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Q16762 (THTR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thiosulfate sulfurtransferase

EC=2.8.1.1
Alternative name(s):
Rhodanese
Gene names
Name:TST
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length297 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10 Ref.12

Catalytic activity

Thiosulfate + cyanide = sulfite + thiocyanate.

Subunit structure

Monomer.

Subcellular location

Mitochondrion matrix.

Domain

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.

Sequence similarities

Contains 2 rhodanese domains.

Ontologies

Keywords
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   DomainRepeat
   LigandRNA-binding
   Molecular functionTransferase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

cyanate catabolic process

Traceable author statement Ref.1. Source: ProtInc

epithelial cell differentiation

Inferred from direct assay PubMed 21492153. Source: UniProt

rRNA import into mitochondrion

Inferred from mutant phenotype Ref.10. Source: UniProtKB

rRNA transport

Inferred from direct assay Ref.12. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

sulfide oxidation, using sulfide:quinone oxidoreductase

Traceable author statement. Source: Reactome

sulfur amino acid catabolic process

Traceable author statement. Source: Reactome

sulfur amino acid metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentextracellular space

Inferred from direct assay PubMed 23580065. Source: UniProt

mitochondrial inner membrane

Inferred from electronic annotation. Source: Ensembl

mitochondrial matrix

Traceable author statement. Source: Reactome

mitochondrion

Inferred from direct assay. Source: HPA

   Molecular_function5S rRNA binding

Inferred from direct assay Ref.10Ref.12. Source: UniProtKB

thiosulfate sulfurtransferase activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 297296Thiosulfate sulfurtransferase
PRO_0000139395

Regions

Domain25 – 143119Rhodanese 1
Domain173 – 288116Rhodanese 2
Region144 – 15916Hinge

Sites

Active site2481Cysteine persulfide intermediate By similarity
Binding site1871Substrate By similarity
Binding site2501Substrate By similarity

Amino acid modifications

Modified residue141N6-acetyllysine; alternate Ref.9
Modified residue141N6-succinyllysine; alternate By similarity
Modified residue1361N6-acetyllysine; alternate By similarity
Modified residue1361N6-succinyllysine; alternate By similarity
Modified residue1631N6-acetyllysine By similarity
Modified residue1751N6-acetyllysine; alternate By similarity
Modified residue1751N6-succinyllysine; alternate By similarity
Modified residue2241N6-acetyllysine; alternate By similarity
Modified residue2241N6-succinyllysine; alternate By similarity
Modified residue2361N6-acetyllysine By similarity
Modified residue2371N6-acetyllysine; alternate By similarity
Modified residue2371N6-succinyllysine; alternate By similarity

Natural variations

Natural variant1021E → D. Ref.3
Corresponds to variant rs35156365 [ dbSNP | Ensembl ].
VAR_051799
Natural variant2281E → G.
Corresponds to variant rs1049270 [ dbSNP | Ensembl ].
VAR_051800

Sequences

Sequence LengthMass (Da)Tools
Q16762 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: BDAE6EE4E47A5650

FASTA29733,429
        10         20         30         40         50         60 
MVHQVLYRAL VSTKWLAESI RTGKLGPGLR VLDASWYSPG TREARKEYLE RHVPGASFFD 

        70         80         90        100        110        120 
IEECRDTASP YEMMLPSEAG FAEYVGRLGI SNHTHVVVYD GEHLGSFYAP RVWWMFRVFG 

       130        140        150        160        170        180 
HRTVSVLNGG FRNWLKEGHP VTSEPSRPEP AVFKATLDRS LLKTYEQVLE NLESKRFQLV 

       190        200        210        220        230        240 
DSRSQGRFLG TEPEPDAVGL DSGHIRGAVN MPFMDFLTED GFEKGPEELR ALFQTKKVDL 

       250        260        270        280        290 
SQPLIATCRK GVTACHVALA AYLCGKPDVA VYDGSWSEWF RRAPPESRVS QGKSEKA 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of human liver rhodanese cDNA."
Aita N., Ishii K., Akamatsu Y., Ogasawara Y., Tanabe S.
Biochem. Biophys. Res. Commun. 231:56-60(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fetal liver.
[2]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASP-102.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[5]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Uterus.
[8]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-8.
Tissue: Platelet.
[9]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Mitochondrial enzyme rhodanese is essential for 5 S ribosomal RNA import into human mitochondria."
Smirnov A., Comte C., Mager-Heckel A.M., Addis V., Krasheninnikov I.A., Martin R.P., Entelis N., Tarassov I.
J. Biol. Chem. 285:30792-30803(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, RNA-BINDING.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Biological significance of 5S rRNA import into human mitochondria: role of ribosomal protein MRP-L18."
Smirnov A., Entelis N., Martin R.P., Tarassov I.
Genes Dev. 25:1289-1305(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, RNA-BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS13938.1.
PIRJC5286.
RefSeqNP_001257412.1. NM_001270483.1.
NP_003303.2. NM_003312.5.
UniGeneHs.474783.

3D structure databases

ProteinModelPortalQ16762.
SMRQ16762. Positions 2-293.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113114. 13 interactions.
IntActQ16762. 2 interactions.
STRING9606.ENSP00000249042.

PTM databases

PhosphoSiteQ16762.

Polymorphism databases

DMDM3122965.

2D gel databases

REPRODUCTION-2DPAGEIPI00216293.

Proteomic databases

MaxQBQ16762.
PaxDbQ16762.
PeptideAtlasQ16762.
PRIDEQ16762.

Protocols and materials databases

DNASU7263.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000249042; ENSP00000249042; ENSG00000128311.
ENST00000403892; ENSP00000385828; ENSG00000128311.
GeneID7263.
KEGGhsa:7263.
UCSCuc003aqg.4. human.

Organism-specific databases

CTD7263.
GeneCardsGC22M037408.
HGNCHGNC:12388. TST.
HPACAB009546.
HPA003044.
HPA003643.
MIM180370. gene.
neXtProtNX_Q16762.
PharmGKBPA37055.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2897.
HOGENOMHOG000157237.
HOVERGENHBG002345.
InParanoidQ16762.
KOK01011.
OMAAPPEYPN.
OrthoDBEOG72ZCGB.
PhylomeDBQ16762.
TreeFamTF315133.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ16762.
BgeeQ16762.
CleanExHS_TST.
GenevestigatorQ16762.

Family and domain databases

Gene3D3.40.250.10. 2 hits.
InterProIPR001763. Rhodanese-like_dom.
IPR001307. Thiosulphate_STrfase_CS.
[Graphical view]
PfamPF00581. Rhodanese. 2 hits.
[Graphical view]
SMARTSM00450. RHOD. 2 hits.
[Graphical view]
SUPFAMSSF52821. SSF52821. 2 hits.
PROSITEPS00380. RHODANESE_1. 1 hit.
PS00683. RHODANESE_2. 1 hit.
PS50206. RHODANESE_3. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiTST_(gene).
GenomeRNAi7263.
NextBio28395.
PROQ16762.
SOURCESearch...

Entry information

Entry nameTHTR_HUMAN
AccessionPrimary (citable) accession number: Q16762
Secondary accession number(s): B3KRM1, Q6IB06
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 128 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM