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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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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).

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.

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.

RRAS belongs to the Ras family which functions in signal transduction pathways. RRAS interacts with RASSF5, NCK1, Bcl-2, ARAF and RALGDS. RRAS binds GTP and GDP, and it has intrinsic GTPase activity. RRAS regulates the organization of the actin cytoskeleton