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Showing drug card for Tetrahydrofolic acid (DB00116)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-04-16 16:47:24
Primary Accession Number DB00116
Secondary Accession Number
  • NUTR00056
Name Tetrahydrofolic acid
Drug Type
  • Approved
  • Nutraceutical
  • Small Molecule
Description Tetrahydrofolic acid is a folic acid derivative. It is produced from dihydrofolic acid by dihydrofolate reductase. It is converted into 5,10-methylenetetrahydrofolate by serine hydroxymethyltransferase. It is a coenzyme in many reactions, especially in the metabolism of amino acids and nucleic acids. It acts as a donor of a group with one carbon atom. It gets this carbon atom by sequestering formaldehyde produced in other processes.
Synonyms
  1. (6S)-tetrahydrofolate
  2. 5,6,7,8-tetrahydrofolate
  3. 5,6,7,8-tetrahydrofolic acid
  4. FH4
  5. H4PteGlu
  6. N-(4-(((2-Amino-1,4,5,6,7,8-hexahydro-4-oxo-6-pteridinyl)methyl)amino)benzoyl)glutamic acid
  7. THF
  8. folate-H4
  9. tetra-H-folate
  10. tetrahydrafolate
  11. tetrahydrofolate
  12. tetrahydropteroyl mono-L-glutamate
  13. tetrahydropteroylglutamate
  14. th-folate
Brand Names Not Available
Brand Mixtures Not Available
Chemical IUPAC Name (2S)-2-[[4-[(2-amino-4-oxo-5,6,7,8-tetrahydro-1H-pteridin-6-yl)methylamino]benzoyl]amino]pentanedioic acid
Chemical Formula C19H23N7O6
Chemical Structure Structure
CAS Registry Number 135-16-0
InChI Identifier InChI=1/C19H23N7O6/c20-19-25-15-14(17(30)26-19)23-11(8-22-15)7-21-10-3-1-9(2-4-10)16(29)24-12(18(31)32)5-6-13(27)28/h1-4,11-12,21,23H,5-8H2,(H,24,29)(H,27,28)(H,31,32)(H4,20,22,25,26,30)/t11?,12-/m0/s1/f/h22,24-25,27,31H,20H2
InChI Key MSTNYGQPCMXVAQ-BHCPNLAADC
KEGG Drug Not Available
KEGG Compound C00101 Link Image
PubChem Compound 91443 Link Image
PubChem Substance 8146989 Link Image
ChEBI ID 20506 Link Image
PharmGKB ID Not Available
HET ID THL Link Image
GenBank ID Not Available
Drug ID Number [DIN] Not Available
RxList Link Not Available
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Tetrahydrofolic_acid Link Image
FDA Label Not Available
Material Safety Data Sheet (MSDS) Not Available
Synthesis Reference Not Available
Average Molecular Weight 445.4292
Monoisotopic Molecular Weight 445.1710
State Solid
Melting Point Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 2.69e-01 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity -2.7 Source: PhysProp
Predicted LogP -0.96 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -3.22 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 1WOO Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES NC1=NC(=O)C2=C(NC[C@@H](CNC3=CC=C(C=C3)C(=O)N[C@@H](CCC(O)=O)C(O)=O)N2)N1
Canonical SMILES NC1=NC(=O)C2=C(NCC(CNC3=CC=C(C=C3)C(=O)NC(CCC(O)=O)C(O)=O)N2)N1
Drug Category
  • Dietary supplement
  • Micronutrient
ATC Codes Not Available
AHFS Codes Not Available
Indication For nutritional supplementation, also for treating dietary shortage or imbalance.
Pharmacology Tetrahydrofolate is the main active metabolite of dietary folate. It is vital as a coenzyme in reactions involving transfers of single carbon groups. Tetrahydrofolate has a role in nucleic and amino acid synthesis. As nucleic and amino acid synthesis is affected by a deficiency of tetrahydrofolate, actively dividing and growing cells tend to be the first affected. Tetrahydrofolate is used to treat topical sprue and megaloblastic and macrocytic anemias, hematologic complications resulting from a deficiency in folic acid.
Mechanism of Action Tetrahydrofolate is transported across cells by receptor-mediated endocytosis where it is needed to maintain normal erythropoiesis, synthesize purine and thymidylate nucleic acids, interconvert amino acids, methylate tRNA, and generate and use formate.
Absorption Not Available
Toxicity Not Available
Protein Binding Not Available
Biotransformation Not Available
Half Life Not Available
Dosage Forms Not Available
Patient Information Not Available
Contraindications Not Available
Interactions Not Available
Drug Interactions Not Available
Food Interactions Not Available
Pathways Not Available
General References
  1. Wikipedia Link Image
Organisms Affected
  • Humans and other mammals
Phase 1 Metabolizing Enzymes
  1. Methylenetetrahydrofolate reductase
Targets
  1. Aminomethyltransferase, mitochondrial
  2. AMT protein
  3. Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial
  4. Serine hydroxymethyltransferase, mitochondrial
  5. Serine hydroxymethyltransferase, cytosolic
  6. C-1-tetrahydrofolate synthase, cytoplasmic
  7. Methionine synthase
  8. Formimidoyltransferase-cyclodeaminase
  9. 10-formyltetrahydrofolate dehydrogenase
  10. Bifunctional purine biosynthesis protein PURH [Includes: Phosphoribosylaminoimidazolecarboxamide formyltransferase
  11. Serine hydroxymethyltransferase 2
  12. SHMT2 protein
  13. Hypothetical protein DKFZp686P09201
  14. SHMT2 protein
  15. Serine hydroxymethyltransferase 1
  16. Methylenetetrahydrofolate reductase
  17. 5,10-methylenetetrahydrofolate reductase
  18. Methionyl-tRNA formyltransferase, mitochondrial
  19. Methylenetetrahydrofolate reductase intermediate form
Phase 1 Metabolizing Enzyme 1 [top]
Enzyme 1 Name Methylenetetrahydrofolate reductase
Enzyme 1 Gene Name MTHFR
Enzyme 1 SwissProt ID P42898 Link Image
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 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 13
Target 1 Name Aminomethyltransferase, mitochondrial
Target 1 Synonyms
  1. Aminomethyltransferase, mitochondrial precursor
  2. EC 2.1.2.10
  3. GCVT
  4. Glycine cleavage system T protein
Target 1 Gene Name AMT
Target 1 Protein Sequence >Aminomethyltransferase, mitochondrial precursor 
MQRAVSVVARLGFRLQAFPPALCRPLSCAQEVLRRTPLYDFHLAHGGKMVAFAGWSLPVQ
YRDSHTDSHLHTRQHCSLFDVSHMLQTKILGSDRVKLMESLVVGDIAELRPNQGTLSLFT
NEAGGILDDLIVTNTSEGHLYVVSNAGCWEKDLALMQDKVRELQNQGRDVGLEVLDNALL
ALQGPTAAQVLQAGVADDLRKLPFMTSAVMEVFGVSGCRVTRCGYTGEDGVEISVPVAGA
VHLATAILKNPEVKLAGLAARDSLRLEAGLCLYGNDIDEHTTPVEGSLSWTLGKRRRAAM
DFPGAKVIVPQLKGRVQRRRVGLMCEGAPMRAHSPILNMEGTKIGTVTSGCPSPSLKKNV
AMGYVPCEYSRPGTMLLVEVRRKQQMAVVSKMPFVPTNYYTLK
Target 1 Number of Residues 409
Target 1 Molecular Weight 43947
Target 1 Theoretical pI 8.69
Target 1 GO Classification
Function
catalytic activity
transferase activity
transferase activity, transferring one-carbon groups
methyltransferase activity
aminomethyltransferase activity
Process
physiological process
metabolism
cellular metabolism
amino acid and derivative metabolism
amino acid metabolism
serine family amino acid metabolism
glycine metabolism
glycine catabolism
Component
cell
intracellular
cytoplasm
Target 1 General Function Amino acid transport and metabolism
Target 1 Specific Function The glycine cleavage system catalyzes the degradation of glycine
Target 1 Pathways
Name SMPDB Link KEGG Link
Glycine, serine and threonine metabolism SMP00004 Link Image map00260 Link Image
Nitrogen metabolism map00910 Link Image
One carbon pool by folate SMP00053 Link Image map00670 Link Image
Target 1 Reactions
  • [protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 391721 Link Image
Target 1 UniProtKB/Swiss-Prot ID P48728 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name GCST_HUMAN Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location
  • Mitochondrion
Target 1 Gene Sequence >1212 bp 
ATGCAGAGGGCTGTAAGTGTGGTGGCCCGTCTGGGCTTTCGCCTGCAGGCATTCCCCCCG
GCCTTGTGTCGTCCACTTAGTTGCGCACAGGAGGTGCTCCGCAGGACACCGCTCTATGAC
TTCCACCTGGCCCACGGCGGGAAAATGGTGGCGTTTGCGGGTTGGAGTCTGCCAGTGCAG
TACCGGGACAGTCACACTGACTCGCACCTGCACACACGCCAGCACTGCTCGCTCTTTGAC
GTGTCTCATATGCTGCAGACCAAGATACTTGGTAGTGACCGGGTGAAGCTGATGGAGAGT
CTAGTGGTTGGAGACATTGCAGAGCTAAGACCAAACCAGGGGACACTGTCGCTGTTTACC
AACGAGGCTGGAGGCATCTTAGATGACTTGATTGTAACCAATACTTCTGAGGGCCACCTG
TATGTGGTGTCCAACGCTGGCTGCTGGGAGAAAGATTTGGCCCTCATGCAGGACAAGGTC
AGGGAGCTTCAGAACCAGGGCAGAGATGTGGGCCTGGAGGTGTTGGATAATGCCCTGCTA
GCTCTGCAAGGCCCCACTGCAGCCCAGGTACTACAGGCCGGCGTGGCAGATGACCTGAGG
AAACTGCCCTTCATGACCAGTGCTGTGATGGAGGTGTTTGGCGTGTCTGGCTGCCGCGTG
ACCCGCTGTGGCTACACAGGAGAGGATGGTGTGGAGATCTCGGTGCCGGTAGCGGGGGCA
GTTCACCTGGCAACAGCTATTCTGAAAAACCCAGAGGTGAAGCTGGCAGGGCTGGCAGCC
AGGGACAGCCTGCGCCTGGAGGCAGGCCTCTGCCTGTATGGGAATGACATTGATGAACAC
ACTACACCTGTGGAGGGCAGCCTCAGTTGGACACTGGGGAAGCGCCGCCGAGCTGCTATG
GACTTCCCTGGAGCCAAGGTCATTGTTCCCCAGCTGAAGGGCAGGGTGCAGCGGAGGCGT
GTGGGGTTGATGTGTGAGGGGGCCCCCATGCGGGCACACAGTCCCATCCTGAACATGGAG
GGTACCAAGATTGGTACTGTGACTAGTGGCTGCCCCTCCCCCTCTCTGAAGAAGAATGTG
GCGATGGGTTATGTGCCCTGCGAGTACAGTCGTCCAGGGACAATGCTGCTGGTAGAGGTG
CGGCGGAAGCAGCAGATGGCTGTAGTCAGCAAGATGCCCTTTGTGCCCACAAACTACTAT
ACCCTCAAGTGA
Target 1 GenBank Gene ID
Target 1 GeneCard ID AMT Link Image
Target 1 GenAtlas ID AMT Link Image
Target 1 HGNC ID HGNC:473 Link Image
Target 1 Chromosome Location 3
Target 1 Locus 3p21.2-p21.1
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Toone JR, Applegarth DA, Coulter-Mackie MB, James ER: Biochemical and molecular investigations of patients with nonketotic hyperglycinemia. Mol Genet Metab. 2000 Jun;70(2):116-21. [PubMed Link Image]
  2. Toone JR, Applegarth DA, Coulter-Mackie MB, James ER: Recurrent mutations in P- and T-proteins of the glycine cleavage complex and a novel T-protein mutation (N145I): a strategy for the molecular investigation of patients with nonketotic hyperglycinemia (NKH). Mol Genet Metab. 2001 Apr;72(4):322-5. [PubMed Link Image]
  3. Hayasaka K, Nanao K, Takada G, Okamura-Ikeda K, Motokawa Y: Isolation and sequence determination of cDNA encoding human T-protein of the glycine cleavage system. Biochem Biophys Res Commun. 1993 Apr 30;192(2):766-71. [PubMed Link Image]
  4. Nanao K, Okamura-Ikeda K, Motokawa Y, Danks DM, Baumgartner ER, Takada G, Hayasaka K: Identification of the mutations in the T-protein gene causing typical and atypical nonketotic hyperglycinemia. Hum Genet. 1994 Jun;93(6):655-8. [PubMed Link Image]
  5. Nanao K, Takada G, Takahashi E, Seki N, Komatsu Y, Okamura-Ikeda K, Motokawa Y, Hayasaka K: Structure and chromosomal localization of the aminomethyltransferase gene (AMT) Genomics. 1994 Jan 1;19(1):27-30. [PubMed Link Image]
  6. Kure S, Mandel H, Rolland MO, Sakata Y, Shinka T, Drugan A, Boneh A, Tada K, Matsubara Y, Narisawa K: A missense mutation (His42Arg) in the T-protein gene from a large Israeli-Arab kindred with nonketotic hyperglycinemia. Hum Genet. 1998 Apr;102(4):430-4. [PubMed Link Image]
  7. Kure S, Shinka T, Sakata Y, Osamu N, Takayanagi M, Tada K, Matsubara Y, Narisawa K: A one-base deletion (183delC) and a missense mutation (D276H) in the T-protein gene from a Japanese family with nonketotic hyperglycinemia. J Hum Genet. 1998;43(2):135-7. [PubMed Link Image]
Target 1 Drug References
  1. Masai E, Sasaki M, Minakawa Y, Abe T, Sonoki T, Miyauchi K, Katayama Y, Fukuda M: A novel tetrahydrofolate-dependent O-demethylase gene is essential for growth of Sphingomonas paucimobilis SYK-6 with syringate. J Bacteriol. 2004 May;186(9):2757-65. [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 2 [top]
Target 2 ID 59
Target 2 Name AMT protein
Target 2 Synonyms Not Available
Target 2 Gene Name AMT
Target 2 Protein Sequence >AMT protein 
AVSVVARLGFRLQAFPPALCRPLSCAQEVLRRTPLYDFHLAHGGKMVAFAGWSLPVQYRD
SHTDSHLHTRQHCSLFDVSHMLQTKILGSDRVKLMESLVVGDIAELRPNQGTLSLFTNEA
GGILDDLIVTNTSEGHLYVVSNAGCWEKDLALMQDKVRELQNQGRDVGLEVLDNALLALQ
GPTAAQVLQAGVADDLRKLPFMTSAVMEVFGVSGCRVTRCGYTGEDGVEISVPVAGAVHL
ATAILKNPEVKLAGLAARDSLRLEAGLCLYGNDIDEHTTPVEGSLSWTLGKRRRAAMDFP
GAKVIVPQLKGRVQRRRVGLMCEGAPMRAHSPILNMEGTKIGTVTSGCPSPSLKKNVAMG
YVPCEYSRPGTMLLVELPSGPCF
Target 2 Number of Residues 389
Target 2 Molecular Weight 41365
Target 2 Theoretical pI 7.70
Target 2 GO Classification
Function
catalytic activity
transferase activity
transferase activity, transferring one-carbon groups
methyltransferase activity
aminomethyltransferase activity
Process
physiological process
metabolism
cellular metabolism
amino acid and derivative metabolism
amino acid metabolism
serine family amino acid metabolism
glycine metabolism
glycine catabolism
Component
cell
intracellular
cytoplasm
Target 2 General Function Amino acid transport and metabolism
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 48257290 Link Image
Target 2 UniProtKB/Swiss-Prot ID Q96IG6 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name Q96IG6_HUMAN Link Image
Target 2 PDB ID Not Available
Target 2 Cellular Location Not Available
Target 2 Gene Sequence >1153 bp 
GGCTGTAAGTGTGGTGGCCCGTCTGGGCTTTCGCCTGCAGGCATTCCCCCCGGCCTTGTG
TCGTCCACTTAGTTGCGCACAGGAGGTGCTCCGCAGGACACCGCTCTATGACTTCCACCT
GGCCCACGGCGGGAAAATGGTGGCGTTTGCGGGTTGGAGTCTGCCAGTGCAGTACCGGGA
CAGTCACACTGACTCGCACCTGCACACACGCCAGCACTGCTCGCTCTTTGACGTGTCTCA
TATGCTGCAGACCAAGATACTTGGTAGTGACCGGGTGAAGCTGATGGAGAGTCTAGTGGT
TGGAGACATTGCAGAGCTAAGACCAAACCAGGGGACACTGTCGCTGTTTACCAACGAGGC
TGGAGGCATCTTAGATGACTTGATTGTAACCAATACTTCTGAGGGCCACCTGTATGTGGT
GTCCAACGCTGGCTGCTGGGAGAAAGATTTGGCCCTCATGCAGGACAAGGTCAGGGAGCT
TCAGAACCAGGGCAGAGATGTGGGCCTGGAGGTGTTGGATAATGCCCTGCTAGCTCTGCA
AGGCCCCACTGCAGCCCAGGTACTACAGGCCGGCGTGGCAGATGACCTGAGGAAACTGCC
CTTCATGACCAGTGCTGTGATGGAGGTGTTTGGCGTGTCTGGCTGCCGCGTGACCCGCTG
TGGCTACACAGGAGAGGATGGTGTGGAGATCTCGGTGCCGGTAGCGGGGGCAGTTCACCT
GGCAACAGCTATTCTGAAAAACCCAGAGGTGAAGCTGGCAGGGCTGGCAGCCAGGGACAG
CCTGCGCCTGGAGGCAGGCCTCTGCCTGTATGGGAATGACATTGATGAACACACTACACC
TGTGGAGGGCAGCCTCAGTTGGACACTGGGGAAGCGCCGCCGAGCTGCTATGGACTTCCC
TGGAGCCAAGGTCATTGTTCCCCAGCTGAAGGGCAGGGTGCAGCGGAGGCGTGTGGGGTT
GATGTGTGAGGGGGCCCCCATGCGGGCACACAGTCCCATCCTGAACATGGAGGGTACCAA
GATTGGTACTGTGACTAGTGGCTGCCCCTCCCCCTCTCTGAAGAAGAATGTGGCGATGGG
TTATGTGCCCTGCGAGTACAGTCGTCCAGGGACAATGCTGCTGGTAGAGCTTCCTTCAGG
ACCCTGCTTCTGA
Target 2 GenBank Gene ID
Target 2 GeneCard ID AMT Link Image
Target 2 GenAtlas ID AMT Link Image
Target 2 HGNC ID HGNC:473 Link Image
Target 2 Chromosome Location 3
Target 2 Locus 3p21.2-p21.1
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Target 2 Drug References
  1. Masai E, Sasaki M, Minakawa Y, Abe T, Sonoki T, Miyauchi K, Katayama Y, Fukuda M: A novel tetrahydrofolate-dependent O-demethylase gene is essential for growth of Sphingomonas paucimobilis SYK-6 with syringate. J Bacteriol. 2004 May;186(9):2757-65. [PubMed Link Image]
  2. Lee HH, Kim DJ, Ahn HJ, Ha JY, Suh SW: Crystal structure of T-protein of the glycine cleavage system. Cofactor binding, insights into H-protein recognition, and molecular basis for understanding nonketotic hyperglycinemia. J Biol Chem. 2004 Nov 26;279(48):50514-23. Epub 2004 Sep 7. [PubMed Link Image]
  3. Scrutton NS, Leys D: Crystal structure of DMGO provides a prototype for a new tetrahydrofolate-binding fold. Biochem Soc Trans. 2005 Aug;33(Pt 4):776-9. [PubMed Link Image]
  4. Gangjee A, Kurup S, Namjoshi O: Dihydrofolate reductase as a target for chemotherapy in parasites. Curr Pharm Des. 2007;13(6):609-39. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 296
Target 3 Name Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial
Target 3 Synonyms
  1. Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial
Target 3 Gene Name MTHFD2
Target 3 Protein Sequence >Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial precursor [Includes: NAD-dependent methylenetetrahydrofolate dehydrogenase 
MAATSLMSALAARLLQPAHSCSLRLRPFHLAAVRNEAVVISGRKLAQQIKQEVRQEVEEW
VASGNKRPHLSVILVGENPASHSYVLNKTRAAAVVGINSETIMKPASISEEELLNLINKL
NNDDNVDGLLVQLPLPEHIDERRICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGV
WEIIKRTGIPTLGKNVVVAGRSKNVGMPIAMLLHTDGAHERPGGDATVTISHRYTPKEQL
KKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINRVHDPVTAKPKLVGDVDFEGVRQ
KAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLRLEEREVLKSKELGVATN
Target 3 Number of Residues 355
Target 3 Molecular Weight 37896
Target 3 Theoretical pI 9.12
Target 3 GO Classification
Function
catalytic activity
Process
physiological process
metabolism
cellular metabolism
aromatic compound metabolism
folic acid and derivative metabolism
folic acid and derivative biosynthesis
Component
Not Available
Target 3 General Function Coenzyme transport and metabolism
Target 3 Specific Function Not Available
Target 3 Pathways
Name SMPDB Link KEGG Link
Glyoxylate and dicarboxylate metabolism map00630 Link Image
One carbon pool by folate SMP00053 Link Image map00670 Link Image
Target 3 Reactions
  • 5,10-methylenetetrahydrofolate + NAD+ = 5,10-methenyltetrahydrofolate + NADH + H+
Target 3 Pfam Domain Function
Target 3 Signals
  • None
Target 3 Transmembrane Regions
  • None
Target 3 Essentiality Non-Essential
Target 3 GenBank ID Protein 35071 Link Image
Target 3 UniProtKB/Swiss-Prot ID P13995 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name MTDC_HUMAN Link Image
Target 3 PDB ID Not Available
Target 3 Cellular Location
  • Mitochondrion
Target 3 Gene Sequence >1035 bp 
ATGTCTGCTTTGGCTGCCCGGCTGCTGCAGCCCGCGCACAGCTGCTCCCTTCGCCTTCGC
CCTTTCCACCTCGCGGCAGTTCGAAATGAAGCTGTTGTCATTTCTGGAAGGAAACTGGCC
CAGCAGATCAAGCAGGAAGTGCGGCAGGAGGTAGAAGAGTGGGTGGCCTCAGGCAACAAA
CGGCCACACCTGAGTGTGATCCTGGTTGGCGAGAATCCTGCAAGTCACTCCTATGTCCTC
AACAAAACCAGGGCAGCTGCAGTTGTGGGAATCAACAGTGAGACAATTATGAAACCAGCT
TCAATTTCAGAGGAAGAATTGTTGAATTTAATCAATAAACTGAATAATGATGATAATGTA
GATGGCCTCCTTGTTCAGTTGCCTCTTCCAGAGCATATTGATGAGAGAAGGATCTGCAAT
GCTGTTTCTCCAGACAAGGATGTTGATGGCTTTCATGTAATTAATGTAGGACGAATGTGT
TTGGATCAGTATTCCATGTTACCGGCTACTCCATGGGGTGTGTGGGAAATAATCAAGCGA
ACTGGCATTCCAACCCTAGGGAAGAATGTGGTTGTGGCTGGAAGGTCAAAAAACGTTGGA
ATGCCCATTGCAATGTTACTGCACACAGATGGGGCGCATGAACGTCCCGGAGGTGATGCC
ACTGTTACAATATCTCATCGATATACTCCCAAAGAGCAGTTGAAGAAACATACAATTCTT
GCAGATATTGTAATATCTGCTGCAGGTATTCCAAATCTGATCACAGCAGATATGATCAAG
GAAGGAGCAGCAGTCATTGATGTGGGAATAAATAGAGTTCACGATCCTGTAACTGCCAAA
CCCAAGTTGGTTGGAGATGTGGATTTTGAAGGAGTCAGACAAAAAGCTGGGTATATCACT
CCAGTTCCTGGAGGTGTTGGCCCCATGACAGTGGCAATGCTAATGAAGAATACCATTATT
GCTGCAAAAAAGGTGCTGAGGCTTGAAGAGCGAGAAGTGCTGAAGTCTAAAGAGCTTGGG
GTAGCCACTAATTAA
Target 3 GenBank Gene ID
Target 3 GeneCard ID MTHFD2 Link Image
Target 3 GenAtlas ID MTHFD2 Link Image
Target 3 HGNC ID HGNC:7434 Link Image
Target 3 Chromosome Location 2
Target 3 Locus 2p13.1
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Peri KG, Belanger C, Mackenzie RE: Nucleotide sequence of the human NAD-dependent methylene tetrahydrofolate dehydrogenase-cyclohydrolase. Nucleic Acids Res. 1989 Nov 11;17(21):8853. [PubMed Link Image]
Target 3 Drug References
  1. Salmassi TM, Leadbetter JR: Analysis of genes of tetrahydrofolate-dependent metabolism from cultivated spirochaetes and the gut community of the termite Zootermopsis angusticollis. Microbiology. 2003 Sep;149(Pt 9):2529-37. [PubMed Link Image]
Drug Target 4 [top]
Target 4 ID 321
Target 4 Name Serine hydroxymethyltransferase, mitochondrial
Target 4 Synonyms
  1. EC 2.1.2.1
  2. Glycine hydroxymethyltransferase
  3. SHMT
  4. Serine hydroxymethyltransferase, mitochondrial precursor
  5. Serine methylase
Target 4 Gene Name SHMT2
Target 4 Protein Sequence >Serine hydroxymethyltransferase, mitochondrial precursor 
MLYFSLFWAARPLQRCGQLVRMAIRAQHSNAAQTQTGEANRGWTGQESLSDSDPEMWELL
QREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQ
RRALEAFDLDPAQWGVNVQPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDV
KRISATSIFFESMPYKLNPKTGLIDYNQLALTARLFRPRLIIAGTSAYARLIDYARMREV
CDEVKAHLLADMAHISGLVAAKVIPSPFKHADIVTTTTHKTLRGARSGLIFYRKGVKAVD
PKTGREIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARA
MADALLERGYSLVSGGTDNHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAIT
PGGLRLGAPALTSRQFREDDFRRVVDFIDEGVNIGLEVKSKTAKLQDFKSFLLKDSETSQ
RLANLRQRVEQFARAFPMPGFDEH
Target 4 Number of Residues 512
Target 4 Molecular Weight 55994
Target 4 Theoretical pI 8.67
Target 4 GO Classification
Function
catalytic activity
transferase activity
transferase activity, transferring one-carbon groups
methyltransferase activity
glycine hydroxymethyltransferase activity
Process
L-serine metabolism
physiological process
metabolism
cellular metabolism
amino acid and derivative metabolism
amino acid metabolism
serine family amino acid metabolism
glycine metabolism
Component
Not Available
Target 4 General Function Amino acid transport and metabolism
Target 4 Specific Function Interconversion of serine and glycine
Target 4 Pathways
Name SMPDB Link KEGG Link
Cyanoamino acid metabolism map00460 Link Image
Glycine, serine and threonine metabolism SMP00004 Link Image map00260 Link Image
Lysine degradation SMP00037 Link Image map00310 Link Image
Methane metabolism map00680 Link Image
One carbon pool by folate SMP00053 Link Image map00670 Link Image
Target 4 Reactions
  • 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
Target 4 Pfam Domain Function
Target 4 Signals
  • None
Target 4 Transmembrane Regions
  • None
Target 4 Essentiality Non-Essential
Target 4 GenBank ID Protein 746436 Link Image
Target 4 UniProtKB/Swiss-Prot ID P34897 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name GLYM_HUMAN Link Image
Target 4 PDB ID Not Available
Target 4 Cellular Location
  • Mitochondrion
Target 4 Gene Sequence >1452 bp 
ATGGCCATTCGGGCTCAGCACAGCAACGCAGCCCAGACTCAGACTGGGGAAGCAAACAGG
GGCTGGACAGGCCAGGAGAGCCTGTCGGACAGTGATCCTGAGATGTGGGAGTTGCTGCAG
AGGGAGAAGGACAGGCAGTGTCGTGGCCTGGAGCTCATTGCCTCAGAGAACTTCTGCAGC
CGAGCTGCGCTGGAGGCCCTGGGGTCCTGTCTGAACAACAAGTACTCGGAGGGTTATCCT
GGCAAGAGATACTATGGGGGAGCAGAGGTGGTGGATGAAATTGAGCTGCTGTGCCAGCGC
CGGGCCTTGGAAGCCTTTGACCTGGATCCTGCACAGTGGGGAGTCAATGTCCAGCCCTAC
TCCGGGTCCCCAGCCAACCTGGCCGTCTACACAGCCCTTCTGCAACCTCACGACCGGATC
ATGGGGCTGGACCTGCCCGATGGGGGCCATCTCACCCACGGCTACATGTCTGACGTCAAG
CGGATATCAGCCACGTCCATCTTCTTCGAGTCTATGCCCTATAAGCTCAACCCCAAAACT
GGCCTCATTGACTACAACCAGCTGGCACTGACTGCTCGACTTTTCCGGCCACGGCTCATC
ATAGCTGGCACCAGCGCCTATGCTCGCCTCATTGACTACGCCCGCATGAGAGAGGTGTGT
GATGAAGTCAAAGCACACCTGCTGGCAGACATGGCCCACATCAGTGGCCTGGTGGCTGCC
AAGGTGATTCCCTCGCCTTTCAAGCACGCGGACATCGTCACCACCACTACTCACAAGACT
CTTCGAGGGGCCAGGTCAGGGCTCATCTTCTACCGGAAAGGGGTGAAGGCTGTGGACCCC
AAGACTGGCCGGGAGATCCCTTACACATTTGAGGACCGAATCAACTTTGCCGTGTTCCCA
TCCCTGCAGGGGGGCCCCCACAATCATGCCATTGCTGCAGTAGCTGTGGCCCTAAAGCAG
GCCTGCACCCCCATGTTCCGGGAGTACTCCCTGCAGGTTCTGAAGAATGCTCGGGCCATG
GCAGATGCCCTGCTAGAGCGAGGCTACTCACTGGTATCAGGTGGTACTGACAACCACCTG
GTGCTGGTGGACCTGCGGCCCAAGGGCCTGGATGGAGCTCGGGCTGAGCGGGTGCTAGAG
CTTGTATCCATCACTGCCAACAAGAACACCTGTCCTGGAGACCGAAGTGCCATCACACCG
GGCGGCCTGCGGCTTGGGGCCCCAGCCTTAACTTCTCGACAGTTCCGTGAGGATGACTTC
CGGAGAGTTGTGGACTTTATAGATGAAGGGGTCAACATTGGCTTAGAGGTGAAGAGCAAG
ACTGCCAAGCTCCAGGATTTCAAATCCTTCCTGCTTAAGGACTCAGAAACAAGTCAGCGT
CTGGCCAACCTCAGGCAACGGGTGGAGCAGTTTGCCAGGGCCTTCCCCATGCCTGGTTTT
GATGAGCATTGA
Target 4 GenBank Gene ID
Target 4 GeneCard ID SHMT2 Link Image
Target 4 GenAtlas ID SHMT2 Link Image
Target 4 HGNC ID HGNC:10852 Link Image
Target 4 Chromosome Location 12
Target 4 Locus 12q12-q14
Target 4 SNPs SNPJam Report Link Image
Target 4 General References
  1. Snell K, Baumann U, Byrne PC, Chave KJ, Renwick SB, Sanders PG, Whitehouse SK: The genetic organization and protein crystallographic structure of human serine hydroxymethyltransferase. Adv Enzyme Regul. 2000;40:353-403. [PubMed Link Image]
  2. Garrow TA, Brenner AA, Whitehead VM, Chen XN, Duncan RG, Korenberg JR, Shane B: Cloning of human cDNAs encoding mitochondrial and cytosolic serine hydroxymethyltransferases and chromosomal localization. J Biol Chem. 1993 Jun 5;268(16):11910-6. [PubMed Link Image]
  3. Stover PJ, Chen LH, Suh JR, Stover DM, Keyomarsi K, Shane B: Molecular cloning, characterization, and regulation of the human mitochondrial serine hydroxymethyltransferase gene. J Biol Chem. 1997 Jan 17;272(3):1842-8. [PubMed Link Image]
Target 4 Drug References
  1. Heil SG, Van der Put NM, Waas ET, den Heijer M, Trijbels FJ, Blom HJ: Is mutated serine hydroxymethyltransferase (SHMT) involved in the etiology of neural tube defects? Mol Genet Metab. 2001 Jun;73(2):164-72. [PubMed Link Image]
  2. Contestabile R, Paiardini A, Pascarella S, di Salvo ML, D'Aguanno S, Bossa F: l-Threonine aldolase, serine hydroxymethyltransferase and fungal alanine racemase. A subgroup of strictly related enzymes specialized for different functions. Eur J Biochem. 2001 Dec;268(24):6508-25. [PubMed Link Image]
  3. Li R, Moore M, King J: Investigating the regulation of one-carbon metabolism in Arabidopsis thaliana. Plant Cell Physiol. 2003 Mar;44(3):233-41. [PubMed Link Image]
  4. Appaji Rao N, Ambili M, Jala VR, Subramanya HS, Savithri HS: Structure-function relationship in serine hydroxymethyltransferase. Biochim Biophys Acta. 2003 Apr 11;1647(1-2):24-9. [PubMed Link Image]
  5. Angelaccio S, Chiaraluce R, Consalvi V, Buchenau B, Giangiacomo L, Bossa F, Contestabile R: Catalytic and thermodynamic properties of tetrahydromethanopterin-dependent serine hydroxymethyltransferase from Methanococcus jannaschii. J Biol Chem. 2003 Oct 24;278(43):41789-97. Epub 2003 Aug 5. [PubMed Link Image]
Drug Target 5 [top]
Target 5 ID 367
Target 5 Name Serine hydroxymethyltransferase, cytosolic
Target 5 Synonyms
  1. EC 2.1.2.1
  2. Glycine hydroxymethyltransferase
  3. SHMT
  4. Serine methylase
Target 5 Gene Name SHMT1
Target 5 Protein Sequence >Serine hydroxymethyltransferase, cytosolic 
MTMPVNGAHKDADLWSSHDKMLAQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRA
VLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKLDPQCWGVNVQPYSG
SPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGY
INYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGV
VPSPFEHCHVVTTTTHKTLRGCRAGMIFYRKGVKSVDPKTGKEILYNLESLINSAVFPGL
QGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGSDNHLIL
VDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQK
VAHFIHRGIELTLQIQSDTGVRATLKEFKERLAGDKYQAAVQALREEVESFASLFPLPGL
PDF
Target 5 Number of Residues 491
Target 5 Molecular Weight 53083
Target 5 Theoretical pI 7.77
Target 5 GO Classification
Function
catalytic activity
transferase activity
transferase activity, transferring one-carbon groups
methyltransferase activity
glycine hydroxymethyltransferase activity
Process
L-serine metabolism
physiological process
metabolism
cellular metabolism
amino acid and derivative metabolism
amino acid metabolism
serine family amino acid metabolism
glycine metabolism
Component
Not Available
Target 5 General Function Amino acid transport and metabolism
Target 5 Specific Function Interconversion of serine and glycine
Target 5 Pathways
Name SMPDB Link KEGG Link
Cyanoamino acid metabolism map00460 Link Image
Glycine, serine and threonine metabolism SMP00004 Link Image map00260 Link Image
Lysine degradation SMP00037 Link Image map00310 Link Image
Methane metabolism map00680 Link Image
One carbon pool by folate SMP00053 Link Image map00670 Link Image
Target 5 Reactions
  • 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
Target 5 Pfam Domain Function
Target 5 Signals
  • None
Target 5 Transmembrane Regions
  • None
Target 5 Essentiality Non-Essential
Target 5 GenBank ID Protein 307422 Link Image
Target 5 UniProtKB/Swiss-Prot ID P34896 Link Image
Target 5 UniProtKB/Swiss-Prot Entry Name GLYC_HUMAN Link Image
Target 5 PDB ID 1BJ4 Link Image
Target 5 PDB File Show
Target 5 3D Structure
Target 5 Cellular Location
  • Cytoplasm
Target 5 Gene Sequence >1452 bp 
ATGACGATGCCAGTCAACGGGGCCCACAAGGATGCTGACCTGTGGTCCTCACATGACAAG
ATGCTGGCACAACCCCTCAAAGACAGTGATGTTGAGGTTTACAACATCATTAAGAAGGAG
AGTAACCGGCAGAGGGTTGGATTGGAGCTGATTGCCTCGGAGAATTTCGCCAGCCGAGCA
GTTTTGGAGGCCCTAGGCTCTTGCTTAAATAACAAATACTCTGAGGGGTACCCGGGCCAG
AGATACTATGGCGGGACTGAGTTTATTGATGAACTGGAGACCCTCTGTCAGAAGCGAGCC
CTGCAGGCCTATAAGCTGGACCCACAGTGCTGGGGGGTCAACGTCCAGCCCTACTCAGGC
TCCCCTGCAAACTTTGCTGTGTACACTGCCCTGGTGGAACCCCATGGGCGCATCATGGGC
CTGGACCTTCCGGATGGGGGCCACCTGACCCATGGGTTCATGACAGACAAGAAGAAAATC
TCTGCCACGTCCATCTTCTTTGAATCTATGCCCTACAAGGTGAACCCAGATACTGGCTAC
ATCAACTATGACCAGCTGGAGGAGAACGCACGCCTCTTCCACCCGAAGCTGATCATCGCA
GGAACCAGCTGCTACTCCCGAAACCTGGAATATGCCCGGCTACGGAAGATTGCAGATGAG
AACGGGGCGTATCTCATGGCGGACATGGCTCACATCAGCGGGCTGGTGGCGGCTGGCGTG
GTGCCCTCCCCATTTGAACACTGCCATGTGGTGACCACCACCACTCACAAGACCCTGCGA
GGCTGCCGAGCTGGCATGATCTTCTACAGGAAAGGAGTGAAAAGTGTGGATCCCAAGACT
GGCAAAGAGATTCTGTACAACCTGGAGTCTCTTATCAATTCTGCTGTGTTCCCTGGCCTG
CAGGGAGGTCCCCACAACCACGCCATTGCTGGGGTTGCTGTGGCACTGAAGCAAGCTATG
ACTCTGGAATTTAAAGTTTATCAACACCAGGTGGTGGCCAACTGCAGGGCTCTGTCTGAG
GCCCTGACGGAGCTGGGCTACAAAATAGTCACAGGTGGTTCTGACAACCATTTGATCCTT
GTGGATCTCCGTTCCAAAGGCACAGATGGTGGAAGGGCTGAGAAGGTGCTAGAAGCCTGT
TCTATTGCCTGCAACAAGAACACCTGTCCAGGTGACAGAAGCGCTCTGCGGCCCAGTGGA
CTGCGGCTGGGGACCCCAGCACTGACGTCCCGTGGACTTTTGGAAAAAGACTTCCAAAAA
GTAGCCCACTTTATTCACAGAGGGATAGAGCTGACCCTGCAGATCCAGAGCGACACTGGT
GTCAGAGCCACCCTGAAAGAGTTCAAGGAGAGACTGGCAGGGGATAAGTACCAGGCGGCC
GTGCAGGCTCTCCGGGAGGAGGTTGAGAGCTTCGCCTCTCTCTTCCCTCTGCCTGGCCTG
CCTGACTTCTAA
Target 5 GenBank Gene ID
Target 5 GeneCard ID SHMT1 Link Image
Target 5 GenAtlas ID SHMT1 Link Image
Target 5 HGNC ID HGNC:10850 Link Image
Target 5 Chromosome Location 17
Target 5 Locus 17p11.2
Target 5 SNPs SNPJam Report Link Image
Target 5 General References
  1. Garrow TA, Brenner AA, Whitehead VM, Chen XN, Duncan RG, Korenberg JR, Shane B: Cloning of human cDNAs encoding mitochondrial and cytosolic serine hydroxymethyltransferases and chromosomal localization. J Biol Chem. 1993 Jun 5;268(16):11910-6. [PubMed Link Image]
  2. Chave KJ, Snell K, Sanders PG: Isolation and characterisation of human genomic sequences encoding cytosolic serine hydroxymethyltransferase. Biochem Soc Trans. 1997 Feb;25(1):53S. [PubMed Link Image]
  3. Renwick SB, Snell K, Baumann U: The crystal structure of human cytosolic serine hydroxymethyltransferase: a target for cancer chemotherapy. Structure. 1998 Sep 15;6(9):1105-16. [PubMed Link Image]
Target 5 Drug References
  1. Scarsdale JN, Radaev S, Kazanina G, Schirch V, Wright HT: Crystal structure at 2.4 A resolution of E. coli serine hydroxymethyltransferase in complex with glycine substrate and 5-formyl tetrahydrofolate. J Mol Biol. 2000 Feb 11;296(1):155-68. [PubMed Link Image]
  2. Rao JV, Prakash V, Rao NA, Savithri HS: The role of Glu74 and Tyr82 in the reaction catalyzed by sheep liver cytosolic serine hydroxymethyltransferase. Eur J Biochem. 2000 Oct;267(19):5967-76. [PubMed Link Image]
  3. Heil SG, Van der Put NM, Waas ET, den Heijer M, Trijbels FJ, Blom HJ: Is mutated serine hydroxymethyltransferase (SHMT) involved in the etiology of neural tube defects? Mol Genet Metab. 2001 Jun;73(2):164-72. [PubMed Link Image]
  4. Ravanel S, Cherest H, Jabrin S, Grunwald D, Surdin-Kerjan Y, Douce R, Rebeille F: Tetrahydrofolate biosynthesis in plants: molecular and functional characterization of dihydrofolate synthetase and three isoforms of folylpolyglutamate synthetase in Arabidopsis thaliana. Proc Natl Acad Sci U S A. 2001 Dec 18;98(26):15360-5. [PubMed Link Image]
  5. Li R, Moore M, King J: Investigating the regulation of one-carbon metabolism in Arabidopsis thaliana. Plant Cell Physiol. 2003 Mar;44(3):233-41. [PubMed Link Image]
Drug Target 6 [top]
Target 6 ID 679
Target 6 Name C-1-tetrahydrofolate synthase, cytoplasmic
Target 6 Synonyms
  1. C1-THF synthase
Target 6 Gene Name MTHFD1
Target 6 Protein Sequence >C-1-tetrahydrofolate synthase, cytoplasmic 
APAEILNGKEISAQIRARLKNQVTQLKEQVPGFTPRLAILQVGNRDDSNLYINVKLKAAE
EIGIKATHIKLPRTTTESEVMKYITSLNEDSTVHGFLVQLPLDSENSINTEEVINAIAPE
KDVDGLTSINAGRLARGDLNDCFIPCTPKGCLELIKETGVPIAGRHAVVVGRSKIVGAPM
HDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYV
PDDKKPNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKRFLEKFKPG
KWMIQYNNLNLKTPVPSDIDISRSCKPKPIGKLAREIGLLSEEVELYGETKAKVLLSALE
RLKHRPDGKYVVVTGITPTPLGEGKSTTTIGLVQALGAHLYQNVFACVRQPSQGPTFGIK
GGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARIFHELTQTDKALFNRLVP
SVNGVRRFSDIQIRRLKRLGIEKTDPTTLTDEEINRFARLDIDPETITWQRVLDTNDRFL
RKITIGQAPTEKGHTRTAQFDISVASEIMAVLALTTSLEDMRERLGKMVVASSKKGEPVS
AEDLGVSGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSIIADRIALKLVGP
EGFVVTEAGFGADIGMEKFFNIKCRYSGLCPHVVVLVATVRALKMHGGGPTVTAGLPLPK
AYIQENLELVEKGFSNLKKQIENARMFGIPVVVAVNAFKTDTESELDLISRLSREHGAFD
AVKCTHWAEGGKGALALAQAVQRAAQAPSSFQLLYDLKLPVEDKIRIIAQKIYGADDIEL
LPEAQHKAEVYTKQGFGNLPICMAKTHLSLSHNPEQKGVPTGFILPIRDIRASVGAGFLY
PLVGTMSTMPGLPTRPCFYDIDLDPETEQVNGLF
Target 6 Number of Residues 949
Target 6 Molecular Weight 101429
Target 6 Theoretical pI 7.32
Target 6 GO Classification
Function
binding
nucleotide binding
purine nucleotide binding
adenyl nucleotide binding
ATP binding
catalytic activity
ligase activity
ligase activity, forming carbon-nitrogen bonds
formate-tetrahydrofolate ligase activity
Process
physiological process
metabolism
cellular metabolism
aromatic compound metabolism
folic acid and derivative metabolism
folic acid and derivative biosynthesis
Component
Not Available
Target 6 General Function Nucleotide transport and metabolism
Target 6 Specific Function Not Available
Target 6 Pathways
Name SMPDB Link KEGG Link
Glyoxylate and dicarboxylate metabolism map00630 Link Image
One carbon pool by folate SMP00053 Link Image map00670 Link Image
Target 6 Reactions
  • 5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH + H+
Target 6 Pfam Domain Function
Target 6 Signals
  • None
Target 6 Transmembrane Regions
  • None
Target 6 Essentiality Non-Essential
Target 6 GenBank ID Protein 307178 Link Image
Target 6 UniProtKB/Swiss-Prot ID P11586 Link Image
Target 6 UniProtKB/Swiss-Prot Entry Name C1TC_HUMAN Link Image
Target 6 PDB ID 1DIA Link Image
Target 6 PDB File Show
Target 6 3D Structure
Target 6 Cellular Location
  • Cytoplasm
Target 6 Gene Sequence >2808 bp 
ATGGCGCCAGCAGAAATCCTGAACGGGAAGGAGATCTCCGCGCAAATAAGGGCGAGACTG
AAAAATCAAGTCACTCAGTTGAAGGAGCAAGTACCTGGTTTCACACCACGCCTGGCAATA
TTACAGGTTGGCAACAGAGATGATTCCAATCTTTATATAAATGTGAAGCTGAAGGCTGCT
GAAGAGATTGGGATCAAAGCCACTCACATTAAGTTACCAAGAACAACCACAGAATCTGAG
GTGATGAAGTACATTACATCTTTGAATGAAGACTCTACTGTACATGGGTTCTTAGTGCAG
CTACCTTTAGATTCAGAGAATTCCATTAACACTGAAGAAGTGATCAATGCTATTGCACCC
GAGAAGGATGTGGATGGATTGACTAGCATCAATGCTGGGAGACTTGCTAGAGGTGACCTC
AATGACTGTTTCATTCCTTGTACGCCTAAGGGATGCTTGGAACTCATCAAAGAGACAGGG
GTGCCGATTGCCGGAAGGCATGCTGTGGTGGTTGGGCGCAGTAAAATAGTTGGGGCCCCG
ATGCATGACTTGCTTCTGTGGAACAATGCCACAGTGACCACCTGCCACTCCAAGACTGCC
CATCTGGATGAGGAGGTAAATAAAGGTGACATCCTGGTGGTTGCAACTGGTCAGCCTGAA
ATGGTTAAAGGGGAGTGGATCAAACCTGGGGCAATAGTCATCGACTGTGGAATCAATTAT
GTCCCAGATGATAAAAAACCAAATGGGAGAAAAGTTGTGGGTGATGTGGCATACGACGAG
GCCAAAGAGAGGGCGAGCTTCATCACTCCTGTTCCTGGCGGCGTAGGGCCCATGACAGTT
GCAATGCTCATGCAGAGCACAGTAGAGAGTGCCAAGCGTTTCCTGGAGAAATTTAAGCCA
GGAAAGTGGATGATTCAGTATAACAACCTTAACCTCAAGACACCTGTTCCAAGTGACATT
GATATATCACGATCTTGTAAACCGAAGCCCATTGGTAAGCTGGCTCGAGAAATTGGTCTG
CTGTCTGAAGAGGTAGAATTATATGGTGAAACAAAGGCCAAAGTTCTGCTGTCAGCACTA
GAACGCCTGAAGCACCGGCCTGATGGGAAATACGTGGTGGTGACTGGAATAACTCCAACA
CCCCTGGGAGAAGGGAAAAGCACAACTACAATCGGGCTAGTGCAAGCCCTTGGTGCCCAT
CTCTACCAGAATGTCTTTGCGTGTGTGCGACAGCCTTCTCAGGGCCCCACCTTTGGAATA
AAAGGTGGCGCTGCAGGAGGCGGCTACTCCCAGGTCATTCCTATGGAAGAGTTTAATCTC
CACCTCACAGGTGACATCCATGCCATCACTGCAGCTAATAACCTCGTTGCTGCGGCCATT
GATGCTCGGATATTTCATGAACTGACCCAGACAGACAAGGCTCTCTTTAATCGTTTGGTG
CCATCAGTAAATGGAGTGAGAAGGTTCTCTGACATCCAAATCCGAAGGTTAAAGAGACTA
GGCATTGAAAAGACTGACCCTACCACACTGACAGATGAAGAGATAAACAGATTTGCAAGA
TTGGACATTGATCCAGAAACCATAACTTGGCAAAGAGTGTTGGATACCAATGATAGATTC
CTGAGGAAGATCACGATTGGACAGGCTCCAACGGAGAAGGGTCACACACGGACGGCCCAG
TTTGATATCTCTGTGGCCAGTGAAATTATGGCTGTCCTGGCTCTCACCACTTCTCTAGAA
GACATGAGAGAGAGACTGGGCAAAATGGTGGTGGCATCCAGTAAGAAAGGAGAGCCCGTC
AGTGCCGAAGATCTGGGGGTGAGTGGTGCACTGACAGTGCTTATGAAGGACGCAATCAAG
CCCAATCTCATGCAGACACTGGAGGGCACTCCAGTGTTTGTCCATGCTGGCCCGTTTGCC
AACATCGCACATGGCAATTCCTCCATCATTGCAGACCGGATCGCACTCAAGCTTGTTGGC
CCAGAAGGGTTTGTAGTGACGGAAGCAGGATTTGGAGCAGACATTGGAATGGAAAAGTTT
TTTAACATCAAATGCCGGTATTCCGGCCTCTGCCCCCACGTGGTGGTGCTTGTTGCCACT
GTCAGGGCTCTCAAGATGCACGGGGGCGGCCCCACGGTCACTGCTGGACTGCCTCTTCCC
AAGGCTTACATACAGGAGAACCTGGAGCTGGTTGAAAAAGGCTTCAGTAACTTGAAGAAA
CAAATTGAAAATGCCAGAATGTTTGGAATTCCAGTAGTAGTGGCCGTGAATGCATTCAAG
ACGGATACAGAGTCTGAGCTGGACCTCATCAGCCGCCTTTCCAGAGAACATGGGGCTTTT
GATGCCGTGAAGTGCACTCACTGGGCAGAAGGGGGCAAGGGTGCCTTAGCCCTGGCTCAG
GCCGTCCAGAGAGCAGCACAAGCACCCAGCAGCTTCCAGCTCCTTTATGACCTCAAGCTC
CCAGTTGAGGATAAAATCAGGATCATTGCACAGAAGATCTATGGAGCAGATGACATTGAA
TTACTTCCCGAAGCTCAACACAAAGCTGAAGTCTACACGAAGCAGGGCTTTGGGAATCTC
CCCATCTGCATGGCTAAAACACACTTGTCTTTGTCTCACAACCCAGAGCAAAAAGGTGTC
CCTACAGGCTTCATTCTGCCCATTCGCGACATCCGCGCCAGCGTTGGGGCTGGTTTTCTG
TACCCCTTAGTAGGAACGATGAGCACAATGCCTGGACTCCCCACCCGGCCCTGTTTTTAT
GATATTGATTTGGACCCTGAAACAGAACAGGTGAATGGATTATTCTAA
Target 6 GenBank Gene ID
Target 6 GeneCard ID MTHFD1 Link Image
Target 6 GenAtlas ID MTHFD1 Link Image
Target 6 HGNC ID HGNC:7432 Link Image
Target 6 Chromosome Location 14
Target 6 Locus 14q24
Target 6 SNPs SNPJam Report Link Image
Target 6 General References
  1. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  2. Hum DW, Bell AW, Rozen R, MacKenzie RE: Primary structure of a human trifunctional enzyme. Isolation of a cDNA encoding methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase. J Biol Chem. 1988 Nov 5;263(31):15946-50. [PubMed Link Image]
  3. Allaire M, Li Y, MacKenzie RE, Cygler M: The 3-D structure of a folate-dependent dehydrogenase/cyclohydrolase bifunctional enzyme at 1.5 A resolution. Structure. 1998 Feb 15;6(2):173-82. [PubMed Link Image]
  4. Hol FA, van der Put NM, Geurds MP, Heil SG, Trijbels FJ, Hamel BC, Mariman EC, Blom HJ: Molecular genetic analysis of the gene encoding the trifunctional enzyme MTHFD (methylenetetrahydrofolate-dehydrogenase, methenyltetrahydrofolate-cyclohydrolase, formyltetrahydrofolate synthetase) in patients with neural tube defects. Clin Genet. 1998 Feb;53(2):119-25. [PubMed Link Image]
Target 6 Drug References
  1. Akar N, Akar E, Ozel D, Deda G, Sipahi T: Common mutations at the homocysteine metabolism pathway and pediatric stroke. Thromb Res. 2001 Apr 15;102(2):115-20. [PubMed Link Image]
  2. Prasannan P, Pike S, Peng K, Shane B, Appling DR: Human mitochondrial C1-tetrahydrofolate synthase: gene structure, tissue distribution of the mRNA, and immunolocalization in Chinese hamster ovary calls. J Biol Chem. 2003 Oct 31;278(44):43178-87. Epub 2003 Aug 22. [PubMed Link Image]
  3. Salmassi TM, Leadbetter JR: Analysis of genes of tetrahydrofolate-dependent metabolism from cultivated spirochaetes and the gut community of the termite Zootermopsis angusticollis. Microbiology. 2003 Sep;149(Pt 9):2529-37. [PubMed Link Image]
  4. Walkup AS, Appling DR: Enzymatic characterization of human mitochondrial C1-tetrahydrofolate synthase. Arch Biochem Biophys. 2005 Oct 15;442(2):196-205. Epub 2005 Aug 30. [PubMed Link Image]
  5. Matakidou A, El Galta R, Rudd MF, Webb EL, Bridle H, Eisen T, Houlston RS: Prognostic significance of folate metabolism polymorphisms for lung cancer. Br J Cancer. 2007 Jul 16;97(2):247-52. Epub 2007 May 29. [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. Hall DA, Jordan-Starck TC, Loo RO, Ludwig ML, Matthews RG: Interaction of flavodoxin with cobalamin-dependent methionine synthase. Biochemistry. 2000 Sep 5;39(35):10711-9. [PubMed Link Image]
  2. Fowler B: The folate cycle and disease in humans. Kidney Int Suppl. 2001 Feb;78:S221-9. [PubMed Link Image]
  3. Fu TF, di Salvo M, Schirch V: Enzymatic determination of homocysteine in cell extracts. Anal Biochem. 2001 Mar;290(2):359-65. [PubMed Link Image]
  4. Jarrett JT, Choi CY, Matthews RG: Changes in protonation associated with substrate binding and Cob(I)alamin formation in cobalamin-dependent methionine synthase. Biochemistry. 1997 Dec 16;36(50):15739-48. [PubMed Link Image]
  5. Jarrett JT, Hoover DM, Ludwig ML, Matthews RG: The mechanism of adenosylmethionine-dependent activation of methionine synthase: a rapid kinetic analysis of intermediates in reductive methylation of Cob(II)alamin enzyme. Biochemistry. 1998 Sep 8;37(36):12649-58. [PubMed Link Image]
Drug Target 8 [top]
Target 8 ID 914
Target 8 Name Formimidoyltransferase-cyclodeaminase
Target 8 Synonyms
  1. EC 2.1.2.5
  2. EC 4.3.1.4
  3. FTCD
  4. Formimidoyltetrahydrofolate cyclodeaminase
  5. Formiminotransferase- cyclodeaminase
  6. Glutamate formiminotransferase
  7. Glutamate formyltransferase
  8. LCHC1
Target 8 Gene Name FTCD
Target 8 Protein Sequence >Formimidoyltransferase-cyclodeaminase 
MSQLVECVPNFSEGKNQEVIDAISGAITQTPGCVLLDVDAGPSTNRTVYTFVGPPECVVE
GALNAARVASRLIDMSRHQGEHPRMGALDVCPFIPVRGVSVDECVLCAQAFGQRLAEELD
VPVYLYGEAARMDSRRTLPAIRAGEYEALPKKLQQADWAPDFGPSSFVPSWGATATGARK
FLIAFNINLLGTKEQAHRIALNLREQGRGKDQPGRLKKVQGIGWYLDEKNLAQVSTNLLD
FEVTALHTVYEETCREAQELSLPVVGSQLVGLVPLKALLDAAAFYCEKENLFILEEEQRI
RLVVSRLGLDSLCPFSPKERIIEYLVPERGPERGLGSKSLRAFVGEVGARSAAPGGGSVA
AAAAAMGAALGSMVGLMTYGRRQFQSLDTTMRRLIPPFREASAKLTTLVDADAEAFTAYL
EAMRLPKNTPEEKDRRTAALQEGLRRAVSVPLTLAETVASLWPALQELARCGNLACRSDL
QVAAKALEMGVFGAYFNVLINLRDITDEAFKDQIHHRVSSLLQEAKTQAALVLDCLETRQ
E
Target 8 Number of Residues 550
Target 8 Molecular Weight 58927
Target 8 Theoretical pI 5.45
Target 8 GO Classification
Function
catalytic activity
transferase activity
binding
vitamin binding
folic acid binding
Process
physiological process
metabolism
Component
Not Available
Target 8 General Function Amino acid transport and metabolism
Target 8 Specific Function Folate-dependent enzyme, that displays both transferase and deaminase activity. Serves to channel one-carbon units from formiminoglutamate to the folate pool
Target 8 Pathways
Name SMPDB Link KEGG Link
One carbon pool by folate SMP00053 Link Image map00670 Link Image
Target 8 Reactions
  • 5-formimidoyltetrahydrofolate + L-glutamate = tetrahydrofolate + N-formimidoyl-L-glutamate
Target 8 Pfam Domain Function
Target 8 Signals
  • None
Target 8 Transmembrane Regions
  • None
Target 8 Essentiality Non-Essential
Target 8 GenBank ID Protein 6537208 Link Image
Target 8 UniProtKB/Swiss-Prot ID O95954 Link Image
Target 8 UniProtKB/Swiss-Prot Entry Name FTCD_HUMAN Link Image
Target 8 PDB ID Not Available
Target 8 Cellular Location
  • Cytoplasm
Target 8 Gene Sequence >1626 bp 
ATGTCCCAGCTGGTGGAATGCGTCCCCAACTTTTCGGAGGGGAAGAACCAGGAGGTGATC
GACGCCATCTCTGGAGCCATCACACAGACCCCGGGCTGCGTGCTGCTGGATGTGGACGCA
GGCCCTTCCACCAACCGCACCGTGTACACCTTCGTGGGGCCGCCGGAGTGCGTGGTGGAG
GGGGCCCTCAACGCTGCCCGGGTAGCTTCCCGACTTATCGACATGAGCAGGCACCAAGGA
GAGCACCCCCGCATGGGGGCCCTAGACGTCTGCCCCTTCATCCCCGTGAGGGGCGTCAGC
GTGGATGAGTGTGTGCTCTGCGCCCAGGCCTTTGGCCAGAGGCTGGCAGAGGAGCTGGAC
GTGCCAGTTTACCTGTACGGCGAGGCAGCCAGGATGGACAGTCGCCGGACCCTGCCGGCC
ATCCGGGCCGGGGAGTACGAGGCCCTCCCTAAGAAGCTCCAGCAGGCCGACTGGGCGCCC
GACTTTGGTCCCAGCTCCTTTGTCCCCAGTTGGGGGGCCACGGCCACGGGGGCGAGGAAG
TTCCTCATTGCTTTTAACATCAACCTGCTCGGCACAAAGGAGCAAGCCCACCGCATCGCG
CTCAACCTGCGGGAGCAGGGCCGCGGGAAGGACCAGCCAGGACGTCTGAAGAAAGTTCAG
GGCATTGGCTGGTACCTGGATGAGAAGAACCTGGCTCAGGTGTCCACCAATCTTCTGGAC
TTTGAGGTCACGGCACTGCACACGGTCTACGAGGAGACCTGCCGAGAAGCACAGGAGCTG
AGCCTCCCAGTGGTGGGCTCACAGCTGGTGGGCCTGGTGCCCCTGAAGGCTCTGCTGGAT
GCGGCCGCCTTCTACTGCGAGAAGGAGAACCTCTTCATCCTGGAGGAGGAGCAGCGGATC
AGGCTGGTGGTGAGCCGGCTGGGCCTGGACTCCCTGTGCCCCTTCAGCCCTAAGGAGCGG
ATCATCGAGTACCTGGTCCCTGAGCGCGGGCCTGAGCGAGGCCTGGGCAGCAAGTCCCTG
CGCGCCTTCGTGGGGGAGGTGGGTGCCCGCTCTGCGGCCCCCGGGGGCGGCTCGGTGGCG
GCGGCCGCTGCGGCCATGGGTGCGGCGCTGGGCTCCATGGTGGGCCTCATGACCTACGGG
CGGCGCCAATTCCAGTCCCTGGACACGACGATGCGGCGCCTGATCCCGCCCTTCCGCGAG
GCTTCGGCCAAGCTAACCACGCTGGTGGATGCCGACGCCGAGGCCTTCACCGCCTACCTG
GAAGCAATGAGGCTCCCCAAGAACACACCTGAGGAAAAGGACAGGCGCACGGCGGCCCTA
CAGGAGGGTCTGAGGCGGGCAGTCTCTGTGCCGCTGACGCTGGCGGAGACGGTGGCCTCG
CTGTGGCCGGCGCTGCAGGAACTGGCCCGGTGTGGGAACCTGGCCTGCCGGTCAGACCTC
CAGGTGGCGGCCAAAGCCCTGGAGATGGGCGTGTTTGGCGCATATTTCAACGTGCTCATC
AACCTGAGGGACATCACAGACGAGGCATTTAAGGACCAGATCCACCATCGTGTTTCCAGC
CTCCTGCAGGAAGCCAAGACCCAGGCTGCACTGGTGCTGGACTGCTTGGAGACCCGGCAG
GAGTGA
Target 8 GenBank Gene ID
Target 8 GeneCard ID FTCD Link Image
Target 8 GenAtlas ID FTCD Link Image
Target 8 HGNC ID HGNC:3974 Link Image
Target 8 Chromosome Location Not Available
Target 8 Locus Not Available
Target 8 SNPs SNPJam Report Link Image
Target 8 General References
  1. Lapierre P, Hajoui O, Homberg JC, Alvarez F: Formiminotransferase cyclodeaminase is an organ-specific autoantigen recognized by sera of patients with autoimmune hepatitis. Gastroenterology. 1999 Mar;116(3):643-9. [PubMed Link Image]
  2. Solans A, Estivill X, de la Luna S: Cloning and characterization of human FTCD on 21q22.3, a candidate gene for glutamate formiminotransferase deficiency. Cytogenet Cell Genet. 2000;88(1-2):43-9. [PubMed Link Image]
  3. Hilton JF, Christensen KE, Watkins D, Raby BA, Renaud Y, de la Luna S, Estivill X, MacKenzie RE, Hudson TJ, Rosenblatt DS: The molecular basis of glutamate formiminotransferase deficiency. Hum Mutat. 2003 Jul;22(1):67-73. [PubMed Link Image]
Target 8 Drug References
  1. Kohls D, Croteau N, Mejia N, MacKenzie RE, Vrielink A: Crystallization and preliminary X-ray analysis of the formiminotransferase domain from the bifunctional enzyme formiminotransferase-cyclodeaminase. Acta Crystallogr D Biol Crystallogr. 1999 Jun;55(Pt 6):1206-8. [PubMed Link Image]
  2. Kohls D, Sulea T, Purisima EO, MacKenzie RE, Vrielink A: The crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase: implications for substrate channeling in a bifunctional enzyme. Structure. 2000 Jan 15;8(1):35-46. [PubMed Link Image]
  3. Cook RJ: Disruption of histidine catabolism in NEUT2 mice. Arch Biochem Biophys. 2001 Aug 15;392(2):226-32. [PubMed Link Image]
  4. Bashour AM, Bloom GS: 58K, a microtubule-binding Golgi protein, is a formiminotransferase cyclodeaminase. J Biol Chem. 1998 Jul 31;273(31):19612-7. [PubMed Link Image]
Drug Target 9 [top]
Target 9 ID 1202
Target 9 Name 10-formyltetrahydrofolate dehydrogenase
Target 9 Synonyms
  1. 10-FTHFDH
  2. Aldehyde dehydrogenase 1 family member L1
  3. EC 1.5.1.6
Target 9 Gene Name ALDH1L1
Target 9 Protein Sequence >10-formyltetrahydrofolate dehydrogenase 
MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKADPLGLEAEKDGVPVFKYSRWR
AKGQALPDVVAKYQALGAELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAIN
WTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNRFLFPEGIKGMVQAV
RLIAEGKAPRLPQPEEGATYEGIQKKETAKINWDQPAEAIHNWIRGNDKVPGAWTEACEQ
KLTFFNSTLNTSGLVPEGDALPIPGAHRPGVVTKAGLILFGNDDKMLLVKNIQLEDGKMI
LASNFFKGAASSVLELTEAELVTAEAVRSVWQRILPKVLEVEDSTDFFKSGAASVDVVRL
VEEVKELCDGLELENEDVYMASTFGDFIQLLVRKLRGDDEEGECSIDYVEMAVNKRTVRM
PHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKI
SARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKI
QGSTIPINQARPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ
VTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMK
SCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIH
DEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVP
RPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDLDAVLSRANATEFGLASGVFT
RDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF
EY
Target 9 Number of Residues 917
Target 9 Molecular Weight 98830
Target 9 Theoretical pI 5.76
Target 9 GO Classification
Function
binding
cofactor binding
transferase activity
transferase activity, transferring one-carbon groups
methyltransferase activity
glycine hydroxymethyltransferase activity
hydroxymethyl-, formyl- and related transferase activity
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on the CH-NH group of donors
oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
formyltetrahydrofolate dehydrogenase activity
Process
biosynthesis
aromatic compound metabolism
folic acid and derivative metabolism
10-formyltetrahydrofolate metabolism
10-formyltetrahydrofolate catabolism
physiological process
metabolism
cellular metabolism
one-carbon compound metabolism
Component
cell
intracellular
cytoplasm
Target 9 General Function Energy production and conversion
Target 9 Specific Function 10-formyltetrahydrofolate + NADP(+) + H(2)O = tetrahydrofolate + CO(2) + NADPH
Target 9 Pathways
Name SMPDB Link KEGG Link
One carbon pool by folate SMP00053 Link Image map00670 Link Image
Target 9 Reactions
  • 10-formyltetrahydrofolate + NADP+ + H2O = tetrahydrofolate + CO2 + NADPH + H+
Target 9 Pfam Domain Function
Target 9 Signals
  • None
Target 9 Transmembrane Regions
  • None
Target 9 Essentiality Non-Essential
Target 9 GenBank ID Protein 3560541 Link Image
Target 9 UniProtKB/Swiss-Prot ID O75891 Link Image
Target 9 UniProtKB/Swiss-Prot Entry Name FTHFD_HUMAN Link Image
Target 9 PDB ID 1S3I Link Image
Target 9 PDB File Show
Target 9 3D Structure
Target 9 Cellular Location
  • Cytoplasm
Target 9 Gene Sequence >2709 bp 
ATGAAGATTGCAGTGATTGGACAGAGCCTGTTTGGCCAGGAAGTTTACTGCCACCTGAGG
AAGGAGGGCCACGAAGTGGTGGGTGTGTTCACTGTTCCAGACAAGGATGGAAAGGCCGAC
CCCCTGGGTCTGGAAGCTGAGAAGGATGGAGTGCCGGTATTCAAGTACTCCCGGTGGCGT
GCAAAAGCGCAAGCTTTGCCTGATGTGGTGGCAAAATACCAGGCTTTGGGGGCCGAACTC
AACGTCCTGCCCTCCTGCAGCCAATTCATCCCCATGGAGATAATCAGTGCCCCCCGGCAT
GGCTCCATCATCTATCACCCGTCACTGCTCCCTAGGCACCGAGGGGCCTCGGCCATCAAC
TGGACCCTCATTCACGGAGATAAGAAAGGGGGGTTTTCCATCTTCTGGGCGGATGATGGT
CTGGACACCGGAGACCTGCTGCTGCAGAAGGAGTGTGAGGTGCTCCCGGACGACACCGTG
AGCACGCTGTACAACCGCTTCCTCTTCCCTGAAGGCATCAAAGGGGTGGTGCAGGCCGTG
AGGCTGATCGCTGAGGGCAAAGCCCCCAGACTCCCTCAGCCTAAGGAAGGAGCCACCTAT
GAGGGGATTCAGAAGAAGGAGACAGCCAAGATCAACTGGGACCAGCCGGCAGAGGCCATT
CACAACTGGATCCGCGGGAACGACAAGGTGCCGGGAGCCTGGACAGAGGCCTGTGAACAG
AAACTGACATTTTTCAACTCAACGCTGAACACTTCAGGCCTGGTGCCCGAGGGAGACGCT
TTGCCCATCCCAGGAGCCCATCGGCCAGGGGTGGTCACCAAAGCAGGACTCATCCTCTTT
GGGAATGATGACAAAATGCTGCTGGTGAAGAATATTCAGCTGGAGGATGGCAAAATGATC
CTGGCCTCGAACTTCTTTAAGGGGGCAGCCAGCAGTGTCCTTGAGCTGACAGAGGCAGAG
CTGGTTACTGCGGAGGCTGTGCGGAGTGTTTGGCAGCGGATCCTCCCCAAAGTACTGGAG
GTTGAAGACTCCACTGATTTCTTCAAGTCAGGGGCCGCGTCTGTGGACGTTGTGAGGCTG
GTGGAGGAAGTGAAGGAGCTGTGTGATGGCCTGGAGTTAGAAAATGAAGATGTGTACATG
GCATCCACCTTTGGGGACTTCATCCAGCTGTTAGTGAGGAAGCTGCGAGGGGACGATGAG
GAGGGCGAGTGCAGCATTGACTACGTGGAAATGGCAGTGAACAAGCGCACTGTCCGCATG
CCCCACCAGCTCTTCATTGGGGGGGAGTTCGTGGATGCCGAGGGCGCCAAGACCTCTGAG
