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Crystallin Zeta, also known as CRYZ, Binds NADP and participates in a one-electron transfer process. CRYZ takes part in the detoxification of xenobiotics and Interacts with (AU)-rich elements (ARE) in the 3'-UTR of target mRNA species. CRYZ improves the mRNA coding for BCL2.

Sclerostin Domain Containing 1 (SOSTDC1) belongs to the sclerostin family and an N-glycosylated, secreted protein with a C-terminal cystine knot-like domain. The SOSTDC1 protein acts as a bone morphogenetic protein (BMP) antagonist. Specifically, SOSTDC1 directly associates with BMPs, prohibiting them from binding their receptors, thus regulating BMP signaling throughout cellular proliferation, differentiation, and programmed cell death. SOSTDC1 may also be involved in the onset of endometrial receptivity for implantation/sensitization for the decidual cell reaction Enhances Wnt signaling and hinders TGF-beta signaling. In addition, SOSTDC1 directly antagonizes the activity of BMP2, BMP4, BMP6 and BMP7 in a dose-dependent manner.

PHD finger protein 11 (PHF11) is a regulator of TH1-type cytokine gene expression. The decline in PHF11 expression observed with an AD-associated genotype may promote the intense TH2 reactions which characterize numerous allergic individuals. PHF11 is linked with raised total serum IgE levels, asthma and acute atopic dermatitis (AD) in children. Even though PHF11 includes a plant homeodomain, a motif frequently found in transcriptional regulators, PHF11 function of has yet been examined.

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.

Prolactin is a pituitary hormone involved in the stimulation of milk production, salt and water regulation, growth, development and reproduction. The initial step in its action is the binding to a specific membrane receptor (prolactin receptor) which belongs to the superfamily of class 1 cytokine receptors. The function of the prolactin receptor is mediated, at least in part, by two families of signaling molecules: Janus kinases and signal transducers and activators of transcription. Prolactin (PRL) is a hormone involved in a variety of important functions including ion transport and osmoregulation, stimulation of milk, protein synthesis as well as the regulation of numerous reproductive functions. PRL exerts its influence on different cell types through a signal transduction pathway which begins with the binding of the hormone to a transmembrane PRL receptor. Immunoreactive PRL receptor, a member of the cytokine receptor family, varies in size (short and long forms) with tissue source and species, from ~40 kDa to 100 kDa. The PRL receptor consists of at least three separate domains: an extracellular region with 5 cysteines which contains the prolactin binding site, a single transmembrane domain and a cytoplasmic region, the length of which appears to influence ligand binding and regulate cellular function.

Lxn also known as Latexin is a member of the protease inhibitor I47 (latexin) family. Lxn's function is hardly reversible, non-competitive, as well as potent inhibitor of CPA1, CPA2 and CPA4. Furthermore, Lxn plays a role in inflammation. Among the diseases associated with LXN are endocervicitis and listeriosis.

Proline-Serine-Threonine Phosphatase Interacting Protein 1 (PSTPIP1) which is a scaffold protein and a regulator of the actin cytoskeleton binds ABL1, PTPN18, WAS, CD2AP, and PTPN12. PSTPIP1 also binds to the cytoplasmic tail of CD2, an effector of T cell activation and adhesion, negatively affecting CD2-triggered T cell activation. Mutations in PSTPIP1 are a cause of PAPA syndrome.

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.

Von Hippel-Lindau disease is a dominant inherited syndrome characterized by the predisposition to develop various kinds of benign and malignant tumors, including clear cell renal carcinomas, pheochromocytomas and hemangioblastomas of the central nervous system and retina. VHL syndrome is caused by germline mutation in the VHL tumor suppressor, and VHL tumors are associated with loss or mutation of the remaining wild-type allele. VHL has two domains: a roughly 100-residue NH2-terminal domain rich in b sheet (b-domain) and a smaller a-helical domain (a-domain), held together by two linkers and a polar interface. VHL protein is also involved in the degradation of hypoxia-inducible factor (HIF).

YWHAH belongs to the 14-3-3 family of proteins which mediate signal transduction by binding to phosphoserine-containing proteins. 14-3-3 ETA is found in plants and mammals, and there is 99% identity to the mouse, rat and bovine orthologs. YWHAH gene contains a 7 base pair repeat sequence in its 5' UTR, and changes in the number of this repeat has been associated with early-onset schizophrenia.
14-3-3 eta is specific to the site of joint inflammation.
14-3-3 proteins are colocalized with Lewy bodies in Parkinson disease, though there is no specific staining for the 14-3-3 eta subunit.
There are 3 different isoforms types of 14-3-3: Beta, Gamma and ETA that are DAL-1/Protein 4.1B-binding proteins.

RGS10 is a member of the RGS family that regulate molecules which perform as GTPase activating proteins (GAPs) for G alpha subunits of heterotrimeric G proteins. RGS proteins can disengage G protein subunits of the Gi alpha, Go alpha and Gq alpha subtypes. They drive G proteins into their inactive GDP-bound forms. All RGS proteins share a conserved 120-amino acid sequence termed the RGS domain. The nucleus localized RGS10 is associates specifically with the activated forms of the two related G-protein subunits, G-alphai3 and G-alphaz but is unable to cooperate with the structurally and functionally distinct G-alpha subunits.

METTL21A, which is a part of the methyltransferase superfamily, is a Protein-lysine methyltransferase that in vitro methylates HSPA1, HSPA5 and HSPA8.

Diphthamide biosynthesis protein 2 (DPH2) is a homodimer and each of its monomers can bind a [4Fe-4S] cluster. DPH2 is the target of ADP ribosylating diphtheria toxin (DT) and Pseudomonas exotoxin A (PE). DPH2 was identified by its ability to complement a diphthamide mutant strain, and thus serves in diphthamide biosynthesis. The loss of DPH2 pre-activates NF-kB and death receptor pathways and renders MCF7 cells hypersensitive to tumor necrosis factor.

VPS29 is a member of a group of genes coding for vacuolar protein sorting (VPS) proteins which, when functionally damaged, lessens the efficient transfer of vacuolar hydrolases. VPS29 is a late Golgi transmembrane protein that operates as the sorting receptor for soluble vacuolar hydrolases, from the prevacuolar endosome back to the Golgi. Moreover, VPS29 takes part in the creation of the inner shell of the retromer coat for retrograde vesicles parting the prevacuolar compartment.

PEDF is a neurotrophic protein that induces extensive neuronal differentiation in retinoblastoma cells. SerpinF1 is a potent inhibitor of angiogenesis. EPC1 doesn’t undergo the stressed to relaxed conformation transition characteristic as of the active serpins since it exhibits no serine protease inhibitory activity.
Aqueous humour level of asymmetric dimethylarginine is correlated with PEDF in humans. ADMA and PEDF levels are increased in response to inflammation in uveitis.
Lack of PEDF expression is a potent factor for the enhancement of tumor growth and angiogenesis in breast cancer.
PEDF & VEGF genes contribute to the development of diabetic retinopathy.
PEDF and VEGF structural changes in blood vessel wall play an important role in the pathophysiology of PD patients.
PEDF-overexpressing tumors exhibited reduced intratumoral angiogenesis.
SerpinF1 is a new promising approach for the treatment of osteosarcoma.
Levels of the natural ocular anti-angiogenic factor SentrinF1 (PEDF) is associated with proliferative retinopathy.
VEGF secreted by retinal pigment epithelial cells upregulates PEDF expression via VEGFR-1 in an autocrine manner.
Sentrin-F1 concentration in the aqueous humor of diabetic patients predicts who will develop progression of retinopathy.
PEDF blocks angiogenic effects of leptin through its anti-oxidative properties.

Prolyl Endopeptidase , also known as PREP is a cytosolic prolyl endopeptidase which cleaves peptide bonds on the C-terminal side of prolyl residues within peptides which are up to about 30 a.a long. In addition, Prolyl endopeptidases have been shown to be implicated in the maturation and degradation of peptide hormones and neuropeptides.

The somatomedins, or insulin-like growth factors (IGFs), comprise a family of peptides that takes part in mammalian growth and development. IGF1 mediates various growth-promoting effects of growth hormone (GH; MIM 139250). Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin' (Daughaday et al., 1972). 3 main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).

Pyruvate kinase is a key enzyme in the glycolytic pathway. The M2 isoenzyme of pyruvate kinase is specifically expressed at high levels in tumor cells, and can be measured in plasma of patients with advanced breast cancer. The marker is useful for measuring disease activity, sensitivity to chemotherapy and recurrence.

The protein encoded by this gene is a member of the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily. The superfamily includes large families of growth and differentiation factors. Bone morphogenetic proteins were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. This particular family member plays an important role in the onset of endochondral bone formation in humans, and a reduction in expression has been associated with a variety of bone diseases, including the heritable disorder Fibrodysplasia Ossificans Progressiva. Alternative splicing in the 5' untranslated region of this gene has been described and three variants are described, all encoding an identical protein.

ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters and goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms (a and f) include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, and X, and the complement factors C1R and C1S. Further isoforms diverge mainly in the C-terminal sequence and lack the hydroxylase domain, and some have been localized to the endoplasmic and sarcoplasmic reticulum.

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.

The term ‘PDGF’ refers to a family of disulphide bond-linked dimeric isoforms that act as autocrine and paracrine growth factors and are produced by a variety of cell types other than platelets.
They act as potent mitogens for almost all mesenchymally-derived cells. Aberrant expression is involved in certain cancers, fibroproliferative disorders and atherosclerosis. The protein also contributes to wound healing and neural regeneration. There are four members of the PDGF family – PDGF A, PDGF B, PDGF C and PDGF D. Two distinct types of PDGF-A exist – a short form that is soluble and a long form that is retained by the extracellular matrix.

Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development.

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.