P25325 (THTM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-mercaptopyruvate sulfurtransferase
Short name=MST
EC=2.8.1.2

Gene names

Name:	MPST
Synonyms:	TST2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	297 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transfer of a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity. May have a role in cyanide degradation or in thiosulfate biosynthesis.
Catalytic activity	3-mercaptopyruvate + cyanide = pyruvate + thiocyanate.
Subunit structure	Monomer or disulfide-linked homodimer By similarity.
Subcellular location	Cytoplasm.
Domain	The structure consists of 2 domains of very similar conformation, suggesting a common evolutionary origin. However, the sequences of the 2 domains are very different.
Sequence similarities	Contains 2 rhodanese domains.
Caution	Was originally (Ref.1) thought to be rhodanese.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Repeat
Molecular function	Transferase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cyanate catabolic process Traceable author statement. Source: ProtInc response to toxin Traceable author statement. Source: ProtInc
Molecular function	3-mercaptopyruvate sulfurtransferase activity Inferred from electronic annotation. Source: EC thiosulfate sulfurtransferase activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 297

296

3-mercaptopyruvate sulfurtransferase

PRO_0000139398

Regions

Domain

25 – 144

120

Rhodanese 1

Domain

174 – 288

115

Rhodanese 2

Region

145 – 160

16

Hinge

Sites

Active site

248

1

Cysteine persulfide intermediate By similarity

Binding site

188

1

Substrate By similarity

Experimental info

Sequence conflict

46 – 48

3

RRE → TQ in CAA42060. Ref.1

Secondary structure

1

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297

Helix Strand Turn

Details...

Helix

13 – 21

9

Beta strand

29 – 33

5

Helix

45 – 51

7

Turn

62 – 64

3

Beta strand

71 – 74

4

Helix

80 – 85

6

Beta strand

96 – 100

5

Helix

110 – 119

10

Beta strand

125 – 128

4

Helix

133 – 137

5

Helix

160 – 162

3

Helix

166 – 175

10

Beta strand

178 – 182

5

Helix

213 – 216

4

Helix

226 – 235

10

Beta strand

244 – 247

4

Helix

255 – 258

4

Helix

276 – 283

8

Sequences

	Sequence		Length	Mass (Da)
	P25325 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 2313CC15A47A42EA	FASTA	297	33,178
	10 20 30 40 50 60 MASPQLCRAL VSAQWVAEAL RAPRAGQPLQ LLDASWYLPK LGRDARREFE ERHIPGAAFF 70 80 90 100 110 120 DIDQCSDRTS PYDHMLPGAE HFAEYAGRLG VGAATHVVIY DASDQGLYSA PRVWWMFRAF 130 140 150 160 170 180 GHHAVSLLDG GLRHWLRQNL PLSSGKSQPA PAEFRAQLDP AFIKTYEDIK ENLESRRFQV 190 200 210 220 230 240 VDSRATGRFR GTEPEPRDGI EPGHIPGTVN IPFTDFLSQE GLEKSPEEIR HLFQEKKVDL 250 260 270 280 290 SKPLVATCGS GVTACHVALG AYLCGKPDVP IYDGSWVEWY MRARPEDVIS EGRGKTH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequence analysis of the human liver rhodanese: comparison with the bovine and chicken enzymes." Pallini R., Guazzi G.C., Cannella C., Cacace M.G. Biochem. Biophys. Res. Commun. 180:887-893(1991) [PubMed: 1953758] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: 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: 15461802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"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. , 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: 10591208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Bone marrow, Muscle and Pancreas.
[6]	Lubec G., Afjehi-Sadat L. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 89-112 AND 119-133, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[7]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]	"Human 3-mercaptopyruvate sulfurtransferase." Structural genomics consortium (SGC) Submitted (SEP-2010) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 11-289.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X59434 mRNA. Translation: CAA42060.1.
CR456523 mRNA. Translation: CAG30409.1.
BT019636 mRNA. Translation: AAV38442.1.
Z73420 Genomic DNA. Translation: CAA97763.1.
BC003508 mRNA. Translation: AAH03508.1.
BC016737 mRNA. Translation: AAH16737.1.
BC018717 mRNA. Translation: AAH18717.1.

IPI

IPI00165360.

PIR

ROHU. JH0461.

RefSeq

NP_001013454.1. NM_001013436.1.
NP_001123989.1. NM_001130517.1.
NP_066949.2. NM_021126.4.

UniGene

Hs.248267.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3OLH	X-ray	2.50	A	11-289	[»]

ProteinModelPortal

P25325.

SMR

P25325. Positions 8-287.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-613N.

IntAct

P25325. 1 interaction.

STRING

P25325.

PTM databases

PhosphoSite

P25325.

Polymorphism databases

DMDM

6226903.

2D gel databases

OGP

P25325.

REPRODUCTION-2DPAGE

IPI00165360.

Proteomic databases

PeptideAtlas

P25325.

PRIDE

P25325.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000341116; ENSP00000342333; ENSG00000128309.
ENST00000397129; ENSP00000380318; ENSG00000128309.
ENST00000397225; ENSP00000380402; ENSG00000128309.
ENST00000401419; ENSP00000384812; ENSG00000128309.
ENST00000404802; ENSP00000383950; ENSG00000128309.
ENST00000429360; ENSP00000411719; ENSG00000128309.
ENST00000452571; ENSP00000391921; ENSG00000128309.

GeneID

4357.

KEGG

hsa:4357.

UCSC

uc003aqj.1. human.

Organism-specific databases

CTD

4357.

GeneCards

GC22P037415.

H-InvDB

HIX0016434.

HGNC

HGNC:7223. MPST.

HPA

HPA001240.

MIM

602496. gene.

neXtProt

NX_P25325.

Orphanet

1035. Encephalopathy due to beta-mercaptolactate-cysteine disulfiduria.

PharmGKB

PA30928.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HBG709927.

HOVERGEN

HBG002345.

OrthoDB

EOG466VMJ.

PhylomeDB

P25325.

Gene expression databases

ArrayExpress

P25325.

Bgee

P25325.

CleanEx

HS_MPST.

Genevestigator

P25325.

GermOnline

ENSG00000128309. Homo sapiens.

Family and domain databases

InterPro

IPR001763. Rhodanese-like.
IPR001307. Thiosulphate_STrfase_CS.
[Graphical view]

Gene3D

G3DSA:3.40.250.10. Rhodanese-like. 2 hits.

KO

K01011.

Pfam

PF00581. Rhodanese. 2 hits.
[Graphical view]

SMART

SM00450. RHOD. 2 hits.
[Graphical view]

SUPFAM

SSF52821. Rhodanese-like. 2 hits.

PROSITE

PS00380. RHODANESE_1. 1 hit.
PS00683. RHODANESE_2. 1 hit.
PS50206. RHODANESE_3. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

NextBio

17143.

SOURCE

Search...

Entry information

Entry name

THTM_HUMAN

Accession

Primary (citable) accession number: P25325
Secondary accession number(s): O75750

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 111 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.