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Literature summary extracted from

  • Mitchell, D. A.; Vasudevan, A.; Linder, M. E.; Deschenes, R. J.
    Protein palmitoylation by a family of DHHC protein S-acyltransferases (2006), J. Lipid Res., 47, 1118-1127.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.3.1.225 Erf4 required by Erf2 for activity, Erf2 and Erf4 copurify as a complex and interact in a yeast two-hybrid assay Saccharomyces cerevisiae

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.225 expression of human DHHC9 in Saccharomyces cerevisiae fails to complement an erf2DELTA strain Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.225 C159S the DHHC15 mutant shows reduced activity compared to the wild-type Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.225 2-Bromopalmitate
-
Drosophila melanogaster
2.3.1.225 2-Bromopalmitate
-
Homo sapiens
2.3.1.225 2-Bromopalmitate
-
Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.1.225 cytoplasmic vesicle HIP14 resides on the Golgi and can be observed on cytoplasmic vesicles Homo sapiens 31410
-
2.3.1.225 endoplasmic reticulum membrane ERF2 encodes a protein with four predicted membrane-spanning domains Saccharomyces cerevisiae 5789
-
2.3.1.225 Golgi membrane HIP14 resides on the Golgi and can be observed on cytoplasmic vesicles Homo sapiens 139
-
2.3.1.225 plasma membrane ERF2 encodes a protein with four predicted membrane-spanning domains Saccharomyces cerevisiae 5886
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.225 42000
-
x * 42000, Erf2 Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.225 palmitoyl-CoA + [Ga protein]-L-cysteine Homo sapiens substrate of DHHC3 and DHHC7 [Ga protein]-S-palmitoyl-L-cysteine + CoA
-
r
2.3.1.225 palmitoyl-CoA + [GAP-43 protein]-L-cysteine Homo sapiens substrate of DHHC7 and DHHC15 [GAP-43 protein]-S-palmitoyl-L-cysteine + CoA
-
r
2.3.1.225 palmitoyl-CoA + [Lck]-L-cysteine Homo sapiens nonreceptor tyrosine kinase [Lck]-S-palmitoyl-L-cysteine + CoA
-
r
2.3.1.225 palmitoyl-CoA + [protein]-L-cysteine Drosophila melanogaster
-
[protein]-S-palmitoyl-L-cysteine + CoA
-
r
2.3.1.225 palmitoyl-CoA + [protein]-L-cysteine Homo sapiens
-
[protein]-S-palmitoyl-L-cysteine + CoA
-
r
2.3.1.225 palmitoyl-CoA + [protein]-L-cysteine Saccharomyces cerevisiae
-
[protein]-S-palmitoyl-L-cysteine + CoA
-
r
2.3.1.225 palmitoyl-CoA + [PSD95]-L-cysteine Homo sapiens possible substrate of DHHC15 and, to a lesser extent, DHHC2, DHHC3, and DHHC7 [Ras]-S-palmitoyl-L-cysteine + CoA
-
r
2.3.1.225 palmitoyl-CoA + [Ras]-L-cysteine Homo sapiens by Ras PAT containing the DHHC9 protein subunit [Ras]-S-palmitoyl-L-cysteine + CoA
-
r
2.3.1.225 palmitoyl-CoA + [Ras]-L-cysteine Saccharomyces cerevisiae yeast Ras protein is a substrate of Erf2 [Ras]-S-palmitoyl-L-cysteine + CoA
-
r
2.3.1.225 palmitoyl-CoA + [SNAP-25]-L-cysteine Homo sapiens substrate of DHHC3 and DHHC7 [SNAP-25]-S-palmitoyl-L-cysteine + CoA
-
r
2.3.1.225 palmitoyl-CoA + [Vac8]-L-cysteine Saccharomyces cerevisiae Vac8 is a substrate of Pfa3, Vac8 is a myristoylated and palmitoylated protein that localizes to the vacuolar membrane and is required for vacuolar fusion [Vac8]-S-palmitoyl-L-cysteine + CoA
-
r
2.3.1.225 palmitoyl-CoA + [Yck2]-L-cysteine Saccharomyces cerevisiae yeast casein kinase Yck2 is a substrate of Akr1 [Yck2]-S-palmitoyl-L-cysteine + CoA
-
r

