Member RAS Oncogene Family

RHOV belongs to the Rho family and to the small GTPase superfamily. RHOV is a 236 aa protein which regulates the actin cytoskeleton by activating the JNK pathway. RHOV is expressed in placenta, pancreas and fetal brain and operates as a lipid anchor at the cytoplasmic side of the cell membrane.

RHOQ (rho-related GTP-binding protein RhoQ) is a small signaling G protein which cycles between an active GTP-bound and an inactive GDP-bound state. In the active state it binds to a diversity of effector proteins to regulate cellular responses. Ras-like protein belongs to the Rac subfamily of the Rho family of GTPases. RHOQ is involved in epithelial cell polarization processes. In addition, RHOQ plays a role in CFTR trafficking to the plasma membrane. RHOQ causes the formation of thin, actin-rich surface projections called filopodia.

RHOG belongs to the Rac subfamily of the Rho family of small G proteins. RHOG is a small monomeric GTP-binding protein (G protein), and is a key element of several intracellular signalling pathways. RHOG is needed for the formation of membrane ruffles during macropinocytosis. RHOG takes part in cell migration and is essential for the formation of cup-like structures during trans-endothelial migration of leukocytes. Similar to various small G proteins RHOG has a role in several cellular signalling mechanisms such as cell motility, gene transcription, endocytosis, neurite outgrowth, protection from anoikis and regulation of the neutrophil NADPH oxidase.

Rho-related GTP-binding protein (RhoD) is a member of the small GTPase superfamily. The small GTPase Rho D promotes the rearrangement of the actin cytoskeleton and cell surface and also regulates endosome motility and distribution.

RHOC is a small signaling G protein/GTPase which is part of the Rac subfamily of the family Rho family of GTPases. RHOC rotats between inactive GDP-bound and active GTP-bound states and has a role as a molecular switch in signal transduction cascades. RHOC promotes reorganization of the actin cytoskeleton and regulates cell shape, attachment, and motility.

Rho-related GTP-binding protein RhoB (RhoB) belongs to the Rho GTP-binding protein family. RhoB facilitates apoptosis in neoplastically transformed cells after DNA damage. RhoB has a negative role in tumorigenesis since deletion causes tumor formation.

RhoA is a member of the small GTPase superfamily, Rho family, whose members are involved in the regulation and timing of cell division. RHOA is a small GTPase protein which acts to regulate the actin cytoskeleton in the formation of stress fibers and also upon 2 known effector proteins: ROCK1 (Rho-associated, coiled-coil containing protein kinase 1) and DIAPH1 (diaphanous homolog 1 (Drosophila).

Ras-related protein Rap-2b (RAP2B) is a part of RAS-related genes family. RAP2B has a threonine residue at aa 61Unlike normal ras proteins which have a nontransforming glutamine residue at that position. The threonine residue makes the intrinsic GTPase activity for Rap2B lower, by this means allows RAP2B to exist in the activated state for a longer period of time than normal ras proteins. RAP2B is a platelet protein which is activated by thrombin and involved in platelet activation. RAP2B may be a candidate oncogene which takes part in carcinogenesis through activation of NF-kappaB pathway.

RAP2A belongs to the RAS oncogene family and a Ras-like small G protein. The RAP2A protein shares 60% identity with Rap1A and exhibits a carboxy-terminal CAAX motif and 2 upstream cysteines similar to those of the H-Ras, K-Ras and N-Ras proteins. In contrast with Rap1A and Rap1B, overexpression of RAP2A doesn’t obstruct the Ras signaling pathway.

RAP1B is a member of a superfamily of RAS-like small GTP-binding proteins which takes part in cell signaling. RAP1B owns an intrinsic GTPase activity and is universally expressed in mammalian tissues. The alleged effector domain of Ras proteins, whose integrity is required for cell transformation as well as interaction with the putative effector protein GAP, is conserved in both Rap 1 proteins.

RAP1A is part of the family of RAS-related proteins which possess 50% amino acid identity with the classical RAS proteins and have various structural characteristics in common. RAP proteins differ from RAS proteins in their 61st amino acid, glutamine in RAS is replaced by threonine in RAP proteins. RAP1A induces morphological reversion of a cell line transformed by a Ras oncogene and counteracts the mitogenic function of Ras, since it can interact with Ras GAPs and RAF in a competitive manner.

