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O55060

- TPMT_MOUSE

UniProt

O55060 - TPMT_MOUSE

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Protein
Thiopurine S-methyltransferase
Gene
Tpmt
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the S-methylation of thiopurine drugs such as 6-mercaptopurine.UniRule annotation

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei35 – 351Substrate
Binding sitei64 – 641S-adenosyl-L-methionine; via carbonyl oxygen
Binding sitei85 – 851S-adenosyl-L-methionine
Binding sitei147 – 1471S-adenosyl-L-methionine

GO - Molecular functioni

  1. thiopurine S-methyltransferase activity Source: MGI

GO - Biological processi

  1. response to testosterone Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Thiopurine S-methyltransferase (EC:2.1.1.67)
Alternative name(s):
Thiopurine methyltransferase
Gene namesi
Name:Tpmt
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:98812. Tpmt.

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 240240Thiopurine S-methyltransferaseUniRule annotation
PRO_0000220105Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 531N6-acetyllysine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO55060.
PaxDbiO55060.
PRIDEiO55060.

PTM databases

PhosphoSiteiO55060.

Expressioni

Gene expression databases

ArrayExpressiO55060.
BgeeiO55060.
CleanExiMM_TPMT.
GenevestigatoriO55060.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

IntActiO55060. 2 interactions.
MINTiMINT-1855972.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni11 – 166
Helixi21 – 3010
Beta strandi38 – 403
Helixi42 – 5211
Beta strandi59 – 624
Helixi70 – 767
Beta strandi80 – 845
Helixi88 – 9710
Beta strandi102 – 1065
Beta strandi114 – 1185
Beta strandi121 – 1288
Turni130 – 1323
Helixi133 – 1364
Beta strandi141 – 1499
Turni150 – 1523
Helixi155 – 1573
Helixi158 – 16710
Beta strandi169 – 18113
Helixi184 – 1863
Beta strandi189 – 1913
Helixi196 – 2038
Turni204 – 2063
Beta strandi207 – 21610
Helixi220 – 2223
Turni223 – 2264
Beta strandi231 – 2399

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GB4X-ray1.25A/B1-240[»]
3BGDX-ray2.00A/B1-240[»]
3BGIX-ray1.80A/B1-240[»]
ProteinModelPortaliO55060.
SMRiO55060. Positions 10-240.

Miscellaneous databases

EvolutionaryTraceiO55060.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni24 – 3512S-adenosyl-L-methionine bindingUniRule annotation
Add
BLAST
Regioni129 – 1302S-adenosyl-L-methionine bindingUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0500.
GeneTreeiENSGT00390000016823.
HOGENOMiHOG000276919.
HOVERGENiHBG003037.
InParanoidiO55060.
KOiK00569.
OrthoDBiEOG7H4DWQ.
PhylomeDBiO55060.
TreeFamiTF328951.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_00812. Thiopur_methtran.
InterProiIPR029063. SAM-dependent_MTases-like.
IPR025835. Thiopurine_S-MeTrfase.
IPR008854. TPMT.
[Graphical view]
PfamiPF05724. TPMT. 1 hit.
[Graphical view]
PIRSFiPIRSF023956. Thiopurine_S-methyltransferase. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51585. SAM_MT_TPMT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O55060-1 [UniParc]FASTAAdd to Basket