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.225 Drosophila melanogaster
-
-
-
2.3.1.225 Homo sapiens
-
-
-
2.3.1.225 Homo sapiens Q8IUH5 DHHC17 or HIP14
-
2.3.1.225 Homo sapiens Q9Y397 DHHC9
-
2.3.1.225 Saccharomyces cerevisiae
-
genes ERF2, PFA3, SWF1, and AKR1
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.1.225 brain DHHC9 Homo sapiens
-
2.3.1.225 colon DHHC9 Homo sapiens
-
2.3.1.225 heart DHHC9 Homo sapiens
-
2.3.1.225 kidney DHHC9 Homo sapiens
-
2.3.1.225 liver DHHC9 Homo sapiens
-
2.3.1.225 lung DHHC9 Homo sapiens
-
2.3.1.225 additional information HIP14 is ubiquitously expressed Homo sapiens
-
2.3.1.225 additional information the Ras PAT activity of DHHC9/GCP16 appears to be restricted to a subset of tissues Homo sapiens
-
2.3.1.225 placenta DHHC9 Homo sapiens
-
2.3.1.225 skeletal muscle DHHC9 Homo sapiens
-
2.3.1.225 small intestine DHHC9 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.225 additional information 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 Homo sapiens ?
-
?
2.3.1.225 palmitoyl-CoA + [Ga protein]-L-cysteine substrate of DHHC3 and DHHC7 Homo sapiens [Ga protein]-S-palmitoyl-L-cysteine + CoA
-
r
2.3.1.225 palmitoyl-CoA + [GAD65]-L-cysteine
-
Homo sapiens [GAD65]-S-palmitoyl-L-cysteine + CoA
-
r
2.3.1.225 palmitoyl-CoA + [GAP-43 protein]-L-cysteine substrate of DHHC7 and DHHC15 Homo sapiens [GAP-43 protein]-S-palmitoyl-L-cysteine + CoA
-
r
2.3.1.225 palmitoyl-CoA + [htt(1-548)]-L-cysteine N-terminal fragment of htt(1-548) Homo sapiens [htt(1-548)]-S-palmitoyl-L-cysteine + CoA
-
r
2.3.1.225 palmitoyl-CoA + [Lck]-L-cysteine nonreceptor tyrosine kinase Homo sapiens [Lck]-S-palmitoyl-L-cysteine + CoA
-
r
2.3.1.225 palmitoyl-CoA + [protein]-L-cysteine
-
Drosophila melanogaster [protein]-S-palmitoyl-L-cysteine + CoA
-
r
2.3.1.225 palmitoyl-CoA + [protein]-L-cysteine
-
Homo sapiens [protein]-S-palmitoyl-L-cysteine + CoA
-
r
2.3.1.225 palmitoyl-CoA + [protein]-L-cysteine
-
Saccharomyces cerevisiae [protein]-S-palmitoyl-L-cysteine + CoA
-
r
2.3.1.225 palmitoyl-CoA + [PSD-95]-L-cysteine low activity Homo sapiens [PSD-95]-S-palmitoyl-L-cysteine + CoA
-
r
2.3.1.225 palmitoyl-CoA + [PSD95]-L-cysteine
-
Homo sapiens [Ras]-S-palmitoyl-L-cysteine + CoA
-
r
2.3.1.225 palmitoyl-CoA + [PSD95]-L-cysteine possible substrate of DHHC15 and, to a lesser extent, DHHC2, DHHC3, and DHHC7 Homo sapiens [Ras]-S-palmitoyl-L-cysteine + CoA
-
r
2.3.1.225 palmitoyl-CoA + [Ras]-L-cysteine by Ras PAT containing the DHHC9 protein subunit Homo sapiens [Ras]-S-palmitoyl-L-cysteine + CoA
-
r
2.3.1.225 palmitoyl-CoA + [Ras]-L-cysteine yeast Ras protein is a substrate of Erf2 Saccharomyces cerevisiae [Ras]-S-palmitoyl-L-cysteine + CoA
-
r
2.3.1.225 palmitoyl-CoA + [SNAP-25]-L-cysteine
-
Homo sapiens [SNAP-25]-S-palmitoyl-L-cysteine + CoA
-
r
2.3.1.225 palmitoyl-CoA + [SNAP-25]-L-cysteine substrate of DHHC3 and DHHC7 Homo sapiens [SNAP-25]-S-palmitoyl-L-cysteine + CoA
-
r
2.3.1.225 palmitoyl-CoA + [Snc1]-L-cysteine yeast SNARES Snc1, Syn8, and Tlg1 are substrates of Swf1, palmitoylating at cysteine residues near the cytoplasmic side of their single transmembrane span Saccharomyces cerevisiae [Snc1]-S-palmitoyl-L-cysteine + CoA
-
r
2.3.1.225 palmitoyl-CoA + [Syn8]-L-cysteine yeast SNARES Snc1, Syn8, and Tlg1 are substrates of Swf1, palmitoylating at cysteine residues near the cytoplasmic side of their single transmembrane span Saccharomyces cerevisiae [Syn8]-S-palmitoyl-L-cysteine + CoA
-
r
2.3.1.225 palmitoyl-CoA + [synaptotagmin I ]-L-cysteine
-
Homo sapiens [synaptotagmin I ]-S-palmitoyl-L-cysteine + CoA
-
r
2.3.1.225 palmitoyl-CoA + [Tlg1]-L-cysteine yeast SNARES Snc1, Syn8, and Tlg1 are substrates of Swf1, palmitoylating at cysteine residues near the cytoplasmic side of their single transmembrane span Saccharomyces cerevisiae [Tlg1]-S-palmitoyl-L-cysteine + CoA
-
r
2.3.1.225 palmitoyl-CoA + [Vac8]-L-cysteine Vac8 is a substrate of Pfa3, Vac8 is a myristoylated and palmitoylated protein that localizes to the vacuolar membrane and is required for vacuolar fusion Saccharomyces cerevisiae [Vac8]-S-palmitoyl-L-cysteine + CoA
-
r
2.3.1.225 palmitoyl-CoA + [Vac8]-L-cysteine Vac8 is a substrate of Pfa3 performing S-palmitoylation of up to three N-terminal cysteines, Vac8 is N-myristoylated at an N-terminal glycine residue. Vac8 is not palmitoylated by Akr1, Erf2/Erf4, Pfa4, or Pfa5 in vitro Saccharomyces cerevisiae [Vac8]-S-palmitoyl-L-cysteine + CoA
-
r
2.3.1.225 palmitoyl-CoA + [Yck2]-L-cysteine yeast casein kinase Yck2 is a substrate of Akr1 Saccharomyces cerevisiae [Yck2]-S-palmitoyl-L-cysteine + CoA
-
r

Subunits

EC Number Subunits Comment Organism
2.3.1.225 ? x * 42000, Erf2 Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
2.3.1.225 Akr1
-
Saccharomyces cerevisiae
2.3.1.225 DHHC17
-
Homo sapiens
2.3.1.225 Erf2
-
Saccharomyces cerevisiae
2.3.1.225 HIP14
-
Homo sapiens
2.3.1.225 Pat
-
Drosophila melanogaster
2.3.1.225 Pat
-
Homo sapiens
2.3.1.225 Pat
-
Saccharomyces cerevisiae
2.3.1.225 Pfa3
-
Saccharomyces cerevisiae
2.3.1.225 protein acyltransferase
-
Drosophila melanogaster
2.3.1.225 protein acyltransferase
-
Homo sapiens
2.3.1.225 protein acyltransferase
-
Saccharomyces cerevisiae
2.3.1.225 Ras PAT
-
Homo sapiens
2.3.1.225 Swf1
-
Saccharomyces cerevisiae

General Information

EC Number General Information Comment Organism
2.3.1.225 evolution homology and phylogeny of DHHC proteins, overview Homo sapiens
2.3.1.225 evolution the enzymes belong to the DHHC family, homology and phylogeny of DHHC proteins, overview Saccharomyces cerevisiae
2.3.1.225 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 Homo sapiens
2.3.1.225 malfunction 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 Saccharomyces cerevisiae
2.3.1.225 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 Homo sapiens
2.3.1.225 additional information 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 Saccharomyces cerevisiae
2.3.1.225 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. 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 Saccharomyces cerevisiae
2.3.1.225 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 Drosophila melanogaster
2.3.1.225 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 Homo sapiens
2.3.1.225 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 Homo sapiens
2.3.1.225 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 Homo sapiens