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RAM1 [ Saccharomyces cerevisiae S288C ]

Gene ID: 851468, updated on 11-Sep-2024

Summary

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Official Symbol
RAM1
Primary source
SGD:S000002248
Locus tag
YDL090C
See related
AllianceGenome:SGD:S000002248; FungiDB:YDL090C; VEuPathDB:YDL090C
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Saccharomyces cerevisiae S288C (strain: S288C)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as
DPR1; FUS8; SCG2; SGP2; STE16
Summary
Enables protein farnesyltransferase activity. Involved in protein farnesylation. Part of protein farnesyltransferase complex. Orthologous to human CHURC1-FNTB (CHURC1-FNTB readthrough). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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Location:
chromosome: IV
Exon count:
1
Sequence:
Chromosome: IV; NC_001136.10 (295034..296329, complement)

Chromosome IV - NC_001136.10Genomic Context describing neighboring genes Neighboring gene RNA-binding signal recognition particle subunit SRP14 Neighboring gene Ubx3p Neighboring gene Nur1p Neighboring gene FG-nucleoporin ASM4

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_001136.10

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Amino acid residues that define both the isoprenoid and CAAX preferences of the Saccharomyces cerevisiae protein farnesyltransferase. Creating the perfect farnesyltransferase. Caplin BE, et al. J Biol Chem, 1998 Apr 17. PMID 9545274
  2. Functional consequence of mutating conserved residues of the yeast farnesyl-protein transferase beta-subunit Ram1(Dpr1). Kurth DD, et al. Biochemistry, 1997 Dec 16. PMID 9398327
  3. Substrate specificity determinants in the farnesyltransferase beta-subunit. Trueblood CE, et al. Proc Natl Acad Sci U S A, 1997 Sep 30. PMID 9380709, Free PMC Article
  4. Yeast protein farnesyltransferase. Site-directed mutagenesis of conserved residues in the beta-subunit. Dolence JM, et al. Biochemistry, 1997 Jul 29. PMID 9230058
  5. A novel yeast mutant defective in the processing of ras proteins: assessment of the effect of the mutation on processing steps. Fujiyama A, et al. EMBO J, 1987 Jan. PMID 3556161, Free PMC Article

See all (66) citations in PubMed

GeneRIFs: Gene References Into Functions

Pathways from PubChem

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Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Homology

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
  
enables prenyltransferase activity IEA
Inferred from Electronic Annotation
more info
  
enables protein farnesyltransferase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables protein farnesyltransferase activity IEA
Inferred from Electronic Annotation
more info
  
enables protein prenyltransferase activity IEA
Inferred from Electronic Annotation
more info
  
enables zinc ion binding RCA
inferred from Reviewed Computational Analysis
more info
 PubMed 
Process Evidence Code Pubs
involved_in protein farnesylation IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in protein farnesylation IDA
Inferred from Direct Assay
more info
 PubMed 
Component Evidence Code Pubs
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
part_of protein farnesyltransferase complex IBA
Inferred from Biological aspect of Ancestor
more info
  
part_of protein farnesyltransferase complex IDA
Inferred from Direct Assay
more info
 PubMed 
part_of protein farnesyltransferase complex IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
protein farnesyltransferase
NP_010193.1
  • Beta subunit of the CAAX farnesyltransferase (FTase); this complex prenylates the a-factor mating pheromone and Ras proteins; required for the membrane localization of Ras proteins and a-factor; homolog of the mammalian FTase beta subunit

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_001136.10 Reference assembly

    Range
    295034..296329 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001180149.1 → NP_010193.1  TPA: protein farnesyltransferase [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_010193.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6VRQ8, E9P902, P22007, Q12422
    UniProtKB/TrEMBL
    A6ZXN7, B3LGY5, C7GJM4, C8Z6L3, N1P7N9
    Conserved Domains (1) summary
    cd02893
    Location:80 → 374
    FTase; Protein farnesyltransferase (FTase)_like proteins containing the protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). FTases are a subgroup of PTase family of lipid-modifying enzymes. PTases catalyze the ...
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P22007.2

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