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Receptor for the neuroprotective and glioprotective factor prosaposin. Ligand binding induces endocytosis, followed by an ERK phosphorylation cascade.

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Protein kinases comprise a large group of encoded factors that regulate cellular processes by catalyzing the transfer of a phosphate group to a hydroxyl acceptor in serine, threonine or tyrosine residues (1,2). Kinases are capable of influencing the oncogenic potential of cell sytems at the level of oncoprotein or tumor suppressor protein phosphorylation states (1,2). STAP-2 is a protein that contains a pleckstrin homology (PH) domain and an SH2 domain, and associates with BRK (3). BRK (breast tumor kinase, Sik) is a 451 amino acid, nonreceptor protein-tyrosine kinase that is overexpressed in breast tumors and metastatic melanoma cell lines (4). Similar to the Src family of intracellular kinses, BRK is comprised of an SH3 domain, an SH2 domain, and a catalytic domain (5). STAP-2 is susceptiple to tyrosine phosphorylation and may be invovled in tyrosine kinase-mediated signaling cascades, whose aberrant function may lead to metastis (3).

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Probable tyrosine protein-kinase, which has strong transforming capabilities on a variety of cell lines. When overexpressed, it can also induce tumor cell invasion as well as metastasis in distant organs. May act by activating both MAP kinase and phosphatidylinositol 3'-kinases (PI3K) pathways (By similarity).

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This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.

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Receptor on natural killer (NK) cells for HLA-C alleles (HLA-Cw1, HLA-Cw3 and HLA-Cw7). Inhibits the activity of NK cells thus preventing cell lysis.

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Acts as a sequence specific DNA binding transcriptional activator or repressor. The isoforms contain a varying set of transactivation and auto-regulating transactivation inhibiting domains thus showing an isoform specific activity. Isoform 2 activates RIPK4 transcription. May be required in conjunction with TP73/p73 for initiation of p53/TP53 dependent apoptosis in response to genotoxic insults and the presence of activated oncogenes. Involved in Notch signaling by probably inducing JAG1 and JAG2. Plays a role in the regulation of epithelial morphogenesis. The ratio of DeltaN-type and TA*-type isoforms may govern the maintenance of epithelial stem cell compartments and regulate the initiation of epithelial stratification from the undifferentiated embryonal ectoderm. Required for limb formation from the apical ectodermal ridge. Activates transcription of the p21 promoter.

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Functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs (By similarity). Involved in bone remodeling and homeostasis. In collaboration with RELA/p65 enhances NFATc1 promoter activity and positively regulates RANKL-induced osteoclast differentiation.

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Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F3 binds specifically to RB1 in a cell-cycle dependent manner. Inhibits adipogenesis, probably through the repression of CEBPA binding to its target gene promoters (By similarity).

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TSC-36 is a secreted extracellular glycoprotein. The amino acid sequence of TSC-36 is similar to follistatin, an inhibitor of activin, as it contains a follistatin module. TSC-36 is a heparin-binding protein suggested to have a role in the negative regulation of cellular growth, as its expression is induced in response to TGF-b1. In addition, TSC-36 is not found in small cell lung cancer (SCLC) cells, a highly aggressive neoplasm, but is detected in some non-small cell lung cancer (NSCLC) cells, a moderately aggressive neoplasm.. May modulate the action of some growth factors on cell proliferation and differentiation. Binds heparin.

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May be involved in microtubule organization and stabilization.

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Lectin which functions in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD). May bind terminally misfolded non-glycosylated proteins as well as improperly folded glycoproteins, retain them in the ER, and possibly transfer them to the ubiquitination machinery and promote their degradation. Possible targets include TRPV4.

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Transcriptional corepressor which does not bind directly to DNA and may regulate transcription through recruitment of histone deacetylases to gene promoters. Regulates cell adhesion, migration and proliferation. May be required for segmental gene expression during hindbrain development.

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No data available.

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Gas2 is a 313 amino acid protein encoded by the human gene GAS2. Gas2 is thought to play a role in apoptosis by acting as a cell death substrate for caspases. Gas2, a component of the microfilament system, is cleaved by a caspase (caspase-3 and caspase-7) at Asparagine 278 during apoptosis. The cleaved form resulting from this dramatically induces the rearrangement of the Actin cytoskeleton and causes potent changes in the shape of the affected cells. Gas2 is believed to also be involved in the membrane ruffling process. During the G0-G1 transition phase Gas2 can be found phosphorylated on its serine residues. Gas2 is a cytoskeleton and peripheral membrane protein that co-localizes with Actin fibers at the cell border and along the stress fibers in growth-arrested fibroblasts. Gas2 is mainly membrane-associated but when hyperphosphorylated it will accumulate at membrane ruffles. Gas2 is specifically expressed at growth arrest and is ubiquitously expressed with highest levels found in liver, lung and kidney. There is no evidence, however, of Gas2 expression in spleen.

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The LIM-only (LMO) proteins, LMO1 and LMO2, are nuclear factors that are characterised by a conserved LIM domain (1). The LIM domain consists of a cysteine-rich zinc-binding motif that is present in a variety of transcription factors, including the LIM homeobox (LHX) proteins expressed in the central nervous system and involved in cell differentiation (2). LMO1 and LMO2 are expressed in the adult CNS in a cell type-specific manner, where they are differentially regulated by neuronal activity and are involved in regulating the cellular differentiated phenotype of neurons (3). LMO2 lacks a specific DNA-binding homeobox domain but rather assembles into transcriptional regulatory complexes to mediate gene expression by interacting with the widely expressed nuclear LIM interactor (NLI) (4). NLI, known also as CLIM-1, and the related protein CLIM-2 facilitate the formation of heteromeric LIM complexes and also enhance the nuclear retention of LIM proteins (5). LMO2 and the related protein LMO4 are expressed in thymic precursor cells (6). LMO4 is also expressed in mature T cells, cranial neural crest cells, somite, dorsal limb bud mesenchyme, motor neurons, and Schwann cell progenitors (7).

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G-protein coupled receptor for CRH (corticotropin-releasing factor), UCN (urocortin), UCN2 and UCN3. Has high affinity for UCN. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and down-stream effectors, such as adenylate cyclase. Promotes the activation of adenylate cyclase, leading to increased intracellular cAMP levels.

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Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinity. Mediates Ras activation through G(s)-alpha- and cAMP-mediated signaling.

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High Mobility Group (HMG) proteins, a group of chromosomal proteins common to all eukaryotes, bind DNA in a non-sequence-specific fashion to promote chromatin function and gene regulation, helping with transcription, replication, recombination, and DNA repair. HMGB4 is HMG2-like, isoform 2, high-mobility group box 4. This gene can be found on Chromosome 1. HMGB4 contains two HMG-box regions, and is found in a variety of eukaryotic chromosomal proteins. HMGB proteins are phosphorylated to various extents. The existence of differentially modified forms increases the number of distinct HMGB protein variants in plant chromatin that may be adapted to certain functions.

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Ligand for members of the frizzled family of seven transmembrane receptors. Can activate or inhibit canonical Wnt signaling, depending on receptor context. In the presence of FZD4, activates beta-catenin signaling. In the presence of ROR2, inhibits the canonical Wnt pathway by promoting beta-catenin degradation through a GSK3-independent pathway which involves down-regulation of beta-catenin-induced reporter gene expression. Suppression of the canonical pathway allows chondrogenesis to occur and inhibits tumor formation. Stimulates cell migration. Decreases proliferation, migration, invasiveness and clonogenicity of carcinoma cells and may act as a tumor suppressor. Mediates motility of melanoma cells. Required during embryogenesis for extension of the primary anterior-posterior axis and for outgrowth of limbs and the genital tubercle. Inhibits type II collagen expression in chondrocytes.

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As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilises single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Plays also a role in base excision repair (BER) probably through interaction with UNG. Through RFWD3 may activate CHEK1 and play a role in replication checkpoint control. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance.

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Fyb (Fyn binding protein) and the anchoring proteins SKAP55 and SKAP55-R (SKAP55-related protein) associate with the tyrosine kinase p59fyn. SKAP55 and SKAP55-R bind to Fyb through their SH3 domains and function as substrates for p59Fyn in resting T cells. SKAP55 contains an N-terminal pleckstrin homology domain and a C-terminal SH3 domain binding motif of adjacent arginine and lysine residues followed by tandem tyrosines (i.e. RKxxYxxY). SKAP55-R, similar in overall structure to SKAP55, contains a coiled-coil N-terminal domain. SKAP55 associates with SLAP-130, another component of the Fyn complex, which plays a role in the regulation of signaling events initiated by lymphocyte antigen receptors leading up to T cell activation. The human SKAP55 gene maps to chromosome 17q21.32 and encodes a 359 amino acid protein.

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Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis.

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May function as part of a signaling pathway that acts to regulate the size of the body fat depot. An increase in the level of LEP may act directly or indirectly on the CNS to inhibit food intake and/or regulate energy expenditure as part of a homeostatic mechanism to maintain constancy of the adipose mass.

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CDO1 (cysteine dioxygenase, type I) is a 200 amino acid protein that belongs to the cysteine dioxygenase family and is involved in organosulfur biosynthesis. Existing as a monomer and expressed at high levels in liver and placenta and at lower levels in brain, pancreas and heart, CDO1 functions as a dioxygenase that uses iron and zinc as cofactors to catalyse the conversion of L-cysteine and oxygen to 3-sulfinoalanine. Via its catalytic activity, CDO1 is involved in pyruvate-, sulfate- and taurine-related metabolic pathways and is a crucial regulator of cysteine concentrations within the cell. Human CDO1 shares 94% amino acid identity with its rat counterpart, suggesting a conserved role between species. The gene encoding CDO1 maps to human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome, while deletion of the q arm or of chromosome 5 altogether is common in therapy-related acute myelogenous leukaemias and myelodysplastic syndrome.PathwayOrganosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 1/2.

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May play a role as a scaffolding protein that may be associated with the abnormal phenotype of leukemia cells. Isoform 2 may possess an antiapoptotic effect and protect cells during normal cell survival through its regulation of caspases.

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This gene encodes a member of the POU protein family characterised by the presence of a bipartite DNA binding domain, consisting of a POU-specific domain and a homeodomain, separated by a variable polylinker. The DNA binding domain may bind to DNA as monomers or as homo- and/or heterodimers, in a sequence-specific manner. The POU family members are transcriptional regulators, many of which are known to control cell type-specific differentiation pathways. This gene is a tumor suppressor involved in Wilms tumor (WT) predisposition. Alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.

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No data available.

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Serine protease which exhibits a preference for Arg over Lys in the substrate P1 position and for Ser or Pro in the P2 position. Shows activity against amyloid precursor protein, myelin basic protein, gelatin, casein and extracellular matrix proteins such as fibronectin, laminin, vitronectin and collagen. Degrades alpha-synuclein and prevents its polymerisation, indicating that it may be involved in the pathogenesis of Parkinson disease and other synucleinopathies. May be involved in regulation of axon outgrowth following spinal cord injury. Tumor cells treated with a neutralising KLK6 antibody migrate less than control cells, suggesting a role in invasion and metastasis.

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This is a receptor for secretin. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.

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Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognised by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway. Somatomedin-B is a growth hormone-dependent serum factor with protease-inhibiting activity.