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Q3BCQ8 (TPMT_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thiopurine S-methyltransferase

EC=2.1.1.67
Alternative name(s):
Thiopurine methyltransferase
Gene names
Name:TPMT
OrganismOryctolagus cuniculus (Rabbit) [Complete proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length245 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Cytoplasm.

Sequence similarities

Belongs to the methyltransferase superfamily. TPMT family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionthiopurine S-methyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 245245Thiopurine S-methyltransferase
PRO_0000220112

Sites

Binding site331S-adenosyl-L-methionine By similarity
Binding site691S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site901S-adenosyl-L-methionine By similarity
Binding site1521S-adenosyl-L-methionine By similarity

Amino acid modifications

Modified residue581N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3BCQ8 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: C3973A3E662AD044

FASTA24528,283
        10         20         30         40         50         60 
MDDARTLLDI KEYPDTEVQK NRVLTLEEWQ DKWVSHKIGF HQEQGHKLLK KHLDAFLKGE 

        70         80         90        100        110        120 
SGLRVFFPLC GKAVEMKWFA DRGHSVVGVE ISELGIREFF SEQNLSYSEE PITEVPGAKV 

       130        140        150        160        170        180 
FKSSAGNISL YCCSIFDLPR VNIGKFDRIW DRGALVAVNP SDRKRYAAVM LSLLRKGFQY 

       190        200        210        220        230        240 
LLAVLSYDPT KHAGPPFYVP DAEIKMLFDT KCKIHCLEKV DAFEERHKSW GIDYIFEKLY 


LLTEK 

« Hide

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

EMBL
GenBank
DDBJ
AY827084 mRNA. Translation: AAX37648.1.
RefSeqNP_001076153.1. NM_001082684.1.
UniGeneOcu.3344.

3D structure databases

ProteinModelPortalQ3BCQ8.
SMRQ3BCQ8. Positions 14-245.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3BCQ8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100009411.

Organism-specific databases

CTD7172.

Phylogenomic databases

eggNOGmaNOG10315.
GeneTreeENSGT00390000016823.
HOVERGENHBG003037.
OrthoDBEOG4C5CKF.

Family and domain databases

InterProIPR008854. Thiopurine_S-MeTrfase.
IPR016822. Thiopurine_S-MeTrfase_sub.
[Graphical view]
PANTHERPTHR10259. PTHR10259. 1 hit.
PfamPF05724. TPMT. 1 hit.
[Graphical view]
PIRSFPIRSF023956. Thiopurine_S-methyltransferase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTPMT_RABIT
AccessionPrimary (citable) accession number: Q3BCQ8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: November 22, 2005
Last modified: November 16, 2011
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families