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    SMY2 Smy2p [ Saccharomyces cerevisiae S288C ]

    Gene ID: 852470, updated on 9-Dec-2024

    Summary

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    Official Symbol
    SMY2
    Official Full Name
    Smy2p
    Primary source
    SGD:S000000376
    Locus tag
    YBR172C
    See related
    AllianceGenome:SGD:S000000376; FungiDB:YBR172C; VEuPathDB:YBR172C
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Summary
    Involved in several processes, including endoplasmic reticulum to Golgi vesicle-mediated transport; nuclear protein quality control by the ubiquitin-proteasome system; and regulation of transcription by RNA polymerase II. Located in endoplasmic reticulum membrane. Is active in nucleus. Human ortholog(s) of this gene implicated in Parkinson's disease. Orthologous to several human genes including GIGYF1 (GRB10 interacting GYF protein 1). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See SMY2 in Genome Data Viewer
    Location:
    chromosome: II
    Exon count:
    1
    Sequence:
    Chromosome: II; NC_001134.8 (579150..581372, complement)

    Chromosome II - NC_001134.8Genomic Context describing neighboring genes Neighboring gene nuclear protein localization protein 4 Neighboring gene Sec63 complex subunit SEC66 Neighboring gene Ump1p Neighboring gene Swd3p

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001134.8

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Smy2p participates in COPII vesicle formation through the interaction with Sec23p/Sec24p subcomplex. Higashio H, et al. Traffic, 2008 Jan. PMID 17973654, Free PMC Article
    2. Sequence and function analysis of a 4.3 kb fragment of Saccharomyces cerevisiae chromosome II including three open reading frames. Schaaff-Gerstenschläger I, et al. Yeast, 1993 Aug. PMID 8212898
    3. Binding specificities of the GYF domains from two Saccharomyces cerevisiae paralogs. Georgiev A, et al. Protein Eng Des Sel, 2007 Sep. PMID 17804396
    4. SMY2 and SYH1 suppress defects in ribosome biogenesis caused by ebp2 mutations. Okano A, et al. Biosci Biotechnol Biochem, 2015. PMID 25849478
    5. Distinct elongation stalls during translation are linked with distinct pathways for mRNA degradation. Veltri AJ, et al. Elife, 2022 Jul 27. PMID 35894211, Free PMC Article

    See all (62) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Distinct elongation stalls during translation are linked with distinct pathways for mRNA degradation.
      Title: Distinct elongation stalls during translation are linked with distinct pathways for mRNA degradation.
    2. These results suggest that Smy2 and Syh1 may be involved in ribosome biogenesis in relation to Ebp2.
      Title: SMY2 and SYH1 suppress defects in ribosome biogenesis caused by ebp2 mutations.
    3. SESA network comprising Smy2, Eap1, Scp160 and Asc1 , specifically inhibits initiation of translation of POM34 mRNA that encodes an integral membrane protein of the nuclear pore complex
      Title: The SESA network links duplication of the yeast centrosome with the protein translation machinery.
    Submit: New GeneRIF Correction

    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 protein binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in endoplasmic reticulum to Golgi vesicle-mediated transport IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in endoplasmic reticulum to Golgi vesicle-mediated transport IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    involved_in nuclear protein quality control by the ubiquitin-proteasome system IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in protein-containing complex disassembly IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in regulation of transcription by RNA polymerase II IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm HDA PubMed 
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cytosol HDA PubMed 
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in endoplasmic reticulum membrane IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    is_active_in nucleus IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    Smy2p
    NP_009731.4
    • GYF domain protein; involved in COPII vesicle formation; regulates Cdc48p function in transcription stress response; interacts with the Sec23p/Sec24p subcomplex; overexpression suppresses the temperature sensitivity of a myo2 mutant; homologous to human GIGYF1 and GIGYF2; similar to S. pombe Mpd2; SMY2 has a paralog, SYH1, that arose from the whole genome duplication

    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_001134.8 Reference assembly

      Range
      579150..581372 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001178520.3 → NP_009731.4  TPA: Smy2p [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_009731.4

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VQG8, P32909
      UniProtKB/TrEMBL
      G2W9H5, N1P8C3
      Conserved Domains (1) summary
      cd00072
      Location:205 → 261
      GYF; GYF domain: contains conserved Gly-Tyr-Phe residues; Proline-binding domain in CD2-binding and other proteins. Involved in signaling lymphocyte activity. Also present in other unrelated proteins (mainly unknown) derived from diverse eukaryotic species.
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P32909.2

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