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myristoyl-CoA + [Gialpha1]-L-cysteine
[protein]-S-myristoyl-L-cysteine + CoA
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GiR1 is myristoylated at its N-terminus and palmitoylated at an adjacent cysteine, substrate of APT1
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palmitoyl-CoA + [Chs3]-L-cysteine
[Chs3]-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 + [G protein alpha subunit Gialpha1]-L-cysteine
[G protein alpha subunit Gialpha1]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [G protein alpha subunit]-L-cysteine
[G protein alpha subunit]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [G-protein alpha subunit Galphai]-L-cysteine
[G-protein alpha subunit Galphai]-S-palmitoyl-L-cysteine + CoA
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-
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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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-
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palmitoyl-CoA + [GAD65]-L-cysteine
[GAD65]-S-palmitoyl-L-cysteine + CoA
-
-
-
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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 + [Gialpha1]-L-cysteine
[Gialpha1]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [GOalpha1]-L-cysteine
[GOalpha1]-S-palmitoyl-L-cysteine + CoA
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-
-
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r
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 + [GSalpha1]-L-cysteine
[GSalpha1]-S-palmitoyl-L-cysteine + CoA
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Gsa is not a myristoylated protein, but is palmitoylated at Cys3
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palmitoyl-CoA + [H-Ras]-L-cysteine
[H-Ras]-S-palmitoyl-L-cysteine + CoA
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 + [Lcb4 protein]-L-cysteine
[Lcb4 prpotein]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [Lck]-L-cysteine
[Lck]-S-palmitoyl-L-cysteine + CoA
nonreceptor tyrosine kinase
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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 + [N-myristoylated G-protein alphai1]-L-cysteine
[N-myristoylated G-protein alphai1]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [N-myristoylated Gly-Cys-Gly tripeptide]-L-cysteine
[N-myristoylated Gly-Cys-Gly tripeptide]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [Pat10]-L-cysteine
[PAT10]-S-palmitoyl-L-cysteine + CoA
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autoacylation
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?
palmitoyl-CoA + [PAT14]-L-cysteine
[PAT14]-S-palmitoyl-L-cysteine + CoA
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autoacylation
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?
palmitoyl-CoA + [Pfa4]-L-cysteine
[Pfa4]-S-palmitoyl-L-cysteine + CoA
autoacylation
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-
?
palmitoyl-CoA + [phospholemman]-L-cysteine
[phospholemman]-S-palmitoyl-L-cysteine + CoA
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isoform DHHC5 palmitoylates cardiac phosphoprotein phospholemman at two juxtamembrane cysteines, C40 and C42. C40 is the principal palmitoylation site
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?
palmitoyl-CoA + [Pin2 protein]-L-cysteine
[Pin2 protein]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [PSD-95]-L-cysteine
[PSD-95]-S-palmitoyl-L-cysteine + CoA
low activity
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palmitoyl-CoA + [PSD95]-L-cysteine
[Ras]-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
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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
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palmitoyl-CoA + [Ras2 protein]-L-cysteine
[Ras2 protein]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [Ras2p]-L-cysteine
[Ras2p]-S-palmitoyl-L-cysteine + CoA
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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
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palmitoyl-CoA + [Ras]-L-cysteine
[Ras]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [RGS4]-L-cysteine
[RGS4]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [Rho2 protein]-L-cysteine
[Rho2 protein]-S-palmitoyl-L-cysteine + CoA
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-
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?
palmitoyl-CoA + [Rho3 protein]-L-cysteine
[Rho3 protein]-S-palmitoyl-L-cysteine + CoA
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-
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?
palmitoyl-CoA + [rhodopsin]-L-cysteine
[rhodopsin]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [short lipid-modified cysteinyl-containing peptide]-L-cysteine
[short lipid-modified cysteinyl-containing peptide]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [Sna4 protein]-L-cysteine
[Sna4 protein]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [SNAP-25]-L-cysteine
[SNAP-25]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [Snc1]-L-cysteine
[Snc1]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [Ste18 protein]-L-cysteine
[Ste18 protein]-S-palmitoyl-L-cysteine + CoA
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-
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?
palmitoyl-CoA + [Swf1]-L-cysteine
[Swf1]-S-palmitoyl-L-cysteine + CoA
autoacylation
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?
palmitoyl-CoA + [Syn8]-L-cysteine
[Syn8]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [synaptotagmin I ]-L-cysteine
[synaptotagmin I ]-S-palmitoyl-L-cysteine + CoA
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palmitoyl-CoA + [Tlg1]-L-cysteine
[Tlg1]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [Vac8 protein]-L-cysteine
[Vac8 protein]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [Vac8p]-L-cysteine
[Vac8p]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [Vac8]-L-cysteine
[Vac8]-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
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?
palmitoyl-CoA + [Yck2p]-L-cysteine
[Yck2p]-S-palmitoyl-L-cysteine + CoA
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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
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palmitoyl-CoA + [Yck2]-L-cysteine
[Yck2]-S-palmitoyl-L-cysteine + CoA
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yeast casein kinase Yck2 is a substrate of Akr1
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palmitoyl-CoA + [Yck3 protein]-L-cysteine
[Yck3 protein]-S-palmitoyl-L-cysteine + CoA
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-
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?
palmitoyl-CoA + [Ycp4 protein]-L-cysteine
[Ycp4 protein]-S-palmitoyl-L-cysteine + CoA
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-
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?
palmitoyl-CoA + [Ygl108 protein]-L-cysteine
[Ygl108 protein]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [Ykl047w protein]-L-cysteine
[Ykl047w protein]-S-palmitoyl-L-cysteine + CoA
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-
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?
palmitoyl-CoA + [Ypl199c protein]-L-cysteine
[Ypl199c protein]-S-palmitoyl-L-cysteine + CoA
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-
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?
palmitoyl-CoA + [Ypl236c protein]-L-cysteine
[Ypl236c protein]-S-palmitoyl-L-cysteine + CoA
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-
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?
stearoyl-CoA + [rhodopsin]-L-cysteine
[rhodopsin]-S-stearoyl-L-cysteine + CoA
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Rhodopsin containing rod outer segment membranes prepared from fresh, dark-adapted bovine retinae
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r
additional information
?