RAN is a GTP-binding protein that participates in nucleocytoplasmic transport. RAN is necessary for the import of protein into the nucleus and also for RNA export. RAN takes part in chromatin condensation and control of cell cycle. The RAN complex with BIRC5 participates in mitotic spindle formation by being as a physical scaffold to assist the delivery of the RAN effector molecule TPX2 to microtubules. RUN increases AR-mediated transactivation.

RAB, Member RAS Oncogene Family-Like 5 (RABL5) belongs to the Ras superfamily of small GTP-binding proteins. The Ras-related superfamily of guanine nucleotide binding proteins includes the R-Ras, Rap, Ral/Rec and Rho/Rab subfamilies. Rab proteins have an essential role in endocytosis or in biosynthetic protein transport. The transporting process of newly synthesized proteins from the endoplasmic reticulum to various stacks of the Golgi complex and to secretory vesicles includes the movement of carrier vesicles and requires Rab protein function.

RAB8, Member RAS Oncogene Family (RAB8B), is a low molecular mass monomeric GTPases which localize on the cytoplasmic surfaces of distinct membrane-bound organelles. RAB8 takes part in polarized vesicular trafficking and neurotransmitter release and also in cell junction dynamics in Sertoli cells. RAB proteins function in intracellular vesicle transport by aiding in the docking or fusion of vesicles with their target membranes.

RAB7A belongs to the Ras superfamily of small Rab GTPases. RAB7A connects with the RIPL effector protein to regulator membrane trafficking from early to late endosome and to lysosomes. RAB7A can also regulate growth receptor endocytic trafficking, degradation, maturation of phagosome and autophagic vacuoles.

Ras-related protein Rab-6B (RAB6B) is a member of the Rab6 family of the small GTPase superfamily. The Rab6 subfamily consists of 3 different isoforms: Rab6A, Rab6A' and Rab6B. Both Rab6A and Rab6A' are ubiquitously expressed while Rab6B is mainly expressed in brain. Rab6 is a main regulator in the retrograde transfer from endosomes via the Golgi to the ER and may act in retrograde tansport in neuronal cells.

RAB6A is a member of the small GTPase superfamily. RAB6A may be involved in protein transport. RAB6A is a regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER) and has a low GTPase activity.

RAB5C is a part of the Ras-related protein family. Members of the Rab protein family are small GTPases of the Ras superfamily guarantee reliability in the process of docking and fusion of vesicles with their right acceptor compartment.

Ras-related protein Rab-5B (RAB5B) belongs to the Rab family of small (monomeric) G proteins. RAB5B is involved in endocytosis and recycling of cell surface molecules. RAB5B interacts with RIN2 and RIN3, which regulate its function, possibly by acting as GEFs. Knockdown of RAB5B abolished group I metabotropic glutamate receptor (mGluR)-mediated neuroprotection.

RAB5A is a member of RAS oncogene family. The small GTPase, RAB5A is a crucial regulatory component of the endocytic pathway. Activation of RAB5A is mediated by GDP-GTP exchange factors (GEFs) that generate the Rab5-GTP complex). RAB5A is required for the fusion of plasma membranes and early endosomes.

RAB4A is a member of the small GTPase superfamily. RAB4A interacts with STX4, RAB11FIP1, RABEP1, CD2AP and KIF3B. In addition, Rab4 is involved in the translocation of glucose transporter (Glu4) in adipocytes. Rab4 overexpression causes a redistribution of receptors on plasma membrane versus endocytic compartments.

RAB3A Interacting Protein Like 1 (RAB3IL1) is a 382 amino acid protein which is a member of the SEC2 family. RAB3IL1 is a guanine nucleotide exchange factor (GEF) for Rab3A. RAB3IL1 competes for interaction with Rab3A and IHPK1 via its coiled coil domain, which doesn’t involve IHPK1 kinase activity.

Ras-related protein Rab-3D (RAB3D) belongs to the Ras superfamily of small Rab GTPases. Rab proteins play a vital role for, either in endocytosis or in biosynthetic protein transport. Rab3D mRNA is primarily expressed in white adipose tissue and, coincident with GLUT4, increases upon differentiation of 3T3-L1 fibroblasts. Rab3D exhibits close structural similarities with Rab 3A, an isoform which is functionally associated with regulated exocytosis in various cell types.

