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RAD51D is a member of the RAD51 protein family whose members are extremely similar to bacterial RecA and Saccharomyces cerevisiae Rad51. RAD51 protein family members take part in the homologous recombination and repair of DNA. RAD51D forms a complex with several other members of the RAD51 family which catalyzes homologous pairing between single- and double-stranded DNA, and participates in the early stage of recombinational repair of DNA.

RAET1E is a member of the MHC class I family. MHC class I family contains main histocompatibility complex (MHC) class I-related genes positioned in a cluster on chromosome 6q24.2-q25.3. RAET1E and RAET1G protein are different from other RAET1 proteins since they have type I membrane-spanning sequences at their C termini instead glycosylphosphatidylinositol anchor sequences.RAET1E acts as a ligand for NKG2D receptor, expressed on the surface of numerous types of immune cells, involves in innate adaptive immune reactions.RAET1E delivers signals to NK cells and advances tumor immune surveillance by inducing the growth of anti-tumor cytotoxic lymphocyte.

RAET1E is a member of the MHC class I family. MHC class I family contains main histocompatibility complex (MHC) class I-related genes positioned in a cluster on chromosome 6q24.2-q25.3. RAET1E and RAET1G protein are different from other RAET1 proteins since they have type I membrane-spanning sequences at their C termini instead glycosylphosphatidylinositol anchor sequences.RAET1E acts as a ligand for NKG2D receptor, expressed on the surface of numerous types of immune cells, involves in innate adaptive immune reactions.RAET1E delivers signals to NK cells and advances tumor immune surveillance by inducing the growth of anti-tumor cytotoxic lymphocyte.

RAET1E is a member of the MHC class I family. MHC class I family contains main histocompatibility complex (MHC) class I-related genes positioned in a cluster on chromosome 6q24.2-q25.3. RAET1E and RAET1G protein are different from other RAET1 proteins since they have type I membrane-spanning sequences at their C termini instead glycosylphosphatidylinositol anchor sequences.RAET1E acts as a ligand for NKG2D receptor, expressed on the surface of numerous types of immune cells, involves in innate adaptive immune reactions.RAET1E delivers signals to NK cells and advances tumor immune surveillance by inducing the growth of anti-tumor cytotoxic lymphocyte.

RAET1E is a member of the MHC class I family. MHC class I family contains main histocompatibility complex (MHC) class I-related genes positioned in a cluster on chromosome 6q24.2-q25.3. RAET1E and RAET1G protein are different from other RAET1 proteins since they have type I membrane-spanning sequences at their C termini instead glycosylphosphatidylinositol anchor sequences.RAET1E acts as a ligand for NKG2D receptor, expressed on the surface of numerous types of immune cells, involves in innate adaptive immune reactions.RAET1E delivers signals to NK cells and advances tumor immune surveillance by inducing the growth of anti-tumor cytotoxic lymphocyte.

RAET1L plays a role as a stress-induced ligand for NKG2D receptor. Retinoic Acid Early Transcript 1L (RAET1L) is linked to the cell membrane by the GPI anchor. HCMV infection triggers RAET1L’sexpression but HCMV alters its function. HCMV-encoded UL16 glycoprotein retains RAET1L/ULBP6 inside the cells, preventing it from reaching the cell surface and being exposed to cells of the immune system. RAET1L has a more restricted expression profile in cell lines and primary human tissues than other NKG2D ligands.

Advanced Glycosylation End Product-Specific Receptor or RAGE is an immunoglobulin, part of the immunoglobulin transmembrane proteins family. RAGE moderates interactions between advanced glycosylation end products, also known as AGE. These signaling has a crucial part in the regulation of TNFalpha,oxidative stress, endothelial dysfunction in type 2 diabetesproduction and expression. RAGE helps the translocation of ABPP (amyloid-beta peptide) through the membrane of cells to the intracellular area in the cortical neurons.

Ras-related protein Ral-A (RALA) is a member of the small GTPase superfamily, Ras family of proteins. RALA mediates a distinct downstream signaling pathway from Ras which facilitates cellular transformation. Furthermore, RALA is thought to be involved in various signaling cascades, including regulation of the cytoskeleton, vesicle trafficking, and endocytosis.

Ras-related protein Ral-A (RALA) is a member of the small GTPase superfamily, Ras family of proteins. RALA mediates a distinct downstream signaling pathway from Ras which facilitates cellular transformation. Furthermore, RALA is thought to be involved in various signaling cascades, including regulation of the cytoskeleton, vesicle trafficking, and endocytosis.

Ras-related protein Ral-A (RALA) is a member of the small GTPase superfamily, Ras family of proteins. RALA mediates a distinct downstream signaling pathway from Ras which facilitates cellular transformation. Furthermore, RALA is thought to be involved in various signaling cascades, including regulation of the cytoskeleton, vesicle trafficking, and endocytosis.

Ras-related protein Ral-B (RALB) is a member of a subfamily of Ras-related GTPases. RALB is activated by a unique nucleotide exchange factor, Ral GDS, and deactivated by a distinct GTPase-activating protein. RALB has a role in the late stages of cytokinesis and is required for the abscission of the bridge joining the sister cells emerging from mitosis. In addition, RALB is required for suppression of apoptosis.

RALY belongs to the heterogeneous nuclear ribonucleoprotein (hnRNP) gene family. RALY takes part in pre-mRNA splicing and also in embryonic development. Moreover, alternate splicing results in multiple transcript variants have been found for RALY.

RAMP belongs to the type I transmembrane family of proteins called RAMP (receptor/calcitonin activity modifying proteins) which include an extracellular N terminus and a cytoplasmic C terminus. RAMPs are essential for CRLR transport to the plasma membrane. CRLR (calcitonin-receptor-like receptor) has seven transmembrane domains. Depending on which members of the RAMP family are expressed CRLR receptor functions as either an adrenomedullin receptor or a calcitonin-gene-related peptide (CGRP) receptor. In the presence of RAMP1, CRLR functions as a CGRP receptor. The RAMP1 protein takes part in the terminal glycosylation, maturation, and presentation of the CGRP receptor to the cell surface.

Receptor activity modifying protein 3 (RAMP3) belongs to the RAMP family of single-transmembrane-domain proteins, named receptor (calcitonin) activity modifying proteins (RAMPs). RAMP3 is needed to transport calcitonin-receptor-like receptor (CRLR) to the plasma membrane. CRLR acts as either a calcitonin gene-related peptide (CGRP) receptor or an adrenomedullin receptor, depending on which members of the RAMP family are expressed. The existence of RAMP3 effects CRLR to function as an adrenomedullin receptor.

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.

RANBP1 is a member of a family of proteins which bind Ran GTPase. Ran GTPase is vital for cell cycle control, mRNA processing, nuclear transport, mitotic spindle assembly, and postmitotic nuclear re-assembly and nuclear architecture maintenance. RANBP1 does not stimulate GTPase activity of RAN however RANBP1 does distinctly raise GTP hydrolysis by the RanGTPase-activating protein (RanGAP1). Additionally, RANBP1 operates as a negative regulator of RCC1 by inhibiting RCC1-stimulated guanine nucleotide release from RAN.

RAN Binding Protein 3, also known as RANBP3, is found in the nucleus and cytoplasm. RANBP3 which owns RanBD1 domain participates in nuclear export as part of a heteromeric complex. RANBP3 is also negatively regulates TGF-beta signaling by interacting with the R-SMAD proteins, SMAD2 and SMAD3.

RAN Binding Protein 3, also known as RANBP3, is found in the nucleus and cytoplasm. RANBP3 which owns RanBD1 domain participates in nuclear export as part of a heteromeric complex. RANBP3 is also negatively regulates TGF-beta signaling by interacting with the R-SMAD proteins, SMAD2 and SMAD3.

RANGRF is a protein which acts as a guanine nucleotide release factor in mouse and regulates the expression and function of the Nav1.5 cardiac sodium channel in human. RANGRF also controls the intracellular trafficking of RAN. In cardiac cells, the RANGRF appears to regulate the cell surface localization of SCN5A.

sRANK Receptor is a part of of the TNF superfamily of ligands and receptors which participates in the regulation of specific immunity and bone turnover. sRANK Receptor was originally acknowledged as a dendritic-cell-membrane protein, which by interacting with RANKL augments the capacity of dendritic cells to stimulate naive T cell proliferation and to endorse the survival of RANK and T cells. The full length human RANK cDNA encodes a type I transmembrane protein of 616 amino acids with a predicted 183 amino acid extracellular domain and a 383 amino acid cytoplasmic domain. sRANK Receptor is also expressed in a various tissues including skeletal muscle, thymus, liver, colon, small intestine and adrenal gland.

