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Secretoglobin Family 1D, Member 1 (SCGB1D1) belongs to the lipophilin subfamily, part of the uteroglobin superfamily, and is an ortholog of prostatein (which is the major secretory glycoprotein of the rat ventral prostate gland). SCGB1D1 binds androgens and other steroids. In addition SCGB1D1 binds chemotherapeutic drugs during the prostate cancer treatment. Steroid hormones regulate the SCGB1D1 transcription. SCGB1D1 is secreted into extracellular space. SCGB1D1 gene product represents one component of a heterodimeric molecule found in human tears whose elution profile is consistent with prostatein (which is a tetrameric molecule comprised of 3 peptide components in heterodimers).

SCGN is a secreted calcium-binding protein which is found in the cytoplasm. It is related to calbindin D-28K and calretinin. Secretagogin is involved in KCL-stimulated calcium flux and cell proliferation.
Secretagogin plays a role in human non-functional pituitary adenomas.

CAB39 protein and STE20-related adaptor-alpha pseudo kinase, form a regulatory complex that is able of stimulating the activity of the LKB1 tumor suppressor protein kinase. CAB39 takes part as a scaffolding component of the STK11/STRAD complex and regulates STK11 activity and cellular localization.

CCNB2 is a member of the cyclin family. CCNB2 is vital for regulation of the cell cycle at the G2/M (mitosis) transition. CCNB2 cooperates with the CDK1 protein kinase to create a serine/threonine kinase holoenzyme complex recognized as maturation promoting factor (MPF).

UL16 Binding Protein 3 (ULBP3) is a ligand for the NKG2D receptor in NK cells. ULBPs activate different signaling pathways resulting in the production of cytokines and chemokines. ULBP3 is a ligand for the KLRK1/NKG2D receptor, along with at least ULBP1 and ULBP2. Binding of ULBPs ligands to KLRK1/NKG2D stimulates calcium mobilization and activation of the JAK2, STAT5, ERK and PI3K kinase/Akt signal transduction pathway. ULBP3 has lower affinity for KLRK1/NKG2D compared to ULBP1 and ULBP2 and stimulates weaker signaling responses than does ULBP2 or ULBP1.

C-Type Lectin Domain Family 10, Member A (CLEC10A) is a part of the C-type lectin superfamily. CLEC10A is expressed in immature myeloid dendritic cells and alternatively activated macrophages. CLEC10A takes part in regulating adaptive and innate immune responses and also binds in a calcium dependent way to terminal galactose and N-acetylgalactosamine, linked to serine or threonine.

COPZ1 is a member of the adaptor complexes small subunit family. Coatomer is an oligomeric complex which contains as a minimum the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. The zeta subunit has a part in regulating the coat assembly and, therefore, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex.

Serpin Peptidase Inhibitor, Clade B Member 8 (SERPINB8) belongs to the ov-serpin subfamily, which, compared with the archetypal serpin PI1, is characterized by a high degree of homology to chicken ovalbumin, absence of N- and C-terminal extensions, lack of a signal peptide, and a serine instead of an asparagine residue at the penultimate position. The superfamily of high molecular weight serine proteinase inhibitors (serpins) control various intracellular and extracellular processes such as complement activation, fibrinolysis, coagulation, cellular differentiation, tumor suppression, apoptosis, and cell migration.

Peptidyl-prolyl cis-trans isomerase FKBP1B (FKBP1B) belongs to the immunophilin protein family which has a role in immunoregulation and basic cellular processes involving protein folding and trafficking. FKBP1B is a cis-trans prolyl isomerase which binds the immunosuppressants FK506 and rapamycin. FKBP1B is extremely similar to the FK506-binding protein 1A. The physiological role of FKBP1B is thought to be in excitation-contraction coupling in cardiac muscle.

CCL28 is part of the subfamily of small cytokine CC genes. CCL28 shows chemotactic activity for resting CD4 or CD8 T cells and eosinophils. CCL28 binds to chemokine receptors CCR3 and CCR10. CCL28 is involved in the physiology of extracutaneous epithelial tissues, including diverse mucosal organs. CCL28 mediates mucosal immunity in HIV exposure and infection. CCL28 is involved in the pathogenesis of inflammatory skin diseases.
Human CCL28 cDNA encodes a 127 amino acid residue precursor protein with a putative 22 amino acid residue signal peptide that is cleaved to produce the 105 amino acid residue mature protein. Human and mouse CCL28 are highly conserved, sharing 83% amino acid identity in their mature regions. CCL28 shares the most homology with CCL27/CTACK. Human and mouse CCL28 RNA expression was found to be highest in normal and pathologic colon with the protein being expressed by epithelial cells. Human CCL28 RNA was also present in normal and asthmatic lung tissues.

Chemokine (C-C motif) ligand 2 (CCL2) is a small cytokine belonging to the CC chemokine family that is also known as monocyte chemotactic protein-1 (MCP-1). It is found at the site of tooth eruption and bone degradation. In the bone, CCL2 is expressed by mature osteoclasts and osteoblasts and is under the control of nuclear factor ?B (NF?B). CCL2 recruits immune cells, such as monocytes, to sites of tissue injury and infection. This chemokine is produced as a protein precursor containing signal peptide of 23 amino acids and a mature peptide of 76 amino acids. It is a monomeric polypeptide, with a molecular weight of approximately 13kDa. As with many other CC chemokines, CCL2 is located on chromosome 17 in humans. The cell surface receptors that bind CCL2 are CCR2 and CCR5.

Chemokine (C-C motif) ligand 2 (CCL2) is a small cytokine belonging to the CC chemokine family that is also known as monocyte chemotactic protein-1 (MCP-1). It is found at the site of tooth eruption and bone degradation. In the bone, CCL2 is expressed by mature osteoclasts and osteoblasts and is under the control of nuclear factor ?B (NF?B). CCL2 recruits immune cells, such as monocytes, to sites of tissue injury and infection. This chemokine is produced as a protein precursor containing signal peptide of 23 amino acids and a mature peptide of 76 amino acids. It is a monomeric polypeptide, with a molecular weight of approximately 13kDa. As with many other CC chemokines, CCL2 is located on chromosome 17 in humans. The cell surface receptors that bind CCL2 are CCR2 and CCR5.

Heterogeneous Nuclear Ribonucleoprotein A/B (HNRNPAB) is a member of the subfamily of ubiquitously expressed heterogeneous nuclearribonucleoproteins (hnRNPs). The hnRNPs are produced by RNA polymerase II and are components of theheterogeneous nuclear RNA (hnRNA) complexes. They are linked with pre-mRNAs in the nucleus and seem to influence pre-mRNA processing and further aspects of mRNA metabolism and transport. Whereas all of the hnRNPsare present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. HNRNPAB, which binds to one of the components of the multiproteineditosome complex, has two repeats of quasi-RRM (RNA recognition motif) domains that bind to RNAs. Among the diseases associated with HNRNPAB are wells syndrome, and cystic fibrosis.

Growth hormone receptor, also known as GHR is part of the cytokine receptor family. GHR binds 2 receptor molecules and in this manner induces signal transduction through receptor dimerization. Furthermore, at high concentrations, growth hormone performs as an antagonist since there is a large difference in affinities at the respective binding sites. The antagonist action can be enhanced further by reducing binding in the low affinity binding site.

Heterotrimeric guanine nucleotide-binding proteins (G proteins) which integrate signals between receptors and effector proteins, are comprised of an alpha, a beta and a gamma subunit. The alpha, beta and gamma subunits are encoded by families of related genes. GNB1 encodes a beta subunit. Beta subunits are vital regulators of alpha subunits, as well as of certain signal transduction receptors and effectors. G proteins are involved as a modulator or transducer in numerous transmembrane signaling systems. The beta and gamma chains are necessary for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.

FABP6 also called ileal fatty acid binding protein, is part of the small family of highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. FABP6 cytosolic protein binds bile acid. FABP6 plays a role in fatty acid uptake, transport, and metabolism. FABP6 stimulates gastric acid and pepsinogen secretion. Seems to be able to bind to bile salts and bilirubins. FABP6 expression is restricted in the small intestine to the ileum where it is involved in the enterohepatic circulation of bile acids. Alternate transcription promoters generate 2 transcript variants, encoding a 128 aa and a 177 aa residue protein. Human FABP6 isoform 2 contains 128 amino acid residues and is acetylated on Ala2. FABP6 binds together fatty acids and bile acids and is directly involved in fatty acid transport and metabolism.

PEST proteolytic signal containing nuclear protein (PCNP) is a nuclear protein involved in cell cycle regulation and tumorigenesis. The PCNP protein is ubiquitinated post-translationally by NIRF (an ubiquitin ligase). The PCNP exists as 3 isoforms produced by alternative splicing events.

Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Natural Human Fractalkine is produced as a long protein (373-amino acid) with an extended mucin-like stalk and a chemokine domain on top. The mucin-like stalk permits it to bind to the cell surface. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.

Chemokine (C-X-C motif) ligand 2 (CXCL2) is a small cytokine belonging to the CXC chemokine family that is also called macrophage inflammatory protein 2-alpha (MIP2-alpha), Growth-regulated protein beta (Gro-beta) and Gro oncogene-2 (Gro-2). CXCL2 is 90% identical in amino acid sequence as a related chemokine, CXCL1. This chemokine is secreted by monocytes and macrophages and is chemotactic for polymorphonuclear leukocytes and hematopoietic stem cells. The gene for CXCL2 is located on human chromosome 4 in a cluster of other CXC chemokines. CXCL2 mobilizes cells by interacting with a cell surface chemokine receptor called CXCR2.

Charged multivesicular body protein 1b (CHMP1B) is a member of the chromatin-modifying protein/charged multivesicular body protein (CHMP) family. CHMP1B is a possible peripherally associated component of the ESCRT-III (endosomal sorting required for transport complex III) which is involved in MVBs (multivesicular bodies) formation and sorting of endosomal cargo proteins into MVBs. The MVBs contain ILVs (intraluminal vesicles) which are created by invagination and scission from the limiting membrane of the endosome and generally are transported to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids.

Pre-mRNA-splicing factor SYF2 (SYF2) may be involved in pre-mRNA splicing. The SYF2 protein interacts with cyclin D-type binding-protein 1, which is believed to be a cell cycle regulator at the G1/S transition. SYF2 is amply expressed in the heart, skeletal muscle and kidney and is expressed at lower levels in other tissues.

Cyclin B1 (CCNB1) is a regulatory protein involved in mitosis. CCNB1 creates a complex with p34(cdc2) to form the maturation-promoting factor (MPF). CCNB1 is vital for the control of the cell cycle at the G2/M (mitosis) transition. CCNB1 builds up steadily during the G2 and is immediately destroyed at mitosis. The 2 alternative transcripts produce a constitutively expressed transcript and a cell cycle-regulated transcript which is expressed predominantly during G2/M phase. These transcripts are a result of alternate transcription initiation sites.

C-type Lectin Domain Family 2, Member B (CLEC2B) belongs to the C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily. Members of the CTL/CTLD family share a common protein fold and have various functions, such as cell adhesion, cell-cell signaling, glycoprotein turnover, and roles in inflammation and immune response. The CLEC2B gene is closely connected to other CTL/CTLD superfamily members on chromosome 12p13 in the natural killer gene complex region. CLEC2B is expressed preferentially in lymphoid tissues, and in most hematopoietic cell types.

Adiponectin is a hormone exclusively expressed from adipose tissue. Many studies demonstrate that adiponectin has direct anti-diabetic, anti-atherogenic and anti-inflammatory functions. APM-1 can increase insulin sensitivity of skeletal muscle, attenuate hepatic lipogenesis and luconeogenesis, regulate NO production in endothelial cells, inhibit proliferation of smooth muscle cells and prevent lipid accumulation of macrophage cells.
In the circulation, adiponectin is present as three different oligomeric complexes, including the high molecular weight (HMW), the middle molecular weight (MMW, also called hexamer) and low molecular weigh (MMW, also called trimer) forms 8. Different oligomeric complex of adiponectin activates different signaling pathways and exerts distinct functions.