RAB3B which belongs to the RAS oncogene family is an extremely homologous monomeric GTPase that takes part in endocytosis and biosynthetic protein transport. The transport of recently synthesized proteins from the endoplasmic reticulum to several stacks of the Golgi complex and to secretory vesicles includes in every phase the movement of carrier vesicles.

Rab3A is a member of the small GTPase superfamily, Rab family. Rab3A is a small, Ras-like GTPase expressed in neuroendocrine cells, in which Rab3A is linked with secretory vesicle membranes and regulates exocytosis. Rab3A protein may have a role in neurotransmitter release by regulating membrane flow in the nerve terminal.

RAB39B, Member RAS Oncogene Family (RAB39B) belongs to the Rab family of proteins. Rab proteins are small GTPases, which are involved in vesicular trafficking. RAB39B gene mutations are linked with X-linked mental retardation.

Ras-related protein Rab-35 (RAB35) is restricted to the plasma membrane and endocytic compartments and controls a fast endocytic recycling pathway. Inhibition of Rab35 function leads to the accumulation of endocytic markers on numerous cytoplasmic vacuoles in cells that failed cytokinesis, which is consistent with a central requirement for Rab35-regulated recycling during cell division.

RAB34 protein which regulates a fast endocytic recycling pathway is restricted to the plasma membrane and endocytic compartments. RAB34 takes part in protein transport, specifically the redistribution of lysosomes to the peri-Golgi region. In fibroblasts, RAB34 protein was co-localized with actin to the membrane ruffles and membranes of moderately large vesicles close to the ruffles.

RAB32 is a member of the small GTPase superfamily. RAB32 controls ER calcium management and disturbs the specific enhancement of calnexin on the MAM (mitochondria-associated membrane), however avoids affecting the ER distribution of protein-disulfide isomerase and mitofusin-2. Furthermore, RAB32 regulates the targeting of PKA (cAMP-dependent protein kinase) to mitochondrial and ER membranes and by inactivation or overexpression enhances the phosphorylation of Drp1 and Bad. Using a combination of its functions as a regulator of MAM properties and a PKA-anchoring protein, the activity and expression level of RAB32 define the speed of apoptosis onset.

RAB31 Member RAS Oncogene Family (RAB31) is a 194 amino lipid-anchored protein which localizes to the cytoplasmic side of the cell membrane and is a member of the Ras related GTPase superfamily. RAB31 is expressed at high levels in the lung, brain and heart. RAB31 functions in a similar mode to other Rab proteins, namely playing a part in protein transport. Small GTP-binding proteins of the RAB family, for example RAB31, play critical roles in vesicle and granule targeting. RAB31 gas the highest expression in the placenta and brain with lower levels in the heart and lung. However, RAB31 is not detected in liver, skeletal muscle, kidney or pancreas.

Rab2B is a member of the small GTPase superfamily, whose members are nontransforming monomeric GTP-binding proteins of the Ras superfamily and contain 4 highly conserved regions involved in GTP binding and hydrolysis. Rab proteins are prenylated, membrane-bound proteins engaged in vesicular fusion and trafficking.

Ras-related protein Rab-2A (RAB2A)is a member of the small GTPase superfamily. RAB protein family members are nontransforming monomeric GTP-binding proteins of the Ras superfamily, which contain four highly conserved regions involved in GTP binding and hydrolysis. In addition, RAB proteins are a fundamental part of endocytic pathways. RAB2A and RAB2B are essential for protein transport from the ER to the Golgi; RAB2A is lipid-anchored to the ER-Golgi intermediate compartment membrane whereas RAB2B is lipid anchored to the cytoplasmic side of the cell membrane. RAB2A also interacts with GOLGA2.

RAB27B is a member of the RAB family and is an important regulator of vesicular transport. RAB27B is expressed in pituitary tissue, but is more extensively expressed in brain and spleen. RAB27B may be functionally redundant to Rab27a, as it can salvage Rab27a mutants.

RAB27A is part of the small GTPase superfamily, Rab family. RAB27A is membrane-bound and participates in protein transport and small GTPase mediated signal transduction. Mutations in this RAB27A are associated with Griscelli syndrome type 2. RAB27A is involved in cytotoxic granule exocytosis in lymphocytes.RAB27A is necessary for both granule maturation and granule docking and priming at the immunologic synapse.

