TSTD1 thiosulfate sulfurtransferase like domain containing 1 [Homo sapiens (human)] - Gene

Summary

Official Symbol: TSTD1provided by HGNC
Official Full Name: thiosulfate sulfurtransferase like domain containing 1provided by HGNC
Primary source: HGNC:HGNC:35410
See related: Ensembl:ENSG00000215845 MIM:616041; AllianceGenome:HGNC:35410
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: KAT; TST
Summary: Predicted to enable thiosulfate-thiol sulfurtransferase activity. Predicted to be involved in sulfide oxidation, using sulfide:quinone oxidoreductase. Located in cytoplasmic ribonucleoprotein granule and cytosol. [provided by Alliance of Genome Resources, Nov 2024]
Expression: Ubiquitous expression in prostate (RPKM 33.0), kidney (RPKM 26.4) and 25 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 1q23.3

Exon count:: 4

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	1	NC_000001.11 (161037631..161038964, complement)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	1	NC_060925.1 (160175138..160176471, complement)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	1	NC_000001.10 (161007421..161008754, complement)

Chromosome 1 - NC_000001.11 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: HPA RNA-seq normal tissues 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

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Data suggest that TSTD1 can utilize thioredoxin as an acceptor in the presence of thioredoxin reductase and NADPH.
Title: Thiosulfate sulfurtransferase-like domain-containing 1 protein interacts with thioredoxin.
Endurance exercise caused an increase in plasma KYNA within the first hour after exercise. In contrast, a bout of high-intensity eccentric exercise did not lead to increased plasma KYNA concentration. Our results show that regular endurance exercise causes adaptations in kynurenine metabolism which can have implications for exercise recommendations for patients with depressive disorder.
Title: Endurance exercise increases skeletal muscle kynurenine aminotransferases and plasma kynurenic acid in humans.
Biosynthesis of a central intermediate in hydrogen sulfide metabolism by a novel human sulfurtransferase and its yeast ortholog.
Title: Biosynthesis of a central intermediate in hydrogen sulfide metabolism by a novel human sulfurtransferase and its yeast ortholog.
The presence of kynurenine aminotransferase III in Corpora amylacea in the human retina and optic nerve indicates that this enzyme may be relevant in mechanisms of neurodegeneration leading to Corpora amylaceaformation.
Title: Presence of L-kynurenine aminotransferase III in retinal ganglion cells and corpora amylacea in the human retina and optic nerve.
Observational study of gene-disease association, gene-environment interaction, and pharmacogenomic / toxicogenomic. (HuGE Navigator)
Title: Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study.
Observational study of gene-disease association. (HuGE Navigator)
Title: Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip.

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Phenotypes

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

Review eQTL and phenotype association data in this region using PheGenI

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

General gene information

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Markers

RH94217 (e-PCR)
- UniSTS:89464

RH70346 (e-PCR)
- UniSTS:48760

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables thiosulfate-thiol sulfurtransferase activity	TAS Traceable Author Statement more info

Process	Evidence Code	Pubs
involved_in sulfide oxidation, using sulfide:quinone oxidoreductase	TAS Traceable Author Statement more info

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasmic ribonucleoprotein granule	IDA Inferred from Direct Assay more info
located_in cytosol	IDA Inferred from Direct Assay more info
located_in cytosol	TAS Traceable Author Statement more info
located_in perinuclear region of cytoplasm	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: thiosulfate:glutathione sulfurtransferase

Names: putative thiosulfate sulfurtransferase KAT; thiosulfate sulfurtransferase (rhodanese)-like domain containing 1; thiosulfate sulfurtransferase/rhodanese-like domain-containing protein 1

NP_001106676.1

EC 2.8.1.3

NP_001106677.1

EC 2.8.1.3

NP_001106678.1

EC 2.8.1.3

NCBI Reference Sequences (RefSeq)

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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_001113205.2 → NP_001106676.1 thiosulfate:glutathione sulfurtransferase isoform 3

Status: VALIDATED

Description

Transcript Variant: This variant (3) uses an alternate splice site in the 3' coding region that results in a frameshift and premature stop codon, compared to variant 1. The encoded protein (isoform 3) has a shorter, distinct C-terminus compared to isoform 1.

Source sequence(s)

AV688621, BC001699

Consensus CDS

CCDS44258.1

UniProtKB/Swiss-Prot

Q8NFU3

Related

ENSP00000325518.10, ENST00000318289.14

Conserved Domains (1) summary

cl00125
Location:7 → 101

RHOD; Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins ...
NM_001113206.2 → NP_001106677.1 thiosulfate:glutathione sulfurtransferase isoform 2

See identical proteins and their annotated locations for NP_001106677.1

Status: VALIDATED

Description

Transcript Variant: This variant (2) lacks an alternate in-frame exon in the 5' coding region, compared to variant 1, that results a shorter protein (isoform 2), compared to isoform 1.

Source sequence(s)

AV688621, CD675389

Consensus CDS

CCDS44257.1

UniProtKB/TrEMBL

R4GNF9

Related

ENSP00000357003.1, ENST00000368024.5

Conserved Domains (1) summary

cl00125
Location:4 → 71

RHOD; Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins ...
NM_001113207.2 → NP_001106678.1 thiosulfate:glutathione sulfurtransferase isoform 1

See identical proteins and their annotated locations for NP_001106678.1

Status: VALIDATED

Description

Transcript Variant: This variant (1) encodes the longest isoform (1).

Source sequence(s)

CD675389

Consensus CDS

CCDS53400.1

UniProtKB/Swiss-Prot

Q5SY48, Q5SY49, Q5SY50, Q5SY51, Q8NFU2, Q8NFU3, Q9BV22

Related

ENSP00000388293.2, ENST00000423014.3

Conserved Domains (1) summary

cl00125
Location:7 → 112

RHOD; Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins ...