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Protein

Thiopurine S-methyltransferase

Gene

Tpmt

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

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 – 351SubstrateBy similarity
Binding sitei64 – 641S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
Binding sitei85 – 851S-adenosyl-L-methionineBy similarity
Binding sitei147 – 1471S-adenosyl-L-methionineBy similarity

GO - Molecular functioni

GO - Biological processi

  • response to organic cyclic compound Source: RGD
  • response to testosterone Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiR-RNO-156581. Methylation.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiopurine S-methyltransferase (EC:2.1.1.67)
Alternative name(s):
Thiopurine methyltransferase
Gene namesi
Name:Tpmt
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 17

Organism-specific databases

RGDi1585162. Tpmt.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 240240Thiopurine S-methyltransferasePRO_0000220113Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiQ9Z0T0.

PTM databases

iPTMnetiQ9Z0T0.

Expressioni

Gene expression databases

ExpressionAtlasiQ9Z0T0. baseline and differential.
GenevisibleiQ9Z0T0. RN.

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9Z0T0.
SMRiQ9Z0T0. Positions 9-240.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni24 – 3512S-adenosyl-L-methionine bindingBy similarityAdd
BLAST
Regioni129 – 1302S-adenosyl-L-methionine bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000016823.
HOVERGENiHBG003037.
PhylomeDBiQ9Z0T0.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_00812. Thiopur_methtran.
InterProiIPR029063. SAM-dependent_MTases.
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.

Q9Z0T0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLGIKEHPD AEVQKNRVLT LDDWQDKWVT RHIAFHQEQG HQLLKKHFDT
60 70 80 90 100
FLKGQSGLRV FFPLCGKAIE MKWFADRGHT VVGVEISEIG IREFFAEQNL
110 120 130 140 150
SYTEEPLTEI AGAKVFKSSS GNISLYCCSI FDLPRANIGK FDRIWDRGAL
160 170 180 190 200
VAVNPGDRDR YADIILSLLR KGYHYLLVVL SYDPTKHTGP PFYVPDAELK
210 220 230 240
KLFGTKCNMQ CLEEVDALEE RHKTWGVDYF FEKLYLLTEK
Length:240
Mass (Da):27,692
Last modified:May 1, 1999 - v1
Checksum:i04608B546BBDC1E3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF120100 mRNA. Translation: AAD17293.1.
RefSeqiXP_006253832.1. XM_006253770.2.
UniGeneiRn.112598.

Genome annotation databases

EnsembliENSRNOT00000022085; ENSRNOP00000022084; ENSRNOG00000016468.
GeneIDi690050.
UCSCiRGD:620089. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF120100 mRNA. Translation: AAD17293.1.
RefSeqiXP_006253832.1. XM_006253770.2.
UniGeneiRn.112598.

3D structure databases

ProteinModelPortaliQ9Z0T0.
SMRiQ9Z0T0. Positions 9-240.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiQ9Z0T0.

Proteomic databases

PRIDEiQ9Z0T0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000022085; ENSRNOP00000022084; ENSRNOG00000016468.
GeneIDi690050.
UCSCiRGD:620089. rat.

Organism-specific databases

CTDi7172.
RGDi1585162. Tpmt.

Phylogenomic databases

GeneTreeiENSGT00390000016823.
HOVERGENiHBG003037.
PhylomeDBiQ9Z0T0.

Enzyme and pathway databases

ReactomeiR-RNO-156581. Methylation.

Miscellaneous databases

PROiQ9Z0T0.

Gene expression databases

ExpressionAtlasiQ9Z0T0. baseline and differential.
GenevisibleiQ9Z0T0. RN.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_00812. Thiopur_methtran.
InterProiIPR029063. SAM-dependent_MTases.
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]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiTPMT_RAT
AccessioniPrimary (citable) accession number: Q9Z0T0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: May 1, 1999
Last modified: June 8, 2016
This is version 86 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.