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    PML1 Pml1p [ Saccharomyces cerevisiae S288C ]

    Gene ID: 850703, updated on 9-Dec-2024

    Summary

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    Official Symbol
    PML1
    Official Full Name
    Pml1p
    Primary source
    SGD:S000004006
    Locus tag
    YLR016C
    See related
    AllianceGenome:SGD:S000004006; FungiDB:YLR016C; VEuPathDB:YLR016C
    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 mRNA binding activity. Involved in mRNA export from nucleus; mRNA splicing, via spliceosome; and maintenance of RNA location. Located in cytoplasm and nucleus. Part of RES complex. Orthologous to human SNIP1 (Smad nuclear interacting protein 1). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See PML1 in Genome Data Viewer
    Location:
    chromosome: XII
    Exon count:
    1
    Sequence:
    Chromosome: XII; NC_001144.5 (176802..177416, complement)

    Chromosome XII - NC_001144.5Genomic Context describing neighboring genes Neighboring gene Ppr1p Neighboring gene Bre2p Neighboring gene S-methyl-5-thioadenosine phosphorylase Neighboring gene Pom34p

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001144.5

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Crystal structure of the Pml1p subunit of the yeast precursor mRNA retention and splicing complex. Trowitzsch S, et al. J Mol Biol, 2009 Jan 16. PMID 19010333
    2. Structure of the yeast Pml1 splicing factor and its integration into the RES complex. Brooks MA, et al. Nucleic Acids Res, 2009 Jan. PMID 19033360, Free PMC Article
    3. An unusual RNA recognition motif acts as a scaffold for multiple proteins in the pre-mRNA retention and splicing complex. Trowitzsch S, et al. J Biol Chem, 2008 Nov 21. PMID 18809678
    4. A novel protein-protein interaction in the RES (REtention and Splicing) complex. Tripsianes K, et al. J Biol Chem, 2014 Oct 10. PMID 25160624, Free PMC Article
    5. Retention and splicing complex (RES) - the importance of cooperativity. Wysoczanski P, et al. RNA Biol, 2016. PMID 26479714, Free PMC Article

    See all (48) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. RES is a 71 kDa heterotrimer composed of the 3 proteins Pml1p, Bud13p and Snu17p. We solved the 3-dimensional structure of the core of the RES complex as well as the 2 dimers, Snu17p-Bud13p and Snu17p-Pml1p
      Title: Retention and splicing complex (RES) - the importance of cooperativity.
    2. The results show that in the RES complex, an FHA domain of Pml1p is flexibly tethered via an unstructured N-terminal region to Snu17p.
      Title: Crystal structure of the Pml1p subunit of the yeast precursor mRNA retention and splicing complex.
    3. Snu17p RRM binds multiple ligand proteins and acts as a platform that displays functional modules of the ligands, including forkhead-associated domain of Pml1p and conserved polylysine motif of Bud13p
      Title: An unusual RNA recognition motif acts as a scaffold for multiple proteins in the pre-mRNA retention and splicing complex.
    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 mRNA binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables molecular_function ND
    No biological Data available
    more info
    		  
    Process Evidence Code Pubs
    involved_in RNA splicing IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in mRNA export from nucleus IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in mRNA processing IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in mRNA splicing, via spliceosome IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in mRNA splicing, via spliceosome IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in maintenance of RNA location IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in maintenance of RNA location IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    part_of RES complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cytoplasm HDA PubMed 
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in nucleus HDA PubMed 
    is_active_in nucleus IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in nucleus IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    Pml1p
    NP_013116.1
    • Subunit of the RES complex; RES complex is required for nuclear retention of unspliced pre-mRNAs; acts in the same pathway as Pml39p and Mlp1p

    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_001144.5 Reference assembly

      Range
      176802..177416 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001181903.1 → NP_013116.1  TPA: Pml1p [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_013116.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VY18, Q06901, Q07930
      UniProtKB/TrEMBL
      A7A0S1, B3LSY9, B5VMV6, C7GXG2, C8ZCY8, G2WIL0
      Conserved Domains (1) summary
      cd00060
      Location:85 → 192
      FHA; Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain. FHA domains may bind phosphothreonine, phosphoserine and sometimes phosphotyrosine. In eukaryotes, many FHA domain-containing proteins ...
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q07930.1

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