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Search results 1 to 4 out of 4 for Son

Category restricted to ProteinDomain (x)

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Categories

Category: ProteinDomain
Type Details Score
Protein Domain
Type: Family
Description: Protein SON is a RNA-binding protein that acts as a mRNA splicing cofactor by promoting efficient splicing of transcripts that possess weak splice sites. It facilitates splicing through the recruitment of SR proteins, such as SC35, to RNAP complexes. It regulates a large number of genes dedicated to cell cycle progression [].
Protein Domain
Type: Family
Description: The downstream neighbour of Son (DONSON) protein, also known as protein humpty dumpy (Hd) in Drosophila, is essential for DNA amplification in the ovary, and is required for cell proliferation during development (the humpty dumpty name arises from the thin-eggshell phenotype of hd mutants) []. Depletion of the Hd protein has been shown to cause severe defects in genome replication and to result in DNA damage. Hd is largely found in nuclear foci; some may traverse the nuclear envelope. Its expression peaks during late G1 and S phase, and it responds to transcription factor E2F1/Dp []. The Hd protein sequence is conserved from plants to humans, and may constitute a new gene family required for cell proliferation in multicellular eukaryotes [].
Protein Domain
Type: Homologous_superfamily
Description: Small GTPases of the Ras family alternate between 2 conformations induced by the binding of either GTP or GDP. Guanine nucleotide exchange factors (GEFs) induce the dissociation of GDP to allow association of the more abundant GTP. The Ras-like family of small GTPases includes, among others, Ras, Rap1, R-ras, and Ral. The family is characterised by similarities in the effector domain. The Ras GTPase Rap1 is activated rapidly in response to activation of a variety of receptors. Rap1 activation is mediated by several second messengers, including calcium, diacylglycerol, and cAMP. GEFs have been identified that mediate these effects. One such GEF is Epac, an exchange protein directly activated by cAMP, which represents a novel cAMP-induced, protein kinase A-independent pathway [].This superfamily represents a multihelical domain found in Ras GEFs. It can be subdivided in two domains: Ras GEF catalytic domain () and Ras GEF N-terminal domain (). In the nucleotide exchange factor Son of sevenless (SOS), both of these domains are required for the Ras specific nucleotide exchange activity, and both of them together are referred to as SOS-cat [].
Protein Domain
Type: Domain
Description: The G-patch domain is an approximately 48 amino acid domain, which is found ina single copy in several RNA-associated proteins and in type D retroviralpolyproteins. It is widespread among eukaryotes but is absent in archaea andbacteria. The G-patch domain has been called after its most notable feature,the presence of six highly conserved glycine residues. The position followingthe first conserved glycine is occupied almost invariably by an aromaticresidue, and several other positions are occupied predominantly by eitherhydrophobic or small residues. Several groups of G-patch containing proteinsare conserved in animals, plants and fungi. In some of these proteins the G-patch is the only recognisable domain but in most of them it is combined withother domains, which include well-defined RNA-binding domains, such as theRRM, dsRBD, SURP and R3H. It has been suggested that the G-patch domain has a specific function in RNA processing and, in particular, that it might be a previously undetected RNA-binding domain mediating a distinct type of RNA-protein interaction.Secondary structure prediction indicates that the G-patch domain probablycontains two α-helices, with four out of the six glycines located withinan intervening loop.Proteins known to contain a G-patch domain include:Eukaryotic 45kDa splicing factor (SPF-45).Mammmalian SON protein, a DNA-binding protein.Human LUCA15, a multidomain RNA-binding protein that is the product of a gene deleted in certain lung tumors.Human DAN26/EPROT, a multidomain protein, which, in addition to the G-patch domain, contains an RNA polymerase II C-terminal repeat-binding domain seen in many proteins of the polyA-addition machinery.Arabidopsis thaliana DRT111, a protein which has been shown to partially restore recombination proficiency and DNA-damage resistance to E. coli mutants.Type D retroviral polyprotein, where the G-patch domain is found directly downstream of the protease domain.