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HMGN1 binds to the inner side of the nucleosomal DNA therefore changing the interaction between the DNA and the histone octamer. HMGN1 participates in the development which maintains transcribable genes in an exceptional chromatin conformation. HMGN1 inhibits the phosphorylation of nucleosomal histones H3 and H2A by RPS6KA5/MSK1 and RPS6KA3/RSK2.

BST1 (Bone Marrow Stromal Cell Antigen 1), is a GPI (glycosylphosphatidylinositol) anchored membrane protein which is part of the CD38 family. BST1 was initially recognized as a bone marrow stromal cell molecule. BST1 is an ectoenzyme sharing more than a few features with ADP-ribosyl cyclase CD38. BST1 together with CD38, exhibit both DP-ribosyl cyclase and cyclinc ADP ribose hydrolase activities. BST1 participates in rheumatoid arthritis due to its enhanced expression in RA-derived bone marrow stromal cell lines. Moreover, BST1 is expressed by cells of the myeloid lineage and could perform as a receptor with a signal transduction capability.

Celiac disease is an enteropathy that is characterized by intestinal lesions of variable severity. Tissue-type transglutaminase (tTG) is believed to be the predominant autoantigen for celiac disease and the corresponding autoantibodies show higher sensitivity and specificity than anti-gliadin antibodies. Highly pure recombinant human tTG is now available to replace the traditionally used tTG fraction from guinea pig.
Tissue-type transglutaminase antigens have been specifically modified for improved handling: exchange of an active site amino acid eliminates the protein cross-linking activity of the enzyme, while maintaining the native three-dimensional structure and the enzyme's secondary GTPase activity. This engineering assures reproducible properties of the antigen preparations through the absence of variable and ill-defined covalent aggregates of tTG antigen and host cell proteins.

Reticulocalbin-2 (RCN2) is a member of the CREC protein family. RCN2 is a calcium-binding protein found in the lumen of the ER. RCN2 contains 6 conserved regions with similarity to a high affinity Ca(+2)-binding motif, the EF-hand.

Eotaxin-2, also called MPIF2 & Ck?6, is a novel CC chemokine produced by activated monocytes and T lymphocytes. Eotaxin-2 selectively chemoattracts cells expressing CCR3 including eosinophils, basophils, Th2 T cells, mast cells, and certain subsets of dendritic cells. Furthermore, Eotaxin-2 inhibits the proliferation of multipotential hematopoietic progenitor cells. The mature protein, which includes C-terminal truncation, contains 78 amino acids (92 amino acids for the mouse homolog, without C-terminal truncation).
CCL24 functions as a chemotactic chemokine for resting t-lymphocytes, and eosinophils. CCL24 has lower chemotactic activity for neutrophils but none for monocytes and activated lymphocytes. CCL24 is a strong suppressor of colony formation by a multipotential hematopoietic progenitor cell line and binds to CCR3.

A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

Chemokine (C-C motif) ligand 14 (CCL14) is a small cytokine belonging to the CC chemokine family. It is also commonly known as HCC-1. It is produced as a protein precursor that is procesed to generate a mature active protein containing 74 amino acids that and is 46% identical in amino acid composition to CCL3 and CCL4. This chemokine is expressed in various tissues including spleen, bone marrow, liver, muscle, and gut. CCL13 activates monocytes, but does not induce their chemotaxis. Human CCL13 is located on chromosome 17 within a cluster of other chemokines belonging to the CC family.

MTHSFD, also known as Methenyltetrahydrofolate Synthetase Domain Containing protein, is linked to Pancreas, Annular and Gastrointestinal Defects. It has also been associated with Immunodeficiency Syndrome. Some of the Gene Ontology annotations that are related to the MTHSFD gene are nucleic acid binding and nucleotide binding.

High Mobility Group Nucleosomal Binding Domain 3 (HMGN3), binds thyroid hormone receptor beta, however it occurs only in the presence of thyroid hormone. Thyroid hormone receptors are hormone-dependent transcription factors which regulate expression of a variety of particular target genes. HMGN3 is considered to reduce the compactness of the chromatin fiber in nucleosomes, in that way enhancing transcription from chromatin templates.

SERPINA1 is secreted and is a serine protease inhibitor which its targets include elastase, plasmin, collagenase, thrombin, leucocytic proteases, trypsin, chymotrypsin, and plasminogen activator. Defects in SERPINA1 gene can cause emphysema or liver disease. Antral SERPINA1 expression is particularly induced by H. pylori infection. lung and prostate cancers have shown a significant increase in SERPINA1 serum levels compared with healthy controls though breast cancers did not show a significant change. SERPINA1 is an endogenous inhibitor of serine proteases and inhibits the catalytic domain of human recombinant matriptase in vitro. Rise in SERPINA1 occurs as an acute phase response to tissue necrosis and inflammation. mutations in SERPINA1 and SLC11A1 genes change the balance between elastase produced by leukocytes during phagocytosis.

Marginal zone B- and B1-cell-specific protein (MZB1) functions as a hormone-regulated adipokine/proinflammatory cytokine which is implicated in causing chronic inflammation and affecting cellular expansion. MZB1 links with immunoglobulin M (IgM) heavy and light chains and stimulate s IgM assembly and secretion. MZB1 exerts its effect by acting as a molecular chaperone or as an oxidoreductase as it exhibits a low level of oxidoreductase activity. MZB1 helps to diversify peripheral B-cell functions by regulating Ca(2+) stores, antibody secretion and integrin activation.

Rho Guanine Nucleotide Exchange Factor 39, also known as ARHGEF39, is a protein coding gene which owns one DH (DBL-homology) domain and one PH domain. ARHGEF39 encourages cell proliferation.

The secreted polypeptide noggin, encoded by the NOG gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, noggin may have a principal role in creating morphogenic gradients. Noggin appears to have pleiotropic effect, both early in development as well as in later stages. It was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of noggin suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. Recently, several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1) were identified; both SYM1 and SYNS1 have multiple joint fusion as their principal feature, and map to the same region (17q22) as NOG. All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse.

Synaptojanin 2 Binding Protein (SYNJ2BP) contains 1 PDZ (DHR) domain which binds to isoform 2A of SYNJ2 (through the unique motif in the C-terminus) and interacts with MAPK12.

Complement Component 4 Binding Protein, Beta (C4BPB) belongs to a superfamily of proteins composed primarily of tandemly arrayed short consensus repeats of approximately 60 amino acids. C4BPB has a regulatory role in the coagulation system also, mediated via the beta-chain binding of protein S, a vitamin K-dependent protein which functions as a cofactor of activated protein C. A single, unique beta-chain of the C4BPB assembles with 7 identical alpha-chains into the principal isoform of C4BPB, which is a multimeric protein that controls activation of the complement cascade via the classical pathway. C4BPB binds as a cofactor to C3b/C4b inactivator (C3bINA), which subsequently hydrolyzes the complement fragment C4b. In addition, C4BPB accelerates the degradation of the C4bC2a complex (C3 convertase) by detaching the complement fragment C2a. Furthermore, C4BPB interacts with anticoagulant protein S and with serum amyloid P component.

TIMP2 belongs to the TIMP gene family. The proteins encoded by this gene family are natural inhibitors of the matrix metalloproteinases, a group of peptidases that take part in degradation of the extracellular matrix. Besides having an inhibitory role against metalloproteinases, the encoded protein has a exclusive part among TIMP family members in its capability to directly suppress the proliferation of endothelial cells. Consequently, the encoded protein is crucial to the conservation of tissue homeostasis by suppressing the production of quiescent tissues as an answer to angiogenic factors, and by inhibiting protease activity in tissues undergoing renovation of the extracellular matrix.

Trafficking Protein Particle Complex 2-Like (TRAPPC2L) takes part in vesicular transport from endoplasmic reticulum to Golgi. TRAPPC2L is a part of the TRAPP small subunits family and is expressed in various organs like testis, liver, bladder, lung, spleen and brain.

Galectins are a family of animal lectins with an affinity for beta-galactosides. This family has at least 14 identified members. Galectins share similarities in the CRD (the carbohydrate recognition domain). Galectins are synthesized as cytosolic proteins. Though localized principally in the cytoplasm and lacking a classical signal peptide, galectins can also be stimulated to secretion by non-classical pathways or alternatively targeted to the nucleus. Galectins are involved in modulating cell-cell and cell-matrix interactions. Human Galectin-7 belongs to the prototypical Galectins containing a single CRD, which is initially identified in human epidermis as a monomer. The Galectin-7 expression is induced by tumor suppressor protein p53 and associated with apoptosis. Galectin-7 is a pro-apoptotic protein which functions intracellularlly upstream of JNK activation and mitochondrial cytochrome c release. The correlation of Galectin-7 with the UV-induced apoptosis of keratinocytes presents a critical mechanism in the maintenance of epidermal homeostasis. Human Galectin-7 is localized in both nucleus and cytoplasm.

RHOG belongs to the Rac subfamily of the Rho family of small G proteins. RHOG is a small monomeric GTP-binding protein (G protein), and is a key element of several intracellular signalling pathways. RHOG is needed for the formation of membrane ruffles during macropinocytosis. RHOG takes part in cell migration and is essential for the formation of cup-like structures during trans-endothelial migration of leukocytes. Similar to various small G proteins RHOG has a role in several cellular signalling mechanisms such as cell motility, gene transcription, endocytosis, neurite outgrowth, protection from anoikis and regulation of the neutrophil NADPH oxidase.

Complement C4c is a degradation product of C4b which is cleaved by C4b/C3b inactivator to yield C4d and C4c.
Complement C4c interacts with C1 and C2 to form C3 convertase of the classic activation pathway. Systemic lupus erythematosus (SLE) is often associated with congenital C4 deficiency. Reduced levels of components of the classic pathway (C1, C2, C4, C3) are common after such activation, e.g. in SLE, acute serum sickness and conditions associated with circulating immune complexes.

Albumin is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted albumin. Albumin is a soluble, monomeric protein which comprises about one-half of the blood serum protein. Albumin functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones and plays a role in stabilizing extracellular fluid volume. Mutations in this gene on chromosome 4 result in various anomalous proteins. Albumin is a globular unglycosylated serum protein of molecular weight 65,000. The human albumin gene is 16,961 nucleotides long from the putative 'cap' site to the first poly (A) addition site. It is split into 15 exons which are symmetrically placed within the 3 domains that are thought to have arisen by triplication of a single primordial domain.
HSA is widely used to stabilize blood volume generally from donors but the fear of contamination such as HIV & Hepatitis has enticed great interest in the recombinant form which is identical to the natural blood.

Histamine N-Methyltransferase or HNMT, is located in the cell cytosol. Sadenosyl-L-methionine acts as a methyl donor for HNMT which inactivates histamine. By inactivation of histamine, it affects the immune system’s response. HNMT acts on histamine in body tissues such as kidney, central nervous system and bronchus. The protein has a crucial part in the airway response to histamine & histamine degradation process and regulation.

Human T-lymphotropic virus (HTLV) is a human, single-stranded RNA retrovirus that causes T-cell leukemia and T-cell lymphoma. The virus activates a subset of T-helper cellscalled Th1cells. The result is a proliferation of Th1 cells and overproduction of Th1 related cytokines (mainly IFN-gamma and TNF-alpha). Feedback mechanisms of these cytokines cause a suppression of the Th2 lymphocytes and a reduction of Th2 cytokine production (mainly IL-4, IL-5, IL-10 and IL-13). The end result is a reduction in the ability of the infected host to mount an adequate immune response to invading organisms that require a predominantly Th2 dependant response (these include parasitic infections and production of mucosal and humoral antibodies).