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palmitoyl-CoA + [G protein alpha subunit Gialpha1]-L-cysteine
[G protein alpha subunit Gialpha1]-S-palmitoyl-L-cysteine + CoA
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purified recombinant Gialpha1
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palmitoyl-CoA + [G protein alpha subunit Gialpha1]-L-cysteine
[G protein alpha subunit Gialpha1]-S-palmitoyl-L-cysteine + CoA
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purified recombinant Gialpha1
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palmitoyl-CoA + [G protein alpha subunit]-L-cysteine
[G protein alpha subunit]-S-palmitoyl-L-cysteine + CoA
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palmitoyl-CoA + [G protein alpha subunit]-L-cysteine
[G protein alpha subunit]-S-palmitoyl-L-cysteine + CoA
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-
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palmitoyl-CoA + [Gialpha1]-L-cysteine
[Gialpha1]-S-palmitoyl-L-cysteine + CoA
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-
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r
palmitoyl-CoA + [Gialpha1]-L-cysteine
[Gialpha1]-S-palmitoyl-L-cysteine + CoA
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recombinant myristoylated G protein alpha subunit and bovine brain betagamma subunits. G-protein substrate specificity of PAT activity, overview. wild-type Gia1 and Gia1G203A mutant form heterotrimers with G protein betagammaC68S
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palmitoyl-CoA + [Gialpha1]-L-cysteine
[Gialpha1]-S-palmitoyl-L-cysteine + CoA
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GiR1 is myristoylated at its amino terminus and palmitoylated at an adjacent cysteine, substrate of APT1
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palmitoyl-CoA + [Gialpha1]-L-cysteine
[Gialpha1]-S-palmitoyl-L-cysteine + CoA
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GiR1 is myristoylated at its N-terminus and palmitoylated at an adjacent cysteine, substrate of APT1
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palmitoyl-CoA + [Gialpha1]-L-cysteine
[Gialpha1]-S-palmitoyl-L-cysteine + CoA
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G protein alpha subunit, wild-type Gia1 and Gia1G203A mutant form heterotrimers with G protein betagammaC68S, myristoylated or not myristoylated
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palmitoyl-CoA + [Gialpha1]-L-cysteine
[Gialpha1]-S-palmitoyl-L-cysteine + CoA
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Gialpha1 is myristoylated at its amino terminus and palmitoylated at an adjacent cysteine, preferred substrate of APT1
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palmitoyl-CoA + [Gialpha1]-L-cysteine
[Gialpha1]-S-palmitoyl-L-cysteine + CoA
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GiR1 is myristoylated at its amino terminus and palmitoylated at an adjacent cysteine, substrate of APT1
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r
palmitoyl-CoA + [Gpa1 protein]-L-cysteine
[Gpa1 protein]-S-palmitoyl-L-cysteine + CoA
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-
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?
palmitoyl-CoA + [Gpa1 protein]-L-cysteine
[Gpa1 protein]-S-palmitoyl-L-cysteine + CoA
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-
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?
palmitoyl-CoA + [Gpa2 protein]-L-cysteine
[Gpa2 protein]-S-palmitoyl-L-cysteine + CoA
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-
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?
palmitoyl-CoA + [Gpa2 protein]-L-cysteine
[Gpa2 protein]-S-palmitoyl-L-cysteine + CoA
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-
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?
palmitoyl-CoA + [H-Ras]-L-cysteine
[H-Ras]-S-palmitoyl-L-cysteine + CoA
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H-Ras is palmitoylated at two cysteine residues immediately upstream of its farnesylated and carboxylmethylated C-terminus, substrate of APT1
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palmitoyl-CoA + [H-Ras]-L-cysteine
[H-Ras]-S-palmitoyl-L-cysteine + CoA
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H-Ras is palmitoylated at two cysteine residues immediately upstream of its farnesylated and carboxylmethylated C-terminus, substrate of APT1
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palmitoyl-CoA + [H-Ras]-L-cysteine
[H-Ras]-S-palmitoyl-L-cysteine + CoA
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H-Ras is palmitoylated at two cysteine residues immediately upstream of its farnesylated and carboxylmethylated C-terminus, substrate of APT1
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palmitoyl-CoA + [Lcb4 protein]-L-cysteine
[Lcb4 prpotein]-S-palmitoyl-L-cysteine + CoA
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-
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?
palmitoyl-CoA + [Lcb4 protein]-L-cysteine
[Lcb4 prpotein]-S-palmitoyl-L-cysteine + CoA
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-
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?
palmitoyl-CoA + [Meh1 protein]-L-cysteine
[Meh1 protein]-S-palmitoyl-L-cysteine + CoA
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-
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?
palmitoyl-CoA + [Meh1 protein]-L-cysteine
[Meh1 protein]-S-palmitoyl-L-cysteine + CoA
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-
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?
palmitoyl-CoA + [Mnn1 protein]-L-cysteine
[Mnn1 protein]-S-palmitoyl-L-cysteine + CoA
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-
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?
palmitoyl-CoA + [Mnn1 protein]-L-cysteine
[Mnn1 protein]-S-palmitoyl-L-cysteine + CoA
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-
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?
palmitoyl-CoA + [Mnn10 protein]-L-cysteine
[Mnn10 protein]-S-palmitoyl-L-cysteine + CoA
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-
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?
