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Beschreibung:
DR1, also known as NC2∫ (negative cofactor 2 subunit ∫), is a TFIID (TATA box-binding protein)-associated protein. DR1 localizes to the nucleus and contains an N-terminal histone fold motif, a TFIID-binding domain and an alanine and glutamine rich region. Via its histone fold motif, DR1 forms a heterodimer with NC2å (DRAP1) to comprise the conserved eukaryotic complex, NC2 (negative cofactor 2). The NC2 complex can both positively and negatively regulate transcription by RNA Pol II. More specifically, NC2 acts as a repressor of TATA-dependent transcription and acts as an activator for DPE-dependent transcription. NC2 represses RNA Pol II transcription by binding to TFIID and inhibiting association of the transcription factors TFIIA and TFIIB. NC2 activity is regulated by phosphorylation. Both subunits, NC2å and DR1, are phosphorylated in vivo.
Beschreibung:
Chromogranins (secretogranins) are acidic glycoproteins that localize within secretory granules of endocrine, neuroendocrine and neuronal tissue. Family members include chromogranin A (Chr-A); chromogranin B (Chr-B), also known as secretogranin I; chromogranin C (also known as secretogranin II or Sg II); and secretogranin III (Sg III or SCG3). High levels of Chr-A expression are characteristic of neuroendocrine tumours. Pancreastatin is a peptide derived from Chr-A which inhibits insulin secretion, exocrine pancreatic secretion and gastric acid secretion. Pancreastatin exists as two forms; the major form is expressed in stomach and colon extracts. In neuroendocrine cells the level Sg II has been shown to increase four-fold in response to histamine, while levels of Chr-A and Chr-B showed little or no increase. Sg III is an acidic secretory protein expressed in neuronal and endocrine cells. In the anterior lobe of the rat pituitary gland, Sg III is present in mammotropes and thyrotropes, moderately in gonadotropes and corticotropes, though not in somatotropes. Sg III and carboxypeptidase E (CPE) bind specifically to cholesterol-rich secretory granule (SG) membranes.
Beschreibung:
May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons.
Beschreibung:
May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons.
Beschreibung:
May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons.
Beschreibung:
EPDR1 is a type II transmembrane protein and is similar to two families of cell adhesion molecules, the protocadherins and ependymins. It may play a role in calcium dependent cell adhesion. There are two named isoforms.
Beschreibung:
Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase.
Beschreibung:
This gene is a member of the type II keratin family clustered on the long arm of chromosome 12. Type I and type II keratins heteropolymerize to form intermediate-sized filaments in the cytoplasm of epithelial cells. The product of this gene typically dimerizes with keratin 18 to form an intermediate filament in simple single-layered epithelial cells. This protein plays a role in maintaining cellular structural integrity and also functions in signal transduction and cellular differentiation. Mutations in this gene cause cryptogenic cirrhosis. Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Jan 2012].
Beschreibung:
This gene is a member of the type II keratin family clustered on the long arm of chromosome 12. Type I and type II keratins heteropolymerize to form intermediate-sized filaments in the cytoplasm of epithelial cells. The product of this gene typically dimerizes with keratin 18 to form an intermediate filament in simple single-layered epithelial cells. This protein plays a role in maintaining cellular structural integrity and also functions in signal transduction and cellular differentiation. Mutations in this gene cause cryptogenic cirrhosis. Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Jan 2012].
Beschreibung:
The endophilins comprise a family of three SH3 domain-containing proteins designated Endophilin I, II and III, or alternatively known as SH3P4, SH3P8 and SH3P13, respectively. These proteins associate with Amphiphysin, Synaptojanin and Dynamin and are implicated in presynaptic vesicle trafficking at nerve terminals. The expression patterns of the endophilins are consistent with their cellular functions at the neuronal synapse, as Endophilin I is ex- pressed only in the brain. Both Endophilin II and Endophilin III are detected in a variety of tissues. Endophilin I is also implicated in modulating G protein-coupled receptor signaling by functioning as an adapter protein and directing 1 adrenergic receptors to the endocytic machinery.
Beschreibung:
Accessory protein for MHC class-II antigen/T-cell receptor interaction. May regulate T-cell activation. Induces the aggregation of lipid rafts.
Beschreibung:
Cleaves C-terminal amino acids linked to proline in peptides such as angiotensin II, III and des-Arg9-bradykinin. This cleavage occurs at acidic pH, but enzymatic activity is retained with some substrates at neutral pH.
Beschreibung:
Cleaves C-terminal amino acids linked to proline in peptides such as angiotensin II, III and des-Arg9-bradykinin. This cleavage occurs at acidic pH, but enzymatic activity is retained with some substrates at neutral pH.
Beschreibung:
Affected males of X-linked anhidrotic ectodermal dysplasia show hypotrichosis, abnormal teeth and absent sweat glands. Some of the patients reported by Halperin and Curtis showed mental defect also, but this is not an invariable feature. Ectodysplasin A (EDA) is a trimeric type II membrane protein that co-localizes with cytoskeletal structures at the lateral and apical surfaces of cells. EDA is expressed in hair follicles and in the epidermis of adult skin. The sequence of the longest isoform includes an interrupted collagenous domain of 19 Gly-X-Y repeats and a motif conserved in the tumor necrosis factor (TNF)-related ligand family. EDA is a member of the TNF-related ligand family involved in the early epithelial-mesenchymal interaction that regulates ectodermal appendage formation. Similar to other members of collagenous membrane proteins and members of TNF-related ligands, EDA is a type II membrane protein which forms trimers.
Beschreibung:
Affected males of X-linked anhidrotic ectodermal dysplasia show hypotrichosis, abnormal teeth and absent sweat glands. Some of the patients reported by Halperin and Curtis showed mental defect also, but this is not an invariable feature. Ectodysplasin A (EDA) is a trimeric type II membrane protein that co-localizes with cytoskeletal structures at the lateral and apical surfaces of cells. EDA is expressed in hair follicles and in the epidermis of adult skin. The sequence of the longest isoform includes an interrupted collagenous domain of 19 Gly-X-Y repeats and a motif conserved in the tumor necrosis factor (TNF)-related ligand family. EDA is a member of the TNF-related ligand family involved in the early epithelial-mesenchymal interaction that regulates ectodermal appendage formation. Similar to other members of collagenous membrane proteins and members of TNF-related ligands, EDA is a type II membrane protein which forms trimers.
Beschreibung:
Affected males of X-linked anhidrotic ectodermal dysplasia show hypotrichosis, abnormal teeth and absent sweat glands. Some of the patients reported by Halperin and Curtis showed mental defect also, but this is not an invariable feature. Ectodysplasin A (EDA) is a trimeric type II membrane protein that co-localizes with cytoskeletal structures at the lateral and apical surfaces of cells. EDA is expressed in hair follicles and in the epidermis of adult skin. The sequence of the longest isoform includes an interrupted collagenous domain of 19 Gly-X-Y repeats and a motif conserved in the tumor necrosis factor (TNF)-related ligand family. EDA is a member of the TNF-related ligand family involved in the early epithelial-mesenchymal interaction that regulates ectodermal appendage formation. Similar to other members of collagenous membrane proteins and members of TNF-related ligands, EDA is a type II membrane protein which forms trimers.
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