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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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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-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.

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.

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-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.

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.

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.

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.

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.