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Ubiquitin Carboxyl-Terminal Esterase L1 (UCHL1) is a part of a family whose products hydrolyze small C-terminal adducts of ubiquitin to create the ubiquitin monomer. UCHL1 is a part of the ubiquitin system, which regulates many biological activities. UCHL1 is a thiol protease that distinguishes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. UCHL1 binds to free monoubiquitin and avoids its degradation in lysosomes.

Nuclear Apoptosis Inducing Factor 1 (NAIF1) is a part of the NAIF1 family. NAIF1 Interacts with HARBI1 and Induces apoptosis.

DEAD Box Protein 56 (DDX56) belongs to the DEAD box protein family. DEAD box proteins, categorized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. DEAD box proteins are implicated in several cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based upon their distribution patterns, certain members of this family are assumed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. DDX56 exhibits ATPase activity in the presence of polynucleotides and associates with nucleoplasmic 65S preribosomal particles.

NADH Dehydrogenase1 Alpha Subcomplex 4 (NDUFA4) is a member of the complex I 9kDa subunit family. Mammalian complex I of mitochondrial respiratory chain is comprised of 45 different subunits. NDUFA4 protein has NADH dehydrogenase activity and oxidoreductase activity. NDUFA4 transfers electrons from NADH to the respiratory chain. The immediate electron acceptor for the NDUFA4 enzyme is assumed to be ubiquinone.

NDUFV3 is one of no less than 41 subunits which form the NADH-ubiquinone oxidoreductase complex that is involved in the mitochondrial respiratory chain and assists in catalyzing the rotenone-sensitive oxidation of NADH and the reduction of ubiquinone. NDUFV3 is 1 of 3 proteins found in the flavoprotein fraction of the complex but it exact function is unknown. Two transcript variants encoding altered isoforms are known for this gene.

a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).

ATP synthase subunit gamma, mitochondrial isoform L (liver) (ATP5C1) is a member of the ATPase gamma chain family. ATP5C1 catalyzes ATP synthesis by using an electrochemical gradient of protons across the inner membrane throughout oxidative phosphorylation. The catalytic portion of mitochondrial ATP synthase is comprised of 5 different subunits (alpha, beta, gamma, delta, and epsilon) gathered with a stoichiometry of 3 alpha, 3 beta, and a single representative of the other 3.

SRGN is identified as a hematopoietic cell granule proteoglycan. Proteoglycans stored in the secretory granules of various hematopoietic cells also hold a protease-resistant peptide core, and is vital for neutralizing hydrolytic enzymes. SRGN is related to the macromolecular complex of granzymes and perforin that acts as a intermediary of granule-mediated apoptosis.

Otubain 1 (OTUB1) belongs to the ovarian tumor (OUT) superfamily of predicted cysteine proteases and inhibits cytokine gene transcription in the immune system through its interaction with a ubiquitin protease and E3 ubiquitin ligase. OTUB1 is a highly specific ubiquitin iso-peptidase, it cleaves ubiquitin from branched poly-ubiquitin chains but not from ubiquitinated substrates. OTUB1 is believed to work in specific ubiquitin-dependent pathways, possibly by providing an editing function of polyubiquitin chain growth. OTUB1 is a hydrolase that removes conjugated ubiquitin from proteins in vitro and may therefore have a significant regulatory role in the level of protein turnover by preventing degradation. Additionally, OTUB1 is a regulator of T-cell anergy, a phenomenon that occurs when T-cells are rendered impassive to antigen re-challenge and no longer respond to their cognate antigen. OTUB1 acts via its interaction with RNF128/GRAIL, which is an essential inductor of CD4 T-cell anergy.

PDRG1 is a 133 amino acid protein that localizes to the cytoplasm and belongs to the prefoldin subunit beta family. PDRG1 is expressed primarily in normal testicular tissue, it is functionally induced by ultraviolet light and is thought to have a role in chaperone-mediated protein folding, possibly having a role in cellular degradation. PDRG1 is linked to Creutzfeldt-Jakob disease, amyotrophic lateral sclerosis, spinal muscular atrophy, ring chromosome 20 epilepsy syndrome and Alagille syndrome.