RAB24 is a member of the small GTPase superfamily which regulates intracellular protein transferring, nonetheless the specific role of RAB24 has not yet been revealed. RAB24 is distributed in the endoplasmic reticulum/cis-Golgi region and on late endosomal structures which suggests connection to autophagy-related courses. RAB24 demonstrates uncommon characteristics such as low intrinsic GTPase activity, and is incompetently prenylated when compared with other Rab proteins indicates that RAB24 has a distinctive part in the degradation of misfolded cellular proteins or trafficking of proteins to the nuclear envelope.

RAB23 belongs to the Rab family of proteins and is restricted to the cytoplasmic side of the cell membrane. RAB23 takes part in intracellular protein transportation and signal transduction facilitated by small GTPases. RAB23 is a vital negative regulator of the Sonic hedgehog signaling pathway. Alterations in the gene encoding RAB23 are the origin for Carpenter syndrome a disorder which can cause obesity, cardiac defects, polysyndactyly and craniosynostosis.

Ras-related protein Rab-22A (RAB22A) belongs to the RAB family of small GTPases. The GTP-bound form of the RAB22A interacts with early-endosomal antigen 1, and may be involved in the transferring of and interaction between endosomal compartments.

Ras-related protein Rab-21 (RAB21) belongs to the Ras superfamily of small GTP-binding proteins. Rab21 is an integrin-associated protein and a positive regulator of integrin traffic. Rab21 associates with the cytoplasmic domains of alpha-integrin chains and their expression influences the endo/exocytic traffic of integrins. This function of Rab21 depends on its GTP/GDP cycle and right membrane targeting.

RAB1B belongs to the RAB protein family, these proteins are low molecular mass monomeric GTPases localized on the cytoplasmic surfaces of distinct membrane bound organelles. RAB1B protein functions in the early secretory pathway and is essential for vesicle transport between the endoplasmic reticulum (ER) and Golgi.

RAB1A belongs to the ras-related superfamily. Rab proteins have a central part in either in endocytosis or in biosynthetic protein transport. Rab1a protein controls vesicle traffic from the endoplasmic reticulum to the Golgi apparatus.

RAB18 belongs to a family of Ras-related small GTPase which is lipid-anchored to the cytoplasmic side of the cell membrane. RAB18 takes part in apical recycling, endocytosis and protein transport between early endosomes and the plasma membrane.

RAB17 is a member of the small GTPase superfamily which are found in several intracellular compartments and have a significant regulatory part in membrane trafficking. RAB17 regulates traffic through the apical recycling endosome, which indicates that RAB17 has a role in polarized arrangement in epithelial cells.

RAB14 belongs to the RAB protein family, low molecular mass monomeric GTPases which is found on the cytoplasmic surfaces of distinct membrane bound organelles. RAB14 has a role in vesicular trafficking and neurotransmitter release throughout the body and is expressed at high levels in brain, lung, kidney, spleen and thymus. In addition, RAB14 takes part in the biosynthetic/recycling pathway between the Golgi and endosomal compartments.

RAB13 is a member of the small GTPase superfamily which are nontransforming monomeric GTP-binding proteins that hold 4 extremely conserved regions that take part in GTP binding and hydrolysis. In addition, RAB proteins have a vital role in the endocytic pathways. The GTPase Rab13 regulates the assembly of functional epithelial tight junctions (TJs) and is expressed in every phase of preimplantation development.

RAB11A is part of the small GTPase superfamily, Rab family. RAB11A is related with both constitutive and regulated secretory pathways, and takes part in protein transport. RAB11A is a well-known marker for protein trafficking, sorting, and recycling in the endosomal pathway. RAB11A is a main regulator of membrane delivery during cytokinesis.

RAB10, Member RAS Oncogene Family (RAB10) belongs to the Ras superfamily of small GTP-binding proteins. RAB10 is a key regulator of endocytic recycling, particularly in the basolateral recycling pathways of polarized epithelial cells. It is required for the recruitment of CNT-1 to endosomal membranes in the intestinal epithelium.

DIRAS1 is a member of a distinct branch of the functionally diverse Ras superfamily of monomeric GTPases. DIRAS1 demonstrates low GTPase activity and exists mainly in the GTP-bound form. Ras proteins operate as binary molecular switches that control intracellular signaling networks. Ras-regulated signal pathways regulate such processes as actin cytoskeletal integrity, proliferation, differentiation, cell adhesion, apoptosis, and cell migration. Ras and ras-related proteins are frequently deregulated in cancers, leading to increased invasion and metastasis, and decreased apoptosis.