palmitoyl-CoA + [Mnn10 protein]-L-cysteine
[Mnn10 protein]-S-palmitoyl-L-cysteine + CoA
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-
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?
palmitoyl-CoA + [Mnn11 protein]-L-cysteine
[Mnn11 protein]-S-palmitoyl-L-cysteine + CoA
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-
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?
palmitoyl-CoA + [Mnn11 protein]-L-cysteine
[Mnn11 protein]-S-palmitoyl-L-cysteine + CoA
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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 G-protein alphai1]-L-cysteine
[N-myristoylated G-protein alphai1]-S-palmitoyl-L-cysteine + CoA
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r
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 + [N-myristoylated Gly-Cys-Gly tripeptide]-L-cysteine
[N-myristoylated Gly-Cys-Gly tripeptide]-S-palmitoyl-L-cysteine + CoA
peptide substrate si tagged via ethylenediamine with fluorescent NBD
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palmitoyl-CoA + [Pin2 protein]-L-cysteine
[Pin2 protein]-S-palmitoyl-L-cysteine + CoA
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-
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?
palmitoyl-CoA + [Pin2 protein]-L-cysteine
[Pin2 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
B3DN87, O80685, Q0WQK2, Q3EBC2, Q3EC11, Q500Z2, Q52T38, Q5M757, Q6DR03, Q7XA86, Q8L5Y5, Q8VYP5, Q8VYS8, Q93VV0, Q94C49, Q9C533, Q9FLM3, Q9LIE4, Q9LIH7, Q9M115, Q9M1K5, Q9M306, Q9SB58 -
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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
PAT10-mediated palmitoylation is critical for vacuolar function by regulating membrane association or the activities of tonoplast proteins
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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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-
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palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
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-
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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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palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
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-
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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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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 + [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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-
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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
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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
-
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 + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
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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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palmitoyl-CoA + [Psr1 protein]-L-cysteine
[Psr1 protein]-S-palmitoyl-L-cysteine + CoA
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?
palmitoyl-CoA + [Psr1 protein]-L-cysteine
[Psr1 protein]-S-palmitoyl-L-cysteine + CoA
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?
palmitoyl-CoA + [Ras1 protein]-L-cysteine
[Ras1 protein]-S-palmitoyl-L-cysteine + CoA
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?
palmitoyl-CoA + [Ras1 protein]-L-cysteine
[Ras1 protein]-S-palmitoyl-L-cysteine + CoA
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?
palmitoyl-CoA + [Ras2 protein]-L-cysteine
[Ras2 protein]-S-palmitoyl-L-cysteine + CoA
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?
palmitoyl-CoA + [Ras2 protein]-L-cysteine
[Ras2 protein]-S-palmitoyl-L-cysteine + CoA
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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 + [Ras]-L-cysteine
[Ras]-S-palmitoyl-L-cysteine + CoA
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yeast Ras protein is a substrate of Erf2
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palmitoyl-CoA + [RGS4]-L-cysteine
[RGS4]-S-palmitoyl-L-cysteine + CoA
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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
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palmitoyl-CoA + [RGS4]-L-cysteine
[RGS4]-S-palmitoyl-L-cysteine + CoA
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RGS4 is palmitoylated at two cysteine residues near its N-terminus (C2 and C12) and a cysteine residue in the RGS core domain, substrate of APT1
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palmitoyl-CoA + [RGS4]-L-cysteine
[RGS4]-S-palmitoyl-L-cysteine + CoA
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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
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palmitoyl-CoA + [rhodopsin]-L-cysteine
[rhodopsin]-S-palmitoyl-L-cysteine + CoA
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PAT incorporates fatty acid into rhodopsin with higher efficiency, 10times higher initial rate, as compared to autoacylation, presence of deacylated, free cysteine residues in dark-adapted rhodopsin increases palmitoylation via PAT
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palmitoyl-CoA + [rhodopsin]-L-cysteine
[rhodopsin]-S-palmitoyl-L-cysteine + CoA
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PAT incorporates fatty acid into rhodopsin with higher efficiency, 10times higher initial rate, as compared to autoacylation, presence of deacylated, free cysteine residues in dark-adapted rhodopsin increases palmitoylation via PAT. Rhodopsin containing rod outer segment membranes prepared from fresh, dark-adapted bovine retinae
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palmitoyl-CoA + [short lipid-modified cysteinyl-containing peptide]-L-cysteine
[short lipid-modified cysteinyl-containing peptide]-S-palmitoyl-L-cysteine + CoA
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minimum requirements for substrate recognition are a free cysteine thiol adjacent to a hydrophobic lipid anchor, either myristate or farnesyl isoprenoid, overview
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palmitoyl-CoA + [short lipid-modified cysteinyl-containing peptide]-L-cysteine
[short lipid-modified cysteinyl-containing peptide]-S-palmitoyl-L-cysteine + CoA
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minimum requirements for substrate recognition are a free cysteine thiol adjacent to a hydrophobic lipid anchor, either myristate or farnesyl isoprenoid, overview
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r
palmitoyl-CoA + [Sna4 protein]-L-cysteine
[Sna4 protein]-S-palmitoyl-L-cysteine + CoA
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?
palmitoyl-CoA + [Sna4 protein]-L-cysteine
[Sna4 protein]-S-palmitoyl-L-cysteine + CoA
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?
palmitoyl-CoA + [SNAP-25]-L-cysteine
[SNAP-25]-S-palmitoyl-L-cysteine + CoA
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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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palmitoyl-CoA + [Snc1]-L-cysteine
[Snc1]-S-palmitoyl-L-cysteine + CoA
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?
