U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

C11D2.4 Queuosine 5'-phosphate N-glycosylase/hydrolase [ Caenorhabditis elegans ]

Gene ID: 177378, updated on 2-Nov-2024

Summary

Go to the top of the page Help
Official Symbol
C11D2.4
Official Full Name
Queuosine 5'-phosphate N-glycosylase/hydrolase
Primary source
WormBase:WBGene00015702
Locus tag
CELE_C11D2.4
See related
AllianceGenome:WB:WBGene00015702
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Caenorhabditis elegans (strain: Bristol N2)
Lineage
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis
Summary
Predicted to enable hydrolase activity. Predicted to be involved in tRNA-guanine transglycosylation. Is expressed in several structures, including body wall musculature; excretory cell; intestine; nervous system; and non-striated muscle. Orthologous to human QNG1 (Q-nucleotide N-glycosylase 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 C11D2.4 in Genome Data Viewer
Location:
chromosome: IV
Exon count:
4
Sequence:
Chromosome: IV; NC_003282.8 (6155492..6156960, complement)

Chromosome IV - NC_003282.8Genomic Context describing neighboring genes Neighboring gene BLOC-1-related complex subunit 5 Neighboring gene ncRNA Neighboring gene ncRNA Neighboring gene ncRNA Neighboring gene PUA domain-containing protein Neighboring gene Ion transport domain-containing protein Neighboring gene ncRNA Neighboring gene ncRNA

Genomic regions, transcripts, and products

Go to the top of the page Help
Genomic Sequence:
NC_003282.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the pageHelp

Related articles in PubMed

  1. SIN-3 acts in distinct complexes to regulate the germline transcriptional program in Caenorhabditis elegans. Robert VJ, et al. Development, 2023 Nov 1. PMID 37818613, Free PMC Article
  2. Novel LOTUS-domain proteins are organizational hubs that recruit C. elegans Vasa to germ granules. Cipriani PG, et al. Elife, 2021 Jul 5. PMID 34223818, Free PMC Article
  3. Genome sequence of the nematode C. elegans: a platform for investigating biology. C. elegans Sequencing Consortium. Science, 1998 Dec 11. PMID 9851916

GeneRIFs: Gene References Into Functions

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

Markers

Homology

Gene Ontology Provided by WormBase

Function Evidence Code Pubs
enables hydrolase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in tRNA-guanine transglycosylation IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in tRNA-guanine transglycosylation IEA
Inferred from Electronic Annotation
more info
  

General protein information

Go to the top of the page Help
Preferred Names
Queuosine 5'-phosphate N-glycosylase/hydrolase
NP_500924.2
  • Confirmed by transcript evidence

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_003282.8 Reference assembly

    Range
    6155492..6156960 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_068523.8 → NP_500924.2  Queuosine 5'-phosphate N-glycosylase/hydrolase [Caenorhabditis elegans]

    See identical proteins and their annotated locations for NP_500924.2

    Status: REVIEWED

    UniProtKB/TrEMBL
    O45069
    Conserved Domains (1) summary
    pfam10343
    Location:56 → 341
    Q_salvage; Potential Queuosine, Q, salvage protein family
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.

Molecular Biology Databases
Research Materials
Tools