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    CIN1 Cin1p [ Saccharomyces cerevisiae S288C ]

    Gene ID: 854531, updated on 17-May-2024

    Summary

    Gene symbol
    CIN1
    Gene description
    Cin1p
    Primary source
    FungiDB:YOR349W
    Locus tag
    YOR349W
    See related
    SGD:S000005876; AllianceGenome:SGD:S000005876; VEuPathDB:YOR349W
    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 GTPase activator activity and beta-tubulin binding activity. Involved in protein folding and tubulin complex assembly. Orthologous to human TBCD (tubulin folding cofactor D). [provided by Alliance of Genome Resources, Apr 2022]
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    Genomic context

    See CIN1 in Genome Data Viewer
    Location:
    chromosome: XV
    Exon count:
    1
    Sequence:
    Chromosome: XV; NC_001147.6 (989789..992833)

    Chromosome XV - NC_001147.6Genomic Context describing neighboring genes Neighboring gene pyruvate kinase PYK2 Neighboring gene proline permease PUT4 Neighboring gene Mne1p Neighboring gene serine/threonine protein kinase MEK1

    Interactions

    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    enables GTPase activator activity IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    enables GTPase activator activity IEA
    Inferred from Electronic Annotation
    more info
     
    enables beta-tubulin binding IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    enables beta-tubulin binding IEA
    Inferred from Electronic Annotation
    more info
     
    enables beta-tubulin binding ISS
    Inferred from Sequence or Structural Similarity
    more info
    PubMed 
    Process Evidence Code Pubs
    involved_in microtubule cytoskeleton organization IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    involved_in post-chaperonin tubulin folding pathway IEA
    Inferred from Electronic Annotation
    more info
     
    involved_in protein folding IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    involved_in protein folding IGI
    Inferred from Genetic Interaction
    more info
    PubMed 
    involved_in protein folding ISS
    Inferred from Sequence or Structural Similarity
    more info
    PubMed 
    involved_in tubulin complex assembly IEA
    Inferred from Electronic Annotation
    more info
     
    involved_in tubulin complex assembly IGI
    Inferred from Genetic Interaction
    more info
    PubMed 
    involved_in tubulin complex assembly IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    Component Evidence Code Pubs
    is_active_in cellular_component ND
    No biological Data available
    more info
     

    General protein information

    Preferred Names
    Cin1p
    NP_014994.3
    • Tubulin folding factor D involved in beta-tubulin (Tub2p) folding; isolated as mutant with increased chromosome loss and sensitivity to benomyl; CIN1 mRNA level is reduced when downstream gene MNE1 is deleted

    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_001147.6 Reference assembly

      Range
      989789..992833
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001183769.3NP_014994.3  TPA: Cin1p [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_014994.3

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6W344, P40987
      UniProtKB/TrEMBL
      A0A8H4BXJ3, A6ZPH9, C7GNR9, C8ZHA0, N1NYZ9
      Conserved Domains (1) summary
      COG5234
      Location:11012
      CIN1; Beta-tubulin folding cofactor D [Posttranslational modification, protein turnover, chaperones / Cytoskeleton]