Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
GTP-Binding Proteins
Guanosine Triphosphate
Molecular Sequence Data
Gene Expression Regulation, Fungal
Amino Acid Sequence
Mutation
Saccharomyces
Base Sequence
Cloning, Molecular
Sequence Homology, Amino Acid
RNA, Fungal
Protein Binding
Plasmids
Monomeric GTP-Binding Proteins
Chromosomes, Fungal
Guanosine Diphosphate
Genetic Complementation Test
rab GTP-Binding Proteins
DNA-Binding Proteins
Guanosine 5'-O-(3-Thiotriphosphate)
Gene Deletion
cdc42 GTP-Binding Protein
Transcription, Genetic
Phenotype
cdc25 Phosphatases
Carrier Proteins
ADP-Ribosylation Factors
Transcription Factors
rho GTP-Binding Proteins
Suppression, Genetic
Binding Sites
Cell Cycle Proteins
Recombinant Fusion Proteins
Signal Transduction
CDC2 Protein Kinase
Pertussis Toxin
Restriction Mapping
Mutagenesis
Guanine Nucleotide Exchange Factors
Sequence Alignment
Virulence Factors, Bordetella
Cell Membrane
beta-Fructofuranosidase
ras Proteins
Nuclear Proteins
Adenosine Diphosphate Ribose
Protein Structure, Tertiary
Genes, Suppressor
Escherichia coli
CDC28 Protein Kinase, S cerevisiae
ADP Ribose Transferases
Botulinum Toxins
RNA, Messenger
Membrane Proteins
Haploidy
Vacuoles
Temperature
Schizosaccharomyces
Transformation, Genetic
Recombination, Genetic
Fermentation
Cdc20 Proteins
DNA Primers
Poly(A)-Binding Proteins
Diploidy
Mitochondria
Silent Information Regulator Proteins, Saccharomyces cerevisiae
Cell Cycle
Alleles
Repressor Proteins
Promoter Regions, Genetic
Substrate Specificity
Glucose
Meiosis
Mutagenesis, Site-Directed
rhoA GTP-Binding Protein
cdc42 GTP-Binding Protein, Saccharomyces cerevisiae
Saccharomycetales
Two-Hybrid System Techniques
Adenosine Triphosphatases
Mitosis
Models, Biological
Biological Transport
DNA Repair
Genes, Mating Type, Fungal
RNA-Binding Proteins
Schizosaccharomyces pombe Proteins
Kluyveromyces
Cell Nucleus
Conserved Sequence
Spheroplasts
Protein Biosynthesis
Galactose
Protein-Serine-Threonine Kinases
Pheromones
Cell Wall
Candida albicans
Ergosterol
Cattle
Open Reading Frames
Genes
Protein Kinases
Sequence Homology, Nucleic Acid
Models, Molecular
Killer Factors, Yeast
Phosphorylation
Culture Media
DNA
Genes, Lethal
Electrophoresis, Polyacrylamide Gel
Membrane Transport Proteins
Chromosome Mapping
Models, Genetic
Species Specificity
Sirtuin 2
Telomere
Gene Expression
Cathepsin A
Macromolecular Substances
DNA Damage
Genotype
Ethanol
RNA, Transfer
Ribosomes
Protein Transport
beta-Galactosidase
Cell Division
Protein Conformation
Organisms, Genetically Modified
Yeasts
Ribosomal Proteins
Endoplasmic Reticulum
Blotting, Northern
Mannosyltransferases
Industrial Microbiology
DNA, Complementary
Inositol
Drug Resistance, Fungal
Pichia
Peptides
Rad52 DNA Repair and Recombination Protein
Protein Processing, Post-Translational
DNA Helicases
Allantoin
Epistasis, Genetic
Genes, Regulator
Adenosine Triphosphate
RNA Processing, Post-Transcriptional
Tacrolimus Binding Proteins
RNA Precursors
Methyl Methanesulfonate
Cytoplasm
Blotting, Western
GTP Cyclohydrolase
Structure-Activity Relationship
Nitrogen
Chromatin
RNA, Ribosomal
Hydrogen-Ion Concentration
Green Fluorescent Proteins
Intracellular Membranes
Trans-Activators
Chitin
Glycerol
Benomyl
Histones
Heat-Shock Proteins
Point Mutation
Sequence Analysis, DNA
Gene Expression Regulation
Ligases
ras-GRF1
Intracellular Signaling Peptides and Proteins
Ubiquitin-Protein Ligase Complexes
Antifungal Agents
Ultraviolet Rays
Microscopy, Fluorescence
Subcellular Fractions
Cdc42: An essential Rho-type GTPase controlling eukaryotic cell polarity. (1/193)
Cdc42p is an essential GTPase that belongs to the Rho/Rac subfamily of Ras-like GTPases. These proteins act as molecular switches by responding to exogenous and/or endogenous signals and relaying those signals to activate downstream components of a biological pathway. The 11 current members of the Cdc42p family display between 75 and 100% amino acid identity and are functional as well as structural homologs. Cdc42p transduces signals to the actin cytoskeleton to initiate and maintain polarized gorwth and to mitogen-activated protein morphogenesis. In the budding yeast Saccharomyces cerevisiae, Cdc42p plays an important role in multiple actin-dependent morphogenetic events such as bud emergence, mating-projection formation, and pseudohyphal growth. In mammalian cells, Cdc42p regulates a