U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

DUS2 dihydrouridine synthase 2 [ Papio anubis (olive baboon) ]

Gene ID: 100999210, updated on 8-Mar-2024

Summary

Go to the top of the page Help
Gene symbol
DUS2
Gene description
dihydrouridine synthase 2
See related
Ensembl:ENSPANG00000022609
Gene type
protein coding
RefSeq status
MODEL
Organism
Papio anubis
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Cercopithecidae; Cercopithecinae; Papio
Also known as
DUS2L
Orthologs
human mouse all
NEW
Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help
See DUS2 in Genome Data Viewer
Location:
chromosome: 18
Exon count:
22
Annotation release Status Assembly Chr Location
104 current Panubis1.0 (GCF_008728515.1) 18 NC_044993.1 (21729406..21789043, complement)
103 previous assembly Panu_3.0 (GCF_000264685.3) 20 NC_018171.2 (50407958..50467585)

Chromosome 18 - NC_044993.1Genomic Context describing neighboring genes Neighboring gene nuclear factor of activated T cells 3 Neighboring gene small nucleolar RNA SNORA48 Neighboring gene ubiquitin-conjugating enzyme E2 N-like Neighboring gene 60S ribosomal protein L31 pseudogene Neighboring gene U6 spliceosomal RNA Neighboring gene DEAD-box helicase 28 Neighboring gene DPEP2 neighbor

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the pageHelp

Related articles in PubMed

  1. 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
  2. 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

Markers

Homology

Gene Ontology Provided by RefSeq

Function Evidence Code Pubs
enables flavin adenine dinucleotide binding IEA
Inferred from Electronic Annotation
more info
 PubMed 
enables tRNA binding IEA
Inferred from Electronic Annotation
more info
 PubMed 
enables tRNA dihydrouridine synthase activity IEA
Inferred from Electronic Annotation
more info
 PubMed 
Process Evidence Code Pubs
involved_in tRNA dihydrouridine synthesis IEA
Inferred from Electronic Annotation
more info
 PubMed 
Component Evidence Code Pubs
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
 PubMed 

General protein information

Go to the top of the page Help
Preferred Names
tRNA-dihydrouridine(20) synthase [NAD(P)+]-like
Names
dihydrouridine synthase 2-like, SMM1 homolog

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

RefSeqs of Annotated Genomes: Papio anubis Annotation Release 104 details...Open this link in a new tab

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

Reference Panubis1.0 Primary Assembly

Genomic

  1. NC_044993.1 Reference Panubis1.0 Primary Assembly

    Range
    21729406..21789043 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_003917081.3 → XP_003917130.1  tRNA-dihydrouridine(20) synthase [NAD(P)+]-like isoform X2

    See identical proteins and their annotated locations for XP_003917130.1

    UniProtKB/TrEMBL
    A0A096NBT9
    Conserved Domains (2) summary
    cd02801
    Location:13 → 252
    DUS_like_FMN; Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also ...
    cd19871
    Location:369 → 436
    DSRM_DUS2L; double-stranded RNA binding motif of tRNA-dihydrouridine(20) synthase [NAD(P)+]-like (DUS2L) and similar proteins

  2. XM_021932372.2 → XP_021788064.1  tRNA-dihydrouridine(20) synthase [NAD(P)+]-like isoform X2

    UniProtKB/TrEMBL
    A0A096NBT9
    Conserved Domains (2) summary
    cd02801
    Location:13 → 252
    DUS_like_FMN; Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also ...
    cd19871
    Location:369 → 436
    DSRM_DUS2L; double-stranded RNA binding motif of tRNA-dihydrouridine(20) synthase [NAD(P)+]-like (DUS2L) and similar proteins

  3. XM_009196725.4 → XP_009194989.2  tRNA-dihydrouridine(20) synthase [NAD(P)+]-like isoform X1

    Conserved Domains (3) summary
    COG0042
    Location:64 → 368
    DusA; tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]
    cd00048
    Location:423 → 487
    DSRM; Double-stranded RNA binding motif. Binding is not sequence specific but is highly specific for double stranded RNA. Found in a variety of proteins including dsRNA dependent protein kinase PKR, RNA helicases, Drosophila staufen protein, E. coli RNase III, ...
    cd02801
    Location:67 → 306
    DUS_like_FMN; Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also ...

  4. XM_021932373.2 → XP_021788065.1  tRNA-dihydrouridine(20) synthase [NAD(P)+]-like isoform X2

    UniProtKB/TrEMBL
    A0A096NBT9
    Conserved Domains (2) summary
    cd02801
    Location:13 → 252
    DUS_like_FMN; Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also ...
    cd19871
    Location:369 → 436
    DSRM_DUS2L; double-stranded RNA binding motif of tRNA-dihydrouridine(20) synthase [NAD(P)+]-like (DUS2L) and similar proteins

  5. XM_031657896.1 → XP_031513756.1  tRNA-dihydrouridine(20) synthase [NAD(P)+]-like isoform X2

    UniProtKB/TrEMBL
    A0A096NBT9
    Conserved Domains (2) summary
    cd02801
    Location:13 → 252
    DUS_like_FMN; Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also ...
    cd19871
    Location:369 → 436
    DSRM_DUS2L; double-stranded RNA binding motif of tRNA-dihydrouridine(20) synthase [NAD(P)+]-like (DUS2L) and similar proteins

  6. XM_009196727.4 → XP_009194991.1  tRNA-dihydrouridine(20) synthase [NAD(P)+]-like isoform X2

    See identical proteins and their annotated locations for XP_009194991.1

    UniProtKB/TrEMBL
    A0A096NBT9
    Conserved Domains (2) summary
    cd02801
    Location:13 → 252
    DUS_like_FMN; Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also ...
    cd19871
    Location:369 → 436
    DSRM_DUS2L; double-stranded RNA binding motif of tRNA-dihydrouridine(20) synthase [NAD(P)+]-like (DUS2L) and similar proteins

  7. XM_009196728.4 → XP_009194992.1  tRNA-dihydrouridine(20) synthase [NAD(P)+]-like isoform X2

    See identical proteins and their annotated locations for XP_009194992.1

    UniProtKB/TrEMBL
    A0A096NBT9
    Related
    ENSPANP00000010244.1, ENSPANT00000017127.3
    Conserved Domains (2) summary
    cd02801
    Location:13 → 252
    DUS_like_FMN; Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also ...
    cd19871
    Location:369 → 436
    DSRM_DUS2L; double-stranded RNA binding motif of tRNA-dihydrouridine(20) synthase [NAD(P)+]-like (DUS2L) and similar proteins

  8. XM_009196729.3 → XP_009194993.1  tRNA-dihydrouridine(20) synthase [NAD(P)+]-like isoform X3

    See identical proteins and their annotated locations for XP_009194993.1

    Conserved Domains (2) summary
    cd00048
    Location:343 → 407
    DSRM; Double-stranded RNA binding motif. Binding is not sequence specific but is highly specific for double stranded RNA. Found in a variety of proteins including dsRNA dependent protein kinase PKR, RNA helicases, Drosophila staufen protein, E. coli RNase III, ...
    cd02801
    Location:4 → 226
    DUS_like_FMN; Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also ...

  9. XM_021932375.2 → XP_021788067.1  tRNA-dihydrouridine(20) synthase [NAD(P)+]-like isoform X4

    Conserved Domains (2) summary
    cd00048
    Location:321 → 385
    DSRM; Double-stranded RNA binding motif. Binding is not sequence specific but is highly specific for double stranded RNA. Found in a variety of proteins including dsRNA dependent protein kinase PKR, RNA helicases, Drosophila staufen protein, E. coli RNase III, ...
    cd02801
    Location:7 → 204
    DUS_like_FMN; Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also ...

RNA

  1. XR_002519397.2 RNA Sequence

  2. XR_001898415.3 RNA Sequence

  3. XR_002519398.2 RNA Sequence

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.