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CDC12 septin CDC12 [ Saccharomyces cerevisiae S288C ]

Gene ID: 856507, updated on 18-Sep-2024

Summary

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Official Symbol
CDC12
Official Full Name
septin CDC12
Primary source
SGD:S000001149
Locus tag
YHR107C
See related
AllianceGenome:SGD:S000001149; FungiDB:YHR107C; VEuPathDB:YHR107C
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
CLA10; PSL7
Summary
Enables several functions, including GTP binding activity; GTPase activity; and phosphatidylinositol phosphate binding activity. A structural constituent of cytoskeleton. Involved in cytoskeleton organization; maintenance of cell polarity; and positive regulation of protein kinase activity. Located in cellular bud scar; mating projection; and septin cytoskeleton. Part of septin complex. Orthologous to several human genes including SEPTIN2 (septin 2). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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See CDC12 in Genome Data Viewer
Location:
chromosome: VIII
Exon count:
1
Sequence:
Chromosome: VIII; NC_001140.6 (326813..328036, complement)

Chromosome VIII - NC_001140.6Genomic Context describing neighboring genes Neighboring gene Ypt35p Neighboring gene thioredoxin-disulfide reductase TRR2 Neighboring gene phosphatidylinositol 4-phosphate-binding protein Neighboring gene cytochrome c lysine N-methyltransferase

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_001140.6

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. LIVE-PAINT allows super-resolution microscopy inside living cells using reversible peptide-protein interactions. Oi C, et al. Commun Biol, 2020 Aug 20. PMID 32820217, Free PMC Article
  2. A septin from the filamentous fungus A. nidulans induces atypical pseudohyphae in the budding yeast S. cerevisiae. Lindsey R, et al. PLoS One, 2010 Mar 25. PMID 20360845, Free PMC Article
  3. Targeting metastable coiled-coil domains by computational design. Barth P, et al. J Am Chem Soc, 2008 Sep 10. PMID 18698842
  4. Interplay of septin amphipathic helices in sensing membrane-curvature and filament bundling. Woods BL, et al. Mol Biol Cell, 2021 Oct 1. PMID 34319771, Free PMC Article
  5. Septin filaments exhibit a dynamic, paired organization that is conserved from yeast to mammals. DeMay BS, et al. J Cell Biol, 2011 Jun 13. PMID 21670216, Free PMC Article

See all (184) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Interplay of septin amphipathic helices in sensing membrane-curvature and filament bundling.
    Title: Interplay of septin amphipathic helices in sensing membrane-curvature and filament bundling.
  2. We studied the interactions between actin and the FH2 domains of formins Cdc12, Bni1 and mDia1 to understand the factors underlying their different rates of polymerization. All-atom molecular dynamics simulations revealed two factors that influence actin filament elongation and correlate with the rates of elongation
    Title: Gating mechanisms during actin filament elongation by formins.
  3. during cytokinesis septin rings, located on both sides of the actomyosin ring, acted as barriers to compartmentalize the cortex around the cleavage site
    Title: Spatial coordination of cytokinetic events by compartmentalization of the cell cortex.
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 GTP binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables GTP binding IEA
Inferred from Electronic Annotation
more info
  
enables GTPase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables GTPase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables molecular adaptor activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables molecular adaptor activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables phosphatidylinositol-4-phosphate binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables phosphatidylinositol-5-phosphate binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables structural constituent of cytoskeleton IDA
Inferred from Direct Assay
more info
 PubMed 
Process Evidence Code Pubs
involved_in cell division IEA
Inferred from Electronic Annotation
more info
  
involved_in cytoskeleton-dependent cytokinesis IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in maintenance of cell polarity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in mitotic actomyosin contractile ring assembly IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in mitotic cytokinesis IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in positive regulation of protein phosphorylation IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in protein localization IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in septin ring assembly IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in septin ring assembly IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
is_active_in cell division site IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cellular bud neck HDA PubMed 
located_in cellular bud neck IEA
Inferred from Electronic Annotation
more info
  
located_in cellular bud neck septin ring IDA
Inferred from Direct Assay
more info
 PubMed 
located_in cellular bud scar IDA
Inferred from Direct Assay
more info
 PubMed 
located_in cytoplasm HDA PubMed 
located_in mating projection IDA
Inferred from Direct Assay
more info
 PubMed 
located_in membrane IEA
Inferred from Electronic Annotation
more info
  
is_active_in microtubule cytoskeleton IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in prospore membrane HDA PubMed 
part_of septin complex IBA
Inferred from Biological aspect of Ancestor
more info
  
part_of septin complex IDA
Inferred from Direct Assay
more info
 PubMed 
part_of septin complex IEA
Inferred from Electronic Annotation
more info
  
part_of septin complex IPI
Inferred from Physical Interaction
more info
 PubMed 
located_in septin filament array IDA
Inferred from Direct Assay
more info
 PubMed 
is_active_in septin ring IBA
Inferred from Biological aspect of Ancestor
more info
  

General protein information

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Preferred Names
septin CDC12
NP_011975.1
  • Component of the septin ring that is required for cytokinesis; septins are GTP-binding proteins that assemble into rod-like hetero-oligomers that can associate with other rods to form filaments; septin rings at the mother-bud neck act as scaffolds for recruiting cell division factors and as barriers to prevent diffusion of specific proteins between mother and daughter cells

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_001140.6 Reference assembly

    Range
    326813..328036 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001179237.1 → NP_011975.1  TPA: septin CDC12 [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_011975.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D3DL57, P32468
    UniProtKB/TrEMBL
    A6ZT15, B3LSM2, C7GLZ3, C8Z9Q0, G2WFI1, N1P284
    Conserved Domains (1) summary
    COG5019
    Location:16 → 404
    CDC3; Septin family protein [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton]
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P32468.1

Gene LinkOut

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