palmitoyl-CoA + [Snc1]-L-cysteine
[Snc1]-S-palmitoyl-L-cysteine + CoA
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yeast SNARES Snc1, Syn8, and Tlg1 are substrates of Swf1, palmitoylating at cysteine residues near the cytoplasmic side of their single transmembrane span
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palmitoyl-CoA + [Syn8]-L-cysteine
[Syn8]-S-palmitoyl-L-cysteine + CoA
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palmitoyl-CoA + [Syn8]-L-cysteine
[Syn8]-S-palmitoyl-L-cysteine + CoA
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yeast SNARES Snc1, Syn8, and Tlg1 are substrates of Swf1, palmitoylating at cysteine residues near the cytoplasmic side of their single transmembrane span
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palmitoyl-CoA + [Tlg1]-L-cysteine
[Tlg1]-S-palmitoyl-L-cysteine + CoA
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?
palmitoyl-CoA + [Tlg1]-L-cysteine
[Tlg1]-S-palmitoyl-L-cysteine + CoA
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yeast SNARES Snc1, Syn8, and Tlg1 are substrates of Swf1, palmitoylating at cysteine residues near the cytoplasmic side of their single transmembrane span
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r
palmitoyl-CoA + [Vac8 protein]-L-cysteine
[Vac8 protein]-S-palmitoyl-L-cysteine + CoA
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palmitoyl-CoA + [Vac8 protein]-L-cysteine
[Vac8 protein]-S-palmitoyl-L-cysteine + CoA
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palmitoyl-CoA + [Vac8p]-L-cysteine
[Vac8p]-S-palmitoyl-L-cysteine + CoA
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recombinant Vac8p is palmitoylated when added to vacuoles and is anchored to membranes after modi¢cation
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palmitoyl-CoA + [Vac8p]-L-cysteine
[Vac8p]-S-palmitoyl-L-cysteine + CoA
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recombinant non-myristoylated His6-Vac8p and myristoylated Vac8-GST
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palmitoyl-CoA + [Vac8p]-L-cysteine
[Vac8p]-S-palmitoyl-L-cysteine + CoA
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recombinant Vac8p is palmitoylated when added to vacuoles and is anchored to membranes after modi¢cation
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palmitoyl-CoA + [Vac8p]-L-cysteine
[Vac8p]-S-palmitoyl-L-cysteine + CoA
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recombinant non-myristoylated His6-Vac8p and myristoylated Vac8-GST
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palmitoyl-CoA + [Vac8]-L-cysteine
[Vac8]-S-palmitoyl-L-cysteine + CoA
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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
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palmitoyl-CoA + [Vac8]-L-cysteine
[Vac8]-S-palmitoyl-L-cysteine + CoA
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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
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palmitoyl-CoA + [Yck1 protein]-L-cysteine
[Yck1 protein]-S-palmitoyl-L-cysteine + CoA
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?
palmitoyl-CoA + [Yck1 protein]-L-cysteine
[Yck1 protein]-S-palmitoyl-L-cysteine + CoA
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palmitoyl-CoA + [Ygl108 protein]-L-cysteine
[Ygl108 protein]-S-palmitoyl-L-cysteine + CoA
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?
palmitoyl-CoA + [Ygl108 protein]-L-cysteine
[Ygl108 protein]-S-palmitoyl-L-cysteine + CoA
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?
additional information
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Kinetics and substrate specificity of PAT, overview
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additional information
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PAT activity displays specificity for the acyl donor, efficiently utilizing long-chain acyl-CoAs, but not free fatty acid or S-palmitoyl-N-acetylcysteamine. PAT also shows thiolase activity
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additional information
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PAT fatty acyl-CoA chain length specificity in vitro, overview. PAT shows G-protein substrate specificity of PAT activity, overview. Mutation of the prenylated cysteine residue to serine, C68S, in the gamma2 subunit yields a nonprenylated gamma that heterodimerizes with the beta1 subunit. The mutant betagammaC68S binds to myristoylated rGialpha1, forming a heterotrimer that is acylated in vitro with efficiency similar to that of the wild-type heterotrimer
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additional information
?
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PAT activity displays specificity for the acyl donor, efficiently utilizing long-chain acyl-CoAs, but not free fatty acid or S-palmitoyl-N-acetylcysteamine. PAT also shows thiolase activity
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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
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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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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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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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additional information
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DHHC3 has a broad protein substrate specificity, but only myristoyl-, palmitoyl-, and palmioleoyl-CoA are effective, and longer acyl-CoAs compete less well. The acyl-CoA chain length specificity of DHHC enzyme autoacylation parallels substrate specificity, overview
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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. Effects of APT1 on palmitate turnover on Gsalpha are not due to effects on the rate of turnover of palmitoyl-CoA
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additional information
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APT1 has acyl-CoA hydrolase activity
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additional information
?
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G-protein substrate specificity of PAT activity, overview. Mutation of the prenylated cysteine residue to serine, C68S, in the gamma2 subunit yields a nonprenylated gamma that heterodimerizes with the beta1 subunit. The mutant betagammaC68S binds to myristoylated rGialpha1, forming a heterotrimer that is acylated in vitro with efficiency similar to that of the wild-type heterotrimer
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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. Effects of APT1 on palmitate turnover on Gsalpha are not due to effects on the rate of turnover of palmitoyl-CoA
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additional information
?
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APT1 has acyl-CoA hydrolase activity
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additional information
?
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PATis speci¢c for palmitoyl-CoA, since myristoyl- and stearyl-CoA can compete with labeled Pal-CoA only at 10-fold higher amounts
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additional information
?
