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PA2G4 belongs to the peptidase M24C family and functions as an RNA-binding protein involved in cellular proliferation and differentiation processes. PA2G4 is a component of pre-ribosomal ribonucleoprotein complexes, participating in ribosome assembly and regulating the later steps of rRNA processing. Also, PA2G4 interacts with ErbB-3 and may function as a modulator of the ErbB-3 mediated signal transduction pathway by regulating the effects of Neuregulin-1. Furthermore, PA2G4 is a transcriptional co-repressor of androgen receptor-regulated genes and other cell cycle regulatory genes through its interactions with histone deacetylases. PA2G4 is implicated in growth inhibition and the induction of differentiation of human cancer cells. In addition, PA2G4 mediates cap-independent translation of specific viral IRESs (internal ribosomal entry site). PA2G4 associates with 28S, 18S and 5.8S mature rRNAs, several rRNA precursors and probably U3 small nucleolar RNA.

Mediator Complex Subunit 20 (MED20) is a subunit of the Mediator complex, which is a multiprotein coactivator of RNA transcription that interacts with DNA-bound transcriptional activators, RNA polymerase II, and general initiation factors. The Mediator functions as a link to transmit information from gene-specific regulatory proteins to the basal RNA polymerase II transcription apparatus. Mediator is recruited to promoters by direct interactions with regulatory proteins and functions as a scaffold for the compilation of a functional preinitiation complex with RNA polymerase II and the general transcription factors.

Coatomer Protein Complex SubunitEpsilon, also known as COPE is an epsilon subunit of coatomer protein complex. Coatomer is a cytosolic protein complex which binds to dilysine motifs and reversibly links with Golgi non-clathrin-coated vesicles. COPE is necessary forbudding from Golgi membranes, and is also essential for the retrograde Golgi-to-ER transport of dilysine-taggedproteins. Coatomer complex contain at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. Alternatively spliced transcript variants encoding dissimilar isoforms have been identifiedfor COPE.

GID Complex Subunit 8, also known as GID8 is a member of the GID8 family. GID8 was recognized through a two hybrid-associated protein screen with RanBPM. GID8 acts together with RanBP9 and includes a protein complex with RanBPM and Muskelin.

Nuclear distribution gene C homolog (NUDC) is a nuclear distribution protein. The NUDC protein has a key role in mitosis and cytokinesis. NUDC is involved in spindle formation during mitosis and in microtubule organization during cytokinesis. NUDC is required for correct formation of mitotic spindles and chromosome separation during mitosis, as well as cell proliferation. NUDC also has a role in neurogenesis and neuronal migration.

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.

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).

S100A8 is a part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a broad range of cells, and participate in the regulation of cellular processes such as cell cycle progression and differentiation. S100A8 plays a role in the inhibition of casein kinase and as a cytokine. S100A8 altered expression is related with cystic fibrosis disease. S100A8 is a calcium-binding protein that has antimicrobial activity against bacteria and fungi.S100A8 is crucial for resistance towards invasion by pathogenic bacteria. S100A8 up-regulates transcription of genes that are under the control of NF-kappa-B. S100A8 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide. S100A8 endorses tubulin polymerization and promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A8 takes part as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.

CINP is a member of the CINP family. CINP cooperates with the components of the replication complex and 2 kinases, CDK2 and CDC7, to provide a working and physical link between CDK2 and CDC7 throughout the firing of the origins of replication.

TARC cDNA encodes a 94 amino acid precursor protein with a 23 amino acid residue signal peptide that is cleaved off to generate the 71 amino acid residue mature secreted protein. Along with CC chemokine family members, CCL-17 has approximately 24-29% amino acid sequence identity with RANTES, MIP-1a, MIP-1b, MCP-1, MCP-2, MCP-3 and I-309. TARC is expressed in thymus, and at a lower level in the lung, colon, and small intestine. TARC is in addition transiently expressed in stimulated peripheral blood mononuclear cells. Recombinant TARC has been shown to be chemotactic for T cell lines but not monocytes or neutrophils. CCL-17 was recently identified to be a specific functional ligand for CCR4, a receptor that is selectively expressed on T cells. CCL17 is one of quite a few Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16. CCL17 shows chemotactic activity for T lymphocytes, but not monocytes or granulocytes. CCL17 binds to chemokine receptors CCR4 and CCR8. This chemokine plays important roles in T cell development in thymus as well as in trafficking and activation of mature T cells.