« Hide

MSLDMKEHPD AEVQKNQVLT LEDWKEKWVT RHISFHQEQG HQLLKKHLDT    50
FLKGQSGLRV FFPLCGKAIE MKWFADRGHT VVGVEISEIG IREFFAEQNL 100
SYTEEPLAEI AGAKVFKSSS GSISLYCCSI FDLPRANIGK FDRIWDRGAL 150
VAINPGDHDR YADIILSLLR KEFQYLVAVL SYDPTKHAGP PFYVPSAELK 200
RLFGTKCSMQ CLEEVDALEE RHKAWGLDYL FEKLYLLTEK 240
Length:240
Mass (Da):27,586
Last modified:June 1, 1998 - v1
Checksum:i2BA57F30E8EB72D2
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti69 – 691I → V in strain: C57BL/6J.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF046887 mRNA. Translation: AAC25919.1.
AF037043 mRNA. Translation: AAD02092.1.
AF037044 mRNA. Translation: AAD02093.1.
AF104832
, AF104825, AF104826, AF104827, AF104828, AF104829, AF104830, AF104831 Genomic DNA. Translation: AAF06075.1.
BC021598 mRNA. Translation: AAH21598.1.
AH009424 Genomic DNA. Translation: AAF74424.1.
CCDSiCCDS26488.1.
RefSeqiNP_058065.2. NM_016785.2.
XP_006516989.1. XM_006516926.1.
UniGeneiMm.10169.

Genome annotation databases

EnsembliENSMUST00000021806; ENSMUSP00000021806; ENSMUSG00000021376.
GeneIDi22017.
KEGGimmu:22017.
UCSCiuc007qhq.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF046887 mRNA. Translation: AAC25919.1 .
AF037043 mRNA. Translation: AAD02092.1 .
AF037044 mRNA. Translation: AAD02093.1 .
AF104832
, AF104825 , AF104826 , AF104827 , AF104828 , AF104829 , AF104830 , AF104831 Genomic DNA. Translation: AAF06075.1 .
BC021598 mRNA. Translation: AAH21598.1 .
AH009424 Genomic DNA. Translation: AAF74424.1 .
CCDSi CCDS26488.1.
RefSeqi NP_058065.2. NM_016785.2.
XP_006516989.1. XM_006516926.1.
UniGenei Mm.10169.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2GB4 X-ray 1.25 A/B 1-240 [» ]
3BGD X-ray 2.00 A/B 1-240 [» ]
3BGI X-ray 1.80 A/B 1-240 [» ]
ProteinModelPortali O55060.
SMRi O55060. Positions 10-240.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O55060. 2 interactions.
MINTi MINT-1855972.

PTM databases

PhosphoSitei O55060.

Proteomic databases

MaxQBi O55060.
PaxDbi O55060.
PRIDEi O55060.

Protocols and materials databases

DNASUi 22017.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000021806 ; ENSMUSP00000021806 ; ENSMUSG00000021376 .
GeneIDi 22017.
KEGGi mmu:22017.
UCSCi uc007qhq.2. mouse.

Organism-specific databases

CTDi 7172.
MGIi MGI:98812. Tpmt.

Phylogenomic databases

eggNOGi COG0500.
GeneTreei ENSGT00390000016823.
HOGENOMi HOG000276919.
HOVERGENi HBG003037.
InParanoidi O55060.
KOi K00569.
OrthoDBi EOG7H4DWQ.
PhylomeDBi O55060.
TreeFami TF328951.

Miscellaneous databases

EvolutionaryTracei O55060.
NextBioi 301740.
PROi O55060.
SOURCEi Search...

Gene expression databases

ArrayExpressi O55060.
Bgeei O55060.
CleanExi MM_TPMT.
Genevestigatori O55060.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
HAMAPi MF_00812. Thiopur_methtran.
InterProi IPR029063. SAM-dependent_MTases-like.
IPR025835. Thiopurine_S-MeTrfase.
IPR008854. TPMT.
[Graphical view ]
Pfami PF05724. TPMT. 1 hit.
[Graphical view ]
PIRSFi PIRSF023956. Thiopurine_S-methyltransferase. 1 hit.
SUPFAMi SSF53335. SSF53335. 1 hit.
PROSITEi PS51585. SAM_MT_TPMT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiTPMT_MOUSE
AccessioniPrimary (citable) accession number: O55060
Secondary accession number(s): Q9JIL7, Q9QUG7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 1, 1998
Last modified: July 9, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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