MPST
3-mercaptopyruvate sulfurtransferase
Also known as: MST, THTM_HUMAN, TST2, TUM1
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P25325
- Gene
- MPST
- Ensembl
- ENSG00000128309
- Chromosome
- 22
- Canonical length
- 297 aa
- Protein class
- Disease related genes, Enzymes, Metabolic proteins, Plasma proteins, Potential drug targets, Predicted intracellular proteins
- Subcellular location
- Mitochondria,Cytosol
- Quaternary structure
- Homodimer
OverviewNCBI Gene
This protein encoded by this gene catalyzes the transfer of a sulfur ion from 3-mercaptopyruvate to cyanide or other thiol compounds. It may be involved in cysteine degradation and cyanide detoxification. There is confusion in literature between this protein (mercaptopyruvate sulfurtransferase, MPST), which appears to be cytoplasmic, and thiosulfate sulfurtransferase (rhodanese, TST, GeneID:7263), which is a mitochondrial protein. Deficiency in MPST activity has been implicated in a rare inheritable disorder known as mercaptolactate-cysteine disulfiduria (MCDU). Alternatively spliced transcript variants encoding same or different isoforms have been identified for this gene. [provided by RefSeq, Jul 2008]
Canonical amino-acid sequenceUniProt
297 residues, UniProt reviewed canonical sequence.
>P25325|MPST
1 MASPQLCRAL VSAQWVAEAL RAPRAGQPLQ LLDASWYLPK LGRDARREFE ERHIPGAAFF
61 DIDQCSDRTS PYDHMLPGAE HFAEYAGRLG VGAATHVVIY DASDQGLYSA PRVWWMFRAF
121 GHHAVSLLDG GLRHWLRQNL PLSSGKSQPA PAEFRAQLDP AFIKTYEDIK ENLESRRFQV
181 VDSRATGRFR GTEPEPRDGI EPGHIPGTVN IPFTDFLSQE GLEKSPEEIR HLFQEKKVDL
241 SKPLVATCGS GVTACHVALG AYLCGKPDVP IYDGSWVEWY MRARPEDVIS EGRGKTHLocalizationUniProt · AlphaFold · HPA
Whether an antibody against MPST can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Intracellular
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.25
- Highest tissue expression
- 371 nTPM
Expression across tissuesHPA
Tissue
- liver: 371 nTPM
- pancreas: 101 nTPM
- duodenum: 100 nTPM
- colon: 96 nTPM
- small intestine: 88 nTPM
- esophagus: 87 nTPM
Single-cell type
- enterocytes: 1,170 nCPM
- esophageal apical cells: 675 nCPM
- hepatocytes: 650 nCPM
- colonocytes: 517 nCPM
- enteric transient amplifying cells: 380 nCPM
- esophageal suprabasal cells: 348 nCPM
Immune cell
- myeloid DC: 104 nTPM
- NK-cell: 88 nTPM
- classical monocyte: 72 nTPM
- eosinophil: 55 nTPM
- basophil: 49 nTPM
- T-reg: 44 nTPM
Brain region
- white matter: 55 nTPM
- medulla oblongata: 53 nTPM
- basal ganglia: 49 nTPM
- thalamus: 47 nTPM
- choroid plexus: 45 nTPM
- cerebellum: 43 nTPM
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 1.34
- gnomAD pLI
- 0
- gnomAD missense Z
- 1.21
- DepMap mean gene effect
- -0.02
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- cyanate catabolic process
- hydrogen sulfide biosynthetic process
- kidney development
- liver development
- response to toxic substance
- spinal cord development
- sulfur amino acid catabolic process
- transsulfuration
Molecular functions
- 3-mercaptopyruvate sulfurtransferase activity
- identical protein binding
- sulfurtransferase activity
- thiosulfate-cyanide sulfurtransferase activity
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads MPST as an antibody target. Whether an autoantibody or antibody against MPST could matter depends on whether native MPST is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
MPST is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.
Annotation status
The present source text does not explicitly label MPST as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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