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GTPase, IMAP Family Member 5 (GIMAP5) is a part of the GTP-binding superfamily and the immuno-associated nucleotide subfamily of nucleotide-binding proteins. GIMAP5 is an antiapoptotic protein which is required for mitochondrial integrity and T-cell survival. Polymorphisms in GIMAP5 are related with systemic lupus erythematosus. Read-through transcription can be found between GIMAP5 and the neighboring upstream GIMAP1 (GTPase, IMAP family member 1) gene. GIMAP5 also contributes to T-cell quiescence.

Gastrokine 3 (GKN3P) is a Pseudogene, which May inhibit gastric epithelial cell proliferation.

LGLAS9 binds galactosides and has high affinity for the Forssman pentasaccharide. LGLAS9 participates in thymocyte-epithelial interactions relevant to the biology of the thymus and Inhibits cell proliferation. LGLAS9 is a ligand for HAVCR2/TIM3. LGLAS9 Induces T-helper type 1 lymphocyte (Th1) death. LGLAS9 performs as an eosinophil chemoattractant LGLAS9 is an S-type lectin which is over-expressed in Hodgkin's disease tissue and takes part in the interaction between the H&RS cells with their surrounding cells.

Legumain, also known as LGMN, is a cysteine endopeptidase which demonstrates strict specificity for hydrolysis of asparaginyl bonds. Furthermore, LGMN can also cleave aspartyl bonds slowly, in particular under acidic conditions. LGMN plays an essential role in the endosomal/lysosomal degradation system as the Legumain deficiency causes the accumulation of pro cathepsins B, H & L, another group of lysosomal cysteine proteases. Furthermore, over expression of LGMN in tumors is important for invasion/metastasis.

Ganglioside GM2 activator (GM2A) is a small glycolipid transport protein which functions as a substrate specific co-factor for the lysosomal enzyme beta-hexosaminidase A. GM2A participates in lipid metabolism. GM2A protein is localized in lysosomes. The GM2A protein forms a large binding pocket for a number of single chain phospholipids and fatty acids. GM2A demonstrates calcium-independent phospholipase activity. GM2A stimulates ganglioside GM2 degradation by presenting GM2 to beta-hexosaminidase A. The Beta-hexosaminidase A, along with GM2A, catalyzes the degradation of the ganglioside GM2, and other molecules containing terminal N-acetyl hexosamines. GM2A gene mutations result in GM2-gangliosidosis type AB or the AB variant of Tay-Sachs disease.

UL16 Binding Protein 3 (ULBP3) is a ligand for the NKG2D receptor in NK cells. ULBPs activate different signaling pathways resulting in the production of cytokines and chemokines. ULBP3 is a ligand for the KLRK1/NKG2D receptor, along with at least ULBP1 and ULBP2. Binding of ULBPs ligands to KLRK1/NKG2D stimulates calcium mobilization and activation of the JAK2, STAT5, ERK and PI3K kinase/Akt signal transduction pathway. ULBP3 has lower affinity for KLRK1/NKG2D compared to ULBP1 and ULBP2 and stimulates weaker signaling responses than does ULBP2 or ULBP1.

Though the exact role of MMACHC is unknown, its C-terminal region shows similarity to TonB, which is a bacterial protein involved in energy transduction for cobalamin (vitamin B12) uptake. Therefore, it is suggested that MMACHC may have a role in the binding and intracellular trafficking of cobalamin. MMACHC mutations are linked with methylmalonic aciduria and homocystinuria type cblC. MMACHC is widely expressed, it is expressed at higher level in the fetal liver, however it is also expressed in the spleen, lymph node, thymus and bone marrow. MMACHC is weakly or not expressed in the peripheral blood leukocytes.

SAR1B is a small GTPase that functions as a homodimer. GTP-Binding Protein SAR1B (SAR1b) is involved in transport from the endoplasmic reticulum to the Golgi apparatus and also in the selection of the protein cargo and the assembly of the COPII coat complex. The SAR1B protein is activated by the guanine nucleotide exchange factor PREB. SAR1B gene defects are a cause of chylomicron retention disease (CMRD), also known as Anderson disease (ANDD).

Matrix Metallopeptidase 23B (MMP23B) belongs to the matrix metalloproteinase (MMP) family, and it is section of a duplicated region of chromosome 1p36.3. MMP23B is a protease. MMP23B regulates the surface expression of some potassium channels by holding them in the endoplasmic reticulum. Members of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis.

SBDS is part of an extremely preserved protein family which exists from archaea to vertebrates and plants. SBDS protein functions in RNA metabolism and has a role in the biogenesis of the 60S ribosomal subunit and translational activation of ribosomes. Shwachman-Diamond syndrome is a rare autosomal recessive disorder produced by mutations in the SBDS gene.

Heterogeneous nuclear ribonucleoprotein A1 (HNRNPA1) is a member of the A/B subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). HNRNPA1 is involved in the packing of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and may control splice site selection. The HNRNPA1 protein may also have a role in HCV RNA replication. In addition, HNRNPA1 is believed to have a key role in the formation of specific myometrial protein species in parturition.
The hnRNP proteins have distinctive nucleic acid binding properties. HNRNPA1 has 2 repeats of quasi-RRM domains that bind to RNAs. HNRNPA1 is one of the most copious core proteins of hnRNP complexes and it is restricted to the nucleoplasm. The HNRNPA1 protein, along with other hnRNP proteins, is exported from the nucleus, most likely bound to mRNA, and is immediately re-imported. The M9 domain of HNRNPA1 functions as both a nuclear localization and nuclear export signal.

Chemokine (C-X-C motif) ligand (CXCL7) is a small cytokine belonging to the CXC chemokine family. It is a protein that is released in large amounts from platelets following their activation. It stimulates various processes including mitogenesis, synthesis of extracellular matrix, glucose metabolism and synthesis of plasminogen activator.

ANXA5 is a member of the annexin family of calcium-dependent phospholipid binding proteins which are involved in membrane-related activity along exocytotic and endocytotic pathways. ANXA5 is a phospholipase A2 and protein kinase C inhibitory protein with calcium channel properties and takes part in cellular signal transduction, inflammation, growth and differentiation. ANXA5 is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. ANXA5 regulates coagulability in the blood stream by binding to phosphatidylserine and sulfatide. ANXA5 protects sinsuoidal endothelial cells from ischemia reperfusion damage. ANXA5 is necessary for normal CFTR chloride channel activity.

NEDD8 is part of the ubiquitin family. Human NEDD8 shares 60% amino acid sequence homology to ubiquitin. The NEDD8 system is essential for the regulation of protein degradation pathways involved in cell cycle progression, morphogenesis and tumorigenesis. NEDD8 is involved in cell cycle control and embryogenesis. Covalent attachment to its substrates requires prior activation by the E-1 complex UbE1c- appbp1 and linkage to the E-2 enzyme UbE2m. Attachment of NEDD8 to cullins activates their associated E-3 ubiquitin ligase activity, and thus promotes polyubiquitination and proteasomal degradation of cyclins and other regulatory proteins.

ADP-ribosylation factor-like protein 5B (ARL5B) is a member of a family of proteins which are structurally similar to ADP-ribosylation factors. ARLs and ARFs belong to the RAS superfamily of regulatory GTPases. ARL5B is most closely related to ARL5, with which it shares 80% sequence identity. Furthermore, Human ARL5B shares 100% identity with mouse ARL8 and 71% identity with the Drosophila homolog.

Myristate, a rare 14-carbon saturated fatty acid, is co-translationally attached by an amide linkage to the N-terminal glycine residue of cellular & viral proteins with various functions. N-Myristoyltransferase 1, also known as NMT1 catalyzes the transfer of myristate from CoA to proteins. NMT1 seems to be irreversible and is essential for full expression of the biologic activities of several N-myristoylated proteins, as well as the alpha subunit of the signal-transducing guanine nucleotide-binding protein, G protein.