ISG15 ubiquitin-like Modifier is conjugated to the intracellular target proteins after IFN-alpha or IFN-beta stimulation. ISG15 enzymatic pathway is partially distinct from that of ubiquitin, differing in substrate specificity and interaction with ligating enzymes. ISG15 conjugation pathway uses a dedicated E1 enzyme, but seems to converge with the ub conjugation pathway at the level of a specific E2 enzyme. ISG15 protein targets include STAT1, SERPINA 3G/SPI2A, JAK1, MAPK3/ERK1, PLCG1, EIF2AK2/PKR, MX1/MXA, and RIG-1. Deconjugated by USP18/UBP43 shows specific chemotactic activity towards neutrophils and activates them to induce release of eosinophil chemotactic factors. ISG15 serves as a trans-acting binding factor directing the association of ligated target proteins to intermediate filaments. ISG15 plays a role in autocrine, paracrine and endocrine mechanisms, as in cell-to-cell signaling, possibly partly by inducing ifn-gamma secretion by monocytes and macrophages. ISG15 displays antiviral activity during viral infections. ISG15 in response to IFN-TAU secreted by the conceptus, ligates to and regulate proteins involved in the release of prostaglandin F2-alpha and thus prevent lysis of the corpus luteum and maintain the pregnancy. ISG15 shares several common properties with other ubiquitin-like molecules, but its activity is strongly regulated by precise signaling pathways that have a role in innate immunity.

PPP3R1 is a Ser/Thr-specific calcium and calmodulin-dependent protein phosphatase which takes a vital part in the T cell activation pathway. Calcineurin is composed of two subunits; calcineurin A (CnA) and calcineurin B (CnB). Dephosphorylation of the nuclear factor of activated T-cells (NF-AT) by Calcineurin is essential for NF-AT activation, nuclear translocation, and early gene expression in T-cells.

NEDD8-activating enzyme E1 catalytic subunit (UBA3) is the catalytic subunit of the dimeric UBA3-NAE1 E1 enzyme, which belongs to the E1 ubiquitin-activating enzyme family. E1 activates NEDD8 by initially adenylating its C-terminal glycine residue with ATP, afterwards linking this residue to the side chain of the catalytic cysteine, generating a NEDD8-UBA3 thioester and free AMP. E1 at last transfers NEDD8 to the catalytic cysteine of UBE2M. The UBA3 enzyme connects with AppBp1, an amyloid beta precursor protein binding protein, to form a heterodimer, and at that point the enzyme complex activates NEDD8, a ubiquitin-like protein, which controls cell division, signaling and embryogenesis.

UbcH10 is an essential mediator of mitotic destruction events and cell cycle progression. It catalyzes the destruction of cyclins A and B in conjunction with the anaphase-promoting complex, and therefore, plays an important role in the control of the cell exit from mitosis This activity is essential at then end of mitosis for the inactivation of their partner kinase Cdc2 and exit from mitosis into G1 of the next cell cycle. In addition, UbcH10 bears homology to yeast PAS2, a gene that is essential for biogenesis of peroxisomes. UbcH10 is useful for in vitro ubiquitinylation reactions.

Human Ubquitin-conjugating enzyme 7 (UbcH7) is a ubiquitin-conjugating enzyme (E2) mediating c-fos degradation, transcription factor NF-B maturation, and human papilloma virus-mediated p53 and Myc protein degradation, in vitro. The ubiquitin-conjugating enzymes (E2s) are essential components of the post-translational protein ubiquitination pathway, mediating the transfer of activated ubiquitin to substrate proteins. The human UBE2L1-UBE2L4 gene could potentially encode different isoforms of the UbcH7. UBE2L3 gene, located at chromosome 22q11.2, is the only identical family member with introns and encodes a polypeptide sequence identical to that of UbcH7.

Proteasome subunit alpha type-2 (PSMA2) is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. PSMA2 is a 20S core alpha subunit of proteasome belonging to the peptidase T1A family. PSMA2 functions as a docking domain for the regulatory particles and exterior gates blocking unregulated access to the inner cavity.

Ubiquitin-conjugating enzyme E2S (UBE2S) belongs to the ubiquitin-conjugating enzyme family. UBE2S is able to form a thiol ester linkage with ubiquitin in a ubiquitin activating enzyme-dependent manner, a typical property of ubiquitin carrier proteins. UBE2S catalyzes the covalent attachment of ubiquitin to other proteins. UBE2S acts as a crucial factor of the anaphase promoting complex/cyclosome (APC/C), which is a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. UBE2S acts by purposely elongating 'Lys-11'-linked polyubiquitin chains initiated by the E2 enzyme UBE2C/UBCH10 on APC/C substrates, augmenting the degradation of APC/C substrates by the proteasome and promoting mitotic exit. UBE2S also acts by elongating ubiquitin chains initiated by the E2 enzyme UBE2D1/UBCH5 in vitro; it is nevertheless uncertain whether UBE2D1/UBCH5 acts as an E2 enzyme for the APC/C in vivo. UBE2S is also involved in ubiquitination and consequent degradation of VHL, resulting in an accumulation of HIF1A.

FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.

NADH dehydrogenase [ubiquinone] iron-sulfur protein 3 (NDUFS3) is a member of the complex I 30 kDa subunit family. NDUFS3 is one of the iron-sulfur protein (IP) components of mitochondrial NADH:ubiquinone oxidoreductase (complex I). This complex is the first enzyme complex in the electron transport chain of mitochondria. The iron-sulfur protein (IP) fraction of complex I consists of seven subunits. NDUFS3 gene mutations are linked with Leigh syndrome resulting from mitochondrial complex indefficiency.

Scavenger mRNA-decapping enzyme (DCPS) is a member of the HIT family. DCPS is required for the complete degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. It was shown that DCPS hydrolyzes the residual m7GpppN cap structure after the complete 3'–5' degradation of the mRNA by the exosome. Furthermore, DCPS releases m7GMP and is incapable of cleaving cap structures attached to a long RNA chain.

TNFSF15 is a cytokine that belongs to the tumor necrosis factor (TNF) ligand family. This protein is abundantly expressed in endothelial cells, but is not expressed in either B or T cells. The expression of TNFSF15 is inducible by TNF and IL-1 alpha. This cytokine is a ligand for receptor TNFRSF25 and decoy receptor TNFRSF21/DR6. It can activate NF-kappaB and MAP kinases, and acts as an autocrine factor to induce apoptosis in endothelial cells. TNFSF15 is also found to inhibit endothelial cell proliferation, and thus may function as an angiogenesis inhibitor. An additional isoform encoded by an alternatively spliced transcript variant has been reported but the sequence of this transcript has not been determined.

Developmental Pluripotency Associated 3 (DPPA3) is a protein which in mice may serve as a maternal factor during the preimplantation stage of development. In mice, the DPPA3 protein has a role in transcriptional repression, cell division, and maintenance of cell pluripotentiality. In humans, related intronless loci are found on chromosomes 14 and X. DPPA3 is expressed in embryonic stem and carcinoma cells. DPPA3 has a low expression in the testis, ovary and thymus. DPPA3 is highly expressed in testicular germ cell tumors.

Alpha-synuclein or SNCA is a synuclein protein. SNCA mainly found in the brain, small concentration of the protein can also be located in other tissues such as heart and muscle. When looking in the brain tissue, SNCA is located in the end of the neuron, in an area called presynaptic terminal. In the presynaptic terminal SNCA has interaction with phospholipids & other proteins. Neurotransmitters are released from the synaptic vesicles in the Presynaptic terminals and act as messengers. Once released, the neurotransmitters send signals across the neurons that are crucial for the brain’s operation.