UniProt Accession

 THTR_HUMAN; Q16762; B3KRM1; Q6IB06 

Genbank Protein ID

 D87292; CR456598; CR456998; AK091874; Z73420; CH471095; BC010148 

Genbank Nucleotide ID

 BAA13327.1; CAG30484.1; CAG33279.1; BAG52433.1; CAA97762.1; EAW60132.1; AAH10148.1 

Protein Name

 Thiosulfate sulfurtransferase 

Protein Synonyms/Alias

 Rhodanese 

Gene Name

 TST 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
14	YRALVSTKWLAESIR	acetylation	[1]
14	YRALVSTKWLAESIR	ubiquitination	[2, 3]
154	RPEPAVFKATLDRSL	acetylation	[4]

Reference

 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 

Functional Description

 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. 

Sequence Annotation

 DOMAIN 25 143 Rhodanese 1.
 DOMAIN 173 288 Rhodanese 2.
 REGION 144 159 Hinge.
 ACT_SITE 248 248 Cysteine persulfide intermediate (By
 BINDING 187 187 Substrate (By similarity).
 BINDING 250 250 Substrate (By similarity).
 MOD_RES 14 14 N6-acetyllysine; alternate.
 MOD_RES 14 14 N6-succinyllysine; alternate (By
 MOD_RES 136 136 N6-acetyllysine (By similarity).
 MOD_RES 164 164 Phosphothreonine (By similarity).
 MOD_RES 165 165 Phosphotyrosine (By similarity).  

Keyword

 Acetylation; Complete proteome; Direct protein sequencing; Mitochondrion; Phosphoprotein; Polymorphism; Reference proteome; Repeat; RNA-binding; Transferase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 297 AA 

Protein Sequence

Gene Ontology

 GO:0005743; C:mitochondrial inner membrane; IEA:Compara.
 GO:0005759; C:mitochondrial matrix; TAS:Reactome.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0008097; F:5S rRNA binding; IDA:UniProtKB.
 GO:0004792; F:thiosulfate sulfurtransferase activity; TAS:ProtInc.
 GO:0009440; P:cyanate catabolic process; TAS:ProtInc.
 GO:0035928; P:rRNA import into mitochondrion; IMP:UniProtKB.
 GO:0070221; P:sulfide oxidation, using sulfide:quinone oxidoreductase; TAS:Reactome.
 GO:0000098; P:sulfur amino acid catabolic process; TAS:Reactome. 

Interpro

 IPR001763; Rhodanese-like_dom.
 IPR001307; Thiosulphate_STrfase_CS. 

Pfam

 PF00581; Rhodanese 

SMART

 SM00450; RHOD 

PROSITE

 PS00380; RHODANESE_1
 PS00683; RHODANESE_2
 PS50206; RHODANESE_3 

PRINTS