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Eptifibatide binds to the platelet receptor glycoprotein (GP) IIb/IIIa of human platelets and inhibits platelet aggregation. Eptifibatide is a cyclic peptide derived from a protein discovered in the venom of the southeastern pygmy rattlesnake (Sistrurus miliarus barbouri). Eptifibatide belongs to the arginin-glycin-aspartat-mimetics and reversibly binds to platelets.

Plasma protease C1 inhibitor (SERPING1) is a part of the serpin superfamily of serine protease inhibitors. SERPING1 plays an important role in regulating activation of both the complement and contact systems. That isdue to the fact that SERPING1 regulates the activation of complement factor C1 in addition to the activity of activated C1 by coupling with the active catalytic site at the light chains of C1r and C1s. SERPING1 insufficiency results in hereditary angioedema, which is characterized by recurrent episodes of localized angioedema of the skin, gastrointestinal mucosa or upper respiratory mucosa.

SERPINI1 (Neuroserpin) is an inhibitory serpin which is expressed primarily in the central nervous system. Even though the physiological target of SERPINI1 is still vague, amassed evidence suggest that SERPINI1 has an imperative role in controlling proteolytic degradation of extracellular matrix (ECM) during synaptogenesis and the subsequent development of neuronal plasticity. The neuroprotective role of SERPINI1 has been demonstrated in transgenic mice lacking SERPINI1 expression. The deficiency of SERPINI1 in these mice is linked with motor neuron disease characterized by axonal degradation. In humans, defects in SERPINI1, caused by point mutations in the neuroserpin gene, trigger a hereditary disorder known as the familial encephalopathy with neuroserpin inclusion bodies (FENIB).

SNAPIN is involved in the neurotransmitter release process through its modulation of the sequential interactions between the SNAREs and synaptotagmin. SNAPIN is part of the SNARE complex of proteins that is needed for synaptic vesicle docking and fusion. SNAPAP is enriched in neurons and exclusively located on synaptic vesicle membrane protein. SNAPIN is also an important factor of the BLOC1 multisubunit protein complex. BLOC1 is required for normal biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules.

ER Lipid Raft Associated 2 (ERLIN2) is a domain-containing protein which is a member of the band 7/mec-2 family. ERLIN2 is a ubiquitously expressed 339 amino acid protein.ERLIN2 which is localized to the lipid raft-like domains in the membrane of the endoplasmic reticulum (ER), plays a key role in the ER-associated degradation (ERAD) pathway that eliminates metabolically regulated and abnormal proteins from the ER.

PCBD1 enzyme takes part in phenylalanine hydroxylation. PCBD1 deficiency results in hyperphenylalaninemia. PCBD1 enzyme controls the homodimerization of HNF1. PCBD1 takes part in tetrahydrobiopterin biosynthesis. PCBD1 prevents the formation of 7-pterins and accelerate the formation of quinonoid-BH2. PCBD1 is a coactivator for HNF1A-dependent transcription.

Integrins are heterodimeric proteins consist of alpha and beta subunits. There are more than 18 alpha and 8 beta subunits discovered in mammals. Integrin family members are membrane receptors that participates in cell adhesion and recognition in a variety of processes including embryogenesis, hemostasis, tissue repair, immune response and metastatic diffusion of tumor cells. ITGB1 encodes a beta subunit.

Pirin (PIR) which belongs to the cupin superfamily, is an Fe(II)-containing nuclear protein expressed in all tissues of the body and concentrated within dot-like subnuclear structures. Pirin may function as a transcriptional cofactor and is involved in the regulation of DNA transcription and replication, as a result of interactions with nuclear factor I/CCAAT box transcription factor as well as B cell lymphoma 3-encoded oncoprotein.

Adiponectin is an important negative regulator in hematopoiesis and immune systems. It may be involved in ending inflammatory responses through its inhibitory functions. Inhibits endothelial nf-kappa-b signaling through a camp-dependent pathway. Inhibits tnf-alpha- induced expression of endothelial adhesion molecules. Involved in the control of fat metabolism and insulin sensitivity.

Fibrinogen silencer-binding protein (FSBP), interacts with X11alpha. The X11alpha/FSBP complex send signals to the nucleus in order to repress glycogen synthase kinase-3beta promoter activity. X11alpha is a neuronal adaptor protein that interacts with the amyloid precursor protein (APP) via a centrally located phosphotyrosine binding domain to inhibit the production of Abeta peptide that is deposited in Alzheimer's diseased brains.

KPNB1 is a member of the importin beta family. The KPNB1 protein is engaged in nuclear protein import, either by coupling itself with an adapter protein (e.g., importin-alpha subunit which binds to nuclear localization signals (NLS) in cargo substrates), or by functioning autonomously as a nuclear transport receptor (acts as NLS receptor, docking of the importin/substrate complex to the nuclear pore complex).

GHBP is a transmembrane receptor for growth hormone. Binding of growth hormone to the receptor leads to receptor dimerization and the activation of an intra- and intercellular signal transduction pathway leading to growth. A common alternate allele of this gene, called GHRd3, lacks exon three and has been well-characterized. Mutations in this gene have been associated with Laron syndrome, also known as the growth hormone insensitivity syndrome (GHIS), a disorder characterized by short stature. Other splice variants, including one encoding a soluble form of the protein (GHRtr), have been observed but have not been thoroughly characterized.

Alpha & Gamma-Adaptin Binding Protein (AAGAB), which is also known as P34, takes part in membrane traffic and interacts with AP1G1 and AP2A1.AAGAB is highly expressed in skin and keratinocytes, with the highest levels in adrenal gland, rectum and thymus.

