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Mediator complex subunit 4 (MED4) is a component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. MED4 is a component of the vitamin D receptor-interacting protein (DRIP) complex which functions as a nuclear receptor coactivator. The DRIP complex is able to activate nuclear receptors in a ligand-dependent manner. MED4 functions as a link to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription apparatus. MED4 is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.

MED7 is a member of the Mediator complex subunit 7 family. The activation of gene transcription is a multistep course which is initiated by factors which identify transcriptional enhancer sites in DNA and collaborate with co-activators to direct transcriptional initiation by the RNA polymerase II apparatus. The gene encode a subunit of the CRSP (cofactor required for SP1 activation) complex, that, together with TFIID, is needed for effective activation by SP1. Additionally, MED7 is also an element of other multisubunit complexes e.g. thyroid hormone receptor-(TR-) associated proteins that cooperate with TR and enables TR function on DNA templates in conjunction with initiation factors and cofactors.

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.

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.

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.

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.

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.

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-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.

RRAS2 (RAS viral (r-ras) oncogene homolog 2) is a member of the Ras like GTPase family that cycle between GTP-bound active and GDP-bound inactive states at the cytoplasmic face of the plasma membrane. RRAS2 is a plasma membrane-associated GTP-binding protein with GTPase activity. RRAS2 is implicated in the pathogenesis of human cancers. Hence, overexpression of active RRAS2 in EpH4 cells induces tumorigenicity through the phosphoinositide 3-kinase, p38 MAPK, and mTOR pathways, as these cells lose their sensitivity to the normal growth inhibitory role of TGF-beta. RRAS2 might transduce growth inhibitory signals across the cell membrane, exerting its effect via an effector shared with the Ras proteins but in an antagonistic manner.
RRAS2 is ubiquitously present in all tissues examined, with the highest levels in the heart, placenta, and skeletal muscle. Moderate levels of RRAS2 are found in the lung and liver and low levels in the brain, kidney, and pancreas.
RRAS2 deficiencies are linked to ovarian cancer.

MAT2A is an important enzyme in cellular metabolism and catalyzes the formation of S-adenosylmethionine (SAMe) from L-methionine and ATP. MAT2A is expressed in extrahepatic tissues. In liver, MAT2A expression associates with growth, dedifferentiation, and cancer. NF-kappa B and AP-1 are necessary for basal MAT2A expression in HepG2 cells and mediate the increase in MAT2A expression in response to TNF-alpha. Up-regulation of MAT2A provides growth improvement and s-adenosylmethionine and methylthioadenosine thus can block mitogenic signaling in colon cancer cells. Lower expression of both MAT2A and MAT2beta and interfere with leptin signaling in liver cancer cells.

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.

Mitochondrial rRNA methyltransferase 1 homolog (MRM1) is a part of the RNA methyltransferase TrmH family. MRM1 methylates the ribose of guanosine G-2270 in the peptidyl transferase center of the mitochondrial large ribosomal RNA (21S).

Oncomodulin is a member of the superfamily of calmodulin proteins, otherwise known as the EF-hand proteins. It is a high-affinity calcium ion-binding protein. Oncomodulin is an oncodevelopmental protein which is found in early embryonic cells in the placenta and also in tumors.

KISS1 is a metastasis suppressor protein that suppresses metastases of melanomas and breast carcinomas without affecting tumorigenicity.KISS1 functions to inhibit chemotaxis and invasion, attenuating metastasis in malignant melanomas. KISS1 is involved in the regulation of cell-matrix adhesion. KISS1 plays a role in cytoskeletal reorganization. A polymorphism in the terminal exon of KISS1 mRNA results in two protein isoforms. Expression of KiSS1 is localized to specific regions of the hypothalamus in numerous species and is regulated by gonadal steroids and across the estrous cycle..KISS1 generates a c-terminally amidated peptide, metastin which functions as the endogenous ligand of the g-protein coupled receptor gpr54. Activation of the receptor inhibits cell proliferation and cell migration, key characteristics of tumor metastasis.

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.

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.

B-Raf Proto-Oncogene, also known as BRAF is a member of the raf/mil family of serine/threonine protein kinases. BRAF participates in regulating the MAP kinase/ERKs signaling pathway, which eventually have an effect on cell division, differentiation, and secretion. Mutations in BRAF have been associated with cardiofaciocutaneous syndrome, which is a disease characterized by heart defects, mental retardation and a distinctive facial appearance. In addition, mutations in BRAF have also been associated with different cancers, including non-Hodgkin lymphoma, colorectal cancer, malignant melanoma, thyroid carcinoma, non-small cell lung carcinoma, as well as adenocarcinoma of lung.

HRAS is part of the Ras oncogene family, whose members are related to the transforming genes of mammalian sarcoma retroviruses. The products encoded by these genes participate in signal transduction pathways. These proteins can bind GTP and GDP, and they have intrinsic GTPase activity. HRAS go trough a continuous cycle of de- and re-palmitoylation, which mediates its rapid exchange between the plasma membrane and the Golgi apparatus. Mutations in HRAS result in Costello syndrome, a disease characterized by increased growth at the prenatal stage, growth deficiency at the postnatal stage, predisposition to tumor formation, mental retardation, skin and musculoskeletal abnormalities, distinctive facial appearance and cardiovascular abnormalities. Defects in this HRAS gene are implicated in a range of cancers, including bladder cancer, follicular thyroid cancer, and oral squamous cell carcinoma.

T-cell leukemia/lymphoma 1B, also known as TCL1B is a member of the TCL1 family. TCL1B is expressed in a variety of tissues as well as the placenta and testis. Moreover, TCL1B enhances the phosphorylation and activation of AKT1 and AKT2.

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.

NME4 is a member of the NDK family. NME4 are ubiquitous enzymes which catalyze transfer of gamma-phosphates, using a phosphohistidine intermediate, between nucleoside and dioxynucleoside tri- and diphosphates. The enzymes are products of the nm23 gene family that include NME4. NME4 has a key part in the synthesis of nucleoside triphosphates other than ATP.

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.