Ephrin-B3 (EFNB3) which belongs to the ephrin gene family is essential in brain development as well as in its maintenance. EFNB3 binds to, and induces the collapse of, commissural axons/growth cones in vitro. EFNB3 loosely binds Eph receptors located on bordering cells, leading to contact-dependent bidirectional signaling into neighboring cells. The EPH and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and are implicated in mediating developmental events, mostly in the nervous system.

NUDT1 is an enzyme that hydrolyzes oxidized purine nucleoside triphosphates, such as 8-oxo-dGTP, 8-oxo-dATP, 2-hydroxy-dATP, and 2-hydroxy rATP, to monophosphates, thereby preventing misincorporation of 8-oxo-dGTP into DNA thus preventing A:T to C:G transversions. NUDT1 is found mostly in the cytoplasm, with some in the mitochondria, suggesting that it is involved in the sanitization of nucleotide pools both for nuclear and mitochondrial genomes. Moreover, NUDT1 is expressed at much higher levels in proliferating cells than in resting cells. Misincorporation of oxidized nucleoside triphosphates into DNA/RNA during replication and transcription can cause mutations which may result in carcinogenesis or neurodegeneration.

Nucleopurin 62kDa C-Terminal Like, which is also known as NUP62CL, is a protein-coding gene. NUP62CL contains a domain found in nucleoporins which are glycoproteins located in nuclear pore complexes.

OGG1 is a DNA glycosylase enzyme which takes part in base excision repair. OGG1 protein is the main enzyme accountable for the excision of 7,8-dihydro-8-oxoguanine (8-oxoG), a mutagenic base byproduct which arises as a result of exposure to reactive oxygen species (ROS). OGG1 shows beta lyase activity that nicks DNA 3'' to the lesion.

TRAF2 protein is related with transduce signals from members of the TNFR superfamily. TRAF2 is located in the cytoplasm binds to TRAF1, TRAF2, or TRAF3, thus inhibiting TRAF function by sequestering the TRAFs in a suppressed state in the cytoplasm. Overexpression of TANK inhibits TRAF2-mediated NF-Kappa-B activation signaled by CD40 and both TNF receptors and inhibits LMP1-mediated NF-kappa-B activation by blocking the association of TRAF2 with LMP1. TRAF2 is necessary for the cellular response to TNF-alpha by connecting upstream signalling molecules to the IKKs and p65.

TCEB1 (elongin C) is a subunit of elongin, which is a common transcription elongation factor that increases the RNA polymerase II transcription elongation past template encoded arresting sites. The SIII complex is comprised of elongins A/A2, B and C. The SIII complex activates elongation by RNA polymerase II by curbing transient pausing of the polymerase at numerous sites within transcription units. Elongin A acts as the transcriptionally active component of the SIII complex, while elongins B and C are regulatory subunits. Elongin A2 is specifically expressed in the testis, and able to forming a stable complex with elongins B and C. The VHL (von Hippel-Lindau) tumor suppressor protein binds to elongins B and C, and thus inhibits transcription elongation.

Immunity-related GTPase family M protein (IRGM) is essential for clearance of severe protozoan and bacterial infections. IRGM belongs to the p47 immunity-related GTPase family. IRGM serves in innate immune response possibly via regulation of autophagy. IRGM regulates proinflammatory cytokine production and inhibit endotoxemia upon infection and also has a part in macrophages adhesion and motility. Polymorphisms which modify the natural expression of the IRGM gene are associated with a susceptibility to Crohn's disease and tuberculosis.

GABARAP is a ligand-gated chloride channel that mediates inhibitory neurotransmission. GABARAP is highly positively charged in its N-terminus and shares sequence similarity with light chain-3 of microtubule-associated proteins 1A and 1B. GABARAP clusters neurotransmitter receptors by mediating interaction with the cytoskeleton.