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Reviewed, UniProtKB/Swiss-Prot Q17QQ2 (TPMT_BOVIN)

Last modified November 3, 2009. Version 31. 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
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length245 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 By similarity.

Catalytic activity

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

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the methyltransferase superfamily. TPMT family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   PTMAcetylation
Gene Ontology (GO)
   Biological processmetabolic process

Inferred from electronic annotation. Source: InterPro

   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_0000278660

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
Q17QQ2-1 [UniParc].

Last modified July 25, 2006. Version 1.
Checksum: C734333BEEC2828F

FASTA24528,335
        10         20         30         40         50         60 
MGDSRALLDS EEYPNTEAQK DRVLTLEEWQ EKWVNHKTGF HQEQGHQLLK KYLDTFLKGE 

        70         80         90        100        110        120 
KALRVFFPLC GKAVEMKWFA DRGHSVVGVE ISELGIRDFF TEQNLSYSEE PIMEIPGAKI 

       130        140        150        160        170        180 
FKSSSGNISL YCCNLFDLPR ANIGKFDRIW DRGALVAVNP SDRKRYSDVM LSLTRPGFRY 

       190        200        210        220        230        240 
LLSVFSYDPT KHAGPPFYVT DGEVKKLFGS VCNIQCLEKV DVFEERHKSW GIDQIIERLY 


LFTEK 

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Basal ganglia.

Cross-references

Sequence databases

BC118238 mRNA. Translation: AAI18239.1.
IPIIPI00705007.
RefSeqNP_001068999.1.
UniGeneBt.15903

3D structure databases

SMRQ17QQ2. Positions 17-245.
ModBaseSearch...

Genome annotation databases

EnsemblENSBTAT00000025698; ENSBTAP00000025698; ENSBTAG00000019300; Bos taurus. [Genome view]
GeneID511644.
KEGGbta:511644.

Organism-specific databases

CTD511644.

Phylogenomic databases

HOVERGENQ17QQ2.
OMAPPFAVSP.

Enzyme and pathway databases

BRENDA2.1.1.67. 251.

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...

Entry information

Entry nameTPMT_BOVIN
AccessionPrimary (citable) accession number: Q17QQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: July 25, 2006
Last modified: November 3, 2009
This is version 31 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