' gene. Function The protein encoded by this gene is a member of the MAP kinase family. MAP kinases, also known as extracel ...). References Further reading * * * * * * * * * * * * * * * External links GeneReviews/NIH/NCBI/UW entry on Legius syndrome SPRED1 Sprouty-related, EVH1 domain-containing protein 1 SPR domain EVH1 domain Human proteins {{gene-2-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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 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). ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
N-terminus
The N-terminus (also known as the amino-terminus, NH2-terminus, N-terminal end or amine-terminus) is the start of a protein or polypeptide, referring to the free amine group (-NH2) located at the end of a polypeptide. Within a peptide, the amine group is bonded to the carboxylic group of another amino acid, making it a chain. That leaves a free carboxylic group at one end of the peptide, called the C-terminus, and a free amine group on the other end called the N-terminus. By convention, peptide sequences are written N-terminus to C-terminus, left to right (in LTR writing systems). This correlates the translation direction to the text direction, because when a protein is translated from messenger RNA, it is created from the N-terminus to the C-terminus, as amino acids are added to the carboxyl end of the protein. Chemistry Each amino acid has an amine group and a carboxylic group. Amino acids link to one another by peptide bonds which form through a dehydration reaction that ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
WH1 Domain
WH1 domain is an evolutionary conserved protein domain. Therefore, it has an important function. Function WH1 domains are found on WASP proteins, which are often involved in actin polymerization. Hence, WH1 is important for all cellular processes involving actin, this includes cell motility, cell trafficking, cell division and cytokinesis, cell signalling, and the establishment and maintenance of cell junctions and cell shape. Structure Tertiary structure of the WH1 domain of the Mena protein revealed structure similarities with the pleckstrin (PH) domain. The overall fold consists of a compact parallel beta-sandwich, closed along one edge by a long alpha helix. A highly conserved cluster of three surface-exposed aromatic side-chains forms the recognition site for the molecule's target ligands. Interactions The WASP protein family control actin polymerization by activating the Arp2/3 complex. WASP is defective in Wiskott–Ald ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cell (biology)
The cell is the basic structural and functional unit of life forms. Every cell consists of a cytoplasm enclosed within a membrane, and contains many biomolecules such as proteins, DNA and RNA, as well as many small molecules of nutrients and metabolites.Cell Movements and the Shaping of the Vertebrate Body in Chapter 21 of Molecular Biology of the Cell '' fourth edition, edited by Bruce Alberts (2002) published by Garland Science. The Alberts text discusses how the "cellular building blocks" move to shape developing embryos. It is also common to describe small molecules such as ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