Prothrombin Complex Concentrate (PCC) is a combination of several blood clotting factors II, VII, IX and X. PCC is used in the treatment of the congenital bleeding disorders associated with Factors II, VII, IX, and X deficiencies. PCC reverses the effect of warfarin (a coumarin anti-coagulant) and is used in cases of significant bleeding in patients with a coagulopathy, for example, gastrointestinal haemorrhage or intracranial haemorrhage. The PCC is also extensively used in treating acquired coagulation abnormalities secondary to vitamin K deficiency, warfarin ingestion, and various types of liver disease.
Hepatitis, anaphylaxis and thrombosis have been reported as complications of prothrombin complex concentrates administration.

EMC2 is an element of the ER membrane protein complex. EMC2 is a member of the EMC2 family and holds 3 TPR repeats.

Clusterin also named Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified.
The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the a and b chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by five disulfide bridges and are flanked by two predicted coiled-coil a-helices and three predicted amphipathic a-helices.
Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% to 80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.
It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, heparin, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
A genuine function of clusterin has not been defined. One tempting hypothesis says that clusterin is an extracellular chaperone protecting cells from stress induced insults caused by degraded and misfolded protein precipitates.
Clusterin is up- or down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others.

Cytohesin 3 (CYTH3) belongs to the PSCD family, whose members have identical structural organization which consists of an N-terminal coiled-coil motif, a central Sec7 domain, and a C-terminal pleckstrin homology (PH) domain, and seem to mediate the regulation of protein sorting and membrane trafficking. CYTH3 is involved in the regulation of Golgi structure and function, and it might have a physiological role in regulating ADP-ribosylation factor protein 6 (ARF) functions, in addition to acting on ARF1.

The centromere is a specialized chromatin domain, present throughout the cell cycle, that acts as a platform on which the transient assembly of the kinetochore occurs during mitosis. All active centromeres are characterized by the presence of long arrays nucleosomes in which CENPA replaces histone H3. CENPM is an additional factor required for centromere assembly.

Tropic 1808 is a candidate chemotropic factor induced by nerve injury. Tpc1808 protein, similar to NGF, could promote the expression of NF-H in a time-dependent manner. Tpc1808 is the gene related to promotion of nerve growth, and both the Tpc1808 gene and the Tpc1808 recombinant protein up-regulate the expression of NF-H in PC12 cells.

CPLX1 is part of the SNARE family complex binding proteins that are catalysts or inhibitors of vesicle exocytosis. CPLX1 shows reduced Ca2+-triggered fast neurotransmitter release at hippocampal glutamatergic synapses, indicating that CPLX1 is a positive regulator of transmitter release. In contrast, CPLX1 inhibits SNARE-mediated liposome and cell fusions in vitro, that result in hypothesis thus acts as a fusion clamp of synaptic exocytosis. CPLX1 regulates a late step in synaptic vesicle exocytosis.

ROBLD3 is a member of the GAMAD family. ROBLD3 is an adapter protein which enhances the efficiency of the MAP kinase cascade and facilitates the activation of MAPK2. ROBLD3 compels the recruitment of MP1 to late endosomes where they form a very stable heterodimeric complex required for ERK activation on endosomes. In humans, a mutation in the ROBLD3 gene has been associated with a primary immunodeficiency syndrome, and suggests a role for the ROBLD3 protein in endosomal biogenesis.

