Reviewed,
UniProtKB/Swiss-Prot P51580 (TPMT_HUMAN)
Last modified
November 3, 2009.
Version 103.
History...
Clusters with 100%,
90%,
50% identity |
Documents (6) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Thiopurine S-methyltransferase EC=2.1.1.67 Alternative name(s): Thiopurine methyltransferase | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) [Complete proteome] | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 245 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Catalyzes the S-methylation of thiopurine drugs such as 6-mercaptopurine. |
| Catalytic activity | S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether. |
| Enzyme regulation | Inhibited by S-adenosyl-L-homocysteine (SAH). |
| Subunit structure | Monomer. |
| Subcellular location | |
| Polymorphism | Individual variation in the toxicity and therapeutic efficacy of thiopurine drugs is associated with a common genetic polymorphism that controls levels of TPMT activity. Genetic polymorphism in the TPMT gene is such that about 90% of Caucasians have high TPMT activity, 10% have intermediate activity and 1 in 300 individuals has low activity. TPMT activity varies among ethnic groups. TPMT*3A is the only mutant allele found in the South West Asians. This is also the most common mutant allele in the Caucasians but is not found in the Chinese. All mutant alleles identified in the Chinese population were TPMT*3C. This allele is found at a low frequency in the Caucasians. This suggests that TPMT*3C is the oldest mutation, with TPMT*3B being acquired later to form the TPMT*3A allele in the Caucasian and South West Asian populations. TPMT*2 appears to be a more recent allele, which has only been detected in Caucasians to date. These ethnic differences may be important in the clinical use of thiopurine drugs. |
| Involvement in disease | Defects in TPMT are the cause of thiopurine S-methyltransferase deficiency (TPMT deficiency) [MIM:610460]. TPMT is an enzyme involved in the normal metabolic inactivation of thiopurine drugs. These drugs are generally used as immunosupressants or cytotoxic drugs and are prescribed for a variety of clinical conditions including leukemia, autoimmune disease and organ transplantation. Patients with intermediate or no TPMT activity are at risk of toxicity after receiving standard doses of thiopurine drugs and it is shown that inter-individual differences in response to these drugs are largely determined by genetic variation at the TPMT locus. |
| Miscellaneous | TPMT deficiency inherited by TPMT*2 and TPMT*3A alleles, are the most prevalent mutant TPMT in humans. TPMT deficiency is associated with lower cellular levels of TPMT protein and the protein encoded by TPMT*2 and TPMT*3A mutant alleles are degradated more rapidely by an ATP-dependent proteasome-mediated pathway. |
| Sequence similarities | Belongs to the methyltransferase superfamily. TPMT family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Coding sequence diversity | Polymorphism |
| Ligand | S-adenosyl-L-methionine |
| Molecular function | Methyltransferase Transferase |
| PTM | Acetylation Phosphoprotein |
| Technical term | 3D-structure Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Molecular function | thiopurine S-methyltransferase activity Ref.1 Traceable author statement. Source: ProtInc |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 245 | 245 | Thiopurine S-methyltransferase | PRO_0000220102 | |||||||||||||||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||||||||||||||
| Binding site | 33 | 1 | S-adenosyl-L-methionine | ||||||||||||||||||||||||||||||||||||||||||||||
| Binding site | 69 | 1 | S-adenosyl-L-methionine; via carbonyl oxygen | ||||||||||||||||||||||||||||||||||||||||||||||
| Binding site | 90 | 1 | S-adenosyl-L-methionine | ||||||||||||||||||||||||||||||||||||||||||||||
| Binding site | 152 | 1 | S-adenosyl-L-methionine | ||||||||||||||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 14 | 1 | Phosphoserine Ref.10 Ref.11 | ||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 58 | 1 | N6-acetyllysine Ref.13 | ||||||||||||||||||||||||||||||||||||||||||||||