ACCATCAATCCCACCGATGGAAGTGTCATCTGCCAGGTATCCCTGGCCCAAGTCACCGAC
GTCGACAAGGCAGTGGCCGCNGCCAAGGGTGCCTTTGAGAATGGACGGTGGGGGAAGATC
AGTGCGCGGGACCGGGGCCGGCTGATGTACAGGTTGGCAGATCTCATGGAGCAGCACCAG
GAGGAGCTGGCCACCATTGAGGCCCTGGATGCGGGTGCCGTCTACACGCTGGCCCTGAAG
ACCCACGTGGGCATGTCCATCCAGACCTTCCGATACTTTGCTGGCTGGTGTGACAAGATC
CAGGGCTCCACCATCCCCATCAACCAGGCCAGACCCAACCGCAACCTGACCTTGACCAGG
AAGGAGCCTGTTGGGGTTTGTGGCATCATCATCCCCTGGAACTATCCCCTGATGATGCTG
TCCTGGAAGACAGCTGCCTGCCTGGCTGCCGGGAACACAGTGGTGATCAAGCCTGCTCAG
GTGACCCCACTCACAGCCTTGAAGTTTGCAGAGCTGACATTAAAGGCCGGGATTCCCAAA
GGTGTGGTCAACGTCCTCCCAGGATCTGGCTCCCTGGTCGGCCAGAGACTCTCAGACCAT
CCTGATGTGAGGAAAATCGGGTTCACAGGCTCCACAGAGGTGGGCAAGCACATCATGAAA
AGCTGTGCCATAAGTAACGTGAAGAAGGTGTCCCTGGAACTGGGCGGGGAGTCACCCTTC
ATCATCTTTGCTGACTGTGACCTCAACAAGGCTGTGCAGATGGGGATGAGTTCTGTTTTC
TTCAGCAAAGGAGAGAATTGCATTGCAGCAGGCCGACTCTTTGTGGAGGACTCCATTCAT
GATGAGTTCGTGCGGAGAGTGGTAGAAGAGGTGCGGAAGATGAAGGTGGGCAACCCGCTG
GACAGGGACACCGACCACGGGCCGCAGAATCACCATGCCCACCTTGTGAAGCTGATGGAG
TACTGCCAGCATGGCGTGAAGGAAGGGGCCACACTGGTCTGCGGCGGGAATCAGGTCCCT
CGGCCAGGGTTCTTCTTTGAGCCAACTGTTTTCACAGACGTGGAAGACCACATGTTCATA
GCCAAGGAGGAGTCCTTCGGGCCTGTCATGATCATCTCTCGGTTTGCTGATGGGGACTTG
GATGCCGTGCTGTCTCGGGCCAATGCCACGGAATTTGGCCTGGCTTCTGGTGTCTTCACC
AGGGACATCAACAAGGCCCTGTATGTCAGTGACAAGCTCCAGGCAGGCACTGTGTTTGTC
AACACGTACAACAAGACCGACGTGGCCGCTCCCTTCGGAGGATTCAAACAGTCTGGATTT
GGCAAAGATCTAGGAGAGGCGGCTCTGAACGAGTACCTGCGGGTCAAGACAGTGACCTTC
GAATACTGA
Target 9 GenBank Gene ID
Target 9 GeneCard ID ALDH1L1 Link Image
Target 9 GenAtlas ID ALDH1L1 Link Image
Target 9 HGNC ID HGNC:3978 Link Image
Target 9 Chromosome Location 3
Target 9 Locus 3q21.2
Target 9 SNPs SNPJam Report Link Image
Target 9 General References Not Available
Target 9 Drug References
  1. Fu TF, Maras B, Barra D, Schirch V: A noncatalytic tetrahydrofolate tight binding site is on the small domain of 10-formyltetrahydrofolate dehydrogenase. Arch Biochem Biophys. 1999 Jul 15;367(2):161-6. [PubMed Link Image]
  2. Krupenko SA, Wagner C: Aspartate 142 is involved in both hydrolase and dehydrogenase catalytic centers of 10-formyltetrahydrofolate dehydrogenase. J Biol Chem. 1999 Dec 10;274(50):35777-84. [PubMed Link Image]
  3. Krupenko SA, Vlasov AP, Wagner C: On the role of conserved histidine 106 in 10-formyltetrahydrofolate dehydrogenase catalysis: connection between hydrolase and dehydrogenase mechanisms. J Biol Chem. 2001 Jun 29;276(26):24030-7. Epub 2001 Apr 24. [PubMed Link Image]
  4. Anguera MC, Field MS, Perry C, Ghandour H, Chiang EP, Selhub J, Shane B, Stover PJ: Regulation of folate-mediated one-carbon metabolism by 10-formyltetrahydrofolate dehydrogenase. J Biol Chem. 2006 Jul 7;281(27):18335-42. Epub 2006 Apr 20. [PubMed Link Image]
  5. Oleinik NV, Krupenko NI, Reuland SN, Krupenko SA: Leucovorin-induced resistance against FDH growth suppressor effects occurs through DHFR up-regulation. Biochem Pharmacol. 2006 Jul 14;72(2):256-66. Epub 2006 Apr 25. [PubMed Link Image]
Drug Target 10 [top]
Target 10 ID 2287
Target 10 Name Bifunctional purine biosynthesis protein PURH [Includes: Phosphoribosylaminoimidazolecarboxamide formyltransferase
Target 10 Synonyms
  1. 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
  2. AICAR transformylase
  3. EC 2.1.2.3
  4. EC 3.5.4.10
  5. IMP cyclohydrolase
  6. IMP synthetase
  7. Inosinicase
Target 10 Gene Name ATIC
Target 10 Protein Sequence >Bifunctional purine biosynthesis protein PURH [Includes: Phosphoribosylaminoimidazolecarboxamide formyltransferase 
MAPGQLALFSVSDKTGLVEFARNLTALGLNLVASGGTAKALRDAGLAVRDVSELTGFPEM
LGGRVKTLHPAVHAGILARNIPEDNADMARLDFNLIRVVACNLYPFVKTVASPGVTVEEA
VEQIDIGGVTLLRAAAKNHARVTVVCEPEDYVVVSTEMQSSESKDTSLETRRQLALKAFT
HTAQYDEAISDYFRKQYSKGVSQMPLRYGMNPHQTPAQLYTLQPKLPITVLNGAPGFINL
CDALNAWQLVKELKEALGIPAAASFKHVSPAGAAVGIPLSEDEAKVCMVYDLYKTLTPIS
AAYARARGADRMSSFGDFVALSDVCDVPTAKIISREVSDGIIAPGYEEEALTILSKKKNG
NYCVLQMDQSYKPDENEVRTLFGLHLSQKRNNGVVDKSLFSNVVTKNKDLPESALRDLIV
ATIAVKYTQSNSVCYAKNGQVIGIGAGQQSRIHCTRLAGDKANYWWLRHHPQVLSMKFKT
GVKRAEISNAIDQYVTGTIGEDEDLIKWKALFEEVPELLTEAEKKEWVEKLTEVSISSDA
FFPFRDNVDRAKRSGVAYIAAPSGSAADKVVIEACDELGIILAHTNLRLFHH
Target 10 Number of Residues 601
Target 10 Molecular Weight 64616
Target 10 Theoretical pI 6.70
Target 10 GO Classification
Function
transferase activity
transferase activity, transferring one-carbon groups
methyltransferase activity
glycine hydroxymethyltransferase activity
hydroxymethyl-, formyl- and related transferase activity
phosphoribosylaminoimidazolecarboxamide formyltransferase activity
catalytic activity
hydrolase activity
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
cyclohydrolase activity
IMP cyclohydrolase activity
Process
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
nucleotide metabolism
purine nucleotide metabolism
purine nucleotide biosynthesis
Component
Not Available
Target 10 General Function Nucleotide transport and metabolism
Target 10 Specific Function 10-formyltetrahydrofolate + 5-amino-1-(5- phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5- formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Target 10 Pathways
Name SMPDB Link KEGG Link
Purine metabolism SMP00050 Link Image map00230 Link Image
Target 10 Reactions
  • 10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Target 10 Pfam Domain Function
Target 10 Signals
  • None
Target 10 Transmembrane Regions
  • None
Target 10 Essentiality Non-Essential
Target 10 GenBank ID Protein 1263196 Link Image
Target 10 UniProtKB/Swiss-Prot ID P31939 Link Image
Target 10 UniProtKB/Swiss-Prot Entry Name PUR9_HUMAN Link Image
Target 10 PDB ID 1P4R Link Image
Target 10 PDB File Show
Target 10 3D Structure
Target 10 Cellular Location
  • Cytoplasmic
Target 10 Gene Sequence >1776 bp 
ATGTCTTCTCTCTCAGCCTTATTTAGTGTCTCTGACAAAACCGGCCTTGTGGAATTTGCA
AGAAACCTGACCGCTCTTGGTTTGAACCTGGTCGCTTCCGGAGGGACTGCAAAAGCTCTC
AGGGATGCTGGTCTGGCAGTCAGAGATGTCTCTGAGTTGACGGGATTTCCTGAAATGTTG
GGGGGACGTGTGAAAACTTTGCATCCTGCAGTCCATGCTGGAATCCTAGCTCGTAATATT
CCAGAAGATAATGCTGACATGGCCAGACTTGATTTCAATCTTATAAGAGTTGTCGCCTGC
AATCTCTATCCCTTTGTAAAGACAGTGGCTTCTCCAGGTGTAACTGTTGAGGAGGCTGTG
GAGCAAATTGACATTGGTGGAGTAACCTTACTGAGAGCTGCAGCCAAAAACCACGCTCGA
GTGACAGTGGTGTGTGAACCAGAGGACTATGTGGTGGTGTCCACGGAGATGCAGAGCTCC
GAGAGTAAGGGCACCTCCTTGGAGACTAGACGCCAGTTAGCCTTGAAGGCATTCACTCAT
ACGGCACAATATGATGAAGCAATTTCAGATTATTTCAGGAAACAGTACAGCAAAGGCGTA
TCTCAGATGCCCTTGAGATATGGAATGAACCCACATCAGACCCCTGCCCAGCTGTACACA
CTGCAGCCCAAGCTTCCCATCACAGTTCTAAATGGAGCCCCTGGATTTATAAACTTGTGC
GATGCTTTGAACGCCTGGCAGCTGGTGAAGGAACTCAAGGAGGCTTTAGGTATTCCAGCC
GCTGCCTCTTTCAAACATGTCAGCCCAGCAGGTGCTGCTGTTGGAATTCCACTCAGTGAA
GATGAGGCCAAAGTCTGCATGGTTTATGATCTCTATAAAACCCTCACACCCATCTCAGCG
GCATATGCAAGAGCAAGAGGGGCTGATAGGATGTCTTCATTTGGTGATTTTGTTGCATTG
TCTGATGTTTGTGATGTACCAACTGCAAAAATTATTTCCAGAGAAGTATCTGATGGTATA
ATTGCCCCAGGATATGAAGAAGAAGCCTTGACAATACTTTCCAAAAAGAAAAATGGAAAC
TATTGTGTCCTTCAGATGGACCAATCTTACAAACCAGATGAAAATGAAGTTCGAACTCTC
TTTGGTCTTCATTTAAGCCAGAAGAGAAATAATGGTGTCGTCGACAAGTCATTATTTAGC
AATGTTGTTACCAAAAATAAAGATTTGCCAGAGTCTGCCCTCCGAGACCTCATCGTAGCC
ACCATTGCTGTCAAGTACACTCAGTCTAACTCTGTGTGCTACGCCAAGAACGGGCAGGTT
ATCGGCATTGGAGCAGGACAGCAGTCTCGTATACACTGCACTCGCCTTGCAGGAGATAAG
GCAAACTATTGGTGGCTTAGACACCATCCACAAGTGCTTTCGATGAAGTTTAAAACAGGA
GTGAAGAGAGCAGAAATCTCCAATGCCATCGATCAATATGTGACTGGAACCATTGGCGAG
GATGAAGATTTGATAAAGTGGAAGGCACTGTTTGAGGAAGTCCCTGAGTTACTCACTGAG
GCAGAGAAGAAGGAATGGGTTGAGAAACTGACTGAAGTTTCTATCAGCTCTGATGCCTTC
TTCCCTTTCCGAGATAACGTAGACAGAGCTAAAAGGAGTGGTGTGGCGTACATTGCGGCT
CCCTCCGGTTCTGCTGCTGACAAAGTTGTGATTGAGGCCTGCGACGAACTGGGAATCATC
CTCGCTCATACGAACCTTCGGCTCTTCCACCACTGA
Target 10 GenBank Gene ID
Target 10 GeneCard ID ATIC Link Image
Target 10 GenAtlas ID ATIC Link Image
Target 10 HGNC ID HGNC:794 Link Image
Target 10 Chromosome Location 2
Target 10 Locus 2q35
Target 10 SNPs SNPJam Report Link Image
Target 10 General References
  1. Rasmussen HH, van Damme J, Puype M, Gesser B, Celis JE, Vandekerckhove J: Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. Electrophoresis. 1992 Dec;13(12):960-9. [PubMed Link Image]
  2. Rayl EA, Moroson BA, Beardsley GP: The human purH gene product, 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase. Cloning, sequencing, expression, purification, kinetic analysis, and domain mapping. J Biol Chem. 1996 Jan 26;271(4):2225-33. [PubMed Link Image]
  3. Yamauchi M, Seki N, Mita K, Saito T, Tsuji S, Hongo E, Morimyo M, Shiomi T, Koyama H, Ayusawa D: Isolation of human purH gene expressed in the rodent transformant cells by subtractive enrichment of 3'-untranslated region of human transcript. DNA Res. 1995 Dec 31;2(6):269-75. [PubMed Link Image]
  4. Sugita T, Aya H, Ueno M, Ishizuka T, Kawashima K: Characterization of molecularly cloned human 5-aminoimidazole-4-carboxamide ribonucleotide transformylase. J Biochem (Tokyo). 1997 Aug;122(2):309-13. [PubMed Link Image]
Target 10 Drug References
  1. Bulock KG, Beardsley GP, Anderson KS: The kinetic mechanism of the human bifunctional enzyme ATIC (5-amino-4-imidazolecarboxamide ribonucleotide transformylase/inosine 5'-monophosphate cyclohydrolase). A surprising lack of substrate channeling. J Biol Chem. 2002 Jun 21;277(25):22168-74. Epub 2002 Apr 10. [PubMed Link Image]
  2. Wolan DW, Greasley SE, Wall MJ, Benkovic SJ, Wilson IA: Structure of avian AICAR transformylase with a multisubstrate adduct inhibitor beta-DADF identifies the folate binding site. Biochemistry. 2003 Sep 23;42(37):10904-14. [PubMed Link Image]
Drug Target 11 [top]
Target 11 ID 3879
Target 11 Name Serine hydroxymethyltransferase 2
Target 11 Synonyms
  1. Mitochondrial
Target 11 Gene Name Not Available
Target 11 Protein Sequence >Serine hydroxymethyltransferase 2 
MLYFSLFWAARPLQRCGQLVRMAIRAQHSNAAQTQTGEANRGWTGQESLSDSDPEMWELL
QREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQ
RRALEAFDLDPAQWGVNVQPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDV
KRISATSIFFESMPYKLNPKTGLIDYNQLALTARLFRPRLIIAGTSAYARLIDYARMREV
CDEVKAHLLADMAHISGLVAAKVIPSPFKHADIVTTTTHKTLRGARSGLIFYRKGVKAVD
PKTGREIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARA
MADALLERGYSLVSGGTDNHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAIT
PGGLRLGAPALTSRQFHEDDFRRVVDFIDEGVNIGLEVKSKTAKLQDFKSFLLKDSETSQ
RLANLRQRVEQFARAFPMPGFDEH
Target 11 Number of Residues 512
Target 11 Molecular Weight 55975
Target 11 Theoretical pI 8.53
Target 11 GO Classification
Function
catalytic activity
transferase activity
transferase activity, transferring one-carbon groups
methyltransferase activity
glycine hydroxymethyltransferase activity
Process
L-serine metabolism
physiological process
metabolism
cellular metabolism
amino acid and derivative metabolism
amino acid metabolism
serine family amino acid metabolism
glycine metabolism
Component
Not Available
Target 11 General Function Amino acid transport and metabolism
Target 11 Specific Function Not Available
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 62898842 Link Image
Target 11 UniProtKB/Swiss-Prot ID Q53ET4 Link Image
Target 11 UniProtKB/Swiss-Prot Entry Name Q53ET4_HUMAN Link Image
Target 11 PDB ID Not Available
Target 11 Cellular Location Not Available
Target 11 Gene Sequence >1515 bp 
ATGCTGTACTTCTCTTTGTTTTGGGCGGCTCGGCCTCTGCAGAGATGTGGGCAGCTGGTC
AGGATGGCCATTCGGGCTCAGCACAGCAACGCAGCCCAGACTCAGACTGGGGAAGCAAAC
AGGGGCTGGACAGGCCAGGAGAGCCTGTCGGACAGTGATCCTGAGATGTGGGAGTTGCTG
CAGAGGGAGAAGGACAGGCAGTGTCGTGGCCTGGAGCTCATTGCCTCAGAGAACTTCTGC
AGCCGAGCTGCGCTGGAGGCCCTGGGGTCCTGTCTGAACAACAAGTACTCGGAGGGTTAT
CCTGGCAAGAGATACTATGGGGGAGCAGAGGTGGTGGATGAAATTGAGCTGCTGTGCCAG
CGCCGGGCCTTGGAAGCCTTTGACCTGGATCCTGCACAGTGGGGAGTCAATGTCCAGCCC
TACTCCGGGTCCCCAGCCAACCTGGCCGTCTACACAGCCCTTCTGCAACCTCACGACCGG
ATCATGGGGCTGGACCTGCCCGATGGGGGCCATCTCACCCACGGCTACATGTCTGACGTC
AAGCGGATATCAGCCACGTCCATCTTCTTCGAGTCTATGCCCTATAAGCTCAACCCCAAA
ACTGGCCTCATTGACTACAACCAGCTGGCACTGACTGCTCGACTTTTCCGGCCACGGCTC
ATCATAGCTGGCACCAGCGCCTATGCTCGCCTCATTGACTACGCCCGCATGAGAGAGGTG
TGTGATGAAGTCAAAGCACACCTGCTGGCAGACATGGCCCACATCAGTGGCCTGGTGGCT
GCCAAGGTGATTCCCTCGCCTTTCAAGCACGCGGACATCGTCACCACCACTACTCACAAG
ACTCTTCGAGGGGCCAGGTCAGGGCTCATCTTCTACCGGAAAGGGGTGAAGGCTGTGGAC
CCCAAGACTGGCCGGGAGATCCCTTACACATTTGAGGACCGAATCAACTTTGCCGTGTTC
CCATCCCTGCAGGGGGGCCCCCACAATCATGCCATTGCTGCAGTAGCTGTGGCCCTAAAG
CAGGCCTGCACCCCCATGTTCCGGGAGTACTCCCTGCAGGTTCTGAAGAATGCTCGGGCC
ATGGCAGATGCCCTGCTAGAGCGAGGCTACTCACTGGTATCAGGTGGTACTGACAACCAC
CTGGTGCTGGTGGACCTGCGGCCCAAGGGCCTGGATGGAGCTCGGGCTGAGCGGGTGCTA
GAGCTTGTATCCATCACTGCCAACAAGAACACCTGTCCTGGAGACCGAAGTGCCATCACA