variety of actin-dependent events and induces the JNK/SAPK protein kinase cascade, which leads to the activation of transcription factors within the nucleus. Cdc42p mediates these processes through interactions with a myriad of downstream effectors, whose number and regulation we are just starting to understand. In addition, Cdc42p has been implicated in a number of human diseases through interactions with its regulators and downstream effectors. While much is known about Cdc42p structure and functional interactions, little is known about the mechanism(s) by which it transduces signals within the cell. Future research should focus on this question as well as on the detailed analysis of the interactions of Cdc42p with its regulators and downstream effectors. (+info)Multisite autophosphorylation of p21-activated protein kinase gamma-PAK as a function of activation. (2/193)
p21-activated protein kinase (PAK) is a family of serine/threonine kinases whose activity is stimulated by binding to small G-proteins such as Cdc42 and subsequent autophosphorylation. Focusing on the ubiquitous gamma-isoform of PAK in this study, baculovirus-infected insect cells were used to obtain recombinant gamma-PAK, while native gamma-PAK was isolated from rabbit reticulocytes. Two-dimensional gel electrophoresis of gamma-PAK followed by immunoblot analysis revealed a similar profile for native and recombinant gamma-PAK, both consisting of multiple protein spots. Following Cdc42-stimulated autophosphorylation, the two-dimensional profiles of native and recombinant gamma-PAK were characterized by a similar acidic shift, suggesting a common response to Cdc42. To understand the effect of differential phosphorylation on its activation status, gamma-PAK autophosphorylation was conducted in the presence or absence of activators such as Cdc42 and histone II-AS, followed by tryptic digestion and comparative two-dimensional phosphopeptide mapping. The major phosphopeptides were subjected to a combination of manual and automated amino acid sequencing. Overall, eight autophosphorylation sites were identified in Cdc42-activated gamma-PAK, six of which are in common with those previously reported in alpha-PAK, while Ser-19 and Ser-165 appear to be uniquely phosphorylated in the gamma-form. Further, the phosphorylation of Ser-141, Ser-165, and Thr-402 was found to correlate with gamma-PAK activation. (+info)Inducible recruitment of Cdc42 or WASP to a cell-surface receptor triggers actin polymerization and filopodium formation. (3/193)
BACKGROUND: Cdc42, a GTP-binding protein of the Rho family, controls actin cytoskeletal organization and helps to generate actin-based protruding structures, such as filopodia. In vitro, Cdc42 regulates actin polymerization by facilitating the creation of free barbed ends - the more rapidly growing ends of actin filaments - and subsequent elongation at these ends. The Wiskott- Aldrich syndrome protein, WASP, which has a pleckstrin-homology domain and a Cdc42/Rac-binding motif, has been implicated in cell signaling and cytoskeleton reorganization. We have investigated the consequences of local recruitment of activated Cdc42 or WASP to the plasma membrane. RESULTS: We used an activated Cdc42 protein that could be recruited to an engineered membrane receptor by adding rapamycin as a bridge, and added antibody-coupled beads to aggregate these receptors. Inducible recruitment of Cdc42 to clusters of receptors stimulated actin polymerization, resulting in the formation of membrane protrusions. Cdc42-induced protrusions were enriched in the vasodilator-stimulated phosphoprotein VASP and the focal-adhesion-associated proteins zyxin and ezrin. The Cdc42 effector WASP could also induce the formation of protrusions, albeit of different morphology. CONCLUSIONS: This is the first demonstration that the local recruitment of activated Cdc42 or its downstream effector, WASP, to a membrane receptor in whole cells is sufficient to trigger actin polymerization that results in the formation of membrane protrusions. Our data suggest that Cdc42-induced actin-based protrusions result from the local and serial recruitment of cytoskeletal proteins including zyxin, VASP, and ezrin. (+info)Crosstalk between the Ras2p-controlled mitogen-activated protein kinase and cAMP pathways during invasive growth of Saccharomyces cerevisiae. (4/193)
The two highly conserved RAS genes of the budding yeast Saccharomyces cerevisiae are redundant for viability. Here we show that haploid invasive growth development depends on RAS2 but not RAS1. Ras1p is not sufficiently expressed to induce invasive growth. Ras2p activates invasive growth using either of two downstream signaling pathways, the filamentation MAPK (Cdc42p/Ste20p/MAPK) cascade or the cAMP-dependent protein kinase (Cyr1p/cAMP/PKA) pathway. This signal branch point can be uncoupled in cells expressing Ras2p mutant proteins that carry amino acid substitutions in the adenylyl cyclase interaction domain and therefore activate invasive growth solely dependent on the MAPK cascade. Both Ras2p-controlled signaling pathways stimulate expression of the filamentation response element-driven reporter gene depending on the transcription factors Ste12p and Tec1p, indicating a crosstalk between the MAPK and the cAMP signaling pathways in haploid cells during invasive growth. (+info)The Cdc42p GTPase is involved in a G2/M morphogenetic checkpoint regulating the apical-isotropic switch and nuclear division in yeast. (5/193)
The Cdc42p GTPase is involved in the signal transduction cascades controlling bud emergence and polarized cell growth in S. cerevisiae. Cells expressing the cdc42(V44A) effector domain mutant allele displayed morphological defects of highly elongated and multielongated budded cells indicative of a defect in the apical-isotropic switch in bud growth. In addition, these cells contained one, two, or multiple nuclei indicative of a G2/M delay in nuclear division and also a defect in cytokinesis and/or cell separation. Actin and chitin were delocalized, and septin ring structure was aberrant and partially delocalized to the tips of elongated cdc42(V44A) cells; however, Cdc42(V44A)p localization was normal. Two-hybrid protein analyses showed that the V44A mutation interfered with Cdc42p's interactions with Cla4p, a p21(Cdc42/Rac)-activated kinase (PAK)-like kinase, and the novel effectors Gic1p and Gic2p, but not with the Ste20p or Skm1p PAK-like kinases, the Bni1p formin, or the Iqg1p IQGAP homolog. Furthermore, the cdc42(V44A) morphological defects were suppressed by deletion of the Swe1p cyclin-dependent kinase inhibitory kinase and by overexpression of Cla4p, Ste20p, the Cdc12 septin protein, or the guanine nucleotide exchange factor Cdc24p. In sum, these results suggest that proper Cdc42p function is essential for timely progression through the apical-isotropic switch and G2/M transition and that Cdc42(V44A)p differentially interacts with a number of effectors and regulators. (+info)Rho family GTPases control entry of Shigella flexneri into epithelial cells but not intracellular motility. (6/193)
Shigella flexneri, an invasive bacterial pathogen, promotes formation of two cytoskeletal structures: the entry focus that mediates bacterial uptake into epithelial cells and the actin-comet tail that enables the bacteria to spread intracellularly. During the entry step, secretion of bacterial invasins causes a massive burst of subcortical actin polymerization leading the formation of localised membrane projections. Fusion of these membrane ruffles leads to bacterial internalization. Inside the cytoplasm, polar expression of the IcsA protein on the bacterial surface allows polymerization of actin filaments and their organization into an actin-comet tail leading to bacterial spread. The Rho family of small GTPases plays an essential role in the organization and regulation of cellular cytoskeletal structures (i.e. filopodia, lamellipodia, adherence plaques and intercellular junctions). We show here that induction of Shigella entry foci is controlled by the Cdc42, Rac and Rho GTPases, but not by RhoG. In contrast, actin-driven intracellular motility of Shigella does not require Rho GTPases. Therefore, Shigella appears to manipulate the epithelial cell cytoskeleton both by Rho GTPase-dependent and -independent processes. (+info)Identification of the stef gene that encodes a novel guanine nucleotide exchange factor specific for Rac1. (7/193)