Natural variations | |||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 49 | 1 | L → S Allele TPMT*5. dbSNP rs72552740. Ref.5 | VAR_005636 | |||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 80 | 1 | A → P in TPMT deficiency; allele TPMT*2; 100-fold reduction in activity; protein shows enhanced degradation; TPMT*2 allele frequency is 0.5%; seems to be restricted to the Caucasian population. dbSNP rs1800462. Ref.15 Ref.18 Ref.19 Ref.21 Ref.22 Ref.24 Ref.25 | VAR_005637 | |||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 154 | 1 | A → T in TPMT deficiency; allele TPMT*3A and allele TPMT*3B; lower activity; protein shows enhanced degradation; TPMT*3A is most common mutant in American Caucasians; TPMT*3A allele frequencies are 4.5% in the Caucasian; 0.8% in the African Americans and 3.2% in the Caucasian Americans population. dbSNP rs1800460. Ref.5 Ref.18 Ref.19 Ref.21 Ref.22 Ref.24 Ref.25 Ref.3 Ref.16 Ref.17 Ref.23 | VAR_005638 | |||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 179 | 1 | Q → H: dbSNP rs6921269. | VAR_052368 | |||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 180 | 1 | Y → F Allele TPMT*6. Ref.5 | VAR_005639 | |||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 215 | 1 | R → H in TPMT deficiency; allele TPMT*8; intermediate activity. dbSNP rs56161402. Ref.20 | VAR_008715 | |||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 227 | 1 | H → Q in TPMT deficiency; allele TPMT*7. dbSNP rs72552736. Ref.9 | VAR_005640 | |||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 240 | 1 | Y → C in TPMT deficiency; allele TPMT*3B and allele TPMT*3C; lower activity; protein shows enhanced degradation; TPMT*3C is the most common mutant in African-Americans and the only allele in the Japanese and Taiwanese individuals; TPMT*3C frequencies are 7.6% in Ghanaian and 0.3% in Caucasian individuals. dbSNP rs1142345. Ref.5 Ref.19 Ref.21 Ref.22 Ref.24 Ref.25 Ref.3 Ref.16 Ref.17 Ref.23 | VAR_005641 | |||||||||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 18 – 21 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 26 – 35 | 10 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 47 – 57 | 11 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 64 – 67 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 75 – 81 | 7 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 85 – 89 | 5 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 93 – 102 | 10 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 107 – 111 | 5 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 119 – 123 | 5 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 126 – 133 | 8 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 135 – 140 | 6 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 146 – 154 | 9 | |||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 155 – 157 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 160 – 162 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 163 – 172 | 10 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 174 – 186 | 13 | |||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 189 – 191 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 201 – 208 | 8 | |||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 209 – 211 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 212 – 221 | 10 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 225 – 230 | 6 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 236 – 244 | 9 | |||||||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Human thiopurine methyltransferase: molecular cloning and expression of T84 colon carcinoma cell cDNA." Honchel R., Aksoy I.A., Szumlanski C., Wood T.C., Otterness D.M., Wieben E.D., Weinshilboum R.M. Mol. Pharmacol. 43:878-887(1993) [PubMed: 8316220] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Kidney. |
| [2] | "Thiopurine methyltransferase pharmacogenetics. Cloning of human liver cDNA and a processed pseudogene on human chromosome 18q21.1." Lee D., Szumlanski C.L., Houtman J., Honchel R., Rojas K., Overhauser J., Weiben E.D., Weinshilboum R.M. Drug Metab. Dispos. 23:398-405(1995) [PubMed: 7628307] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [3] | "Thiopurine methyltransferase pharmacogenetics: human gene cloning and characterization of a common polymorphism." Szumlanski C., Otterness D., Her C., Lee D., Brandriff B., Kelsell D., Spurr N., Lennard L., Wieben E., Weinshilboum R.M. DNA Cell Biol. 15:17-30(1996) [PubMed: 8561894] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS TPMT DEFICIENCY THR-154 AND CYS-240. |
| [4] | "Promoter and intronic sequences of the human thiopurine S-methyltransferase (TPMT) gene isolated from a human PAC1 genomic library." Krynetski E.Y., Fessing M.Y., Yates C.R., Sun D., Schuetz J.D., Evans W.E. Pharm. Res. 14:1672-1678(1997) [PubMed: 9453052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [5] | "Human thiopurine methyltransferase pharmacogenetics: gene sequence polymorphisms." Otterness D., Szumlanski C., Lennard L., Klemetsdal B., Aarbakke J., Park-Hah J.O., Iven H., Schmiegelow K., Branum E., O'Brien J., Weinshilboum R.M. Clin. Pharmacol. Ther. 62:60-73(1997) [PubMed: 9246020] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-49 AND PHE-180, VARIANTS TPMT DEFICIENCY THR-154 AND CYS-240. |