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PATis speci¢c for palmitoyl-CoA, since myristoyl- and stearyl-CoA can compete with labeled Pal-CoA only at 10-fold higher amounts
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
myristoyl-CoA + [Gialpha1]-L-cysteine
[protein]-S-myristoyl-L-cysteine + CoA
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GiR1 is myristoylated at its N-terminus and palmitoylated at an adjacent cysteine, substrate of APT1
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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 + [G protein alpha subunit]-L-cysteine
[G protein alpha subunit]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [G-protein alpha subunit Galphai]-L-cysteine
[G-protein alpha subunit Galphai]-S-palmitoyl-L-cysteine + CoA
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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 + [Gialpha1]-L-cysteine
[Gialpha1]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [H-Ras]-L-cysteine
[H-Ras]-S-palmitoyl-L-cysteine + CoA
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
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 + [Ras1p]-L-cysteine
[Ras1p]-S-palmitoyl-L-cysteine + CoA
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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
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palmitoyl-CoA + [Ras2p]-L-cysteine
[Ras2p]-S-palmitoyl-L-cysteine + CoA
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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
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palmitoyl-CoA + [Ras]-L-cysteine
[Ras]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [RGS4]-L-cysteine
[RGS4]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [rhodopsin]-L-cysteine
[rhodopsin]-S-palmitoyl-L-cysteine + CoA
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PAT incorporates fatty acid into rhodopsin with higher efficiency, 10times higher initial rate, as compared to autoacylation, presence of deacylated, free cysteine residues in dark-adapted rhodopsin increases palmitoylation via PAT
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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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palmitoyl-CoA + [Vac8p]-L-cysteine
[Vac8p]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [Vac8]-L-cysteine
[Vac8]-S-palmitoyl-L-cysteine + CoA
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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
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palmitoyl-CoA + [Yck2p]-L-cysteine
[Yck2p]-S-palmitoyl-L-cysteine + CoA
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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
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palmitoyl-CoA + [Yck2]-L-cysteine
[Yck2]-S-palmitoyl-L-cysteine + CoA
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yeast casein kinase Yck2 is a substrate of Akr1
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r
additional information
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palmitoyl-CoA + [G protein alpha subunit]-L-cysteine
[G protein alpha subunit]-S-palmitoyl-L-cysteine + CoA
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palmitoyl-CoA + [G protein alpha subunit]-L-cysteine
[G protein alpha subunit]-S-palmitoyl-L-cysteine + CoA
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palmitoyl-CoA + [Gialpha1]-L-cysteine
[Gialpha1]-S-palmitoyl-L-cysteine + CoA
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palmitoyl-CoA + [Gialpha1]-L-cysteine
[Gialpha1]-S-palmitoyl-L-cysteine + CoA
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GiR1 is myristoylated at its amino terminus and palmitoylated at an adjacent cysteine, substrate of APT1
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palmitoyl-CoA + [Gialpha1]-L-cysteine
[Gialpha1]-S-palmitoyl-L-cysteine + CoA
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Gialpha1 is myristoylated at its amino terminus and palmitoylated at an adjacent cysteine, preferred substrate of APT1
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palmitoyl-CoA + [H-Ras]-L-cysteine
[H-Ras]-S-palmitoyl-L-cysteine + CoA
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H-Ras is palmitoylated at two cysteine residues immediately upstream of its farnesylated and carboxylmethylated C-terminus, substrate of APT1
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palmitoyl-CoA + [H-Ras]-L-cysteine
[H-Ras]-S-palmitoyl-L-cysteine + CoA
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H-Ras is palmitoylated at two cysteine residues immediately upstream of its farnesylated and carboxylmethylated C-terminus, substrate of APT1
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palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
B3DN87, O80685, Q0WQK2, Q3EBC2, Q3EC11, Q500Z2, Q52T38, Q5M757, Q6DR03, Q7XA86, Q8L5Y5, Q8VYP5, Q8VYS8, Q93VV0, Q94C49, Q9C533, Q9FLM3, Q9LIE4, Q9LIH7, Q9M115, Q9M1K5, Q9M306, Q9SB58 -
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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
PAT10-mediated palmitoylation is critical for vacuolar function by regulating membrane association or the activities of tonoplast proteins
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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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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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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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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 + [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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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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palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
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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 + [Ras]-L-cysteine
[Ras]-S-palmitoyl-L-cysteine + CoA
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yeast Ras protein is a substrate of Erf2
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palmitoyl-CoA + [RGS4]-L-cysteine
[RGS4]-S-palmitoyl-L-cysteine + CoA
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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
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palmitoyl-CoA + [RGS4]-L-cysteine
[RGS4]-S-palmitoyl-L-cysteine + CoA
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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
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palmitoyl-CoA + [Vac8p]-L-cysteine
[Vac8p]-S-palmitoyl-L-cysteine + CoA
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recombinant Vac8p is palmitoylated when added to vacuoles and is anchored to membranes after modi¢cation
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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
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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
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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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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
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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. Effects of APT1 on palmitate turnover on Gsalpha are not due to effects on the rate of turnover of palmitoyl-CoA
