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Reviewed, UniProtKB/Swiss-Prot Q9Z0T0 (TPMT_RAT)

Last modified June 16, 2009. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length240 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 240240Thiopurine S-methyltransferase
PRO_0000220113

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

Sequences

Sequence LengthMass (Da)Tools
Q9Z0T0-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 04608B546BBDC1E3

FASTA24027,692
        10         20         30         40         50         60 
MSLGIKEHPD AEVQKNRVLT LDDWQDKWVT RHIAFHQEQG HQLLKKHFDT FLKGQSGLRV 

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

       130        140        150        160        170        180 
GNISLYCCSI FDLPRANIGK FDRIWDRGAL VAVNPGDRDR YADIILSLLR KGYHYLLVVL 

       190        200        210        220        230        240 
SYDPTKHTGP PFYVPDAELK KLFGTKCNMQ CLEEVDALEE RHKTWGVDYF FEKLYLLTEK 

« Hide

References

[1]Krynetski E.Y., Fessing M.Y., Evans W.E.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.

Cross-references

Sequence databases

AF120100 mRNA. Translation: AAD17293.1.
IPIIPI00208135.
RefSeqXP_001058187.1.
UniGeneRn.112598

3D structure databases

SMRQ9Z0T0. Positions 10-240.
ModBaseSearch...

Proteomic databases

PRIDEQ9Z0T0.

Genome annotation databases

GeneID681730.
KEGGrno:681730.

Organism-specific databases

RGD620089. Tpmt.

Phylogenomic databases

HOVERGENQ9Z0T0.

Enzyme and pathway databases

BRENDA2.1.1.67. 248.

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

NextBio721509.

Entry information

Entry nameTPMT_RAT
AccessionPrimary (citable) accession number: Q9Z0T0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: May 1, 1999
Last modified: June 16, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

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