| [6] | "Genomic structure of thiopurine S-methyltransferase gene." Nakamura Y. Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [7] | "The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. Beck S.Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [8] | "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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Bone marrow. |
| [9] | "Detection of known and new mutations in the thiopurine S-methyltransferase gene by single-strand conformation polymorphism analysis." Spire-Vayron de la Moureyre C., Debuysere H., Sabbagh N., Marez D., Vinner E., Chevalier E.D., Lo-Guidice J.-M., Broly F. Hum. Mutat. 12:177-185(1998) [PubMed: 9711875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 210-245, VARIANT TPMT DEFICIENCY GLN-227. |
| [10] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, MASS SPECTROMETRY. |
| [11] | "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, MASS SPECTROMETRY. Tissue: Liver. |
| [12] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [13] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-58, MASS SPECTROMETRY. |
| [14] | "The crystal structure of human thiopurine S-methyltransferase in complex with SAH." Structural genomics consortium (SGC) Submitted (AUG-2005) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 16-245. |
| [15] | "A single point mutation leading to loss of catalytic activity in human thiopurine S-methyltransferase." Krynetski E.Y., Schuetz J.D., Galpin A.J., Pui C.-H., Relling M.V., Evans W.E. Proc. Natl. Acad. Sci. U.S.A. 92:949-953(1995) [PubMed: 7862671] [Abstract] Cited for: VARIANT TPMT DEFICIENCY PRO-80. |
| [16] | "Thiopurine S-methyltransferase deficiency: two nucleotide transitions define the most prevalent mutant allele associated with loss of catalytic activity in Caucasians." Tai H.-L., Krynetski E.Y., Yates C.R., Loennechen T., Fessing M.Y., Krynetskaia N.F., Evans W.E. Am. J. Hum. Genet. 58:694-702(1996) [PubMed: 8644731] [Abstract] Cited for: VARIANTS TPMT DEFICIENCY THR-154 AND CYS-240. |
| [17] | "Azathioprine-induced severe pancytopenia due to a homozygous two-point mutation of the thiopurine methyltransferase gene in a patient with juvenile HLA-B27-associated spondylarthritis." Leipold G., Schuetz E., Haas J.P., Oellerich M. Arthritis Rheum. 40:1896-1898(1997) [PubMed: 9336428] [Abstract] Cited for: VARIANTS TPMT DEFICIENCY THR-154 AND CYS-240. |
| [18] | "Enhanced proteolysis of thiopurine S-methyltransferase (TPMT) encoded by mutant alleles in humans (TPMT*3A, TPMT*2): mechanisms for the genetic polymorphism of TPMT activity." Tai H.-L., Krynetski E.Y., Schuetz E.G., Yanishevski Y., Evans W.E. Proc. Natl. Acad. Sci. U.S.A. 94:6444-6449(1997) [PubMed: 9177237] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS TPMT DEFICIENCY PRO-80 AND THR-154, MECHANISM FOR THE GENETIC POLYMORPHISM OF TPMT ACTIVITY. |
| [19] | "Thiopurine methyltransferase alleles in British and Ghanaian populations." Ameyaw M.-M., Collie-Duguid E.S.R., Powrie R.H., Ofori-Adjei D., McLeod H.L. Hum. Mol. Genet. 8:367-370(1999) [PubMed: 9931345] [Abstract] Cited for: VARIANTS TPMT DEFICIENCY PRO-80; THR-154 AND CYS-240. |
| [20] | "Polymorphism of the thiopurine S-methyltransferase gene in African-Americans." Hon Y.Y., Fessing M.Y., Pui C.-H., Relling M.V., Krynetski E.Y., Evans W.E. Hum. Mol. Genet. 8:371-376(1999) [PubMed: 9931346] [Abstract] Cited for: VARIANT TPMT DEFICIENCY HIS-215. |
| [21] | "The frequency and distribution of thiopurine methyltransferase alleles in Caucasian and Asian populations." Collie-Duguid E.S.R., Pritchard S.C., Powrie R.H., Sludden J., Collier D.A., Li T., McLeod H.L. Pharmacogenetics 9:37-42(1999) [PubMed: 10208641] [Abstract] Cited for: VARIANTS TPMT DEFICIENCY PRO-80; THR-154 AND CYS-240, FREQUENCY AND DISTRIBUTION OF ALLELES. |
| [22] | "Genetic analysis of thiopurine methyltransferase polymorphism in a Japanese population." Hiratsuka M., Inoue T., Omori F., Agatsuma Y., Mizugaki M. Mutat. Res. 448:91-95(2000) [PubMed: 10751626] [Abstract] Cited for: VARIANTS TPMT DEFICIENCY PRO-80; THR-154 AND CYS-240, FREQUENCY AND DISTRIBUTION OF ALLELES. |
| [23] | "Severe azathioprine-induced myelotoxicity in a kidney transplant patient with thiopurine S-methyltransferase-deficient genotype (TPMT*3A/*3C)." Kurzawski M., Dziewanowski K., Ciechanowski K., Drozdzik M. Transpl. Int. 18:623-625(2005) [PubMed: 15819814] [Abstract] Cited for: VARIANTS TPMT DEFICIENCY THR-154 AND CYS-240. |
| [24] | "Molecular analysis of thiopurine S-methyltransferase alleles in Taiwan aborigines and Taiwanese." Lu H.-F., Shih M.-C., Chang Y.-S., Chang J.-Y., Ko Y.-C., Chang S.-J., Chang J.-G. J. Clin. Pharm. Ther. 31:93-98(2006) [PubMed: 16476125] [Abstract] Cited for: VARIANTS TPMT DEFICIENCY PRO-80; THR-154 AND CYS-240, FREQUENCY AND DISTRIBUTION OF ALLELES. |
| [25] | "Frequency of the thiopurine S-methyltransferase alleles in the ancient genetic population isolate of Sardinia." Rossino R., Vincis C., Alves S., Prata M.J., Macis M.D., Nucaro A.L., Schirru E., Congia M. J. Clin. Pharm. Ther. 31:283-287(2006) [PubMed: 16789994] [Abstract] Cited for: VARIANTS TPMT DEFICIENCY PRO-80; THR-154 AND CYS-240, FREQUENCY AND DISTRIBUTION OF ALLELES. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| S62904 mRNA. Translation: AAB27277.1. U12387 mRNA. Translation: AAC50130.1. U30518 U30517 Genomic DNA. Translation: AAC50368.1. AF019369 AF019368 Genomic DNA. Translation: AAC51865.1. U81562 Genomic DNA. Translation: AAB71625.1. U81563 Genomic DNA. Translation: AAB71626.1. U81564 Genomic DNA. Translation: AAB71627.1. U81565 Genomic DNA. Translation: AAB71628.1. U81566 Genomic DNA. Translation: AAB71629.1. U81567 Genomic DNA. Translation: AAB71630.1. U81568 Genomic DNA. Translation: AAB71631.1. Different initiation. U81569 Genomic DNA. Translation: AAB71632.1. Different initiation. U81570 Genomic DNA. Translation: AAB71633.1. U81571 Genomic DNA. Translation: AAB71634.1. U81572 Genomic DNA. Translation: AAB71635.1. U81573 Genomic DNA. Translation: AAB71636.1. AB045146 Genomic DNA. Translation: BAA97037.1. AL589723 Genomic DNA. Translation: CAH71233.1. BC009596 mRNA. Translation: AAH09596.1. AF035426 Genomic DNA. Translation: AAC32289.1. AF021876 mRNA. Translation: AAB80746.1. AF021877 mRNA. Translation: AAB80747.1. | |||||||||||||||||||
| IPI | IPI00019400. | ||||||||||||||||||
| PIR | I57946. | ||||||||||||||||||
| RefSeq | NP_000358.1. | ||||||||||||||||||
| UniGene | Hs.444319 | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| |||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| STRING | P51580. | ||||||||||||||||||
PTM databases | |||||||||||||||||||
| PhosphoSite | P51580. | ||||||||||||||||||
Proteomic databases | |||||||||||||||||||
| PeptideAtlas | P51580. | ||||||||||||||||||
| PRIDE | P51580. | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| Ensembl | ENST00000309983; ENSP00000312304; ENSG00000137364; Homo sapiens. [Genome view] | ||||||||||||||||||
| GeneID | 7172. | ||||||||||||||||||
| KEGG | hsa:7172. | ||||||||||||||||||
| UCSC | uc003ncm.1. human. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| CTD | 7172. | ||||||||||||||||||
| GeneCards | GC06M018236. | ||||||||||||||||||
| H-InvDB | HIX0018948. | ||||||||||||||||||
| HGNC | HGNC:12014. TPMT. | ||||||||||||||||||
| HPA | HPA019851. | ||||||||||||||||||
| MIM | 187680. gene. 610460. phenotype. | ||||||||||||||||||
| Orphanet | 3315. Thiopurine s-methyltranferase deficiency. | ||||||||||||||||||
| PharmGKB | PA356. | ||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| HOVERGEN | P51580. | ||||||||||||||||||
| OMA | PPFAVSP. | ||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||
| BRENDA | 2.1.1.67. 247. | ||||||||||||||||||
| Reactome | REACT_13433. Biological oxidations. | ||||||||||||||||||
Gene expression databases | |||||||||||||||||||
| ArrayExpress | P51580. | ||||||||||||||||||
| Bgee | P51580. | ||||||||||||||||||
| Genevestigator | P51580. | ||||||||||||||||||
| GermOnline | ENSG00000137364. Homo sapiens. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR008854. Thiopurine_S-MeTrfase. IPR016822. Thiopurine_S-MeTrfase_sub. [Graphical view] | ||||||||||||||||||
| Pfam | PF05724. TPMT. 1 hit. [Graphical view] | ||||||||||||||||||
| PIRSF | PIRSF023956. Thiopurine_S-methyltransferase. 1 hit. | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other Resources | |||||||||||||||||||
| DrugBank | DB01033. Mercaptopurine. | ||||||||||||||||||
| NextBio | 28108. | ||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||
Entry information
| Entry name | TPMT_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P51580 Secondary accession number(s): O14806 Q9UE62 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Human chromosome 6 Human chromosome 6: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