Alpha 1-microglobulin (A1M) is a lipocalin superfamily member (kernal lipocalins). A1M is a low molecular weight protein component of plasma. A1M is distributed in plasma and extravascular compartments of all organs. Alpha-1 Microglobulin is found in mammals, birds, amphibians and fish. The primary sites of A1M synthesis are the liver and the kidney. Around the opening of the lipocalin pocket three lysyl residues are situated; those residues carry yellow-brown modification derived from the binding and degradation of heme and kynurenin (a tryptophan metabolite). A1-Microglobulin’s reductase and dehydrogenase have broad biological substrate specificity properties due to its’ free cysteine side-chain which is located in a flexible loop. Alpha-1-microglobulin is glycosylated by three separate carbohydrate chains: two complex carbohydrates which are N-linked to asparagines at residues 17 and 96, and the other simple carbohydrate which is O-linked to threonine at position 5. The carbohydrates comprise 22% of the total molecular mass of the protein. The glycosylation varies between species.
A1M exists in two forms- a free form and complexed to other macromolecules: in humans- complexed to immunoglobulin A (IgA), in rat- complexed to alpha-1-inhibitor-3. Free A1M is exceptionally heterogeneous in charge (therefore also known as protein HC), and is found tightly linked to a chromophore. The free Alpha-1-microglobulin is a monomeric protein composed of one 188 residue polypeptide and contains three cysteines, two of which (residues 75 and 173) form a conserved intra-molecular disulphide link. The chromophoric group is covalently bound to the free cysteine residue at position 34. A1M binds retinol as a major ligand, but this is probably distinct from its covalent chromophore.
Half of all human plasma A1M (approximately 0.03mg/ml) forms a 1:1 complex with about 5% of plasma immunoglobulin A. The resulting macromolecular complexes’ molecular weight is 200000, and a plasma concentration of 0.3mg/ml. The complex can exhibit both antibody activity and affect many of the biological actions of free Alpha-1-microglobulin.
Alpha-1-microglobulin was first discovered in pathological human urine.
It was suggested that A1M might be involved in tissue defense against reactive oxygen species, oxidation by heme and kynurenin. Evidence also suggests that A1M functions in the regulation of the immune system. Other functions include inhibition of stimulation of cultured lymphocytes by protein antigens; induction of cell division of lymphocytes, a mitogenic effect that can either be enhanced or inhibited by the action of other plasma components; inhibition of neutrophil granulocyte migration in vitro; and inhibition of chemotaxis.

SQSTM1 is an adapter protein which binds ubiquitin and mediates the activation of NFKB1 by TNF-a, NGF and IL-1. SQSTM1 is involved in titin/TTN downstream signaling in muscle cells. SQSTM1 controls signaling cascades through ubiquitination. SQSTM1 participates in cell differentiation, apoptosis, immune response and regulation of K(+) channels. Mutations in UBA domain of the SQSTM1 protein cause Paget’s disease because the UBA is essential for aggregate sequestration and cell survival.

SNCA or Alpha-synuclein is a protein with undisclosed function that mainly concentrated in the brain tissue, mainly in the tips of the neurons in the presynaptic terminals. Almost 1% of the proteins in the brain tissues are synucleins. The protein is located mainly in the hippocampus, thalamus, cerebellum & neocortex. Smaller amounts of the SNCA protein can be found in the neuroglial cells. The MITF protein regulates the SNCA expression in melanocytic cells.

Smac/Diablo is a proapoptotic protein that increases caspase activation in the cytochrome c/Apaf-1/caspase-9 pathway by its binding to the inhibitor of apoptosis proteins (IAPs) and removing their inhibitory activity. Smac/Diablo is a mitochondrial protein which enters the cytosol when cells go through apoptosis, and it moderates the caspase inhibition of IAPs.
Smac/DIABLO expression is associated with the result of renal cell carcinoma.
Dimeric form of Smac/DIABLO implies that once expressed in the cell the protein has a little probability of dissociation and, thus, loss of function.
Survivin, Smac/DIABLO, & PKC-? play an important part in the inhibition of apoptosis by FGF-2 in human small cell lung cancer cells. Mitochondrial survivin associates with Smac/DIABLO, delaying its release. Decreased expression of Smac protein takes part in ovarian carcinogenesis and chemotherapeutic resistance. Smac/DIABLO plays a role in tumor cells during the pathway of apoptosis induction. SMAC protein is regulated by XIAP and degraded by proteasome. SMAC protein takes part inleukemic cell apoptosis.
Smac is released during stress-induced apoptosis in multiple myeloma cells.

Clusterin also known as Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified.
The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the a and b chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by 5 disulfide bridges and are flanked by 2 predicted coiled-coil a-helices and 3 predicted amphipathic a-helices.
Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% -80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.
It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, heparin, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
Clusterin is up/down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others.

S100A8 is a part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a broad range of cells, and participate in the regulation of cellular processes such as cell cycle progression and differentiation. S100A8 plays a role in the inhibition of casein kinase and as a cytokine. S100A8 altered expression is related with cystic fibrosis disease. S100A8 is a calcium-binding protein that has antimicrobial activity against bacteria and fungi.S100A8 is crucial for resistance towards invasion by pathogenic bacteria. S100A8 up-regulates transcription of genes that are under the control of NF-kappa-B. S100A8 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide. S100A8 endorses tubulin polymerization and promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A8 takes part as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.