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Information on EC 2.3.1.225 - protein S-acyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P39010
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2.3.1.225 protein S-acyltransferaseIUBMB Comments
The enzyme catalyses the posttranslational protein palmitoylation that plays a role in protein-membrane interactions, protein trafficking, and enzyme activity. Palmitoylation increases the hydrophobicity of proteins or protein domains and contributes to their membrane association.
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Word Map
- 2.3.1.225
-
palmitoylation
- palmitate
-
s-acylation
- huntingtin
-
palmitoylation-dependent
-
huntingtin-interacting
- 2-bromopalmitate
-
s-acyltransferases
- medicine
-
autoacylation
-
16-carbon
- snap25
-
acyl-acyl
-
palmitoylation-deficient
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
hip14, dhhc3, palmitoyl acyltransferase, dhhc5, zdhhc5, dhhc2, akr1p, zdhhc3, protein acyltransferase, dhhc protein, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Erf2
Pfa3
Pfa4
Swf1
SYSTEMATIC NAME
IUBMB Comments
palmitoyl-CoA:[protein]-L-cysteine S-palmitoyltransferase
The enzyme catalyses the posttranslational protein palmitoylation that plays a role in protein-membrane interactions, protein trafficking, and enzyme activity. Palmitoylation increases the hydrophobicity of proteins or protein domains and contributes to their membrane association.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
palmitoyl-CoA + [Lcb4 protein]-L-cysteine
[Lcb4 prpotein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Meh1 protein]-L-cysteine
[Meh1 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Sna4 protein]-L-cysteine
[Sna4 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Vac8 protein]-L-cysteine
[Vac8 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Yck1 protein]-L-cysteine
[Yck1 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Yck2 protein]-L-cysteine
[Yck2 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Yck3 protein]-L-cysteine
[Yck3 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Ykl047w protein]-L-cysteine
[Ykl047w protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Ypl199c protein]-L-cysteine
[Ypl199c protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Ypl236c protein]-L-cysteine
[Ypl236c protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Chs3]-L-cysteine
[Chs3]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Gpa1 protein]-L-cysteine
[Gpa1 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Gpa2 protein]-L-cysteine
[Gpa2 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [H-Ras]-L-cysteine
[H-Ras]-S-palmitoyl-L-cysteine + CoA
-
H-Ras is palmitoylated at two cysteine residues immediately upstream of its farnesylated and carboxylmethylated C-terminus, substrate of APT1
-
-
r
palmitoyl-CoA + [Lcb4 protein]-L-cysteine
[Lcb4 prpotein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Meh1 protein]-L-cysteine
[Meh1 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Mnn1 protein]-L-cysteine
[Mnn1 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Mnn10 protein]-L-cysteine
[Mnn10 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Mnn11 protein]-L-cysteine
[Mnn11 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Pfa4]-L-cysteine
[Pfa4]-S-palmitoyl-L-cysteine + CoA
autoacylation
-
-
?