RANK, is part of the tumor necrosis factor receptor family. RANK is widely expressed with uppermost levels in the skeletal muscle, thymus, liver, colon, small intestine, adrenal gland as well as dendritic cells. Furthermore, in activated human peripheral blood T lymphocytes, RANK expression is induced by IL4 and TGF-b.

Tumor necrosis factor receptor superfamily member 11A or TNFRSF11A or RANK, is a protein, part of the tumor necrosis factor receptor (TNFR) group of proteins. RANK acts as the receptor of RANK-Ligand and regulates osteoclast activation & differentiation. RANK protein has been linked to activation of NF-kappa B & c-jun N-terminal kinase, enhancement of T cell growth, bone remodeling and repair, dendritic cell function, lymph node development, immune cell function, mammary gland development & thermal regulation.

Regulated upon Activation, Normal T-cell Expressed, and Secreted or RANTES is an 8 kDa protein classified as a chemotactic cytokine or chemokine. Rantes has recently been renamed CCL5. RANTES is chemotactic for T cells, eosinophils and basophils and plays an active role in recruiting leukocytes into inflammatory sites. With the help of particular cytokines (i.e. IL-2 and IFN-g) that are released by T cells, RANTES also induces the proliferation and activation of certain natural killer (NK) cells to form CHAK (CC-Chemokine-activated killer) cells. Rantes is also an HIV-suppressive factor released from CD8+ T cells. The Rantes chemokine has been localized to chromosome 17 in humans.

Regulated upon Activation, Normal T-cell Expressed, and Secreted or RANTES is an 8 kDa protein classified as a chemotactic cytokine or chemokine. It has recently been renamed CCL5. RANTES is chemotactic for T cells, eosinophils and basophils and plays an active role in recruiting leukocytes into inflammatory sites. With the help of particular cytokines (i.e. IL-2 and IFN-?) that are released by T cells, RANTES also induces the proliferation and activation of certain natural killer (NK) cells to form CHAK (CC-Chemokine-activated killer) cells. It is also a HIV-suppressive factor released from CD8+ T cells. This chemokine has been localized to chromosome 17 in humans.

Regulated upon Activation, Normal T-cell Expressed, and Secreted or RANTES is an 8 kDa protein classified as a chemotactic cytokine or chemokine. It has recently been renamed CCL5. RANTES is chemotactic for T cells, eosinophils and basophils and plays an active role in recruiting leukocytes into inflammatory sites. With the help of particular cytokines (i.e. IL-2 and IFN-?) that are released by T cells, RANTES also induces the proliferation and activation of certain natural killer (NK) cells to form CHAK (CC-Chemokine-activated killer) cells. It is also a HIV-suppressive factor released from CD8+ T cells. This chemokine has been localized to chromosome 17 in humans.

Regulated upon Activation, Normal T-cell Expressed, and Secreted or RANTES is an 8 kDa protein classified as a chemotactic cytokine or chemokine. It has recently been renamed CCL5. RANTES is chemotactic for T cells, eosinophils and basophils and plays an active role in recruiting leukocytes into inflammatory sites. With the help of particular cytokines (i.e. IL-2 and IFN-?) that are released by T cells, RANTES also induces the proliferation and activation of certain natural killer (NK) cells to form CHAK (CC-Chemokine-activated killer) cells. It is also a HIV-suppressive factor released from CD8+ T cells. This chemokine has been localized to chromosome 17 in humans.

Regulated upon Activation, Normal T-cell Expressed, and Secreted or RANTES is an 8 kDa protein classified as a chemotactic cytokine or chemokine. It has recently been renamed CCL5. RANTES is chemotactic for T cells, eosinophils and basophils and plays an active role in recruiting leukocytes into inflammatory sites. With the help of particular cytokines (i.e. IL-2 and IFN-?) that are released by T cells, RANTES also induces the proliferation and activation of certain natural killer (NK) cells to form CHAK (CC-Chemokine-activated killer) cells. It is also a HIV-suppressive factor released from CD8+ T cells. This chemokine has been localized to chromosome 17 in humans.

