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Synonyms
hip14, dhhc3, palmitoyl acyltransferase, dhhc5, zdhhc5, dhhc2, akr1p, zdhhc3, protein acyltransferase, dhhc protein,
more
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palmitoyl-CoA + [GAD65]-L-cysteine
[GAD65]-S-palmitoyl-L-cysteine + CoA
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palmitoyl-CoA + [htt(1-548)]-L-cysteine
[htt(1-548)]-S-palmitoyl-L-cysteine + CoA
N-terminal fragment of htt(1-548)
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palmitoyl-CoA + [Lck]-L-cysteine
[Lck]-S-palmitoyl-L-cysteine + CoA
nonreceptor tyrosine kinase
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palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
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palmitoyl-CoA + [PSD-95]-L-cysteine
[PSD-95]-S-palmitoyl-L-cysteine + CoA
low activity
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palmitoyl-CoA + [SNAP-25]-L-cysteine
[SNAP-25]-S-palmitoyl-L-cysteine + CoA
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palmitoyl-CoA + [synaptotagmin I ]-L-cysteine
[synaptotagmin I ]-S-palmitoyl-L-cysteine + CoA
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palmitoyl-CoA + [endothelial nitric oxide synthase]-L-cysteine
[endothelial nitric oxide synthase]-S-palmitoyl-L-cysteine + CoA
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isozyme DHHC-21
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palmitoyl-CoA + [Ga protein]-L-cysteine
[Ga protein]-S-palmitoyl-L-cysteine + CoA
substrate of DHHC3 and DHHC7
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palmitoyl-CoA + [GAP-43 protein]-L-cysteine
[GAP-43 protein]-S-palmitoyl-L-cysteine + CoA
substrate of DHHC7 and DHHC15
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palmitoyl-CoA + [N-myristoylated G-protein alphai1]-L-cysteine
[N-myristoylated G-protein alphai1]-S-palmitoyl-L-cysteine + CoA
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palmitoyl-CoA + [N-myristoylated Gly-Cys-Gly tripeptide]-L-cysteine
[N-myristoylated Gly-Cys-Gly tripeptide]-S-palmitoyl-L-cysteine + CoA
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peptide substrate si tagged via ethylenediamine with fluorescent NBD
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palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [PSD95]-L-cysteine
[Ras]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [Ras]-L-cysteine
[Ras]-S-palmitoyl-L-cysteine + CoA
by Ras PAT containing the DHHC9 protein subunit
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palmitoyl-CoA + [SNAP-25]-L-cysteine
[SNAP-25]-S-palmitoyl-L-cysteine + CoA
substrate of DHHC3 and DHHC7
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r
additional information
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palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
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palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
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r
palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
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r
palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
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S-palmitoylation is the reversible addition of palmitate or other long chain fatty acids to proteins at cysteine residues via a thioester linkage. The types of proteins that undergo palmitoylation are quite diverse and include intrinsic and peripherally associated membrane proteins, as well as mitochondrial proteins
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palmitoyl-CoA + [PSD95]-L-cysteine
[Ras]-S-palmitoyl-L-cysteine + CoA
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palmitoyl-CoA + [PSD95]-L-cysteine
[Ras]-S-palmitoyl-L-cysteine + CoA
possible substrate of DHHC15 and, to a lesser extent, DHHC2, DHHC3, and DHHC7
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r
additional information
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complexity of HIP14's substrate specificity, in vitro, HIP14 has PAT activity for the N-terminal fragment of htt(1-548), SNAP-25, PSD-95, GAD65, and synaptotagmin I but not for synaptotagmin VII and paralemmin
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additional information
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complexity of HIP14's substrate specificity, in vitro, HIP14 has PAT activity for the N-terminal fragment of htt(1-548), SNAP-25, PSD-95, GAD65, and synaptotagmin I but not for synaptotagmin VII and paralemmin
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additional information
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complexity of HIP14's substrate specificity, in vitro, HIP14 has PAT activity for the N-terminal fragment of htt(1-548), SNAP-25, PSD-95, GAD65, and synaptotagmin I but not for synaptotagmin VII and paralemmin
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additional information
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in the absence of cellular factors, palmitoyl-CoA is capable of spontaneously S-acylating cysteinyl thiols, overview. G protein alpha subunit GsR is first acylated at Cys-3, then the palmitate is transferred to the amino group of Gly-2 through a cyclic intermediate as is postulated for hedgehog
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additional information
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DHHC2 has a broad protein substrate specificity. DHHC2 transfers fatty acids from all acyl-CoA chain lengths tested, consistent with it having a broad specificity for long chain acyl-CoAs, and acyl-CoAs of 14 carbons and longer inhibit palmitoyl-CoA labeling of both substrate and enzyme. The acyl-CoA chain length specificity of DHHC enzyme autoacylation parallels substrate specificity, overview
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palmitoyl-CoA + [Lck]-L-cysteine
[Lck]-S-palmitoyl-L-cysteine + CoA
nonreceptor tyrosine kinase
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r
palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
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palmitoyl-CoA + [endothelial nitric oxide synthase]-L-cysteine
[endothelial nitric oxide synthase]-S-palmitoyl-L-cysteine + CoA
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isozyme DHHC-21
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r
palmitoyl-CoA + [Ga protein]-L-cysteine
[Ga protein]-S-palmitoyl-L-cysteine + CoA
substrate of DHHC3 and DHHC7
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palmitoyl-CoA + [GAP-43 protein]-L-cysteine
[GAP-43 protein]-S-palmitoyl-L-cysteine + CoA
substrate of DHHC7 and DHHC15
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palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [PSD95]-L-cysteine
[Ras]-S-palmitoyl-L-cysteine + CoA
possible substrate of DHHC15 and, to a lesser extent, DHHC2, DHHC3, and DHHC7
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palmitoyl-CoA + [Ras]-L-cysteine
[Ras]-S-palmitoyl-L-cysteine + CoA
by Ras PAT containing the DHHC9 protein subunit
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palmitoyl-CoA + [SNAP-25]-L-cysteine
[SNAP-25]-S-palmitoyl-L-cysteine + CoA
substrate of DHHC3 and DHHC7
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r
additional information
?
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in the absence of cellular factors, palmitoyl-CoA is capable of spontaneously S-acylating cysteinyl thiols, overview. G protein alpha subunit GsR is first acylated at Cys-3, then the palmitate is transferred to the amino group of Gly-2 through a cyclic intermediate as is postulated for hedgehog
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palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
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r
palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
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palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
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palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
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S-palmitoylation is the reversible addition of palmitate or other long chain fatty acids to proteins at cysteine residues via a thioester linkage. The types of proteins that undergo palmitoylation are quite diverse and include intrinsic and peripherally associated membrane proteins, as well as mitochondrial proteins
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Alopecia
Mice with alopecia, osteoporosis, and systemic amyloidosis due to mutation in Zdhhc13, a gene coding for palmitoyl acyltransferase.
Amyloidosis
Mice with alopecia, osteoporosis, and systemic amyloidosis due to mutation in Zdhhc13, a gene coding for palmitoyl acyltransferase.
Anthrax
Anthrax toxin requires ZDHHC5-mediated palmitoylation of its surface-processing host enzymes.
Brain Injuries
Palmitoyl Acyltransferase zD17 Mediates Neuronal Responses in Acute Ischemic Brain Injury by Regulating JNK Activation in a Signaling Module.
Breast Neoplasms
LXR Activation Down-regulates Lipid Raft Markers FLOT2 and DHHC5 in MCF-7 Breast Cancer Cells.
Breast Neoplasms
Protein Acyltransferase DHHC3 Regulates Breast Tumor Growth, Oxidative Stress, and Senescence.
Carcinoma
Nitrodibenzofuran: a One- and Two-Photon Sensitive Protecting Group that is Superior to Brominated Hydroxycoumarin for Thiol Caging in Peptides.
Carcinoma, Hepatocellular
Prognostic significance of cytoskeleton-associated membrane protein 4 and its palmitoyl acyltransferase DHHC2 in hepatocellular carcinoma.
Carcinoma, Non-Small-Cell Lung
Systematic siRNA Screen Unmasks NSCLC Growth Dependence by Palmitoyltransferase DHHC5.
Cardiomyopathies
Palmitoyl acyltransferase Aph2 in cardiac function and the development of cardiomyopathy.
Dwarfism
PROTEIN S-ACYL TRANSFERASE10 Is Critical for Development and Salt Tolerance in Arabidopsis.
Glioma
DHHC protein family targets different subsets of glioma stem cells in specific niches.
Glioma
EZH2 Palmitoylation Mediated by ZDHHC5 in p53-Mutant Glioma Drives Malignant Development and Progression.
Herpes Simplex
The Absence of DHHC3 Affects Primary and Latent Herpes Simplex Virus 1 Infection.
Huntington Disease
Dysregulated striatal neuronal processing and impaired motor behavior in mice lacking huntingtin interacting protein 14 (HIP14).
Huntington Disease
Palmitoylation of caspase-6 by HIP14 regulates its activation.
Huntington Disease
Palmitoylation of huntingtin by HIP14 is essential for its trafficking and function.
Huntington Disease
The Palmitoyl acyltransferase HIP14 Shares a High Proportion of Interactors with Huntingtin: Implications for a Role in the Pathogenesis of Huntington Disease.
Huntington Disease
Tracking brain palmitoylation change: predominance of glial change in a mouse model of Huntington's disease.
Infections
Purification of Recombinant DHHC Proteins Using an Insect Cell Expression System.
Infections
The Absence of DHHC3 Affects Primary and Latent Herpes Simplex Virus 1 Infection.
Infertility
PROTEIN S-ACYL TRANSFERASE10 Is Critical for Development and Salt Tolerance in Arabidopsis.
Insulin Resistance
Brain insulin resistance impairs hippocampal synaptic plasticity and memory by increasing GluA1 palmitoylation through FoxO3a.
Insulinoma
A Targeted RNAi Screen Identifies Endocytic Trafficking Factors That Control GLP-1 Receptor Signaling in Pancreatic ?-Cells.
Lung Abscess
Whole-genome sequence of Corynebacterium pseudotuberculosis PAT10 strain isolated from sheep in Patagonia, Argentina.
Lung Neoplasms
Systematic siRNA Screen Unmasks NSCLC Growth Dependence by Palmitoyltransferase DHHC5.
Malaria
The Plasmodium palmitoyl-S-acyl-transferase DHHC2 is essential for ookinete morphogenesis and malaria transmission.
Neoplasm Metastasis
miR-96-5p enhances cell proliferation and invasion via targeted regulation of ZDHHC5 in gastric cancer.
Neoplasms
Antioxidant functions of DHHC3 suppress anti-cancer drug activities.
Neoplasms
Artemisinin inhibits NRas palmitoylation by targeting the protein acyltransferase ZDHHC6.
Neoplasms
DHHC-7 and -21 are palmitoylacyltransferases for sex steroid receptors.
Neoplasms
Discovery and characterization of inhibitors of human palmitoyl acyltransferases.
Neoplasms
Huntingtin interacting protein 14 is an oncogenic human protein: palmitoyl acyltransferase.
Neoplasms
Identification of CKAP4/p63 as a major substrate of the palmitoyl acyltransferase DHHC2, a putative tumor suppressor, using a novel proteomics method.
Neoplasms
Inhibiting PD-L1 palmitoylation enhances T-cell immune responses against tumours.
Neoplasms
miR-96-5p enhances cell proliferation and invasion via targeted regulation of ZDHHC5 in gastric cancer.
Neoplasms
Palmitoylation of cytoskeleton associated protein 4 by DHHC2 regulates antiproliferative factor-mediated signaling.
Neoplasms
Protein Acyltransferase DHHC3 Regulates Breast Tumor Growth, Oxidative Stress, and Senescence.
Neoplasms
Retraction: miR-96-5p enhances cell proliferation and invasion via targeted regulation of ZDHHC5 in gastic cancer.
Neoplasms
S-acylated Golga7b stabilises DHHC5 at the plasma membrane to regulate cell adhesion.
Neoplasms
Systematic siRNA Screen Unmasks NSCLC Growth Dependence by Palmitoyltransferase DHHC5.
Nervous System Diseases
Palmitoyl Acyltransferase zD17 Mediates Neuronal Responses in Acute Ischemic Brain Injury by Regulating JNK Activation in a Signaling Module.
Neuralgia
Palmitoylation of ?-catenin promotes kinesin-mediated membrane trafficking of Na
Osteoporosis
Mice with alopecia, osteoporosis, and systemic amyloidosis due to mutation in Zdhhc13, a gene coding for palmitoyl acyltransferase.
Paralysis
Sudden death due to paralysis and synaptic and behavioral deficits when Hip14/Zdhhc17 is deleted in adult mice.
Prostatic Neoplasms
Antioxidant functions of DHHC3 suppress anti-cancer drug activities.
Stomach Neoplasms
miR-96-5p enhances cell proliferation and invasion via targeted regulation of ZDHHC5 in gastric cancer.
Tuberculosis
Characterization of protein acyltransferase function of recombinant purified GlnA1 from Mycobacterium tuberculosis: A moon lighting property.
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evolution
homology and phylogeny of DHHC proteins, overview
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
evolution
homology and phylogeny of DHHC proteins, overview
evolution
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the enzyme is an Asp-His-His-Cys motif (DHHC) palmitoyl transferase family member
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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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
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
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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 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
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
additional information
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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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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
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COS-7 cells are cotransfected with the cDNAs for eNOS and HA-tagged DHHC-21
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DHHC16, cloning of cDNA from Jurkat cells, insertion into pmCFP via pENTR/D-TOPO, and expression in T cells deficient in Lck, the T lymphocyte-specific Src family kinase, transient expression of cyan fluorescent protein CFP-tagged DHHC16 in HEK293Acells
DHHC2, cloning of cDNA from Jurkat cells, insertion into pmCFP via pENTR/D-TOPO, and expression in T cells deficient in Lck, the T lymphocyte-specific Src family kinase, transient expression of cyan fluorescent protein CFP-tagged DHHC2 in HEK293Acells
DHHC4, cloning of cDNA from Jurkat cells, insertion into pmCFP via pENTR/D-TOPO, and expression in T cells deficient in Lck, the T lymphocyte-specific Src family kinase, transient expression of cyan fluorescent protein CFP-tagged DHHC4 in HEK293A cells, quantitative expression analysis
expression of FLAG- and His6-tagged DHHC2 in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system
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expression of human DHHC9 in Saccharomyces cerevisiae fails to complement an erf2DELTA strain
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Linder, M. E.; Deschenes, R. J.
New insights into the mechanisms of protein palmitoylation
Biochemistry
42
4311-4320
2003
Saccharomyces cerevisiae, Drosophila melanogaster, Homo sapiens, Rattus norvegicus
brenda
Jennings, B. C.; Linder, M. E.
DHHC protein S-acyltransferases use similar ping-pong kinetic mechanisms but display different acyl-CoA specificities
J. Biol. Chem.
287
7236-7245
2012
Homo sapiens, Mus musculus (Q8R173)
brenda
Fernandez-Hernando, C.; Fukata, M.; Bernatchez, P. N.; Fukata, Y.; Lin, M. I.; Bredt, D. S.; Sessa, W. C.
Identification of Golgi-localized acyl transferases that palmitoylate and regulate endothelial nitric oxide synthase
J. Cell. Biol.
174
369-377
2006
Homo sapiens
brenda
Mitchell, D. A.; Vasudevan, A.; Linder, M. E.; Deschenes, R. J.
Protein palmitoylation by a family of DHHC protein S-acyltransferases
J. Lipid Res.
47
1118-1127
2006
Drosophila melanogaster, Homo sapiens, Homo sapiens (Q8IUH5), Homo sapiens (Q9Y397), Saccharomyces cerevisiae
brenda
Zeidman, R.; Buckland, G.; Cebecauer, M.; Eissmann, P.; Davis, D.M.; Magee, A.I.
DHHC2 is a protein S-acyltransferase for Lck
Mol. Membr. Biol.
28
473-486
2011
Homo sapiens (Q969W1), Homo sapiens (Q9NPG8), Homo sapiens (Q9UIJ5)
brenda
Sharma, C.; Wang, H.X.; Li, Q.; Knoblich, K.; Reisenbichler, E.S.; Richardson, A.L.; Hemler, M.E.
Protein acyltransferase DHHC3 regulates breast tumor growth, oxidative stress, and senescence
Cancer Res.
77
6880-6890
2017
Homo sapiens (Q9NYG2), Homo sapiens
brenda
Ko, P.J.; Woodrow, C.; Dubreuil, M.M.; Martin, B.R.; Skouta, R.; Bassik, M.C.; Dixon, S.J.
A ZDHHC5-GOLGA7 protein acyltransferase complex promotes nonapoptotic cell death
Cell Chem. Biol.
26
1716-1724
2019
Homo sapiens (Q9C0B5)
brenda