Midkine (MK) is the product of a retinoic acid responsive gene, MK, and is a member of a family of heparin binding factors. It contains 121 amino acid residues including 10 conserved cysteine residues, all of which appear to be disulphide linked.
Midkine is expressed during embryogenesis, showing an expression pattern that suggests functions in neurogenesis, cell migration, secondary organogenetic induction, and mesoderm-epithelial interaction.
The widespread downregulation of MK in the adult human is reverted in a number of cancers, in which polypeptides are able to act as both transforming growth factors and promoters of angiogenesis.
Midkine (MK), induces chemotaxis of human neutrophils and was found to trigger mobilization of intracellular calcium of these cells.
Midkine induces histamine release from rat peritoneal mast cells with a rapid response in a dose dependent manner.
Midkine is also a potent stimulator of collagen and glycosaminoglycan synthesis.

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.

CA14 is a part of the Carbonic anhydrases family. Carbonic anhydrases (CAs) are a large family of zinc metalloenzymes which catalyze the reversible hydration of carbon dioxide. They present wide variety in tissue distribution and in their subcellular localization. CA14 is a type I membrane protein which shares highest sequence similarity with the other transmembrane CA isoform, CA XII. Nevertheless, they have different patterns of tissue-specific expression and therefore take different physiologic parts.

cAMP-dependent protein kinase inhibitor beta (PKIB) belongs to the cAMP-dependent protein kinase inhibitor family. PKIB may interact with the catalytic subunit of cAMP-dependent protein kinase and function as a competitive inhibitor.

Lipocalin-2 also called Neutrophil Gelatinase Associated Lipocalin (NGAL) belongs to a family of lipocans which include 25 proteins (including a1-microglobulin and b-lactoglobulin), which are characterized by their ability to bind small lipophilic substances in their hydrophobic core.
They thereby serve as transporters of substances like retinal, biliverdins & prostaglandins. There are indications that NGAL is involved in modulation of the inflammatory response and is found in the plasma of patients after stroke.

The galectins are a family of beta-galactoside-binding proteins implicated in modulating cell-cell and cell-matrix interactions. Galectin-1 is an autocrine negative growth factor that regulates cell proliferation. Galectin-1 regulates cell apoptosis and cell differentiation. Galectin-1 binds CD45, CD3 and CD4 & inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of lyn kinase. Galectin-1 and its ligands are one of the master regulators of immune responses as T-cell homeostasis and survival, T-cell immune disorders, inflammation and allergies as well as host–pathogen interactions. Galectin-1 expression or overexpression in tumors and/or the tissue surrounding them must be considered as a sign of the malignant tumor progression that is often related to the long-range dissemination of tumoral cells (metastasis), to their dissemination into the surrounding normal tissue, and to tumor immune-escape. Galectin-1 in its oxidized form plays a number of important roles in the regeneration of the central nervous system after injury. The targeted overexpression (or delivery) of Galectin-1 should be considered as a method of choice for the treatment of some kinds of inflammation-related diseases, neurodegenerative pathologies and muscular dystrophies. In contrast, the targeted inhibition of Galectin-1 expression is what should be developed for therapeutic applications against cancer progression. Galectin-1 is thus a promising molecular target for the development of new and original therapeutic tools. There is 88% homology between the human and mouse galectin-1.

C-type Lectin Domain Family 1 Member B, also known as CLEC1B. NK-Natural killer cells express multiple calcium-dependent (C-type) lectin-like receptors, for instance CD94 (KLRD1; MIM 602894) and NKG2D (KLRC4; MIM 602893), which interact with major histocompatibility complex class I molecules and either inhibit or else activate cytotoxicity and cytokine secretion. CLEC1B is a C-type lectin-like receptor which is expressed in myeloid cells as well as in NK cells.

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.

Relaxin-3 (RLN3) belongs to the relaxin family. Relaxins are endocrine and autocrine/paracrine hormones. Relaxin, which is produced by the ovary, targets the mammalian reproductive system to ripen the cervix, elongate the pubic symphysis and inhibit uterine contraction. Unlike human Relaxins 1 and 2, Relaxin 3 does not seem to have a role in reproduction; however it is involved in stress response in the brain stem. RLN3 is the only known ligand for the G-protein-coupled receptor GPCR135, titled RXFP3. In addition, RLN3 binds the LGR7 (RXFP1) receptor, however with lower affinity than Relaxin-2. Even though binding of RLN3 to LGR7 increases intracellular cAMP, binding to GPCR135 suppresses cAMP accumulation, indicating coupling to Gi, Go, or Gz by this receptor.

Members of the Rho (or ARH) protein family and other Ras-related small GTP-binding proteins are involved in various cellular procedures, such as cell cytoskeletal organization, secretion, proliferation, and signaling. The GTPBPs are active only in the GTP-bound state. At least 3 types of proteins firmly regulate cycling between the GTP-bound and GDP-bound states: GDP-dissociation inhibitors (GDIs), GTPase-activating proteins (GAPs) and guanine nucleotide-releasing factors (GRFs). ARHGDIB and the other GDIs lower the level of GDP dissociation from Ras-like GTPases.

Eukaryotic elongation factor-2 kinase (EEF2K) is threonine kinase which regulates protein synthesis by means of controlling the rate of peptide chain elongation. Upon activation through a diversity of upstream kinases including AMPK or TRPM7, EEF2K phosphorylates the elongation factor EEF2 at a sole site, renders it unable to bind ribosomes and therefore inactive. In turn, the rate of protein synthesis is being reduced.