Version 5.4
Homo sapiens Gene: TST
Summary
InnateDB Gene IDBG-6238.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol TST
Gene Name thiosulfate sulfurtransferase (rhodanese)
Synonyms RDS
Species Homo sapiens
Ensembl Gene ENSG00000128311
Encoded Proteins
IDBP-6240
thiosulfate sulfurtransferase (rhodanese)
IDBP-293927
thiosulfate sulfurtransferase (rhodanese)
IDBP-375037
thiosulfate sulfurtransferase (rhodanese)
IDBP-809119
thiosulfate sulfurtransferase (rhodanese)
Protein Structure
Useful resources Stemformatics EHFPI ImmGen
Entrez Gene
Summary This is one of two neighboring genes encoding similar proteins that each contain two rhodanese domains. The encoded protein is localized to the mitochondria and catalyzes the conversion of thiosulfate and cyanide to thiocyanate and sulfite. In addition, the protein interacts with 5S ribosomal RNA and facilitates its import into the mitochondria. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2012]
Gene Information
Type Protein coding
Genomic Location Chromosome 22:37010859-37020183
Strand Reverse strand
Band q12.3
Transcripts
ENST00000249042 ENSP00000249042
ENST00000403892 ENSP00000385828
ENST00000438203 ENSP00000400764
ENST00000622841 ENSP00000478739
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 14 experimentally validated interaction(s) in this database.
Experimentally validated
Total 14 [view]
Protein-Protein 14 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0004792 thiosulfate sulfurtransferase activity
GO:0008097 5S rRNA binding
Biological Process
GO:0000096 sulfur amino acid metabolic process
GO:0000098 sulfur amino acid catabolic process
GO:0008152 metabolic process
GO:0009440 cyanate catabolic process
GO:0030855 epithelial cell differentiation
GO:0034641 cellular nitrogen compound metabolic process
GO:0035928 rRNA import into mitochondrion
GO:0044281 small molecule metabolic process
GO:0051029 rRNA transport
GO:0070221 sulfide oxidation, using sulfide:quinone oxidoreductase
Cellular Component
GO:0005615 extracellular space
GO:0005739 mitochondrion
GO:0005743 mitochondrial inner membrane
GO:0005759 mitochondrial matrix
GO:0070062 extracellular vesicular exosome
Orthologs
Species
Mus musculus
Bos taurus
Gene ID
Gene Order
ENSMUSG00000044986
View Gene Order
ENSBTAG00000030650
Not yet available
Pathways
NETPATH
REACTOME
REACT_116010
Sulfide oxidation to sulfate pathway
REACT_115654
Degradation of cysteine and homocysteine pathway
REACT_115639
Sulfur amino acid metabolism pathway
REACT_13
Metabolism of amino acids and derivatives pathway
REACT_111217
Metabolism pathway
KEGG
hsa00920
Sulfur metabolism pathway
hsa00270
Cysteine and methionine metabolism pathway
hsa04122
Sulfur relay system pathway
INOH
PID NCI
Cross-References
SwissProt Q16762
TrEMBL B1AH48
UniProt Splice Variant
Entrez Gene 7263
UniGene Hs.474783
RefSeq NM_003312 NM_001270483
HUGO HGNC:12388
OMIM 180370
CCDS CCDS13938
HPRD 01583
IMGT
EMBL AK091874 BC010148 CH471095 CR456598 CR456998 D87292 Z73420
GenPept AAH10148 BAA13327 BAG52433 CAA97762 CAG30484 CAG33279 EAW60132
RNA Seq Atlas 7263

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca