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Showing drug card for L-Methionine (DB00134)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-04-16 16:47:26
Primary Accession Number DB00134
Secondary Accession Number
  • NUTR00038
Name L-Methionine
Drug Type
  • Approved
  • Nutraceutical
  • Small Molecule
Description A sulfur containing essential amino acid that is important in many body functions. It is a chelating agent for heavy metals. [PubChem]
Synonyms
  1. (S)-2-Amino-4-(methylthio)butanoic acid
  2. 2-Amino-4-(methylthio)butyric acid
  3. L-(-)-Methionine
  4. L-a-Amino-g-methylthiobutyric acid
  5. Methionine
  6. a-Amino-g-methylmercaptobutyric acid
  7. g-Methylthio-a-aminobutyric acid
Brand Names
  1. Acimethin
  2. Cymethion
Brand Mixtures Not Available
Chemical IUPAC Name (2S)-2-amino-4-methylsulfanylbutanoic acid
Chemical Formula C5H11NO2S
Chemical Structure Structure
CAS Registry Number 63-68-3
InChI Identifier InChI=1/C5H11NO2S/c1-9-3-2-4(6)5(7)8/h4H,2-3,6H2,1H3,(H,7,8)/t4-/m0/s1/f/h7H
InChI Key FFEARJCKVFRZRR-XWEZEGGSDQ
KEGG Drug D04983 Link Image
KEGG Compound C01733 Link Image
PubChem Compound 6137 Link Image
PubChem Substance 8144963 Link Image
ChEBI ID 16811 Link Image
PharmGKB ID Not Available
HET ID MET Link Image
GenBank ID Not Available
Drug ID Number [DIN] Not Available
RxList Link Not Available
PDRhealth Link http://www.pdrhealth.com/drug_info/nmdrugprofiles/nutsupdrugs/lme_0173.shtml Link Image
Wikipedia Link Not Available
FDA Label Not Available
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 149.2110
Monoisotopic Molecular Weight 149.0510
State Solid
Melting Point 276-279 oC
Experimental Water Solubility 56.6 mg/mL at 25 oC [YALKOWSKY,SH & DANNENFELSER,RM (1992)] Source: PhysProp
Predicted Water Solubility 2.39e+01 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity -1.9 Source: PhysProp
Predicted LogP -1.85 Calculated using ALOGPS
Experimental LogS -0.42 [ADME Research, USCD]
Predicted LogS -0.80 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point Not Available
Mass Spectrum Not Available
MOL File Show Link Image | Download Link Image
SDF File Show Link Image | Download Link Image
PDB File Show Link Image | Download Link Image
2D Structure
3D Structure
Experimental PDB ID 1WKM Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES CSCC[C@H](N)C(O)=O
Canonical SMILES CSCCC(N)C(O)=O
Drug Category
  • Dietary supplement
  • Essential Amino Acids
  • Micronutrient
ATC Codes
AHFS Codes Not Available
Indication Used for protein synthesis including the formation of SAMe, L-homocysteine, L-cysteine, taurine, and sulfate.
Pharmacology L-Methionine is a principle supplier of sulfur which prevents disorders of the hair, skin and nails; helps lower cholesterol levels by increasing the liver's production of lecithin; reduces liver fat and protects the kidneys; a natural chelating agent for heavy metals; regulates the formation of ammonia and creates ammonia-free urine which reduces bladder irritation; influences hair follicles and promotes hair growth. L-methionine may protect against the toxic effects of hepatotoxins, such as acetaminophen. Methionine may have antioxidant activity.
Mechanism of Action The mechanism of the possible anti-hepatotoxic activity of L-methionine is not entirely clear. It is thought that metabolism of high doses of acetaminophen in the liver lead to decreased levels of hepatic glutathione and increased oxidative stress. L-methionine is a precursor to L-cysteine. L-cysteine itself may have antioxidant activity. L-cysteine is also a precursor to the antioxidant glutathione. Antioxidant activity of L-methionine and metabolites of L-methionine appear to account for its possible anti-hepatotoxic activity. Recent research suggests that methionine itself has free-radical scavenging activity by virtue of its sulfur, as well as its chelating ability.
Absorption Absorbed from the lumen of the small intestine into the enterocytes by an active transport process.
Toxicity Doses of L-methionine of up to 250 mg daily are generally well tolerated. Higher doses may cause nausea, vomiting and headache. Healthy adults taking 8 grams of L-methionine daily for four days were found to have reduced serum folate levels and leucocytosis. Healthy adults taking 13.9 grams of L-methionine daily for five days were found to have changes in serum pH and potassium and increased urinary calcium excretion. Schizophrenic patients given 10 to 20 grams of L-methionine daily for two weeks developed functional psychoses. Single doses of 8 grams precipitated encephalopathy in patients with cirrhosis.
Protein Binding Not Available
Biotransformation Hepatic
Half Life Not Available
Dosage Forms
Form Route
Capsule Oral
Powder Oral
Tablet Oral
Tablet Oral
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions Not Available
Food Interactions
  • Take with food.
Pathways Not Available
General References
  1. PDRhealth Link Image
Organisms Affected
  • Humans and other mammals
Phase 1 Metabolizing Enzymes
  1. Glutamine Synthetase
  2. Methylenetetrahydrofolate reductase
Targets
  1. Peptide methionine sulfoxide reductase
  2. Methionine-R-sulfoxide reductase
  3. S-adenosylmethionine synthetase isoform type-2
  4. S-adenosylmethionine synthetase isoform type-1
  5. Methionine-R-sulfoxide reductase B2
  6. Methionyl-tRNA synthetase, cytoplasmic
  7. Methionine synthase
  8. Methionine synthase reductase, mitochondrial
  9. Betaine--homocysteine S-methyltransferase 1
  10. Methionine aminopeptidase 2
  11. Methionine adenosyltransferase 2 subunit beta
  12. Methionyl-tRNA synthetase, mitochondrial
  13. Betaine--homocysteine S-methyltransferase 2
Phase 1 Metabolizing Enzyme 1 [top]
Enzyme 1 Name Glutamine Synthetase
Enzyme 1 Gene Name GLUL
Enzyme 1 SwissProt ID P15104 Link Image
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 Protein Sequence >sp|P15104|GLNA_HUMAN Glutamine synthetase (EC 6.3.1.2) 
TTSASSHLNKGIKQVYMSLPQGEKVQAMYIWIDGTGEGLRCKTRTLDSEPKCVEELPEWN
FDGSSTLQSEGSNSDMYLVPAAMFRDPFRKDPNKLVLCEVFKYNRRPAETNLRHTCKRIM
DMVSNQHPWFGMEQEYTLMGTDGHPFGWPSNGFPGPQGPYYCGVGADRAYGRDIVEAHYR
ACLYAGVKIAGTNAEVMPAQWEFQIGPCEGISMGDHLWVARFILHRVCEDFGVIATFDPK
PIPGNWNGAGCHTNFSTKAMREENGLKYIEEAIEKLSKRHQYHIRAYDPKGGLDNARRLT
GFHETSNINDFSAGVANRSASIRIPRTVGQEKKGYFEDRRPSANCDPFSVTEALIRTCLL
NETGDEPFQYKN
Phase 1 Metabolizing Enzyme 2 [top]
Enzyme 2 Name Methylenetetrahydrofolate reductase
Enzyme 2 Gene Name MTHFR
Enzyme 2 SwissProt ID P42898 Link Image
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 Protein Sequence >sp|P42898|MTHR_HUMAN Methylenetetrahydrofolate reductase 
MVNEARGNSSLNPCLEGSASSGSESSKDSSRCSTPGLDPERHERLREKMRRRLESGDKWF
SLEFFPPRTAEGAVNLISRFDRMAAGGPLYIDVTWHPAGDPGSDKETSSMMIASTAVNYC
GLETILHMTCCRQRLEEITGHLHKAKQLGLKNIMALRGDPIGDQWEEEEGGFNYAVDLVK
HIRSEFGDYFDICVAGYPKGHPEAGSFEADLKHLKEKVSAGADFIITQLFFEADTFFRFV
KACTDMGITCPIVPGIFPIQGYHSLRQLVKLSKLEVPQEIKDVIEPIKDNDAAIRNYGIE
LAVSLCQELLASGLVPGLHFYTLNREMATTEVLKRLGMWTEDPRRPLPWALSAHPKRREE
DVRPIFWASRPKSYIYRTQEWDEFPNGRWGNSSSPAFGELKDYYLFYLKSKSPKEELLKM
WGEELTSEESVFEVFVLYLSGEPNRNGHKVTCLPWNDEPLAAETSLLKEELLRVNRQGIL
TINSQPNINGKPSSDPIVGWGPSGGYVFQKAYLEFFTSRETAEALLQVLKKYELRVNYHL
VNVKGENITNAPELQPNAVTWGIFPGREIIQPTVVDPVSFMFWKDEAFALWIERWGKLYE
EESPSRTIIQYIHDNYFLVNLVDNDFPLDNCLWQVVEDTLELLNRPTQNARETEAP
Drug Target 1 [top]
Target 1 ID 191
Target 1 Name Peptide methionine sulfoxide reductase
Target 1 Synonyms
  1. EC 1.8.4.11
  2. PMSR
  3. Peptide Met(O
  4. Peptide-methionine (S)-S-oxide reductase
  5. Protein- methionine-S-oxide reductase
Target 1 Gene Name MSRA
Target 1 Protein Sequence >Peptide methionine sulfoxide reductase 
MLSATRRACQLLLLHSLFPVPRMGNSASNIVSPQEALPGRKEQTPVAAKHHVNGNRTVEP
FPEGTQMAVFGMGCFWGAERKFWVLKGVYSTQVGFAGGYTSNPTYKEVCSEKTGHAEVVR
VVYQPEHMSFEELLKVFWENHDPTQGMRQGNDHGTQYRSAIYPTSAKQMEAALSSKENYQ
KVLSEHGFGPITTDIREGQTFYYAEDYHQQYLSKNPNGYCGLGGTGVSCPVGIKK
Target 1 Number of Residues 238
Target 1 Molecular Weight 26133
Target 1 Theoretical pI 8.21
Target 1 GO Classification
Function
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on sulfur group of donors
oxidoreductase activity, acting on sulfur group of donors, disulfide as acceptor
protein-methionine-S-oxide reductase activity
Process
physiological process
metabolism
macromolecule metabolism
protein metabolism
Component
Not Available
Target 1 General Function Posttranslational modification, protein turnover, chaperones
Target 1 Specific Function Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine
Target 1 Pathways Not Available
Target 1 Reactions
  • (1) peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 6136945 Link Image
Target 1 UniProtKB/Swiss-Prot ID Q9UJ68 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name MSRA_HUMAN Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location Not Available
Target 1 Gene Sequence >708 bp 
ATGCTCTCGGCCACCCGGAGGGCTTGCCAGCTCCTCCTCCTCCACAGCCTCTTTCCCGTC
CCGAGGATGGGCAACTCGGCCTCGAACATCGTCAGCCCCCAGGAGGCCTTGCCGGGCCGG
AAGGAACAGACCCCTGTAGCGGCCAAACATCATGTCAATGGCAACAGAACAGTCGAACCT
TTCCCAGAGGGAACACAGATGGCTGTATTTGGAATGGGATGTTTCTGGGGAGCTGAAAGG
AAATTCTGGGTCTTGAAAGGAGTGTATTCAACTCAAGTTGGTTTTGCAGGAGGCTATACT
TCAAATCCTACTTATAAAGAAGTCTGCTCAGAAAAAACTGGCCATGCAGAAGTCGTCCGA
GTGGTGTACCAGCCAGAACACATGAGTTTTGAGGAACTGCTCAAGGTCTTCTGGGAGAAT
CACGACCCGACCCAAGGTATGCGCCAGGGGAACGACCATGGCACTCAGTACCGCTCGGCC
ATCTACCCGACCTCTGCCAAGCAAATGGAGGCAGCCCTGAGCTCCAAAGAGAACTACCAA
AAGGTTCTTTCAGAGCACGGCTTCGGCCCCATCACTACCGACATCCGGGAGGGACAGACT
TTCTACTATGCGGAAGACTACCACCAGCAGTACCTGAGCAAGAACCCCAATGGCTACTGC
GGCCTTGGGGGCACCGGCGTGTCCTGCCCAGTGGGTATTAAAAAATAA
Target 1 GenBank Gene ID
Target 1 GeneCard ID MSRA Link Image
Target 1 GenAtlas ID MSRA Link Image
Target 1 HGNC ID HGNC:7377 Link Image
Target 1 Chromosome Location 8
Target 1 Locus 8p23.1
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Kuschel L, Hansel A, Schonherr R, Weissbach H, Brot N, Hoshi T, Heinemann SH: Molecular cloning and functional expression of a human peptide methionine sulfoxide reductase (hMsrA). FEBS Lett. 1999 Jul 30;456(1):17-21. [PubMed Link Image]
Target 1 Drug References
  1. Schallreuter KU, Rubsam K, Chavan B, Zothner C, Gillbro JM, Spencer JD, Wood JM: Functioning methionine sulfoxide reductases A and B are present in human epidermal melanocytes in the cytosol and in the nucleus. Biochem Biophys Res Commun. 2006 Mar 31;342(1):145-52. Epub 2006 Feb 3. [PubMed Link Image]
  2. Rouhier N, Vieira Dos Santos C, Tarrago L, Rey P: Plant methionine sulfoxide reductase A and B multigenic families. Photosynth Res. 2006 Sep;89(2-3):247-62. Epub 2006 Sep 22. [PubMed Link Image]
  3. Oien DB, Moskovitz J: Ablation of the mammalian methionine sulfoxide reductase A affects the expression level of cysteine deoxygenase. Biochem Biophys Res Commun. 2007 Jan 12;352(2):556-9. Epub 2006 Nov 20. [PubMed Link Image]
  4. Gand A, Antoine M, Boschi-Muller S, Branlant G: Characterization of the amino acids involved in substrate specificity of methionine sulfoxide reductase A. J Biol Chem. 2007 Jul 13;282(28):20484-91. Epub 2007 May 11. [PubMed Link Image]
  5. Su Z, Limberis J, Martin RL, Xu R, Kolbe K, Heinemann SH, Hoshi T, Cox BF, Gintant GA: Functional consequences of methionine oxidation of hERG potassium channels. Biochem Pharmacol. 2007 Sep 1;74(5):702-11. Epub 2007 Jun 7. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 317
Target 2 Name Methionine-R-sulfoxide reductase
Target 2 Synonyms
  1. EC 1.8.4.-
  2. Selenoprotein X 1
Target 2 Gene Name SEPX1
Target 2 Protein Sequence >Methionine-R-sulfoxide reductase 
MSFCSFFGGEVFQNHFEPGVYVCAKCGYELFSSRSKYAHSSPWPAFTETIHADSVAKRPE
HNRSEALKVSCGKCGNGLGHEFLNDGPKPGQSRFCIFSSSLKFVPKGKETSASQGH
Target 2 Number of Residues 117
Target 2 Molecular Weight 12713
Target 2 Theoretical pI 8.39
Target 2 GO Classification Not Available
Target 2 General Function Posttranslational modification, protein turnover, chaperones
Target 2 Specific Function Not Available
Target 2 Pathways Not Available
Target 2 Reactions Not Available
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 6649219 Link Image
Target 2 UniProtKB/Swiss-Prot ID Q9NZV6 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name MSRX_HUMAN Link Image
Target 2 PDB ID Not Available
Target 2 Cellular Location Not Available
Target 2 Gene Sequence >351 bp 
ATGTCGTTCTGCAGCTTCTTCGGGGGCGAGGTTTTCCAGAATCACTTTGAACCTGGCGTT
TACGTGTGTGCCAAGTGTGGCTATGAGCTGTTCTCCAGCCGCTCGAAGTATGCACACTCG
TCTCCATGGCCGGCGTTCACCGAGACCATTCACGCCGACAGCGTGGCCAAGCGTCCGGAG
CACAATAGATCTGAAGCCTTGAAGGTGTCCTGTGGCAAGTGTGGCAATGGGTTGGGCCAC
GAGTTCCTGAACGACGGCCCCAAGCCGGGGCAGTCCCGATTCTGAATATTCAGCAGCTCG
CTGAAGTTTGTCCCTAAAGGCAAAGAAACTTCTGCCTCCCAGGGTCACTAG
Target 2 GenBank Gene ID
Target 2 GeneCard ID SEPX1 Link Image
Target 2 GenAtlas ID SEPX1 Link Image
Target 2 HGNC ID HGNC:14133 Link Image
Target 2 Chromosome Location 16
Target 2 Locus 16p13.3
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Lescure A, Gautheret D, Carbon P, Krol A: Novel selenoproteins identified in silico and in vivo by using a conserved RNA structural motif. J Biol Chem. 1999 Dec 31;274(53):38147-54. [PubMed Link Image]
  2. Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed Link Image]
  3. Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed Link Image]
Target 2 Drug References
  1. Kim HY, Gladyshev VN: Alternative first exon splicing regulates subcellular distribution of methionine sulfoxide reductases. BMC Mol Biol. 2006 Mar 16;7:11. [PubMed Link Image]
  2. Kim HY, Fomenko DE, Yoon YE, Gladyshev VN: Catalytic advantages provided by selenocysteine in methionine-S-sulfoxide reductases. Biochemistry. 2006 Nov 21;45(46):13697-704. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 334
Target 3 Name S-adenosylmethionine synthetase isoform type-2
Target 3 Synonyms
  1. AdoMet synthetase 2
  2. EC 2.5.1.6
  3. MAT-II
  4. Methionine adenosyltransferase 2
  5. Methionine adenosyltransferase II
Target 3 Gene Name MAT2A
Target 3 Protein Sequence >S-adenosylmethionine synthetase isoform type-2 
MNGQLNGFHEAFIEEGTFLFTSESVGEGHPDKICDQISDAVLDAHLQQDPDAKVACETVA
KTGMILLAGEITSRAAVDYQKVVREAVKHIGYDDSSKGFDYKTCNVLVALEQQSPDIAQG
VHLDRNEEDIGAGDQGLMFGYATDETEECMPLTIVLAHKLNAKLAELRRNGTLPWLRPDS
KTQVTVQYMQDRGAVLPIRVHTIVISVQHDEEVCLDEMRDALKEKVIKAVVPAKYLDEDT
IYHLQPSGRFVIGGPQGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARW
VAKSLVKGGLCRRVLVQVSYAIGVSHPLSISIFHYGTSQKSERELLEIVKKNFDLRPGVI
VRDLDLKKPIYQRTAAYGHFGRDSFPWEVPKKLKY
Target 3 Number of Residues 401
Target 3 Molecular Weight 43661
Target 3 Theoretical pI 6.45
Target 3 GO Classification
Function
binding
nucleotide binding
purine nucleotide binding
adenyl nucleotide binding
ATP binding
catalytic activity
transferase activity
transferase activity, transferring alkyl or aryl (other than methyl) groups
methionine adenosyltransferase activity
Process
physiological process
metabolism
cellular metabolism
one-carbon compound metabolism
Component
Not Available
Target 3 General Function Coenzyme transport and metabolism
Target 3 Specific Function Catalyzes the formation of S-adenosylmethionine from methionine and ATP
Target 3 Pathways
Name SMPDB Link KEGG Link
Methionine metabolism SMP00033 Link Image map00271 Link Image
Selenoamino acid metabolism SMP00029 Link Image map00450 Link Image
Target 3 Reactions
  • ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine
Target 3 Pfam Domain Function
Target 3 Signals
  • None
Target 3 Transmembrane Regions
  • None
Target 3 Essentiality Non-Essential
Target 3 GenBank ID Protein 36327 Link Image
Target 3 UniProtKB/Swiss-Prot ID P31153 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name METK2_HUMAN Link Image
Target 3 PDB ID Not Available
Target 3 Cellular Location Not Available
Target 3 Gene Sequence >1188 bp 
ATGAACGGACAGCTCAACGGCTTCCACGAGGCGTTCATCGAGGAGGGCACATTCCTTTTC
ACCTCAGAGTCGGTCGGGGAAGGCCACCCAGATAAGATTTGTGACCAAATCAGTGATGCT
GTCCTTGATGCCCACCTTCAGCAGGATCCTGATGCCAAAGTAGCTTGTGAAACTGTTGCT
AAAACTGGAATGATCCTTCTTGCTGGGGAAATTACATCCAGAGCTGCTGTTGACTACCAG
AAAGTGGTTCGTGAAGCTGTTAAACACATTGGATATGATGATTCTTCCAAAGGTTTTGAC
TACAAGACTTGTAACGTGCTGGTAGCCTTGGAGCAACAGTCACCAGATATTGCTCAAGGT
GTTCATCTTGACAGAAATGAAGAAGACATTGGTGCTGGAGACCAGGGCTTAATGTTTGGC
TATGCCACTGATGAAACTGAGGAGTGTATGCCTTTAACCATTGTCTTGGCACACAAGCTA
AATGCCAAACTGGCAGAACTACGCCGTAATGGCACTTTGCCTTGGTTACGCCCTGATTCT
AAAACTCAAGTTACTGTGCAGTATATGCAGGATCGAGGTGCTGTGCTTCCCATCAGAGTC
CACACAATTGTTATATCTGTTCAGCATGATGAAGAGGTTTGTCTTGATGAAATGAGGGAT
GCCCTAAAGGAGAAAGTCATCAAAGCAGTTGTGCCTGCGAAATACCTTGATGAGGATACA
ATCTACCACCTACAGCCAAGTGGCAGATTTGTTATTGGTGGGCCTCAGGGTGATGCTGGT
TTGACTGGACGGAAAATCATTGTGGACACTTATGGCGGTTGGGGTGCTCATGGAGGAGGT
GCCTTTTCAGGAAAGGATTATACCAAGGTCGACCGTTCAGCTGCTTATGCTGCTCGTTGG
GTGGCAAAATCCCTTGTTAAAGGAGGTCTGTGCCGGAGGGTTCTTGTTCAGGTCTCTTAT
GCTATTGGAGTTTCTCATCCATTATCTATCTCCATTTTCCATTATGGTACCTCTCAGAAG
AGTGAGAGAGAGCTATTAGAGATTGTGAAGAAGAATTTCGATCTCCGCCCTGGGGTCATT
GTCAGGGATCTGGATCTGAAGAAGCCAATTTATCAGAGGACTGCAGCCTATGGCCACTTT
GGTAGGGACAGCTTCCCATGGGAAGTGCCCAAAAAGCTTAAATATTGA
Target 3 GenBank Gene ID
Target 3 GeneCard ID MAT2A Link Image
Target 3 GenAtlas ID MAT2A Link Image
Target 3 HGNC ID HGNC:6904 Link Image
Target 3 Chromosome Location 2
Target 3 Locus 2p11.2
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Horikawa S, Tsukada K: Molecular cloning and developmental expression of a human kidney S-adenosylmethionine synthetase. FEBS Lett. 1992 Nov 2;312(1):37-41. [PubMed Link Image]
Target 3 Drug References
  1. Lin WC, Lin WL: Ameliorative effect of Ganoderma lucidum on carbon tetrachloride-induced liver fibrosis in rats. World J Gastroenterol. 2006 Jan 14;12(2):265-70. [PubMed Link Image]
  2. Yang H, Magilnick N, Noureddin M, Mato JM, Lu SC: Effect of hepatocyte growth factor on methionine adenosyltransferase genes and growth is cell density-dependent in HepG2 cells. J Cell Physiol. 2007 Mar;210(3):766-73. [PubMed Link Image]
  3. Rodriguez JL, Boukaba A, Sandoval J, Georgieva EI, Latasa MU, Garcia-Trevijano ER, Serviddio G, Nakamura T, Avila MA, Sastre J, Torres L, Mato JM, Lopez-Rodas G: Transcription of the MAT2A gene, coding for methionine adenosyltransferase, is up-regulated by E2F and Sp1 at a chromatin level during proliferation of liver cells. Int J Biochem Cell Biol. 2007;39(4):842-50. Epub 2007 Jan 20. [PubMed Link Image]
  4. Chen H, Xia M, Lin M, Yang H, Kuhlenkamp J, Li T, Sodir NM, Chen YH, Josef-Lenz H, Laird PW, Clarke S, Mato JM, Lu SC: Role of methionine adenosyltransferase 2A and S-adenosylmethionine in mitogen-induced growth of human colon cancer cells. Gastroenterology. 2007 Jul;133(1):207-18. Epub 2007 Apr 11. [PubMed Link Image]
Drug Target 4 [top]
Target 4 ID 453
Target 4 Name S-adenosylmethionine synthetase isoform type-1
Target 4 Synonyms
  1. AdoMet synthetase 1
  2. EC 2.5.1.6
  3. MAT-I/III
  4. Methionine adenosyltransferase 1
  5. Methionine adenosyltransferase I/III
Target 4 Gene Name MAT1A
Target 4 Protein Sequence >S-adenosylmethionine synthetase isoform type-1 
MNGPVDGLCDHSLSEGVFMFTSESVGEGHPDKICDQISDAVLDAHLKQDPNAKVACETVC
KTGMVLLCGEITSMAMVDYQRVVRDTIKHIGYDDSAKGFDFKTCNVLVALEQQSPDIAQC
VHLDRNEEDVGAGDQGLMFGYATDETEECMPLTIILAHKLNARMADLRRSGLLPWLRPDS
KTQVTVQYMQDNGAVIPVRIHTIVISVQHNEDITLEEMRRALKEQVIRAVVPAKYLDEDT
VYHLQPSGRFVIGGPQGDAGVTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARW
VAKSLVKAGLCRRVLVQVSYAIGVAEPLSISIFTYGTSQKTERELLDVVHKNFDLRPGVI
VRDLDLKKPIYQKTACYGHFGRSEFPWEVPRKLVF
Target 4 Number of Residues 401
Target 4 Molecular Weight 43648
Target 4 Theoretical pI 6.24
Target 4 GO Classification
Function
binding
nucleotide binding
purine nucleotide binding
adenyl nucleotide binding
ATP binding
catalytic activity
transferase activity
transferase activity, transferring alkyl or aryl (other than methyl) groups
methionine adenosyltransferase activity
Process
physiological process
metabolism
cellular metabolism
one-carbon compound metabolism
Component
Not Available
Target 4 General Function Coenzyme transport and metabolism
Target 4 Specific Function Catalyzes the formation of S-adenosylmethionine from methionine and ATP
Target 4 Pathways
Name SMPDB Link KEGG Link
Methionine metabolism SMP00033 Link Image map00271 Link Image
Selenoamino acid metabolism SMP00029 Link Image map00450 Link Image
Target 4 Reactions
  • ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine
Target 4 Pfam Domain Function
Target 4 Signals
  • None
Target 4 Transmembrane Regions
  • None
Target 4 Essentiality Non-Essential
Target 4 GenBank ID Protein 220066 Link Image
Target 4 UniProtKB/Swiss-Prot ID Q00266 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name METK1_HUMAN Link Image
Target 4 PDB ID 1O9T Link Image
Target 4 PDB File Show
Target 4 3D Structure
Target 4 Cellular Location Not Available
Target 4 Gene Sequence >1188 bp 
ATGAATGGACCGGTGGATGGCTTGTGTGACCACTCTCTAAGTGAAGGAGTCTTCATGTTC
ACATCGGAGTCTGTGGGAGAGGGACACCCGGATAAGATCTGTGACCAGATCAGTGATGCA
GTGCTGGATGCCCATCTCAAGCAAGACCCCAATGCCAAGGTGGCCTGTGAGACAGTGTGC
AAGACCGGCATGGTGCTGCTGTGTGGTGAGATCACCTCAATGGCCATGGTGGACTACCAG
CGGGTGGTGAGGGACACCATCAAGCACATCGGCTACGATGACTCAGCCAAGGGCTTTGAC
TTCAAGACTTGCAACGTGCTGGTGGCTTTGGAGCAGCAATCCCCAGATATTGCCCAGTGC
GTCCATCTGGACAGAAATGAGGAGGATGTGGGGGCAGGAGATCAGGGTTTGATGTTCGGC
TATGCCACCGACGAGACAGAGGAGTGCATGCCCCTCACCATCATCCTTGCTCACAAGCTC
AACGCCCGGATGGCAGACCTCAGGCGCTCCGGCCTCCTCCCCTGGCTGCGGCCTGACTCT
AAGACTCAGGTGACAGTTCAGTACATGCAGGACAATGGCGCAGTCATCCCTGTGCGCATC
CACACCATCGTCATCTCTGTGCAGCACAACGAAGACATCACGCTGGAGGAGATGCGCAGG
GCCCTGAAGGAGCAAGTCATCAGGGCCGTGGTGCCGGCCAAGTACCTGGACGAAGACACC
GTCTACCACCTGCAGCCCAGTGGGCGGTTTGTCATCGGAGGTCCCCAGGGGGATGCGGGT
GTCACTGGCCGTAAGATTATTGTGGACACCTATGCGGCCTGGGGGGCTCATGGTGGTGGG
GCCTTCTCTGGGAAGGACTACACCAAGGTGGACCGCTCAGCCGCATATGCTGCCCGCTGG
GTGGCCAAGTCTCTGGTGAAAGCAGGGCTCTGCCGGAGAGTGCTTGTCCAGGTTTCCTAT
GCCATTGGTGTGGCCGAGCCGCTGTCCATTTCCATCTTCACCTACGGAACCTCTCAGAAG
ACAGAGCGAGAGCTGCTGGATGTGGTGCATAAGAACTTCGACCTCCGGCCGGGCGTCATT
GTCAGGGACTTGGATTTGAAGAAGCCCATCTACCAGAAGACAGCATGCTACGGCCATTTC
GGAAGAAGCGAGTTCCCATGGGAGGTTCCCAGGAAGCTTGTATTTTAG
Target 4 GenBank Gene ID
Target 4 GeneCard ID MAT1A Link Image
Target 4 GenAtlas ID MAT1A Link Image
Target 4 HGNC ID HGNC:6903 Link Image
Target 4 Chromosome Location 10
Target 4 Locus 10q22
Target 4 SNPs SNPJam Report Link Image
Target 4 General References
  1. Chamberlin ME, Ubagai T, Mudd SH, Thomas J, Pao VY, Nguyen TK, Levy HL, Greene C, Freehauf C, Chou JY: Methionine adenosyltransferase I/III deficiency: novel mutations and clinical variations. Am J Hum Genet. 2000 Feb;66(2):347-55. [PubMed Link Image]
  2. Horikawa S, Tsukada K: Molecular cloning and nucleotide sequence of cDNA encoding the human liver S-adenosylmethionine synthetase. Biochem Int. 1991 Sep;25(1):81-90. [PubMed Link Image]
  3. Ubagai T, Lei KJ, Huang S, Mudd SH, Levy HL, Chou JY: Molecular mechanisms of an inborn error of methionine pathway. Methionine adenosyltransferase deficiency. J Clin Invest. 1995 Oct;96(4):1943-7. [PubMed Link Image]
  4. Alvarez L, Corrales F, Martin-Duce A, Mato JM: Characterization of a full-length cDNA encoding human liver S-adenosylmethionine synthetase: tissue-specific gene expression and mRNA levels in hepatopathies. Biochem J. 1993 Jul 15;293 ( Pt 2):481-6. [PubMed Link Image]
  5. Chamberlin ME, Ubagai T, Mudd SH, Wilson WG, Leonard JV, Chou JY: Demyelination of the brain is associated with methionine adenosyltransferase I/III deficiency. J Clin Invest. 1996 Aug 15;98(4):1021-7. [PubMed Link Image]
  6. Chamberlin ME, Ubagai T, Mudd SH, Levy HL, Chou JY: Dominant inheritance of isolated hypermethioninemia is associated with a mutation in the human methionine adenosyltransferase 1A gene. Am J Hum Genet. 1997 Mar;60(3):540-6. [PubMed Link Image]
Target 4 Drug References
  1. Linnebank M, Lagler F, Muntau AC, Roschinger W, Olgemoller B, Fowler B, Koch HG: Methionine adenosyltransferase (MAT) I/III deficiency with concurrent hyperhomocysteinaemia: two novel cases. J Inherit Metab Dis. 2005;28(6):1167-8. [PubMed Link Image]
  2. Prudova A, Bauman Z, Braun A, Vitvitsky V, Lu SC, Banerjee R: S-adenosylmethionine stabilizes cystathionine beta-synthase and modulates redox capacity. Proc Natl Acad Sci U S A. 2006 Apr 25;103(17):6489-94. Epub 2006 Apr 13. [PubMed Link Image]
  3. Yang H, Magilnick N, Noureddin M, Mato JM, Lu SC: Effect of hepatocyte growth factor on methionine adenosyltransferase genes and growth is cell density-dependent in HepG2 cells. J Cell Physiol. 2007 Mar;210(3):766-73. [PubMed Link Image]
  4. Rodriguez JL, Boukaba A, Sandoval J, Georgieva EI, Latasa MU, Garcia-Trevijano ER, Serviddio G, Nakamura T, Avila MA, Sastre J, Torres L, Mato JM, Lopez-Rodas G: Transcription of the MAT2A gene, coding for methionine adenosyltransferase, is up-regulated by E2F and Sp1 at a chromatin level during proliferation of liver cells. Int J Biochem Cell Biol. 2007;39(4):842-50. Epub 2007 Jan 20. [PubMed Link Image]
  5. Chen H, Xia M, Lin M, Yang H, Kuhlenkamp J, Li T, Sodir NM, Chen YH, Josef-Lenz H, Laird PW, Clarke S, Mato JM, Lu SC: Role of methionine adenosyltransferase 2A and S-adenosylmethionine in mitogen-induced growth of human colon cancer cells. Gastroenterology. 2007 Jul;133(1):207-18. Epub 2007 Apr 11. [PubMed Link Image]
Drug Target 5 [top]
Target 5 ID 480
Target 5 Name Methionine-R-sulfoxide reductase B2
Target 5 Synonyms
  1. EC 1.8.4.-
Target 5 Gene Name MSRB2
Target 5 Protein Sequence >Methionine-R-sulfoxide reductase B2 
MGAGAETGRGQRAAAPERRHGRLLWLLRGLTLGTAPRRAVRGQAGGGGPGTAGIVGEAGS
LATCELPLAKSEWQKKLTPEQFYVTREKGTEPPFSGIYLNNKEAGMYHCVCCDSPLFSSE
KKYCSGTGWPSFSEAHGTSGSDESHTGILRRLDTSLGSARTEVVCKQCEAHLGHVFPDGP
GPNGQRFCINSVALKFKPRKH
Target 5 Number of Residues 204
Target 5 Molecular Weight 21468
Target 5 Theoretical pI 9.16
Target 5 GO Classification Not Available
Target 5 General Function Posttranslational modification, protein turnover, chaperones
Target 5 Specific Function Not Available
Target 5 Pathways Not Available
Target 5 Reactions Not Available
Target 5 Pfam Domain Function
Target 5 Signals
  • None
Target 5 Transmembrane Regions
  • None
Target 5 Essentiality Non-Essential
Target 5 GenBank ID Protein 4929731 Link Image
Target 5 UniProtKB/Swiss-Prot ID Q9Y3D2 Link Image
Target 5 UniProtKB/Swiss-Prot Entry Name MSRB2_HUMAN Link Image
Target 5 PDB ID Not Available
Target 5 Cellular Location Not Available
Target 5 Gene Sequence >606 bp 
ATGGGAGCAGGGGCAGAGACGGGCAGAGGGCAGAGGGCGGCAGCGCCGGAGCGGCGTCAT
GGCCGGCTCCTCTGGTTGCTCCGGGGCCTGACCCTCGGAACTGCGCCTCGGCGGGCGGTG
CGGGGCCAAGCGGGCGGCGGCGGGCCCGGCACCGCGGGGATCGTGGGGGAGGCAGGGTCT
CTTGCAACGTGTGAGCTGCCTCTTGCCAAGAGTGAGTGGCAAAAGAAACTAACCCCGGAG
CAGTTCTACGTCACAAGAGAAAAGGGAACGGAACCGCCTTTCAGTGGGATCTACCTGAAT
AACAAGGAAGCAGGAATGTATCATTGCGTGTGCTGCGACAGTCCACTCTTCAGTTCTGAG
AAAAAGTACTGCTCTGGCACTGGGTGGCCTTCGTTTTCTGAGGCTCATGGTACGTCTGGC
TCTGATGAAAGCCACACAGGGATCCTGAGACGTCTGGATACCTCGTTAGGATCAGCTCGC
ACAGAGGTTGTCTGCAAGCAGTGTGAAGCTCATCTAGGTCACGTGTTTCCTGATGGACCT
GGGCCCAATGGTCAGAGGTTTTGCATCAACAGTGTGGCTTTGAAGTTCAAACCAAGGAAA
CACTGA
Target 5 GenBank Gene ID
Target 5 GeneCard ID MSRB2 Link Image
Target 5 GenAtlas ID MSRB2 Link Image
Target 5 HGNC ID HGNC:17061 Link Image
Target 5 Chromosome Location 10
Target 5 Locus 10p12
Target 5 SNPs SNPJam Report Link Image
Target 5 General References
  1. Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W: Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. Genome Res. 2000 May;10(5):703-13. [PubMed Link Image]
Target 5 Drug References
  1. Schallreuter KU, Rubsam K, Chavan B, Zothner C, Gillbro JM, Spencer JD, Wood JM: Functioning methionine sulfoxide reductases A and B are present in human epidermal melanocytes in the cytosol and in the nucleus. Biochem Biophys Res Commun. 2006 Mar 31;342(1):145-52. Epub 2006 Feb 3. [PubMed Link Image]
  2. Ranaivoson FM, Kauffmann B, Neiers F, Wu J, Boschi-Muller S, Panjikar S, Aubry A, Branlant G, Favier F: The X-ray structure of the N-terminal domain of PILB from Neisseria meningitidis reveals a thioredoxin-fold. J Mol Biol. 2006 Apr 28;358(2):443-54. Epub 2006 Feb 28. [PubMed Link Image]
Drug Target 6 [top]
Target 6 ID 600
Target 6 Name Methionyl-tRNA synthetase, cytoplasmic
Target 6 Synonyms
  1. EC 6.1.1.10
  2. MetRS
  3. Methionine--tRNA ligase
Target 6 Gene Name MARS
Target 6 Protein Sequence >Methionyl-tRNA synthetase 