The Rho family GTPases are involved in a variety of cellular events by changing the organization of actin cytoskeletal networks in response to extracellular signals. However, it is not clearly known how their activities are spatially and temporally regulated. Here we report the identification of a novel guanine nucleotide exchange factor for Rac1, STEF, which is related in overall amino acid sequence and modular structure to mouse Tiam1 and Drosophila SIF proteins. STEF protein contains two pleckstrin homology domains, a PDZ domain and a Dbl homology domain. The in vitro assay showed that STEF protein specifically enhanced the dissociation of GDP from Rac1 but not that from either RhoA or Cdc42. Expression of a truncated STEF protein in culture cells induced membrane ruffling with altered actin localization, which implies that this protein also activates Rac1 in vivo. The stef transcript was observed in restricted parts of mice, including cartilaginous tissues and the cortical plate of the central nervous system during embryogenesis. These findings suggested that STEF protein participates in the control of cellular events in several developing tissues, possibly changing the actin cytoskeletal network by activating Rac1. (+info)Activation of Ste20 by Nef from human immunodeficiency virus induces cytoskeletal rearrangements and downstream effector functions in Saccharomyces cerevisiae. (8/193)
The negative factor (Nef) from human and simian immunodeficiency viruses is important for the pathogenesis of acquired immune deficiency syndrome. Among other targets, it activates the Nef-associated kinase, which is related to the p21-activated kinase. In this study, we demonstrate that Nef activates Ste20, the homolog of p21-activated kinase in Saccharomyces cerevisiae. Nef binds to the adaptor proteins Bem1 and Ste20 via its proline-rich (PXXP) and diarginine (RR) motifs, respectively. These interactions induce the mitogen-activated protein kinase and increase the rates of budding, sizes of cells, and patterns of mating projections. These effects of Nef depend on the small GTPase Cdc42 and guanine nucleotide exchange factor Cdc24. Thus, studies in S. cerevisiae identified specific interactions between Nef and cellular proteins and their associated signaling cascade. (+info)Some common effects of chromosomal deletions include:
1. Genetic disorders: Chromosomal deletions can lead to a variety of genetic disorders, such as Down syndrome, which is caused by a deletion of a portion of chromosome 21. Other examples include Prader-Willi syndrome (deletion of chromosome 15), and Williams syndrome (deletion of chromosome 7).
2. Birth defects: Chromosomal deletions can increase the risk of birth defects, such as heart defects, cleft palate, and limb abnormalities.
3. Developmental delays: Children with chromosomal deletions may experience developmental delays, learning disabilities, and intellectual disability.
4. Increased cancer risk: Some chromosomal deletions can increase the risk of developing certain types of cancer, such as chronic myelogenous leukemia (CML) and breast cancer.
5. Reproductive problems: Chromosomal deletions can lead to reproductive problems, such as infertility or recurrent miscarriage.
Chromosomal deletions can be diagnosed through a variety of techniques, including karyotyping (examination of the chromosomes), fluorescence in situ hybridization (FISH), and microarray analysis. Treatment options for chromosomal deletions depend on the specific effects of the deletion and may include medication, surgery, or other forms of therapy.
There are several types of genomic instability, including:
1. Chromosomal instability (CIN): This refers to changes in the number or structure of chromosomes, such as aneuploidy (having an abnormal number of chromosomes) or translocations (the movement of genetic material between chromosomes).
2. Point mutations: These are changes in a single base pair in the DNA sequence.
3. Insertions and deletions: These are changes in the number of base pairs in the DNA sequence, resulting in the insertion or deletion of one or more base pairs.
4. Genomic rearrangements: These are changes in the structure of the genome, such as chromosomal breaks and reunions, or the movement of genetic material between chromosomes.
Genomic instability can arise from a variety of sources, including environmental factors, errors during DNA replication and repair, and genetic mutations. It is often associated with cancer, as cancer cells have high levels of genomic instability, which can lead to the development of resistance to chemotherapy and radiation therapy.
Research into genomic instability has led to a greater understanding of the mechanisms underlying cancer and other diseases, and has also spurred the development of new therapeutic strategies, such as targeted therapies and immunotherapies.
In summary, genomic instability is a key feature of cancer cells and is associated with various diseases, including cancer, neurodegenerative disorders, and aging. It can arise from a variety of sources and is the subject of ongoing research in the field of molecular biology.
List of MeSH codes (D08)
List of MeSH codes (D12.776.476)
SEPT7
Guanine nucleotide exchange factor
List of MeSH codes (D12.776.157)
List of MeSH codes (D12.644)
Wiskott-Aldrich syndrome protein
Cell polarity
cdc42 GTP-Binding Protein, Saccharomyces cerevisiae | Profiles RNS
Direct interaction of the Wiskott-Aldrich syndrome protein with the GTPase Cdc42 - PubMed
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REPLACED MEDICAL SUBJECT HEADINGS WITH REPLACED-BY HEADINGS - 2002
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CDC42 Antibody - N-terminal region (AVARP01017 P050) | Aviva Systems Biology | Aviva Systems Biology
SMART: RhoGEF domain annotation
Pesquisa | Biblioteca Virtual em SaĆŗde - BRASIL
Pharos : Target Details - CDC42
WikiGenes - Arhgdia - Rho GDP dissociation inhibitor (GDI) alpha
TERM
Emerging roles of small GTPases in secondary cell wall development. - PDF Download Free
Cross-species analysis of LZTR1 loss-of-function mutants demonstrates dependency to RIT1 orthologs | eLife
Establishment of left/right asymmetry in neuroblast migration by UNC-40/DCC, UNC-73/Trio and DPY-19 proteins in C. elegans |...
SMED30028687
Active GTP-bound2
GTPases7
- We show here that WAS protein interacts with a member of the Rho family of GTPases, Cdc42. (nih.gov)
- Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. (embl.de)
- The Rho family GTPases Rho, Rac and CDC42 regulate a diverse array of cellular processes. (embl.de)
- It does not share significant sequence homology with other subtypes of small G-protein GEF motifs such as the Cdc25 domain and the Sec7 domain, which specifically interact with Ras and ARF family small GTPases, respectively, nor with other Rho protein interactive motifs, indicating that the Dbl family proteins are evolutionarily unique. (embl.de)
- RAS GTPases are highly conserved proteins involved in the regulation of mitogenic signaling. (elifesciences.org)
- Ras GTPases exhibit high affinity toward guanine nucleotides and act as molecular switches by mediating GTP hydrolysis. (elifesciences.org)
- Although GAPs and GEFs can rapidly affect the nucleotide cycling of RAS proteins, and hence their activity, other accessory proteins can modulate downstream signaling by regulating the stability and/or activity of RAS GTPases. (elifesciences.org)
Yeast2
- 15. The fission yeast cell wall stress sensor-like proteins Mtl2 and Wsc1 act by turning on the GTPase Rho1p but act independently of the cell wall integrity pathway. (nih.gov)
- This protein is highly similar to Saccharomyces cerevisiae Cdc 42, and is able to complement the yeast cdc42-1 mutant. (avivasysbio.com)
Annotation1
- Gene prediction and annotation identified six protein-coding genes in the delimited Sptm1 region, and the gene encoding a putative cold-responsive protein kinase was selected as a strong candidate. (bvsalud.org)
Regulate3
- T lymphocytes of affected males with WAS exhibit a severe disturbance of the actin cytoskeleton, suggesting that the WAS protein could regulate its organization. (nih.gov)
- This protein could regulate actin polymerization through its direct binding to Neural Wiskott-Aldrich syndrome protein (N-WASP), which subsequently activates Arp2/3 complex. (avivasysbio.com)
- In active state binds to a variety of effector proteins to regulate cellular responses. (nih.gov)
Effector2
- Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization. (nih.gov)
- Tagging of a fungal effector with a fluorescent protein and tracking its localization in cells of its natural host provides insight into its putative in planta localization and helps to narrow down the location of putative host interactors. (bvsalud.org)
Conformational1
- Upon GTP binding, RAS proteins undergo a conformational change, which promotes the interaction with different protein effectors that activate downstream signaling pathways, including Raf/MEK/ERK mitogen activated protein kinase (MAPK) and phosphoinositide 3-kinase (PI3K) pathways. (elifesciences.org)
Adaptor3
- Taken together these data suggest that the WAS protein might function as a signal transduction adaptor downstream of Cdc42, and in affected males, the cytoskeletal abnormalities may result from a defect in Cdc42 signaling. (nih.gov)
- We have previously described a novel Cullin 3 RING E3 ubiquitin ligase complex formed by the substrate adaptor protein LZTR1 that binds, ubiquitinates, and promotes proteasomal degradation of the RAS GTPase RIT1. (elifesciences.org)
- Using elegant cross-species biochemistry and genetic approaches, this paper describes the role of the ubiquitin adaptor protein LZTR1 in regulation of the RAS-related GTPase RIT1 as its principal substrate involved in the RASopathy, Noonan syndrome. (elifesciences.org)
Mutant2
MeSH1
- cdc42 GTP-Binding Protein, Saccharomyces cerevisiae" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (wakehealth.edu)
Implicated in the regulation1
- The Rho family of GTP-binding proteins has been implicated in the regulation of various cellular functions including actin cytoskeleton-dependent morphological change. (embl.de)
Guanine3
- Activation of Rho proteins through release of bound GDP and subsequent binding of GTP, is catalysed by guanine nucleotide exchange factors (GEFs) in the Dbl family. (embl.de)
- The guanine nucleotide exchange factor (GEF) Dbl targets Rho family proteins thereby stimulating their GDP/GTP exchange, and thus is believed to be involved in receptor-mediated regulation of the proteins. (embl.de)
- In differentiating xylem cells, a speciļ¬c GTPase-activating protein (GAP)/guanine nucleotide exchange factor (GEF) pair facilitates local activation of ROP11 to establish de novo plasma membrane domains. (docksci.com)
GTPase4
- 14. Rga5p is a specific Rho1p GTPase-activating protein that regulates cell integrity in Schizosaccharomyces pombe. (nih.gov)
- 17. Schizosaccharomyces pombe rho2p GTPase regulates cell wall alpha-glucan biosynthesis through the protein kinase pck2p. (nih.gov)
- CDC42 is a small GTPase of the Rho-subfamily, which regulates signaling pathways that control diverse cellular functions including cell morphology, migration, endocytosis and cell cycle progression. (avivasysbio.com)
- Alternative splicing of this gene results in multiple transcript variants.The protein encoded by this gene is a small GTPase of the Rho-subfamily, which regulates signaling pathways that control diverse cellular functions including cell morphology, migration, endocytosis and cell cycle progression. (avivasysbio.com)
Kinase1
- We subsequently surveyed the physical region at the 5HL locus for across the barley pan genome variation in the presence of known resistance gene candidates and identified a rich source of high confidence protein kinase and antifungal genes in the QTL region. (bvsalud.org)
Interaction2
Small1
- 11. Rom1p and Rom2p are GDP/GTP exchange proteins (GEPs) for the Rho1p small GTP binding protein in Saccharomyces cerevisiae. (nih.gov)
Migration1
- Mediates CDC42-dependent cell migration. (nih.gov)
Mutations1
- The disease arises from mutations in the gene encoding the WAS protein. (nih.gov)
Gene1
- Description of the protein which includes the UniProt Function and the NCBI Gene Summary. (nih.gov)
Family1
- The proteins encoded by members of the Dbl family share a common domain, presented in this entry, of about 200 residues (designated the Dbl homology or DH domain) that has been shown to encode a GEF activity specific for a number of Rho family members. (embl.de)
Types1
- Its activity is directed by intracellular signals mediated by various types of receptors such as G protein-coupled receptors. (embl.de)
Specifically1
- The product of oncogene Dbl was reported to specifically catalyze the dissociation of GDP from this protein. (avivasysbio.com)
Product1
- Association of the proto-oncogene product dbl with G protein betagamma subunits. (embl.de)
Domains1
- There are 39736 RhoGEF domains in 38458 proteins in SMART's nrdb database. (embl.de)
Class1
- Click on the protein counts, or double click on taxonomic names to display all proteins containing RhoGEF domain in the selected taxonomic class. (embl.de)