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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HIP14 resides on the Golgi and can be observed on cytoplasmic vesicles
brenda
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ERF2 encodes a protein with four predicted membrane-spanning domains
brenda
B3DN87, O80685, Q0WQK2, Q3EBC2, Q3EC11, Q500Z2, Q52T38, Q5M757, Q6DR03, Q7XA86, Q8L5Y5, Q8VYP5, Q8VYS8, Q93VV0, Q94C49, Q9C533, Q9FLM3, Q9LIE4, Q9LIH7, Q9M115, Q9M1K5, Q9M306, Q9SB58 -
brenda
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enzyme class II
brenda
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enzyme class II
brenda
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enzyme class II
brenda
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enzyme class II
brenda
B3DN87, O80685, Q0WQK2, Q3EBC2, Q3EC11, Q500Z2, Q52T38, Q5M757, Q6DR03, Q7XA86, Q8L5Y5, Q8VYP5, Q8VYS8, Q93VV0, Q94C49, Q9C533, Q9FLM3, Q9LIE4, Q9LIH7, Q9M115, Q9M1K5, Q9M306, Q9SB58 -
brenda
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brenda
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-
brenda
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brenda
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brenda
DHHC2 is present in at least some areas of the endoplasmic reticulum and Golgi
brenda
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brenda
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-
brenda
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brenda
Golgi stack, trans-Golgi network/early endosome
brenda
Golgi, the trans-Golg network/early endosome
brenda
predominately localised in the Golgi apparatus
brenda
B3DN87, O80685, Q0WQK2, Q3EBC2, Q3EC11, Q500Z2, Q52T38, Q5M757, Q6DR03, Q7XA86, Q8L5Y5, Q8VYP5, Q8VYS8, Q93VV0, Q94C49, Q9C533, Q9FLM3, Q9LIE4, Q9LIH7, Q9M115, Q9M1K5, Q9M306, Q9SB58 -
brenda
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-
brenda
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-
brenda
-
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brenda
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brenda
DHHC2 is present in at least some areas of the endoplasmic reticulum and Golgi
brenda
HIP14 resides on the Golgi and can be observed on cytoplasmic vesicles
brenda
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isozymes DHHC-2, -3, -7, -8, and -21
brenda
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-
brenda
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-
brenda
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enzyme class I
brenda
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enzyme class I
brenda
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enzyme class I
brenda
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enzyme class I
brenda
B3DN87, O80685, Q0WQK2, Q3EBC2, Q3EC11, Q500Z2, Q52T38, Q5M757, Q6DR03, Q7XA86, Q8L5Y5, Q8VYP5, Q8VYS8, Q93VV0, Q94C49, Q9C533, Q9FLM3, Q9LIE4, Q9LIH7, Q9M115, Q9M1K5, Q9M306, Q9SB58 PATs are transmembrane proteins
brenda
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-
brenda
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PAT activity is highly enriched in low density membranes dependent upon cholesterol
brenda
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-
brenda
associated
brenda
localized to synaptic membranes
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B3DN87, O80685, Q0WQK2, Q3EBC2, Q3EC11, Q500Z2, Q52T38, Q5M757, Q6DR03, Q7XA86, Q8L5Y5, Q8VYP5, Q8VYS8, Q93VV0, Q94C49, Q9C533, Q9FLM3, Q9LIE4, Q9LIH7, Q9M115, Q9M1K5, Q9M306, Q9SB58 -
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isozymes DHHC-2, -3, -7, -8, and -21
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high enzyme level
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ERF2 encodes a protein with four predicted membrane-spanning domains
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B3DN87, O80685, Q0WQK2, Q3EBC2, Q3EC11, Q500Z2, Q52T38, Q5M757, Q6DR03, Q7XA86, Q8L5Y5, Q8VYP5, Q8VYS8, Q93VV0, Q94C49, Q9C533, Q9FLM3, Q9LIE4, Q9LIH7, Q9M115, Q9M1K5, Q9M306, Q9SB58 -
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Sec18p is a vacuolar PAT
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Sec18p is a vacuolar PAT
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additional information
Arabidopsis PAT proteins display a complex targeting pattern and are detected at the endoplasmic reticulum, Golgi, endosomal compartments, and the vacuolar membrane, but most proteins are targeted to the plasma membrane
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additional information
Arabidopsis PAT proteins display a complex targeting pattern and are detected at the endoplasmic reticulum, Golgi, endosomal compartments, and the vacuolar membrane, but most proteins are targeted to the plasma membrane
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additional information
Arabidopsis PAT proteins display a complex targeting pattern and are detected at the endoplasmic reticulum, Golgi, endosomal compartments, and the vacuolar membrane, but most proteins are targeted to the plasma membrane
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additional information
Arabidopsis PAT proteins display a complex targeting pattern and are detected at the endoplasmic reticulum, Golgi, endosomal compartments, and the vacuolar membrane, but most proteins are targeted to the plasma membrane
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additional information
Arabidopsis PAT proteins display a complex targeting pattern and are detected at the endoplasmic reticulum, Golgi, endosomal compartments, and the vacuolar membrane, but most proteins are targeted to the plasma membrane
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additional information
Arabidopsis PAT proteins display a complex targeting pattern and are detected at the endoplasmic reticulum, Golgi, endosomal compartments, and the vacuolar membrane, but most proteins are targeted to the plasma membrane
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additional information
Arabidopsis PAT proteins display a complex targeting pattern and are detected at the endoplasmic reticulum, Golgi, endosomal compartments, and the vacuolar membrane, but most proteins are targeted to the plasma membrane
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additional information
Arabidopsis PAT proteins display a complex targeting pattern and are detected at the endoplasmic reticulum, Golgi, endosomal compartments, and the vacuolar membrane, but most proteins are targeted to the plasma membrane
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additional information
Arabidopsis PAT proteins display a complex targeting pattern and are detected at the endoplasmic reticulum, Golgi, endosomal compartments, and the vacuolar membrane, but most proteins are targeted to the plasma membrane
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additional information
Arabidopsis PAT proteins display a complex targeting pattern and are detected at the endoplasmic reticulum, Golgi, endosomal compartments, and the vacuolar membrane, but most proteins are targeted to the plasma membrane
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brenda
additional information
Arabidopsis PAT proteins display a complex targeting pattern and are detected at the endoplasmic reticulum, Golgi, endosomal compartments, and the vacuolar membrane, but most proteins are targeted to the plasma membrane
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brenda