MRLFVSDGVPGCLPVLAAAGRARGRAEVLISTVGPEDCVVPFLTRPKVPVLQLDSGNYLF
STSAICRYFFLLSGWEQDDLTNQWLEWEATELQPALSAALYYLVVQGKKGEDVLGSVRRA
LTHIDHSLSRQNCPFLAGETESLADIVLWGALYPLLQDPAYLPEELSALHSWFQTLSTQE
PCQRAAETVLKQQGVLALRPYLQKQPQPSPAEGRAVTNEPEEEELATLSEEEIAMAVTAW
EKGLESLPPLRPQQNPVLPVAGERNVLITSALPYVNNVPHLGNIIGCVLSADVFARYSRL
RQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKYHIIHADIYRWFNISFDIFGRTTTP
QQTKITQDIFQQLLKRGFVLQDTVEQLRCEHCARFLADRFVEGVCPFCGYEEARGDQCDK
CGKLINAVELKKPQCKVCRSCPVVQSSQHLFLDLPKLEKRLEEWLGRTLPGSDWTPNAQF
ITRSWLRDGLKPRCITRDLKWGTPVPLEGFEDKVFYVWFDATIGYLSITANYTDQWERWW
KNPEQVDLYQFMAKDNVPFHSLVFPCSALGAEDNYTLVSHLIATEYLNYEDGKFSKSRGV
GVFGDMAQDTGIPADIWRFYLLYIRPEGQDSAFSWTDLLLKNNSELLNNLGNFINRAGMF
VSKFFGGYVPEMVLTPDDQRLLAHVTLELQHYHQLLEKVRIRDALRSILTISRHGNQYIQ
VNEPWKRIKGSEADRQRAGTVTGLAVNIAALLSVMLQPYMPTVSATIQAQLQLPPPACSI
LLTNFLCTLPAGHQIGTVSPLFQKLENDQIESLRQRFGGGQAKTSPKPAVVETVTTAKPQ
QIQALMDEVTKQGNIVRELKAQKADKNEVAAEVAKLLDLKKQLAVAEGKPPEAPKGKKKK
Target 6 Number of Residues 915
Target 6 Molecular Weight 101117
Target 6 Theoretical pI 6.05
Target 6 GO Classification
Function
methionine-tRNA ligase activity
binding
nucleotide binding
purine nucleotide binding
adenyl nucleotide binding
ATP binding
catalytic activity
ligase activity
ligase activity, forming phosphoric ester bonds
RNA ligase activity
tRNA ligase activity
Process
methionyl-tRNA aminoacylation
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
RNA metabolism
tRNA metabolism
tRNA aminoacylation
tRNA aminoacylation for protein translation
Component
Not Available
Target 6 General Function Translation, ribosomal structure and biogenesis
Target 6 Specific Function Not Available
Target 6 Pathways
Name SMPDB Link KEGG Link
Aminoacyl-tRNA biosynthesis map00970 Link Image
Methionine metabolism SMP00033 Link Image map00271 Link Image
Selenoamino acid metabolism SMP00029 Link Image map00450 Link Image
Target 6 Reactions
  • ATP + L-methionine + tRNAMet = AMP + diphosphate + L-methionyl-tRNAMet
Target 6 Pfam Domain Function
Target 6 Signals
  • None
Target 6 Transmembrane Regions
  • None
Target 6 Essentiality Non-Essential
Target 6 GenBank ID Protein 1702932 Link Image
Target 6 UniProtKB/Swiss-Prot ID P56192 Link Image
Target 6 UniProtKB/Swiss-Prot Entry Name SYM_HUMAN Link Image
Target 6 PDB ID Not Available
Target 6 Cellular Location
  • Cytoplasm (Probable)
Target 6 Gene Sequence >2703 bp 
ATGAGACTGTTCGTGAGTGATGGCGTCCCGGGTTGCTTGCCGGTGCTGGCCGCCGCCGGG
AGAGCCCGGGGCAGAGCAGAGGTGCTGATCAGCACTGTAGGCCCGGAAGATTGTGTGGTC
CCGTTCCTGACCCGGCCTAAGGTCCCTGTCTTGCAGGTGGATAGCGGCAACTACCTCTTC
TCCACTAGTGCAATCTGCCGATATTTTTTTTTGTTATCTGGCTGGGAGCAAGATGACCTC
ACTAACCAGTGGCTGGAATGGGAAGCGACAGAGCTGCAGCCAGCTTTGTCTGCTCCCCTG
TACTATTTAGTGGTCCAAGGCAAGAAGGGGGAAGATGTTCTTGGTTCAGTGCGGAGAGCC
CTGACTCACATTGACCACAGCTTGAGTCGTCAGAACTGTCCTTTCCTGGCTGGGGAGACA
GAATCTCTAGCCGACATTGTTTTGTGGGGAGCCCAATACCCATTACTGCAAGATCCCGCC
TACCTCCCTGAGGAGCTGAGTGCCCTGCACAGCTGGTTCCAGACACTGAGTACCCAGGAA
CCATGTCAGCGAGCTGCAGAGACTGTACTGAAACAGCAAGGTGTCCTGGCTCTCCGGCCT
TACCTCCAAAAGCAGCCCCAGCCCAGCCCCGCTGAGGGAAGGGCTGTCACCAATGAGCCT
GAGGAGGAGGAGCTGGCTACCCTATCTGAGGAGGAGATTGCTATGGCTGTTACTGCTTGG
GAGAAGGGCCTAGAAAGTTTGCCCCCGCTGCGGCCCCAGCAGAATCCAGTGTTGCCTGTG
GCTGGAGAAAGGAATGTGCTCATCACCAGTGCCCTCCCTTACGTCAACAATGTCCCCCAC
CTTGGGAACATCATTGGTTGTGTGCTCAGTGCCGATGTCTTTGCCAGGTACTCTCGCCTC
CGCCAGTGGAACACCCTCTATCTGTGTGGGACAGATGAGTATGGTACAGCAACAGAGACC
AAGGCTCTGGAGGAGGGACTAACCCCCCAGGAGATCTGCGACAAGTACCACATCATCCAT
GCTGACATCTACCGCTGGTTTAACATTTCGTTTGATATTTTTGGTCGCACCACCACTCCA
CAGCAGACCAAAATCACCCAGGACATTTTCCAGCAGTTGCTGAAACGAGGTTTTGTGCTG
CAAGATACTGTGGAGCAACTGCGATGTGAGCACTGTGCTCGCTTCCTGGCTGACCGCTTC
GTGGAGGGCGTGTGTCCCTTCTGTGGCTATGAGGAGGCTCGGGGTGACCAGTGTGACAAG
TGTGGCAAGCTCATCAATGCTGTCGAGCTTAAGAAGCCTCAGTGTAAAGTCTGCCGATCA
TGCCCTGTGGTGCAGTCGAGCCAGCACCTGTTTCTGGACCTGCCTAAGCTGGAGAAGCGA
CTGGAGGAGTGGTTGGGGAGGACATTGCCTGGCAGTGACTGGACACCCAATGCCCAGTTT
ATCACCCGTTCTTGGCTTCGGGATGGCCTCAAGCCACGCTGCATAACCCGAGACCTCAAA
TGGGGAACCCCTGTACCCTTAGAAGGTTTTGAAGACAAGGTATTCTATGTCTGGTTTGAT
GCCACTATTGGCTATCTGTCCATCACAGCCAACTACACAGACCAGTGGGAGAGATGGTGG
AAGAACCCAGAGCAAGTGGACCTGTATCAGTTCATGGCCAAAGACAATGTTCCTTTCCAT
AGCTTAGTCTTTCCTTGCTCAGCCCTAGGAGCTGAGGATAACTATACCTTGGTCAGCCAC
CTCATTGCTACAGAGTACCTGAACTATGAGGATGGGAAATTCTCTAAGAGCCGCGGTGTG
GGAGTGTTTGGGGACATGGCCCAGGACACGGGGATCCCTGCTGACATCTGGCGCTTCTAT
CTGCTGTACATTCGGCCTGAGGGCCAGGACAGTGCTTTCTCCTGGACGGACCTGCTGCTG
AAGAATAATTCTGAGCTGCTTAACAACCTGGGCAACTTCATCAACAGAGCTGGGATGTTT
GTGTCTAAGTTCTTTGGGGGCTATGTGCCTGAGATGGTGCTCACCCCTGATGATCAGCGC
CTGCTGGGCCATGTCACCCTGGAGCTCCAGCACTATCACCAGCTACTTGAGAAGGTTCGG
ATCCGGGATGCCTTGCGCAGTATCCTCACCATATCTCGACATGGCAACCAATATATTCAG
GTGAATGAGCCCTGGAAGCGGATTAAAGGCAGTGAGGCTGACAGGCAACGGGCAGGAACA
GTGACTGGCTTGGCAGTGAATATAGCTGCCTTGCTCTCTGTCATGCTTCAGCCTTACATG
CCCACGGTTAGTGCCACAATCCAGGCCCAGCTGCAGCTCCCACCTCCAGCCTGCAGTATC
CTGCTGACAAACTTCCTGTGTACCTTACCAGCAGGACACCAGATTGGCACAGTCAGTCCC
TTGTTCCAAAAATTGGAAAATGACCAGATTGAAAGTTTAAGGCAGCGCTTTGGAGGGGGC
CAGGCAAAAACGTCCCCGAAGCCAGCAGTTGTAGAGACTGTTACAACAGCCAAGCCACAG
CAGATACAAGCGCTGATGGATGAAGTGACAAAACAAGGAAACATTGTCCGAGAACTGAAA
GCACAAAAGGCAGACAAGAACGAGGTTGCTGCGGAGGTGGCGAAACTCTTGGATCTAAAG
AAACAGTTGGCTGTAGCTGAGGGGAAACCCCCTGAAGCCCCTAAAGGCAAGAAGAAAAAG
TAA
Target 6 GenBank Gene ID
Target 6 GeneCard ID MARS Link Image
Target 6 GenAtlas ID MARS Link Image
Target 6 HGNC ID HGNC:6898 Link Image
Target 6 Chromosome Location 12
Target 6 Locus 12q13.2
Target 6 SNPs SNPJam Report Link Image
Target 6 General References
  1. Lage H, Dietel M: Cloning of a human cDNA encoding a protein with high homology to yeast methionyl-tRNA synthetase. Gene. 1996 Oct 31;178(1-2):187-9. [PubMed Link Image]
Target 6 Drug References
  1. Jakubowski H: Pathophysiological consequences of homocysteine excess. J Nutr. 2006 Jun;136(6 Suppl):1741S-1749S. [PubMed Link Image]
  2. Vaughan MD, Sampson PB, Daub E, Honek JF: Investigation of bioisosteric effects on the interaction of substrates/ inhibitors with the methionyl-tRNA synthetase from Escherichia coli. Med Chem. 2005 May;1(3):227-37. [PubMed Link Image]
  3. Chwatko G, Boers GH, Strauss KA, Shih DM, Jakubowski H: Mutations in methylenetetrahydrofolate reductase or cystathionine beta-synthase gene, or a high-methionine diet, increase homocysteine thiolactone levels in humans and mice. FASEB J. 2007 Jun;21(8):1707-13. Epub 2007 Feb 27. [PubMed Link Image]
Drug Target 7 [top]
Target 7 ID 809
Target 7 Name Methionine synthase
Target 7 Synonyms
  1. 5-methyltetrahydrofolate-- homocysteine methyltransferase
  2. EC 2.1.1.13
  3. MS
  4. Methionine synthase, vitamin-B12 dependent
Target 7 Gene Name MTR
Target 7 Protein Sequence >Methionine synthase 
MSPALQDLSQPEGLKKTLRDEINAILQKRIMVLDGGMGTMIQREKLNEEHFRGQEFKDHA
RPLKGNNDILSITQPDVIYQIHKEYLLAGADIIETNTFSSTSIAQADYGLEHLAYRMNMC
SAGVARKAAEEVTLQTGIKRFVAGALGPTNKTLSVSPSVERPDYRNITFDELVEAYQEQA
KGLLDGGVDILLIETIFDTANAKAALFALQNLFEEKYAPRPIFISGTIVDKSGRTLSGQT
GEGFVISVSHGEPLCIGLNCALGAAEMRPFIEIIGKCTTAYVLCYPNAGLPNTFGDYDET
PSMMAKHLKDFAMDGLVNIVGGCCGSTPDHIREIAEAVKNCKPRVPPATAFEGHMLLSGL
EPFRIGPYTNFVNIGERCNVAGSRKFAKLIMAGNYEEALCVAKVQVEMGAQVLDVNMDDG
MLDGPSAMTRFCNLIASEPDIAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEDD
FLEKARKIKKYGAAMVVMAFDEEGQATETDTKIRVCTRAYHLLVKKLGFNPNDIIFDPNI
LTIGTGMEEHNLYAINFIHATKVIKETLPGARISGGLSNLSFSFRGMEAIREAMHGVFLY
HAIKSGMDMGIVNAGNLPVYDDIHKELLQLCEDLIWNKDPEATEKLLRYAQTQGTGGKKV
IQTDEWRNGPVEERLEYALVKGIEKHIIEDTEEARLNQKKYPRPLNIIEGPLMNGMKIVG
DLFGAGKMFLPQVIKSARVMKKAVGHLIPFMEKEREETRVLNGTVEEEDPYQGTIVLATV
KGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILKAALDHKADIIGLSGLITPSLDEM
IFVAKEMERLAIRIPLLIGGATTSKTHTAVKIAPRYSAPVIHVLDASKSVVVCSQLLDEN
LKDEYFEEIMEEYEDIRQDHYESLKERRYLPLSQARKSGFQMDWLSEPHPVKPTFIGTQV
FEDYDLQKLVDYIDWKPFFDVWQLRGKYPNRGFPKIFNDKTVGGEARKVYDDAHNMLNTL
ISQKKLRARGVVGFWPAQSIQDDIHLYAEAAVPQAAEPIATFYGLRQQAEKDSASTEPYY
CLSDFIAPLHSGIRDYLGLFAVACFGVEELSKAYEDDGDDYSSIMVKALGDRLAEAFAEE
LHERVRRELWAYCGSEQLDVADLRRLRYKGIRPAPGYPSQPDHTEKLTMWRLADIEQSTG
IRLTESLAMAPASAVSGLYFSNLKSKYFAVGKISKDQVEDYALRKNISVAEVEKWLGPIL
GYDTD
Target 7 Number of Residues 1286
Target 7 Molecular Weight 140529
Target 7 Theoretical pI 5.27
Target 7 GO Classification
Function
homocysteine S-methyltransferase activity
vitamin binding
cobalamin binding
transferase activity, transferring one-carbon groups
methyltransferase activity
S-methyltransferase activity
methionine synthase activity
catalytic activity
transferase activity
transferase activity, transferring alkyl or aryl (other than methyl) groups
dihydropteroate synthase activity
binding
ion binding
cation binding
transition metal ion binding
cobalt ion binding
Process
amino acid and derivative metabolism
amino acid metabolism
sulfur amino acid metabolism
sulfur amino acid biosynthesis
methionine biosynthesis
physiological process
metabolism
cellular metabolism
aromatic compound metabolism
folic acid and derivative metabolism
folic acid and derivative biosynthesis
Component
cell
intracellular
Target 7 General Function Amino acid transport and metabolism
Target 7 Specific Function Not Available
Target 7 Pathways
Name SMPDB Link KEGG Link
Methionine metabolism SMP00033 Link Image map00271 Link Image
One carbon pool by folate SMP00053 Link Image map00670 Link Image
Target 7 Reactions
  • 5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + L-methionine
Target 7 Pfam Domain Function
Target 7 Signals
  • None
Target 7 Transmembrane Regions
  • None
Target 7 Essentiality Non-Essential
Target 7 GenBank ID Protein 1923221 Link Image
Target 7 UniProtKB/Swiss-Prot ID Q99707 Link Image
Target 7 UniProtKB/Swiss-Prot Entry Name METH_HUMAN Link Image
Target 7 PDB ID Not Available
Target 7 Cellular Location
  • Cytoplasm
Target 7 Gene Sequence >3798 bp 
ATGTCACCCGCGCTCCAAGACCTGTCGCAACCCGAAGGTCTGAAGAAAACCCTGCGGGAT
GAGATCAATGCCATTCTGCAGAAGAGGATTATGGTGCTGGATGGAGGGATGGGGACCATG
ATCCAGCGGGAGAAGCTAAACGAAGAACACTTCCGAGGTCAGGAATTTAAAGATCATGCC
AGGCCGCTGAAAGGCAACAATGACATTTTAAGTATAACTCAGCCTGATGTCATTTACCAA
ATCCATAAGGAATACTTGCTGGCTGGGGCAGATATCATTGAAACAAATACTTTTAGCAGC
ACTAGTATTGCCCAAGCTGACTATGGCCTTGAACACTTGGCCTACCGGATGAACATGTGC
TCTGCAGGAGTGGCCAGAAAAGCTGCCGAGGAGGTAACTCTCCAGACAGGAATTAAGAGG
TTTGTGGCAGGGGCTCTGGGTCCGACTAATAAGACACTCTCTGTGTCCCCATCTGTGGAA
AGGCCGGATTATAGGAACATCACATTTGATGAGCTTGTTGAAGCATACCAAGAGCAGGCC
AAAGGACTTCTGGATGGCGGGGTTGATATCTTACTCATTGAAACTATTTTTGATACTGCC
AATGCCAAGGCAGCCTTGTTTGCACTCCAAAATCTTTTTGAGGAGAAATATGCTCCCCGG
CCTATCTTTATTTCAGGGACGATCGTTGATAAAAGTGGGCGGACTCTTTCCGGACAGACA
GGAGAGGGATTTGTCATCAGCGTGTCTCATGGAGAACCACTCTGCATTGGATTAAATTGT
GCTTTGGGTGCAGCTGAGATGAGACCTTTTATTGAAATAATTGGAAAATGTACAACAGCC
TATGTCCTCTGTTATCCCAATGCAGGTCTTCCCAACACCTTTGGTGACTATGATGAAACG
CCTTCTATGATGGCCAAGCACCTAAAGGATTTTGCTATGGATGGCTTGGTCAATATAGTT
GGAGGATGCTGTGGGTCAACACCAGATCATATCAGGGAAATTGCTGAAGCTGTGAAAAAT
TGTAAGCCTAGAGTTCCACCTGCCACTGCTTTTGAAGGACATATGTTACTGTCTGGTCTA
GAGCCCTTCAGGATTGGACCGTACACCAACTTTGTTAACATTGGAGAGCGCTGTAATGTT
GCAGGATCAAGGAAGTTTGCTAAACTCATCATGGCAGGAAACTATGAAGAAGCCTTGTGT
GTTGCCAAAGTGCAGGTGGAAATGGGAGCCCAGGTGTTGGATGTCAACATGGATGATGGC
ATGCTAGATGGTCCAAGTGCAATGACCAGATTTTGCAACTTAATTGCTTCCGAGCCAGAC
ATCGCAAAGGTACCTTTGTGCATCGACTCCTCCAATTTTGCTGTGATTGAAGCTGGGTTA
AAGTGCTGCCAAGGGAAGTGCATTGTCAATAGCATTAGTCTGAAGGAAGGAGAGGACGAC
TTCTTGGAGAAGGCCAGGAAGATTAAAAAGTATGGAGCTGCTATGGTGGTCATGGCTTTT
GATGAAGAAGGACAGGCAACAGAAACAGACACAAAAATCAGAGTGTGCACCCGGGCCTAC
CATCTGCTTGTGAAAAAACTGGGCTTTAATCCAAATGACATTATTTTTGACCCTAATATC
CTAACCATTGGGACTGGAATGGAGGAACACAACTTGTATGCCATTAATTTTATCCATGCA
ACAAAAGTCATTAAAGAAACATTACCTGGAGCCAGAATAAGTGGAGGTCTTTCCAACTTG
TCCTTCTCCTTCCGAGGAATGGAAGCCATTCGAGAAGCAATGCATGGGGTTTTCCTTTAC
CATGCAATCAAGTCTGGCATGGACATGGGGATAGTGAATGCTGGAAACCTCCCTGTGTAT
GATGATATCCATAAGGAACTTCTGCAGCTCTGTGAAGATCTCATCTGGAATAAAGACCCT
GAGGCCACTGAGAAGCTCTTACGTTATGCCCAGACTCAAGGCACAGGAGGGAAGAAAGTC
ATTCAGACTGATGAGTGGAGAAATGGCCCTGTCGAAGAACGCCTTGAGTATGCCCTTGTG
AAGGGCATTGAAAAACATATTATTGAGGATACTGAGGAAGCCAGGTTAAACCAAAAAAAA
TATCCCCGACCTCTCAATATAATTGAAGGACCCCTGATGAATGGAATGAAAATTGTTGGT
GATCTTTTTGGAGCTGGAAAAATGTTTCTACCTCAGGTTATAAAGTCAGCCCGGGTTATG
AAGAAGGCTGTTGGCCACCTTATCCCTTTCATGGAAAAAGAAAGAGAAGAAACCAGAGTG
CTTAACGGCACAGTAGAAGAAGAGGACCCTTACCAGGGCACCATCGTGCTGGCCACTGTT
AAAGGCGACGTGCACGACATAGGCAAGAACATAGTTGGAGTAGTCCTTGGCTGCAATAAT
TTCCGAGTTATTGATTTAGGAGTCATGACTCCATGTGATAAGATACTGAAAGCTGCTCTT
GACCACAAAGCAGATATAATTGGCCTGTCAGGACTCATCACTCCTTCCCTGGATGAAATG
ATTTTTGTTGCCAAGGAAATGGAGAGATTAGCTATAAGGATTCCATTGTTGATTGGAGGA
GCAACCACTTCAAAAACCCACACAGCAGTTAAAATAGCTCCGAGATACAGTGCACCTGTA
ATCCATGTCCTGGACGCGTCCAAGAGTGTGGTGGTGTGTTCCCAGCTGTTAGATGAAAAT
CTAAAGGATGAATACTTTGAGGAAATCATGGAAGAATATGAAGATATTAGACAGGACCAT
TATGAGTCTCTCAAGGAGAGGAGATACTTACCCTTAAGTCAAGCCAGAAAAAGTGGTTTC
CAAATGGATTGGCTGTCTGAACCTCACCCAGTGAAGCCCACGTTTATTGGGACCCAGGTC
TTTGAAGACTATGACCTGCAGAAGCTGGTGGACTACATTGACTGGAAGCCTTTCTTTGAT
GTCTGGCAGCTCCGGGGCAAGTACCCGAATCGAGGCTTCCCCAAGATATTTAACGACAAA
ACAGTAGGTGGAGAGGCCAGGAAGGTCTACGATGATGCCCACAATATGCTGAACACACTG
ATTAGTCAAAAGAAACTCCGGGCCCGGGGTGTGGTTGGGTTCTGGCCAGCACAGAGTATC
CAAGACGACATTCACCTGTACGCAGAGGCTGCTGTGCCCCAGGCTGCAGAGCCCATAGCC
ACTTTCTATGGGTTAAGGCAACAGGCTGAGAAGGACTCTGCCAGCACGGAGCCATACTAC
TGCCTCTCAGACTTCATCGCTCCCTTGCATTCTGGCATCCGTGACTACCTGGGCCTGTTT
GCCGTTGCCTGCTTTGGGGTAGAAGAGCTGAGCAAGGCCTATGAGGATGATGGTGACGAC
TACAGCAGCATCATGGTCAAGGCGCTGGGGGACCGGCTGGCAGAGGCCTTTGCAGAAGAG
CTCCATGAAAGAGTTCGCCGAGAACTGTGGGCCTACTGTGGCAGTGAGCAGCTGGACGTC
GCAGACCTGCGAAGGTTGCGGTACAAGGGCATCCGCCCGGCTCCTGGCTACCCCAGCCAG
CCCGACCACACCGAGAAGCTCACCATGTGGAGACTCGCAGACATCGAGCAGTCTACAGGC
ATTAGGTTAACAGAATCATTAGCAATGGCACCTGCTTCAGCAGTCTCAGGCCTCTACTTC
TCCAATTTGAAGTCCAAATATTTTGCTGTGGGGAAGATTTCCAAGGATCAGGTTGAGGAT
TATGCATTGAGGAAGAACATATCTGTGGCTGAGGTTGAGAAATGGCTTGGACCCATTTTG
GGATATGATACAGACTAA
Target 7 GenBank Gene ID
Target 7 GeneCard ID MTR Link Image
Target 7 GenAtlas ID MTR Link Image
Target 7 HGNC ID HGNC:7468 Link Image
Target 7 Chromosome Location 1
Target 7 Locus 1q43
Target 7 SNPs SNPJam Report Link Image
Target 7 General References
  1. Li YN, Gulati S, Baker PJ, Brody LC, Banerjee R, Kruger WD: Cloning, mapping and RNA analysis of the human methionine synthase gene. Hum Mol Genet. 1996 Dec;5(12):1851-8. [PubMed Link Image]
  2. Gulati S, Baker P, Li YN, Fowler B, Kruger W, Brody LC, Banerjee R: Defects in human methionine synthase in cblG patients. Hum Mol Genet. 1996 Dec;5(12):1859-65. [PubMed Link Image]
  3. Leclerc D, Campeau E, Goyette P, Adjalla CE, Christensen B, Ross M, Eydoux P, Rosenblatt DS, Rozen R, Gravel RA: Human methionine synthase: cDNA cloning and identification of mutations in patients of the cblG complementation group of folate/cobalamin disorders. Hum Mol Genet. 1996 Dec;5(12):1867-74. [PubMed Link Image]
  4. Chen LH, Liu ML, Hwang HY, Chen LS, Korenberg J, Shane B: Human methionine synthase. cDNA cloning, gene localization, and expression. J Biol Chem. 1997 Feb 7;272(6):3628-34. [PubMed Link Image]
Target 7 Drug References
  1. Taurog RE, Matthews RG: Activation of methyltetrahydrofolate by cobalamin-independent methionine synthase. Biochemistry. 2006 Apr 25;45(16):5092-102. [PubMed Link Image]
  2. Hughes JA: In vivo hydrolysis of S-adenosyl-L-methionine in Escherichia coli increases export of 5-methylthioribose. Can J Microbiol. 2006 Jun;52(6):599-602. [PubMed Link Image]
  3. Reynolds E: Vitamin B12, folic acid, and the nervous system. Lancet Neurol. 2006 Nov;5(11):949-60. [PubMed Link Image]
  4. Banks EC, Doughty SW, Toms SM, Wheelhouse RT, Nicolaou A: Inhibition of cobalamin-dependent methionine synthase by substituted benzo-fused heterocycles. FEBS J. 2007 Jan;274(1):287-99. [PubMed Link Image]
  5. Yamada K, Kawata T, Wada M, Mori K, Tamai H, Tanaka N, Tadokoro T, Tobimatsu T, Toraya T, Maekawa A: Testicular injury to rats fed on soybean protein-based vitamin B12-deficient diet can be reduced by methionine supplementation. J Nutr Sci Vitaminol (Tokyo). 2007 Apr;53(2):95-101. [PubMed Link Image]
Drug Target 8 [top]
Target 8 ID 840
Target 8 Name Methionine synthase reductase, mitochondrial
Target 8 Synonyms
  1. EC 1.16.1.8
  2. MSR
  3. Methionine synthase reductase, mitochondrial precursor
Target 8 Gene Name MTRR
Target 8 Protein Sequence >Methionine synthase reductase, mitochondrial precursor 
MGAASVRAGARLVEVALCSFTVTCLEVMRRFLLLYATQQGQAKAIAEEICEQAVVHGFSA
DLHCISESDKYDLKTETAPLVVVVSTTGTGDPPDTARKFVKEIQNQTLPVDFFAHLRYGL
LGLGDSEYTYFCNGGKIIDKRLQELGARHFYDTGHADDCVGLELVVEPWIAGLWPALRKH
FRSSRGQEEISGALPVASPASLRTDLVKSELLHIESQVELLRFDDSGRKDSEVLKQNAVN
SNQSNVVIEDFESSLTRSVPPLSQASLNIPGLPPEYLQVHLQESLGQEESQVSVTSADPV
FQVPISKAVQLTTNDAIKTTLLVELDISNTDFSYQPGDAFSVICPNSDSEVQSLLQRLQL
EDKREHCVLLKIKADTKKKGATLPQHIPAGCSLQFIFTWCLEIRAIPKKAFLRALVDYTS
DSAEKRRLQELCSKQGAADYSRFVRDACACLLDLLLAFPSCQPPLSLLLEHLPKLQPRPY
SCASSSLFHPGKLHFVFNIVEFLSTATTEVLRKGVCTGWLALLVASVLQPNIHASHEDSG
KALAPKISISPRTTNSFHLPDDPSIPIIMVGPGTGIAPFIGFLQHREKLQEQHPDGNFGA
MWLFFGCRHKDRDYLFRKELRHFLKHGILTHLKVSFSRDAPVGEEEAPAKYVQDNIQLHG
QQVARILLQENGHIYVCGDAKNMAKDVHDALVQIISKEVGVEKLEAMKTLATLKEEKRYL
QDIWS
Target 8 Number of Residues 737
Target 8 Molecular Weight 80437
Target 8 Theoretical pI 6.47
Target 8 GO Classification
Function
binding
nucleotide binding
FMN binding
transporter activity
electron transporter activity
catalytic activity
oxidoreductase activity
Process
physiological process
metabolism
cellular metabolism
generation of precursor metabolites and energy
electron transport
Component
Not Available
Target 8 General Function Inorganic ion transport and metabolism
Target 8 Specific Function Involved in the reductive regeneration of cob(I)alamin cofactor required for the maintenance of methionine synthase in a functional state
Target 8 Pathways Not Available
Target 8 Reactions
  • 2 [methionine synthase]-methylcob(I)alamin + 2 S-adenosylhomocysteine + NADP+ = 2 [methionine synthase]-cob(I)alamin + NADPH + H+ + 2 S-adenosyl-L-methionine
Target 8 Pfam Domain Function
Target 8 Signals
  • None
Target 8 Transmembrane Regions
  • None
Target 8 Essentiality Non-Essential
Target 8 GenBank ID Protein 6572540 Link Image
Target 8 UniProtKB/Swiss-Prot ID Q9UBK8 Link Image
Target 8 UniProtKB/Swiss-Prot Entry Name MTRR_HUMAN Link Image
Target 8 PDB ID Not Available
Target 8 Cellular Location
  • Isoform B, isoform C:Cytoplasm. Isoform A:Mitochondrion (Probable)
Target 8 Gene Sequence >2178 bp 
ATGGGCGCTGCGTCAGTGCGCGCTGGCGCAAGGTTGGTGGAAGTCGCGTTGTGCAGTTTC
ACTGTTACATGCCTTGAAGTGATGAGGAGGTTTCTGTTACTATATGCTACACAGCAGGGA
CAGGCAAAGGCCATCGCAGAAGAAATGTGTGAGCAAGCTGTGGTACATGGATTTTCTGCA
GATCTTCACTGTATTAGTGAATCCGATAAGTATGACCTAAAAACCGAAACAGCTCCTCTT
GTTGTTGTGGTTTCTACCACGGGCACCGGAGACCCACCCGACACAGCCCGCAAGTTTGTT
AAGGAAATACAGAACCAAACACTGCCGGTTGATTTCTTTGCTCACCTGCGGTATGGGTTA
CTGGGTCTCGGTGATTCAGAATACACCTACTTTTGCAATGGGGGGAAGATAATTGATAAA
CGACTTCAAGAGCTTGGAGCCCGGCATTTCTATGACACTGGACATGCAGATGACTGTGTA
GGTTTAGAACTTGTGGTTGAGCCGTGGATTGCTGGACTCTGGCCAGCCCTCAGAAAGCAT
TTTAGGTCAAGCAGAGGACAAGAGGAGATAAGTGGCGCACTCCCGGTGGCATCACCTGCA
TCCTTGAGGACAGACCTTGTGAAGTCAGAGCTGCTACACATTGAATCTCAAGTCGAGCTT
CTGAGATTCGATGATTCAGGAAGAAAGGATTCTGAGGTTTTGAAGCAAAATGCAGTGAAC
AGCAACCAATCCAATGTTGTAATTGAAGACTTTGAGTCCTCACTTACCCGTTCGGTACCC
CCACTCTCACAAGCCTCTCTGAATATTCCTGGTTTACCCCCAGAATATTTACAGGTACAT
CTGCAGGAGTCTCTTGGCCAGGAGGAAAGCCAAGTATCTGTGACTTCAGCAGATCCAGTT
TTTCAAGTGCCAATTTCAAAGGCAGTTCAACTTACTACGAATGATGCCATAAAAACCACT
CTGCTGGTAGAATTGGACATTTCAAATACAGACTTTTCCTATCAGCCTGGAGATGCCTTC
AGCGTGATCTGCCCTAACAGTGATTCTGAGGTACAAAGCCTACTCCAAAGACTGCAGCTT
GAAGATAAAAGAGAGCACTGCGTCCTTTTGAAAATAAAGGCAGACACAAAGAAGAAAGGA
GCTACCTTACCCCAGCATATACCTGCGGGATGTTCTCTCCAGTTCATTTTTACCTGGTGT
CTTGAAATCCGAGCAATTCCTAAAAAGGCATTTTTGCGAGCCCTTGTGGACTATACCAGT
GACAGTGCTGAAAAGCGCAGGCTACAGGAGCTGTGCAGTAAACAAGGGGCAGCCGATTAT
AGCCGCTTTGTACGAGATGCCTGTGCCTGCTTGTTGGATCTCCTCCTCGCTTTCCCTTCT
TGCCAGCCACCACTCAGTCTCCTGCTCGAACATCTTCCTAAACTTCAACCCAGACCATAT
TCGTGTGCAAGCTCAAGTTTATTTCACCCAGGAAAGCTCCATTTTGTCTTCAACATTGTG
GAATTTCTGTCTACTGCCACAACAGAGGTTCTGCGGAAGGGAGTATGTACAGGCTGGCTG
GCCTTGTTGGTTGCTTCAGTTCTTCAGCCAAACATACATGCATCCCATGAAGACAGCGGG
AAAGCCCTGGCTCCTAAGATATCCATCTCTCCTCGAACAACAAATTCTTTCCACTTACCA
GATGACCCCTCAATCCCCATCATAATGGTGGGTCCAGGAACCGGCATAGCCCCGTTTATT
GGGTTCCTACAACATAGAGAGAAACTCCAAGAACAACACCCAGATGGAAATTTTGGAGCA
ATGTGGTTGTTTTTTGGCTGCAGGCATAAGGATAGGGATTATCTATTCAGAAAAGAGCTC
AGACATTTCCTTAAGCATGGGATCTTAACTCATCTAAAGGTTTCCTTCTCAAGAGATGCT
CCTGTTGGGGAGGAGGAAGCCCCAGCAAAGTATGTACAAGACAACATCCAGCTTCATGGC
CAGCAGGTGGCGAGAATCCTCCTCCAGGAGAACGGCCATATTTATGTGTGTGGAGATGCA
AAGAATATGGCCAAGGATGTACATGATGCCCTTGTGCAAATAATAAGCAAAGAGGTTGGA
GTTGAAAAACTAGAAGCAATGAAAACCCTGGCCACTTTAAAAGAAGAAAAACGCTACCTT
CAGGATATTTGGTCATAA
Target 8 GenBank Gene ID
Target 8 GeneCard ID MTRR Link Image
Target 8 GenAtlas ID MTRR Link Image
Target 8 HGNC ID HGNC:7473 Link Image
Target 8 Chromosome Location 5
Target 8 Locus 5p15.3-p15.2
Target 8 SNPs SNPJam Report Link Image
Target 8 General References
  1. Wilson A, Platt R, Wu Q, Leclerc D, Christensen B, Yang H, Gravel RA, Rozen R: A common variant in methionine synthase reductase combined with low cobalamin (vitamin B12) increases risk for spina bifida. Mol Genet Metab. 1999 Aug;67(4):317-23. [PubMed Link Image]
  2. Wilson A, Leclerc D, Rosenblatt DS, Gravel RA: Molecular basis for methionine synthase reductase deficiency in patients belonging to the cblE complementation group of disorders in folate/cobalamin metabolism. Hum Mol Genet. 1999 Oct;8(11):2009-16. [PubMed Link Image]
  3. Leclerc D, Odievre M, Wu Q, Wilson A, Huizenga JJ, Rozen R, Scherer SW, Gravel RA: Molecular cloning, expression and physical mapping of the human methionine synthase reductase gene. Gene. 1999 Nov 15;240(1):75-88. [PubMed Link Image]
  4. Leclerc D, Wilson A, Dumas R, Gafuik C, Song D, Watkins D, Heng HH, Rommens JM, Scherer SW, Rosenblatt DS, Gravel RA: Cloning and mapping of a cDNA for methionine synthase reductase, a flavoprotein defective in patients with homocystinuria. Proc Natl Acad Sci U S A. 1998 Mar 17;95(6):3059-64. [PubMed Link Image]
Target 8 Drug References
  1. Kim DJ, Park BL, Koh JM, Kim GS, Kim LH, Cheong HS, Shin HD, Hong JM, Kim TH, Shin HI, Park EK, Kim SY: Methionine synthase reductase polymorphisms are associated with serum osteocalcin levels in postmenopausal women. Exp Mol Med. 2006 Oct 31;38(5):519-24. [PubMed Link Image]
  2. Tvedegaard KC, Rudiger NS, Pedersen BN, Moller J: Detection of MTRR 66A-->G polymorphism using the real-time polymerase chain reaction machine LightCycler for determination of composition of allele after restriction cleavage. Scand J Clin Lab Invest. 2006;66(8):685-93. [PubMed Link Image]
  3. Elmore CL, Wu X, Leclerc D, Watson ED, Bottiglieri T, Krupenko NI, Krupenko SA, Cross JC, Rozen R, Gravel RA, Matthews RG: Metabolic derangement of methionine and folate metabolism in mice deficient in methionine synthase reductase. Mol Genet Metab. 2007 May;91(1):85-97. Epub 2007 Mar 21. [PubMed Link Image]
Drug Target 9 [top]
Target 9 ID 941
Target 9 Name Betaine--homocysteine S-methyltransferase 1
Target 9 Synonyms
  1. EC 2.1.1.5
Target 9 Gene Name BHMT
Target 9 Protein Sequence >Betaine--homocysteine S-methyltransferase 
MPPVGGKKAKKGILERLNAGEIVIGDGGFVFALEKRGYVKAGPWTPEAAVEHPEAVRQLH
REFLRAGSNVMQTFTFYASEDKLENRGNYVLEKISGQEVNEAACDIARQVADEGDALVAG
GVSQTPSYLSCKSETEVKKVFLQQLEVFMKKNVDFLIAEYFEHVEEAVWAVETLIASGKP
VAATMCIGPEGDLHGVPPGECAVRLVKAGASIIGVNCHFDPTISLKTVKLMKEGLEAAQL
KAHLMSQPLAYHTPDCNKQGFIDLPEFPFGLEPRVATRWDIQKYAREAYNLGVRYIGGCC
GFEPYHIRAIAEELAPERGFLPPASEKHGSWGSGLDMHTKPWVRARARKEYWENLRIASG
RPYNPSMSKPDGWGVTKGTAELMQQKEATTEQQLKELFEKQKFKSQ
Target 9 Number of Residues 412
Target 9 Molecular Weight 44971
Target 9 Theoretical pI 6.85
Target 9 GO Classification
Function
catalytic activity
transferase activity
transferase activity, transferring one-carbon groups
methyltransferase activity
S-methyltransferase activity
homocysteine S-methyltransferase activity
Process
Not Available
Component
Not Available
Target 9 General Function Amino acid transport and metabolism
Target 9 Specific Function Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline
Target 9 Pathways
Name SMPDB Link KEGG Link
Glycine, serine and threonine metabolism SMP00004 Link Image map00260 Link Image
Target 9 Reactions
  • trimethylammonioacetate + L-homocysteine = dimethylglycine + L-methionine
Target 9 Pfam Domain Function
Target 9 Signals
  • None
Target 9 Transmembrane Regions
  • None
Target 9 Essentiality Non-Essential
Target 9 GenBank ID Protein 1522683 Link Image
Target 9 UniProtKB/Swiss-Prot ID Q93088 Link Image
Target 9 UniProtKB/Swiss-Prot Entry Name BHMT_HUMAN Link Image
Target 9 PDB ID 1LT8 Link Image
Target 9 PDB File Show
Target 9 3D Structure
Target 9 Cellular Location
  • Cytoplasm
Target 9 Gene Sequence >1221 bp 
ATGCCACCCGTTGGGGGCAAAAAGGCCAAGAAGGGCATCCTAGAACGTTTAAATGCTGGA
GAGATTGTGATTGGAGATGGAGGGTTTGTCTTTGCACTGGAGAAGAGGGGCTACGTAAAG
GCAGGACCCTGGACTCCTGAAGCTGCTGTGGAGCACCCAGAAGCAGTTCGCCAGCTTCAT
CGAGAGTTCCTCAGAGCTGGCTCAAACGTCATGCAGACCTTCACCTTCTATGCGAGTGAA
GACAAGCTGGAGAACAGGGGCAACTATGTCTTAGAGAAGATATCTGGGCAGGAAGTCAAT
GAAGCTGCTTGCGACATCGCCCGACAAGTGGCTGATGAAGGAGATGCTTTGGTAGCAGGA
GGAGTGAGTCAGACACCTTCATACCTTAGCTGCAAGAGTGAAACTGAAGTCAAAAAAGTA
TTTCTGCAACAGTTAGAGGTCTTTATGAAGAAGAACGTGGACTTCTTGATTGCAGAGTAT
TTTGAACACGTTGAAGAAGCTGTGTGGGCAGTTGAAACCTTGATAGCATCCGGTAAACCT
GTGGCAGCAACCATGTGCATTGGCCCAGAAGGAGATTTGCATGGCGTGCCCCCCGGCGAG
TGTGCAGTGCGCCTGGTGAAAGCAGGAGCATCCATCATTGGTGTGAACTGCCACTTTGAC
CCCACCATTAGTTTAAAAACAGTGAAGCTCATGAAGGAGGGCTTGGAGGCTGCCCAACTG
AAAGCTCACCTGATGAGCCAGCCCTTGGCTTACCACACTCCTGACTGCAACAAGCAGGGA
TTCATCGATCTCCCAGAATTCCCATTTGGACTGGAACCCAGAGTTGCCACCAGATGGGAT
ATTCAAAAATACGCCAGAGAGGCCTACAACCTGGGGGTCAGGTACATTGGCGGGTGCTGT
GGATTTGAGCCCTACCACATCAGGGCAATTGCAGAGGAGCTGGCCCCAGAAAGGGGCTTT
TTGCCACCAGCTTCAGAAAAACATGGCAGCTGGGGAAGTGGTTTGGACATGCACACCAAA
CCCTGGGTTAGAGCAAGGGCCAGGAAGGAATACTGGGAGAATCTTCGGATAGCCTCAGGC
CGGCCATACAACCCTTCAATGTCAAAGCCAGATGGCTGGGGAGTGACCAAAGGAACAGCC
GAGCTGATGCAGCAGAAAGAAGCCACAACTGAGCAGCAGCTGAAAGAGCTCTTTGAAAAA
CAAAAATTCAAATCACAGTAG
Target 9 GenBank Gene ID
Target 9 GeneCard ID BHMT Link Image
Target 9 GenAtlas ID BHMT Link Image
Target 9 HGNC ID HGNC:1047 Link Image
Target 9 Chromosome Location 5
Target 9 Locus 5q13.1-q15
Target 9 SNPs SNPJam Report Link Image
Target 9 General References
  1. Park EI, Garrow TA: Interaction between dietary methionine and methyl donor intake on rat liver betaine-homocysteine methyltransferase gene expression and organization of the human gene. J Biol Chem. 1999 Mar 19;274(12):7816-24. [PubMed Link Image]
  2. Weisberg IS, Park E, Ballman KV, Berger P, Nunn M, Suh DS, Breksa AP 3rd, Garrow TA, Rozen R: Investigations of a common genetic variant in betaine-homocysteine methyltransferase (BHMT) in coronary artery disease. Atherosclerosis. 2003 Apr;167(2):205-14. [PubMed Link Image]
  3. Garrow TA: Purification, kinetic properties, and cDNA cloning of mammalian betaine-homocysteine methyltransferase. J Biol Chem. 1996 Sep 13;271(37):22831-8. [PubMed Link Image]
  4. Sunden SL, Renduchintala MS, Park EI, Miklasz SD, Garrow TA: Betaine-homocysteine methyltransferase expression in porcine and human tissues and chromosomal localization of the human gene. Arch Biochem Biophys. 1997 Sep 1;345(1):171-4. [PubMed Link Image]
  5. Millian NS, Garrow TA: Human betaine-homocysteine methyltransferase is a zinc metalloenzyme. Arch Biochem Biophys. 1998 Aug 1;356(1):93-8. [PubMed Link Image]
Target 9 Drug References
  1. Sparks JD, Collins HL, Chirieac DV, Cianci J, Jokinen J, Sowden MP, Galloway CA, Sparks CE: Hepatic very-low-density lipoprotein and apolipoprotein B production are increased following in vivo induction of betaine-homocysteine S-methyltransferase. Biochem J. 2006 Apr 15;395(2):363-71. [PubMed Link Image]
  2. Slow S, Garrow TA: Liver choline dehydrogenase and kidney betaine-homocysteine methyltransferase expression are not affected by methionine or choline intake in growing rats. J Nutr. 2006 Sep;136(9):2279-83. [PubMed Link Image]
  3. Liu J, Xie Y, Cooper R, Ducharme DM, Tennant R, Diwan BA, Waalkes MP: Transplacental exposure to inorganic arsenic at a hepatocarcinogenic dose induces fetal gene expression changes in mice indicative of aberrant estrogen signaling and disrupted steroid metabolism. Toxicol Appl Pharmacol. 2007 May 1;220(3):284-91. Epub 2007 Feb 6. [PubMed Link Image]
  4. Hazra A, Wu K, Kraft P, Fuchs CS, Giovannucci EL, Hunter DJ: Twenty-four non-synonymous polymorphisms in the one-carbon metabolic pathway and risk of colorectal adenoma in the Nurses' Health Study. Carcinogenesis. 2007 Jul;28(7):1510-9. Epub 2007 Mar 26. [PubMed Link Image]
