Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O55060 (TPMT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length240 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the S-methylation of thiopurine drugs such as 6-mercaptopurine. HAMAP-Rule MF_00812

Catalytic activity

S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether. HAMAP-Rule MF_00812

Subunit structure

Monomer. Ref.5

Subcellular location

Cytoplasm HAMAP-Rule MF_00812.

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. TPMT family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processresponse to testosterone

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionthiopurine S-methyltransferase activity

Inferred from direct assay Ref.1. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 240240Thiopurine S-methyltransferase HAMAP-Rule MF_00812
PRO_0000220105

Regions

Region24 – 3512S-adenosyl-L-methionine binding HAMAP-Rule MF_00812
Region129 – 1302S-adenosyl-L-methionine binding HAMAP-Rule MF_00812

Sites

Binding site351Substrate
Binding site641S-adenosyl-L-methionine; via carbonyl oxygen
Binding site851S-adenosyl-L-methionine
Binding site1471S-adenosyl-L-methionine

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 [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] [Europe PMC] [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] [Europe PMC] [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.
[5]"Structural basis of substrate recognition in thiopurine s-methyltransferase."
Peng Y., Feng Q., Wilk D., Adjei A.A., Salavaggione O.E., Weinshilboum R.M., Yee V.C.
Biochemistry 47:6216-6225(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH S-ADENOSYL-L-HOMOCYSTEINE AND 6-MERCAPTOPURINE, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
AH009424 Genomic DNA. Translation: AAF74424.1.
RefSeqNP_058065.2. NM_016785.2.
XP_006516989.1. XM_006516926.1.
UniGeneMm.10169.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GB4X-ray1.25A/B1-240[»]
3BGDX-ray2.00A/B1-240[»]
3BGIX-ray1.80A/B1-240[»]
ProteinModelPortalO55060.
SMRO55060. Positions 10-240.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO55060. 2 interactions.
MINTMINT-1855972.

PTM databases

PhosphoSiteO55060.

Proteomic databases

PaxDbO55060.
PRIDEO55060.

Protocols and materials databases

DNASU22017.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021806; ENSMUSP00000021806; ENSMUSG00000021376.
GeneID22017.
KEGGmmu:22017.
UCSCuc007qhq.2. mouse.

Organism-specific databases

CTD7172.
MGIMGI:98812. Tpmt.

Phylogenomic databases

eggNOGCOG0500.
GeneTreeENSGT00390000016823.
HOGENOMHOG000276919.
HOVERGENHBG003037.
InParanoidO55060.
KOK00569.
OrthoDBEOG7H4DWQ.
TreeFamTF328951.

Gene expression databases

ArrayExpressO55060.
BgeeO55060.
CleanExMM_TPMT.
GenevestigatorO55060.

Family and domain databases

HAMAPMF_00812. Thiopur_methtran.
InterProIPR025835. Thiopurine_S-MeTrfase.
IPR008854. TPMT.
[Graphical view]
PfamPF05724. TPMT. 1 hit.
[Graphical view]
PIRSFPIRSF023956. Thiopurine_S-methyltransferase. 1 hit.
PROSITEPS51585. SAM_MT_TPMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO55060.
NextBio301740.
PROO55060.
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: March 19, 2014
This is version 108 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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