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InterPro: IPR008854 Thiopurine S-methyltransferase

Protein matches Help

UniProtKB

Matches:

495 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR008854 Thiopurine_S-MeTrfase

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF05724	TPMT	495
Signatures in BioMart

InterPro Relationships Help

Children

IPR016822 Thiopurine S-methyltransferase, subgroup

GO Term annotation Help

Process

GO:0008152 metabolic process

Function

GO:0008119 thiopurine S-methyltransferase activity

Component

GO:0005737 cytoplasm

InterPro annotation

Entry Details in BioMart

Abstract

This family consists of thiopurine S-methyltransferase proteins from both eukaryotes and prokaryotes. Thiopurine S-methyltransferase (TPMT) is a cytosolic enzyme that catalyses S-methylation of aromatic and heterocyclic sulphydryl compounds, including anticancer and immunosuppressive thiopurines [1].

Structural links Help

PDB - click here

SCOP: c.66.1.36

CATH: 3.40.50.150

Database links Help

Enzyme: EC:2.1.1.67

PANDIT: PF05724

Blocks: IPB008854

Pfam Clan: CL0102.19

AC	CL0102.19
ID	Methyltransfer
DE	Methyltransferase superfamily
PF00145	IPR001525	DNA methylase, C-5 cytosine-specific
PF00398	IPR001737	Ribosomal RNA adenine methylase transferase
PF00891	IPR001077	O-methyltransferase, family 2
PF01135	IPR000682	Protein-L-isoaspartate(D-aspartate) O-methyltransferase
PF01170	IPR000241	Putative RNA methylase
PF01189	IPR001678	Bacterial Fmu (Sun)/eukaryotic nucleolar NOL1/Nop2p
PF01209	IPR004033	UbiE/COQ5 methyltransferase
PF01234	IPR000940	Methyltransferase, NNMT/PNMT/TEMT
PF01269	IPR000692	Fibrillarin
PF01358	IPR000176	Poly A polymerase regulatory subunit
PF01555	IPR002941	DNA methylase N-4/N-6
PF01564	IPR001045	Spermine synthase
PF01596	IPR002935	O-methyltransferase, family 3
PF01728	IPR002877	Ribosomal RNA methyltransferase RrmJ/FtsJ
PF01739	IPR000780	MCP methyltransferase, CheR-type
PF01795	IPR002903	S-adenosyl-L-methionine-dependent methyltransferase, MraW
PF01861	IPR002723	Protein of unknown function DUF43
PF02005	IPR002905	N2,N2-dimethylguanosine tRNA methyltransferase
PF02086	IPR012327	D12 class N6 adenine-specific DNA methyltransferase
PF02353	IPR003333	Cyclopropane-fatty-acyl-phospholipid synthase
PF02384	IPR003356	DNA methylase, adenine-specific
PF02390	IPR003358	tRNA (guanine-N-7) methyltransferase
PF02475	IPR003402	Protein of unknown function Met10
PF02527	IPR003682	rRNA small subunit methyltransferase G
PF03141	IPR004159	Protein of unknown function DUF248, methyltransferase putative
PF03269	IPR004951	Protein of unknown function DUF268, Caenorhabditis species
PF03291	IPR004971	mRNA capping enzyme, large subunit
PF03602	IPR016065	Protein of unknown function methylase putative
PF03848	IPR015985	Tellurite resistance methyltransferase, TehB, core
PF04378	IPR007473	Protein of unknown function DUF519
PF04445	IPR007536	Protein of unknown function DUF548
PF04672	IPR006764	Protein of unknown function DUF574
PF04816	IPR006901	Protein of unknown function DUF633
PF05063	IPR007757	MT-A70
PF05148	IPR007823	Methyltransferase-related
PF05175	IPR007848	Methyltransferase small
PF05219	IPR007884	DREV methyltransferase
PF05401	IPR008715	NodS
PF05430	IPR008471	Protein of unknown function DUF752
PF05724	IPR008854	Thiopurine S-methyltransferase
PF05891	IPR008576	Protein of unknown function DUF858, methyltransferase-like
PF05958	IPR010280	(Uracil-5)-methyltransferase
PF05971	IPR010286	S-adenosyl-L-methionine dependent methyltransferase, predicted
PF06080	IPR010342	Protein of unknown function DUF938
PF06325	IPR010456	Ribosomal L11 methyltransferase
PF06460	IPR009461	Coronavirus NSP13
PF06859	IPR010675	Bicoid-interacting 3
PF06962	IPR010719	Putative rRNA methylase
PF07021	IPR010743	Methionine biosynthesis MetW
PF07109	IPR010940	Magnesium-protoporphyrin IX methyltransferase, C-terminal
PF07279	IPR009902	Protein of unknown function DUF1442
PF07669	IPR011639	Restriction endonuclease, Eco57I
PF07757	IPR011671	AdoMet-dependent methyltransferase, predicted
PF07942	IPR012901	N2227-like
PF08003	IPR010017	tRNA (mo5U34)-methyltransferase
PF08123	IPR013110	Histone methylation DOT1
PF08241	IPR013216	Methyltransferase type 11
PF08242	IPR013217	Methyltransferase type 12
PF08704	IPR014816	tRNA methyltransferase complex GCD14 subunit
PF09243	IPR015324	Ribosomal protein Rsm22, bacterial-type
PF09445	IPR019012	RNA cap guanine-N2 methyltransferase
PF10294	IPR019410	Methyltransferase-16, putative
PF10672	IPR019614	S-adenosylmethionine-dependent methyltransferase

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR008854

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O55060 Thiopurine S-methyltransferase

O86262 Thiopurine S-methyltransferase

P51580 Thiopurine S-methyltransferase

Q17QQ2 Thiopurine S-methyltransferase

Q6C6X6 Probable thiopurine S-methyltransferase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR008854	Thiopurine S-methyltransferase
IPR016822	Thiopurine S-methyltransferase, subgroup
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Fessing MY, Krynetski EY, Zambetti GP, Evans WE. Functional characterization of the human thiopurine S-methyltransferase (TPMT) gene promoter. Eur. J. Biochem. 256 510-7 1998 [PubMed: 9780226] http://dx.doi.org/10.1046/j.1432-1327.1998.2560510.x

Additional Reading Open in usermanual
	Scheuermann TH, Lolis E, Hodsdon ME. Tertiary structure of thiopurine methyltransferase from Pseudomonas syringae, a bacterial orthologue of a polymorphic, drug-metabolizing enzyme. J. Mol. Biol. 333 2003 573-85 [PubMed: 14556746] http://dx.doi.org/10.1016/j.jmb.2003.08.039
	Wu H, Horton JR, Battaile K, Allali-Hassani A, Martin F, Zeng H, Loppnau P, Vedadi M, Bochkarev A, Plotnikov AN, Cheng X. Structural basis of allele variation of human thiopurine-S-methyltransferase. Proteins 67 2007 198-208 [PubMed: 17243178] http://dx.doi.org/10.1002/prot.21272

InterPro 23.1