U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

Links from Protein

    • Showing Current items.

    CEM1 fatty acid synthase CEM1 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 856790, updated on 9-Dec-2024

    Summary

    Go to the top of the page Help
    Official Symbol
    CEM1
    Official Full Name
    fatty acid synthase CEM1
    Primary source
    SGD:S000000863
    Locus tag
    YER061C
    See related
    AllianceGenome:SGD:S000000863; FungiDB:YER061C; VEuPathDB:YER061C
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Summary
    Predicted to enable 3-oxoacyl-[acyl-carrier-protein] synthase activity. Predicted to be involved in fatty acid biosynthetic process. Located in mitochondrion. Orthologous to human OXSM (3-oxoacyl-ACP synthase, mitochondrial). [provided by Alliance of Genome Resources, Dec 2024]
    NEW
    Try the new Gene table
    Try the new Transcript table

    Genomic context

    Go to the top of the page Help
    See CEM1 in Genome Data Viewer
    Location:
    chromosome: V
    Exon count:
    1
    Sequence:
    Chromosome: V; NC_001137.3 (278298..279626, complement)

    Chromosome V - NC_001137.3Genomic Context describing neighboring genes Neighboring gene purine-cytosine permease Neighboring gene purine-cytosine permease Neighboring gene glycerol-1-phosphatase GPP2 Neighboring gene Tho1p

    Genomic regions, transcripts, and products

    Go to the top of the page Help
    Genomic Sequence:
    NC_001137.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

    Go to the top of the pageHelp

    Related articles in PubMed

    1. Identification of a new nuclear gene (CEM1) encoding a protein homologous to a beta-keto-acyl synthase which is essential for mitochondrial respiration in Saccharomyces cerevisiae. Harington A, et al. Mol Microbiol, 1993 Aug. PMID 8412701
    2. Subcellular relocalization of a long-chain fatty acid CoA ligase by a suppressor mutation alleviates a respiration deficiency in Saccharomyces cerevisiae. Harington A, et al. EMBO J, 1994 Dec 1. PMID 7988550, Free PMC Article
    3. Cloning, expression, and characterization of the human mitochondrial beta-ketoacyl synthase. Complementation of the yeast CEM1 knock-out strain. Zhang L, et al. J Biol Chem, 2005 Apr 1. PMID 15668256
    4. Intersection of RNA processing and the type II fatty acid synthesis pathway in yeast mitochondria. Schonauer MS, et al. Mol Cell Biol, 2008 Nov. PMID 18779316, Free PMC Article
    5. The Antifungal Plant Defensin HsAFP1 from Heuchera sanguinea Induces Apoptosis in Candida albicans. Aerts AM, et al. Front Microbiol, 2011. PMID 21993350, Free PMC Article

    See all (47) citations in PubMed

    GeneRIFs: Gene References Into Functions

    Interactions

    Go to the top of the page Help
    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Go to the top of the page Help

    Homology

    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    enables 3-oxoacyl-[acyl-carrier-protein] synthase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables 3-oxoacyl-[acyl-carrier-protein] synthase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables 3-oxoacyl-[acyl-carrier-protein] synthase activity ISA
    Inferred from Sequence Alignment
    more info
    		 PubMed 
    enables transferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in fatty acid biosynthetic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in fatty acid biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in fatty acid biosynthetic process ISA
    Inferred from Sequence Alignment
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in mitochondrion HDA PubMed 
    is_active_in mitochondrion IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in mitochondrion IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

    Go to the top of the page Help
    Preferred Names
    fatty acid synthase CEM1
    NP_010983.2
    • Mitochondrial beta-keto-acyl synthase; possible role in fatty acid synthesis; required for mitochondrial respiration; human homolog OXSM can complement yeast cem1 null mutant

    NCBI Reference Sequences (RefSeq)

    Go to the top of the page Help

    NEW Try the new Transcript table

    Genome Annotation

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

    Reference assembly

    Genomic

    1. NC_001137.3 Reference assembly

      Range
      278298..279626 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001178952.2 → NP_010983.2  TPA: fatty acid synthase CEM1 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_010983.2

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D3DLW6, P39525
      UniProtKB/TrEMBL
      A6ZR15, B3LS75, C7GTC9, C8Z767, N1PA42
      Conserved Domains (1) summary
      cd00834
      Location:3 → 436
      KAS_I_II; Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen ...
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P39525.1

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

    Other Literature Sources
    Molecular Biology Databases
    Research Materials
    Tools
    Miscellaneous