What is rhoa

SignaLink: a signaling pathway resource with multi-layered regulatory networks More SignaLink i. Search reactions for this EC number in Rhea. Homo sapiens Human. This is known as the 'taxonomic identifier' or 'taxid'. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first. Human Gene Nomenclature Database More HGNC i.

MIM i. VEuPathDB i. Constitutively active. Decreased substrate adhesion-dependent cell spreading. Decreased stress fibers assembly. Decreased cytoplasmic microtubule organization. DisGeNET i. MalaCards human disease database More MalaCards i. Open Targets More OpenTargets i. PharmGKB i. Pharos i. ChEMBL i. Drug and drug target database More DrugBank i. BioMuta curated single-nucleotide variation and disease association database More BioMuta i.

DMDM i. Microbial infection O-linked Glc threonine; by C. Microbial infection ADP-ribosylasparagine; by botulinum toxin 1 Publication Manual assertion inferred by curator from i Ref. Encyclopedia of Proteome Dynamics More EPD i. MassIVE i. MaxQB i. PaxDb, a database of protein abundance averages across all three domains of life More PaxDb i. PeptideAtlas More PeptideAtlas i. PRIDE i. ProteomicsDB: a multi-organism proteome resource More ProteomicsDB i.

Consortium for Top Down Proteomics More TopDownProteomics i. GlyGen i. MetOSite database of methionine sulfoxide sites More MetOSite i. PhosphoSitePlus i. SwissPalm database of S-palmitoylation events More SwissPalm i. Bgee i. ExpressionAtlas i. Genevisible search portal to normalized and curated expression data from Genevestigator More Genevisible i. Human Protein Atlas More HPA i.

BioGRID i. CORUM i. Database of interacting proteins More DIP i. Protein interaction database and analysis system More IntAct i. Molecular INTeraction database More MINT i.

BindingDB database of measured binding affinities More BindingDB i. RNAct i. BMRB i. The initial residue 14 has been shown to be important for catalytic function as a G14V mutation confers a decrease in GTPase activity to one-tenth that of the wild type GTPases. Residue Lys18 is also important for binding to the triphosphoryl group. The phenolic ring of Tyr interacts with Pro and Ala and Val14 to close off the phosphate binding pocket and also causes Val and Val of switch I to flip outward and form hydrophobic interactions with Tyr and Leu of switch II placing it in a stable conformation.

The switch I and II regions are also sites of regulatory influence as they undergo conformational changes in response to GEF binding, which interferes with the phosphate binding loop and the magnesium binding site to displace the GDP molecule with itself subsequently being displaced as well following GTP binding to the GTPase 2. The inherent GTPase ability of RhoA to hydrolyze GTP is weak, as it serves as a timing mechanism to control the activity of the protein following its activation so that it can transduce the signal through its downstream effectors before hydrolysis changes it into the off conformation 3.

GAP proteins have an arginine finger that induces a orientation change in the GTP molecule bound to RhoA increasing its electrophilicity and therefore the rate of the hydrolysis reaction Gln in this region is an important residue for GTPase activity as it forms a hydrogen bond with the water molecules WAT-3 that will mediate nucleophilic attack on the bound GTP.

Stabilization of switch II occurs through interaction with switch I as mentioned above as well as hydrogen bonding with Lys and Glu later on and the 67 DRL69 segment connecting H1 and H2 with strands B2 and B3 through hydrophobic contact.

This hydrophobic pocket also serves as the binding site for the water molecule WAT-1 that aids in base binding and forms a hydrogen bond with it at Gly and causing rearrangements in Lys, Asn, Cys 5. The water molecule WAT-3 is the only one that is in the right location to perform a nucleophilic attack of the bound GTP molecule that defines the catalytic function of the protein. This nucleophilic attack results in the formation of GDP being bound to the protein with an inorganic phosphoryl group being released.

Sema4D in semaphorin signaling. Sema4D induced cell migration and growth-cone collapse. Semaphorin interactions. Sema4D mediated inhibition of cell attachment and migration. S1P2 pathway. S1P3 pathway. S1P1 pathway. S1P4 pathway. S1P5 pathway. PKA Signaling. Ras Pathway. GPCR Pathway. Pancreatic Adenocarcinoma. Breast Cancer Regulation by Stathmin1. Cytoskeletal Signaling. This gene is overexpressed in Whole Blood x4.

This gene is overexpressed in Peripheral blood mononuclear cells 6. Show more. Nervous system 5 Intestine 4. This gene was present in the common ancestor of animals and fungi.

All consequence types are included: molecular consequences e. Residual Variation Intolerance Score : Ectodermal dysplasia with facial dysmorphism and acral, ocular, and brain anomalies EDFAOB [MIM]: A neuroectodermal syndrome characterized by linear hypopigmentation, alopecia, apparently asymptomatic leukoencephalopathy, and facial, ocular, dental and acral anomalies.

Patients show no intellectual or neurologic impairment. Quality Products:. Q 4 18 ENSP O 4 18 ENSP P 4 18 ENSP MalaCards Medline Plus. RHOA 28 RHOA Rhoa