Search Results

Overview

Uniprot IDQ16762
Protein NameThiosulfate sulfurtransferase
Gene NameTST
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
136 GGFRNWLKEGHPVTS
14 YRALVSTKWLAESIR
163 TLDRSLLKTYEQVLE
175 VLENLESKRFQLVDS
236 LRALFQTKKVDLSQP
237 RALFQTKKVDLSQPL
24 AESIRTGKLGPGLRV
250 PLIATCRKGVTACHV
293 ESRVSQGKSEKA***

Function

Catalyzes the transfer of sulfur ion from thiosulfate to cyanide, although other thiol compounds, besides cyanide, can act as sulfur ion acceptors (By similarity). It also has weak mercaptopyruvate sulfurtransferase (MST) activity (By similarity). Has a pivotal role in cyanide detoxification (PubMed:40033006). 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 (PubMed:20663881, PubMed:21685364)

Protein Sequence

10 MVHQVLYRAL 20 VSTKWLAESI 30 RTGKLGPGLR 40 VLDASWYSPG 50 TREARKEYLE 60 RHVPGASFFD 70 IEECRDTASP 80 YEMMLPSEAG 90 FAEYVGRLGI 100 SNHTHVVVYD 110 GEHLGSFYAP 120 RVWWMFRVFG 130 HRTVSVLNGG 140 FRNWLKEGHP 150 VTSEPSRPEP 160 AVFKATLDRS 170 LLKTYEQVLE 180 NLESKRFQLV 190 DSRSQGRFLG 200 TEPEPDAVGL 210 DSGHIRGAVN 220 MPFMDFLTED 230 GFEKGPEELR 240 ALFQTKKVDL 250 SQPLIATCRK 260 GVTACHVALA 270 AYLCGKPDVA 280 VYDGSWSEWF 290 RRAPPESRVS QGKSEKA

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005615 extracellular space
Cellular Component GO:0005759 mitochondrial matrix
Cellular Component GO:0005739 mitochondrion
Molecular Function GO:0008097 5S rRNA binding
Molecular Function GO:0016783 sulfurtransferase activity
Molecular Function GO:0004792 thiosulfate-cyanide sulfurtransferase activity
Biological Process GO:0009440 cyanate catabolic process
Biological Process GO:0030855 epithelial cell differentiation
Biological Process GO:0035928 rRNA import into mitochondrion
Biological Process GO:0051029 rRNA transport
Biological Process GO:0000098 sulfur amino acid catabolic process

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[3] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.