Reviewed,
UniProtKB/Swiss-Prot Q9Z0T0 (TPMT_RAT)
Last modified
June 16, 2009.
Version 51.
History...
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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 | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 240 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 | S-adenosylhomocysteine metabolic process Inferred from direct assay. Source: RGD S-adenosylmethionine metabolic processInferred from direct assay. Source: RGD |
| Cellular component | cytosol Inferred from direct assay. Source: RGD tight junctionNon-traceable author statement. Source: RGD |
| Molecular function | thiopurine S-methyltransferase activity Inferred from direct assay. Source: RGD |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 240 | 240 | Thiopurine S-methyltransferase | PRO_0000220113 | |||||
Sites | |||||||||
| Binding site | 28 | 1 | S-adenosyl-L-methionine By similarity | ||||||
| Binding site | 64 | 1 | S-adenosyl-L-methionine; via carbonyl oxygen By similarity | ||||||
| Binding site | 85 | 1 | S-adenosyl-L-methionine By similarity | ||||||
| Binding site | 147 | 1 | S-adenosyl-L-methionine By similarity | ||||||
Sequences
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References
| [1] | Krynetski E.Y., Fessing M.Y., Evans W.E. Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. |
Cross-references
Sequence databases | |
|---|---|
| AF120100 mRNA. Translation: AAD17293.1. | |
| IPI | IPI00208135. |
| RefSeq | XP_001058187.1. |
| UniGene | Rn.112598 |
3D structure databases | |
| SMR | Q9Z0T0. Positions 10-240. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | Q9Z0T0. |
Genome annotation databases | |
| GeneID | 681730. |
| KEGG | rno:681730. |
Organism-specific databases | |
| RGD | 620089. Tpmt. |
Phylogenomic databases | |
| HOVERGEN | Q9Z0T0. |
Enzyme and pathway databases | |
| BRENDA | 2.1.1.67. 248. |
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... |
Other Resources | |
| NextBio | 721509. |
Entry information
| Entry name | TPMT_RAT | ||||||||
| Accession | Primary (citable) accession number: Q9Z0T0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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