DUS2 dihydrouridine synthase 2 [Homo sapiens (human)] - Gene

Summary

Official Symbol: DUS2provided by HGNC
Official Full Name: dihydrouridine synthase 2provided by HGNC
Primary source: HGNC:HGNC:26014
See related: Ensembl:ENSG00000167264 MIM:609707; AllianceGenome:HGNC:26014
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: SMM1; DUS2L; URLC8
Summary: This gene encodes a cytoplasmic protein that catalyzes the conversion of uridine residues to dihydrouridine in the D-loop of tRNA. The resulting modified bases confer enhanced regional flexibility to tRNA. The encoded protein may increase the rate of translation by inhibiting an interferon-induced protein kinase. This gene has been implicated in pulmonary carcinogenesis. Alternatively spliced transcript variants have been described for this gene. [provided by RefSeq, Nov 2012]
Expression: Broad expression in testis (RPKM 12.7), lymph node (RPKM 5.7) and 24 other tissues See more
Orthologs: mouse all
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Location:: 16q22.1

Exon count:: 17

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	16	NC_000016.10 (68023284..68079320)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	16	NC_060940.1 (73819064..73875073)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	16	NC_000016.9 (68057187..68113223)

Chromosome 16 - NC_000016.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

Go to the top of the page Help

See details

Project title: HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

we establish that while hDus2 dsRBD retains a conventional dsRNA recognition capability, the presence of an N-terminal extension appended to the canonical domain provides additional residues for binding tRNA in a structure-specific mode of action.
Title: Molecular basis for transfer RNA recognition by the double-stranded RNA-binding domain of human dihydrouridine synthase 2.
Here, the X-ray crystal structure of a construct of hDus2 encompassing the catalytic and tRNA-recognition domains (residues 1-340) determined at 1.9 A resolution is presented.
Title: From bacterial to human dihydrouridine synthase: automated structure determination.
This is the first reported case of a tRNA-modifying enzyme (dihydrouridine synthase 2) carrying a dsRNA binding domain used to bind tRNAs.
Title: An extended dsRBD is required for post-transcriptional modification in human tRNAs.
crystals belonged to space group P2(1) and contained a single molecule of HsDus2L in the asymmetric unit
Title: Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of human dihydrouridine synthase.
Observational study of gene-disease association. (HuGE Navigator)
Title: Genetic variants in nuclear-encoded mitochondrial genes influence AIDS progression.
hDUS2 interacts with protein kinase PKR through its dsRNA binding/dimerization domain and inhibits its kinase activity.
Title: Interaction of human tRNA-dihydrouridine synthase-2 with interferon-induced protein kinase PKR.

Submit: New GeneRIF Correction

Phenotypes

Go to the top of the page Help

Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Variation

Go to the top of the page Help

See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

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

Bdy91f03 (e-PCR)
- UniSTS:71954

D16S3211 (e-PCR)
- UniSTS:53870

SHGC-57903 (e-PCR)
- UniSTS:49297

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables FMN binding	IDA Inferred from Direct Assay more info	PubMed
enables NADPH binding	IDA Inferred from Direct Assay more info	PubMed
enables double-stranded RNA binding	IDA Inferred from Direct Assay more info	PubMed
enables flavin adenine dinucleotide binding	IEA Inferred from Electronic Annotation more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein kinase inhibitor activity	IDA Inferred from Direct Assay more info	PubMed
enables tRNA binding	IEA Inferred from Electronic Annotation more info
enables tRNA dihydrouridine synthase activity	IBA Inferred from Biological aspect of Ancestor more info
enables tRNA dihydrouridine synthase activity	IDA Inferred from Direct Assay more info	PubMed
enables tRNA-dihydrouridine20 synthase activity	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in antiviral innate immune response	IPI Inferred from Physical Interaction more info	PubMed
involved_in tRNA dihydrouridine synthesis	IBA Inferred from Biological aspect of Ancestor more info
involved_in tRNA dihydrouridine synthesis	IDA Inferred from Direct Assay more info	PubMed

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	IDA Inferred from Direct Assay more info
located_in cytosol	TAS Traceable Author Statement more info
located_in endoplasmic reticulum	IEA Inferred from Electronic Annotation more info
located_in mitochondrion	HTP more info	PubMed

General protein information

Go to the top of the page Help

Preferred Names: tRNA-dihydrouridine(20) synthase [NAD(P)+]-like

Names: SMM1 homolog; dihydrouridine synthase 2-like, SMM1 homolog; tRNA-dihydrouridine(20) synthase (NAD(P)(+)); up-regulated in lung cancer protein 8

NP_001258691.1

EC 1.3.1.91

NP_001258692.1

EC 1.3.1.91

NP_060273.1

EC 1.3.1.91

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001271762.2 → NP_001258691.1 tRNA-dihydrouridine(20) synthase [NAD(P)+]-like isoform 1

See identical proteins and their annotated locations for NP_001258691.1

Status: REVIEWED

Description

Transcript Variant: This variant (2) differs in the 5' UTR compared to variant 1. Both variants 1 and 2 encode the same isoform (1).

Source sequence(s)

AC130462, AK000406, BC006527

Consensus CDS

CCDS10859.1

UniProtKB/Swiss-Prot

A8K3G3, Q4H4D9, Q9NX74

UniProtKB/TrEMBL

B4DKP8

Related

ENSP00000351769.6, ENST00000358896.10

Conserved Domains (2) summary

cd00048
Location:369 → 433

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: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 ...
NM_001271763.2 → NP_001258692.1 tRNA-dihydrouridine(20) synthase [NAD(P)+]-like isoform 2

Status: REVIEWED

Description

Transcript Variant: This variant (3) lacks two alternate exons, resulting in the loss of an in-frame segment in the coding region, compared to variant 1. The encoded isoform (2) is shorter than isoform 1.

Source sequence(s)

AC130462, AK000406, AK296663, BC006527

Consensus CDS

CCDS61970.1

UniProtKB/TrEMBL

B4DKP8, E7EUN9

Related

ENSP00000409498.1, ENST00000432752.5

Conserved Domains (3) summary

COG0042
Location:10 → 279

DusA; tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]

cd00048
Location:334 → 398

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:13 → 217

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 ...
NM_017803.5 → NP_060273.1 tRNA-dihydrouridine(20) synthase [NAD(P)+]-like isoform 1

See identical proteins and their annotated locations for NP_060273.1

Status: REVIEWED

Description

Transcript Variant: This variant (1) represents the longest transcript and encodes the longer isoform (1).

Source sequence(s)

AC130462, AK000406, BC006527

Consensus CDS

CCDS10859.1

UniProtKB/Swiss-Prot

A8K3G3, Q4H4D9, Q9NX74

UniProtKB/TrEMBL

B4DKP8

Related

ENSP00000455229.1, ENST00000565263.6

Conserved Domains (2) summary

cd00048
Location:369 → 433

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: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 ...