  5. Uthus EO, Reeves PG, Saari JT: Copper deficiency decreases plasma homocysteine in rats. J Nutr. 2007 Jun;137(6):1370-4. [PubMed Link Image]
Drug Target 10 [top]
Target 10 ID 2795
Target 10 Name Methionine aminopeptidase 2
Target 10 Synonyms
  1. EC 3.4.11.18
  2. Initiation factor 2-associated 67 kDa glycoprotein
  3. MetAP 2
  4. Peptidase M 2
  5. p67
  6. p67eIF2
Target 10 Gene Name METAP2
Target 10 Protein Sequence >Methionine aminopeptidase 2 
MAGVEEVAASGSHLNGDLDPDDREEGAASTAEEAAKKKRRKKKKSKGPSAAGEQEPDKES
GASVDEVARQLERSALEDKERDEDDEDGDGDGDGATGKKKKKKKKKRGPKVQTDPPSVPI
CDLYPNGVFPKGQECEYPPTQDGRTAAWRTTSEEKKALDQASEEIWNDFREAAEAHRQVR
KYVMSWIKPGMTMIEICEKLEDCSRKLIKENGLNAGLAFPTGCSLNNCAAHYTPNAGDTT
VLQYDDICKIDFGTHISGRIIDCAFTVTFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDV
GEAIQEVMESYEVEIDGKTYQVKPIRNLNGHSIGQYRIHAGKTVPIVKGGEATRMEEGEV
YAIETFGSTGKGVVHDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINENFGTLAFCRRWL
DRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSRGDDY
Target 10 Number of Residues 485
Target 10 Molecular Weight 52892
Target 10 Theoretical pI 5.57
Target 10 GO Classification
Function
metallopeptidase activity
metalloexopeptidase activity
catalytic activity
hydrolase activity
peptidase activity
exopeptidase activity
aminopeptidase activity
methionyl aminopeptidase activity
Process
physiological process
metabolism
macromolecule metabolism
protein metabolism
cellular protein metabolism
proteolysis
Component
Not Available
Target 10 General Function Translation, ribosomal structure and biogenesis
Target 10 Specific Function Removes the amino-terminal methionine from nascent proteins
Target 10 Pathways Not Available
Target 10 Reactions
  • Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides
Target 10 Pfam Domain Function
Target 10 Signals
  • None
Target 10 Transmembrane Regions
  • None
Target 10 Essentiality Non-Essential
Target 10 GenBank ID Protein 903982 Link Image
Target 10 UniProtKB/Swiss-Prot ID P50579 Link Image
Target 10 UniProtKB/Swiss-Prot Entry Name AMPM2_HUMAN Link Image
Target 10 PDB ID 1B6A Link Image
Target 10 PDB File Show
Target 10 3D Structure
Target 10 Cellular Location
  • Cytoplasmic
Target 10 Gene Sequence >1437 bp 
ATGGCGGGCGTGGAGGAGGTAGCGGCCTCCGGGAGCCACCTGAATGGCGACCTGGATCCA
GACGACAGGGAAGAAGGAGCTGCCTCTACGGCTGAGGAAGCAGCCAAGAAAAAAAGACGA
AAGAAGAAGAAGAGCAAAGGGCCTTCTGCAGCAGGGGAACAGGAACCTGATAAAGAATCA
GGAGCCTCAGTGGATGAAGTAGCAAGACAGTTGGAAAGATCAGCATTGGAAGATAAAGAA
AGAGATGAAGATGATGAAGATGGAGATGGCGATGGAGATGGAGCAACTGGAAAGAAGAAG
AAAAAGAAGAAGAAGAAGAGAGGACCAAAAGTTCAAACAGACCCTCCCTCAGTTCCAATA
TGTGACCTGTATCCTAATGGTGTATTTCCCAAAGGACAAGAATGCGAATACCCACCCACA
CAAGATGGGCGAACAGCTGCTTGGAGAACTACAAGTGAAGAAAAGAAAGCATTAGATCAG
GCAAGTGAAGAGATTTGGAATGATTTTCGAGAAGCTGCAGAAGCACATCGACAAGTTAGA
AAATACGTAATGAGCTGGATCAAGCCTGGGATGACAATGATAGAAATCTGTGAAAAGTTG
GAAGACTGTTCACGCAAGTTAATAAAAGAGAATGGATTAAATGCAGGCCTGGCATTTCCT
ACTGGATGTTCTCTCAATAATTGTGCTGCCCATTATACTCCCAATGCCGGTGACACAACA
GTATTACAGTATGATGACATCTGTAAAATAGACTTTGGAACACATATAAGTGGTAGGATT
ATTGACTGTGCTTTTACTGTCACTTTTAATCCCAAATATGATACGTTATTAAAAGCTGTA
AAAGATGCTACTAACACTGGAATAAAGTGTGCTGGAATTGATGTTCGTCTGTGTGATGTT
GGTGAGGCCATCCAAGAAGTTATGGAGTCCTATGAAGTTGAAATAGATGGGAAGACATAT
CAAGTGAAACCAATCCGTAATCTAAATGGACATTCAATTGGGCAATATAGAATACATGCT
GGAAAAACAGTGCCGATTGTGAAAGGAGGGGAGGCAACAAGAATGGAGGAAGGAGAAGTA
TATGCAATTGAAACCTTTGGTAGTACAGGAAAAGGTGTTGTTCATGATGATATGGAATGT
TCACATTACATGAAAAATTTTGATGTTGGACATGTGCCAATAAGGCTTCCAAGAACAAAA
CACTTGTTAAATGTCATCAATGAAAACTTTGGAACCCTTGCCTTCTGCCGCAGATGGCTG
GATCGCTTGGGAGAAAGTAAATACTTGATGGCTCTGAAGAATCTGTGTGACTTGGGCATT
GTAGATCCATATCCACCATTATGTGACATTAAAGGATCATATACAGCGCAATTTGAACAT
ACCATCCTGTTGCGTCCAACATGTAAAGAAGTTGTCAGCAGAGGAGATGACTATTAA
Target 10 GenBank Gene ID
Target 10 GeneCard ID METAP2 Link Image
Target 10 GenAtlas ID METAP2 Link Image
Target 10 HGNC ID HGNC:16672 Link Image
Target 10 Chromosome Location 12
Target 10 Locus 12q22
Target 10 SNPs SNPJam Report Link Image
Target 10 General References
  1. Arfin SM, Kendall RL, Hall L, Weaver LH, Stewart AE, Matthews BW, Bradshaw RA: Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes. Proc Natl Acad Sci U S A. 1995 Aug 15;92(17):7714-8. [PubMed Link Image]
  2. Li X, Chang YH: Molecular cloning of a human complementary DNA encoding an initiation factor 2-associated protein (p67). Biochim Biophys Acta. 1995 Feb 21;1260(3):333-6. [PubMed Link Image]
  3. Liu S, Widom J, Kemp CW, Crews CM, Clardy J: Structure of human methionine aminopeptidase-2 complexed with fumagillin. Science. 1998 Nov 13;282(5392):1324-7. [PubMed Link Image]
Target 10 Drug References
  1. Nonato MC, Widom J, Clardy J: Human methionine aminopeptidase type 2 in complex with L- and D-methionine. Bioorg Med Chem Lett. 2006 May 15;16(10):2580-3. Epub 2006 Mar 15. [PubMed Link Image]
  2. Sheppard GS, Wang J, Kawai M, Fidanze SD, BaMaung NY, Erickson SA, Barnes DM, Tedrow JS, Kolaczkowski L, Vasudevan A, Park DC, Wang GT, Sanders WJ, Mantei RA, Palazzo F, Tucker-Garcia L, Lou P, Zhang Q, Park CH, Kim KH, Petros A, Olejniczak E, Nettesheim D, Hajduk P, Henkin J, Lesniewski R, Davidsen SK, Bell RL: Discovery and optimization of anthranilic acid sulfonamides as inhibitors of methionine aminopeptidase-2: a structural basis for the reduction of albumin binding. J Med Chem. 2006 Jun 29;49(13):3832-49. [PubMed Link Image]
  3. Addlagatta A, Matthews BW: Structure of the angiogenesis inhibitor ovalicin bound to its noncognate target, human Type 1 methionine aminopeptidase. Protein Sci. 2006 Aug;15(8):1842-8. Epub 2006 Jul 5. [PubMed Link Image]
  4. Upadhya R, Zhang HS, Weiss LM: System for expression of microsporidian methionine amino peptidase type 2 (MetAP2) in the yeast Saccharomyces cerevisiae. Antimicrob Agents Chemother. 2006 Oct;50(10):3389-95. Epub 2006 Aug 17. [PubMed Link Image]
  5. Hu X, Addlagatta A, Lu J, Matthews BW, Liu JO: Elucidation of the function of type 1 human methionine aminopeptidase during cell cycle progression. Proc Natl Acad Sci U S A. 2006 Nov 28;103(48):18148-53. Epub 2006 Nov 17. [PubMed Link Image]
Drug Target 11 [top]
Target 11 ID 3921
Target 11 Name Methionine adenosyltransferase 2 subunit beta
Target 11 Synonyms
  1. DTDP-4-keto-6-deoxy-D-glucose 4- reductase
  2. MAT II beta
  3. Methionine adenosyltransferase 2 beta subunit
  4. Methionine adenosyltransferase II beta
Target 11 Gene Name MAT2B
Target 11 Protein Sequence >Methionine adenosyltransferase 2 subunit beta 
MVGREKELSIHFVPGSCRLVEEEVNIPNRRVLVTGATGLLGRAVHKEFQQNNWHAVGCGF
RRARPKFEQVNLLDSNAVHHIIHDFQPHVIVHCAAERRPDVVENQPDAASQLNVDASGNL
AKEAAAVGAFLIYISSDYVFDGTNPPYREEDIPAPLNLYGKTKLDGEKAVLENNLGAAVL
RIPILYGEVEKLEESAVTVMFDKVQFSNKSANMDHWQQRFPTHVKDVATVCRQLAEKRML
DPSIKGTFHWSGNEQMTKYEMACAIADAFNLPSSHLRPITDSPVLGAQRPRNAQLDCSKL
ETLGIGQRTPFRIGIKESLWPFLIDKRWRQTVFH
Target 11 Number of Residues 339
Target 11 Molecular Weight 37552
Target 11 Theoretical pI 7.39
Target 11 GO Classification
Function
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on CH-OH group of donors
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
dTDP-4-dehydrorhamnose reductase activity
Process
physiological process
metabolism
macromolecule metabolism
macromolecule biosynthesis
carbohydrate biosynthesis
polysaccharide biosynthesis
extracellular polysaccharide biosynthesis
Component
Not Available
Target 11 General Function Cell wall/membrane/envelope biogenesis
Target 11 Specific Function Non-catalytic regulatory subunit of S-adenosylmethionine synthetase 2 (MAT2A), an enzyme that catalyzes the formation of S- adenosylmethionine from methionine and ATP. Regulates the activity of S-adenosylmethionine synthetase 2 by changing its kinetic properties, rendering the enzyme more susceptible to S- adenosylmethionine inhibition
Target 11 Pathways Not Available
Target 11 Reactions Not Available
Target 11 Pfam Domain Function
Target 11 Signals
  • None
Target 11 Transmembrane Regions
  • None
Target 11 Essentiality Non-Essential
Target 11 GenBank ID Protein 6815285 Link Image
Target 11 UniProtKB/Swiss-Prot ID Q9NZL9 Link Image
Target 11 UniProtKB/Swiss-Prot Entry Name MAT2B_HUMAN Link Image
Target 11 PDB ID Not Available
Target 11 Cellular Location Not Available
Target 11 Gene Sequence >1005 bp 
ATGGTGGGGAGGGAGAAAGAACTGTCTATACACTTTGTTCCCGGGAGCTGTCGGCTGGTG
GAGGAGGAAGTTAACATCCCTAATAGGAGGGTTCTGGTTACTGGTGCCACTGGGCTTCTT
GGCAGAGCTGTACACAAAGAATTTCAGCAGAATAATTGGCATGCAGTTGGCTGTGGTTTC
AGAAGAGCAAGACCAAAATTTGAACAGGTTAATCTGTTGGATTCTAATGCAGTTCATCAC
ATCATTCATGATTTTCAGCCCCATGTTATAGTACATTGTGCAGCAGAGAGAAGACCAGAT
GTTGTAGAAAATCAGCCAGATGCTGCCTCTCAACTTAATGTGGATGCTTCTGGGAATTTA
GCAAAGGAAGCAGCTGCTGTTGGAGCATTTCTCATCTACATTAGCTCAGATTATGTATTT
GATGGAACAAATCCACCTTACAGAGAGGAAGACATACCAGCTCCCCTAAATTTGTATGGC
AAAACAAAATTAGATGGAGAAAAGGCTGTCCTGGAGAACAATCTAGGAGCTGCTGTTTTG
AGGATTCCTATTCTGTATGGGGAAGTTGAAAAGCTCGAAGAAAGTGCTGTGACTGTTATG
TTTGATAAAGTGCAGTTCAGCAACAAGTCAGCAAACATGGATCACTGGCAGCAGAGGTTC
CCCACACATGTCAAAGATGTGGCCACTGTGTGCCGGCAGCTAGCAGAGAAGAGAATGCTG
GATCCATCAATTAAGGGAACCTTTCACTGGTCTGGCAATGAACAGATGACTAAGTATGAA
ATGGCATGTGCAATTGCAGATGCCTTCAACCTCCCCAGCAGTCACTTAAGACCTATTACT
GACAGCCCTGTCCTAGGAGCACAACGTCCGAGAAATGCTCAGCTTGACTGCTCCAAATTG
GAGACCTTGGGCATTGGCCAACGAACACCATTTCGAATTGGAATCAAAGAATCACTTTGG
CCTTTCCTCATTGACAAGAGATGGAGACAAACGGTCTTTCATTAG
Target 11 GenBank Gene ID
Target 11 GeneCard ID MAT2B Link Image
