| Identification |
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| Name | Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha |
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| Synonyms | - CAAX farnesyltransferase subunit alpha
- FTase-alpha
- Ras proteins prenyltransferase subunit alpha
- Type I protein geranyl-geranyltransferase subunit alpha
- GGTase-I-alpha
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| Gene Name | RAM2 |
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| Enzyme Class | |
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| Biological Properties |
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| General Function | Involved in protein prenyltransferase activity |
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| Specific Function | Catalyzes the transfer of a farnesyl or geranyl-geranyl moiety from farnesyl or geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. The alpha subunit is thought to participate in a stable complex with the substrate. The beta subunit binds the peptide substrate |
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| Cellular Location | Not Available |
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| SMPDB Pathways | Not Available |
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| KEGG Pathways | Not Available |
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| SMPDB Reactions | Not Available |
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| KEGG Reactions | Not Available |
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| Metabolites | | YMDB ID | Name | View |
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| YMDB00219 | Pyrophosphate | Show | | YMDB00229 | Farnesyl pyrophosphate | Show | | YMDB00359 | 2-trans,6-trans,10-trans-geranylgeranyl diphosphate | Show | | YMDB00631 | geranylgeranyl diphosphate | Show |
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| GO Classification | | Component |
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| Not Available | | Function |
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| catalytic activity | | transferase activity | | transferase activity, transferring alkyl or aryl (other than methyl) groups | | prenyltransferase activity | | protein prenyltransferase activity | | Process |
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| protein prenylation | | protein amino acid prenylation | | metabolic process | | macromolecule metabolic process | | macromolecule modification | | protein modification process | | protein amino acid lipidation |
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| Gene Properties |
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| Chromosome Location | chromosome 11 |
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| Locus | YKL019W |
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| Gene Sequence | >951 bp
ATGGAGGAGTACGATTATTCAGACGTTAAACCTTTGCCCATTGAGACAGACTTGCAGGAT
GAACTGTGCAGGATTATGTATACCGAGGATTATAAGCGGTTGATGGGACTCGCAAGGGCT
CTGATCAGCCTTAACGAACTGTCACCCAGGGCACTACAGCTAACAGCCGAAATTATCGAC
GTGGCGCCAGCCTTCTACACCATATGGAACTACCGATTCAATATCGTCAGGCACATGATG
AGTGAATCCGAAGACACTGTCTTGTACCTGAACAAGGAATTAGACTGGCTAGATGAAGTT
ACGCTGAATAATCCAAAGAACTATCAGATCTGGTCCTATAGACAGTCTCTTTTGAAGCTA
CATCCGTCTCCTTCCTTCAAAAGAGAGCTGCCTATCTTAAAACTGATGATTGATGATGAT
TCCAAGAATTATCACGTTTGGTCGTACAGAAAGTGGTGCTGTTTGTTCTTCAGTGACTTT
CAACATGAGCTCGCCTACGCCAGCGACCTCATCGAGACAGACATTTATAACAACAGCGCA
TGGACTCATAGGATGTTTTACTGGGTGAACGCTAAAGATGTCATTTCAAAAGTGGAATTG
GCCGACGAGCTCCAGTTCATTATGGACAAGATTCAATTGGTTCCGCAGAACATCAGTCCG
TGGACCTACCTCCGTGGTTTCCAAGAGCTATTCCATGATAGGCTACAGTGGGATAGCAAA
GTAGTCGACTTCGCCACAACCTTCATCGGTGACGTATTGTCACTTCCAATTGGCTCACCA
GAGGATTTGCCCGAGATCGAGTCCTCATATGCCCTGGAATTCCTGGCATATCACTGGGGG
GCAGACCCTTGTACCCGAGACAACGCTGTTAAGGCCTATAGCTTGCTAGCAATCAAATAC
GATCCTATTAGAAAAAACTTGTGGCACCACAAAATAAATAATCTGAACTGA |
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| Protein Properties |
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| Pfam Domain Function | |
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| Protein Residues | 316 |
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| Protein Molecular Weight | 37507.30078 |
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| Protein Theoretical pI | 4.75 |
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| Signalling Regions | |
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| Transmembrane Regions | |
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| Protein Sequence | >Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
MEEYDYSDVKPLPIETDLQDELCRIMYTEDYKRLMGLARALISLNELSPRALQLTAEIID
VAPAFYTIWNYRFNIVRHMMSESEDTVLYLNKELDWLDEVTLNNPKNYQIWSYRQSLLKL
HPSPSFKRELPILKLMIDDDSKNYHVWSYRKWCCLFFSDFQHELAYASDLIETDIYNNSA
WTHRMFYWVNAKDVISKVELADELQFIMDKIQLVPQNISPWTYLRGFQELFHDRLQWDSK
VVDFATTFIGDVLSLPIGSPEDLPEIESSYALEFLAYHWGADPCTRDNAVKAYSLLAIKY
DPIRKNLWHHKINNLN |
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| References |
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| External Links | |
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| General Reference | - He, B., Chen, P., Chen, S. Y., Vancura, K. L., Michaelis, S., Powers, S. (1991). "RAM2, an essential gene of yeast, and RAM1 encode the two polypeptide components of the farnesyltransferase that prenylates a-factor and Ras proteins." Proc Natl Acad Sci U S A 88:11373-11377.1763050
- Dujon, B., Alexandraki, D., Andre, B., Ansorge, W., Baladron, V., Ballesta, J. P., Banrevi, A., Bolle, P. A., Bolotin-Fukuhara, M., Bossier, P., et, a. l. .. (1994). "Complete DNA sequence of yeast chromosome XI." Nature 369:371-378.8196765
- Burkett, T. J., Garfinkel, D. J. (1994). "Molecular characterization of the SPT23 gene: a dosage-dependent suppressor of Ty-induced promoter mutations from Saccharomyces cerevisiae." Yeast 10:81-92.8203154
- Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
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