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Human Metabolome Database Version 2.5

 

Showing metabocard for S-Adenosylhomocysteine (HMDB00939)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:23
Accession Number HMDB00939
Secondary Accession Numbers Not Available
Common Name S-Adenosylhomocysteine
Description S-Adenosylhomocysteine (AdoHcy) is the immediate precursor of all of the homocysteine produced in the body. The reaction is catalyzed by S-adenosylhomocysteine hydrolase and is reversible with the equilibrium favoring formation of AdoHcy. In vivo, the reaction is driven in the direction of homocysteine formation by the action of the enzyme adenosine deaminase, which converts the second product of the S-adenosylhomocysteine hydrolase reaction, adenosine, to inosine. Except for methyl transfer from betaine and from methylcobalamin in the methionine synthase reaction, AdoHcy is the product of all methylation reactions that involve S-adenosylmethionine (AdoMet) as the methyl donor. Methylation is significant in epigenetic regulation of protein expression via DNA and histone methylation. The inhibition of these AdoMet-mediated processes by AdoHcy is a proven mechanism for metabolic alteration. Because the conversion of AdoHcy to homocysteine is reversible, with the equilibrium favoring the formation of AdoHcy, increases in plasma homocysteine are accompanied by an elevation of AdoHcy in most cases. Disturbances in the transmethylation pathway indicated by abnormal S-adenosylmethionine, S-adenosylhomocysteine or their ratio have been reported in many neurodegenerative diseases, such as dementia, depression or Parkinson's disease. (PMID: 18065573, 17892439)
Synonyms
  1. (S)-5'-(S)-(3-Amino-3-carboxypropyl)-5'-thioadenosine
  2. 2-S-adenosyl-L-homocysteine
  3. 5'-Deoxy-S-adenosyl-L-homocysteine
  4. 5'-S-(3-amino-3-carboxypropyl)-5'-thio-L-Adenosine
  5. Adenosyl-homo-CYS
  6. Adenosyl-L-homocysteine
  7. Adenosylhomo-CYS
  8. Adenosylhomocysteine
  9. Adohcy
  10. Formycinylhomocysteine
  11. L-5'-S-(3-amino-3-carboxypropyl)-5'-thior-Adenosine
  12. L-S-adenosyl-Homocysteine
  13. L-S-Adenosylhomocysteine
  14. S-(5'-adenosyl)-L-homocysteine
  15. S-(5'-deoxyadenosin-5'-yl)-L-homocysteine
  16. S-(5'-Deoxyadenosine-5')-L-homocysteine
  17. S-adenosyl-homocysteine
  18. S-Adenosyl-L-homocysteine
  19. SAH
Chemical IUPAC Name (2S)-2-amino-4-[[(2S,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxy-oxolan-2-yl]methylsulfanyl]butanoic acid
Chemical Formula C14H20N6O5S
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Nucleoside Analogues
Sub Class
  • Deoxy nucleosides
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • 1,2-diol
  • thioether
  • primary amine
  • primary aliphatic amine (alkylamine)
  • primary aromatic amine
  • carboxylic acid
  • aromatic compound
  • heterocyclic compound
  • alpha-aminoacid
Biofunction
  • Component of Arginine and proline metabolism
  • Component of Glycerophospholipid metabolism
  • Component of Glycine, serine and threonine metabolism
  • Component of Histidine metabolism
  • Component of Methionine metabolism
  • Component of Nicotinate and nicotinamide metabolism
  • Component of Selenoamino acid metabolism
  • Component of Tryptophan metabolism
  • Component of Tyrosine metabolism
  • Component of Ubiquinone biosynthesis
Application
Source
  • Endogenous
Average Molecular Weight 384.411
Monoisotopic Molecular Weight 384.121582
Isomeric SMILES N[C@@H](CCSC[C@H]1O[C@H]([C@H](O)[C@@H]1O)N1C=NC2=C(N)N=CN=C12)C(O)=O
Canonical SMILES NC(CCSCC1OC(C(O)C1O)N1C=NC2=C(N)N=CN=C12)C(O)=O
KEGG Compound ID C00021 Link Image
BioCyc ID ADENOSYL-HOMO-CYS Link Image
BiGG ID 33543 Link Image
Wikipedia Link SAH Link Image
NuGOwiki Link HMDB00939 Link Image
Metagene Link HMDB00939 Link Image
METLIN ID 296 Link Image
PubChem Compound 439155 Link Image
PubChem Substance 10298220 Link Image
ChEBI ID 16680 Link Image
CAS Registry Number 979-92-0
InChI Identifier InChI=1/C14H20N6O5S/c15-6(14(23)24)1-2-26-3-7-9(21)10(22)13(25-7)20-5-19-8-11(16)17-4-18-12(8)20/h4-7,9-10,13,21-22H,1-3,15H2,(H,23,24)(H2,16,17,18)/t6-,7+,9+,10+,13+/m0/s1
Synthesis Reference Holy, Antonin; Rosenberg, Ivan. Studies on S-adenosyl-L-homocysteine hydrolase. Part XV. An improved synthesis of S-adenosyl-L-homocysteine and related compounds. Collection of Czechoslovak Chemical Communications (1985), 50(7), 1514-18.
Melting Point (Experimental) 209-211 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 4.08 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.37 [Predicted by ALOGPS]; -3.3 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID 1AF7 Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • endoplasmic reticulum
  • mitochondria
  • nucleus
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
Tissue Location
Tissue References
Lymphoblast
Myelin
Neuron
Placenta
Concentrations (Normal)
Biofluid Blood
Value 0.46 +/- 0.02 uM
Age Elderly:>65 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Cheng H, Gomes-Trolin C, Aquilonius SM, Steinberg A, Lofberg C, Ekblom J, Oreland L: Levels of L-methionine S-adenosyltransferase activity in erythrocytes and concentrations of S-adenosylmethionine and S-adenosylhomocysteine in whole blood of patients with Parkinson's disease. Exp Neurol. 1997 Jun;145(2 Pt 1):580-5. [PubMed Link Image]
Biofluid CSF
Value 0.01 (0.009-0.014) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Struys EA, Jansen EE, de Meer K, Jakobs C: Determination of S-adenosylmethionine and S-adenosylhomocysteine in plasma and cerebrospinal fluid by stable-isotope dilution tandem mass spectrometry. Clin Chem. 2000 Oct;46(10):1650-6. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 0.49 +/- 0.05 uM
Age Elderly:>65 yrs old
Sex Both
Condition Parkinson's disease
Comments Not Available
References
  • Cheng H, Gomes-Trolin C, Aquilonius SM, Steinberg A, Lofberg C, Ekblom J, Oreland L: Levels of L-methionine S-adenosyltransferase activity in erythrocytes and concentrations of S-adenosylmethionine and S-adenosylhomocysteine in whole blood of patients with Parkinson's disease. Exp Neurol. 1997 Jun;145(2 Pt 1):580-5. [PubMed Link Image]
Biofluid Blood
Value 0.016 (0.009-0.025) uM
Age Adult:>18 yrs old
Sex Both
Condition Neurodegenerative disease
Comments Not Available
References
  • Obeid R, Kostopoulos P, Knapp JP, Kasoha M, Becker G, Fassbender K, Herrmann W: Biomarkers of folate and vitamin B12 are related in blood and cerebrospinal fluid. Clin Chem. 2007 Feb;53(2):326-33. Epub 2007 Jan 2. [PubMed Link Image]
Associated Disorders
Condition References
Neurodegenerative disease
  • Obeid R, Kostopoulos P, Knapp JP, Kasoha M, Becker G, Fassbender K, Herrmann W: Biomarkers of folate and vitamin B12 are related in blood and cerebrospinal fluid. Clin Chem. 2007 Feb;53(2):326-33. Epub 2007 Jan 2. [PubMed Link Image]
Parkinson's disease
  • Cheng H, Gomes-Trolin C, Aquilonius SM, Steinberg A, Lofberg C, Ekblom J, Oreland L: Levels of L-methionine S-adenosyltransferase activity in erythrocytes and concentrations of S-adenosylmethionine and S-adenosylhomocysteine in whole blood of patients with Parkinson's disease. Exp Neurol. 1997 Jun;145(2 Pt 1):580-5. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Betaine Metabolism SMP00123 Link Image map00260 Link Image
Carnitine Synthesis SMP00465 Link Image
Glycine and Serine Metabolism SMP00004 Link Image map00260 Link Image
Methionine Metabolism SMP00033 Link Image map00270 Link Image
General References
  1. Miller AL: The methionine-homocysteine cycle and its effects on cognitive diseases. Altern Med Rev. 2003 Feb;8(1):7-19. [PubMed Link Image]
  2. Hershfield MS, Kredich NM, Koller CA, Mitchell BS, Kurtzberg J, Kinney TR, Falletta JM: S-adenosylhomocysteine catabolism and basis for acquired resistance during treatment of T-cell acute lymphoblastic leukemia with 2'-deoxycoformycin alone and in combination with 9-beta-D-arabinofuranosyladenine. Cancer Res. 1983 Jul;43(7):3451-8. [PubMed Link Image]
  3. Struys EA, Jansen EE, de Meer K, Jakobs C: Determination of S-adenosylmethionine and S-adenosylhomocysteine in plasma and cerebrospinal fluid by stable-isotope dilution tandem mass spectrometry. Clin Chem. 2000 Oct;46(10):1650-6. [PubMed Link Image]
  4. Wang J, Dudman NP, Wilcken DE: Effects of homocysteine and related compounds on prostacyclin production by cultured human vascular endothelial cells. Thromb Haemost. 1993 Dec 20;70(6):1047-52. [PubMed Link Image]
  5. Palella TD, Schatz RA, Wilens TE, Fox IH: S-Adenosylhomocysteine accumulation and selective cytotoxicity in cultured J Lab Clin Med. 1982 Aug;100(2):269-78. [PubMed Link Image]
  6. van Guldener C, Stehouwer CD: Homocysteine and methionine metabolism in renal failure. Semin Vasc Med. 2005 May;5(2):201-8. [PubMed Link Image]
  7. Muskiet FA: The importance of (early) folate status to primary and secondary coronary artery disease prevention. Reprod Toxicol. 2005 Sep-Oct;20(3):403-10. [PubMed Link Image]
  8. Augoustides-Savvopoulou P, Luka Z, Karyda S, Stabler SP, Allen RH, Patsiaoura K, Wagner C, Mudd SH: Glycine N -methyltransferase deficiency: a new patient with a novel mutation. J Inherit Metab Dis. 2003;26(8):745-59. [PubMed Link Image]
  9. Fowler B: Homocysteine: overview of biochemistry, molecular biology, and role in disease processes. Semin Vasc Med. 2005 May;5(2):77-86. [PubMed Link Image]
  10. Gordon RK, Ginalski K, Rudnicki WR, Rychlewski L, Pankaskie MC, Bujnicki JM, Chiang PK: Anti-HIV-1 activity of 3-deaza-adenosine analogs. Inhibition of S-adenosylhomocysteine hydrolase and nucleotide congeners. Eur J Biochem. 2003 Sep;270(17):3507-17. [PubMed Link Image]
  11. Metz J: Cobalamin deficiency and the pathogenesis of nervous system disease. Annu Rev Nutr. 1992;12:59-79. [PubMed Link Image]
  12. Mulder C, Schoonenboom NS, Jansen EE, Verhoeven NM, van Kamp GJ, Jakobs C, Scheltens P: The transmethylation cycle in the brain of Alzheimer patients. Neurosci Lett. 2005 Sep 30;386(2):69-71. [PubMed Link Image]
  13. Delabar U, Kloor D, Luippold G, Muhlbauer B: Simultaneous determination of adenosine, S-adenosylhomocysteine and S-adenosylmethionine in biological samples using solid-phase extraction and high-performance liquid chromatography. J Chromatogr B Biomed Sci Appl. 1999 Mar 19;724(2):231-8. [PubMed Link Image]
  14. Hermes M, von Hippel S, Osswald H, Kloor D: S-adenosylhomocysteine metabolism in different cell lines: effect of hypoxia and cell density. Cell Physiol Biochem. 2005;15(5):233-44. [PubMed Link Image]
  15. Weir DG, Molloy AM, Keating JN, Young PB, Kennedy S, Kennedy DG, Scott JM: Correlation of the ratio of S-adenosyl-L-methionine to S-adenosyl-L-homocysteine in the brain and cerebrospinal fluid of the pig: implications for the determination of this methylation ratio in human brain. Clin Sci (Lond). 1992 Jan;82(1):93-7. [PubMed Link Image]
  16. Wikipedia Link Image
Metabolic Enzymes
  1. Phosphatidylethanolamine N-methyltransferase
  2. Hydroxyindole O-methyltransferase
  3. Catechol O-methyltransferase
  4. Histone-lysine N-methyltransferase, H3 lysine-79 specific
  5. Glycine N-methyltransferase
  6. Histone-lysine N-methyltransferase, H3 lysine-4 specific SET7
  7. Phenylethanolamine N-methyltransferase
  8. Arsenite methyltransferase
  9. tRNA
  10. Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific
  11. Histone-lysine N-methyltransferase SETDB1
  12. Protein-S-isoprenylcysteine O-methyltransferase
  13. Indolethylamine N-methyltransferase
  14. DNA
  15. Hexaprenyldihydroxybenzoate methyltransferase, mitochondrial precursor
  16. Methionine synthase reductase, mitochondrial precursor
  17. Nicotinamide N-methyltransferase
  18. Histone-lysine N-methyltransferase SUV39H2
  19. Guanidinoacetate N-methyltransferase
  20. Thiopurine S-methyltransferase
  21. N6-adenosine-methyltransferase 70 kDa subunit
  22. Putative adenosylhomocysteinase 3
  23. Adenosylhomocysteinase
  24. Putative adenosylhomocysteinase 2
  25. Histone-lysine N-methyltransferase, H3 lysine-4 specific SET1
  26. DNA
  27. DNA
  28. tRNA
  29. Histone-lysine N-methyltransferase SETDB2
  30. Histamine N-methyltransferase
  31. cDNA FLJ76252, highly similar to Homo sapiens S-adenosylhomocysteine hydrolase
  32. Probable histone-lysine N-methyltransferase ASH1L
  33. Histone-lysine N-methyltransferase NSD3
  34. SET domain-containing protein 1B
  35. Histone-lysine N-methyltransferase SETD2
  36. Histone-lysine N-methyltransferase SETMAR
  37. Histone-lysine N-methyltransferase SUV420H1
  38. Histone-lysine N-methyltransferase SUV420H2
  39. N(2),N(2)-dimethylguanosine tRNA methyltransferase
  40. tRNA
  41. tRNA
  42. 5-methyltetrahydrofolate-homocysteine methyltransferase reductase
  43. DNA (cytosine-5)-methyltransferase 3-like
  44. Euchromatic histone-lysine N-methyltransferase 2 (Euchromatic histone- lysine N-methyltransferase 2, isoform CRA_c) (HLA-B associated transcript 8)
  45. Enhancer of zeste homolog 1
  46. Enhancer of zeste homolog 2 (Drosophila) (Enhancer of zeste homolog 2 (Drosophila), isoform CRA_a)
  47. cDNA FLJ75818, highly similar to Homo sapiens PR/SET domain containing protein 8 (SET8), mRNA
  48. Wolf-Hirschhorn syndrome candidate 1 (Wolf-Hirschhorn syndrome candidate 1, isoform CRA_e)
  49. EHMT1 protein
  50. cDNA FLJ78356, highly similar to Homo sapiens PIMT isozyme I
  51. Uncharacterized protein PRMT5 (Protein arginine methyltransferase 5, isoform CRA_d)
  52. Uncharacterized protein CARM1 (Coactivator-associated arginine methyltransferase 1, isoform CRA_b)
  53. cDNA, FLJ92918, Homo sapiens suppressor of variegation 3-9 homolog 1 (Drosophila)(SUV39H1), mRNA (Suppressor of variegation 3-9 homolog 1 (Drosophila), isoform CRA_a)
  54. RNA (Guanine-7-) methyltransferase
  55. cDNA FLJ43496 fis, clone PEBLM2001465, highly similar to Probable diphthine synthase (EC 2.1.1.98)
Enzyme 1 [top]
Enzyme 1 ID 5310
Enzyme 1 Name Phosphatidylethanolamine N-methyltransferase
Enzyme 1 Synonyms
  1. PEAMT
  2. PEMT
  3. PEMT2
Enzyme 1 Gene Name PEMT
Enzyme 1 Protein Sequence >Phosphatidylethanolamine N-methyltransferase
MTRLLGYVDPLDPSFVAAVITITFNPLYWNVVARWEHKTRKLSRAFGSPYLACYSLSVTI
LLLNFLRSHCFTQAMLSQPRMESLDTPAAYSLGLALLGLGVVLVLSSFFALGFAGTFLGD
YFGILKEARVTVFPFNILDNPMYWGSTANYLGWAIMHASPTGLLLTVLVALTYIMALLYE
EPFTAEIYRQKASGSHKRS
Enzyme 1 Number of Residues 199
Enzyme 1 Molecular Weight 22166
Enzyme 1 Theoretical pI 8.96
Enzyme 1 GO Classification
Function
  • N-methyltransferase activity
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • cellular lipid metabolism
  • lipid metabolism
  • membrane lipid metabolism
  • metabolism
  • phospholipid metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Catalyzes three sequential methylation of phosphatidylethanolamine (PE) by AdoMet, thus producing phosphatidylcholine (PC)
Enzyme 1 Pathways
Enzyme 1 Reactions
  • S-adenosyl-L-methionine + phosphatidylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • 13-33 46-66 94-114 158-178
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 5825555 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q9UBM1 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name PEMT_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >600 bp
ATGACCCGGCTGCTGGGCTACGTGGACCCCCTGGATCCCAGCTTTGTGGCTGCCGTCATC
ACCATCACCTTCAATCCGCTCTACTGGAATGTGGTTGCACGATGGGAACACAAGACCCGC
AAGCTGAGCAGGGCCTTCGGATCCCCCTACCTGGCCTGCTACTCTCTAAGCGTCACCATC
CTGCTCCTGAACTTCCTGCGCTCGCACTGCTTCACGCAGGCCATGCTGAGCCAGCCCAGG
ATGGAGAGCCTGGACACCCCCGCGGCCTACAGCCTGGGCCTCGCGCTCCTGGGACTGGGC
GTCGTGCTCGTGCTCTCCAGCTTCTTTGCACTGGGGTTCGCTGGAACTTTCCTAGGTGAT
TACTTCGGGATCCTCAAGGAGGCGAGAGTGACCGTGTTCCCCTTCAACATCCTGGACAAC
CCCATGTACTGGGGAAGCACAGCCAACTACTTGGGCTGGGCCATCATGCACGCCAGCCCC
ACGGGCCTGCTCCTGACGGTGCTGGTGGCCCTCACCTACATAATGGCTCTCCTATACGAA
GAGCCCTTCACCGCTGAGATCTACCGGCAGAAAGCCTCCGGGTCCCACAAGAGGAGCTGA
Enzyme 1 GenBank Gene ID AF176807 Link Image
Enzyme 1 GeneCard ID PEMT Link Image
Enzyme 1 GenAtlas ID PEMT Link Image
Enzyme 1 HGNC ID HGNC:8830 Link Image
Enzyme 1 Chromosome Location 17
Enzyme 1 Locus 17p11.2
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Walkey CJ, Shields DJ, Vance DE: Identification of three novel cDNAs for human phosphatidylethanolamine N-methyltransferase and localization of the human gene on chromosome 17p11.2. Biochim Biophys Acta. 1999 Jan 4;1436(3):405-12. [PubMed Link Image]
