Search results

HSP70 is a human heat shock protein. HSP-70 is an important part of the cell's machinery for protein folding, and help to protect cells from stress. In most species, there are many proteins that belong to the HSP70 family. Some of these are only expressed under stress conditions, while some are present in cells under normal growth conditions and are not heat-inducible. They can be found in different cellular compartments (nuclear, cytosolic, mitochondrial, endoplasmic reticulum, etc...).

DNAL4 is a member of the dynein light chain family. DNAL4 is a component of the dynein motor complex in cells that converts the chemical energy contained in ATP into the mechanical energy of movement. Dynein transports various cellular cargos by moving the length of cytoskeletal microtubules towards the minus-end of the microtubule, which is typically oriented towards the cell center.

Arfaptin 2 (ARFIP2) is a Rac1 binding protein essential for Rac-mediated actin polymerization and the succeeding formation of membrane ruffles and lamellipodia. ARFIP2 is a putative target protein of ADP-ribosylation factor. ARFIP2 is also involved in membrane ruffling. ARFIP2 expression is increased at sites of neurodegeneration. In addition, ARFIP2 interacts with the ADP ribosylation factor ARF6, a GTPase which associates with the plasma membrane and intracellular endosome vesicles, in a GTP dependent mode. Furthermore, Arfaptin 2 controls the aggregation of mutant Huntingtin protein by weakening proteasome function.

ADP-ribosylation factor-like protein 5B (ARL5B) is a member of a family of proteins which are structurally similar to ADP-ribosylation factors. ARLs and ARFs belong to the RAS superfamily of regulatory GTPases. ARL5B is most closely related to ARL5, with which it shares 80% sequence identity. Furthermore, Human ARL5B shares 100% identity with mouse ARL8 and 71% identity with the Drosophila homolog.

Actin-related protein 2/3 complex subunit 3 (ARPC3) which Belongs to the ARPC3 family is one of 7 subunits of the human Arp2/3 protein complex. The Arp2/3 complex is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. ARPC3 which is localized to the cytoplasm and cytoskeleton, interacts with p20-ARC and takes part in the structural integrity of the protein complex.

cAMP-regulated phosphoprotein 19 (ARPP19) is protein phosphatase inhibitor which specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-62 during mitosis, ARPP19 specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, a vital condition to maintain cyclin-B1-CDK1 activity high during M phase. ARPP19 protein may indirectly boost GAP-43 expression. The 19 kDa cAMP-regulated phosphoprotein has a role in regulating mitosis by obstructing protein phosphatase-2A.

Autophagy Related 3 (ATG3) is a conjugating enzyme essential for the cytoplasm to vacuole transport (Cvt), autophagy, and mitochondrial homeostasis. ATG3 is localizes to the cytoplasm and is expressed in tissues with predominant levels found in kidney, placenta, liver, heart and skeletal muscle. ATG3 catalyzes a reaction which is necessary for autophagy. That reaction is the formation of the Atg8-phosphatidylethanolamine (ATG-PE) conjugate.

ATOH1 activates E box-dependent transcription in collaboration with TCF3/E47, but the activity is entirely provoked by the negative regulator of neurogenesis HES1. ATOH1 takes part in the differentiation of divisions of neural cells by activating E box-dependent transcription.

ATPaseTransporting Beta 2 (ATP1B2) is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na+ and K+ ions across the plasma membrane. The precise function of the beta-2 subunit is not known. The ATP1B2 protein is composed of 3 subunits: alpha (catalytic), beta and gamma.

EFNA3 belongs to the ephrin (EPH) family. The ephrins and EPH-related receptors include thelargest subfamily of receptor protein-tyrosine kinases which have been implicated in mediating developmental events, especially in the nervous system and in erythropoiesis. Ephrins are divided into the ephrin-A (EFNA) class and the ephrin-B (EFNB) class, based on their structures and sequence relationships. The Ephrins from the EFNA class are anchored to the membrane by aglycosylphosphatidylinositol linkage, while the others from the EFNB class are transmembrane proteins.

IGFBP5 is a member of the insulin-like growth factor binding protein (IGFBP) family and encodes a protein with an IGFBP domain and a thyroglobulin type-I domain. The protein forms a ternary complex with insulin-like growth factor acid-labile subunit (IGFALS) and either insulin-like growth factor (IGF) I or II. In this form, it circulates in the plasma, prolonging the half-life of IGFs and altering their interaction with cell surface receptors. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.

STIP1 is an adaptor protein that mediates the functions of HSP70 & HSP90 in protein folding. STIP1 supports the transfer of proteins from HSP70 to HSP90 by binding together HSP90 and substrate-bound HSP70. STIP1 stimulates the ATPase activity of HSP70 and inhibits the ATPase activity of HSP90, suggesting that it regulates both the conformations and ATPase cycles of these chaperones. STIP1 genetic variations are involved in regulating corticosteroid response in asthmatic subjects with reduced lung function.

Bone Morphogenetic protein-8b (BMP8B) belongs to a family of secreted signaling molecules which can induce ectopic bone growth. BMP8B is known for having a possible bone inductive activity as it is related to BMP5 and BMP7. BMP8B is the osteoinductive factor accountable for epithelial osteogenesis.

Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence.

Phosphoribosylaminoimidazole Carboxylase (PAICS) is an enzyme involved in nucleotide biosynthesis and particularly in purine biosynthesis. PAICS is a bifunctional enzyme containing phosphoribosylaminoimidazole carboxylase activity at its N-terminal region and phosphoribosylaminoimidazole succinocarboxamide synthetase at its C-terminal region. PAICS catalyzes the conversion of 5'-phosphoribosyl-5-aminoimidazole(AIR) into 5'-phosphoribosyl-4-carboxy-5-aminoimidazole (CAIR) as described in the reaction. PAICS catalyzes steps six and seven of purine biosynthesis.

The PARK7 is a ubiquitously expressed protein involved in various cellular processes including spermatogenesis and fertilization, cancer, RNA-binding, androgen-receptor signaling and oxidative stress. Mutations in the PARK7 are the cause of autosomal recessive early-onset Parkinson’s disease 7 (Park7).

PDK1 takes part in the regulation of enzymatic activity of mammalian pyruvate dehydrogenase which is part of a mitochondrial multienzyme complex to catalyze the oxidative decarboxylation of pyruvate and is one of the major enzymes responsible for the regulation of homeostasis of carbohydrate fuels in mammals. PDK1 inhibits glioblastoma growth. PDK1 inhibits the mitochondrial pyruvate dehydrogenase complex by phosphorylation of the e1 alpha subunit, therefore contributing to the regulation of glucose metabolism. PDK1 kinase activity is negatively regulated by binding to 14-3-3.

CCNA2 is a member of the highly conserved cyclin family, whose members are characterized by a dramatic periodicity in protein abundance through the cell cycle. Cyclins act as regulators of CDK kinases. Various cyclins demonstrate distinct expression and degradation patterns which contribute to the temporal coordination of each mitotic event. Contrary to cyclin A1, which is present only in germ cells, CCNA2 is expressed in all tissues tested. CCNA2 binds and activates CDC2 or CDK2 kinases, and consequently promotes both cell cycle G1/S and G2/M transitions.

CTK-19 is a member of the keratin family. The keratins are intermediate filament proteins responsible for the structural integrity of epithelial cells and are subdivided into cytokeratins and hair keratins. The type I cytokeratins consist of acidic proteins which are arranged in pairs of heterotypic keratin chains. Unlike its related family members, this smallest known acidic cytokeratin is not paired with a basic cytokeratin in epithelial cells. It is specifically expressed in the periderm, the transiently superficial layer that envelopes the developing epidermis. The type I cytokeratins are clustered in a region of chromosome 17q12-q21.

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.

GOPC is a PDZ domain-containing Golgi protein which binds the extreme C terminus of proteins in a sequence-specific manner. GOPC participates in intracellular protein trafficking and degradation. GOPC regulates CFTR chloride currents and acid-induced ACCN3 currents by modulating cell surface expression of both channels. GOPC regulates the intracellular trafficking of the ADR1B receptor. GOPC takes part in autophagy. GOPC over expression results in CFTR intracellular retention and degradation in the lysosomes.

Phosphoserine aminotransferase (PSAT1) catalyzes the conversion of 3-phosphohydroxypyruvate into 3-phosphoserine which is dephosphorylated consequently by phosphoserine phosphatase to form L-serine. PSAT1 is probably a phosphoserine aminotransferase, based on similarity to proteins in mouse, rabbit, and Drosophila. PSAT1 is expressed at high levels in the brain, liver, kidney and pancreas, and very weakly expressed in the thymus, prostate, testis and colon. Defects in the PSAT1 gene are the cause of phosphoserine aminotransferase deficiency (PSATD). PSATD is distinguished biochemically by low plasma and cerebrospinal fluid concentrations of serine and glycine and clinically by intractable seizures, acquired microcephaly, hypertonia, and psychomotor retardation.

Proteasome 26S Subunit, Non-ATPase 5, also known as PSMD5 is a member of the proteasome subunit S5B/HSM3 family. The 26S proteasome is an enzymatic complex which degrades ubiquitinated proteins in eukaryotic cells. Furthermore, PSMD5 acts as a chaperones which is involved in the assembly of the 26s proteasome, particularly of the base subcomplex of the PA700/19S regulatory complex. PSMD5 is full of dileucine repeats, which have been involved in trafficking of various transmembrane proteins.