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Description:
The large binding pocket can accommodate several single chain phospholipids and fatty acids, GM2A also exhibits some calcium-independent phospholipase activity (By similarity). Binds gangliosides and stimulates ganglioside GM2 degradation. It stimulates only the breakdown of ganglioside GM2 and glycolipid GA2 by beta-hexosaminidase A. It extracts single GM2 molecules from membranes and presents them in soluble form to beta-hexosaminidase A for cleavage of N-acetyl-D-galactosamine and conversion to GM3.
Description:
Glycosylphosphatidylinositol (GPI) acts as a membrane anchor for cell surface proteins. Glycosylphosphatidylinositol anchor attachment 1 protein (GPAA1), also designated GPI anchor attachment protein 1 or GAA1 protein homolog, is a membrane protein localized to the endoplasmic reticulum which is involved in GPI-anchor biosynthesis. GPAA1 is crucial for GPI-anchoring of precursor proteins and catalyzes the attachment of GPI to proteins containing a C-terminal GPR attachment signal. GAA1 contains an N-terminal signal sequence, one cAMP- and cGMP-dependent protein kinase phosphorylation site, two potential N-glycosylation sites, one leucine zipper pattern and eight putative transmembrane domains. GPAA1 is ubiquitously expressed and shows higher levels of expression in fetal tissues than in adult tissues.
Description:
GMD is a 372 amino acid protein that utilizes NADP as a cofactor to catalyze the conversion of GDP-mannose to GDP-4-keto-6-deoxymannose. GMD mutations are involved in resistance to TRAIL (tumor necrosis factor-related apoptosis-inducing ligand)-induced apoptosis. The gene encoding GMD maps to human chromosome 6, which contains 170 million base pairs and comprises nearly 6% of the human genome. Deletion of a portion of the q arm of chromosome 6 is associated with early onset intestinal cancer, suggesting the presence of a cancer susceptibility locus. Additionally, Porphyria cutanea tarda, Parkinson's disease, Stickler syndrome and a susceptibility to bipolar disorder are all associated with genes that map to chromosome 6.
Description:
The large binding pocket can accommodate several single chain phospholipids and fatty acids, GM2A also exhibits some calcium-independent phospholipase activity (By similarity). Binds gangliosides and stimulates ganglioside GM2 degradation. It stimulates only the breakdown of ganglioside GM2 and glycolipid GA2 by beta-hexosaminidase A. It extracts single GM2 molecules from membranes and presents them in soluble form to beta-hexosaminidase A for cleavage of N-acetyl-D-galactosamine and conversion to GM3.
Description:
Growth hormone 2 (GH2) is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Mutations in this gene lead to placental growth hormone/lactogen deficiency. The major role of GH2 in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues.
Description:
Glycosylphosphatidylinositol (GPI) acts as a membrane anchor for cell surface proteins. Glycosylphosphatidylinositol anchor attachment 1 protein (GPAA1), also designated GPI anchor attachment protein 1 or GAA1 protein homolog, is a membrane protein localized to the endoplasmic reticulum which is involved in GPI-anchor biosynthesis. GPAA1 is crucial for GPI-anchoring of precursor proteins and catalyzes the attachment of GPI to proteins containing a C-terminal GPR attachment signal. GAA1 contains an N-terminal signal sequence, one cAMP- and cGMP-dependent protein kinase phosphorylation site, two potential N-glycosylation sites, one leucine zipper pattern and eight putative transmembrane domains. GPAA1 is ubiquitously expressed and shows higher levels of expression in fetal tissues than in adult tissues.
Description:
E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. It is unclear whether it also mediates the formation of other types of polyubiquitin chains. The E3 ubiquitin-protein ligase activity is required for its tumor suppressor function. The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Regulates centrosomal microtubule nucleation. Required for normal cell cycle progression from G2 to mitosis. Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle. Involved in transcriptional regulation of P21 in response to DNA damage. Required for FANCD2 targeting to sites of DNA damage. May function as a transcriptional regulator. Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation. Contributes to homologous recombination repair (HRR) via its direct interaction with PALB2, fine-tunes recombinational repair partly through its modulatory role in the PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA breaks. Component of the BRCA1-RBBP8 complex which regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage via BRCA1-mediated ubiquitination of RBBP8.