CCGGGCGGCCTGCGGCTTGGGGCCCCAGCCTTAACTTCTCGACAGTTCCATGAGGATGAC
TTCCGGAGAGTTGTGGACTTTATAGATGAAGGGGTCAACATTGGCTTAGAGGTGAAGAGC
AAGACTGCCAAGCTCCAGGATTTCAAATCCTTCCTGCTTAAGGACTCAGAAACAAGTCAG
CGTCTGGCCAACCTCAGGCAACGGGTGGAGCAGTTTGCCAGGGCCTTCCCCATGCCTGGT
TTTGATGAGCATTGA
Target 11 GenBank Gene ID
Target 11 GeneCard ID Not Available
Target 11 GenAtlas ID Not Available
Target 11 HGNC ID HGNC:10852 Link Image
Target 11 Chromosome Location Not Available
Target 11 Locus Not Available
Target 11 SNPs Not Available
Target 11 General References
  1. Maruyama K, Sugano S: Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. Gene. 1994 Jan 28;138(1-2):171-4. [PubMed Link Image]
  2. Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S: Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. Gene. 1997 Oct 24;200(1-2):149-56. [PubMed Link Image]
Target 11 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]
  3. Chang WN, Tsai JN, Chen BH, Huang HS, Fu TF: Serine hydroxymethyltransferase isoforms are differentially inhibited by leucovorin-Characterization and comparison of recombinant zebrafish serine hydroxymethyltransferases. Drug Metab Dispos. 2007 Jul 30;. [PubMed Link Image]
Drug Target 12 [top]
Target 12 ID 3884
Target 12 Name SHMT2 protein
Target 12 Synonyms Not Available
Target 12 Gene Name SHMT2
Target 12 Protein Sequence >SHMT2 protein 
ELRCCTSLCFGRLGLCRDVGSWSGWPFGLSTATQPRLRLGKQTGAGQARRACRTVILRCG
SCCRGRRTGSVVAWSSLPQRYYGGAEVVDEIELLCQRRALEAFDLDPAQWGVNVQPYSGS
PANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLNPKTGLI
DYNQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLADMAHISGLVAAKVI
PSPFKHADIVTTTTHKTLRGARSGLIFYRKGVKAVDPKTGREIPYTFEDRINFAVFPSLQ
GGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARAMADALLERGYSLVSGGTDNHLVLV
DLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDFRRV
VDFIDEGVNIGLEVKSKTAKLQDFKSFLLKDSETSQRLANLRQRVEQFARAFPMPGFDEH
Target 12 Number of Residues 488
Target 12 Molecular Weight 52910
Target 12 Theoretical pI 9.66
Target 12 GO Classification
Function
catalytic activity
transferase activity
transferase activity, transferring one-carbon groups
methyltransferase activity
glycine hydroxymethyltransferase activity
Process
L-serine metabolism
physiological process
metabolism
cellular metabolism
amino acid and derivative metabolism
amino acid metabolism
serine family amino acid metabolism
glycine metabolism
Component
Not Available
Target 12 General Function Amino acid transport and metabolism
Target 12 Specific Function Not Available
Target 12 Pathways Not Available
Target 12 Reactions Not Available
Target 12 Pfam Domain Function
Target 12 Signals
  • None
Target 12 Transmembrane Regions
  • None
Target 12 Essentiality Non-Essential
Target 12 GenBank ID Protein 60552225 Link Image
Target 12 UniProtKB/Swiss-Prot ID Q5BJF5 Link Image
Target 12 UniProtKB/Swiss-Prot Entry Name Q5BJF5_HUMAN Link Image
Target 12 PDB ID Not Available
Target 12 Cellular Location Not Available
Target 12 Gene Sequence >1445 bp 
CCGAGTTGCGATGCTGTACTTCTCTTTGTTTTGGGCGGCTCGGCCTCTGCAGAGATGTGG
GCAGCTGGTCAGGATGGCCATTCGGGCTCAGCACAGCAACGCAGCCCAGACTCAGACTGG
GGAAGCAAACAGGGGCTGGACAGGCCAGGAGAGCCTGTCGGACAGTGATCCTGAGATGTG
GGAGTTGCTGCAGAGGGAGAAGGACAGGCAGTGTCGTGGCCTGGAGCTCATTGCCTCAGA
GATACTATGGGGGAGCAGAGGTGGTGGATGAAATTGAGCTGCTGTGCCAGCGCCGGGCCT
TGGAAGCCTTTGACCTGGATCCTGCACAGTGGGGAGTCAATGTCCAGCCCTACTCCGGGT
CCCCAGCCAACCTGGCCGTCTACACAGCCCTTCTGCAACCTCACGACCGGATCATGGGGC
TGGACCTGCCCGATGGGGGCCATCTCACCCACGGCTACATGTCTGACGTCAAGCGGATAT
CAGCCACGTCCATCTTCTTCGAGTCTATGCCCTATAAGCTCAACCCCAAAACTGGCCTCA
TTGACTACAACCAGCTGGCACTGACTGCTCGACTTTTCCGGCCACGGCTCATCATAGCTG
GCACCAGCGCCTATGCTCGCCTCATTGACTACGCCCGCATGAGAGAGGTGTGTGATGAAG
TCAAAGCACACCTGCTGGCAGACATGGCCCACATCAGTGGCCTGGTGGCTGCCAAGGTGA
TTCCCTCGCCTTTCAAGCACGCGGACATCGTCACCACCACTACTCACAAGACTCTTCGAG
GGGCCAGGTCAGGGCTCATCTTCTACCGGAAAGGGGTGAAGGCTGTGGACCCCAAGACTG
GCCGGGAGATCCCTTACACATTTGAGGACCGAATCAACTTTGCCGTGTTCCCATCCCTGC
AGGGGGGCCCCCACAATCATGCCATTGCTGCAGTAGCTGTGGCCCTAAAGCAGGCCTGCA
CCCCCATGTTCCGGGAGTACTCCCTGCAGGTTCTGAAGAATGCTCGGGCCATGGCAGATG
CCCTGCTAGAGCGAGGCTACTCACTGGTATCAGGTGGTACTGACAACCACCTGGTGCTGG
TGGACCTGCGGCCCAAGGGCCTGGATGGAGCTCGGGCTGAGCGGGTGCTAGAGCTTGTAT
CCATCACTGCCAACAAGAACACCTGTCCTGGAGACCGAAGTGCCATCACACCGGGCGGCC
TGCGGCTTGGGGCCCCAGCCTTAACTTCTCGACAGTTCCGTGAGGATGACTTCCGGAGAG
TTGTGGACTTTATAGATGAAGGGGTCAACATTGGCTTAGAGGTGAAGAGCAAGACTGCCA
AGCTCCAGGATTTCAAATCCTTCCTGCTTAAGGACTCAGAAACAAGTCAGCGTCTGGCCA
ACCTCAGGCAACGGGTGGAGCAGTTTGCCAGGGCCTTCCCCATGCCTGGTTTTGATGAGC
ATTGA
Target 12 GenBank Gene ID
Target 12 GeneCard ID SHMT2 Link Image
Target 12 GenAtlas ID SHMT2 Link Image
Target 12 HGNC ID HGNC:10852 Link Image
Target 12 Chromosome Location 12
Target 12 Locus 12q12-q14
Target 12 SNPs SNPJam Report Link Image
Target 12 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Target 12 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]
Drug Target 13 [top]
Target 13 ID 3885
Target 13 Name Hypothetical protein DKFZp686P09201
Target 13 Synonyms Not Available
Target 13 Gene Name DKFZp686P09201
Target 13 Protein Sequence >Hypothetical protein DKFZp686P09201 
MAIRAQHSNAAQTQTGEANRGWTGQESLSDSDPEMWELLQREKDRQCRGLELIASENFCS
RAALEALGSCLNNKYPEGYPGKRYYGGAEVVDEIELLCQRRALEAFDLDPAQWGVNVQPY
SGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLNPKT
GLIDYNQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLADMAHISGLVAA
KVIPSPFKHADIVTTTTHKTLRGARSGLIFYRKGVKAVDPKTGREIPYTFEDRINFAVFP
SLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARAMADALLERGYSLVSGGTDNHL
VLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDF
RRVVDFIDEGVNIGLEVKSKTAKLQDFKSFLLKDSETSQRLANLRQRVEQFARAFPMPGF
DEH
Target 13 Number of Residues 491
Target 13 Molecular Weight 53466
Target 13 Theoretical pI 8.27
Target 13 GO Classification
Function
catalytic activity
transferase activity
transferase activity, transferring one-carbon groups
methyltransferase activity
glycine hydroxymethyltransferase activity
Process
L-serine metabolism
physiological process
metabolism
cellular metabolism
amino acid and derivative metabolism
amino acid metabolism
serine family amino acid metabolism
glycine metabolism
Component
Not Available
Target 13 General Function Amino acid transport and metabolism
Target 13 Specific Function Not Available
Target 13 Pathways Not Available
Target 13 Reactions Not Available
Target 13 Pfam Domain Function
Target 13 Signals
  • None
Target 13 Transmembrane Regions
  • None
Target 13 Essentiality Non-Essential
Target 13 GenBank ID Protein 57997528 Link Image
Target 13 UniProtKB/Swiss-Prot ID Q5HYG8 Link Image
Target 13 UniProtKB/Swiss-Prot Entry Name Q5HYG8_HUMAN Link Image
Target 13 PDB ID Not Available
Target 13 Cellular Location Not Available
Target 13 Gene Sequence >1452 bp 
ATGGCCATTCGGGCTCAGCACAGCAACGCAGCCCAGACTCAGACTGGGGAAGCAAACAGG
GGCTGGACAGGCCAGGAGAGCCTGTCGGACAGTGATCCTGAGATGTGGGAGTTGCTGCAG
AGGGAGAAGGACAGGCAGTGTCGTGGCCTGGAGCTCATTGCCTCAGAGAACTTCTGCAGC
CGAGCTGCGCTGGAGGCCCTGGGGTCCTGTCTGAACAACAAGTACCCGGAGGGTTATCCT
GGCAAGAGATACTATGGGGGAGCAGAGGTGGTGGATGAAATTGAGCTGCTGTGCCAGCGC
CGGGCCTTGGAAGCCTTTGACCTGGATCCTGCACAGTGGGGAGTCAATGTCCAGCCCTAC
TCCGGGTCCCCAGCCAACCTGGCCGTCTACACAGCCCTTCTGCAACCTCACGACCGGATC
ATGGGGCTGGACCTGCCCGATGGGGGCCATCTCACCCACGGCTACATGTCTGACGTCAAG
CGGATATCAGCCACGTCCATCTTCTTCGAGTCTATGCCCTATAAGCTCAACCCCAAAACT
GGCCTCATTGACTACAACCAGCTGGCACTGACTGCTCGACTTTTCCGGCCACGGCTCATC
ATAGCTGGCACCAGCGCCTATGCTCGCCTCATTGACTACGCCCGCATGAGAGAGGTGTGT
GATGAAGTCAAAGCACACCTGCTGGCAGACATGGCCCACATCAGTGGCCTGGTGGCTGCC
AAGGTGATTCCCTCGCCTTTCAAGCACGCGGACATCGTCACCACCACTACTCACAAGACT
CTTCGAGGGGCCAGGTCAGGGCTCATCTTCTACCGGAAAGGGGTGAAGGCTGTGGACCCC
AAGACTGGCCGGGAGATCCCTTACACATTTGAGGACCGAATCAACTTTGCCGTGTTCCCA
TCCCTGCAGGGGGGCCCCCACAATCATGCCATTGCTGCAGTAGCTGTGGCCCTAAAGCAG
GCCTGCACCCCCATGTTCCGGGAGTACTCCCTGCAGGTTCTGAAGAATGCTCGGGCCATG
GCAGATGCCCTGCTAGAGCGAGGCTACTCACTGGTATCAGGTGGTACTGACAACCACCTG
GTGCTGGTGGACCTGCGGCCCAAGGGCCTGGATGGAGCTCGGGCTGAGCGGGTGCTAGAG
CTTGTATCCATCACTGCCAACAAGAACACCTGTCCTGGAGACCGAAGTGCCATCACACCG
GGCGGCCTGCGGCTTGGGGCCCCAGCCTTAACTTCTCGACAGTTCCGTGAGGATGACTTC
CGGAGAGTTGTGGACTTTATAGATGAAGGGGTCAACATTGGCTTAGAGGTGAAGAGCAAG
ACTGCCAAGCTCCAGGATTTCAAATCCTTCCTGCTTAAGGACTCAGAAACAAGTCAGCGT
CTGGCCAACCTCAGGCAACGGGTGGAGCAGTTTGCCAGGGCCTTCCCCATGCCTGGTTTT
GATGAGCATTGA
Target 13 GenBank Gene ID
Target 13 GeneCard ID DKFZp686P09201 Link Image
Target 13 GenAtlas ID DKFZp686P09201 Link Image
Target 13 HGNC ID HGNC:10852 Link Image
Target 13 Chromosome Location Not Available
Target 13 Locus Not Available
Target 13 SNPs SNPJam Report Link Image
Target 13 General References Not Available
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]
Drug Target 14 [top]
Target 14 ID 3901
Target 14 Name SHMT2 protein
Target 14 Synonyms Not Available
Target 14 Gene Name Not Available
Target 14 Protein Sequence >SHMT2 protein 
MLYFSLFWAARPLQRCGQLVRMAIRAQHSNAAQTQTGEANRGWTGQESLSDSDPEMWELL
QREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQ
RRALEAFDLDPAQWGVNVQPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDV
KRISATSIFFESMPYKLNLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLA
DMAHISGLVAAKVIPSPFKHADIVTTTTHKTLRGARSGLIFYRKGVKAVDPKTGREIPYT
FEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARAMADALLERGY
SLVSGGTDNHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPA
LTSRQFREDDFRRVVDFIDEGVNIGLEVKSKTAKLQDFKSFLLKDSETSQRLANLRQRVE
QFARAFPMPGFDEH
Target 14 Number of Residues 502
Target 14 Molecular Weight 54863
Target 14 Theoretical pI 8.68
Target 14 GO Classification
Function
catalytic activity
transferase activity
transferase activity, transferring one-carbon groups
methyltransferase activity
glycine hydroxymethyltransferase activity
Process
L-serine metabolism
physiological process
metabolism
cellular metabolism
amino acid and derivative metabolism
amino acid metabolism
serine family amino acid metabolism
glycine metabolism
Component
Not Available
Target 14 General Function Amino acid transport and metabolism
Target 14 Specific Function Not Available
Target 14 Pathways Not Available
Target 14 Reactions Not Available
Target 14 Pfam Domain Function
Target 14 Signals
  • None
Target 14 Transmembrane Regions
  • None
Target 14 Essentiality Non-Essential
Target 14 GenBank ID Protein 21619733 Link Image
Target 14 UniProtKB/Swiss-Prot ID Q8N1A5 Link Image
Target 14 UniProtKB/Swiss-Prot Entry Name Q8N1A5_HUMAN Link Image
Target 14 PDB ID Not Available
Target 14 Cellular Location Not Available
Target 14 Gene Sequence >1485 bp 
ATGCTGTACTTCTCTTTGTTTTGGGCGGCTCGGCCTCTGCAGAGATGTGGGCAGCTGGTC
AGGATGGCCATTCGGGCTCAGCACAGCAACGCAGCCCAGACTCAGACTGGGGAAGCAAAC
AGGGGCTGGACAGGCCAGGAGAGCCTGTCGGACAGTGATCCTGAGATGTGGGAGTTGCTG
CAGAGGGAGAAGGACAGGCAGTGTCGTGGCCTGGAGCTCATTGCCTCAGAGAACTTCTGC
AGCCGAGCTGCGCTGGAGGCCCTGGGGTCCTGTCTGAACAACAAGTACTCGGAGGGTTAT
CCTGGCAAGAGATACTATGGGGGAGCAGAGGTGGTGGATGAAATTGAGCTGCTGTGCCAG
CGCCGGGCCTTGGAAGCCTTTGACCTGGATCCTGCACAGTGGGGAGTCAATGTCCAGCCC
TACTCCGGGTCCCCAGCCAACCTGGCCGTCTACACAGCCCTTCTGCAACCTCACGACCGG
ATCATGGGGCTGGACCTGCCCGATGGGGGCCATCTCACCCACGGCTACATGTCTGACGTC
AAGCGGATATCAGCCACGTCCATCTTCTTCGAGTCTATGCCCTATAAGCTCAACCTGGCA
CTGACTGCTCGACTTTTCCGGCCACGGCTCATCATAGCTGGCACCAGCGCCTATGCTCGC
CTCATTGACTACGCCCGCATGAGAGAGGTGTGTGATGAAGTCAAAGCACACCTGCTGGCA
GACATGGCCCACATCAGTGGCCTGGTGGCTGCCAAGGTGATTCCCTCGCCTTTCAAGCAC
GCGGACATCGTCACCACCACTACTCACAAGACTCTTCGAGGGGCCAGGTCAGGGCTCATC
TTCTACCGGAAAGGGGTGAAGGCTGTGGACCCCAAGACTGGCCGGGAGATCCCTTACACA
TTTGAGGACCGAATCAACTTTGCCGTGTTCCCATCCCTGCAGGGGGGCCCCCACAATCAT
GCCATTGCTGCAGTAGCTGTGGCCCTAAAGCAGGCCTGCACCCCCATGTTCCGGGAGTAC
TCCCTGCAGGTTCTGAAGAATGCTCGGGCCATGGCAGATGCCCTGCTAGAGCGAGGCTAC
TCACTGGTATCAGGTGGTACTGACAACCACCTGGTGCTGGTGGACCTGCGGCCCAAGGGC
CTGGATGGAGCTCGGGCTGAGCGGGTGCTAGAGCTTGTATCCATCACTGCCAACAAGAAC
ACCTGTCCTGGAGACCGAAGTGCCATCACACCGGGCGGCCTGCGGCTTGGGGCCCCAGCC
TTAACTTCTCGACAGTTCCGTGAGGATGACTTCCGGAGAGTTGTGGACTTTATAGATGAA
GGGGTCAACATTGGCTTAGAGGTGAAGAGCAAGACTGCCAAGCTCCAGGATTTCAAATCC
TTCCTGCTTAAGGACTCAGAAACAAGTCAGCGTCTGGCCAACCTCAGGCAACGGGTGGAG
CAGTTTGCCAGGGCCTTCCCCATGCCTGGTTTTGATGAGCATTGA
Target 14 GenBank Gene ID
Target 14 GeneCard ID Not Available
Target 14 GenAtlas ID Not Available
Target 14 HGNC ID HGNC:10852 Link Image
Target 14 Chromosome Location Not Available
Target 14 Locus Not Available
Target 14 SNPs Not Available
Target 14 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Target 14 Drug References
