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Reviewed, UniProtKB/Swiss-Prot O55060 (TPMT_MOUSE)

Last modified October 13, 2009. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Thiopurine S-methyltransferase
    EC=2.1.1.67
Alternative name(s):
    Thiopurine methyltransferase
Gene names
Name: Tpmt
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length240 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein 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 term3D-structure
Gene Ontology (GO)
   Molecular functionthiopurine S-methyltransferase activity Ref.1

Inferred from direct assay. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 240240Thiopurine S-methyltransferase
PRO_0000220105

Sites

Binding site281S-adenosyl-L-methionine By similarity
Binding site641S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site851S-adenosyl-L-methionine By similarity
Binding site1471S-adenosyl-L-methionine By similarity

Amino acid modifications

Modified residue531N6-acetyllysine By similarity

Natural variations

Natural variant691I → V in strain: C57BL/6J.

Secondary structure

......................................... 240
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O55060-1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 2BA57F30E8EB72D2

FASTA24027,586
        10         20         30         40         50         60 
MSLDMKEHPD AEVQKNQVLT LEDWKEKWVT RHISFHQEQG HQLLKKHLDT FLKGQSGLRV 

        70         80         90        100        110        120 
FFPLCGKAIE MKWFADRGHT VVGVEISEIG IREFFAEQNL SYTEEPLAEI AGAKVFKSSS 

       130        140        150        160        170        180 
GSISLYCCSI FDLPRANIGK FDRIWDRGAL VAINPGDHDR YADIILSLLR KEFQYLVAVL 

       190        200        210        220        230        240 
SYDPTKHAGP PFYVPSAELK RLFGTKCSMQ CLEEVDALEE RHKAWGLDYL FEKLYLLTEK 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and functional characterization of the cDNA encoding the murine thiopurine S-methyltransferase (TPMT)."
Fessing M.Y., Belkov V.M., Krynetski E.Y., Evans W.E.
FEBS Lett. 424:143-145(1998) [PubMed: 9539138] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C3H.
[2]"Mouse thiopurine methyltransferase pharmacogenetics: cDNA cloning and characterization and processed pseudogene cloning."
Adjei A.A., Johnson G.B., Otterness D.M., Weinshilboum R.M.
Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: C57BL/6J and DBA/2J.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Liver.
[4]Krynetski E.Y., Fessing M.Y., Edick M.J., Evans W.E.
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE OF 43-227.
Strain: 129/Ola.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF046887 mRNA. Translation: AAC25919.1.
AF037043 mRNA. Translation: AAD02092.1.
AF037044 mRNA. Translation: AAD02093.1.
AF104832 expand/collapse EMBL AC list , AF104825, AF104826, AF104827, AF104828, AF104829, AF104830, AF104831 Genomic DNA. Translation: AAF06075.1.
BC021598 mRNA. Translation: AAH21598.1.
AF218593 expand/collapse EMBL AC list , AF218588, AF218589, AF218590, AF218591, AF218592 Genomic DNA. Translation: AAF74424.1.
IPIIPI00115215.
RefSeqNP_058065.2.
UniGeneMm.10169

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2GB4X-ray1.25A/B1-240[»]
3BGDX-ray2.00A/B1-240[»]
3BGIX-ray1.80A/B1-240[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGO55060.

PTM databases

PhosphoSiteO55060.

Proteomic databases

PRIDEO55060.

Genome annotation databases

EnsemblENSMUST00000021806; ENSMUSP00000021806; ENSMUSG00000021376; Mus musculus. [Genome view]
GeneID22017.
UCSCuc007qhq.1. mouse.

Organism-specific databases

CTD22017.
MGIMGI:98812. Tpmt.

Phylogenomic databases

HOGENOMO55060.
HOVERGENO55060.

Enzyme and pathway databases

BRENDA2.1.1.67. 244.

Gene expression databases

ArrayExpressO55060.
BgeeO55060.
CleanExMM_TPMT.
GenevestigatorO55060.
GermOnlineENSMUSG00000021376. Mus musculus.

Family and domain databases

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

Other Resources

NextBio301740.
SOURCESearch...

Entry information

Entry nameTPMT_MOUSE
AccessionPrimary (citable) accession number: O55060
Secondary accession number(s): Q9JIL7, Q9QUG7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 1, 1998
Last modified: October 13, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents