2.5.1.58: protein farnesyltransferase
This is an abbreviated version!
For detailed information about protein farnesyltransferase, go to the full flat file.
Word Map on EC 2.5.1.58
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2.5.1.58
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farnesylation
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prenylation
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geranylgeranylation
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isoprenoids
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beta-subunits
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isoprenylation
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15-carbon
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lamins
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manumycin
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geranylgeranyltransferase-i
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farnesyl-protein
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h-ras
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medicine
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peptidomimetic
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prelamin
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ggtase-i
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p21ras
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tetrapeptide
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farnesol
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tetrahydroquinoline
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ras-dependent
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pharmacology
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progerin
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3hmevalonate
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ras-induced
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lovastatin
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tipifarnib
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drug development
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ras-mediated
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ras-transformed
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lonafarnib
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hutchinson-gilford
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dimethylallyl
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geranylgeraniol
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isoprene
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analysis
- 2.5.1.58
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farnesylation
-
prenylation
-
geranylgeranylation
-
isoprenoids
- beta-subunits
-
isoprenylation
-
15-carbon
- lamins
- manumycin
-
geranylgeranyltransferase-i
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farnesyl-protein
- h-ras
- medicine
-
peptidomimetic
-
prelamin
- ggtase-i
-
p21ras
- tetrapeptide
- farnesol
- tetrahydroquinoline
-
ras-dependent
- pharmacology
-
progerin
-
3hmevalonate
-
ras-induced
- lovastatin
- tipifarnib
- drug development
-
ras-mediated
-
ras-transformed
- lonafarnib
-
hutchinson-gilford
-
dimethylallyl
- geranylgeraniol
- isoprene
- analysis
Reaction
Synonyms
AfFTase, CAAX farnesyltransferase, EhFT, Era1, farnesyl protein transferase, farnesyltransferase, farnesyltransferase ternary complex part II, farnesyltransferase, farnesyl pyrophosphate-protein, farnesyltransferase, protein, FntA, FntB, FPT, fptase, FTase, hFTase, HIT5, Pf-PFT, PfPFT, PFT, PFTase, prenyl transferase, prenylprotein transferase, prenyltransferase, protein cysteine farnesyltransferase, protein farnesyl transferase, protein farnesyltransferase, protein prenyltransferase, protein-farnesyltransferase, R-PFT, Ram1, RAS farnesyltransferase, Ras protein farnesyltransferase, rFPTase, rFTase, rPFTase, TbFTase, yPFTase
ECTree
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General Information
General Information on EC 2.5.1.58 - protein farnesyltransferase
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malfunction
physiological function
additional information
combined FTase/GGTase-I deficiency significantly reduces K-Ras-induced lung tumors and improves survival without obvious pulmonary toxicity
malfunction
combined FTase/GGTase-I deficiency significantly reduces K-Ras-induced lung tumors and improves survival without obvious pulmonary toxicity. Enzyme deficiency is involved in progeria, also known as Hutchinson-Gilford progeria syndrome, a fatal and rare genetic disease caused by the mutation of the LMNA gene
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key negative regulator controlling abscisic acid sensitivity
physiological function
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posttranslational modification of proteins involved in intracellular signal transduction network
physiological function
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posttranslational modification of proteins involved in intracellular signal transduction network
physiological function
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posttranslational modification of proteins involved in intracellular signal transduction network
physiological function
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ras1 deletion phenotype can be mimicked chemically by inhibition of farnesyl transferase in the wild-type strain
physiological function
farnesyltransferase alpha subunit regulates vacuolar protein sorting-associated protein 4A (Vps4A)-dependent intracellular trafficking through recycling endosomes. The enzyme FTase alpha controls trafficking of transferrin receptor upstream of thie Vps4A protein
physiological function
farnesyltransferase alpha subunit regulates vacuolar protein sorting-associated protein 4A (Vps4A)-dependent intracellular trafficking through recycling endosomes. The enzyme FTase alpha controls trafficking of transferrin receptor upstream of thie Vps4A protein
physiological function
FTase catalyzes farnesyl isoprenoid linked to the cysteine residue of the CAAX protein through a thioether linkage, which will enhance the hydrophobicity of the CAAX protein. Meanwhile, the formed CAAX-protein-isoprenoid complex is attached to the endoplasmic reticulum surface
physiological function
FTase catalyzes farnesyl isoprenoid linked to the cysteine residue of the CAAX protein through a thioether linkage, which will enhance the hydrophobicity of the CAAX protein. Meanwhile, the formed CAAX-protein-isoprenoid complex is attached to the endoplasmic reticulum surface. FTase is involvedin hematologic malignancies due via prenylation of Ras. The enzyme is also important in the pathological process of neurological diseases, such as neuroinflammatory disease and Parkinson's disease
physiological function
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protein prenylation is a posttranslational modification critical for many cellular processes such as DNA replication, signaling, and trafficking. Protein farnesyltransferase recognizes the CAAX motif on the protein substrate
physiological function
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dimerization of subunits alpha and beta is required for farnesylation activity
physiological function
heat-intolerant mutant hit5 carries a mutation in the beta-subunit of the protein farnesyltransferase. The mutant is thermosensitive to prolonged heat incubation at 37°C for 4 d but thermotolerant to sudden heat shock at 44°C for 40 min. hit5/abi3 and hit5/aba3 double mutants have the same temperature-dependent phenotypes as hit5. Exogenous supplementation of neither abscisic acid nor the abscisic acid synthesis inhibitor fluridone alter the temperature-dependent phenotypes of hit5. The hit5/hsp101 double mutant is still sensitive to prolonged heat incubation, yet its ability to tolerate sudden heat shock is lost
physiological function
mutants of HSP40 protein J3 but not J2 manifest the heat-shock tolerant phenotype of beta-subunit Hit5/Era1 mutants. The basal transcript levels of HSP101 in Hit5/Era1 and J3 mutants are higher than those in the wild type. The capacities of J3/HSP101 and Hit5/HSP101 double mutants to tolerate heat-shock stress decline compared to those of J3 and Hit5/Era1 mutants, but they are still greater than that of the wild type. A lack of farnesylated J3 contributes to the heat-dependent phenotypes of Hit5/Era1 mutants, in part by the modulation of HSP101 activity
physiological function
targeted disruption of beta-subunit RAM1 results in the reduction of hyphal growth and sporulation, and an increase in the sensitivity to various stresses. Loss of RAM1 also leads to the attenuation of virulence on the plant host, decreased appressorium formation and invasive growth. Ras GTPases, RAS1 and RAS2, can interact with Ram1, and their plasma membrane localization is regulated by Ram1 through their C-terminal farnesylation sites. Adding farnesyltransferase inhibitor Tipifarnib can result in similar defects as in a Ram1 deletion mutant, including decreased appressorium formation and invasive growth
physiological function
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ras1 deletion phenotype can be mimicked chemically by inhibition of farnesyl transferase in the wild-type strain
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physiological function
Pyricularia oryzae ATCC MYA-4617
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targeted disruption of beta-subunit RAM1 results in the reduction of hyphal growth and sporulation, and an increase in the sensitivity to various stresses. Loss of RAM1 also leads to the attenuation of virulence on the plant host, decreased appressorium formation and invasive growth. Ras GTPases, RAS1 and RAS2, can interact with Ram1, and their plasma membrane localization is regulated by Ram1 through their C-terminal farnesylation sites. Adding farnesyltransferase inhibitor Tipifarnib can result in similar defects as in a Ram1 deletion mutant, including decreased appressorium formation and invasive growth
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comparison of the substrate specificities of PFTases from three organisms, Rattus norvegicus, Saccharomyces cerevisiae, and Candida albicans, using CVa2X libraries, overview. Rattus norvegicus PFTase shares more peptide substrates with Saccharomyces cerevisiae PFTase than with Candida albicans PFTase
additional information
comparison of the substrate specificities of PFTases from three organisms, Rattus norvegicus, Saccharomyces cerevisiae, and Candida albicans, using CVa2X libraries, overview. Rattus norvegicus PFTase shares more peptide substrates with Saccharomyces cerevisiae PFTase than with Candida albicans PFTase
additional information
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comparison of the substrate specificities of PFTases from three organisms, Rattus norvegicus, Saccharomyces cerevisiae, and Candida albicans, using CVa2X libraries, overview. Rattus norvegicus PFTase shares more peptide substrates with Saccharomyces cerevisiae PFTase than with Candida albicans PFTase
additional information
comparison of the substrate specificities of PFTases from three organisms, Rattus norvegicus, Saccharomyces cerevisiae, and Candida albicans, using CVa2X libraries, overview. Rattus norvegicus PFTase shares more peptide substrates with Saccharomyces cerevisiae PFTase than with Candida albicans PFTase
additional information
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comparison of the substrate specificities of PFTases from three organisms, Rattus norvegicus, Saccharomyces cerevisiae, and Candida albicans, using CVa2X libraries, overview. Rattus norvegicus PFTase shares more peptide substrates with Saccharomyces cerevisiae PFTase than with Candida albicans PFTase
additional information
FTase and GGTase-I recognize the same CAAX sequence motif in a protein substrate and catalyze the attachment of farnesyl and geranygeranyl groups to the protein, respectively. The X is the key residue that determines the farnesylation or geranylgeranylation of the CAAX-containing protein. When X is serine, methionine or glutamine the protein substrate is preferentially activated by FTase, but when X is leucine or phenylalanine the protein substrate is preferentially activated by GGTase-I
additional information
FTase and GGTase-I recognize the same CAAX sequence motif in a protein substrate and catalyze the attachment of farnesyl and geranygeranyl groups to the protein, respectively. The X is the key residue that determines the farnesylation or geranylgeranylation of the CAAX-containing protein. When X is serine, methionine or glutamine the protein substrate is preferentially activated by FTase, but when X is leucine or phenylalanine the protein substrate is preferentially activated by GGTase-I
additional information
FTase and GGTase-I recognize the same CAAX sequence motif in a protein substrate and catalyze the attachment of farnesyl and geranygeranyl groups to the protein, respectively. The X is the key residue that determines the farnesylation or geranylgeranylation of the CAAX-containing protein. When X is serine, methionine or glutamine the protein substrate is preferentially activated by FTase, but when X is leucine or phenylalanine the protein substrate is preferentially activated by GGTase-I
additional information
FTase and GGTase-I recognize the same CAAX sequence motif in a protein substrate and catalyze the attachment of farnesyl and geranygeranyl groups to the protein, respectively. The X is the key residue that determines the farnesylation or geranylgeranylation of the CAAX-containing protein. When X is serine, methionine or glutamine the protein substrate is preferentially activated by FTase, but when X is leucine or phenylalanine the protein substrate is preferentially activated by GGTase-I
additional information
ligand interaction analysis with FTase alpha subunit, mass spectrometry, overview. Modelling of dimeric FTase alpha subunits
additional information
ligand interaction analysis with FTase alpha subunit, mass spectrometry, overview. Modelling of dimeric FTase alpha subunits