Receptor-associated Protein (aka RAP) averts the GCM-mediated enhancement of axon growth- ApoE-containing lipoproteins which are known to bind to receptors of the LDLr superfamily. In the presence of RAP, GCM doesn’t increase the axon extension rate in relation to base medium. Furthermore, the addition of RAP to the base medium doesn’t change the rate of axon extension. This implies that the growth stimulatory effect of apoE-containing lipoproteins secreted by glial cells is mediated by the LDLr family receptors. RAP annuls the growth stimulatory effect of GCM.

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.

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.

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.

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.

43 kDa receptor-associated protein of the synapse (RAPSN), is expressed in the postsynaptic membrane of skeletal muscle. RAPSN is essential for the clustering of nicotinic acetylcholine receptors (nAChR). In addition RAPSN self-associates via at least two of its seven tetra-tricopeptide repeats (TPRs). RAPSN interacts with the large intracellular domain of the nAChR a subunit all the way through the hydrophobic surface of the coiled-coil domain. RAPSN modifies trafficking of AChR within the cell. Overexpression inhibits agrin-induced AChR clustering pathway. RAPSN also plays a role in postsynaptic congenital myasthenic syndromes.

Retinoic acid receptor alpha (RAR) belongs to the large family of ligand responsive gene regulatory proteins that includes receptors for steroid and thyroid hormones. These proteins contain two highly conserved domains that are involved in determining their DNA and ligand-binding activities. There are three isotypes of RAR proteins: alpha, beta, and gamma. The RAR proteins are encoded by distinct genetic loci and possess distinct transcriptional properties. Typically, RAR-alpha represses target gene transcription in the absence of hormone, whereas RAR-beta and gamma fail to repress under these conditions. RARA is a receptor for retinoic acid that has profound effects on vertebrate development. Retinoic acid is a morphogen and is a powerful teratogen. RARA controls cell function by directly regulating gene expression.
Chromosomal aberrations involving RARA cause acute promyelocytic leukemia (APL).

Retinoic Acid Receptor Responder 1 (RARRES1) is a part of the TIGs family. TIGs operate like tumor suppressor genes in human cancers and are greatly expressed in skin, hair follicles and endothelial cells plus in pancreas, spleen and intestine. TIGs are growth regulators which mediate the growth suppressive effects of retinoids.

RARRES2 is a secreted chemotactic protein that initiates chemotaxis through the ChemR23 G protein-coupled seven-transmembrane domain ligand. RARRES2 acts as an adipokine, and is truncated on both termini from the proprotein. RARRES2 is structurally related to the cathelicidin precursors, cystatin C and kininogens. RARRES2 promotes calcium mobilization and chemotaxis of immature dendritic cells and macrophages. RARRES2 is secreted as a precursor of little biological activity, which requires proteolytic cleavage of its COOH-terminal domain to be exchangeed into a potent and highly specific agonist of ChemR23. RARRES2 signals via its receptor, ChemR23 (CMKLR1), as a positive regulator of adipocyte differentiation and metabolic function. The Chemerin receptor acts as a coreceptor for SIV and some primary HIV-1 strains.

RARRES2 is a secreted chemotactic protein that initiates chemotaxis through the ChemR23 G protein-coupled seven-transmembrane domain ligand. RARRES2 is upregulated by the synthetic retinoid tazarotene and found in many tissues. RARRES2 acts as an adipokine and is truncated on both termini from the proprotein. RARRES2 is structurally related to the cathelicidin precursors, cystatin C and kininogens. RARRES2 promotes calcium mobilization and chemotaxis of immature dendritic cells and macrophages. RARRES2 is secreted as a precursor of little biological activity, which requires proteolytic cleavage of its COOH-terminal domain to be exchangeed into a potent and highly specific agonist of ChemR23.

RARRES2 is a secreted chemotactic protein that initiates chemotaxis through the ChemR23 G protein-coupled seven-transmembrane domain ligand. RARRES2 is upregulated by the synthetic retinoid tazarotene and found in a vast variety of tissues. RARRES2 acts as an adipokine, and is truncated on both termini from the proprotein. RARRES2 is structurally related to the cathelicidin precursors, cystatin C and kininogens. RARRES2 promotes calcium mobilization and chemotaxis of immature dendritic cells and macrophages. RARRES2 is secreted as a precursor of little biological activity, which requires proteolytic cleavage of its COOH-terminal domain to be exchangeed into a potent and highly specific agonist of ChemR23. RARRES2 signals via its receptor, ChemR23 (CMKLR1), as a positive regulator of adipocyte differentiation and metabolic function. The Chemerin receptor acts as a coreceptor for SIV and some primary HIV-1 strains. The Chemerin receptor has another ligand, called tazarotene-induced gene.

RARRES2 is a secreted chemotactic protein that initiates chemotaxis through the ChemR23 G protein-coupled seven-transmembrane domain ligand. RARRES2 is upregulated by the synthetic retinoid tazarotene and found in a vast variety of tissues. RARRES2 acts as an adipokine, and is truncated on both termini from the proprotein. RARRES2 is structurally related to the cathelicidin precursors, cystatin C and kininogens. RARRES2 promotes calcium mobilization and chemotaxis of immature dendritic cells and macrophages. RARRES2 is secreted as a precursor of little biological activity, which requires proteolytic cleavage of its COOH-terminal domain to be exchangeed into a potent and highly specific agonist of ChemR23. RARRES2 signals via its receptor, ChemR23 (CMKLR1), as a positive regulator of adipocyte differentiation and metabolic function. The Chemerin receptor acts as a coreceptor for SIV and some primary HIV-1 strains. The Chemerin receptor has another ligand, called tazarotene-induced gene.

RASD Family Member 2 (RASD2) which binds to GTP and owns a GTPase activity is a part of the Ras super family of small GTPases. RASD2 regulates signaling pathways involving G-proteins-coupled receptor and heterotrimeric proteins. RASD2 encodes a Ras-related protein that enriched in striatum.

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

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.

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.

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.

Retinoblastoma (RB) is an embryonic malignant neoplasm of retinal origin. It almost always presents in early childhood and is often bilateral. Spontaneous regression ('cure') occurs in some cases. Retinoblastoma acts as a regulator of other genes and forms a complex with adenovirus e1a and with sv40 large t antigen. Retinoblastoma acts as a tumor suppressor and modulats functionally certain cellular proteins with which t and e1a compete for pocket binding. Retinoblastoma is potent inhibitor of e2f-mediated trans-activation, recruits and targets histone methyltransferase suv39h1 leading to epigenetic transcriptional repression, inhibits the intrinsic kinase activity of taf1.

Retinoblastoma binding protein 4 (RBBP4) is a ubiquitously expressed nuclear protein which is a member of a highly conserved subfamily of WD-repeat proteins. RBBP4 is present in protein complexes involved in histone acetylation and chromatin assembly. In addition, RBBP4 is part of co-repressor complexes, which is a fundamental component of transcriptional silencing. RBBP4 is observed among several cellular proteins which bind directly to a retinoblastoma protein to regulate cell proliferation. RBBP4 also is a part of the Mi-2 complex which is implicated in chromatin remodeling and transcriptional repression connected with histone deacetylation.

RBBP9, restricts to the nucleus and cytoplasm, is a retinoblastoma binding protein which takes part in the regulation of cell proliferation and differentiation. RBBP9 cooperates with retinoblastoma (Rb) and offers cellular resistance to the growth-inhibitory effects of TGFbeta1, therefore enabling the cellular transformation process.

Ribokinase (RBKS) is a member of the pfkB family of carbohydrate kinases. Ribokinase phosphorylates ribose to form ribose-5-phosphate in the presence of ATP and magnesium as a first step in ribose metabolism.

RNA Binding Motif Protein 11 (RBM11) which contains 1 RNA recognition motif is a part of the RBM family. The RBM gene family encodes proteins with an RNA binding motif which participate in the modulation of apoptosis. RBM11 is expressed in testis, kidney, spleen, brain, spinal cord and mammary gland and can be found as 2 isoforms produced by alternative splicing.

RNA binding motif protein 17 (RBM17) is a splice factor which binds to the single stranded 3'AG at the exon/intron border and promotes its utilization in the 2nd catalytic step. The RBM17 protein is involved in the regulation of alternative splicing and the utilization of cryptic splice sites. RBM17 protein also stimulates the utilization of a cryptic splice site created by the beta-110 mutation in the HBB gene. The ensuing frameshift leads to sickle cell anemia.