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Q3BCR4 (TPMT_CHLAE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Thiopurine S-methyltransferase

EC=2.1.1.67
Alternative name(s):
Thiopurine methyltransferase
Gene names
Name:TPMT
OrganismChlorocebus aethiops (Green monkey) (Cercopithecus aethiops)
Taxonomic identifier9534 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeChlorocebus

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
Phosphoprotein
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_0000220098

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 residue141Phosphoserine By similarity
Modified residue581N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3BCR4 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 5905C0A3A98ECB85

FASTA24528,147
        10         20         30         40         50         60 
MDGSRTSLDI EEYSNTEVQK NQVLTLEEWQ DKWVNGKTAF HLEQGHQLLK KHLDTFLKGK 

        70         80         90        100        110        120 
SGLRVFFPLC GKAVEMKWFA NRGHSVVGVE ISELGIREFF TEQNLSYTEE PITEIPGAKV 

       130        140        150        160        170        180 
FKSSSGNISL YCCSIFDFPR TNIGKLDMIW DRGALVAVNP GDRKRYADTM LSLLGKKFQC 

       190        200        210        220        230        240 
LLCVFSYDPT KHPGPPFYVP HAEIERLFGK ICNIHCLEKV DAFEERHKSW GIDYLLEKLY 


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
AY827078 mRNA. Translation: AAX37642.1.

3D structure databases

ProteinModelPortalQ3BCR4.
SMRQ3BCR4. Positions 17-245.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG003037.

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_CHLAE
AccessionPrimary (citable) accession number: Q3BCR4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: November 22, 2005
Last modified: October 19, 2011
This is version 30 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