Other Proteins

Cell adhesion protein that mediates homophilic cell adhesion in a calcium-independent manner (By similarity). Plays a role as coinhibitory receptor in immune response, insulin action and functions also as an activator during angiogenesis. Its coinhibitory receptor function is phosphorylation- and PTPN6 -dependent, which in turn, suppress signal transduction of associated receptors by dephosphorylation of their downstream effectors.Plays a role in immune response, of T-cells, natural killer (NK) and neutrophils.

Participates in at least several B-cell activation processes as well as of other cell types. It is a costimulator of DNA-synthesis. It induces the expression of class II MHC molecules on resting B-cells. It enhances both secretion and cell surface expression of IgE and IgG1. It also regulates the expression of the low affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes. Positively regulates IL31RA expression in macrophages. Stimulates autophagy in dendritic cells by interfering with mTORC1 signaling and through the induction of RUFY4.

Constitutes 1-2% of the total bone protein. It binds strongly to apatite and calcium.

Has neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons. Binds, in a calcium-dependent manner, to cultured neocortical neurons and promotes cell survival.

Type II interferon produced by immune cells such as T-cells and NK cells that plays crucial roles in antimicrobial, antiviral, and antitumor responses by activating effector immune cells and enhancing antigen presentation. Primarily signals through the JAK-STAT pathway after interaction with its receptor IFNGR1 to affect gene regulation. Upon IFNG binding, IFNGR1 intracellular domain opens out to allow association of downstream signaling components JAK2, JAK1 and STAT1, leading to STAT1 activation, nuclear translocation and transcription of IFNG-regulated genes. Many of the induced genes are transcription factors such as IRF1 that are able to further drive regulation of a next wave of transcription. Plays a role in class I antigen presentation pathway by inducing a replacement of catalytic proteasome subunits with immunoproteasome subunits. In turn, increases the quantity, quality, and repertoire of peptides for class I MHC loading. Increases the efficiency of peptide generation also b

Non-enzymatic component of C3 and C5 convertases and thus essential for the propagation of the classical complement pathway. Covalently binds to immunoglobulins and immune complexes and enhances the solubilization of immune aggregates and the clearance of IC through CR1 on erythrocytes.

PCK1 (Phosphoenolpyruvate carboxykinase 1; also PEPCK-C [cytosolic]) is a monomeric, 67-68 kDa member of the PEP carboxykinase family of enzymes. It is expressed in postnatal cells such as mammary epithelium, white and brown adipocytes, skeletal muscle cells and hepatocytes. PCK1 has multiple functions, some of which are cell-specific. In particular, PCK1 has both cataplerotic (Greek: to fill down, or remove) and anaplerotic (to fill up, or replace) activity, where it removes and replaces elements of the TCA cycle. It is also gluconeogenic, and promotes glucose formation via PEP generation. Finally, it is glyceroneogenic, creating glycerol-3-phosphate that is used to reesterify and store just-released free fatty acids in adipocytes. It contains one kinase domain (aa 27-615), and two potential acetylation sites at Lys70 and 71. There are four potential splice forms. Two have alternative start sites at Met460 and Met315, while two others show a deletion of aa 34-546, plus a thre

EGF is the founding member of the EGF-family of proteins. Members of this protein family have highly similar structural and functional characteristics. EGF contains 9 EGF-like domains and 9 LDL-receptor class B repeats. Human EGF is a 645-Da protein with 53 amino acid residues and three intramolecular disulfide bonds. As a low-molecular-weight polypeptide, EGF was first purified from the mouse submandibular gland, but since then it was found in many human tissues including submandibular gland, parotid gland. It can also be found in human platelets, macrophages, urine, saliva, milk, and plasma. EGF is a growth factor that stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. It results in cellular proliferation, differentiation, and survival. Salivary EGF, which seems also regulated by dietary inorganic iodine, also plays an important physiological role in the maintenance of oro-esophageal and gastric tissue integ

Angiopoietin-2 (Ang-2; also ANGPT2) is a secreted glycoprotein that plays a complex role in angiogenesis and inflammation. Both Ang-2 and the related Angiopoietin-1 (Ang-1) are ligands for the receptor tyrosine kinase Tie-2. While Ang-1 is a potent Tie 2 agonist, Ang-2 may act as either a Tie-2 antagonist or agonist, depending upon its state of multimerization. The higher the order of oligomer, the more effective Ang-2 becomes as a Tie-2 agonist. The short isoform appears to block the binding of either Ang-1 or full-length Ang-2 to Tie-2. Ang-2 functions as a pro-angiogenic factor, although it can also induce EC death and vessel regression. Upon its release from quiescent EC, it regulates vascular remodeling by promoting EC survival, proliferation, and migration and destabilizing the interaction between EC and perivascular cells. In addition, ANG-2 is strongly expressed in the vasculature of many tumors and it has been suggested that ANG-2 may act synergistically with other cytokines s