Reviewed,
UniProtKB/Swiss-Prot Q3BCQ8 (TPMT_RABIT)
Last modified
June 16, 2009.
Version 24.
History...
Clusters with 100%,
90%,
50% identity |
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Thiopurine S-methyltransferase EC=2.1.1.67 Alternative name(s): Thiopurine methyltransferase | ||
| Gene names |
| ||
| Organism | Oryctolagus cuniculus (Rabbit) | ||
| Taxonomic identifier | 9986 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus |
Protein attributes
| Sequence length | 245 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Catalyzes the S-methylation of thiopurine drugs such as 6-mercaptopurine. |
| Catalytic activity | S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether. |
| Subunit structure | Monomer By similarity. |
| Subcellular location | |
| Sequence similarities | Belongs to the methyltransferase superfamily. TPMT family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | S-adenosyl-L-methionine |
| Molecular function | Methyltransferase Transferase |
| Gene Ontology (GO) | |
| Biological process | metabolic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | thiopurine S-methyltransferase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 245 | 245 | Thiopurine S-methyltransferase | PRO_0000220112 | |||||
Sites | |||||||||
| Binding site | 33 | 1 | S-adenosyl-L-methionine By similarity | ||||||
| Binding site | 69 | 1 | S-adenosyl-L-methionine; via carbonyl oxygen By similarity | ||||||
| Binding site | 90 | 1 | S-adenosyl-L-methionine By similarity | ||||||
| Binding site | 152 | 1 | S-adenosyl-L-methionine By similarity | ||||||
Sequences
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References
| [1] | "Thiopurine S-methyltransferase pharmacogenetics: variant allele functional and comparative genomics." Salavaggione O.E., Wang L., Wiepert M., Yee V.C., Weinshilboum R.M. Pharmacogenet. Genomics 15:801-815(2005) [PubMed: 16220112] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
Cross-references
Sequence databases | |
|---|---|
| AY827084 mRNA. Translation: AAX37648.1. | |
| RefSeq | NP_001076153.1. |
| UniGene | Ocu.3344 |
3D structure databases | |
| SMR | Q3BCQ8. Positions 17-245. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 100009411. |
Phylogenomic databases | |
| HOVERGEN | Q3BCQ8. |
Enzyme and pathway databases | |
| BRENDA | 2.1.1.67. 255. |
Family and domain databases | |
| InterPro | IPR008854. Thiopurine_S-MeTrfase. IPR016822. Thiopurine_S-MeTrfase_sub. [Graphical view] |
| Pfam | PF05724. TPMT. 1 hit. [Graphical view] |
| PIRSF | PIRSF023956. Thiopurine_S-methyltransferase. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | TPMT_RABIT | ||||||||
| Accession | Primary (citable) accession number: Q3BCQ8 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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