U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

TPI1 TPI1 [ Nakaseomyces glabratus ]

Gene ID: 2888881, updated on 19-Jun-2024

Summary

Go to the top of the page Help
Gene symbol
TPI1
Gene description
TPI1
Locus tag
GVI51_H08217
See related
FungiDB:GVI51_H08217; VEuPathDB:GVI51_H08217
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Nakaseomyces glabratus (strain: ATCC 2001, nat-host: Homo sapiens, culture-collection: ATCC:2001, type-material: type material of Cryptococcus glabratus)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces
Old locus tag
CAGL0H08327g
NEW
Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help
See TPI1 in Genome Data Viewer
Location:
chromosome: H
Exon count:
1
Sequence:
Chromosome: H; NC_088958.1 (820164..820910)

Chromosome H - NC_088958.1Genomic Context describing neighboring genes Neighboring gene HSP10 Neighboring gene uncharacterized protein Neighboring gene uncharacterized protein Neighboring gene uncharacterized protein

Genomic regions, transcripts, and products

Go to the top of the page Help
Genomic Sequence:
NC_088958.1

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the pageHelp

Related articles in PubMed

  1. De novo genome assembly of Candida glabrata reveals cell wall protein complement and structure of dispersed tandem repeat arrays. Xu Z, et al. Mol Microbiol, 2020 Jun. PMID 32068314
  2. Manual GO annotation of predictive protein signatures: the InterPro approach to GO curation. Burge S, et al. Database (Oxford), 2012. PMID 22301074, Free PMC Article
  3. TreeGrafter: phylogenetic tree-based annotation of proteins with Gene Ontology terms and other annotations. Tang H, et al. Bioinformatics, 2019 Feb 1. PMID 30032202, Free PMC Article

GeneRIFs: Gene References Into Functions

General gene information

Go to the top of the page Help
  • CAGL0H08327g
    Putative triose-phosphate isomerase; protein abundance decreased in ace2 mutant cells

Gene Ontology Provided by RefSeq

Function Evidence Code Pubs
enables triose-phosphate isomerase activity IEA
Inferred from Electronic Annotation
more info
 PubMed 
Process Evidence Code Pubs
involved_in gluconeogenesis IEA
Inferred from Electronic Annotation
more info
 PubMed 
involved_in glyceraldehyde-3-phosphate biosynthetic process IEA
Inferred from Electronic Annotation
more info
 PubMed 
involved_in glycerol catabolic process IEA
Inferred from Electronic Annotation
more info
 PubMed 
involved_in glycolytic process IEA
Inferred from Electronic Annotation
more info
 PubMed 
Component Evidence Code Pubs
located_in cytosol IEA
Inferred from Electronic Annotation
more info
 PubMed 

General protein information

Go to the top of the page Help
Preferred Names
TPI1
XP_447161.1
  • CAGL0H08327g
    Putative triose-phosphate isomerase; protein abundance decreased in ace2 mutant cells

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_088958.1 Reference assembly

    Range
    820164..820910
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_447161.1 → XP_447161.1  TPI1 [Nakaseomyces glabratus]

    See identical proteins and their annotated locations for XP_447161.1

    Status: PROVISIONAL

    UniProtKB/Swiss-Prot
    Q6FRI3
    UniProtKB/TrEMBL
    A0A0W0EMN7
    Conserved Domains (1) summary
    cd00311
    Location:5 → 245
    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 ...
Nucleotide Protein
Heading Accession and Version

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.