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TPI1 triose-phosphate isomerase TPI1 [ Saccharomyces cerevisiae S288C ]

Gene ID: 851620, updated on 18-Sep-2024

Summary

Official Symbol
TPI1
Official Full Name
triose-phosphate isomerase TPI1
Primary source
SGD:S000002457
Locus tag
YDR050C
See related
AllianceGenome:SGD:S000002457; FungiDB:YDR050C; VEuPathDB:YDR050C
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Saccharomyces cerevisiae S288C (strain: S288C)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary
Enables triose-phosphate isomerase activity. Involved in glycolytic process. Located in mitochondrion. Used to study cancer and triosephosphate isomerase deficiency. Human ortholog(s) of this gene implicated in carbohydrate metabolic disorder and triosephosphate isomerase deficiency. Orthologous to human TPI1 (triosephosphate isomerase 1). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

See TPI1 in Genome Data Viewer
Location:
chromosome: IV
Exon count:
1
Sequence:
Chromosome: IV; NC_001136.10 (555726..556472, complement)

Chromosome IV - NC_001136.10Genomic Context describing neighboring genes Neighboring gene uroporphyrinogen decarboxylase HEM12 Neighboring gene Vms1p Neighboring gene acid phosphatase DET1 Neighboring gene protein serine/threonine kinase activating protein DBF4

Bibliography

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Pathways from PubChem

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables isomerase activity IEA
Inferred from Electronic Annotation
more info
 
enables triose-phosphate isomerase activity IBA
Inferred from Biological aspect of Ancestor
more info
 
enables triose-phosphate isomerase activity IDA
Inferred from Direct Assay
more info
PubMed 
enables triose-phosphate isomerase activity IEA
Inferred from Electronic Annotation
more info
 
Process Evidence Code Pubs
involved_in gluconeogenesis IBA
Inferred from Biological aspect of Ancestor
more info
 
involved_in gluconeogenesis IEA
Inferred from Electronic Annotation
more info
 
involved_in glyceraldehyde-3-phosphate biosynthetic process IBA
Inferred from Biological aspect of Ancestor
more info
 
involved_in glycerol catabolic process IBA
Inferred from Biological aspect of Ancestor
more info
 
involved_in glycolytic process IBA
Inferred from Biological aspect of Ancestor
more info
 
involved_in glycolytic process IEA
Inferred from Electronic Annotation
more info
 
involved_in glycolytic process IMP
Inferred from Mutant Phenotype
more info
PubMed 

General protein information

Preferred Names
triose-phosphate isomerase TPI1
NP_010335.1
  • Triose phosphate isomerase, abundant glycolytic enzyme; mRNA half-life is regulated by iron availability; transcription is controlled by activators Reb1p, Gcr1p, and Rap1p through binding sites in the 5' non-coding region; inhibition of Tpi1p activity by PEP (phosphoenolpyruvate) stimulates redox metabolism in respiring cells; E104D mutation in human homolog TPI1 causes a rare autosomal disease; human TPI1 can complement yeast null mutant

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_001136.10 Reference assembly

    Range
    555726..556472 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001180358.1NP_010335.1  TPA: triose-phosphate isomerase TPI1 [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_010335.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6VS37, P00942
    UniProtKB/TrEMBL
    A6ZY16, B3LGL8, B5VFV0, C7GTA0, C8Z4W9, G2WAF5, N1P6G4
    Conserved Domains (1) summary
    cd00311
    Location:5245
    TIM; Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of dihydroxyacetone phosphate and D-glyceraldehyde-3-phosphate. The reaction is very efficient and requires neither cofactors nor metal ions. TIM, usually ...