U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

TPT1 tRNA 2'-phosphotransferase [ Saccharomyces cerevisiae S288C ]

Gene ID: 854051, updated on 2-Nov-2024

Summary

Go to the top of the page Help
Official Symbol
TPT1
Official Full Name
tRNA 2'-phosphotransferase
Primary source
SGD:S000005462
Locus tag
YOL102C
See related
AllianceGenome:SGD:S000005462; FungiDB:YOL102C; VEuPathDB:YOL102C
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 tRNA 2'-phosphotransferase activity. Involved in tRNA splicing, via endonucleolytic cleavage and ligation. Located in cytoplasm and nucleus. Orthologous to human TRPT1 (tRNA phosphotransferase 1). [provided by Alliance of Genome Resources, Nov 2024]
NEW
Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help
See TPT1 in Genome Data Viewer
Location:
chromosome: XV
Exon count:
1
Sequence:
Chromosome: XV; NC_001147.6 (125997..126689, complement)

Chromosome XV - NC_001147.6Genomic Context describing neighboring genes Neighboring gene gag protein Neighboring gene gag-pol fusion protein Neighboring gene myo-inositol transporter ITR2 Neighboring gene Izh4p Neighboring gene serine/threonine protein kinase PKH2

Genomic regions, transcripts, and products

Go to the top of the page Help
Genomic Sequence:
NC_001147.6

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the pageHelp

Related articles in PubMed

  1. An enzyme from Saccharomyces cerevisiae uses NAD+ to transfer the splice junction 2'-phosphate from ligated tRNA to an acceptor molecule. McCraith SM, et al. J Biol Chem, 1991 Jun 25. PMID 2050693
  2. A highly specific phosphatase from Saccharomyces cerevisiae implicated in tRNA splicing. McCraith SM, et al. Mol Cell Biol, 1990 Mar. PMID 2154680, Free PMC Article
  3. An NAD derivative produced during transfer RNA splicing: ADP-ribose 1"-2" cyclic phosphate. Culver GM, et al. Science, 1993 Jul 9. PMID 8392224
  4. A 2'-phosphotransferase implicated in tRNA splicing is essential in Saccharomyces cerevisiae. Culver GM, et al. J Biol Chem, 1997 May 16. PMID 9148937
  5. A conditional lethal yeast phosphotransferase (tpt1) mutant accumulates tRNAs with a 2'-phosphate and an undermodified base at the splice junction. Spinelli SL, et al. RNA, 1997 Dec. PMID 9404890, Free PMC Article

See all (37) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Structural and biochemical insights into the molecular mechanism of TRPT1 for nucleic acid ADP-ribosylation.
    Title: Structural and biochemical insights into the molecular mechanism of TRPT1 for nucleic acid ADP-ribosylation.
  2. identified four residues-Arg23, His24, Arg71, and Arg138-as essential for Tpt1 function in vivo
    Title: Structure-function analysis of the yeast NAD+-dependent tRNA 2'-phosphotransferase Tpt1.
  3. examined 21 Tpt1 protein variants mutated in conserved residues or blocks of residues and show that one of them, Tpt1 K69A/R71S protein, accumulates large amounts of intermediate with trinucleotide substrate due to a very slow second step
    Title: Analysis of 2'-phosphotransferase (Tpt1p) from Saccharomyces cerevisiae: evidence for a conserved two-step reaction mechanism.
Submit: New GeneRIF Correction

Pathways from PubChem

Go to the top of the page

Interactions

Go to the top of the page Help
Products Interactant Other Gene Complex Source Pubs Description

General gene information

Go to the top of the page Help

Homology

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables tRNA 2'-phosphotransferase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables tRNA 2'-phosphotransferase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables tRNA 2'-phosphotransferase activity IEA
Inferred from Electronic Annotation
more info
  
enables transferase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in tRNA processing IEA
Inferred from Electronic Annotation
more info
  
involved_in tRNA splicing, via endonucleolytic cleavage and ligation IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in tRNA splicing, via endonucleolytic cleavage and ligation IDA
Inferred from Direct Assay
more info
 PubMed 
Component Evidence Code Pubs
located_in cytoplasm IDA
Inferred from Direct Assay
more info
 PubMed 
located_in nucleus IDA
Inferred from Direct Assay
more info
 PubMed 

General protein information

Go to the top of the page Help
Preferred Names
tRNA 2'-phosphotransferase
NP_014539.1
  • tRNA 2'-phosphotransferase; catalyzes the final step in tRNA splicing, transferring the 2'-PO(4) from the splice junction to NAD(+), forming ADP-ribose 1''-2''cyclic phosphate and nicotinamide; ADP-ribosyltransferase that ADP-ribosylates 5'-phosphorylated ssDNA and ssRNAs; human and mouse orthologs complement the inviability of the yeast null mutant

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_001147.6 Reference assembly

    Range
    125997..126689 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001183356.1 → NP_014539.1  TPA: tRNA 2'-phosphotransferase [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_014539.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6W1W6, Q12272
    UniProtKB/TrEMBL
    G2WMD3, N1NX51
    Conserved Domains (1) summary
    pfam01885
    Location:9 → 190
    PTS_2-RNA; RNA 2'-phosphotransferase, Tpt1 / KptA family
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
Q12272.1

Gene LinkOut

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

Other Literature Sources
Molecular Biology Databases
Research Materials
Tools