E3 Ubiquitin-Protein Ligase CHIP is a cytoplasmic protein. CHIP is highly expressed in skeletal muscle, heart, pancreas, brain and placenta. CHIP interacts with the molecular chaperones Hsc70-Hsp70 and Hsp90 through its TPR domain; lead to in client substrate ubiquitylation and degradation by the proteasome. CHIP targets misfolded chaperone substrates towards proteasomal degradation. CHIP mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. CHIP plays a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome. It also may regulate the receptor stability and activity through proteasomal degradation.
Syntaxin-binding protein 1, also known as N-Sec1, Protein unc-18 homolog 1, MUNC18-1 and STXBP1, is a peripheral membrane protein which belongs to theSTXBP / unc-18 / SEC1 family. STXBP1 is an evolutionally conserved neuronal Sec1/Munc-18 (SM) protein that is essential in synaptic vesicle release in several species. It may participate in the regulation of synaptic vesicle docking and fusion, possibly through interaction with GTP-binding proteins. STXBP1 is essential for neurotransmission and binds syntaxin, a component of the synaptic vesicle fusion machinery probably in a 1:1 ratio. It can interact with syntaxins 1, 2, and 3 but not syntaxin 4. STXBP1 may also play a role in determining the specificity of intracellular fusion reactions. Defects in STXBP1 are the cause of epileptic encephalopathy early infantile type 4 (EIEE4). Affected individuals have neonatal or infantile onset of seizures, suppression-burst pattern on EEG, profound mental retardation, and MRI evidence of hypomyelination.
Syntaxin-binding protein 3, also known as Platelet Sec1 protein, Protein unc-18 homolog 3, Protein unc-18 homolog C, Unc-18C, Unc18-3 and STXBP3, is a cytoplasm protein which belongs to theSTXBP/unc-18/SEC1 family. STXBP3 is expressed in cells that exhibit granule exocytosis, such as neutrophils, mast cells, platelets and endothelial cells. STXBP3, together with STX4 and VAMP2, may play a role in insulin-dependent movement of GLUT4 and in docking / fusion of intracellular GLUT4-containing vesicles with the cell surface in adipocytes. STXBP3 participates in the consolidation and secretion of secondary and tertiary granules. STXBP3 contains one SEC1 domain. Phosphorylation at Ser129 may stimulate granule release. Human STXBP3 shares 90% aa identity with mouse STXBP3. STXBP3 interacts with DOC2B; the interaction is direct, occurs at the cell membrane, excludes interaction with STX4 and regulates glucose-stimulated insulin secretion. Interacts with STX4.
Sulfotransferase 4A1 (ST4A1) is a member of the Sulfotransferase 1 family. ST4A1 is highly expressed in the cerebral cortex and frontal lobe, but no expression is detected in the pancreas. ST4A1 is a brain-specific sulfotransferase believed to be involved in the metabolism of neurotransmitters. ST4A1 acts on catecholamines and T4 in a manner that may not involve sulfonation. ST4A1 may have a role in the metabolism of drugs and neurotransmitters in the CNS. In addition, ST4A1 is related to schizophrenia.
Human Sulfotransferase (SULT1C4) is an enzyme that in humans is encoded by the SULT1C4 gene, belongs to the sulfotransferase 1 family. SULT1C4 is expressed at high levels in fetal lung and kidney and at low levels in fetal heart, adult kidney, ovary and spinal chord. Sulfotransferase utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of drugs, xenobiotic compounds, hormones, and neurotransmitters. It shows activity towards p-nitrophenol and N-hydroxy-2-acetylamino-fluorene (N-OH-2AAF). SULT1C4 plays an important role incatalyzing the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds.
Sulfotransferase 1A1 (SULT1A1) is a cytosolic sulfotransferases that is expressed in the liver; lung; adrenal; brain; platelets; and skin. SULT1A1 is a phenol sulfotransferases with thermostable enzyme activity. SULT1A1 utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of catecholamines; phenolic drugs and neurotransmitters. It is responsible for the sulfonation and activation of minoxidil. SULT1A1 mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products and could so participate as modulating factor of cancer risk.
Sulfotransferase 1A2 (SULT1A2) is a member of the Sulfotransferase 1 family. Sulfotransferase enzymes catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. SULT1A2 is a cytoplasmic protein and exists as a homodimer. SULT1A2 mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products and might thus participate as a modulating factor of cancer risk.
SULT1A3 belongs to the sulfotransferase 1 family. Sulfotransferase enzymes catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. They are different in their tissue distributions and substrate specificities while their gene structure (number and length of exons) is similar. SULT1A3 gene encodes a phenol sulfotransferase with thermolabile enzyme activity. Four sulfotransferase genes are located on the p arm of chromosome 16; this gene and SULT1A4 arose from a segmental duplication. It is the most centromeric of the four sulfotransferase genes. Exons of this gene overlap with exons of a gene that encodes a protein containing GIY-YIG domains (GIYD1). SULT1A3 is expressed in liver, colon, kidney, lung, brain, spleen, small intestine, placenta and leukocyte. SULT1A3 is a sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of phenolic monoamines (neurotransmitters such as dopamine, norepinephrine and serotonin) and phenolic and catechol drugs.
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