Description:
SMAD2 or Mothers against decapentaplegic homolog 2 is a polypeptide that, as its name describes, is a homolog of the Drosophila gene: "Mothers against decepentaplegic". It belongs to the SMAD family of proteins, which belong to the TGF-Beta superfamily of modulators. Like many other TGF-Beta family members SMAD2 is involved in cell signalling. SMAD2 modulates signals of activin and TGF-Beta's. It interacts with SMAD anchor for receptor activation (SARA). The binding of ligands causes the phosphorylation of the SMAD2 protein and the dissociation from SARA and the association with SMAD4. It is subsequently transferred to the nucleus where it forms complexes with other proteins and acts as a transcription factor. SMAD2 is a receptor regulated SMAD (R-SMAD) and is activated by bone morphogenetic protein type 1 receptor kinase. Smad2 (Mothers against decapentaplegic homolog 2; SMAD 2; Mothers against DPP homolog 2;)
Description:
E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. It is unclear whether it also mediates the formation of other types of polyubiquitin chains. The E3 ubiquitin-protein ligase activity is required for its tumor suppressor function. The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Regulates centrosomal microtubule nucleation. Required for normal cell cycle progression from G2 to mitosis. Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle. Involved in transcriptional regulation of P21 in response to DNA damage. Required for FANCD2 targeting to sites of DNA damage. May function as a transcriptional regulator. Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation. Contributes to homologous recombination repair (HRR) via its direct interaction with PALB2, fine-tunes recombinational repair partly through its modulatory role in the PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA breaks. Component of the BRCA1-RBBP8 complex which regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage via BRCA1-mediated ubiquitination of RBBP8.
Description:
The protein encoded by this gene belongs to a small class of the protein tyrosine phosphatase (PTP) family. PTPs are cell signaling molecules that play regulatory roles in a variety of cellular processes. PTPs in this class contain a protein tyrosine phosphatase catalytic domain and a characteristic C-terminal prenylation motif. This PTP has been shown to primarily associate with plasmic and endosomal membrane through its C-terminal prenylation. This PTP was found to interact with the beta-subunit of Rab geranylgeranyltransferase II (beta GGT II), and thus may function as a regulator of GGT II activity. Overexpression of this gene in mammalian cells conferred a transformed phenotype, which suggested its role in tumorigenesis. Alternatively spliced transcript variants have been described. Related pseudogenes exist on chromosomes 11, 12 and 17.
Description:
GM130, a cis-Golgi matrix protein, interacts specifically with p115 and provides a membrane docking site. Both GM130 and p115 are involved in vesicle tethering to Golgi membranes. The protein p115 also binds p400, alternatively called giantin. Giantin, the majority of whose mass projects into the cytoplasm, is involved in the docking of COPI vesicles via p115 to the Golgi membrane. Giantin, which also is known as macrogolgin or Golgi complex-associated protein, is involved in cross-bridge formation in the Golgi complex. Giantin, which can form a homodimer, is a single-pass type I membrane protein that is an antigen in Sjoegren syndrome and in chronic rheumatoid arthritis.
Description:
Plays a role in the regulation of the actin cytoskeleton through its interactions with actin capping protein (CP). May function to target CK2 to the plasma membrane thereby serving as an adapter to facilitate the phosphorylation of CP by protein kinase 2 (CK2). Appears to target ATM to the plasma membrane. Appears to also inhibit tumor cell growth by inhibiting AKT-mediated cell-survival. Also implicated in PI3K-regulated muscle differentiation, the regulation of AP-1 activity (plasma membrane bound AP-1 regulator that translocates to the nucleus) and the promotion of apoptosis induced by tumor necrosis factor TNF. When bound to PKB, it inhibits it probably by decreasing PKB level of phosphorylation.
Description:
The intracellular stimulation of guanylate cyclase (GC) by calcium, a key event in the recovery of the dark state of rod photoreceptors after exposure to light, is mediated by guanylate cyclase-activating proteins (GCAP). GCAPs are calcium-binding proteins belonging to the calmodulin superfamily and are specifically expressed in retina. GCAP3 (Guanylyl cyclase-activating protein 3), also known as GUCA1C (Guanylate cyclase activator 1C), is a 209 amino acid EF-hand calcium binding protein that is activated by the decrease in calcium from the absorption of light by rhodopsin. Activation of GCAP3 leads to stimulation of guanylate cyclase 1 and 2 (GC1 and GC2), which increases cGMP concentration. Calcium sensitive regulation of GC is essential in recovery of the rod receptor dark state following light exposure. There are two isoforms of GCAP3 that are produced as a result of alternative splicing events.
Description:
ADRM1 is a 407 amino acid protein that localizes to both the nucleus and the cytoplasm and is thought to be involved in protein recruitment and cell adhesion. An integral membrane protein, ADRM1 functions to recruit UCH-L5, a deubiquitinating enzyme, to the 26S proteasome, and once at the proteasome it promotes the activity of UCH-L5. Additionally, ADRM1 is thought to mediate lymphocyte adhesion in endothelial cells and may thus play a role in lymphocyte homing. ADRM1 expression is induced by IFN-g in some cancer cell lines and its expression is upregulated in other metastatic cells, suggesting a role in carcinogenesis. Two isoforms of ADRM1 exist due to alternative splicing events.
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