2.3.1.225: protein S-acyltransferase
This is an abbreviated version!
For detailed information about protein S-acyltransferase, go to the full flat file.
Word Map on EC 2.3.1.225
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2.3.1.225
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palmitoylation
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palmitate
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s-acylation
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huntingtin
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palmitoylation-dependent
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huntingtin-interacting
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2-bromopalmitate
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s-acyltransferases
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medicine
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autoacylation
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16-carbon
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snap25
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acyl-acyl
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palmitoylation-deficient
- 2.3.1.225
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palmitoylation
- palmitate
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s-acylation
- huntingtin
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palmitoylation-dependent
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huntingtin-interacting
- 2-bromopalmitate
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s-acyltransferases
- medicine
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autoacylation
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16-carbon
- snap25
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acyl-acyl
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palmitoylation-deficient
Reaction
Synonyms
Akr1, Akr1p, APT1, Asp-His-His-Cys motif palmitoyl transferase, At3g51390, DHHC palmitoyl transferase, DHHC protein, DHHC protein acyltransferase, DHHC-2, DHHC-21, DHHC-21 palmitoyl transferase, DHHC-3, DHHC-3 palmitoyl transferase, DHHC-7, DHHC-8, DHHC-CRD S-acyltransferase, DHHC16, DHHC17, DHHC2, DHHC3, DHHC4, DHHC5, Erf2, Erf2p, G-protein palmitoyltransferase, HIP14, palmitoyl acyltransferase, Pat, PAT10, PAT14, PAT15, PAT21, PAT24, PAT4, Pfa3, Pfa4, PFA5, protein acyl transferase, protein acyltransferase, protein S-acyl transferase 4, Ras PAT, S-protein acyltransferase, SEC18p, Swf1, ZDHHC3, ZDHHC5
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General Information
General Information on EC 2.3.1.225 - protein S-acyltransferase
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evolution
malfunction
metabolism
physiological function
additional information
evolution
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the enzyme is an Asp-His-His-Cys motif (DHHC) palmitoyl transferase family member
evolution
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the enzymes belong to the DHHC family, homology and phylogeny of DHHC proteins, overview
evolution
B3DN87, O80685, Q0WQK2, Q3EBC2, Q3EC11, Q500Z2, Q52T38, Q5M757, Q6DR03, Q7XA86, Q8L5Y5, Q8VYP5, Q8VYS8, Q93VV0, Q94C49, Q9C533, Q9FLM3, Q9LIE4, Q9LIH7, Q9M115, Q9M1K5, Q9M306, Q9SB58
the PAT enzymes of Arabidopsis thaliana belong to the DHHC-CRD-containing PAT family, PAT enzymes share a common structure mainly composed of four predicted transmembrane domains and a stretch of Asp-His-His-Cys, DHHC, within a Cys-rich domain
evolution
TIP1 is a plant member of an evolutionarily conserved group of proteins that contains six ankyrin repeats and a DHHC-CRD and that are predicted to be integral membrane proteins
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apt1 null cells exhibit almost no acylprotein thioesterase activity toward palmitoyl-Gialpha1
malfunction
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depletion of cellular cholesterol with the drug methyl-beta-cyclodextrin results in inhibition of palmitoyltransferase activity and a redistribution of the remaining activity to membranes of higher density, the process is reversible by cholesterol addition
malfunction
expression of DHHC15 mutant C159S reduced PSD-95 synaptic clustering as well as the clustering of cell-surface AMPA receptor GluR2 subunits, which is dependent upon PSD-95 palmitoylation
malfunction
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human HIP14 complements the temperature-sensitive growth phenotype rescuing the defect in receptor endocytosis that results from deleting AKR1. Expression of human DHHC9 in yeast fails to complement an erf2DELTA strain. Deletion of the SWF1 gene abolishes the palmitoylation of Snc1, Syn8, and Tlg1 in vivo. Vac8 palmitoylation is significantly reduced but not absent in cells lacking Pfa3. Deletion of the ERF2 gene results in a decrease in Ras2 palmitoylation and a reduced presence on the plasma membrane. The erf2 erf4 double mutant is no more severe than either of the single mutants, and overexpression of ERF2 suppresses some but not all alleles of erf4
malfunction
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palmitoylation of wild-type eNOS by DHHC-21 is diminished by mutation of the two sites of eNOS palmitoylation, cysteines 15 and 26, palmitoylation deficient mutants of eNOS, i.e. G2A, C15/26S, and L2S, release less nitric oxide. Inhibition of DHHC-21 palmitoyl transferase, but not DHHC-3, in human endothelial cells reduces eNOS palmitoylation, eNOS targeting, and stimulated NO production
malfunction
the TIP GROWTH DEFECTIVE1 mutation affects cell growth throughout the plant and has a particularly strong effect on root hair growth. Inhibition of acylation in wild-type Arabidopsis thaliana roots by 2-bromopalmitate reproduces the Tip1- mutant phenotype
malfunction
PAT10 loss of function results in pleiotropic growth defects, including smaller leaves, dwarfism, and sterility. pat10 mutants are hypersensitive to salt stresses
malfunction
apex-associated re-positioning of nucleus during root hair elongation was impaired by PAT4 loss-of-function
both male and female gametogenesis require a fully functional protein S-acyl transferase 21. It is possible that AtPAT21 palmitoylates one or more such proteins that are involved in the repair of SPO11-mediated double-stranded breaks during meiosis
metabolism
the enzyme is involved in lipid catabolism during early seedling growth. It affects lipid breakdown through the beta-oxidation process
mice homozygous for DHHC5, are born at half the expected rate, and survivors show a marked deficit in contextual fear conditioning, an indicator of defective hippocampal-dependent learning. DHHC5 is highly enriched in a post-synaptic density preparation and co-immunoprecipitates with post-synaptic density protein PSD-95, an interaction that is mediated through binding of the carboxyl terminus of DHHC5 and the PDZ3 domain of PSD-95
physiological function
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palmitoyltransferase facilitates the enrichment of fatty acylated signaling molecules in plasma membrane subdomains. Fatty acylation, involving the enzyme, is one mechanism for targeting proteins to lipid rafts, low density, sphingomyelin- and cholesterol-enriched membranes. When reconstituted into cell membranes, the population of purified recombinant Gi that is palmitoylated is highly enriched in the low density membrane fractions, whereas the bulk unmodified Gi-protein is largely excluded, the effect requires palmitoyltransferase activity and is abolished if the palmitoylated cysteine was mutated.
physiological function
B3DN87, O80685, Q0WQK2, Q3EBC2, Q3EC11, Q500Z2, Q52T38, Q5M757, Q6DR03, Q7XA86, Q8L5Y5, Q8VYP5, Q8VYS8, Q93VV0, Q94C49, Q9C533, Q9FLM3, Q9LIE4, Q9LIH7, Q9M115, Q9M1K5, Q9M306, Q9SB58
protein lipid modification of cysteine residues, referred to as S-palmitoylation or S-acylation, is an important secondary and reversible modification that regulates membrane association, trafficking, and function of target proteins. This enzymatic reaction is mediated by protein S-acyl transferases, PATs
physiological function
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protein palmitoylation refers to the posttranslational addition of a 16 carbon fatty acid to the side chain of cysteine, forming a thioester linkage. This acyl modification is readily reversible, providing a potential regulatory mechanism to mediate protein-membrane interactions and subcellular trafficking of proteins. Membrane localization of Yck2 is dependent on Akr1. S-Palmitoylation of up to three N-terminal cysteines og Vac8 is proposed to influence its function through localization of the protein to specific vacuolar membrane microdomains. Enzyme Swf1 is a PAT for transmembraneproteins palmitoylated at juxtamembranous cysteine residues. If Tlg1 is not palmitoylated by Swf1, it becomes asubstrate for the ubiquitin ligase, Tul1, palmitoylation appears to act as a stability factor, protecting Tlg1 from the cellular quality control machinery
physiological function
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protein palmitoylation refers to the posttranslational addition of a 16 carbon fatty acid to the side chain of cysteine, forming a thioester linkage. This acyl modification is readily reversible, providing a potential regulatory mechanism to mediate protein-membrane interactions and subcellular trafficking of proteins. Palmitoylation plays a vital role in the nervous system, where substrates are abundant
physiological function
protein palmitoylation refers to the posttranslational addition of a 16 carbon fatty acid to the side chain of cysteine, forming a thioester linkage. This acyl modification is readily reversible, providing a potential regulatory mechanism to mediate protein-membrane interactions and subcellular trafficking of proteins. Palmitoylation plays a vital role in the nervous system, where substrates are abundant
physiological function
protein palmitoylation refers to the posttranslational addition of a 16 carbon fatty acid to the side chain of cysteine, forming a thioester linkage. This acyl modification is readily reversible, providing a potential regulatory mechanism to mediate protein-membrane interactions and subcellular trafficking of proteins. Palmitoylation plays a vital role in the nervous system, where substrates are abundant. DHHC15 is a regulator of PSD-95 palmitoylation in vivo
physiological function
protein palmitoylation refers to the posttranslational addition of a 16 carbon fatty acid to the side chain of cysteine, forming a thioester linkage. This acyl modification is readily reversible, providing a potential regulatory mechanism to mediate protein-membrane interactions and subcellular trafficking of proteins. Palmitoylation plays a vital role in the nervous system, where substrates are abundant. HIP14 complements the temperature-sensitive growth phenotype and rescues the defect in receptor endocytosis that results from deleting yeast AKR1. role for HIP14 as a regulator of neuronal protein trafficking mediated by its PAT activity. HIP14's oncogenic properties are mediated through Ras proteins
physiological function
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regulatory role of DHHC-21 in governing eNOS localization and function. eNOS fatty acylation is required for an efficient interaction with DHHC proteins and NO release, overview
physiological function
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reversible modification by palmitate is a feature of many signaling proteins that are associated with the cytoplasmic leaflet of the plasma membrane
physiological function
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reversible modification by palmitate is a feature of many signaling proteins that are associated with the cytoplasmic leaflet of the plasma membrane
physiological function
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reversible protein palmitoylation plays a role in protein-membrane interactions, protein trafficking, and enzyme activity. Mechanisms that underlie addition and removal of palmitate from proteins, detailed overview. Palmitoylation increases the hydrophobicity of proteins or protein domains and contributes to their membrane association
physiological function
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reversible protein palmitoylation plays a role in protein-membrane interactions, protein trafficking, and enzyme activity. Mechanisms that underlie addition and removal of palmitate from proteins, detailed overview. Palmitoylation increases the hydrophobicity of proteins or protein domains and contributes to their membrane association
physiological function
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reversible protein palmitoylation plays a role in protein-membrane interactions, protein trafficking, and enzyme activity. Mechanisms that underlie addition and removal of palmitate from proteins, detailed overview. Palmitoylation increases the hydrophobicity of proteins or protein domains and contributes to their membrane association
physiological function
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reversible protein palmitoylation plays a role in protein-membrane interactions, protein trafficking, and enzyme activity. Mechanisms that underlie addition and removal of palmitate from proteins, detailed overview. Palmitoylation increases the hydrophobicity of proteins or protein domains and contributes to their membrane association
physiological function
S-acylation is a reversible hydrophobic protein modification that offers swift, flexible control of protein hydrophobicity and affects protein association with membranes, signal transduction, and vesicle trafficking within cells. S-acylation is essential for normal plant cell growth. TIP1 binds the acyl group palmitate and it can rescue the morphological, temperature sensitivity, and yeast casein kinase2 localization defects of the yeast S-acyl transferase mutant akr1DELTA
physiological function
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the enzyme has a role for regulated cycles of acylation and deacylation accompanying activation of G-protein signal transduction pathways
physiological function
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the enzyme has a role for regulated cycles of acylation and deacylation accompanying activation of G-protein signal transduction pathways
physiological function
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vacuole fusion requires Sec18p-dependent acylation of the armadillo-repeat protein Vac8p
physiological function
disruption of PAT14 gene by T-DNA insertion results in an accelerated senescence phenotype. This coincides with increased transcript levels of some senescence-specific and pathogen-resistant marker genes. Early senescence of PAT14 mutants does not involve the signaling molecules jasmonic acid and abscisic acid, or autophagy, but associates with salicylic acid homeostasis and signaling
physiological function
functional loss of isoofrm PAT14 results in precocious leaf senescence and senescence is dependent on salicylic acid. Overexpressing PAT14 suppresses the expression of salicylic acid responsive genes. Introducing the salicylic acid deficient mutants, npr1-5 and NahG, but not other hormonal mutants, completely suppresses the precocious leaf senescence of PAT14 loss-of-function mutants
physiological function
isoform DHHC5 palmitoylates cardiac phosphoprotein phospholemman at two juxtamembrane cysteines, C40 and C42. Phospholemman interaction with and palmitoylation by DHHC5 is independent of the DHHC5 PSD-95/Discslarge/ZO-1 homology binding motif, but requires an about 120 amino acid region of the DHHC5 intracellular C-tail immediately after the fourth transmembrane domain. Phospholemman mutant C42A but not phospholemman mutant C40A inhibits the cardiac Na pump
physiological function
isoform PAT10 expression partially complements the yeast akr1 PAT mutant. Loss-of function mutants have a pleiotropic phenotype involving cell expansion and division, vascular patterning, and fertility that is rescued by wild-type AtPAT10 but not by catalytically inactive mutant C192A
physiological function
isoform PAT10 plays a secondary role in root hair growth. Treatment with palmitoylation-specific inhibitor 2-bromopalmitate compromises root hair elongation and polarity and impairs the dynamic polymerization of actin microfilaments, the asymmetric plasma membrane localization of phosphatidylinositol (4,5)-bisphosphate, the dynamic distribution of RabA4b-positive post-Golgi secretion, and endocytic trafficking in root hairs
physiological function
protein palmitoylation, contributed primarily by the Golgi-localized isoform TIP1 and secondarily by protein S-acyl transferases from other endomembrane compartments, plays a key role in the polar growth of root hairs. Treatment with specific inhibitor 2-bromopalmitate compromises root hair elongation and polarity and impairs the dynamic polymerization of actin microfilaments, the asymmetric plasma membrane localization of phosphatidylinositol (4,5)-bisphosphate, the dynamic distribution of RabA4b-positive post-Golgi secretion, and endocytic trafficking in root hairs
physiological function
CIL56 is a synthetic oxime that can trigger a form of nonapoptotic cell death that is distinct from apoptosis, necroptosis, ferroptosis, and classic necrosis. This unconventional form of cell death is promoted by a plasma membrane protein acyltransferase complex comprising ZDHHC5 and GOLGA7
physiological function
the enzyme mediates root hair elongation by positively regulating the membrane association of ROP2 and actin microfilament organization. It controls nucleus position during root hair tip growth
physiological function
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vacuole fusion requires Sec18p-dependent acylation of the armadillo-repeat protein Vac8p
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DHHC9 is a subunit of a human Ras PAT, but has no S-palmitoylation activity on its own, expression of human DHHC9 in yeast fails to complement an erf2DELTA strain
additional information
DHHC9 is a subunit of a human Ras PAT, but has no S-palmitoylation activity on its own, expression of human DHHC9 in yeast fails to complement an erf2DELTA strain
additional information
DHHC9 is a subunit of a human Ras PAT, but has no S-palmitoylation activity on its own, expression of human DHHC9 in yeast fails to complement an erf2DELTA strain
additional information
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Erf2, Pfa3, and Akr1 share a common sequence referred to as aDHHC(aspartate-histidinehistidine-cysteine) domain. The DHHC domain of Erf2 is located between transmembrane 2 (TM2) and TM3. The DHHC motif is essential for catalytic activity in vitro and the function of these proteins in vivo
additional information
expression of AtPATs can retarget Vac8p-GFP in yeast Vac8p mutant cells, overview. Vac8p-GFP is targeted to the vacuolar membrane in wild-type cells
additional information
expression of AtPATs can retarget Vac8p-GFP in yeast Vac8p mutant cells, overview. Vac8p-GFP is targeted to the vacuolar membrane in wild-type cells
additional information
expression of AtPATs can retarget Vac8p-GFP in yeast Vac8p mutant cells, overview. Vac8p-GFP is targeted to the vacuolar membrane in wild-type cells
additional information
expression of AtPATs can retarget Vac8p-GFP in yeast Vac8p mutant cells, overview. Vac8p-GFP is targeted to the vacuolar membrane in wild-type cells
additional information
expression of AtPATs can retarget Vac8p-GFP in yeast Vac8p mutant cells, overview. Vac8p-GFP is targeted to the vacuolar membrane in wild-type cells
additional information
expression of AtPATs can retarget Vac8p-GFP in yeast Vac8p mutant cells, overview. Vac8p-GFP is targeted to the vacuolar membrane in wild-type cells
additional information
expression of AtPATs can retarget Vac8p-GFP in yeast Vac8p mutant cells, overview. Vac8p-GFP is targeted to the vacuolar membrane in wild-type cells
additional information
expression of AtPATs can retarget Vac8p-GFP in yeast Vac8p mutant cells, overview. Vac8p-GFP is targeted to the vacuolar membrane in wild-type cells
additional information
expression of AtPATs can retarget Vac8p-GFP in yeast Vac8p mutant cells, overview. Vac8p-GFP is targeted to the vacuolar membrane in wild-type cells
additional information
expression of AtPATs can retarget Vac8p-GFP in yeast Vac8p mutant cells, overview. Vac8p-GFP is targeted to the vacuolar membrane in wild-type cells
additional information
expression of AtPATs can retarget Vac8p-GFP in yeast Vac8p mutant cells, overview. Vac8p-GFP is targeted to the vacuolar membrane in wild-type cells
additional information