Target 11 GenAtlas ID MAT2B Link Image
Target 11 HGNC ID HGNC:6905 Link Image
Target 11 Chromosome Location 5
Target 11 Locus 5q34-q35.1
Target 11 SNPs SNPJam Report Link Image
Target 11 General References
  1. LeGros HL Jr, Halim AB, Geller AM, Kotb M: Cloning, expression, and functional characterization of the beta regulatory subunit of human methionine adenosyltransferase (MAT II). J Biol Chem. 2000 Jan 28;275(4):2359-66. [PubMed Link Image]
  2. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  3. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
Target 11 Drug References
  1. LeGros L, Halim AB, Chamberlin ME, Geller A, Kotb M: Regulation of the human MAT2B gene encoding the regulatory beta subunit of methionine adenosyltransferase, MAT II. J Biol Chem. 2001 Jul 6;276(27):24918-24. Epub 2001 May 3. [PubMed Link Image]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  3. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 12 [top]
Target 12 ID 3995
Target 12 Name Methionyl-tRNA synthetase, mitochondrial
Target 12 Synonyms
  1. EC 6.1.1.10
  2. Methionine--tRNA ligase 2
  3. Methionyl-tRNA synthetase, mitochondrial precursor
  4. Mitochondrial methionine--tRNA ligase
  5. MtMetRS
Target 12 Gene Name MARS2
Target 12 Protein Sequence >Methionyl-tRNA synthetase, mitochondrial 
MLRTSVLRLLGRTGASRLSLLEDFGPRYYSSGSLSAGDDACDVRAYFTTPIFYVNAAPHI
GHLYSALLADALCRHRRLRGPSTAATRFSTGTDEHGLKIQQAAATAGLAPTELCDRVSEQ
FQQLFQEAGISCTDFIRTTEARHRVAVQHFWGVLKSRGLLYKGVYEGWYCASDECFLPEA
KVTQQPGPSGDSFPVSLESGHPVSWTKEENYIFRLSQFRKPLQRWLRGNPQAITPEPFHH
VVLQWLDEELPDLSVSRRSSHLHWGIPVPGDDSQTIYVWLDALVNYLTVIGYPNAEFKSW
WPATSHIIGKDILKFHAIYWPAFLLGAGMSPPQRICVHSHWTVCGQKMSKSLGNVVDPRT
CLNRYTVDGFRYFLLRQGVPNWDCDYYDEKVVKLLNSELADALGGLLNRCTAKRINPSET
YPAFCTTCFPSEPGLVGPSVRAQAEDYALVSAVATLPKQVADHYDNFRIYKALEAVSSCV
RQTNGFVQRHAPWKLNWESPVDAPWLGTVLHVALECLRVFGTLLQPVTPSLADKLLSRLG
VSASERSLGELYFLPRFYGHPCPFEGRRLGPETGLLFPRLDQSRTWLVKAHRT
Target 12 Number of Residues 602
Target 12 Molecular Weight 66591
Target 12 Theoretical pI 8.14
Target 12 GO Classification
Function
methionine-tRNA ligase activity
binding
nucleotide binding
purine nucleotide binding
adenyl nucleotide binding
ATP binding
catalytic activity
ligase activity
ligase activity, forming phosphoric ester bonds
RNA ligase activity
tRNA ligase activity
Process
methionyl-tRNA aminoacylation
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
RNA metabolism
tRNA metabolism
tRNA aminoacylation
tRNA aminoacylation for protein translation
Component
Not Available
Target 12 General Function Translation, ribosomal structure and biogenesis
Target 12 Specific Function ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met)
Target 12 Pathways
Name SMPDB Link KEGG Link
Aminoacyl-tRNA biosynthesis map00271 Link Image
Target 12 Reactions
  • ATP + L-methionine + tRNAMet = AMP + diphosphate + L-methionyl-tRNAMet
Target 12 Pfam Domain Function
Target 12 Signals
  • None
Target 12 Transmembrane Regions
  • None
Target 12 Essentiality Non-Essential
Target 12 GenBank ID Protein 37196758 Link Image
Target 12 UniProtKB/Swiss-Prot ID Q96GW9 Link Image
Target 12 UniProtKB/Swiss-Prot Entry Name SYMM_HUMAN Link Image
Target 12 PDB ID Not Available
Target 12 Cellular Location
  • Mitochondrion
Target 12 Gene Sequence >1782 bp 
ATGCTGCGAACGTCCGTCCTCCGCCTGCTAGGACGCACGGGGGCTAGTAGGCTGTCTCTC
CTGGAGGACTTCGGCCCACGCTACTACAGTTCGGGCTCCCTCAGTGCCGGCGATGATGCT
TGTGATGTGCGCGCCTACTTCACTACACCCATTTTCTACGTGAACGCGGCGCCGCACATC
GGGCACCTGTACTCGGCACTACTGGCGGACGCCCTATGCCGCCACCGTCGCCTCCGAGGT
CCCAGCACGGCCGCCACGCGATTCTCCACTGGTACCGACGAGCACGGGCTGAAGATTCAG
CAGGCAGCAGCTACCGCGGGCCTGGCCCCGACCGAGCTGTGCGACCGAGTCTCTGAGCAG
TTCCAGCAGCTTTTCCAGGAGGCCGGTATCTCCTGCACAGATTTCATCCGCACCACGGAG
GCCCGGCACCGGGTGGCTGTGCAGCACTTCTGGGGGGTGCTTAAGTCCCGCGGTCTGCTC
TACAAGGGCGTCTATGAAGGTTGGTATTGCGCTTCCGACGAGTGCTTCCTGCCTGAGGCC
AAGGTCACCCAGCAGCCGGGCCCATCGGGGGATTCGTTTCCTGTATCTCTCGAGAGCGGG
CATCCAGTCTCCTGGACCAAGGAAGAAAACTACATTTTCAGGCTTTCCCAGTTCCGGAAG
CCACTCCAGCGGTGGCTGCGGGGCAACCCTCAGGCGATCACCCCCGAACCATTTCATCAC
GTAGTTCTTCAGTGGCTGGACGAGGAGCTGCCCGACCTGTCCGTGTCTCGCAGAAGTAGC
CACTTGCACTGGGGCATTCCGGTGCCCGGGGATGATTCGCAGACCATCTATGTATGGCTG
GATGCCCTGGTCAACTACCTCACTGTAATTGGCTACCCAAATGCTGAGTTCAAATCTTGG
TGGCCGGCCACCTCTCATATCATAGGTAAGGACATTCTCAAATTCCATGCCATCTATTGG
CCTGCCTTCCTGTTAGGGGCCGGCATGAGCCCGCCACAGCGCATCTGTGTCCATTCCCAC
TGGACAGTCTGTGGCCAAAAGATGTCCAAGAGCTTGGGCAACGTGGTGGATCCTAGGACT
TGCCTTAACCGCTATACCGTGGATGGCTTCCGCTACTTTCTCCTTCGGCAGGGCGTCCCC
AACTGGGACTGTGACTACTATGATGAAAAGGTGGTTAAGTTGCTGAACTCCGAGCTGGCA
GATGCCTTGGGAGGTCTCTTGAACCGATGCACTGCCAAAAGAATAAATCCTTCTGAGACC
TACCCAGCCTTCTGCACTACCTGCTTCCCTAGTGAGCCAGGGTTGGTGGGGCCGTCAGTT
CGTGCTCAGGCAGAGGATTATGCTCTGGTGAGCGCAGTGGCCACTTTGCCAAAGCAGGTA
GCAGACCACTATGATAACTTTCGGATATATAAGGCTCTGGAGGCCGTGTCCAGCTGTGTC
CGGCAAACTAATGGTTTTGTCCAAAGGCATGCACCATGGAAGCTGAACTGGGAGAGCCCA
GTGGATGCTCCCTGGCTGGGTACTGTGCTTCATGTGGCCTTGGAATGTTTGCGAGTCTTT
GGGACTTTGCTGCAGCCTGTCACCCCAAGCCTAGCTGACAAGATGATGTCTAGGCTGGGG
GTCTCTGCCTCAGAGAGGAGTCTTGGAGAGCTCTATTTCTTGCCTCGATTCTATGGACAT
CCATGCCCTTTTGAAGGGAGGAGGCTGGGACCTGAAACTGGGCTTTTGTTTCCAAGACTA
GACCAGTCCAGGACTTGGCTGGTGAAAGCCCACCGGACCTAG
Target 12 GenBank Gene ID
Target 12 GeneCard ID MARS2 Link Image
Target 12 GenAtlas ID MARS2 Link Image
Target 12 HGNC ID HGNC:25133 Link Image
Target 12 Chromosome Location 2
Target 12 Locus 2q33.1
Target 12 SNPs SNPJam Report Link Image
Target 12 General References Not Available
Target 12 Drug References
  1. Spencer AC, Heck A, Takeuchi N, Watanabe K, Spremulli LL: Characterization of the human mitochondrial methionyl-tRNA synthetase. Biochemistry. 2004 Aug 3;43(30):9743-54. [PubMed Link Image]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  3. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 13 [top]
Target 13 ID 3996
Target 13 Name Betaine--homocysteine S-methyltransferase 2
Target 13 Synonyms
  1. EC 2.1.1.5
Target 13 Gene Name BHMT2
Target 13 Protein Sequence >Betaine--homocysteine S-methyltransferase 2 
MAPAGRPGAKKGILERLESGEVVIGDGSFLITLEKRGYVKAGLWTPEAVIEHPDAVRQLH
MEFLRAGSNVMQTFTFSASEDNMESKWEDVNAAACDLAREVAGKGDALVAGGICQTSIYK
YQKDEARIKKLFRQQLEVFAWKNVDFLIAEYFEHVEEAVWAVEVLKESDRPVAVTMCIGP
EGDMHDITPGECAVRLVKAGASIVGVNCRFGPDTSLKTMELMKEGLEWAGLKAHLMVQPL
GFHAPDCGKEGFVDLPEYPFGLESRVATRWDIQKYAREAYNLGVRYIGGCCGFEPYHIRA
IAEELAPERGFLPPASEKHGSWGSGLDMHTKPWIRARARREYWENLLPASGRPFCPSLSK
PDF
Target 13 Number of Residues 369
Target 13 Molecular Weight 40355
Target 13 Theoretical pI 5.68
Target 13 GO Classification
Function
catalytic activity
transferase activity
transferase activity, transferring one-carbon groups
methyltransferase activity
S-methyltransferase activity
homocysteine S-methyltransferase activity
Process
Not Available
Component
Not Available
Target 13 General Function Amino acid transport and metabolism
Target 13 Specific Function Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline
Target 13 Pathways
Name SMPDB Link KEGG Link
Methionine metabolism map00260 Link Image
Target 13 Reactions
  • trimethylammonioacetate + L-homocysteine = dimethylglycine + L-methionine
Target 13 Pfam Domain Function
Target 13 Signals
  • None
Target 13 Transmembrane Regions
  • None
Target 13 Essentiality Non-Essential
Target 13 GenBank ID Protein 11907831 Link Image
Target 13 UniProtKB/Swiss-Prot ID Q9H2M3 Link Image
Target 13 UniProtKB/Swiss-Prot Entry Name BHMT2_HUMAN Link Image
Target 13 PDB ID Not Available
Target 13 Cellular Location Not Available
Target 13 Gene Sequence >1092 bp 
ATGGCACCTGCTGGACGCCCGGGGGCCAAGAAGGGGATTTTGGAGCGCCTGGAGAGTGGG
GAGGTTGTGATTGGAGATGGCAGCTTTCTCATTACTCTGGAGAAGAGAGGCTATGTGAAG
GCTGGGCTCTGGACTCCAGAGGCAGTGATAGAACACCCAGACGCAGTTCGTCAACTTCAC
ATGGAATTCTTGAGAGCAGGATCAAATGTCATGCAGACTTTTACCTTTTCTGCCAGTGAG
GACAATATGGAAAGCAAGTGGGAAGATGTAAATGCTGCTGCCTGTGACCTCGCCAGGGAA
GTGGCTGGCAAAGGTGATGCTTTGGTAGCAGGGGGGATCTGCCAGACATCAATATACAAA
TACCAGAAGGATGAAGCTAGAATTAAAAAACTTTTTCGACAACAGCTAGAAGTTTTTGCC
TGGAAAAATGTGGACTTCTTGATTGCAGAGTATTTTGAGCACGTTGAAGAAGCTGTGTGG
GCTGTGGAAGTCTTAAAAGAATCAGATAGACCCGTGGCAGTTACCATGTGCATAGGCCCA
GAGGGAGACATGCATGATATAACCCCCGGAGAATGTGCTGTGAGGCTGGTGAAGGCAGGG
GCTTCCATCGTTGGCGTGAACTGCCGCTTTGGGCCCGACACCAGCTTGAAGACGATGGAG
CTCATGAAGGAGGGTCTTGAGTGGGCAGGGCTGAAAGCGCACCTCATGGTGCAGCCTCTG
GGGTTCCACGCGCCTGACTGTGGCAAAGAGGGGTTTGTGGATCTCCCAGAATATCCCTTT
GGACTGGAGTCCAGAGTTGCCACCAGATGGGATATTCAAAAATACGCCAGAGAGGCCTAC
AACCTGGGGGTCAGGTACATTGGCGGGTGCTGTGGATTTGAGCCCTACCACATCAGGGCA
ATTGCAGAGGAGCTGGCCCCAGAAAGGGGCTTTTTGCCACCAGCTTCAGAAAAACACGGC
AGCTGGGGAAGTGGTTTGGACATGCACACCAAACCCTGGATTAGAGCAAGGGCTCGAAGG
GAGTATTGGGAGAATCTGCTGCCAGCTTCAGGCAGACCTTTCTGTCCTTCGCTGTCAAAG
CCAGACTTCTAA
Target 13 GenBank Gene ID
Target 13 GeneCard ID BHMT2 Link Image
Target 13 GenAtlas ID BHMT2 Link Image
Target 13 HGNC ID HGNC:1048 Link Image
Target 13 Chromosome Location 5
Target 13 Locus 5q13
Target 13 SNPs SNPJam Report Link Image
Target 13 General References
  1. Chadwick LH, McCandless SE, Silverman GL, Schwartz S, Westaway D, Nadeau JH: Betaine-homocysteine methyltransferase-2: cDNA cloning, gene sequence, physical mapping, and expression of the human and mouse genes. Genomics. 2000 Nov 15;70(1):66-73. [PubMed Link Image]
Target 13 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]

This project is supported by Genome Alberta & Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government. This project is also supported in part by GenomeQuest, Inc., an enterprise genomic information company serving the life science community.