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O55060

- TPMT_MOUSE

UniProt

O55060 - TPMT_MOUSE

Protein

Thiopurine S-methyltransferase

Gene

Tpmt

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

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

    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

    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

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 240240Thiopurine S-methyltransferasePRO_0000220105Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei53 – 531N6-acetyllysineBy 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

    1
    240
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO55060.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni24 – 3512S-adenosyl-L-methionine bindingAdd
    BLAST
    Regioni129 – 1302S-adenosyl-L-methionine binding

    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

    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: October 1, 2014
    This is version 113 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