expression of AtPATs can retarget Vac8p-GFP in yeast Vac8p mutant cells, overview. Vac8p-GFP is targeted to the vacuolar membrane in wild-type cells
additional information
expression of AtPATs can retarget Vac8p-GFP in yeast Vac8p mutant cells, overview. Vac8p-GFP is targeted to the vacuolar membrane in wild-type cells
additional information
expression of AtPATs can retarget Vac8p-GFP in yeast Vac8p mutant cells, overview. Vac8p-GFP is targeted to the vacuolar membrane in wild-type cells
additional information
expression of AtPATs can retarget Vac8p-GFP in yeast Vac8p mutant cells, overview. Vac8p-GFP is targeted to the vacuolar membrane in wild-type cells
additional information
expression of AtPATs can retarget Vac8p-GFP in yeast Vac8p mutant cells, overview. Vac8p-GFP is targeted to the vacuolar membrane in wild-type cells
additional information
expression of AtPATs can retarget Vac8p-GFP in yeast Vac8p mutant cells, overview. Vac8p-GFP is targeted to the vacuolar membrane in wild-type cells
additional information
expression of AtPATs can retarget Vac8p-GFP in yeast Vac8p mutant cells, overview. Vac8p-GFP is targeted to the vacuolar membrane in wild-type cells
additional information
expression of AtPATs can retarget Vac8p-GFP in yeast Vac8p mutant cells, overview. Vac8p-GFP is targeted to the vacuolar membrane in wild-type cells
additional information
expression of AtPATs can retarget Vac8p-GFP in yeast Vac8p mutant cells, overview. Vac8p-GFP is targeted to the vacuolar membrane in wild-type cells
additional information
expression of AtPATs can retarget Vac8p-GFP in yeast Vac8p mutant cells, overview. Vac8p-GFP is targeted to the vacuolar membrane in wild-type cells
additional information
expression of AtPATs can retarget Vac8p-GFP in yeast Vac8p mutant cells, overview. Vac8p-GFP is targeted to the vacuolar membrane in wild-type cells
additional information
expression of AtPATs can retarget Vac8p-GFP in yeast Vac8p mutant cells, overview. Vac8p-GFP is targeted to the vacuolar membrane in wild-type cells
additional information
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expression of AtPATs can retarget Vac8p-GFP in yeast Vac8p mutant cells, overview. Vac8p-GFP is targeted to the vacuolar membrane in wild-type cells
additional information
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one enzyme family is lysosomal and is involved in protein degradation. The second is cytosolic and removes palmitoyl moieties preferentially from proteins associated with membranes. PAT activity requires detergent, e.g. Triton X-100, for solubilization
additional information
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one enzyme family is lysosomal and is involved in protein degradation. The second is cytosolic and removes palmitoyl moieties preferentially from proteins associated with membranes. PAT activity requires detergent, e.g. Triton X-100, for solubilization
additional information
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one enzyme family is lysosomal and is involved in protein degradation. The second is cytosolic and removes palmitoyl moieties preferentially from proteins associated with membranes. PAT activity requires detergent, e.g. Triton X-100, for solubilization
additional information
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one enzyme family is lysosomal and is involved in protein degradation. The second is cytosolic and removes palmitoyl moieties preferentially from proteins associated with membranes. PAT activity requires detergent, e.g. Triton X-100, for solubilization
additional information
overexpression of DHHC2 causes increased S-acylation of LckN10-GFP. In resting Jurkat T cells, endogenous DHHC2 and Lck, a non-receptor tyrosine kinase of the Src family, are in close proximity to each other at the cell periphery, but completely non-overlapping, DHHC2 is a PAT for Lck in vivo
additional information
overexpression of DHHC2 causes increased S-acylation of LckN10-GFP. In resting Jurkat T cells, endogenous DHHC2 and Lck, a non-receptor tyrosine kinase of the Src family, are in close proximity to each other at the cell periphery, but completely non-overlapping, DHHC2 is a PAT for Lck in vivo
additional information
overexpression of DHHC2 causes increased S-acylation of LckN10-GFP. In resting Jurkat T cells, endogenous DHHC2 and Lck, a non-receptor tyrosine kinase of the Src family, are in close proximity to each other at the cell periphery, but completely non-overlapping, DHHC2 is a PAT for Lck in vivo
additional information
overexpression of DHHC4 does not cause increased S-acylation of LckN10-GFP
additional information
overexpression of DHHC4 does not cause increased S-acylation of LckN10-GFP
additional information
overexpression of DHHC4 does not cause increased S-acylation of LckN10-GFP
additional information
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role of G-protein betagamma subunits in substrate affinity for PAT may be to provide a mechanism for substrate presentation to PAT.
additional information
TIP1 encodes an ankyrin repeat protein with a DHHC Cys-rich domain
additional information
bioinformatic identification of functionally and structurally relevant residues and motifs in protein S-acyltransferases