  1. Heil SG, Van der Put NM, Waas ET, den Heijer M, Trijbels FJ, Blom HJ: Is mutated serine hydroxymethyltransferase (SHMT) involved in the etiology of neural tube defects? Mol Genet Metab. 2001 Jun;73(2):164-72. [PubMed Link Image]
  2. Contestabile R, Paiardini A, Pascarella S, di Salvo ML, D'Aguanno S, Bossa F: l-Threonine aldolase, serine hydroxymethyltransferase and fungal alanine racemase. A subgroup of strictly related enzymes specialized for different functions. Eur J Biochem. 2001 Dec;268(24):6508-25. [PubMed Link Image]
  3. Vatsyayan R, Roy U: Molecular cloning and biochemical characterization of Leishmania donovani serine hydroxymethyltransferase. Protein Expr Purif. 2007 Apr;52(2):433-40. Epub 2006 Oct 26. [PubMed Link Image]
  4. Rajaram V, Bhavani BS, Kaul P, Prakash V, Appaji Rao N, Savithri HS, Murthy MR: Structure determination and biochemical studies on Bacillus stearothermophilus E53Q serine hydroxymethyltransferase and its complexes provide insights on function and enzyme memory. FEBS J. 2007 Aug;274(16):4148-60. Epub 2007 Jul 25. [PubMed Link Image]
  5. Prabhu V, Chatson KB, Lui H, Abrams GD, King J: Effects of sulfanilamide and methotrexate on 13C fluxes through the glycine decarboxylase/serine hydroxymethyltransferase enzyme system in arabidopsis. Plant Physiol. 1998 Jan;116(1):137-44. [PubMed Link Image]
Drug Target 15 [top]
Target 15 ID 3907
Target 15 Name Serine hydroxymethyltransferase 1
Target 15 Synonyms
  1. Soluble
Target 15 Gene Name SHMT1
Target 15 Protein Sequence >Serine hydroxymethyltransferase 1 
MTMPVNGAHKDADLWSSHDKMLAQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRA
VLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKLDPQCWGVNVQPYSG
SPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGY
INYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGV
VPSPFEHCHVVTTTTHKTLRGCRAGMIFYRKGVKSVDPKTGKEILYNLESLINSAVFPGL
QGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGSDNHLIL
VDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQK
VAHFIHRGIELTLQIQSDTGVRATLKEFKERLAGDKYQAAVQALREEVESFASFFPLPGL
PDF
Target 15 Number of Residues 491
Target 15 Molecular Weight 53117
Target 15 Theoretical pI 7.77
Target 15 GO Classification
Function
catalytic activity
transferase activity
transferase activity, transferring one-carbon groups
methyltransferase activity
glycine hydroxymethyltransferase activity
Process
L-serine metabolism
physiological process
metabolism
cellular metabolism
amino acid and derivative metabolism
amino acid metabolism
serine family amino acid metabolism
glycine metabolism
Component
Not Available
Target 15 General Function Amino acid transport and metabolism
Target 15 Specific Function Not Available
Target 15 Pathways Not Available
Target 15 Reactions Not Available
Target 15 Pfam Domain Function
Target 15 Signals
  • None
Target 15 Transmembrane Regions
  • None
Target 15 Essentiality Non-Essential
Target 15 GenBank ID Protein 14124914 Link Image
Target 15 UniProtKB/Swiss-Prot ID Q96HY0 Link Image
Target 15 UniProtKB/Swiss-Prot Entry Name Q96HY0_HUMAN Link Image
Target 15 PDB ID 1BJ4 Link Image
Target 15 PDB File Show
Target 15 3D Structure
Target 15 Cellular Location Not Available
Target 15 Gene Sequence >1452 bp 
ATGACGATGCCAGTCAACGGGGCCCACAAGGATGCTGACCTGTGGTCCTCACATGACAAG
ATGCTGGCACAACCCCTCAAAGACAGTGATGTTGAGGTTTACAACATCATTAAGAAGGAG
AGTAACCGGCAGAGGGTTGGATTGGAGCTGATTGCCTCGGAGAATTTCGCCAGCCGAGCA
GTTTTGGAGGCCCTAGGCTCTTGCTTAAATAACAAATACTCTGAGGGGTACCCGGGCCAG
AGATACTATGGCGGGACTGAGTTTATTGATGAACTGGAGACCCTCTGTCAGAAGCGAGCC
CTGCAGGCCTATAAGCTGGACCCACAGTGCTGGGGGGTCAACGTCCAGCCCTACTCAGGC
TCCCCTGCAAACTTTGCTGTGTACACTGCCCTGGTGGAACCCCATGGGCGCATCATGGGC
CTGGACCTTCCGGATGGGGGCCACCTGACCCATGGGTTCATGACAGACAAGAAGAAAATC
TCTGCCACGTCCATCTTCTTTGAATCTATGCCCTACAAGGTGAACCCAGATACTGGCTAC
ATCAACTATGACCAGCTGGAGGAGAACGCACGCCTCTTCCACCCGAAGCTGATCATCGCA
GGAACCAGCTGCTACTCCCGAAACCTGGAATATGCCCGGCTACGGAAGATTGCAGATGAG
AACGGGGCGTATCTCATGGCGGACATGGCTCACATCAGCGGGCTGGTGGCGGCTGGCGTG
GTGCCCTCCCCATTTGAACACTGCCATGTGGTGACCACCACCACTCACAAGACCCTGCGA
GGCTGCCGAGCTGGCATGATCTTCTACAGGAAAGGAGTGAAAAGTGTGGATCCCAAGACT
GGCAAAGAGATTCTGTACAACCTGGAGTCTCTTATCAATTCTGCTGTGTTCCCTGGCCTG
CAGGGAGGTCCCCACAACCACGCCATTGCTGGGGTTGCTGTGGCACTGAAGCAAGCTATG
ACTCTGGAATTTAAAGTTTATCAACACCAGGTGGTGGCCAACTGCAGGGCTCTGTCTGAG
GCCCTGACGGAGCTGGGCTACAAAATAGTCACAGGTGGTTCTGACAACCATTTGATCCTT
GTGGATCTCCGTTCCAAAGGCACAGATGGTGGAAGGGCTGAGAAGGTGCTAGAAGCCTGT
TCTATTGCCTGCAACAAGAACACCTGTCCAGGTGACAGAAGCGCTCTGCGGCCCAGTGGA
CTGCGGCTGGGGACCCCAGCACTGACGTCCCGTGGACTTTTGGAAAAAGACTTCCAAAAA
GTAGCCCACTTTATTCACAGAGGGATAGAGCTGACCCTGCAGATCCAGAGCGACACTGGT
GTCAGAGCCACCCTGAAAGAGTTCAAGGAGAGACTGGCAGGGGATAAGTACCAGGCGGCC
GTGCAGGCTCTCCGGGAGGAGGTTGAGAGCTTCGCCTCTTTCTTCCCTCTGCCTGGCCTG
CCTGACTTCTAA
Target 15 GenBank Gene ID
Target 15 GeneCard ID SHMT1 Link Image
Target 15 GenAtlas ID SHMT1 Link Image
Target 15 HGNC ID HGNC:10850 Link Image
Target 15 Chromosome Location 17
Target 15 Locus 17p11.2
Target 15 SNPs SNPJam Report Link Image
Target 15 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Target 15 Drug References
  1. Scarsdale JN, Radaev S, Kazanina G, Schirch V, Wright HT: Crystal structure at 2.4 A resolution of E. coli serine hydroxymethyltransferase in complex with glycine substrate and 5-formyl tetrahydrofolate. J Mol Biol. 2000 Feb 11;296(1):155-68. [PubMed Link Image]
  2. Rao JV, Prakash V, Rao NA, Savithri HS: The role of Glu74 and Tyr82 in the reaction catalyzed by sheep liver cytosolic serine hydroxymethyltransferase. Eur J Biochem. 2000 Oct;267(19):5967-76. [PubMed Link Image]
  3. Heil SG, Van der Put NM, Waas ET, den Heijer M, Trijbels FJ, Blom HJ: Is mutated serine hydroxymethyltransferase (SHMT) involved in the etiology of neural tube defects? Mol Genet Metab. 2001 Jun;73(2):164-72. [PubMed Link Image]
  4. Franca TC, Pascutti PG, Ramalho TC, Figueroa-Villar JD: A three-dimensional structure of Plasmodium falciparum serine hydroxymethyltransferase in complex with glycine and 5-formyl-tetrahydrofolate. Homology modeling and molecular dynamics. Biophys Chem. 2005 May 1;115(1):1-10. Epub 2004 Dec 15. [PubMed Link Image]
  5. Prabhu V, Chatson KB, Lui H, Abrams GD, King J: Effects of sulfanilamide and methotrexate on 13C fluxes through the glycine decarboxylase/serine hydroxymethyltransferase enzyme system in arabidopsis. Plant Physiol. 1998 Jan;116(1):137-44. [PubMed Link Image]
Drug Target 16 [top]
Target 16 ID 3917
Target 16 Name Methylenetetrahydrofolate reductase
Target 16 Synonyms
  1. EC 1.5.1.20
Target 16 Gene Name MTHFR
Target 16 Protein Sequence >Methylenetetrahydrofolate reductase 
MVNEARGNSSLNPCLEGSASSGSESSKDSSRCSTPGLDPERHERLREKMRRRLESGDKWF
SLEFFPPRTAEGAVNLISRFDRMAAGGPLYIDVTWHPAGDPGSDKETSSMMIASTAVNYC
GLETILHMTCCRQRLEEITGHLHKAKQLGLKNIMALRGDPIGDQWEEEEGGFNYAVDLVK
HIRSEFGDYFDICVAGYPKGHPEAGSFEADLKHLKEKVSAGADFIITQLFFEADTFFRFV
KACTDMGITCPIVPGIFPIQGYHSLRQLVKLSKLEVPQEIKDVIEPIKDNDAAIRNYGIE
LAVSLCQELLASGLVPGLHFYTLNREMATTEVLKRLGMWTEDPRRPLPWALSAHPKRREE
DVRPIFWASRPKSYIYRTQEWDEFPNGRWGNSSSPAFGELKDYYLFYLKSKSPKEELLKM
WGEELTSEESVFEVFVLYLSGEPNRNGHKVTCLPWNDEPLAAETSLLKEELLRVNRQGIL
TINSQPNINGKPSSDPIVGWGPSGGYVFQKAYLEFFTSRETAEALLQVLKKYELRVNYHL
VNVKGENITNAPELQPNAVTWGIFPGREIIQPTVVDPVSFMFWKDEAFALWIERWGKLYE
EESPSRTIIQYIHDNYFLVNLVDNDFPLDNCLWQVVEDTLELLNRPTQNARETEAP
Target 16 Number of Residues 666
Target 16 Molecular Weight 74597
Target 16 Theoretical pI 5.00
Target 16 GO Classification
Function
methylenetetrahydrofolate reductase (NADPH) activity
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on the CH-NH group of donors
oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
methylenetetrahydrofolate reductase (NADPH) activity
Process
physiological process
metabolism
cellular metabolism
amino acid and derivative metabolism
amino acid metabolism
sulfur amino acid metabolism
methionine metabolism
Component
Not Available
Target 16 General Function Amino acid transport and metabolism
Target 16 Specific Function Catalyzes the conversion of 5,10- methylenetetrahydrofolate to 5-methyltetrahydrofolate, a co- substrate for homocysteine remethylation to methionine
Target 16 Pathways
Name SMPDB Link KEGG Link
Methane metabolism map00670 Link Image
Target 16 Reactions
  • 5-methyltetrahydrofolate + NAD(P)+ = 5,10-methylenetetrahydrofolate + NAD(P)H + H+
Target 16 Pfam Domain Function
Target 16 Signals
  • None
Target 16 Transmembrane Regions
  • None
Target 16 Essentiality Non-Essential
Target 16 GenBank ID Protein 6139053 Link Image
Target 16 UniProtKB/Swiss-Prot ID P42898 Link Image
Target 16 UniProtKB/Swiss-Prot Entry Name MTHR_HUMAN Link Image
Target 16 PDB ID Not Available
Target 16 Cellular Location Not Available
Target 16 Gene Sequence >1971 bp 
ATGGTGAACGAAGCCAGAGGAAACAGCAGCCTCAACCCCTGCTTGGAGGGCAGTGCCAGC
AGTGGCAGTGAGAGCTCCAAAGATAGTTCGAGATGTTCCACCCCGGGCCTGGACCCTGAG
CGGCATGAGAGACTCCGGGAGAAGATGAGGCGGCGATTGGAATCTGGTGACAAGTGGTTC
TCCCTGGAATTCTTCCCTCCTCGAACTGCTGAGGGAGCTGTCAATCTCATCTCAAGGTTT
GACCGGATGGCAGCAGGTGGCCCCCTCTACATAGACGTGACCTGGCACCCAGCAGGTGAC
CCTGGCTCAGACAAGGAGACCTCCTCCATGATGATCGCCAGCACCGCCGTGAACTACTGT
GGCCTGGAGACCATCCTGCACATGACCTGCTGCCGTCAGCGCCTGGAGGAGATCACGGGC
CATCTGCACAAAGCTAAGCAGCTGGGCCTGAAGAACATCATGGCGCTGCGGGGAGACCCA
ATAGGTGACCAGTGGGAAGAGGAGGAGGGAGGCTTCAACTACGCAGTGGACCTGGTGAAG
CACATCCGAAGTGAGTTTGGTGACTACTTTGACATCTGTGTGGCAGGTTACCCCAAAGGC
CACCCCGAAGCAGGGAGCTTTGAGGCTGACCTGAAGCACTTGAAGGAGAAGGTGTCTGCG
GGAGCCGATTTCATCATCACGCAGCTTTTCTTTGAGGCTGACACATTCTTCCGCTTTGTG
AAGGCATGCACCGACATGGGCATCACTTGCCCCATCGTCCCCGGGATCTTTCCCATCCAG
GGCTACCACTCCCTTCGGCAGCTTGTGAAGCTGTCCAAGCTGGAGGTGCCACAGGAGATC
AAGGACGTGATTGAGCCAATCAAAGACAACGATGCTGCCATCCGCAACTATGGCATCGAG
CTGGCCGTGAGCCTGTGCCAGGAGCTTCTGGCCAGTGGCTTGGTGCCAGGCCTCCACTTC
TACACCCTCAACCGCGAGATGGCTACCACAGAGGTGCTGAAGCGCCTGGGGATGTGGACT
GAGGACCCCAGGCGTCCCCTACCCTGGGCTCTCAGTGCCCACCCCAAGCGCCGAGAGGAA
GATGTACGTCCCATCTTCTGGGCCTCCAGACCAAAGAGTTACATCTACCGTACCCAGGAG
TGGGACGAGTTCCCTAACGGCCGCTGGGGCAATTCCTCTTCCCCTGCCTTTGGGGAGCTG
AAGGACTACTACCTCTTCTACCTGAAGAGCAAGTCCCCCAAGGAGGAGCTGCTGAAGATG
TGGGGGGAGGAGCTGACCAGTGAAGCAAGTGTCTTTGAAGTCTTTGTTCTTTACCTCTCG
GGAGAACCAAACCGGAATGGTCACAAAGTGACTTGCCTGCCCTGGAACGATGAGCCCCTG
GCGGCTGAGACCAGCCTGCTGAAGGAGGAGCTGCTGCGGGTGAACCGCCAGGGCATCCTC
ACCATCAACTCACAGCCCAACATCAACGGGAAGCCGTCCTCCGACCCCATCGTGGGCTGG
GGCCCCAGCGGGGGCTATGTCTTCCAGAAGGCCTACTTAGAGTTTTTCACTTCCCGCGAG
ACAGCGGAAGCACTTCTGCAAGTGCTGAAGAAGTACGAGCTCCGGGTTAATTACCACCTT
GTCAATGTGAAGGGTGAAAACATCACCAATGCCCCTGAACTGCAGCCGAATGCTGTCACT
TGGGGCATCTTCCCTGGGCGAGAGATCATCCAGCCCACCGTAGTGGATCCCGTCAGCTTC
ATGTTCTGGAAGGACGAGGCCTTTGCCCTGTGGATTGAGCGGTGGGGAAAGCTGTATGAG
GAGGAGTCCCCGTCCCGCACCATCATCCAGTACATCCACGACAACTACTTCCTGGTCAAC
CTGGTGGACAATGACTTCCCACTGGACAACTGCCTCTGGCAGGTGGTGGAAGACACATTG
GAGCTTCTCAACAGGCCCACCCAGAATGCGAGAGAAACGGAGGCTCCATGA
Target 16 GenBank Gene ID
Target 16 GeneCard ID MTHFR Link Image
Target 16 GenAtlas ID MTHFR Link Image
Target 16 HGNC ID HGNC:7436 Link Image
Target 16 Chromosome Location 1
Target 16 Locus 1p36.3
Target 16 SNPs SNPJam Report Link Image
Target 16 General References
  1. Frosst P, Blom HJ, Milos R, Goyette P, Sheppard CA, Matthews RG, Boers GJ, den Heijer M, Kluijtmans LA, van den Heuvel LP, et al.: A candidate genetic risk factor for vascular disease: a common mutation in methylenetetrahydrofolate reductase. Nat Genet. 1995 May;10(1):111-3. [PubMed Link Image]
  2. Goyette P, Frosst P, Rosenblatt DS, Rozen R: Seven novel mutations in the methylenetetrahydrofolate reductase gene and genotype/phenotype correlations in severe methylenetetrahydrofolate reductase deficiency. Am J Hum Genet. 1995 May;56(5):1052-9. [PubMed Link Image]
  3. Goyette P, Sumner JS, Milos R, Duncan AM, Rosenblatt DS, Matthews RG, Rozen R: Human methylenetetrahydrofolate reductase: isolation of cDNA, mapping and mutation identification. Nat Genet. 1994 Jun;7(2):195-200. [PubMed Link Image]
  4. Goyette P, Sumner JS, Milos R, Duncan AM, Rosenblatt DS, Matthews RG, Rozen R: Human methylenetetrahydrofolate reductase: isolation of cDNA mapping and mutation identification. Nat Genet. 1994 Aug;7(4):551. [PubMed Link Image]
  5. Goyette P, Christensen B, Rosenblatt DS, Rozen R: Severe and mild mutations in cis for the methylenetetrahydrofolate reductase (MTHFR) gene, and description of five novel mutations in MTHFR. Am J Hum Genet. 1996 Dec;59(6):1268-75. [PubMed Link Image]
  6. Goyette P, Pai A, Milos R, Frosst P, Tran P, Chen Z, Chan M, Rozen R: Gene structure of human and mouse methylenetetrahydrofolate reductase (MTHFR) Mamm Genome. 1998 Aug;9(8):652-6. [PubMed Link Image]
