Version 5.4
Homo sapiens Protein: TPMT
Summary
InnateDB Protein IDBP-63866.5
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol TPMT
Protein Name thiopurine S-methyltransferase
Synonyms
Species Homo sapiens
Ensembl Protein ENSP00000312304
InnateDB Gene IDBG-63864 (TPMT)
Protein Structure
UniProt Annotation
Function Catalyzes the S-methylation of thiopurine drugs such as 6-mercaptopurine. {ECO:0000269PubMed:18484748}.
Subcellular Localization Cytoplasm.
Disease Associations Thiopurine S-methyltransferase deficiency (TPMT deficiency) [MIM:610460]: Enzyme involved in the normal metabolic inactivation of thiopurine drugs. These drugs are generally used as immunosuppressants or cytotoxic drugs and are prescribed for a variety of clinical conditions including leukemia, autoimmune disease and organ transplantation. Patients with intermediate or no TPMT activity are at risk of toxicity after receiving standard doses of thiopurine drugs and it is shown that inter-individual differences in response to these drugs are largely determined by genetic variation at the TPMT locus. {ECO:0000269PubMed:10208641, ECO:0000269PubMed:10751626, ECO:0000269PubMed:15819814, ECO:0000269PubMed:16220112, ECO:0000269PubMed:16476125, ECO:0000269PubMed:16789994, ECO:0000269PubMed:7862671, ECO:0000269PubMed:8561894, ECO:0000269PubMed:8644731, ECO:0000269PubMed:9246020, ECO:0000269PubMed:9336428, ECO:0000269PubMed:9711875, ECO:0000269PubMed:9931345, ECO:0000269PubMed:9931346}. Note=The disease is caused by mutations affecting the gene represented in this entry.
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 3 experimentally validated interaction(s) in this database.
Experimentally validated
Total 3 [view]
Protein-Protein 2 [view]
Protein-DNA 1 [view]
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0008119 thiopurine S-methyltransferase activity
GO:0008757 S-adenosylmethionine-dependent methyltransferase activity
Biological Process
GO:0006139 nucleobase-containing compound metabolic process
GO:0006805 xenobiotic metabolic process
GO:0032259 methylation
GO:0044281 small molecule metabolic process
Cellular Component
GO:0005829 cytosol
GO:0070062 extracellular vesicular exosome
Protein Structure and Domains
PDB ID
InterPro IPR008854 TPMT family
IPR025835 Thiopurine S-methyltransferase
IPR029063 S-adenosyl-L-methionine-dependent methyltransferase-like
PFAM PF05724
PRINTS
PIRSF PIRSF023956
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt P51580
PhosphoSite PhosphoSite-P51580
TrEMBL A0A024QZW0
UniProt Splice Variant
Entrez Gene 7172
UniGene Hs.660747
RefSeq NP_000358
HUGO HGNC:12014
OMIM 187680
CCDS CCDS4543
HPRD 01760
IMGT
EMBL AB045146 AF019364 AF019365 AF019366 AF019367 AF019368 AF019369 AF021876 AF021877 AF035426 AL589723 BC009596 CH471087 S62904 U12387 U30512 U30513 U30514 U30515 U30516 U30517 U30518 U81562 U81563 U81564 U81565 U81566 U81567 U81568 U81569 U81570 U81571 U81572 U81573
GenPept AAB27277 AAB71625 AAB71626 AAB71627 AAB71628 AAB71629 AAB71630 AAB71631 AAB71632 AAB71633 AAB71634 AAB71635 AAB71636 AAB80746 AAB80747 AAC32289 AAC50130 AAC50368 AAC51865 AAH09596 BAA97037 CAH71233 EAW55396 EAW55397

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca