Search results

The bone morphogenetic protein (BMP) receptors are a family of transmembrane serine/threonine kinases that include the type I receptors BMPR1A and BMPR1B and the type II receptor BMPR2. These receptors are also closely related to the receptors, ACVR1 and ACVR2. The ligands of these receptors are members of the TGF-beta superfamily. TGF-betas transduce their signals through the formation of heteromeric complexes with 2 different types of serine (threonine) kinase receptors: type I receptors of about 50-55 kD and type II receptors of about 70-80 kD. Type II receptors bind ligands in the absence of type I receptors, but they require their respective type I receptors for signaling, whereas type I receptors require their respective type II receptors for ligand binding.

NTRK2 plays a role in the growth and the development of the central and the peripheral nervous systems using the regulation of neuron proliferation, migration, survival, differentiation, and synapse production. NTRK2 is a receptor for B-DNF and NT4. NTRK2 binds to neurotrophin-3 which regulates neuron survival through NTRK2. NTRK-2 activates numerous effectors such as SHC-1, SH2B-1, PLCG-1 and SH2B-2 that control overlapping signaling cascades.

C-Src Tyrosine Kinase, also known as CSK, regulates cell growth, migration, differentiation, and immune response. CSK Phosphorylates tyrosine residues located in the C-terminal tails of Src-family kinases. CSK is a protein coding gene which suppresses signaling by several surface receptors. Among CSK's related pathways are PI-3K cascade and Signaling by FGFR.

Ephrin type-B receptor 4 isoform b (Ephb4) belongs to the Eph receptor tyrosine kinase family which functions in neuronal guidance and mediate venal/arterial separation. EPHB4-mediated forward signaling regulates cellular repulsion and segregation form EFNB2-expressing cells. Furthermore, Ephb4 has a role in postnatal blood vessel remodeling, morphogenesis and permeability and is therefore essential in the context of tumor angiogenesis.

Kallikrein-3 (KLK3) is a part of the kallikrein-related peptidase family. Kallikreins are a subgroup of serine proteases having various physiological functions. Numerous kallikreins take part in carcinogenesis and some may be prospective cancer and other disease biomarkers. Kallikrein-3 is 1 of the 15 kallikrein subfamily members located in a cluster on chromosome 19 and is a protease present in seminal plasma. KLK3 hydrolyzes semenogelin-1 consequently leading to the liquefaction of the seminal coagulum. KLK3 acts normally in the liquefaction of seminal coagulum, probably by hydrolysis of the high molecular mass seminal vesicle protein. Serum level of the KLK3 protein, called PSA in the clinical setting, is beneficial in the diagnosis and monitoring of prostatic carcinoma.

Neurotrophic Receptor Tyrosine Kinase 3 (NTRK3)belongs to the receptor tyrosine kinases family and is a high affinity catalytic receptor of neurotrophin NT-3. NTRK3 mediates multiple effects of this neurotrophic factor, which includes neuronal differentiation and survival. NTRK3 inducesvarious pleiotorpic responses in malignant cells, including enhanced tumor cell invasiveness and chemotoxis.Increased NTRK3 expression was observed in neuroblastoma, medulloblastoma, and in neuroectodermal brain tumors.

TPRKB is a member of the CGI121/TPRKB family. TPRKB is localized to nucleus and cytoplasm and is ubiquitously expressed. TPRKB is known to cooperate with TP53RK/PRPK.

Calmodulin-2 acts as an intracellular calcium sensor protein. When the intracellular Ca2+ concentration increases, calmodulin can bind up to four Ca2+, changing its conformation and regulating cellular functions such as activation or inhibition of a large number of enzymes, ion channels, and receptors. P53 protein stimulates CALM2 gene expression in 041 cells. CALM-2 is involved in the processes of Ca(2+)-induced neuronal cell death and the blockage of calmodulin attenuates brain injury after cerebral ischemia. Calmodulin-2 mediates the control of a large number of enzymes and other proteins by ca(2+). among the enzymes to be stimulated by the calmodulin-ca(2+) complex are a number of protein kinases and phosphatases.

The bone morphogenetic protein (BMP) receptors are a family of transmembrane serine/threonine kinases that include the type I receptors BMPR1A and BMPR1B and the type II receptor BMPR2. These receptors are also closely related to the activin receptors, ACVR1 and ACVR2. The ligands of these receptors are members of the TGF-beta superfamily. TGF-betas and activins transduce their signals through the formation of heteromeric complexes with 2 different types of serine (threonine) kinase receptors: type I receptors of about 50-55 kD and type II receptors of about 70-80 kD. Type II receptors bind ligands in the absence of type I receptors, but they require their respective type I receptors for signaling, whereas type I receptors require their respective type II receptors for ligand binding.

Fructosamine 3 Kinase (FN3K) catalyzes the phosphorylation of fructosamines which may result in deglycation, the non-enzymatic reaction of glucose with primary amines followed by Amadori re-arrangement. Phosphorylation of fructosamines instigates metabolism of the modified amine and brings about the de-glycation of fructoselysine and of glycated proteins. A high concentration of glucose may affect non-enzymatic oxidation of proteins by reaction of glucose and lysine residues (glycation). Fructosamines, the proteins altered in this way, are less active or functional.

MAP3K12 Binding Inhibitory Protein 1 (MBIP) is a part of the ATAC complex which consists of histones H3 and H4 with a histone acetyltransferase activity. MBIP inhibits the MAP3K12 activity in order to induce the activation of the JNK/SAPK pathway.

PFKM is a regulatory glycolytic enzyme that converts fructose 6-phosphate and ATP into fructose 1,6-bisphosphate (through PFK-1), fructose 2,6-bisphosphate (through PFK-2) and ADP. Three phosphofructokinase isozymes exist in humans: muscle, liver and platelet. Mutations in PFKM gene have been related with glycogen storage disease type VII, also identified as Tarui disease.

Cyclin-dependent kinase inhibitor 1B (CDKN1B) is a member of the Cip/Kip family of cyclin dependent kinase (Cdk) inhibitor proteins. The CDKN1B protein binds to and prevents the activation of cyclin E-CDK2 or cyclin D-CDK4 complexes, and so controls the cell cycle progression at G1. CDKN1B is often referred to as a cell cycle inhibitor protein since its major function is to stop or slow down the cell division cycle. The degradation of the CDKN1B protein, which is triggered by its CDK dependent phosphorylation and ensuing ubiquitination by SCF complexes, is compulsory for the cellular transition from inactive to the proliferative state.

TIE-1 (tyrosine kinase with Ig and EGF homology domains 1) and TIE-2/Tek comprise a receptor tyrosine kinase (RTK) subfamily with unique structural characteristics: two immunoglobulin-like domains flanking three epidermal growth factor (EGF)-like domains and followed by three fibronectin type III-like repeats in the extracellular region and a split tyrosine kinase domain in the cytoplasmic region. These receptors are expressed primarily on endothelial and hematopoietic progenitor cells and play critical roles in angiogenesis, vasculogenesis and hematopoiesis. Human TIE-1 cDNA encodes a 1124 amino acid (aa) residue precursor protein with an 18 residue putative signal peptide, a 727 residue extracellular domain and a 354 residue cytoplasmic domain. Whereas two ligands have been described for TIE-2 [angiopoietin-1 (Ang1) and angiopoietin-2 (Ang2)], so far no ligand was found for TIE-1.

YWHAB belongs to the 14-3-3 family of proteins which are in charge for signal transduction by binding to phosphoserine-containing proteins. YWHAB is found in both plants and mammals. YWHAB protein interacts with RAF1 and CDC25 phosphatases,thus linking mitogenic signaling and the cell cycle machinery. YWHAB is an adapter protein involved in the regulation of a large spectrum of both general and specialized signaling pathway. YWHAB binds to a large number of proteins by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.

Dysbindin domain-containing protein 2 (DBNDD2) is a member of the dysbindin family. DBNDD2 regulates the activity of casein kinase-1 and inhibits CSNK1D autophosphorylation (in vitro). DBNDD2 also interacts with CSNK1D and CSNK1E. DBNDD2 is detected in brain.

Proprotein Convertase Subtilisin/Kexin Type 1 Inhibitor (PCSK1N) takes part in the control of the neuroendocrine secretory pathway. PCSK1N inhibits prohormone convertase 1, which regulates the proteolytic cleavage of neuroendocrine peptide precursors. PCSK1Nslows down convertase-mediated processing of proopiomelanocortin and proenkephalin and also monitors the intracellular timing of PCSK1.

CDKN2C is a member of the CDKN2 cyclin-dependent kinase inhibitor family. CDKN2C cooperates with CDK4 or CDK6, and inhibits the activation of the CDK kinases, therefore acts as a cell growth regulator which regulates cell cycle G1 progression. CDKN2C suppresses the cell growth and proliferation with a correlated dependency on endogenous retinoblastoma protein RB. Studies in the knockout mice show CDKN2C takes part in regulating spermatogenesis, in addition to suppressing tumorigenesis.

YWHAB belongs to the 14-3-3 family of proteins which are in charge for signal transduction by binding to phosphoserine-containing proteins. YWHAB is found in both plants and mammals. YWHAB protein interacts with RAF1 and CDC25 phosphatases,thus linking mitogenic signaling and the cell cycle machinery. YWHAB is an adapter protein involved in the regulation of a large spectrum of both general and specialized signaling pathway. YWHAB binds to a large number of proteins by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.

YWHAZ accession number NP_ 663723 belongs to the 14-3-3 family of proteins which are in charge for checkpoint control, apoptotic & nutrient sensing pathways as well as signal transduction by binding to phosphoserine-containing proteins. The 14-3-3 protein family is found in both plants and mammals, and KCIP-1 protein is 99% identical to the mouse, rat and sheep orthologs. KCIP-1 interacts with IRS1 protein, signifying a role in regulating insulin. 14-3-3 proteins are highly conserved and ubiquitously expressed. YWHAZ function as an adapter protein involved in the regulation of a large spectrum of both general and specialized signaling pathway. YWHAZ binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.

AK1 is a small ubiquitous enzyme which is essential for maintenance and cell growth. It is involved in the regulation of adenine nucleotide composition within a cell by catalyzing the reversible transfer of the terminal phosphate group between ATP and AMP. The AK1 protein is found in the cytosol of skeletal muscle, brain and erythrocytes. Defects in the AK1 gene are the cause of a form of hemolytic anemia.

PKLR is a pyruvate kinase which catalyzes the transphosphorylation of phohsphoenolpyruvate into pyruvate and ATP. That is the rate-limiting step of glycolysis. PKLR gene encodes the L- and R-type isoenzymes through alternate splicing events controlled by different promoters. L-type isoform can also appear as a tetramer and is upregulated by glucose with implications in maturity-onset diabetes of the young.

Phosphomevalonate kinase (PMVK) is a cytosolic enzyme. PMVK is expressed highly in the heart, liver, skeletal muscle, kidney and pancreas and slightly lower in the brain, placenta, and lung. PMVK catalyzes the conversion of mevalonate 5-phosphate into mevalonate 5-diphosphate in the fifth reaction of the cholesterol biosynthetic pathway. Induced by sterol, PMVK participates in isopentenyl diphosphate biosynthesis via the mevalonate pathway.