Q504A5 (TPMT_DANRE) Reviewed, UniProtKB/Swiss-Prot
Last modified
October 19, 2011.
Version 40.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Probable thiopurine S-methyltransferase Short name=Thiopurine methyltransferase EC=2.1.1.67 | ||||
| Gene names |
| ||||
| Organism | Danio rerio (Zebrafish) (Brachydanio rerio) | ||||
| Taxonomic identifier | 7955 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Ostariophysi › Cypriniformes › Cyprinidae › Danio |
Protein attributes
| Sequence length | 232 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Catalyzes the S-methylation of thiopurine drugs such as 6-mercaptopurine By similarity. |
| Catalytic activity | S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the methyltransferase superfamily. TPMT family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | S-adenosyl-L-methionine |
| Molecular function | Methyltransferase Transferase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| 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 – 232 | 232 | Probable thiopurine S-methyltransferase | PRO_0000284920 | |||||
Sites | |||||||||
| Binding site | 18 | 1 | S-adenosyl-L-methionine By similarity | ||||||
| Binding site | 54 | 1 | S-adenosyl-L-methionine; via carbonyl oxygen By similarity | ||||||
| Binding site | 75 | 1 | S-adenosyl-L-methionine By similarity | ||||||
| Binding site | 137 | 1 | S-adenosyl-L-methionine By similarity | ||||||
Sequences
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References
| [1] | NIH - Zebrafish Gene Collection (ZGC) project Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Eye. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BC095104 mRNA. Translation: AAH95104.1. |
| IPI | IPI00607312. |
| UniGene | Dr.85410. |
3D structure databases | |
| HSSP | HSSP built from PDB template 2BZG based on UniProtKB O43213. |
| ProteinModelPortal | Q504A5. |
| SMR | Q504A5. Positions 3-230. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q504A5. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Organism-specific databases | |
| ZFIN | ZDB-GENE-050522-141. zgc:109981. |
Phylogenomic databases | |
| eggNOG | fiNOG06887. |
| HOGENOM | HBG444929. |
| HOVERGEN | HBG003037. |
| InParanoid | Q504A5. |
| OrthoDB | EOG4C5CKF. |
Family and domain databases | |
| InterPro | IPR008854. Thiopurine_S-MeTrfase. IPR016822. Thiopurine_S-MeTrfase_sub. [Graphical view] |
| PANTHER | PTHR10259. PTHR10259. 1 hit. |
| Pfam | PF05724. TPMT. 1 hit. [Graphical view] |
| PIRSF | PIRSF023956. Thiopurine_S-methyltransferase. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | TPMT_DANRE | ||||||||
| Accession | Primary (citable) accession number: Q504A5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with