additional information
Arabidopsis PAT proteins display a complex targeting pattern and are detected at the endoplasmic reticulum, Golgi, endosomal compartments, and the vacuolar membrane, but most proteins are targeted to the plasma membrane
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additional information
Arabidopsis PAT proteins display a complex targeting pattern and are detected at the endoplasmic reticulum, Golgi, endosomal compartments, and the vacuolar membrane, but most proteins are targeted to the plasma membrane
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additional information
Arabidopsis PAT proteins display a complex targeting pattern and are detected at the endoplasmic reticulum, Golgi, endosomal compartments, and the vacuolar membrane, but most proteins are targeted to the plasma membrane
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additional information
Arabidopsis PAT proteins display a complex targeting pattern and are detected at the endoplasmic reticulum, Golgi, endosomal compartments, and the vacuolar membrane, but most proteins are targeted to the plasma membrane
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additional information
Arabidopsis PAT proteins display a complex targeting pattern and are detected at the endoplasmic reticulum, Golgi, endosomal compartments, and the vacuolar membrane, but most proteins are targeted to the plasma membrane
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brenda
additional information
Arabidopsis PAT proteins display a complex targeting pattern and are detected at the endoplasmic reticulum, Golgi, endosomal compartments, and the vacuolar membrane, but most proteins are targeted to the plasma membrane
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brenda
additional information
Arabidopsis PAT proteins display a complex targeting pattern and are detected at the endoplasmic reticulum, Golgi, endosomal compartments, and the vacuolar membrane, but most proteins are targeted to the plasma membrane
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brenda
additional information
Arabidopsis PAT proteins display a complex targeting pattern and are detected at the endoplasmic reticulum, Golgi, endosomal compartments, and the vacuolar membrane, but most proteins are targeted to the plasma membrane
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additional information
Arabidopsis PAT proteins display a complex targeting pattern and are detected at the endoplasmic reticulum, Golgi, endosomal compartments, and the vacuolar membrane, but most proteins are targeted to the plasma membrane
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additional information
Arabidopsis PAT proteins display a complex targeting pattern and are detected at the endoplasmic reticulum, Golgi, endosomal compartments, and the vacuolar membrane, but most proteins are targeted to the plasma membrane
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additional information
Arabidopsis PAT proteins display a complex targeting pattern and are detected at the endoplasmic reticulum, Golgi, endosomal compartments, and the vacuolar membrane, but most proteins are targeted to the plasma membrane
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additional information
Arabidopsis PAT proteins display a complex targeting pattern and are detected at the endoplasmic reticulum, Golgi, endosomal compartments, and the vacuolar membrane, but most proteins are targeted to the plasma membrane
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additional information
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Arabidopsis PAT proteins display a complex targeting pattern and are detected at the endoplasmic reticulum, Golgi, endosomal compartments, and the vacuolar membrane, but most proteins are targeted to the plasma membrane
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additional information
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no activity in cytosol, subcellular localization study, overview
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additional information
the DHHC protein is not associated with early endosomes
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additional information
the DHHC protein is not associated with early endosomes
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additional information
the DHHC protein is not associated with early endosomes
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additional information
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the isozymes colocalize with eNOS in the Golgi and plasma membrane and interact with eNOS in endothelial cells
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additional information
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low or undetectable levels in Golgi, endoplasmic reticulum, and mitochondria of rat liver, subcellular localization study, overview
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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
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
malfunction
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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
metabolism
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
physiological function
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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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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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
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?
x * 34700, calculated
additional information
identification of conserved sequence motifs within Arabidopsis PATs, e.g. the central DHHC-CRD domain, overview. The DHHC motif within the central region is always located to the vicinity of the C-terminal transmembrane domains. Protein topology of Arabidopsis PATs, overview
additional information
identification of conserved sequence motifs within Arabidopsis PATs, e.g. the central DHHC-CRD domain, overview. The DHHC motif within the central region is always located to the vicinity of the C-terminal transmembrane domains. Protein topology of Arabidopsis PATs, overview
additional information
identification of conserved sequence motifs within Arabidopsis PATs, e.g. the central DHHC-CRD domain, overview. The DHHC motif within the central region is always located to the vicinity of the C-terminal transmembrane domains. Protein topology of Arabidopsis PATs, overview
additional information
identification of conserved sequence motifs within Arabidopsis PATs, e.g. the central DHHC-CRD domain, overview. The DHHC motif within the central region is always located to the vicinity of the C-terminal transmembrane domains. Protein topology of Arabidopsis PATs, overview
additional information
identification of conserved sequence motifs within Arabidopsis PATs, e.g. the central DHHC-CRD domain, overview. The DHHC motif within the central region is always located to the vicinity of the C-terminal transmembrane domains. Protein topology of Arabidopsis PATs, overview
additional information
identification of conserved sequence motifs within Arabidopsis PATs, e.g. the central DHHC-CRD domain, overview. The DHHC motif within the central region is always located to the vicinity of the C-terminal transmembrane domains. Protein topology of Arabidopsis PATs, overview
additional information
identification of conserved sequence motifs within Arabidopsis PATs, e.g. the central DHHC-CRD domain, overview. The DHHC motif within the central region is always located to the vicinity of the C-terminal transmembrane domains. Protein topology of Arabidopsis PATs, overview
additional information
identification of conserved sequence motifs within Arabidopsis PATs, e.g. the central DHHC-CRD domain, overview. The DHHC motif within the central region is always located to the vicinity of the C-terminal transmembrane domains. Protein topology of Arabidopsis PATs, overview
additional information
identification of conserved sequence motifs within Arabidopsis PATs, e.g. the central DHHC-CRD domain, overview. The DHHC motif within the central region is always located to the vicinity of the C-terminal transmembrane domains. Protein topology of Arabidopsis PATs, overview
additional information
identification of conserved sequence motifs within Arabidopsis PATs, e.g. the central DHHC-CRD domain, overview. The DHHC motif within the central region is always located to the vicinity of the C-terminal transmembrane domains. Protein topology of Arabidopsis PATs, overview
additional information
identification of conserved sequence motifs within Arabidopsis PATs, e.g. the central DHHC-CRD domain, overview. The DHHC motif within the central region is always located to the vicinity of the C-terminal transmembrane domains. Protein topology of Arabidopsis PATs, overview
additional information
identification of conserved sequence motifs within Arabidopsis PATs, e.g. the central DHHC-CRD domain, overview. The DHHC motif within the central region is always located to the vicinity of the C-terminal transmembrane domains. Protein topology of Arabidopsis PATs, overview
additional information
identification of conserved sequence motifs within Arabidopsis PATs, e.g. the central DHHC-CRD domain, overview. The DHHC motif within the central region is always located to the vicinity of the C-terminal transmembrane domains. Protein topology of Arabidopsis PATs, overview
additional information
identification of conserved sequence motifs within Arabidopsis PATs, e.g. the central DHHC-CRD domain, overview. The DHHC motif within the central region is always located to the vicinity of the C-terminal transmembrane domains. Protein topology of Arabidopsis PATs, overview
additional information
identification of conserved sequence motifs within Arabidopsis PATs, e.g. the central DHHC-CRD domain, overview. The DHHC motif within the central region is always located to the vicinity of the C-terminal transmembrane domains. Protein topology of Arabidopsis PATs, overview
additional information
identification of conserved sequence motifs within Arabidopsis PATs, e.g. the central DHHC-CRD domain, overview. The DHHC motif within the central region is always located to the vicinity of the C-terminal transmembrane domains. Protein topology of Arabidopsis PATs, overview
additional information
identification of conserved sequence motifs within Arabidopsis PATs, e.g. the central DHHC-CRD domain, overview. The DHHC motif within the central region is always located to the vicinity of the C-terminal transmembrane domains. Protein topology of Arabidopsis PATs, overview
additional information
identification of conserved sequence motifs within Arabidopsis PATs, e.g. the central DHHC-CRD domain, overview. The DHHC motif within the central region is always located to the vicinity of the C-terminal transmembrane domains. Protein topology of Arabidopsis PATs, overview
additional information
identification of conserved sequence motifs within Arabidopsis PATs, e.g. the central DHHC-CRD domain, overview. The DHHC motif within the central region is always located to the vicinity of the C-terminal transmembrane domains. Protein topology of Arabidopsis PATs, overview
additional information
identification of conserved sequence motifs within Arabidopsis PATs, e.g. the central DHHC-CRD domain, overview. The DHHC motif within the central region is always located to the vicinity of the C-terminal transmembrane domains. Protein topology of Arabidopsis PATs, overview
additional information
identification of conserved sequence motifs within Arabidopsis PATs, e.g. the central DHHC-CRD domain, overview. The DHHC motif within the central region is always located to the vicinity of the C-terminal transmembrane domains. Protein topology of Arabidopsis PATs, overview
additional information
identification of conserved sequence motifs within Arabidopsis PATs, e.g. the central DHHC-CRD domain, overview. The DHHC motif within the central region is always located to the vicinity of the C-terminal transmembrane domains. Protein topology of Arabidopsis PATs, overview
additional information
identification of conserved sequence motifs within Arabidopsis PATs, e.g. the central DHHC-CRD domain, overview. The DHHC motif within the central region is always located to the vicinity of the C-terminal transmembrane domains. Protein topology of Arabidopsis PATs, overview
additional information
-
identification of conserved sequence motifs within Arabidopsis PATs, e.g. the central DHHC-CRD domain, overview. The DHHC motif within the central region is always located to the vicinity of the C-terminal transmembrane domains. Protein topology of Arabidopsis PATs, overview
additional information
-
yeast S-palmitoyltransferases contain DHHC-cysteine rich domains
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Arabidopsis thaliana (Q7XA86), Arabidopsis thaliana
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Arabidopsis thaliana (Q8VYP5)
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Howie, J.; Reilly, L.; Fraser, N.J.; Vlachaki Walker, J.M.; Wypijewski, K.J.; Ashford, M.L.; Calaghan, S.C.; McClafferty, H.; Tian, L.; Shipston, M.J.; Boguslavskyi, A.; Shattock, M.J.; Fuller, W.
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Arabidopsis thaliana (Q8VYP5)
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Sharma, C.; Wang, H.X.; Li, Q.; Knoblich, K.; Reisenbichler, E.S.; Richardson, A.L.; Hemler, M.E.
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Homo sapiens (Q9NYG2), Homo sapiens
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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
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Homo sapiens (Q9C0B5)
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Li, Y.; Qi, B.
Progress toward understanding protein S-acylation Prospective in plants
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Li, Y.; Xu, J.; Li, G.; Wan, S.; Batistic, O.; Sun, M.; Zhang, Y.; Scott, R.; Qi, B.
Protein S-acyl transferase 15 is involved in seed triacylglycerol catabolism during early seedling growth in Arabidopsis
J. Exp. Bot.
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Arabidopsis thaliana (Q500Z2)
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Quiroga, R.; Valdez Taubas, J.
Bioinformatic identification of functionally and structurally relevant residues and motifs in protein S-acyltransferases
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Giardia intestinalis (V6U0K4)
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Li, Y.; Li, H.J.; Morgan, C.; Bomblies, K.; Yang, W.; Qi, B.
Both male and female gametogenesis require a fully functional protein S-acyl transferase 21 in Arabidopsis thaliana
Plant J.
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754-767
2019
Arabidopsis thaliana (Q6DR03)
brenda
Wan, Z.Y.; Zhang, Y.; Li, S.
Protein S-acyl transferase 4 controls nucleus position during root hair tip growth
Plant Signal. Behav.
12
e1311438
2017
Arabidopsis thaliana (Q9C744)
brenda