palmitoyl-CoA + [Pin2 protein]-L-cysteine
[Pin2 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Psr1 protein]-L-cysteine
[Psr1 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Ras1 protein]-L-cysteine
[Ras1 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Ras1p]-L-cysteine
[Ras1p]-S-palmitoyl-L-cysteine + CoA
-
Ras oncogene homologues, Ras1p and Ras2p, undergo reversible palmitoylation by Erf2p on a Cys residue adjacent to the canonical CaaX box prenylation motif at the C-terminus of the protein
-
-
r
palmitoyl-CoA + [Ras2 protein]-L-cysteine
[Ras2 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Ras2p]-L-cysteine
[Ras2p]-S-palmitoyl-L-cysteine + CoA
-
Ras oncogene homologues, Ras1p and Ras2p, undergo reversible palmitoylation by Erf2p on a Cys residue adjacent to the canonical CaaX box prenylation motif at the C-terminus of the protein. both Erf2p and Erf4p are involved in the palmitoylation of Ras2p, overview. Mutation of the palmitoylated Cys to Ser abolishes palmitoylation and results in a mislocalization of Ras2p from the plasma membrane to endomembranes. Yeast Erf2p-Erf4p Ras PAT work best with yeast Ras2 protein and less well with mammalian myristoylated GiR subunits or mammalian Ha-Ras. Long chain acyl-CoA substrates, 16 and 18 carbons, are preferred over shorter acyl chains, below 14 carbons
-
-
r
palmitoyl-CoA + [Ras]-L-cysteine
[Ras]-S-palmitoyl-L-cysteine + CoA
-
yeast Ras protein is a substrate of Erf2
-
-
r
palmitoyl-CoA + [RGS4]-L-cysteine
[RGS4]-S-palmitoyl-L-cysteine + CoA
-
RGS4 is palmitoylated at two cysteine residues near its amino terminus (C2 and C12) and a cysteine residue in the RGS core domain, substrate of APT1
-
-
r
palmitoyl-CoA + [Rho2 protein]-L-cysteine
[Rho2 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Rho3 protein]-L-cysteine
[Rho3 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Ste18 protein]-L-cysteine
[Ste18 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Swf1]-L-cysteine
[Swf1]-S-palmitoyl-L-cysteine + CoA
autoacylation
-
-
?
palmitoyl-CoA + [Vac8 protein]-L-cysteine
[Vac8 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Yck2p]-L-cysteine
[Yck2p]-S-palmitoyl-L-cysteine + CoA
-
Akr1p is a palmitoyltransferase for Yck2p that catalyzes the transfer of palmitate from palmitoyl-CoA to a C-terminal Cys residue, formation of an Akr1p-palmitoyl intermediate
-
-
r
palmitoyl-CoA + [Yck2]-L-cysteine
[Yck2]-S-palmitoyl-L-cysteine + CoA
-
yeast casein kinase Yck2 is a substrate of Akr1
-
-
r
palmitoyl-CoA + [Ycp4 protein]-L-cysteine
[Ycp4 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Ygl108 protein]-L-cysteine
[Ygl108 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Gialpha1]-L-cysteine
[Gialpha1]-S-palmitoyl-L-cysteine + CoA
-
Gialpha1 is myristoylated at its amino terminus and palmitoylated at an adjacent cysteine, preferred substrate of APT1
-
-
r
palmitoyl-CoA + [Gialpha1]-L-cysteine
[Gialpha1]-S-palmitoyl-L-cysteine + CoA
-
GiR1 is myristoylated at its amino terminus and palmitoylated at an adjacent cysteine, substrate of APT1
-
-
r
palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
-
r
palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
-
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
-
-
r
palmitoyl-CoA + [Snc1]-L-cysteine
[Snc1]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Snc1]-L-cysteine
[Snc1]-S-palmitoyl-L-cysteine + CoA
-
yeast SNARES Snc1, Syn8, and Tlg1 are substrates of Swf1, palmitoylating at cysteine residues near the cytoplasmic side of their single transmembrane span
-
-
r
palmitoyl-CoA + [Syn8]-L-cysteine
[Syn8]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Syn8]-L-cysteine
[Syn8]-S-palmitoyl-L-cysteine + CoA
-
yeast SNARES Snc1, Syn8, and Tlg1 are substrates of Swf1, palmitoylating at cysteine residues near the cytoplasmic side of their single transmembrane span
-
-
r
palmitoyl-CoA + [Tlg1]-L-cysteine
[Tlg1]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Tlg1]-L-cysteine
[Tlg1]-S-palmitoyl-L-cysteine + CoA
-
yeast SNARES Snc1, Syn8, and Tlg1 are substrates of Swf1, palmitoylating at cysteine residues near the cytoplasmic side of their single transmembrane span
-
-
r
palmitoyl-CoA + [Vac8p]-L-cysteine
[Vac8p]-S-palmitoyl-L-cysteine + CoA
-
recombinant Vac8p is palmitoylated when added to vacuoles and is anchored to membranes after modi¢cation
-
-
r
palmitoyl-CoA + [Vac8p]-L-cysteine
[Vac8p]-S-palmitoyl-L-cysteine + CoA
-
recombinant non-myristoylated His6-Vac8p and myristoylated Vac8-GST
-
-
r
palmitoyl-CoA + [Vac8]-L-cysteine
[Vac8]-S-palmitoyl-L-cysteine + CoA
-
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
-
-
r
palmitoyl-CoA + [Vac8]-L-cysteine
[Vac8]-S-palmitoyl-L-cysteine + CoA
-
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
-
-
r
additional information
?
-
-
in the absence of cellular factors, palmitoyl-CoA is capable of spontaneously S-acylating cysteinyl thiols, overview. Effects of APT1 on palmitate turnover on Gsalpha are not due to effects on the rate of turnover of palmitoyl-CoA
-
-
?
additional information
?
-
-
APT1 has acyl-CoA hydrolase activity
-
-
?
additional information
?
-
-
PATis speci¢c for palmitoyl-CoA, since myristoyl- and stearyl-CoA can compete with labeled Pal-CoA only at 10-fold higher amounts
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
palmitoyl-CoA + [Gialpha1]-L-cysteine
[Gialpha1]-S-palmitoyl-L-cysteine + CoA
-
Gialpha1 is myristoylated at its amino terminus and palmitoylated at an adjacent cysteine, preferred substrate of APT1
-
-
r
palmitoyl-CoA + [H-Ras]-L-cysteine
[H-Ras]-S-palmitoyl-L-cysteine + CoA
-
H-Ras is palmitoylated at two cysteine residues immediately upstream of its farnesylated and carboxylmethylated C-terminus, substrate of APT1
-
-
r
palmitoyl-CoA + [Ras1p]-L-cysteine
[Ras1p]-S-palmitoyl-L-cysteine + CoA
-
Ras oncogene homologues, Ras1p and Ras2p, undergo reversible palmitoylation by Erf2p on a Cys residue adjacent to the canonical CaaX box prenylation motif at the C-terminus of the protein
-
-
r
palmitoyl-CoA + [Ras2p]-L-cysteine
[Ras2p]-S-palmitoyl-L-cysteine + CoA
-
Ras oncogene homologues, Ras1p and Ras2p, undergo reversible palmitoylation by Erf2p on a Cys residue adjacent to the canonical CaaX box prenylation motif at the C-terminus of the protein. both Erf2p and Erf4p are involved in the palmitoylation of Ras2p, overview. Mutation of the palmitoylated Cys to Ser abolishes palmitoylation and results in a mislocalization of Ras2p from the plasma membrane to endomembranes. Yeast Erf2p-Erf4p Ras PAT work best with yeast Ras2 protein and less well with mammalian myristoylated GiR subunits or mammalian Ha-Ras. Long chain acyl-CoA substrates, 16 and 18 carbons, are preferred over shorter acyl chains, below 14 carbons
-
-
r
palmitoyl-CoA + [Ras]-L-cysteine
[Ras]-S-palmitoyl-L-cysteine + CoA
-
yeast Ras protein is a substrate of Erf2
-
-
r
palmitoyl-CoA + [RGS4]-L-cysteine
[RGS4]-S-palmitoyl-L-cysteine + CoA
-
RGS4 is palmitoylated at two cysteine residues near its amino terminus (C2 and C12) and a cysteine residue in the RGS core domain, substrate of APT1
-
-
r
palmitoyl-CoA + [Vac8p]-L-cysteine
[Vac8p]-S-palmitoyl-L-cysteine + CoA
-
recombinant Vac8p is palmitoylated when added to vacuoles and is anchored to membranes after modi¢cation
-
-
r
palmitoyl-CoA + [Vac8]-L-cysteine
[Vac8]-S-palmitoyl-L-cysteine + CoA
-
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
-
-
r
palmitoyl-CoA + [Yck2p]-L-cysteine
[Yck2p]-S-palmitoyl-L-cysteine + CoA
-
Akr1p is a palmitoyltransferase for Yck2p that catalyzes the transfer of palmitate from palmitoyl-CoA to a C-terminal Cys residue, formation of an Akr1p-palmitoyl intermediate
-
-
r
palmitoyl-CoA + [Yck2]-L-cysteine
[Yck2]-S-palmitoyl-L-cysteine + CoA
-
yeast casein kinase Yck2 is a substrate of Akr1
-
-
r
additional information
?
-
-
in the absence of cellular factors, palmitoyl-CoA is capable of spontaneously S-acylating cysteinyl thiols, overview. Effects of APT1 on palmitate turnover on Gsalpha are not due to effects on the rate of turnover of palmitoyl-CoA
-
-
?
palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
-
r
palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
-
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
-
-
r
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
both intermediate formation and acyl transfer to Yck2p by Akr1p are stimulated by ATP
Erf4
-
required by Erf2 for activity, Erf2 and Erf4 copurify as a complex and interact in a yeast two-hybrid assay
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
ERF2 encodes a protein with four predicted membrane-spanning domains
-
ERF2 encodes a protein with four predicted membrane-spanning domains
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
the enzymes belong to the DHHC family, homology and phylogeny of DHHC proteins, overview
malfunction
physiological function
additional information
malfunction
-
apt1 null cells exhibit almost no acylprotein thioesterase activity toward palmitoyl-Gialpha1
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
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
physiological function
-
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
-
vacuole fusion requires Sec18p-dependent acylation of the armadillo-repeat protein Vac8p
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
additional information
-
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
yeast S-palmitoyltransferases contain DHHC-cysteine rich domains
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C164R
substitution of the conserved cysteine in the DHHC motif. Overexpression of this mutant allows to partially complement an isoform Swf1 gene deletion and to acylate the Swf1 substrates Tlg1, Syn8, and Snc1. Mutant protein is not acylated
H162Q
substitution in the DHHC motif, mutant is partially active
H162Q/C164R
substitutions in the DHHC motif, mutant is inactive
additional information
additional information
substitution of the conserved cysteine in the DHHC motif to DHHA or DHHR still allows for acylation of substrate Chs3. Mutant protein is not acylated
additional information
substitution of the conserved cysteine in the DHHC motif to DHHA or DHHR still allows for acylation of substrate Chs3. Mutant protein is not acylated
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Veit, M.; Dietrich, L.E.P.; Ungermann, C.
Biochemical characterization of the vacuolar palmitoyl acyltransferase
FEBS Lett.
540
101-105
2003
Saccharomyces cerevisiae, Saccharomyces cerevisiae BJ3505
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
Gonzalez Montoro, A.; Chumpen Ramirez, S.; Valdez Taubas, J.
The canonical DHHC motif is not absolutely required for the activity of the yeast S-acyltransferases Swf1 and Pfa4
J. Biol. Chem.
290
22448-22459
2015
Saccharomyces cerevisiae (Q04629), Saccharomyces cerevisiae (Q12006)
Li, Y.; Qi, B.
Progress toward understanding protein S-acylation Prospective in plants
Front. Plant Sci.
8
346
2017
Saccharomyces cerevisiae (P39010), Saccharomyces cerevisiae (P42836), Saccharomyces cerevisiae (Q03289), Saccharomyces cerevisiae (Q04629), Saccharomyces cerevisiae (Q06551), Saccharomyces cerevisiae (Q12006), Saccharomyces cerevisiae ATCC 204508 (P39010), Saccharomyces cerevisiae ATCC 204508 (P42836), Saccharomyces cerevisiae ATCC 204508 (Q03289), Saccharomyces cerevisiae ATCC 204508 (Q04629), Saccharomyces cerevisiae ATCC 204508 (Q06551), Saccharomyces cerevisiae ATCC 204508 (Q12006)
EXTERNAL LINKS (specific for EC-Number 2.3.1.225)
Transporter Classification Database (TCDB): 8.A.114.1.5, 8.A.114.1.3, 8.A.114.1.7, 8.A.114.1.1, 8.A.114.1.2, 8.A.114.1.6, 8.A.114.1.4
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