Target 16 Drug References
  1. Ubbink JB, Christianson A, Bester MJ, Van Allen MI, Venter PA, Delport R, Blom HJ, van der Merwe A, Potgieter H, Vermaak WJ: Folate status, homocysteine metabolism, and methylene tetrahydrofolate reductase genotype in rural South African blacks with a history of pregnancy complicated by neural tube defects. Metabolism. 1999 Feb;48(2):269-74. [PubMed Link Image]
  2. Heijmans BT, Gussekloo J, Kluft C, Droog S, Lagaay AM, Knook DL, Westendorp RG, Slagboom EP: Mortality risk in men is associated with a common mutation in the methylene-tetrahydrofolate reductase gene (MTHFR). Eur J Hum Genet. 1999 Feb-Mar;7(2):197-204. [PubMed Link Image]
  3. Tsai MY, Welge BG, Hanson NQ, Bignell MK, Vessey J, Schwichtenberg K, Yang F, Bullemer FE, Rasmussen R, Graham KJ: Genetic causes of mild hyperhomocysteinemia in patients with premature occlusive coronary artery diseases. Atherosclerosis. 1999 Mar;143(1):163-70. [PubMed Link Image]
  4. Holmes ZR, Regan L, Chilcott I, Cohen H: The C677T MTHFR gene mutation is not predictive of risk for recurrent fetal loss. Br J Haematol. 1999 Apr;105(1):98-101. [PubMed Link Image]
  5. Larsson J, Hultberg B, Hillarp A: Hyperhomocysteinemia and the MTHFR C677T mutation in central retinal vein occlusion. Acta Ophthalmol Scand. 2000 Jun;78(3):340-3. [PubMed Link Image]
Drug Target 17 [top]
Target 17 ID 3918
Target 17 Name 5,10-methylenetetrahydrofolate reductase
Target 17 Synonyms
  1. NADPH
Target 17 Gene Name MTHFR
Target 17 Protein Sequence >5,10-methylenetetrahydrofolate reductase 
MVNEARGNSSLNPCLEGSASSGSESSKDSSRCSTPGLDPERHERLREKMRRRLESGDKWF
SLEFFPPRTAEGAVNLISRFDRMAAGGPLYIDVTWHPAGDPGSDKETSSMMIASTAVNYC
GLETILHMTCCRQRLEEITGHLH
Target 17 Number of Residues 145
Target 17 Molecular Weight 15818
Target 17 Theoretical pI 6.34
Target 17 GO Classification
Function
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on the CH-NH group of donors
oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
methylenetetrahydrofolate reductase (NADPH) activity
Process
physiological process
metabolism
cellular metabolism
amino acid and derivative metabolism
amino acid metabolism
sulfur amino acid metabolism
methionine metabolism
Component
Not Available
Target 17 General Function Amino acid transport and metabolism
Target 17 Specific Function Not Available
Target 17 Pathways Not Available
Target 17 Reactions Not Available
Target 17 Pfam Domain Function
Target 17 Signals
  • None
Target 17 Transmembrane Regions
  • None
Target 17 Essentiality Non-Essential
Target 17 GenBank ID Protein 55962397 Link Image
Target 17 UniProtKB/Swiss-Prot ID Q5SNW5 Link Image
Target 17 UniProtKB/Swiss-Prot Entry Name Q5SNW5_HUMAN Link Image
Target 17 PDB ID Not Available
Target 17 Cellular Location Not Available
Target 17 Gene Sequence >431 bp 
ATGGTGAACGAAGCCAGAGGAAACAGCAGCCTCAACCCCTGCTTGGAGGGCAGTGCCAGC
AGTGGCAGTGAGAGCTCCAAAGATAGTTCGAGATGTTCCACCCCGGGCCTGGACCCCGAG
CGGCATGAGAGACTCCGGGAGAAGATGAGGCGGCGATTGGAATCTGGTGACAAGTGGTTC
TCCCTGGAATTCTTCCCTCCTCGAACTGCTGAGGGAGCTGTCAATCTCATCTCAAGGTTT
GACCGGATGGCAGCAGGTGGCCCCCTCTACATAGACGTGACCTGGCACCCAGCAGGTGAC
CCTGGCTCAGACAAGGAGACCTCCTCCATGATGATCGCCAGCACCGCCGTGAACTACTGT
GGCCTGGAGACCATCCTGCACATGACCTGCTGCCGTCAGCGCCTGGAGGAGATCACGGGC
CATCTGCACAA
Target 17 GenBank Gene ID
Target 17 GeneCard ID MTHFR Link Image
Target 17 GenAtlas ID MTHFR Link Image
Target 17 HGNC ID HGNC:7436 Link Image
Target 17 Chromosome Location 1
Target 17 Locus 1p36.3
Target 17 SNPs SNPJam Report Link Image
Target 17 General References Not Available
Target 17 Drug References
  1. Ott K, Vogelsang H, Marton N, Becker K, Lordick F, Kobl M, Schuhmacher C, Novotny A, Mueller J, Fink U, Ulm K, Siewert JR, Hofler H, Keller G: The thymidylate synthase tandem repeat promoter polymorphism: A predictor for tumor-related survival in neoadjuvant treated locally advanced gastric cancer. Int J Cancer. 2006 Dec 15;119(12):2885-94. [PubMed Link Image]
  2. Leopardi P, Marcon F, Caiola S, Cafolla A, Siniscalchi E, Zijno A, Crebelli R: Effects of folic acid deficiency and MTHFR C677T polymorphism on spontaneous and radiation-induced micronuclei in human lymphocytes. Mutagenesis. 2006 Sep;21(5):327-33. Epub 2006 Sep 1. [PubMed Link Image]
  3. 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]
  4. 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]
  5. Siva A, De Lange M, Clayton D, Monteith S, Spector T, Brown MJ: The heritability of plasma homocysteine, and the influence of genetic variation in the homocysteine methylation pathway. QJM. 2007 Aug;100(8):495-9. Epub 2007 Jul 17. [PubMed Link Image]
Drug Target 18 [top]
Target 18 ID 3919
Target 18 Name Methionyl-tRNA formyltransferase, mitochondrial
Target 18 Synonyms
  1. EC 2.1.2.9
  2. Methionyl-tRNA formyltransferase, mitochondrial precursor
  3. MtFMT
Target 18 Gene Name MTFMT
Target 18 Protein Sequence >Methionyl-tRNA formyltransferase, mitochondrial 
MRVLVRRCWGPPLAHGARRGRPSPQWRALARLGWEDCRDSRVREKPPWRVLFFGTDQFAR
EALRALHAARENKEEELIDKLEVVTMPSPSPKGLPVKQYAVQSQLPVYEWPDVGSGEYDV
GVVASFGRLLNEALILKFPYGILNVHPSCLPRWRGPAPVIHTVLHGDTVTGVTIMQIRPK
RFDVGPILKQETVPVPPKSTAKELEAVLSRLGANMLISVLKNLPESLSNGRQQPMEGATY
APKISAGTSCIKWEEQTSEQIFRLYRAIGNIIPLQTLWMANTIKLLDLVEVNSSVLADPK
LTGQALIPGSVIYHKQSQILLVYCKDGWIGVRSVMLKKSLTATDFYNGYLHPWYQKNSQA
QPSQCRFQTLRLPTKKKQKKTVAMQQCIE
Target 18 Number of Residues 395
Target 18 Molecular Weight 43833
Target 18 Theoretical pI 10.19
Target 18 GO Classification
Function
catalytic activity
transferase activity
transferase activity, transferring one-carbon groups
methyltransferase activity
glycine hydroxymethyltransferase activity
hydroxymethyl-, formyl- and related transferase activity
methionyl-tRNA formyltransferase activity
Process
biosynthesis
physiological process
metabolism
macromolecule metabolism
macromolecule biosynthesis
protein biosynthesis
Component
Not Available
Target 18 General Function Translation, ribosomal structure and biogenesis
Target 18 Specific Function Formylates methionyl-tRNA in mitochondria. A single tRNA(Met) gene gives rise to both an initiator and an elongator species via an unknown mechanism
Target 18 Pathways
Name SMPDB Link KEGG Link
Aminoacyl-tRNA biosynthesis map00271 Link Image
Target 18 Reactions
  • 10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O = tetrahydrofolate + N-formylmethionyl-tRNAfMet
Target 18 Pfam Domain Function
Target 18 Signals
  • None
Target 18 Transmembrane Regions
  • None
Target 18 Essentiality Non-Essential
Target 18 GenBank ID Protein 133777035 Link Image
Target 18 UniProtKB/Swiss-Prot ID Q96DP5 Link Image
Target 18 UniProtKB/Swiss-Prot Entry Name FMT_HUMAN Link Image
Target 18 PDB ID Not Available
Target 18 Cellular Location
  • Mitochondrion
Target 18 Gene Sequence >1170 bp 
ATGAGGGTGTTGGTGCGGCGCTGTTGGGGTCCTCCGCTGGCTCATGGCGCCAGGCGTGGG
AGGCCGAGTCCCCAGTGGCGAGCACTGGCCCGACTCGGCTGGGAGGACTGCCGGGACTCC
AGAGTCCGCGAGAAGCCTCCCTGGCGGGTGCTCTTCTTCGGCACGGACCAGTTCGCCCGC
GAGGCGCTGCGGGCGCTGCACGCCGCCAGGGAAAACAAAGAAGAAGAGTTAATCGACAAA
CTGGAGGTGGTCACAATGCCTTCCCCATCACCAAAAGGACTGCCAGTGAAGCAATATGCT
GTGCAGTCTCAGCTTCCCGTATATGAGTGGCCGGATGTGGGATCTGGAGAATATGATGTT
GGAGTAGTGGCTTCGTTTGGCCGACTTTTGAATGAGGCTCTTATTCTTAAATTTCCCTAT
GGCATATTGAATGTTCATCCCAGTTGCCTCCCGAGATGGCGTGGCCCAGCCCCTGTAATC
CATACAGTGCTTCACGGAGACACAGTTACTGGAGTAACAATTATGCAAATTAGACCTAAA
AGGTTTGATGTAGGCCCAATTCTCAAACAAGAAACTGTTCCTGTGCCACCCAAGAGCACT
GCAAAGGAATTGGAAGCAGTGTTGTCAAGACTGGGTGCCAACATGCTCATTTCAGTTTTG
AAAAATTTGCCTGAAAGTCTGAGCAATGGAAGGCAGCAGCCAATGGAGGGGGCGACTTAC
GCCCCTAAGATTTCTGCTGGTACCAGTTGTATAAAATGGGAGGAACAAACTTCAGAACAA
ATATTCAGACTTTACCGTGCCATTGGAAATATAATTCCGTTGCAGACGCTCTGGATGGCG
AATACCATTAAACTTCTGGATTTGGTAGAAGTTAACAGTTCAGTCCTTGCTGATCCAAAA
TTAACGGGACAGGCTCTTATTCCAGGATCAGTAATATACCACAAACAGTCACAAATACTA
TTGGTTTATTGCAAGGATGGTTGGATTGGTGTTCGATCAGTGATGCTCAAGAAATCACTA
ACAGCTACTGACTTCTACAATGGATATTTGCACCCCTGGTACCAGAAAAATTCCCAAGCT
CAACCAAGCCAATGCAGATTTCAGACTCTCAGACTTCCAACAAAGAAGAAGCAGAAAAAA
ACTGTTGCTATGCAACAATGCATTGAGTAG
Target 18 GenBank Gene ID
Target 18 GeneCard ID MTFMT Link Image
Target 18 GenAtlas ID MTFMT Link Image
Target 18 HGNC ID HGNC:29666 Link Image
Target 18 Chromosome Location 15
Target 18 Locus 15q22.31
Target 18 SNPs SNPJam Report Link Image
Target 18 General References Not Available
Target 18 Drug References
  1. Li Y, Holmes WB, Appling DR, RajBhandary UL: Initiation of protein synthesis in Saccharomyces cerevisiae mitochondria without formylation of the initiator tRNA. J Bacteriol. 2000 May;182(10):2886-92. [PubMed Link Image]
Drug Target 19 [top]
Target 19 ID 3920
Target 19 Name Methylenetetrahydrofolate reductase intermediate form
Target 19 Synonyms Not Available
Target 19 Gene Name MTHFR
Target 19 Protein Sequence >Methylenetetrahydrofolate reductase intermediate form 
MCRGCGCLPPDAPCPTLCSRNPAMVNEARGNSSLNPCLEGSASSGSESSKDSSRCSTPGL
DPERHERLREKMRRRLESGDKWFSLEFFPPRTAEGAVNLIS
Target 19 Number of Residues 102
Target 19 Molecular Weight 10987
Target 19 Theoretical pI 7.70
Target 19 GO Classification
Function
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on the CH-NH group of donors
oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
methylenetetrahydrofolate reductase (NADPH) activity
Process
physiological process
metabolism
cellular metabolism
amino acid and derivative metabolism
amino acid metabolism
sulfur amino acid metabolism
methionine metabolism
Component
Not Available
Target 19 General Function Not Available
Target 19 Specific Function Not Available
Target 19 Pathways Not Available
Target 19 Reactions Not Available
Target 19 Pfam Domain Function
Target 19 Signals
  • None
Target 19 Transmembrane Regions
  • None
Target 19 Essentiality Non-Essential
Target 19 GenBank ID Protein 7271189 Link Image
Target 19 UniProtKB/Swiss-Prot ID Q9NY62 Link Image
Target 19 UniProtKB/Swiss-Prot Entry Name Q9NY62_HUMAN Link Image
Target 19 PDB ID Not Available
Target 19 Cellular Location Not Available
Target 19 Gene Sequence >305 bp 
ATGTGTCGGGGGTGTGGCTGCCTGCCCCCTGATGCTCCCTGCCCCACCCTGTGCAGTAGG
AACCCAGCCATGGTGAACGAAGCCAGAGGAAACAGCAGCCTCAACCCCTGCTTGGAGGGC
AGTGCCAGCAGTGGCAGTGAGAGCTCCAAAGATAGTTCGAGATGTTCCACCCCGGGCCTG
GACCCTGAGCGGCATGAGAGACTCCGGGAGAAGATGAGGCGGCGATTGGAATCTGGTGAC
AAGTGGTTCTCCCTGGAATTCTTCCCTCCTCGAACTGCTGAGGGAGCTGTCAATCTCATC
TCAAG
Target 19 GenBank Gene ID
Target 19 GeneCard ID MTHFR Link Image
Target 19 GenAtlas ID MTHFR Link Image
Target 19 HGNC ID HGNC:7436 Link Image
Target 19 Chromosome Location 1
Target 19 Locus 1p36.3
Target 19 SNPs SNPJam Report Link Image
Target 19 General References
  1. Tran P, Leclerc D, Chan M, Pai A, Hiou-Tim F, Wu Q, Goyette P, Artigas C, Milos R, Rozen R: Multiple transcription start sites and alternative splicing in the methylenetetrahydrofolate reductase gene result in two enzyme isoforms. Mamm Genome. 2002 Sep;13(9):483-92. [PubMed Link Image]
Target 19 Drug References
  1. Heijmans BT, Gussekloo J, Kluft C, Droog S, Lagaay AM, Knook DL, Westendorp RG, Slagboom EP: Mortality risk in men is associated with a common mutation in the methylene-tetrahydrofolate reductase gene (MTHFR). Eur J Hum Genet. 1999 Feb-Mar;7(2):197-204. [PubMed Link Image]
  2. Larsson J, Hultberg B, Hillarp A: Hyperhomocysteinemia and the MTHFR C677T mutation in central retinal vein occlusion. Acta Ophthalmol Scand. 2000 Jun;78(3):340-3. [PubMed Link Image]
  3. Dilley A, Hooper WC, El-Jamil M, Renshaw M, Wenger NK, Evatt BL: Mutations in the genes regulating methylene tetrahydrofolate reductase (MTHFR C-->T677) and cystathione beta-synthase (CBS G-->A919, CBS T-->c833) are not associated with myocardial infarction in African Americans. Thromb Res. 2001 Jul 15;103(2):109-15. [PubMed Link Image]
  4. Huang L, Zhang J, Hayakawa T, Tsuge H: Assays of methylenetetrahydrofolate reductase and methionine synthase activities by monitoring 5-methyltetrahydrofolate and tetrahydrofolate using high-performance liquid chromatography with fluorescence detection. Anal Biochem. 2001 Dec 15;299(2):253-9. [PubMed Link Image]
  5. Tsai AW, Cushman M, Tsai MY, Heckbert SR, Rosamond WD, Aleksic N, Yanez ND, Psaty BM, Folsom AR: Serum homocysteine, thermolabile variant of methylene tetrahydrofolate reductase (MTHFR), and venous thromboembolism: Longitudinal Investigation of Thromboembolism Etiology (LITE). Am J Hematol. 2003 Mar;72(3):192-200. [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.