  2. Shields DJ, Agellon LB, Vance DE: Structure, expression profile and alternative processing of the human phosphatidylethanolamine N-methyltransferase (PEMT) gene. Biochim Biophys Acta. 2001 May 31;1532(1-2):105-14. [PubMed Link Image]
  3. Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9543-8. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5333
Enzyme 2 Name Hydroxyindole O-methyltransferase
Enzyme 2 Synonyms
  1. HIOMT
  2. Acetylserotonin O-methyltransferase
  3. ASMT
Enzyme 2 Gene Name ASMT
Enzyme 2 Protein Sequence >Hydroxyindole O-methyltransferase
MGSSEDQAYRLLNDYANGFMVSQVLFAACELGVFDLLAEAPGPLDVAAVAAGVRASAHGT
ELLLDICVSLKLLKVETRGGKAFYRNTELSSDYLTTVSPTSQCSMLKYMGRTSYRCWGHL
ADAVREGRNQYLETFGVPAEELFTAIYRSEGERLQFMQALQEVWSVNGRSVLTAFDLSVF
PLMCDLGGGAGALAKECMSLYPGCKITVFDIPEVVWTAKQHFSFQEEEQIDFQEGDFFKD
PLPEADLYILARVLHDWADGKCSHLLERIYHTCKPGGGILVIESLLDEDRRGPLLTQLYS
LNMLVQTEGQERTPTHYHMLLSSAGFRDFQFKKTGAIYDAILARK
Enzyme 2 Number of Residues 345
Enzyme 2 Molecular Weight 38453
Enzyme 2 Theoretical pI 4.82
Enzyme 2 GO Classification
Function
  • O-methyltransferase activity
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
Component
Enzyme 2 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 2 Specific Function S-adenosyl-L-methionine + N-acetylserotonin = S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
Enzyme 2 Pathways
Enzyme 2 Reactions
  • S-adenosyl-L-methionine + N-acetylserotonin = S-adenosyl-L-homocysteine + melatonin
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein Not Available
Enzyme 2 UniProtKB/Swiss-Prot ID P46597 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name HIOM_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence Not Available
Enzyme 2 GenBank Gene ID U11098 Link Image
Enzyme 2 GeneCard ID ASMT Link Image
Enzyme 2 GenAtlas ID ASMT Link Image
Enzyme 2 HGNC ID HGNC:750 Link Image
Enzyme 2 Chromosome Location X
Enzyme 2 Locus Xp22.3 or Yp11.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Rodriguez IR, Mazuruk K, Schoen TJ, Chader GJ: Structural analysis of the human hydroxyindole-O-methyltransferase gene. Presence of two distinct promoters. J Biol Chem. 1994 Dec 16;269(50):31969-77. [PubMed Link Image]
  2. Donohue SJ, Roseboom PH, Illnerova H, Weller JL, Klein DC: Human hydroxyindole-O-methyltransferase: presence of LINE-1 fragment in a cDNA clone and pineal mRNA. DNA Cell Biol. 1993 Oct;12(8):715-27. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5504
Enzyme 3 Name Catechol O-methyltransferase
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name COMT
Enzyme 3 Protein Sequence >Catechol O-methyltransferase
MPEAPPLLLAAVLLGLVLLVVLLLLLRHWGWGLCLIGWNEFILQPIHNLLMGDTKEQRIL
NHVLQHAEPGNAQSVLEAIDTYCEQKEWAMNVGDKKGKIVDAVIQEHQPSVLLELGAYCG
YSAVRMARLLSPGARLITIEINPDCAAITQRMVDFAGVKDKVTLVVGASQDIIPQLKKKY
DVDTLDMVFLDHWKDRYLPDTLLLEECGLLRKGTVLLADNVICPGAPDFLAHVRGSSCFE
CTHYQSFLEYREVVDGLEKAIYKGPGSEAGP
Enzyme 3 Number of Residues 271
Enzyme 3 Molecular Weight 30037
Enzyme 3 Theoretical pI 5.15
Enzyme 3 GO Classification
Function
  • O-methyltransferase activity
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
Component
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol
Enzyme 3 Pathways
Enzyme 3 Reactions
  • S-adenosyl-L-methionine + a catechol = S-adenosyl-L-homocysteine + a guaiacol
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-32
Enzyme 3 Transmembrane Regions Not Available
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 180920 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P21964 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name COMT_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >816 bp
ATGCCGGAGGCCCCGCCTCTGCTGTTGGCAGCTGTGTTGCTGGGCCTGGTGCTGCTGGTG
GTGCTGCTGCTGCTTCTGAGGCACTGGGGCTGGGGCCTGTGCCTTATCGGCTGGAACGAG
TTCATCCTGCAGCCCATCCACAACCTGCTCATGGGTGACACCAAGGAGCAGCGCATCCTG
AACCACGTGCTGCAGCATGCGGAGCCCGGGAACGCACAGAGCGTGCTGGAGGCCATTGAC
ACCTACTGCGAGCAGAAGGAGTGGGCCATGAACGTGGGCGACAAGAAAGGCAAGATCGTG
GACGCCGTGATTCAGGAGCACCAGCCCTCCGTGCTGCTGGAGCTGGGGGCCTACTGTGGC
TACTCAGCTGTGCGCATGGCCCGCCTGCTGTCACCAGGGGCGAGGCTCATCACCATCGAG
ATCAACCCCGACTGTGCCGCCATCACCCAGCGGATGGTGGATTTCGCTGGCGTGAAGGAC
AAGGTCACCCTTGTGGTTGGAGCGTCCCAGGACATCATCCCCCAGCTGAAGAAGAAGTAT
GATGTGGACACACTGGACATGGTCTTCCTCGACCACTGGAAGGACCGGTACCTGCCGGAC
ACGCTTCTCTTGGAGGAATGTGGCCTGCTGCGGAAGGGGACAGTGCTACTGGCTGACAAC
GTGATCTGCCCAGGTGCGCCAGACTTCCTAGCACACGTGCGCGGGAGCAGCTGCTTTGAG
TGCACACACTACCAATCGTTCCTGGAATACAGGGAGGTGGTGGACGGCCTGGAGAAGGCC
ATCTACAAGGGCCCAGGCAGCGAAGCAGGGCCCTGA
Enzyme 3 GenBank Gene ID M65212 Link Image
Enzyme 3 GeneCard ID COMT Link Image
Enzyme 3 GenAtlas ID COMT Link Image
Enzyme 3 HGNC ID HGNC:2228 Link Image
Enzyme 3 Chromosome Location 22
Enzyme 3 Locus 22q11.21-q11.23|22q11.21
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Lundstrom K, Salminen M, Jalanko A, Savolainen R, Ulmanen I: Cloning and characterization of human placental catechol-O-methyltransferase cDNA. DNA Cell Biol. 1991 Apr;10(3):181-9. [PubMed Link Image]
  2. Bertocci B, Miggiano V, Da Prada M, Dembic Z, Lahm HW, Malherbe P: Human catechol-O-methyltransferase: cloning and expression of the membrane-associated form. Proc Natl Acad Sci U S A. 1991 Feb 15;88(4):1416-20. [PubMed Link Image]
  3. Tenhunen J, Salminen M, Lundstrom K, Kiviluoto T, Savolainen R, Ulmanen I: Genomic organization of the human catechol O-methyltransferase gene and its expression from two distinct promoters. Eur J Biochem. 1994 Aug 1;223(3):1049-59. [PubMed Link Image]
  4. Tilgmann C, Kalkkinen N: Purification and partial sequence analysis of the soluble catechol-O-methyltransferase from human placenta: comparison to the rat liver enzyme. Biochem Biophys Res Commun. 1991 Jan 31;174(2):995-1002. [PubMed Link Image]
  5. Ulmanen I, Lundstrom K: Cell-free synthesis of rat and human catechol O-methyltransferase. Insertion of the membrane-bound form into microsomal membranes in vitro. Eur J Biochem. 1991 Dec 18;202(3):1013-20. [PubMed Link Image]
  6. Lachman HM, Papolos DF, Saito T, Yu YM, Szumlanski CL, Weinshilboum RM: Human catechol-O-methyltransferase pharmacogenetics: description of a functional polymorphism and its potential application to neuropsychiatric disorders. Pharmacogenetics. 1996 Jun;6(3):243-50. [PubMed Link Image]
  7. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5639
Enzyme 4 Name Histone-lysine N-methyltransferase, H3 lysine-79 specific
Enzyme 4 Synonyms
  1. Histone H3-K79 methyltransferase
  2. H3-K79-HMTase
  3. DOT1-like protein
Enzyme 4 Gene Name DOT1L
Enzyme 4 Protein Sequence >Histone-lysine N-methyltransferase, H3 lysine-79 specific
MGEKLELRLKSPVGAEPAVYPWPLPVYDKHHDAAHEIIETIRWVCEEIPDLKLAMENYVL
IDYDTKSFESMQRLCDKYNRAIDSIHQLWKGTTQPMKLNTRPSTGLLRHILQQVYNHSVT
DPEKLNNYEPFSPEVYGETSFDLVAQMIDEIKMTDDDLFVDLGSGVGQVVLQVAAATNCK
HHYGVEKADIPAKYAETMDREFRKWMKWYGKKHAEYTLERGDFLSEEWRERIANTSVIFV
NNFAFGPEVDHQLKERFANMKEGGRIVSSKPFAPLNFRINSRNLSDIGTIMRVVELSPLK
GSVSWTGKPVSYYLHTIDRTILENYFSSLKNPKLREEQEAARRRQQRESKSNAATPTKGP
EGKVAGPADAPMDSGAEEEKAGAATVKKPSPSKARKKKLNKKGRKMAGRKRGRPKKMNTA
NPERKPKKNQTALDALHAQTVSQTAASSPQDAYRSPHSPFYQLPPSVQRHSPNPLLVAPT
PPALQKLLESFKIQYLQFLAYTKTPQYKASLQELLGQEKEKNAQLLGAAQQLLSHCQAQK
EEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQLEQDNRALRGQSLQLL
KARCEELQLDWATLSLEKLLKEKQALKSQISEKQRHCLELQISIVELEKSQRQQELLQLK
SCVPPDDALSLHLRGKGALGRELEPDASRLHLELDCTKFSLPHLSSMSPELSMNGQAAGY
ELCGVLSRPSSKQNTPQYLASPLDQEVVPCTPSHVGRPRLEKLSGLAAPDYTRLSPAKIV
LRRHLSQDHTVPGRPAASELHSRAEHTKENGLPYQSPSVPGSMKLSPQDPRPLSPGALQL
AGEKSSEKGLRERAYGSSGELITSLPISIPLSTVQPNKLPVSIPLASVVLPSRAERARST
PSPVLQPRDPSSTLEKQIGANAHGAGSRSLALAPAGFSYAGSVAISGALAGSPASLTPGA
EPATLDESSSSGSLFATVGSRSSTPQHPLLLAQPRNSLPASPAHQLSSSPRLGGAAQGPL
PEASKGDLPSDSGFSDPESEAKRRIVFTITTGAGSAKQSPSSKHSPLTASARGDCVPSHG
QDSRRRGRRKRASAGTPSLSAGVSPKRRALPSVAGLFTQPSGSPLNLNSMVSNINQPLEI
TAISSPETSLKSSPVPYQDHDQPPVLKKERPLSQTNGAHYSPLTSDEEPGSEDEPSSARI
ERKIATISLESKSPPKTLENGGGLAGRKPAPAGEPVNSSKWKSTFSPISDIGLAKSADSP
LQASSALSQNSLFTFRPALEEPSADAKLAAHPRKGFPGSLSGADGLSPGTNPANGCTFGG
GLAADLSLHSFSDGASLPHKGPEAAGLSSPLSFPSQRGKEGSDANPFLSKRQLDGLAGLK
GEGSRGKEAGEGGLPLCGPTDKTPLLSGKAAKARDREVDLKNGHNLFISAAAVPPGSLLS
GPGLAPAASSAGGAASSAQTHRSFLGPFPPGPQFALGPMSLQANLGSVAGSSVLQSLFSS
VPAAAGLVHVSSAATRLTNSHAMGSFSGVAGGTVGGVVFNHAVPSASAHPFGARVGRGAA
CGSATLGPSPLQAAASASASSFQAPASVETRPPPPPPPPPPPLPPPAHLGRSPAGPPVLH
