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Ras association domain-containing protein 3 (RASSF3) is a ubiquitously expressed protein found in normal and cancerous tissues. RASSF3 is a member of RASSF family whose members contain a highly conserved Ras association domain (Ral GDS/AF-6 or RA) and function as Ras effectors/tumor suppressors. RASSF3 contains an N-terminal RA domain and a coiled-coil SARAH domain and may have 3 isoforms (RASSF3A, RASSF3B and RASSF3C) due to alternative splicing. RASSF3B and RASSF3C are shorter than RASSF3A and do not contain the RA and SARAH domain.

RASSF1A protein is a potential tumor suppressor like the RAS effector proteins. Presence or absence expression of this gene has been related with the pathogenesis of a variety of cancers, which suggests the tumor suppressor function of this RASSF1A gene. The inactivation of RASSF1A was found to be associated with the hypermethylation of its CpG-island promoter region. RASSF1A required for death receptor-dependent apoptosis.

RASSF1A is a protein similar to the RAS effector proteins. Loss or altered expression of the RASSF1A gene has been linked to the pathogenesis of a variety of cancers, which suggests the tumor suppressor function of the RASSF1A gene. The inactivation of the RASSF1A gene was found to be interconnected with the hypermethylation of its CpG-island promoter region. The RASSF1A protein was found to interact with DNA repair protein XPA. RASSF1A was also shown to inhibit the accumulation of cyclin D1, and thus induce cell cycle arrest.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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-Like Family 12, also known as RASL12 belongs to the small GTPase superfamily, and to the Ras family.

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.

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.

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.

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.

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.

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.

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.

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.

NRAS binds GDP/GTP and has intrinsic GTPase activity. NRAS is a membrane protein that shuttles between the Golgi apparatus and the plasma membrane. This transport is regulated through palmitoylation and depalmitoylation by the ZDHHC9-GOLGA7 complex. NRAS is activated to a GTP-bound form by a GTPase activating protein and inactivated to a GDP-bound form by a guanine nucleotide-exchange factor. Defects in this NRAS gene result in juvenile myelomonocytic leukemia.