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Protein

Thiosulfate sulfurtransferase

Gene

TST

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Formation of iron-sulfur complexes, cyanide detoxification or modification of sulfur-containing enzymes. Other thiol compounds, besides cyanide, can act as sulfur ion acceptors. Also has weak mercaptopyruvate sulfurtransferase (MST) activity (By similarity). Together with MRPL18, acts as a mitochondrial import factor for the cytosolic 5S rRNA. Only the nascent unfolded cytoplasmic form is able to bind to the 5S rRNA.By similarity2 Publications

Catalytic activityi

Thiosulfate + cyanide = sulfite + thiocyanate.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei187SubstrateBy similarity1
Active sitei248Cysteine persulfide intermediatePROSITE-ProRule annotation1
Binding sitei250SubstrateBy similarity1

GO - Molecular functioni

  • 5S rRNA binding Source: UniProtKB
  • thiosulfate sulfurtransferase activity Source: ProtInc

GO - Biological processi

  • cyanate catabolic process Source: ProtInc
  • epithelial cell differentiation Source: UniProtKB
  • rRNA import into mitochondrion Source: UniProtKB
  • rRNA transport Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciZFISH:HS05179-MONOMER.
ReactomeiR-HSA-1614517. Sulfide oxidation to sulfate.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiosulfate sulfurtransferase (EC:2.8.1.1)
Alternative name(s):
Rhodanese
Gene namesi
Name:TST
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:12388. TST.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • mitochondrial inner membrane Source: Ensembl
  • mitochondrial matrix Source: ProtInc
  • mitochondrion Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

DisGeNETi7263.
OpenTargetsiENSG00000128311.
PharmGKBiPA37055.

Polymorphism and mutation databases

BioMutaiTST.
DMDMi3122965.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001393952 – 297Thiosulfate sulfurtransferaseAdd BLAST296

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei14N6-acetyllysine; alternateCombined sources1
Modified residuei14N6-succinyllysine; alternateBy similarity1
Glycosylationi35O-linked (GlcNAc)By similarity1
Modified residuei38PhosphoserineBy similarity1
Modified residuei136N6-acetyllysine; alternateBy similarity1
Modified residuei136N6-succinyllysine; alternateBy similarity1
Modified residuei163N6-acetyllysineBy similarity1
Modified residuei175N6-acetyllysine; alternateBy similarity1
Modified residuei175N6-succinyllysine; alternateBy similarity1
Modified residuei224N6-acetyllysine; alternateBy similarity1
Modified residuei224N6-succinyllysine; alternateBy similarity1
Modified residuei236N6-acetyllysineBy similarity1
Modified residuei237N6-acetyllysine; alternateBy similarity1
Modified residuei237N6-succinyllysine; alternateBy similarity1

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ16762.
MaxQBiQ16762.
PaxDbiQ16762.
PeptideAtlasiQ16762.
PRIDEiQ16762.

2D gel databases

REPRODUCTION-2DPAGEIPI00216293.

PTM databases

iPTMnetiQ16762.
PhosphoSitePlusiQ16762.
SwissPalmiQ16762.

Expressioni

Gene expression databases

BgeeiENSG00000128311.
CleanExiHS_TST.
ExpressionAtlasiQ16762. baseline and differential.
GenevisibleiQ16762. HS.

Organism-specific databases

HPAiCAB009546.
HPA003044.
HPA003643.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi113114. 13 interactors.
IntActiQ16762. 4 interactors.
STRINGi9606.ENSP00000249042.

Structurei

3D structure databases

ProteinModelPortaliQ16762.
SMRiQ16762.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini25 – 143Rhodanese 1PROSITE-ProRule annotationAdd BLAST119
Domaini173 – 288Rhodanese 2PROSITE-ProRule annotationAdd BLAST116

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni144 – 159HingeAdd BLAST16

Domaini

Contains two rhodanese domains with different primary structures but with near identical secondary structure conformations suggesting a common evolutionary origin. Only the C-terminal rhodanese domain contains the catalytic cysteine residue (By similarity).By similarity

Sequence similaritiesi

Contains 2 rhodanese domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1529. Eukaryota.
COG2897. LUCA.
GeneTreeiENSGT00510000046773.
HOGENOMiHOG000157237.
HOVERGENiHBG002345.
InParanoidiQ16762.
KOiK01011.
OMAiSRAQGRY.
OrthoDBiEOG091G0X2Q.
PhylomeDBiQ16762.
TreeFamiTF315133.

Family and domain databases

Gene3Di3.40.250.10. 2 hits.
InterProiIPR001763. Rhodanese-like_dom.
IPR001307. Thiosulphate_STrfase_CS.
[Graphical view]
PfamiPF00581. Rhodanese. 2 hits.
[Graphical view]
SMARTiSM00450. RHOD. 2 hits.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 2 hits.
PROSITEiPS00380. RHODANESE_1. 1 hit.
PS00683. RHODANESE_2. 1 hit.
PS50206. RHODANESE_3. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q16762-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVHQVLYRAL VSTKWLAESI RTGKLGPGLR VLDASWYSPG TREARKEYLE
60 70 80 90 100
RHVPGASFFD IEECRDTASP YEMMLPSEAG FAEYVGRLGI SNHTHVVVYD
110 120 130 140 150
GEHLGSFYAP RVWWMFRVFG HRTVSVLNGG FRNWLKEGHP VTSEPSRPEP
160 170 180 190 200
AVFKATLDRS LLKTYEQVLE NLESKRFQLV DSRSQGRFLG TEPEPDAVGL
210 220 230 240 250
DSGHIRGAVN MPFMDFLTED GFEKGPEELR ALFQTKKVDL SQPLIATCRK
260 270 280 290
GVTACHVALA AYLCGKPDVA VYDGSWSEWF RRAPPESRVS QGKSEKA
Length:297
Mass (Da):33,429
Last modified:January 23, 2007 - v4
Checksum:iBDAE6EE4E47A5650
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_051799102E → D.1 PublicationCorresponds to variant rs35156365dbSNPEnsembl.1
Natural variantiVAR_051800228E → G.Corresponds to variant rs1049270dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87292 mRNA. Translation: BAA13327.1.
CR456598 mRNA. Translation: CAG30484.1.
CR456998 mRNA. Translation: CAG33279.1.
AK091874 mRNA. Translation: BAG52433.1.
Z73420 Genomic DNA. Translation: CAA97762.1.
CH471095 Genomic DNA. Translation: EAW60132.1.
BC010148 mRNA. Translation: AAH10148.1.
CCDSiCCDS13938.1.
PIRiJC5286.
RefSeqiNP_001257412.1. NM_001270483.1.
NP_003303.2. NM_003312.5.
UniGeneiHs.474783.

Genome annotation databases

EnsembliENST00000249042; ENSP00000249042; ENSG00000128311.
ENST00000403892; ENSP00000385828; ENSG00000128311.
ENST00000622841; ENSP00000478739; ENSG00000128311.
GeneIDi7263.
KEGGihsa:7263.
UCSCiuc003aqg.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87292 mRNA. Translation: BAA13327.1.
CR456598 mRNA. Translation: CAG30484.1.
CR456998 mRNA. Translation: CAG33279.1.
AK091874 mRNA. Translation: BAG52433.1.
Z73420 Genomic DNA. Translation: CAA97762.1.
CH471095 Genomic DNA. Translation: EAW60132.1.
BC010148 mRNA. Translation: AAH10148.1.
CCDSiCCDS13938.1.
PIRiJC5286.
RefSeqiNP_001257412.1. NM_001270483.1.
NP_003303.2. NM_003312.5.
UniGeneiHs.474783.

3D structure databases

ProteinModelPortaliQ16762.
SMRiQ16762.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113114. 13 interactors.
IntActiQ16762. 4 interactors.
STRINGi9606.ENSP00000249042.

PTM databases

iPTMnetiQ16762.
PhosphoSitePlusiQ16762.
SwissPalmiQ16762.

Polymorphism and mutation databases

BioMutaiTST.
DMDMi3122965.

2D gel databases

REPRODUCTION-2DPAGEIPI00216293.

Proteomic databases

EPDiQ16762.
MaxQBiQ16762.
PaxDbiQ16762.
PeptideAtlasiQ16762.
PRIDEiQ16762.

Protocols and materials databases

DNASUi7263.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000249042; ENSP00000249042; ENSG00000128311.
ENST00000403892; ENSP00000385828; ENSG00000128311.
ENST00000622841; ENSP00000478739; ENSG00000128311.
GeneIDi7263.
KEGGihsa:7263.
UCSCiuc003aqg.5. human.

Organism-specific databases

CTDi7263.
DisGeNETi7263.
GeneCardsiTST.
HGNCiHGNC:12388. TST.
HPAiCAB009546.
HPA003044.
HPA003643.
MIMi180370. gene.
neXtProtiNX_Q16762.
OpenTargetsiENSG00000128311.
PharmGKBiPA37055.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1529. Eukaryota.
COG2897. LUCA.
GeneTreeiENSGT00510000046773.
HOGENOMiHOG000157237.
HOVERGENiHBG002345.
InParanoidiQ16762.
KOiK01011.
OMAiSRAQGRY.
OrthoDBiEOG091G0X2Q.
PhylomeDBiQ16762.
TreeFamiTF315133.

Enzyme and pathway databases

BioCyciZFISH:HS05179-MONOMER.
ReactomeiR-HSA-1614517. Sulfide oxidation to sulfate.

Miscellaneous databases

GeneWikiiTST_(gene).
GenomeRNAii7263.
PROiQ16762.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000128311.
CleanExiHS_TST.
ExpressionAtlasiQ16762. baseline and differential.
GenevisibleiQ16762. HS.

Family and domain databases

Gene3Di3.40.250.10. 2 hits.
InterProiIPR001763. Rhodanese-like_dom.
IPR001307. Thiosulphate_STrfase_CS.
[Graphical view]
PfamiPF00581. Rhodanese. 2 hits.
[Graphical view]
SMARTiSM00450. RHOD. 2 hits.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 2 hits.
PROSITEiPS00380. RHODANESE_1. 1 hit.
PS00683. RHODANESE_2. 1 hit.
PS50206. RHODANESE_3. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTHTR_HUMAN
AccessioniPrimary (citable) accession number: Q16762
Secondary accession number(s): B3KRM1, Q6IB06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 150 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.