APPPPNAALPPPPTLLASNPEPALLQSLASLPPNQAFLPPTSAASLPPANASLSIKLTSL
PHKGARPSFTVHHQPLPRLALAQAAPGIPQASATGPSAVWVSLGMPPPYAAHLSGVKPR
Enzyme 4 Number of Residues 1739
Enzyme 4 Molecular Weight 184855
Enzyme 4 Theoretical pI 9.88
Enzyme 4 GO Classification Not Available
Enzyme 4 General Function Cell cycle control, cell division, chromosome partitioning
Enzyme 4 Specific Function Histone methyltransferase. Methylates 'Lys-79' of histone H3. Nucleosomes are preferred as substrate compared to free histones
Enzyme 4 Pathways
Enzyme 4 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 22001120 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q8TEK3 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name DOT1L_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >4614 bp
ATGGGGGAGAAGCTGGAGCTGAGACTGAAGTCGCCCGTGGGGGCTGAGCCCGCCGTCTAC
CCGTGGCCGCTGCCGGTCTACGATAAACATCACGATGCTGCTCATGAAATCATCGAGACC
ATCCGATGGGTCTGTGAAGAAATCCCGGATCTCAAGCTCGCTATGGAGAATTACGTTTTA
ATTGACTATGACACCAAAAGCTTCGAGAGCATGCAGAGGCTCTGCGACAAGTACAACCGT
GCCATCGACAGCATCCACCAGCTGTGGAAGGGCACCACGCAGCCCATGAAGCTGAACACG
CGGCCGTCCACTGGACTCCTGCGCCATATCCTGCAGCAGGTCTACAACCACTCGGTGACC
GACCCCGAGAAGCTCAACAACTACGAGCCCTTCTCCCCCGAGGTGTACGGGGAGACCTCC
TTCGACCTGGTGGCCCAGATGATTGATGAGATCAAGATGACCGACGACGACCTGTTTGTG
GACTTGGGGAGCGGTGTGGGCCAGGTCGTGCTCCAGGTTGCTGCTGCCACCAACTGCAAA
CATCACTATGGCGTCGAGAAAGCAGACATCCCGGCCAAGTATGCGGAGACCATGGACCGC
GAGTTCAGGAAGTGGATGAAATGGTATGGAAAAAAGCATGCAGAATACACATTGGAGAGA
GGCGATTTCCTCTCAGAAGAGTGGAGGGAGCGAATCGCCAACACGAGTGTTATATTTGTG
AATAATTTTGCCTTTGGTCCTGAGGTGGATCACCAGCTGAAGGAGCGGTTTGCAAACATG
AAGGAAGGTGGCAGAATCGTGTCCTCGAAACCCTTTGCACCTCTGAACTTCAGAATAAAC
AGTAGAAACTTGAGTGACATCGGCACCATCATGCGCGTGGTGGAGCTCTCGCCCCTGAAG
GGCTCGGTGTCGTGGACGGGGAAGCCAGTCTCCTACTACCTGCACACTATCGACCGCACC
ATACTTGAAAACTATTTTTCTAGTCTGAAAAACCCAAAACTCAGGGAGGAACAGGAGGCA
GCCCGGCGCCGCCAGCAGCGCGAGAGCAAGAGCAACGCGGCCACGCCCACTAAGGGCCCA
GAGGGCAAGGTGGCCGGCCCCGCCGACGCCCCCATGGACTCTGGTGCTGAGGAAGAGAAG
GCGGGAGCAGCCACCGTGAAGAAGCCGTCTCCCTCCAAAGCCCGCAAGAAGAAGCTAAAC
AAGAAGGGGAGGAAGATGGCTGGCCGCAAGCGCGGGCGCCCCAAGAAGATGAACACTGCG
AACCCCGAGCGGAAGCCCAAGAAGAACCAAACTGCACTGGATGCCCTGCACGCTCAGACC
GTGTCTCAGACGGCGGCCTCCTCACCCCAGGATGCCTACAGATCCCCTCACAGCCCGTTC
TACCAGCTACCTCCGAGCGTGCAGCGGCACTCCCCCAACCCGCTGCTGGTGGCGCCCACC
CCGCCCGCGCTGCAGAAGCTTCTAGAGTCCTTCAAGATCCAGTACCTGCAGTTCCTGGCA
TACACAAAGACCCCCCAGTACAAGGCCAGCCTGCAGGAGCTGCTGGGCCAGGAGAAGGAG
AAGAACGCCCAGCTCCTGGGTGCGGCTCAGCAGCTCCTCAGCCACTGCCAGGCCCAGAAG
GAGGAGATCAGGAGGCTGTTTCAGCAAAAATTGGATGAGCTGGGTGTGAAGGCGCTGACC
TACAACGACCTGATTCAAGCGCAGAAGGAGATCTCCGCCCATAACCAGCAGCTGCGGGAG
CAGTCGGAGCAGCTGGAGCAGGACAACCGCGCGCTCCGCGGCCAGAGCTTGCAGCTGCTC
AAGGCTCGCTGCGAGGAGCTGCAGCTGGACTGGGCCACGCTGTCGCTGGAGAAGCTGTTG
AAGGAGAAGCAGGCCCTGAAGAGCCAGATCTCGGAGAAGCAGAGGCACTGCCTGGAGCTG
CAGATCAGCATTGTGGAGCTAGAGAAGAGCCAGCGGCAGCAGGAGCTCCTGCAGCTCAAG
TCCTGTGTGCCGCCTGACGACGCCCTGTCCCTGCACCTGCGTGGGAAGGGCGCCCTGGGC
CGCGAGCTGGAGCCTGACGCCAGCCGGCTGCACCTGGAGCTGGACTGCACCAAGTTCTCG
CTGCCTCACTTGAGCAGCATGAGCCCGGAGCTCTCCATGAACGGCCAGGCTGCTGGCTAT
GAGCTCTGCGGTGTGCTGAGCCGGCCTTCGTCGAAGCAGAACACGCCCCAGTACCTGGCC
TCACCCCTGGACCAGGAGGTGGTGCCCTGTACCCCTAGCCACGTCGGCCGGCCGCGCCTG
GAGAAGCTGTCTGGCCTAGCCGCACCCGACTACACTAGGCTGTCCCCGGCCAAGATTGTG
CTGAGGCGGCACCTGAGCCAGGACCACACGGTGCCCGGCAGGCCGGCTGCCAGTGAGCTG
CATTCGAGAGCTGAGCACACCAAGGAGAACGGCCTTCCCTACCAGAGCCCCAGCGTGCCT
GGCAGCATGAAGCTGAGCCCTCAGGACCCGCGGCCCCTGTCCCCTGGGGCCTTGCAGCTT
GCTGGAGAGAAGAGCAGTGAGAAGGGCCTGAGAGAGCGCGCCTACGGCAGCAGCGGGGAG
CTCATCACCAGCCTGCCCATCAGCATCCCGCTCAGCACCGTGCAGCCCAACAAGCTCCCG
GTCAGCATTCCCCTGGCCAGCGTGGTGCTGCCCAGCCGCGCCGAGAGGGCGAGGAGCACC
CCCAGTCCCGTGCTGCAGCCCCGTGACCCCTCGTCCACACTTGAAAAGCAGATTGGTGCT
AATGCCCACGGTGCTGGGAGCAGAAGCCTTGCCCTGGCCCCCGCAGGCTTCTCCTACGCT
GGCTCGGTGGCCATCAGCGGGGCCTTGGCGGGCAGCCCGGCCTCTCTCACACCTGGAGCC
GAGCCGGCCACCTTGGATGAGTCCTCCAGCTCTGGGAGCCTTTTTGCCACCGTGGGGTCC
CGCAGCTCCACGCCACAGCACCCCCTGCTGCTGGCACAGCCCCGGAACTCGCTTCCTGCC
TCTCCCGCCCACCAGCTCTCCTCCAGTCCCCGGCTTGGTGGGGCCGCCCAGGGCCCGTTG
CCCGAGGCCAGCAAGGGAGACCTGCCCTCCGATTCCGGCTTCTCAGATCCTGAGAGTGAA
GCCAAGAGGAGGATTGTGTTCACCATCACCACTGGTGCGGGCAGTGCCAAGCAGTCGCCC
TCCAGCAAGCACAGCCCCCTGACCGCCAGCGCCCGTGGGGACTGTGTGCCGAGCCACGGG
CAGGACAGTCGCAGGCGCGGCCGGCGGAAGCGAGCATCTGCGGGGACGCCCAGCTTGAGC
GCAGGCGTGTCCCCCAAGCGCCGAGCCCTGCCGTCCGTCGCTGGCCTTTTCACACAGCCT
TCGGGGTCTCCCCTCAACCTCAACTCCATGGTCAGTAACATCAACCAGCCCCTGGAGATT
ACAGCCATCTCGTCCCCGGAGACCTCCCTGAAGAGCTCCCCTGTGCCCTACCAGGACCAC
GACCAGCCCCCCGTGCTCAAGAAGGAGCGGCCTCTGAGCCAGACCAATGGGGCACACTAC
TCCCCACTCACCTCAGACGAGGAGCCAGGCTCTGAGGACGAGCCCAGCAGTGCTCGAATT
GAGAGAAAAATTGCAACAATCTCCTTAGAAAGCAAATCTCCCCCGAAAACCTTGGAAAAT
GGTGGTGGCTTGGCGGGAAGGAAGCCCGCGCCCGCCGGCGAGCCAGTCAATAGCAGCAAG
TGGAAGTCCACCTTCTCGCCCATCTCCGACATCGGCCTGGCCAAGTCGGCGGACAGCCCG
CTGCAGGCCAGCTCCGCCCTCAGCCAGAACTCCCTGTTCACGTTCCGGCCCGCCCTGGAG
GAGCCCTCTGCCGATGCCAAGCTGGCCGCTCACCCCAGGAAAGGCTTTCCCGGCTCCCTG
TCGGGGGCTGACGGACTCAGCCCGGGCACCAACCCTGCCAACGGCTGCACCTTCGGCGGG
GGCCTGGCCGCGGACCTGAGTTTACACAGCTTCAGTGATGGTGCTTCTCTTCCCCACAAG
GGCCCCGAGGCGGCCGGCCTGAGCTCCCCGCTGAGCTTCCCCTCGCAGCGCGGCAAGGAG
GGCTCGGACGCCAACCCTTTCCTGAGCAAGAGGCAGCTGGACGGCCTGGCTGGGCTGAAG
GGCGAGGGCAGCCGCGGCAAGGAGGCAGGGGAGGGCGGCCTACCGCTGTGCGGGCCCACG
GACAAGACCCCACTGCTGAGCGGCAAGGCCGCCAAGGCCCGGGACCGCGAGGTCGACCTC
AAGAATGGCCACAACCTCTTCATCTCTGCGGCGGCCGTGCCTCCCGGAAGCCTCCTCAGC
GGCCCCGGCCTGGCCCCGGCGGCGTCCTCCGCAGGCGGCGCGGCGTCCTCCGCCCAGACG
CACCGGTCCTTCCTGGGCCCCTTCCCGCCGGGACCGCAGTTCGCGCTCGGCCCCATGTCC
CTGCAGGCCAACCTCGGCTCCGTGGCCGGCTCCTCCGTGCTGCAGTCGCTGTTCAGCTCT
GTGCCGGCCGCCGCAGGCCTGGTGCACGTGTCGTCCGCTGCCACCAGACTGACCAACTCG
CACGCCATGGGCAGCTTTTCCGGGGTGGCAGGCGGCACAGTTGGAGGTAACTAG
Enzyme 4 GenBank Gene ID AF509504 Link Image
Enzyme 4 GeneCard ID DOT1L Link Image
Enzyme 4 GenAtlas ID DOT1L Link Image
Enzyme 4 HGNC ID HGNC:24948 Link Image
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Feng Q, Wang H, Ng HH, Erdjument-Bromage H, Tempst P, Struhl K, Zhang Y: Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain. Curr Biol. 2002 Jun 25;12(12):1052-8. [PubMed Link Image]
  2. Nagase T, Nakayama M, Nakajima D, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2001 Apr 27;8(2):85-95. [PubMed Link Image]
  3. Jikuya H, Takano J, Kikuno R, Hirosawa M, Nagase T, Nomura N, Ohara O: Characterization of long cDNA clones from human adult spleen. II. The complete sequences of 81 cDNA clones. DNA Res. 2003 Feb 28;10(1):49-57. [PubMed Link Image]
  4. Min J, Feng Q, Li Z, Zhang Y, Xu RM: Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase. Cell. 2003 Mar 7;112(5):711-23. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5640
Enzyme 5 Name Glycine N-methyltransferase
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name GNMT
Enzyme 5 Protein Sequence >Glycine N-methyltransferase
MVDSVYRTRSLGVAAEGLPDQYADGEAARVWQLYIGDTRSRTAEYKAWLLGLLRQHGCQR
VLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYALKERWNRRHEPAFDKWVIEEANWMT
LDKDVPQSAEGGFDAVICLGNSFAHLPDCKGDQSEHRLALKNIASMVRAGGLLVIDHRNY
DHILSTGCAPPGKNIYYKSDLTKDVTTSVLIVNNKAHMVTLDYTVQVPGAGQDGSPGLSK
FRLSYYPHCLASFTELLQAAFGGKCQHSVLGDFKPYKPGQTYIPCYFIHVLKRTD
Enzyme 5 Number of Residues 295
Enzyme 5 Molecular Weight 32743
Enzyme 5 Theoretical pI 7.03
Enzyme 5 GO Classification Not Available
Enzyme 5 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 5 Specific Function Catalyzes the methylation of glycine by using S- adenosylmethionine (AdoMet) to form N-methylglycine (sarcosine) with the concomitant production of S-adenosylhomocysteine (AdoHcy). Possible crucial role in the regulation of tissue concentration of AdoMet and of metabolism of methionine
Enzyme 5 Pathways
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
Enzyme 5 Reactions
  • S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 8671584 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q14749 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name GNMT_HUMAN Link Image
Enzyme 5 PDB ID 1R74 Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >888 bp
ATGGTGGACAGCGTGTACCGGACCCGCTCCCTGGGGGTGGCGGCCGAAGGGCTCCCGGAC
CAGTACGCGGACGGGGAGGCGGCGCGCGTGTGGCAGCTGTATATCGGAGACACCCGCAGC
CGCACCGCCGAGTACAAGGCATGGCTGCTTGGGCTGCTGCGCCAGCACGGCTGCCAGCGG
GTGCTCGACGTAGCCTGTGGCACTGGGGTGGACTCCATTATGCTGGTGGAAGAGGGCTTC
AGTGTGACGAGTGTGGATGCCAGTGACAAGATGCTGAAGTATGCACTTAAGGAGCGCTGG
AACCGGCGGCACGAGCCCGCCTTCGACAAGTGGGTCATCGAAGAAGCCAACTGGATGACT
CTGGACAAAGATGTGCCCCAGTCAGCAGAGGGTGGCTTTGATGCTGTCATCTGCCTTGGA
AACAGTTTCGCTCACTTGCCAGACTGCAAAGGGGACCAGAGTGAGCACCGGCTGGCGCTG
AAAAACATTGCGAGCATGGTGCGGGCAGGGGGCCTACTGGTCATTGATCATCGCAACTAC
GACCACATCCTCAGTACAGGCTGTGCACCCCCAGGGAAGAACATCTACTATAAGAGTGAC
TTGACCAAGGACGTCACAACATCAGTGCTGATAGTGAACAACAAGGCCCACATGGTGACC
CTGGACTATACGGTGCAGGTGCCGGGGGCTGGCCAGGATGGCTCTCCTGGCTTGAGTAAG
TTCCGGCTCTCCTACTACCCACACTGTCTGGCATCCTTCACGGAGCTGCTCCAAGCAGCC
TTCGGAGGTAAGTGCCAGCACAGCGTCCTGGGCGACTTCAAGCCTTACAAGCCAGGCCAA
ACCTACATTCCCTGCTACTTCATCCACGTGCTCAAGAGGACAGACTGA
Enzyme 5 GenBank Gene ID AF101477 Link Image
Enzyme 5 GeneCard ID GNMT Link Image
Enzyme 5 GenAtlas ID GNMT Link Image
Enzyme 5 HGNC ID HGNC:4415 Link Image
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Chen YM, Shiu JY, Tzeng SJ, Shih LS, Chen YJ, Lui WY, Chen PH: Characterization of glycine-N-methyltransferase-gene expression in human hepatocellular carcinoma. Int J Cancer. 1998 Mar 2;75(5):787-93. [PubMed Link Image]
  2. Chen YM, Chen LY, Wong FH, Lee CM, Chang TJ, Yang-Feng TL: Genomic structure, expression, and chromosomal localization of the human glycine N-methyltransferase gene. Genomics. 2000 May 15;66(1):43-7. [PubMed Link Image]
  3. Luka Z, Cerone R, Phillips JA 3rd, Mudd HS, Wagner C: Mutations in human glycine N-methyltransferase give insights into its role in methionine metabolism. Hum Genet. 2002 Jan;110(1):68-74. Epub 2001 Dec 7. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5641
Enzyme 6 Name Histone-lysine N-methyltransferase, H3 lysine-4 specific SET7
Enzyme 6 Synonyms
  1. Histone H3-K4 methyltransferase
  2. H3-K4-HMTase
  3. SET domain-containing protein 7
  4. Set9
  5. SET7/9
Enzyme 6 Gene Name SETD7
Enzyme 6 Protein Sequence >Histone-lysine N-methyltransferase, H3 lysine-4 specific SET7
MDSDDEMVEEAVEGHLDDDGLPHGFCTVTYSSTDRFEGNFVHGEKNGRGKFFFFDGSTLE
GYYVDDALQGQGVYTYEDGGVLQGTYVDGELNGPAQEYDTDGRLIFKGQYKDNIRHGVCW
IYYPDGGSLVGEVNEDGEMTGEKIAYVYPDERTALYGKFIDGEMIEGKLATLMSTEEGRP
HFELMPGNSVYHFDKSTSSCISTNALLPDPYESERVYVAESLISSAGEGLFSKVAVGPNT
VMSFYNGVRITHQEVDSRDWALNGNTLSLDEETVIDVPEPYNHVSKYCASLGHKANHSFT
PNCIYDMFVHPRFGPIKCIRTLRAVEADEELTVAYGYDHSPPGKSGPEAPEWYQVELKAF
QATQQK
Enzyme 6 Number of Residues 366
Enzyme 6 Molecular Weight 40721
Enzyme 6 Theoretical pI 4.25
Enzyme 6 GO Classification Not Available
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function Histone methyltransferase. Methylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation
Enzyme 6 Pathways
Enzyme 6 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 18030038 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q8WTS6 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name SETD7_HUMAN Link Image
Enzyme 6 PDB ID 1N6C Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1101 bp
ATGGATAGCGACGACGAGATGGTGGAGGAGGCGGTGGAAGGGCACCTGGACGATGACGGA
TTACCGCACGGGTTCTGCACAGTCACCTACTCCTCCACAGACAGATTTGAGGGGAACTTT
GTTCACGGAGAAAAGAACGGACGGGGGAAGTTCTTCTTCTTTGATGGCAGCACCCTGGAG
GGGTATTATGTGGATGATGCCTTGCAGGGCCAGGGAGTTTACACTTACGAAGATGGGGGA
GTTCTCCAGGGCACGTATGTAGACGGAGAGCTGAACGGTCCAGCCCAGGAATATGACACA
GATGGGAGACTGATCTTCAAGGGGCAGTATAAAGATAACATTCGTCATGGAGTGTGCTGG
ATATATTACCCAGATGGAGGAAGCCTTGTAGGAGAAGTAAATGAAGATGGGGAGATGACT
GGAGAGAAGATAGCCTATGTGTACCCTGATGAGAGGACCGCACTTTATGGGAAATTTATT
GATGGAGAGATGATAGAAGGCAAACTGGCTACCCTTATGTCCACTGAAGAAGGGAGGCCT
CACTTTGAACTGATGCCTGGAAATTCAGTGTACCACTTTGATAAGTCGACTTCATCTTGC
ATTTCTACCAATGCTCTTCTTCCAGATCCTTATGAATCAGAAAGGGTTTATGTTGCTGAA
TCTCTTATTTCCAGTGCTGGAGAAGGACTTTTTTCAAAGGTAGCTGTGGGACCTAATACT
GTTATGTCTTTTTATAATGGAGTTCGAATTACACACCAAGAGGTTGACAGCAGGGACTGG
GCCCTTAATGGGAACACCCTCTCCCTTGATGAAGAAACGGTCATTGATGTGCCTGAGCCC
TATAACCACGTATCCAAGTACTGTGCCTCCTTGGGACACAAGGCAAATCACTCCTTCACT
CCAAACTGCATCTACGATATGTTTGTCCACCCCCGTTTTGGGCCCATCAAATGCATCCGC
ACCCTGAGAGCAGTGGAGGCCGATGAAGAGCTCACCGTTGCCTATGGCTATGACCACAGC
CCCCCCGGGAAGAGTGGGCCTGAAGCCCCTGAGTGGTACCAGGTGGAGCTGAAGGCCTTC
CAGGCCACCCAGCAAAAGTGA
Enzyme 6 GenBank Gene ID AF448510 Link Image
Enzyme 6 GeneCard ID SETD7 Link Image
Enzyme 6 GenAtlas ID SETD7 Link Image
Enzyme 6 HGNC ID HGNC:30412 Link Image
Enzyme 6 Chromosome Location 4
Enzyme 6 Locus 4q28
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Wang H, Cao R, Xia L, Erdjument-Bromage H, Borchers C, Tempst P, Zhang Y: Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase. Mol Cell. 2001 Dec;8(6):1207-17. [PubMed Link Image]
  2. Nishioka K, Chuikov S, Sarma K, Erdjument-Bromage H, Allis CD, Tempst P, Reinberg D: Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation. Genes Dev. 2002 Feb 15;16(4):479-89. [PubMed Link Image]
  3. Nagase T, Kikuno R, Hattori A, Kondo Y, Okumura K, Ohara O: Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Dec 31;7(6):347-55. [PubMed Link Image]
  4. Wilson JR, Jing C, Walker PA, Martin SR, Howell SA, Blackburn GM, Gamblin SJ, Xiao B: Crystal structure and functional analysis of the histone methyltransferase SET7/9. Cell. 2002 Oct 4;111(1):105-15. [PubMed Link Image]
  5. Jacobs SA, Harp JM, Devarakonda S, Kim Y, Rastinejad F, Khorasanizadeh S: The active site of the SET domain is constructed on a knot. Nat Struct Biol. 2002 Nov;9(11):833-8. [PubMed Link Image]
  6. Xiao B, Jing C, Wilson JR, Walker PA, Vasisht N, Kelly G, Howell S, Taylor IA, Blackburn GM, Gamblin SJ: Structure and catalytic mechanism of the human histone methyltransferase SET7/9. Nature. 2003 Feb 6;421(6923):652-6. Epub 2003 Jan 22. [PubMed Link Image]
  7. Kwon T, Chang JH, Kwak E, Lee CW, Joachimiak A, Kim YC, Lee J, Cho Y: Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet. EMBO J. 2003 Jan 15;22(2):292-303. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5643
Enzyme 7 Name Phenylethanolamine N-methyltransferase
Enzyme 7 Synonyms
  1. PNMTase
  2. Noradrenaline N-methyltransferase
Enzyme 7 Gene Name PNMT
Enzyme 7 Protein Sequence >Phenylethanolamine N-methyltransferase
MSGADRSPNAGAAPDSAPGQAAVASAYQRFEPRAYLRNNYAPPRGDLCNPNGVGPWKLRC
LAQTFATGEVSGRTLIDIGSGPTVYQLLSACSHFEDITMTDFLEVNRQELGRWLQEEPGA
FNWSMYSQHACLIEGKGECWQDKERQLRARVKRVLPIDVHQPQPLGAGSPAPLPADALVS
AFCLEAVSPDLASFQRALDHITTLLRPGGHLLLIGALEESWYLAGEARLTVVPVSEEEVR
EALVRSGYKVRDLRTYIMPAHLQTGVDDVKGVFFAWAQKVGL
Enzyme 7 Number of Residues 282
Enzyme 7 Molecular Weight 30855
Enzyme 7 Theoretical pI 5.96
Enzyme 7 GO Classification
Function
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
Component
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function Converts noradrenaline to adrenaline
Enzyme 7 Pathways
Enzyme 7 Reactions
  • S-adenosyl-L-methionine + phenylethanolamine = S-adenosyl-L-homocysteine + N-methylphenylethanolamine
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 190142 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P11086 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name PNMT_HUMAN Link Image
Enzyme 7 PDB ID 1N7J Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >849 bp
ATGAGCGGCGCAGACCGTAGCCCCAATGCGGGCGCAGCCCCTGACTCGGCCCCGGGCCAG
GCGGCGGTGGCTTCGGCCTACCAGCGCTTCGAGCCGCGCGCCTACCTCCGCAACAACTAC
GCGCCCCCTCGCGGGGACCTGTGCAACCCGAACGGCGTCGGGCCGTGGAAGCTGCGCTGC
TTGGCGCAGACCTTCGCCACCGGTGAAGTGTCCGGACGCACCCTCATCGACATTGGTTCA
GGCCCCACCGTGTACCAGCTGCTCAGTGCCTGCAGCCACTTTGAGGACATCACCATGACA
GATTTCCTGGAGGTCAACCGCCAGGAGCTGGGGCGCTGGCTGCAGGAGGAGCCGGGGGCC
TTCAACTGGAGCATGTACAGCCAACATGCCTGCCTCATTGAGGGCAAGGGGGAATGCTGG
CAGGATAAGGAGCGCCAGCTGCGAGCCAGGGTGAAACGGGTCCTGCCCATCGACGTGCAC
CAGCCCCAGCCCCTGGGTGCTGGGAGCCCAGCTCCCCTGCCTGCTGACGCCCTGGTCTCT
GCCTTCTGCTTGGAGGCTGTGAGCCCAGATCTTGCCAGCTTTCAGCGGGCCCTGGACCAC
ATCACCACGCTGCTGAGGCCTGGGGGGCACCTCCTCCTCATCGGGGCCCTGGAGGAGTCG
TGGTACCTGGCTGGGGAGGCCAGGCTGACGGTGGTGCCAGTGTCTGAGGAGGAGGTGAGG
GAGGCCCTGGTGCGTAGTGGCTACAAGGTCCGGGACCTCCGCACCTATATCATGCCTGCC
CACCTTCAGACAGGCGTAGATGATGTCAAGGGCGTCTTCTTCGCCTGGGCTCAGAAGGTT
GGGCTGTGA
Enzyme 7 GenBank Gene ID J03727 Link Image
Enzyme 7 GeneCard ID PNMT Link Image
Enzyme 7 GenAtlas ID PNMT Link Image
Enzyme 7 HGNC ID HGNC:9160 Link Image
Enzyme 7 Chromosome Location 17
Enzyme 7 Locus 17q21-q22
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Kaneda N, Ichinose H, Kobayashi K, Oka K, Kishi F, Nakazawa A, Kurosawa Y, Fujita K, Nagatsu T: Molecular cloning of cDNA and chromosomal assignment of the gene for human phenylethanolamine N-methyltransferase, the enzyme for epinephrine biosynthesis. J Biol Chem. 1988 Jun 5;263(16):7672-7. [PubMed Link Image]
  2. Baetge EE, Behringer RR, Messing A, Brinster RL, Palmiter RD: Transgenic mice express the human phenylethanolamine N-methyltransferase gene in adrenal medulla and retina. Proc Natl Acad Sci U S A. 1988 May;85(10):3648-52. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5645
Enzyme 8 Name Arsenite methyltransferase
Enzyme 8 Synonyms
  1. S-adenosyl-L- methionine:arsenic(IIImethyltransferase
  2. Methylarsonite methyltransferase
Enzyme 8 Gene Name AS3MT
Enzyme 8 Protein Sequence >Arsenite methyltransferase
MAALRDAEIQKDVQTYYGQVLKRSADLQTNGCVTTARPVPKHIREALQNVHEEVALRYYG
CGLVIPEHLENCWILDLGSGSGRDCYVLSQLVGEKGHVTGIDMTKGQVEVAEKYLDYHME
KYGFQASNVTFFHGNIEKLAEAGIKNESHDIVVSNCVINLVPDKQQVLQEAYRVLKHGGE
LYFSDVYTSLELPEEIRTHKVLWGECLGGALYWKELAVLAQKIGFCPPRLVTANLITIQN
KELERVIGDCRFVSATFRLFKHSKTGPTKRCQVIYNGGITGHEKELMFDANFTFKEGEIV
EVDEETAAILKNSRFAQDFLIRPIGEKLPTSGGCSALELKDIITDPFKLAEESDSMKSRC
VPDAAGGCCGTKKSC
Enzyme 8 Number of Residues 375
Enzyme 8 Molecular Weight 41747
Enzyme 8 Theoretical pI 6.14
Enzyme 8 GO Classification Not Available
Enzyme 8 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 8 Specific Function Catalyzes the transfer of a methyl group from AdoMet to trivalent arsenicals producing methylated and dimethylated arsenicals. It methylates arsenite to form methylarsonate, Me- AsO(3)H(2), which is reduced by methylarsonate reductase to methylarsonite, Me-As(OH)2. Methylarsonite is also a substrate and it is converted into the much less toxic compound dimethylarsinate (cacodylate), Me(2)As(O)-OH
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions
  • (1) S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + methylarsonate
  • (2) S-adenosyl-L-methionine + methylarsonite = S-adenosyl-L-homocysteine + dimethylarsinate
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 9963861 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q9HBK9 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name AS3MT_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1017 bp
ATGGCTGCACTTCGTGACGCTGAGATACAGAAGGACGTGCAGACCTACTACGGGCAGGTG
CTGAAGAGATCGGCAGACCTCCAGACCAACGGCTGTGTCACCACAGCCAGGCCGGTCCCC
AAGCACATCCGGGAAGCCTTGCAAAATGTACACGAAGAAGTAGCCCTAAGATATTATGGC
TGTGGTCTGGTGATCCCTGAGCATCTAGAAAACTGCTGGATTTTGGATCTGGGTAGTGGA
AGTGGCAGAGATTGCTATGTACTTAGCCAGCTGGTTGGTGAAAAAGGACACGTGACTGGA
ATAGACATGACCAAAGGCCAGGTGGAAGTGGCTGAAAAGTATCTTGACTATCACATGGAA
AAATATGGCTTCCAGGCATCTAATGTGACTTTTTTCCATGGCAACATTGAGAAGTTGGCA
GAGGCTGGAATCAAGAATGAGAGCCATGATATTGTTGTATCAAACTGTGTTATTAACCTT
GTGCCTGATAAACAACAAGTGCTTCAGGAGGCATATCGGGTGCTGAAGCATGGTGGGGAG
TTATATTTCAGTGACGTCTATACGAGCCTTGAACTGCCAGAAGAAATCAGGACACACAAA
GTTTTATGGGGTGAGTGTCTGGGTGGTGCTTTATACTGGAAGGAACTTGCTGTCCTTGCT
CAAAAAATTGGGTTCTGCCCTCCACGTTTGGTCACTGCCAATCTCATTACAATTCAAAAC
AAGGAACTGGAAAGAGTTATCGGTGACTGTCGTTTTGTTTCTGCAACATTTCGCCTCTTC
AAACACTCTAAGACAGGACCAACCAAGAGATGCCAAGTTATTTACAATGGAGGAATTACA
GGACATGAAAAAGAACTAATGTTTGATGCCAATTTTACATTTAAGGAAGGTGAAATTGTT
GAAGTGGATGAAGAAACAGCAGCTATCTTGAAGAATTCAAGATTTGCTCAAGATTTTCTG
ATCAGACCAATTGGAGAGAAGTTGCCAACATCTGGAGCTGTTCTGCTTTGGAGTTAA
Enzyme 8 GenBank Gene ID AF226730 Link Image
Enzyme 8 GeneCard ID AS3MT Link Image
Enzyme 8 GenAtlas ID AS3MT Link Image
Enzyme 8 HGNC ID HGNC:17452 Link Image
Enzyme 8 Chromosome Location Not Available
Enzyme 8 Locus Not Available
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References Not Available
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5646
Enzyme 9 Name tRNA
Enzyme 9 Synonyms
  1. 5-methylaminomethyl-2-thiouridylate-methyltransferase
  2. Mitochondrial tRNA-specific 2-thiouridylase 1
  3. MTO2 homolog
Enzyme 9 Gene Name TRMU
Enzyme 9 Protein Sequence >tRNA
MQALRHVVCALSGGVDSAVAALLLRRRGYQVTGVFMKNWDSLDEHGVCTADKDCEDAYRV
CQILDIPFHQVSYVKEYWNDVFSDFLNEYEKGRTPNPDIVCNKHIKFSCFFHYAVDNLGA
DAIATGHYARTSLEDEEVFEQKHVKKPEGLFRNRFEVRNAVKLLQAADSFKDQTFFLSQV
SQDALRRTIFPLGGLTKEFVKKIAAENRLHHVLQKKESMGMCFIGKRNFEHFLLQYLQPR
PGHFISIEDNKVLGTHKGWFLYTLGQRANIGGLREPWYVVEKDSVKGDVFVAPRTDHPAL
YRDLLRTSRVHWIAEEPPAALVRDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTAVQAV
RALATGQFAVFYKGDECLGSGKILRLGPSAYTLQKGQRRAGMATESPSDSPEDGPGLSPL
L
Enzyme 9 Number of Residues 421
Enzyme 9 Molecular Weight 47745
Enzyme 9 Theoretical pI 8.12
Enzyme 9 GO Classification
Function
  • RNA methyltransferase activity
  • catalytic activity
  • methyltransferase activity
  • tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase activity
  • tRNA methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • RNA metabolism
  • RNA processing
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • tRNA processing
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 9 General Function Translation, ribosomal structure and biogenesis
Enzyme 9 Specific Function Responsible for the biosynthesis of 5-taurinomethyl-2- thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) in the wobble position
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions
  • S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing 5-methylaminomethyl-2-thiouridylate
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-20
Enzyme 9 Transmembrane Regions Not Available
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 17432490 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID O75648 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name TRMU_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1266 bp
ATGCAGGCCTTGCGGCACGTCGTGTGCGCCCTGTCCGGCGGCGTGGACAGCGCCGTGGCC
GCGCTGCTGCTGAGGCGGAGAGGTTACCAGGTGACAGGGGTGTTTATGAAGAACTGGGAC
TCACTGGATGAACATGGGGTCTGTACTGCCGACAAAGACTGTGAAGATGCTTACAGAGTT
TGCCAGATCTTAGACATCCCTTTCCATCAAGTGTCCTACGTAAAGGAGTATTGGAATGAT
GTGTTCAGTGACTTTTTGAATGAGTATGAAAAAGGAAGGACTCCCAATCCTGACATAGTT
TGCAACAAGCACATCAAATTTAGTTGCTTTTTTCATTATGCTGTGGATAATCTTGGGGCA
GATGCCATTGCCACAGGTCACTATGCAAGAACTTCCCTGGAAGATGAAGAAGTCTTTGAG
CAGAAGCACGTTAAGAAGCCCGAAGGGCTTTTCAGAAATCGGTTTGAAGTTAGAAATGCG
GTAAAACTCCTCCAGGCAGCTGACAGCTTTAAAGACCAGACCTTCTTTCTCAGCCAGGTT
TCCCAGGATGCCCTGAGGAGAACCATCTTCCCTCTGGGGGGATTAACGAAAGAGTTTGTA
AAGAAAATCGCTGCTGAGAATAGACTTCATCATGTGCTTCAGAAGAAAGAGAGCATGGGC
ATGTGTTTCATCGGGAAGAGGAATTTTGAACATTTCCTTCTTCAGTATCTGCAGCCTCGA
CCTGGTCACTTTATTTCCATAGAAGACAATAAGGTTCTGGGAACACATAAAGGTTGGTTC
CTGTATACCTTGGGCCAGAGAGCAAACATAGGTGGCCTGAGAGAGCCCTGGTACGTGGTG
GAGAAGGACAGCGTCAAGGGTGACGTGTTTGTGGCCCCCCGGACAGACCACCCAGCCCTG
TACAGGGACCTGCTGAGGACCAGCCGCGTGCACTGGATTGCGGAGGAGCCTCCCGCAGCA
CTGGTCCGGGACAAGATGATGGAGTGCCACTTCCGATTCCGCCACCAGATGGCACTAGTG
CCCTGTGTGCTGACCCTCAATCAAGATGGCACCGTGTGGGTGACAGCTGTGCAGGCTGTG
CGTGCCCTTGCCACAGGACAGTTTGCTGTGTTCTACAAGGGGGACGAGTGCCTGGGCAGC
GGGAAGATCCTGCGGCTGGGGCCGTCTGCCTACACGCTCCAGAAGGGCCAGCGCAGAGCT
GGGATGGCCACTGAGAGCCCCAGTGACAGCCCAGAAGATGGTCCAGGCCTGAGTCCCTTG
CTCTGA
Enzyme 9 GenBank Gene ID AY062123 Link Image
Enzyme 9 GeneCard ID TRMU Link Image
Enzyme 9 GenAtlas ID TRMU Link Image
Enzyme 9 HGNC ID HGNC:25481 Link Image
Enzyme 9 Chromosome Location Not Available
Enzyme 9 Locus Not Available
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5647
Enzyme 10 Name Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific
Enzyme 10 Synonyms
  1. H3-K36-HMTase
  2. H4-K20-HMTase
  3. Nuclear receptor-binding SET domain-containing protein 1
  4. NR-binding SET domain-containing protein
  5. Androgen receptor-associated coregulator 267
Enzyme 10 Gene Name NSD1
Enzyme 10 Protein Sequence >Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific
MDQTCELPRRNCLLPFSNPVNLDAPEDKDSPFGNGQSNFSEPLNGCTMQLSTVSGTSQNA
YGQDSPSCYIPLRRLQDLASMINVEYLNGSADGSESFQDPEKSDSRAQTPIVCTSLSPGG
PTALAMKQEPSCNNSPELQVKVTKTIKNGFLHFENFTCVDDADVDSEMDPEQPVTEDESI
EEIFEETQTNATCNYETKSENGVKVAMGSEQDSTPESRHGAVKSPFLPLAPQTETQKNKQ
RNEVDGSNEKAALLPAPFSLGDTNITIEEQLNSINLSFQDDPDSSTSTLGNMLELPGTSS
SSTSQELPFCQPKKKSTPLKYEVGDLIWAKFKRRPWWPCRICSDPLINTHSKMKVSNRRP
YRQYYVEAFGDPSERAWVAGKAIVMFEGRHQFEELPVLRRRGKQKEKGYRHKVPQKILSK
WEASVGLAEQYDVPKGSKNRKCIPGSIKLDSEEDMPFEDCTNDPESEHDLLLNGCLKSLA
FDSEHSADEKEKPCAKSRARKSSDNPKRTSVKKGHIQFEAHKDERRGKIPENLGLNFISG
DISDTQASNELSRIANSLTGSNTAPGSFLFSSCGKNTAKKEFETSNGDSLLGLPEGALIS
KCSREKNKPQRSLVCGSKVKLCYIGAGDEEKRSDSISICTTSDDGSSDLDPIEHSSESDN
SVLEIPDAFDRTENMLSMQKNEKIKYSRFAATNTRVKAKQKPLISNSHTDHLMGCTKSAE
PGTETSQVNLSDLKASTLVHKPQSDFTNDALSPKFNLSSSISSENSLIKGGAANQALLHS
KSKQPKFRSIKCKHKENPVMAEPPVINEECSLKCCSSDTKGSPLASISKSGKVDGLKLLN
NMHEKTRDSSDIETAVVKHVLSELKELSYRSLGEDVSDSGTSKPSKPLLFSSASSQNHIP
IEPDYKFSTLLMMLKDMHDSKTKEQRLMTAQNLVSYRSPGRGDCSTNSPVGVSKVLVSGG
STHNSEKKGDGTQNSANPSPSGGDSALSGELSASLPGLLSDKRDLPASGKSRSDCVTRRN
CGRSKPSSKLRDAFSAQMVKNTVNRKALKTERKRKLNQLPSVTLDAVLQGDRERGGSLRG
GAEDPSKEDPLQIMGHLTSEDGDHFSDVHFDSKVKQSDPGKISEKGLSFENGKGPELDSV
MNSENDELNGVNQVVPKKRWQRLNQRRTKPRKRMNRFKEKENSECAFRVLLPSDPVQEGR
DEFPEHRTPSASILEEPLTEQNHADCLDSAGPRLNVCDKSSASIGDMEKEPGIPSLTPQA
ELPEPAVRSEKKRLRKPSKWLLEYTEEYDQIFAPKKKQKKVQEQVHKVSSRCEEESLLAR
GRSSAQNKQVDENSLISTKEEPPVLEREAPFLEGPLAQSELGGGHAELPQLTLSVPVAPE
VSPRPALESEELLVKTPGNYESKRQRKPTKKLLESNDLDPGFMPKKGDLGLSKKCYEAGH
LENGITESCATSYSKDFGGGTTKIFDKPRKRKRQRHAAAKMQCKKVKNDDSSKEIPGSEG
ELMPHRTATSPKETVEEGVEHDPGMPASKKMQGERGGGAALKENVCQNCEKLGELLLCEA
QCCGAFHLECLGLTEMPRGKFICNECRTGIHTCFVCKQSGEDVKRCLLPLCGKFYHEECV
QKYPPTVMQNKGFRCSLHICITCHAANPANVSASKGRLMRCVRCPVAYHANDFCLAAGSK
ILASNSIICPNHFTPRRGCRNHEHVNVSWCFVCSEGGSLLCCDSCPAAFHRECLNIDIPE
GNWYCNDCKAGKKPHYREIVWVKVGRYRWWPAEICHPRAVPSNIDKMRHDVGEFPVLFFG
SNDYLWTHQARVFPYMEGDVSSKDKMGKGVDGTYKKALQEAAARFEELKAQKELRQLQED
RKNDKKPPPYKHIKVNRPIGRVQIFTADLSEIPRCNCKATDENPCGIDSECINRMLLYEC
HPTVCPAGGRCQNQCFSKRQYPEVEIFRTLQRGWGLRTKTDIKKGEFVNEYVGELIDEEE
CRARIRYAQEHDITNFYMLTLDKDRIIDAGPKGNYARFMNHCCQPNCETQKWSVNGDTRV
GLFALSDIKAGTELTFNYNLECLGNGKTVCKCGAPNCSGFLGVRPKNQPIATEEKSKKFK
KKQQGKRRTQGEITKEREDECFSCGDAGQLVSCKKPGCPKVYHADCLNLTKRPAGKWECP
WHQCDICGKEAASFCEMCPSSFCKQHREGMLFISKLDGRLSCTEHDPCGPNPLEPGEIRE
YVPPPVPLPPGPSTHLAEQSTGMAAQAPKMSDKPPADTNQMLSLSKKALAGTCQRPLLPE
RPLERTDSRPQPLDKVRDLAGSGTKSQSLVSSQRPLDRPPAVAGPRPQLSDKPSPVTSPS
SSPSVRSQPLERPLGTADPRLDKSIGAASPRPQSLEKTSVPTGLRLPPPDRLLITSSPKP
QTSDRPTDKPHASLSQRLPPPEKVLSAVVQTLVAKEKALRPVDQNTQSKNRAALVMDLID
LTPRQKERAASPHQVTPQADEKMPVLESSSWPASKGLGHMPRAVEKGCVSDPLQTSGKAA
APSEDPWQAVKSLTQARLLSQPPAKAFLYEPTTQASGRASAGAEQTPGPLSQSPGLVKQA
KQMVGGQQLPALAAKSGQSFRSLGKAPASLPTEEKKLVTTEQSPWALGKASSRAGLWPIV
AGQTLAQSCWSAGSTQTLAQTCWSLGRGQDPKPEQNTLPALNQAPSSHKCAESEQK
Enzyme 10 Number of Residues 2696
Enzyme 10 Molecular Weight 296654
Enzyme 10 Theoretical pI 8.08
Enzyme 10 GO Classification
Function
  • acid-amino acid ligase activity
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • protein binding
  • transition metal ion binding
  • ubiquitin-protein ligase activity
  • zinc ion binding
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein modification
  • protein ubiquitination
  • regulation of biological process
  • regulation of cellular metabolism
  • regulation of metabolism
  • regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • regulation of physiological process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
  • ubiquitin cycle
Component
  • protein complex
  • ubiquitin ligase complex
Enzyme 10 General Function Not Available
Enzyme 10 Specific Function Histone methyltransferase. Preferentially methylates 'Lys-36' of histone H3 and 'Lys-20' of histone H4 (in vitro). Transcriptional intermediary factor capable of both negatively or positively influencing transcription, depending on the cellular context
Enzyme 10 Pathways
Enzyme 10 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 16755530 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q96L73 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name NSD1_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >7284 bp
ATGCCCCTGAAGACAAGGACAGCCCTTTCGGATGATCCAGATTCCAGTACCAGTACATTA
GGAAACATGCTAGAATTACCTGGAACTTCATCATCATCTACTTCACAGGAATTGCCATTT
TGTCAACCTAAGAAAAAGTCTACGCCACTGAAGTATGAAGTTGGAGATCTCATCTGGGCA
AAATTCAAGAGACGCCCATGGTGGCCCTGCAGGATTTGTTCTGATCCGTTGATTAACACA
CATTCAAAAATGAAAGTTTCCAACCGGAGGCCCTATCGGCAGTACTACGTGGAGGCTTTT
GGAGATCCTTCTGAGAGAGCCTGGGTGGCTGGAAAAGCAATCGTCATGTTTGAAGGCAGA
CATCAATTCGAAGAGCTACCTGTCCTTAGGAGAAGAGGGAAACAGAAAGAAAAAGGATAT
AGGCATAAGGTTCCTCAGAAAATTTTGAGTAAATGGGAAGCCAGTGTTGGACTTGCAGAA
CAGTATGATGTTCCCAAGGGGTCAAAGAACCGAAAATGTATTCCTGGTTCAATCAAGTTG
GACAGTGAAGAAGATATGCCATTTGAAGACTGCACAAATGATCCTGAGTCAGAACATGAC
CTGTTGCTTAATGGCTGTTTGAAATCACTGGCTTTTGATTCTGAACATTCTGCAGATGAG
AAGGAAAAGCCTTGTGCTAAATCTCGAGCCAGAAAGAGCTCTGATAATCCAAAAAGGACT
AGTGTGAAAAAGGGCCACATACAATTTGAAGCACATAAAGATGAACGGAGGGGAAAGATT
CCAGAGAACCTTGGCCTAAACTTTATCTCTGGGGATATATCTGATACGCAGGCCTCTAAT
GAACTTTCCAGGATAGCAAATAGCCTCACAGGGTCCAACACTGCCCCAGGAAGTTTTCTG
TTTTCTTCCTGTGGAAAAAACACTGCAAAGAAAGAATTTGAGACTTCAAATGGTGACTCT
TTATTGGGCTTGCCTGAGGGTGCTTTGATCTCAAAGTGTTCTCGAGAGAAGAATAAACCC
CAACGAAGCCTGGTGTGTGGTTCAAAAGTGAAGCTCTGCTATATTGGAGCAGGTGATGAG
GAAAAGCGAAGTGATTCCATTAGTATCTGTACCACTTCTGATGATGGAAGCAGTGACCTG
GATCCCATAGAACACAGCTCAGAGTCTGATAACAGTGTCCTTGAAATTCCAGATGCTTTC
GATAGAACAGAGAACATGTTATCTATGCAGAAAAATGAAAAGATAAAGTATTCTAGGTTT
GCTGCCACAAACACTAGGGTAAAAGCAAAACAGAAGCCTCTCATTAGTAACTCACATACA
GACCACTTAATGGGTTGTACTAAGAGTGCAGAGCCTGGAACCGAGACGTCTCAGGTTAAT
CTCTCTGATCTGAAGGCATCTACTCTTGTTCACAAACCCCAGTCAGATTTTACAAATGAT
GCTCTCTCTCCAAAATTCAACCTGTCATCAAGCATATCCAGTGAGAACTCGTTAATAAAG
GGTGGGGCAGCAAATCAAGCTCTATTACATTCGAAAAGCAAACAGCCCAAGTTCCGAAGT
ATAAAGTGCAAACACAAAGAAAATCCAGTTATGGCAGAACCCCCAGTTATAAATGAGGAG
TGCAGTTTGAAATGCTGCTCTTCTGATACCAAAGGCTCTCCTTTGGCCAGCATTTCTAAA
AGTGGGAAAGTGGATGGTCTAAAACTACTGAACAATATGCATGAGAAAACCAGGGATTCA
AGTGACATAGAAACAGCAGTGGTGAAACATGTTTTATCCGAGTTGAAGGAACTCTCTTAC
AGATCCTTAGGTGAGGATGTCAGTGACTCTGGAACATCAAAGCCATCAAAACCATTACTT
TTCTCTTCTGCTTCTAGTCAGAATCACATACCTATTGAACCAGACTACAAATTCAGTACA
TTGCTAATGATGTTGAAAGATATGCATGATAGTAAGACGAAGGAGCAGCGGTTGATGACT
GCTCAAAACCTGGTCTCTTACCGGAGTCCTGGTCGTGGGGACTGTTCTACTAATAGTCCT
GTAGGAGTCTCTAAGGTTTTGGTTTCAGGAGGCTCCACACACAATTCAGAGAAAAAGGGA
GATGGCACTCAGAACTCCGCCAATCCTAGCCCTAGTGGGGGTGACTCTGCATTATCTGGC
GAGTTGTCTGCTTCCCTACCTGGCTTACTGTCCGACAAGAGAGACCTCCCTGCTTCTGGT
AAAAGTCGTTCAGACTGTGTTACTAGGCGCAACTGTGGACGATCAAAGCCTTCATCCAAA
TTGCGAGATGCTTTTTCAGCCCAAATGGTAAAGAACACAGTGAACCGTAAAGCCTTAAAG
ACCGAGCGCAAAAGAAAACTGAATCAGCTTCCAAGTGTGACTCTTGATGCTGTACTGCAG
GGAGACCGAGAACGTGGAGGTTCATTGAGAGGTGGGGCAGAAGATCCTAGTAAAGAGGAT
CCCCTTCAGATAATGGGCCACTTAACAAGTGAAGATGGTGACCATTTTTCTGATGTGCAT
TTCGATAGCAAGGTTAAGCAATCTGATCCTGGTAAAATTTCTGAAAAAGGACTCTCTTTT
GAAAACGGAAAAGGCCCAGAGCTGGACTCTGTAATGAACAGTGAGAATGATGAACTCAAT
GGTGTAAATCAAGTGGTGCCTAAAAAGCGGTGGCAGCGTTTAAACCAAAGGCGCACTAAA
CCTCGTAAGCGCATGAACAGATTTAAAGAGAAAGAAAACTCTGAGTGTGCCTTTAGGGTC
TTACTTCCTAGTGACCCTGTGCAGGAGGGGCGGGATGAGTTTCCAGAGCATAGAACTCCT
TCAGCAAGCATACTTGAGGAACCACTGACAGAGCAAAATCATGCTGACTGCTTAGATTCA
GCTGGGCCACGGTTAAATGTTTGTGATAAATCCAGTGCCAGCATTGGTGACATGGAAAAG
GAGCCAGGAATTCCCAGTTTGACACCACAGGCTGAGCTCCCTGAACCAGCTGTGCGGTCA
GAGAAGAAACGCCTTAGGAAGCCAAGCAAGTGGCTTTTGGAATATACAGAAGAATATGAT
CAGATATTTGCTCCTAAGAAAAAACAAAAGAAGGTACAGGAGCAGGTGCACAAGGTAAGT
TCCCGCTGTGAAGAGGAAAGCCTTCTAGCCCGAGGTCGATCTAGTGCTCAGAACAAGCAG
GTGGACGAGAATTCTTTGATTTCAACCAAAGAAGAGCCTCCAGTTCTTGAAAGGGAGGCT
CCGTTTTTGGAGGGCCCCTTGGCTCAGTCAGAACTTGGAGGTGGACATGCTGAGTTGCCG
CAGCTGACCTTGTCTGTGCCTGTGGCTCCGGAAGTCTCTCCACGGCCTGCCCTTGAGTCT
GAGGAATTGCTAGTTAAAACGCCAGGAAATTATGAAAGTAAACGTCAAAGAAAACCAACT
AAGAAACTTCTTGAATCCAATGATTTAGACCCTGGATTTATGCCCAAGAAGGGGGACCTT
GGCCTTTCTAAAAAGTGCTATGAAGCTGGTCACCTGGAGAATGGCATAACTGAATCTTGT
GCCACATCTTATTCAAAAGATTTTGGTGGAGGCACTACCAAGATATTTGACAAGCCAAGG
AAGCGAAAACGACAGAGGCATGCTGCAGCCAAGATGCAGTGTAAAAAAGTGAAAAATGAT
GACTCGTCAAAAGAGATTCCAGGCTCAGAGGGAGAACTAATGCCTCACAGGACGGCCACA
AGCCCCAAGGAGACTGTTGAGGAAGGTGTAGAACACGATCCCGGGATGCCTGCCTCTAAA
AAAATGCAGGGTGAACGCGGTGGAGGAGCTGCACTCAAGGAGAATGTCTGTCAGAATTGT
GAAAAATTGGGTGAGCTGCTGTTATGTGAGGCTCAGTGCTGTGGGGCTTTCCACCTGGAG
TGCCTTGGATTGACTGAGATGCCAAGAGGAAAATTTATCTGCAATGAATGTCGCACAGGA
ATCCATACCTGTTTTGTATGTAAGCAGAGTGGGGAAGATGTTAAAAGGTGCCTTCTACCC
TTGTGTGGAAAGTTTTACCATGAAGAGTGTGTCCAGAAGTACCCACCCACTGTTATGCAG
AACAAGGGCTTCCGGTGCTCCCTCCACATCTGTATAACCTGTCATGCTGCTAATCCAGCC
AATGTTTCTGCATCTAAAGGTCGGTTGATGCGCTGTGTCCGCTGTCCTGTGGCATACCAC
GCCAATGACTTTTGCCTGGCTGCTGGGTCAAAGATCCTTGCATCTAATAGTATCATCTGC
CCTAATCACTTTACCCCTAGGCGGGGCTGCCGAAATCATGAGCATGTTAATGTTAGCTGG
TGCTTTGTGTGCTCAGAAGGAGGCAGCCTTCTGTGCTGTGATTCTTGCCCTGCTGCTTTT
CATCGTGAATGCCTGAACATTGATATCCCTGAAGGAAACTGGTATTGCAATGACTGTAAA
GCAGGCAAAAAGCCACACTACAGGGAGATTGTCTGGGTAAAAGTTGGACGATACAGGTGG
TGGCCAGCTGAGATCTGCCATCCTCGAGCTGTTCCTTCCAACATTGATAAGATGAGACAT
GATGTGGGAGAGTTCCCAGTCCTCTTTTTTGGATCTAATGACTATTTGTGGACTCACCAG
GCCCGAGTCTTCCCTTACATGGAGGGTGACGTGAGCAGCAAGGATAAGATGGGCAAAGGA
GTGGATGGGACATATAAAAAAGCTCTTCAGGAAGCTGCAGCAAGGTTTGAGGAATTAAAG
GCCCAAAAAGAGCTAAGACAGCTGCAGGAAGACCGAAAGAATGACAAGAAGCCACCACCT
TATAAACATATAAAGGTAAACCGTCCTATTGGCAGGGTACAGATCTTCACTGCAGACTTA
TCTGAAATACCCCGTTGCAACTGTAAAGCTACTGATGAGAACCCCTGTGGGATAGACTCT
GAATGCATCAACCGCATGCTGCTCTATGAGTGCCACCCCACAGTGTGTCCTGCCGGAGGG
CGCTGTCAAAACCAGTGCTTTTCCAAGCGCCAATATCCAGAGGTTGAAATTTTCCGCACA
TTACAGCGGGGTTGGGGTCTACGGACAAAAACAGATATTAAAAAGGGTGAATTTGTGAAT
GAGTATGTGGGTGAGCTTATAGATGAAGAAGAATGCAGAGCTCGAATTCGCTATGCTCAA
GAACATGATATCACTAATTTCTATATGCTCACCCTAGACAAAGACCGAATCATTGATGCT
GGTCCCAAAGGAAACTATGCTCGGTTCATGAATCATTGCTGCCAGCCCAACTGTGAAACA
CAGAAGTGGTCTGTGAATGGAGATACCCGTGTAGGCCTTTTTGCACTAAGTGACATTAAA
GCAGGCACTGAACTTACCTTCAACTACAACCTAGAATGTCTTGGGAATGGAAAGACTGTT
TGCAAATGTGGAGCCCCGAACTGCAGTGGCTTCTTGGGTGTAAGGCCAAAGAATCAACCC
ATTGCCACGGAAGAAAAGTCAAAGAAATTCAAGAAGAAGCAACAGGGAAAGCGCAGGACC
CAGGGTGAAATCACAAAGGAGCGAGAAGATGAGTGTTTTAGTTGTGGGGATGCTGGCCAG
CTCGTCTCCTGCAAGAAACCAGGCTGCCCAAAAGTTTACCACGCAGACTGTCTCAATCTG
ACCAAGCGACCAGCAGGGAAATGGGAATGTCCGTGGCATCAGTGTGACATCTGCGGGAAG
GAAGCAGCCTCCTTCTGTGAGATGTGCCCCAGCTCCTTTTGTAAGCAGCATCGAGAAGGG
ATGCTTTTCATTTCCAAACTGGATGGGCGTCTGTCTTGTACTGAGCATGACCCCTGTGGG
CCCAATCCTCTGGAACCTGGGGAGATCCGTGAGTATGTGCCTCCCCCAGTACCGCTGCCT
CCAGGGCCAAGCACTCACCTGGCAGAGCAATCAACAGGAATGGCTGCTCAGGCACCCAAA
ATGTCAGATAAACCTCCTGCTGACACCAACCAGATGCTGTCGCTCTCCAAAAAAGCTCTG
GCAGGGACTTGTCAGAGGCCACTGCTACCTGAAAGACCTCTTGAGAGAACTGACTCCAGG
CCCCAGCCTTTAGATAAGGTCAGAGACCTCGCTGGCTCAGGGACCAAATCCCAATCCTTG
GTTTCCAGCCAGAGGCCACTGGACAGGCCACCAGCAGTGGCAGGACCAAGACCCCAGCTA
AGCGACAAACCCTCTCCAGTGACCAGCCCAAGCTCCTCACCCTCAGTCAGGTCCCAACCA
CTGGAAAGACCTCTGGGGACGGCTGACCCAAGGCTGGATAAATCCATAGGTGCTGCCAGC
CCAAGGCCCCAGTCACTGGAGAAAACCTCAGTTCCCACTGGCCTGAGACTTCCGCCGCCA
GACAGACTGCTCATTACTAGCAGTCCCAAACCCCAGACTTCAGACAGGCCTACTGACAAA
CCCCATGCCTCTTTGTCCCAGAGACTCCCACCTCCTGAGAAAGTACTATCAGCTGTGGTC
CAGACCCTTGTAGCTAAAGAAAAAGCACTGAGGCCTGTGGACCAGAATACTCAGTCAAAA
AATAGAGCTGCTTTGGTGATGGATCTCATAGACCTAACTCCTCGCCAGAAGGAGCGGGCA
GCTTCACCTCATCAGGTCACACCACAGGCTGATGAGAAGATGCCAGTGTTGGAGTCAAGT
TCATGGCCTGCCAGCAAAGGTCTGGGGCATATGCCGAGAGCTGTTGAGAAAGGCTGTGTG
TCAGATCCTCTTCAGACATCTGGGAAAGCAGCAGCCCCTTCAGAGGACCCCTGGCAAGCT
GTTAAATCACTCACCCAGGCCAGACTTCTTTCTCAGCCTCCTGCCAAGGCCTTTTTATAT
GAGCCAACAACTCAGGCCTCAGGAAGAGCTTCTGCAGGGGCTGAGCAGACCCCAGGGCCT
CTTAGCCAATCCCCGGGCCTGGTGAAGCAGGCGAAGCAGATGGTCGGAGGCCAGCAACTA
CCTGCACTTGCCGCCAAGAGTGGGCAATCTTTTAGGTCTCTCGGGAAGGCCCCAGCCTCC
CTCCCCACTGAAGAAAAGAAGTTGGTAACCACAGAGCAAAGTCCCTGGGCCCTGGGAAAA
GCCTCATCACGGGCAGGGCTCTGGCCCATAGTGGCTGGACAGACACTGGCACAGTCTTGC
TGGTCTGCTGGGAGCACACAGACATTGGCACAGACTTGCTGGTCTCTTGGAAGAGGGCAA
GACCCCAAACCAGAGCAAAATACACTTCCAGCTCTTAACCAGGCTCCTTCCAGTCACAAG
TGTGCAGAATCAGAACAGAAGTAG
Enzyme 10 GenBank Gene ID AF380302 Link Image
Enzyme 10 GeneCard ID NSD1 Link Image
Enzyme 10 GenAtlas ID NSD1 Link Image
Enzyme 10 HGNC ID HGNC:14234 Link Image
Enzyme 10 Chromosome Location Not Available
Enzyme 10 Locus Not Available
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Wang X, Yeh S, Wu G, Hsu CL, Wang L, Chiang T, Yang Y, Guo Y, Chang C: Identification and characterization of a novel androgen receptor coregulator ARA267-alpha in prostate cancer cells. J Biol Chem. 2001 Nov 2;276(44):40417-23. Epub 2001 Aug 16. [PubMed Link Image]
  2. Kurotaki N, Harada N, Yoshiura K, Sugano S, Niikawa N, Matsumoto N: Molecular characterization of NSD1, a human homologue of the mouse Nsd1 gene. Gene. 2001 Nov 28;279(2):197-204. [PubMed Link Image]
  3. Jaju RJ, Fidler C, Haas OA, Strickson AJ, Watkins F, Clark K, Cross NC, Cheng JF, Aplan PD, Kearney L, Boultwood J, Wainscoat JS: A novel gene, NSD1, is fused to NUP98 in the t(5;11)(q35;p15.5) in de novo childhood acute myeloid leukemia. Blood. 2001 Aug 15;98(4):1264-7. [PubMed Link Image]
  4. Kurotaki N, Imaizumi K, Harada N, Masuno M, Kondoh T, Nagai T, Ohashi H, Naritomi K, Tsukahara M, Makita Y, Sugimoto T, Sonoda T, Hasegawa T, Chinen Y, Tomita Ha HA, Kinoshita A, Mizuguchi T, Yoshiura Ki K, Ohta T, Kishino T, Fukushima Y, Niikawa N, Matsumoto N: Haploinsufficiency of NSD1 causes Sotos syndrome. Nat Genet. 2002 Apr;30(4):365-6. Epub 2002 Mar 18. [PubMed Link Image]
  5. Douglas J, Hanks S, Temple IK, Davies S, Murray A, Upadhyaya M, Tomkins S, Hughes HE, Cole TR, Rahman N: NSD1 mutations are the major cause of Sotos syndrome and occur in some cases of Weaver syndrome but are rare in other overgrowth phenotypes. Am J Hum Genet. 2003 Jan;72(1):132-43. Epub 2002 Dec 2. [PubMed Link Image]
  6. Rio M, Clech L, Amiel J, Faivre L, Lyonnet S, Le Merrer M, Odent S, Lacombe D, Edery P, Brauner R, Raoul O, Gosset P, Prieur M, Vekemans M, Munnich A, Colleaux L, Cormier-Daire V: Spectrum of NSD1 mutations in Sotos and Weaver syndromes. J Med Genet. 2003 Jun;40(6):436-40. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5648
Enzyme 11 Name Histone-lysine N-methyltransferase SETDB1
Enzyme 11 Synonyms
  1. SET domain bifurcated 1
  2. ERG-associated protein with SET domain
  3. ESET
  4. Histone H3-K9 methyltransferase 4
  5. H3-K9-HMTase 4
Enzyme 11 Gene Name SETDB1
Enzyme 11 Protein Sequence >Histone-lysine N-methyltransferase SETDB1
MSSLPGCIGLDAATATVESEEIAELQQAVVEELGISMEELRHFIDEELEKMDCVQQRKKQ
LAELETWVIQKESEVAHVDQLFDDASRAVTNCESLVKDFYSKLGLQYRDSSSEDESSRPT
EIIEIPDEDDDVLSIDSGDAGSRTPKDQKLREAMAALRKSAQDVQKFMDAVNKKSSSQDL
HKGTLSQMSGELSKDGDLIVSMRILGKKRTKTWHKGTLIAIQTVGPGKKYKVKFDNKGKS
LLSGNHIAYDYHPPADKLYVGSRVVAKYKDGNQVWLYAGIVAETPNVKNKLRFLIFFDDG
YASYVTQSELYPICRPLKKTWEDIEDISCRDFIEEYVTAYPNRPMVLLKSGQLIKTEWEG
TWWKSRVEEVDGSLVRILFLDDKRCEWIYRGSTRLEPMFSMKTSSASALEKKQGQLRTRP
NMGAVRSKGPVVQYTQDLTGTGTQFKPVEPPQPTAPPAPPFPPAPPLSPQAGDSDLESQL
AQSRKQVAKKSTSFRPGSVGSGHSSPTSPALSENVSGGKPGINQTYRSPLGSTASAPAPS
ALPAPPAPPVFHGMLERAPAEPSYRAPMEKLFYLPHVCSYTCLSRVRPMRNEQYRGKNPL
LVPLLYDFRRMTARRRVNRKMGFHVIYKTPCGLCLRTMQEIERYLFETGCDFLFLEMFCL
DPYVLVDRKFQPYKPFYYILDITYGKEDVPLSCVNEIDTTPPPQVAYSKERIPGKGVFIN
TGPEFLVGCDCKDGCRDKSKCACHQLTIQATACTPGGQINPNSGYQYKRLEECLPTGVYE
CNKRCKCDPNMCTNRLVQHGLQVRLQLFKTQNKGWGIRCLDDIAKGSFVCIYAGKILTDD
FADKEGLEMGDEYFANLDHIESVENFKEGYESDAPCSSDSSGVDLKDQEDGNSGTEDPEE
SNDDSSDDNFCKDEDFSTSSVWRSYATRRQTRGQKENGLSETTSKDSHPPDLGPPHIPVP
PSIPVGGCNPPSSEETPKNKVASWLSCNSVSEGGFADSDSHSSFKTNEGGEGRAGGSRME
AEKASTSGLGIKDEGDIKQAKKEDTDDRNKMSVVTESSRNYGYNPSPVKPEGLRRPPSKT
SMHQSRRLMASAQSNPDDVLTLSSSTESEGESGTSRKPTAGQTSATAVDSDDIQTISSGS
EGDDFEDKKNMTGPMKRQVAVKSTRGFALKSTHGIAIKSTNMASVDKGESAPVRKNTRQF
YDGEESCYIIDAKLEGNLGRYLNHSCSPNLFVQNVFVDTHDLRFPWVAFFASKRIRAGTE
LTWDYNYEVGSVEGKELLCCCGAIECRGRLL
Enzyme 11 Number of Residues 1291
Enzyme 11 Molecular Weight 143158
Enzyme 11 Theoretical pI 5.84
Enzyme 11 GO Classification
Function
  • DNA binding
  • binding
  • catalytic activity
  • cation binding
  • histone-lysine N-methyltransferase activity
  • ion binding
  • methyltransferase activity
  • nucleic acid binding
  • protein methyltransferase activity
  • protein-lysine N-methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
  • transition metal ion binding
  • zinc ion binding
Process
  • DNA metabolism
  • DNA packaging
  • cellular metabolism
  • chromatin modification
  • establishment and/or maintenance of chromatin architecture
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 11 General Function Not Available
Enzyme 11 Specific Function Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. H3 'Lys-9' trimethylation is coordinated with DNA methylation. Probably forms a complex with MBD1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation. Its activity is dependent on MBD1 and is heritably maintained through DNA replication by being recruited by CAF-1. SETDB1 is targeted to histone H3 by TRIM28/TIF1B, a factor recruited by KRAB zinc-finger proteins
Enzyme 11 Pathways
Enzyme 11 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 40789075 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q15047 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name SETB1_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >3903 bp
AGCTGGAAGACGGGAGAGGACAAAAGCATGTCTTCCCTTCCTGGGTGCATTGGTTTGGAT
GCAGCAACAGCTACAGTGGAGTCTGAAGAGATTGCAGAGCTGCAACAGGCAGTGGTTGAG
GAACTGGGTATCTCTATGGAGGAACTTCGGCATTTCATCGATGAGGAACTGGAGAAGATG
GATTGTGTACAGCAACGCAAGAAGCAGCTAGCAGAGTTAGAGACATGGGTAATACAGAAA
GAATCTGAGGTGGCTCACGTTGACCAACTCTTTGATGATGCATCCAGGGCAGTGACTAAT
TGTGAGTCTTTGGTGAAGGACTTCTACTCCAAGCTGGGACTACAATACCGGGACAGTAGC
TCTGAGGACGAATCTTCCCGGCCTACAGAAATAATTGAGATTCCTGATGAAGATGATGAT
GTCCTCAGTATTGATTCAGGTGATGCTGGGAGCAGAACTCCAAAAGACCAGAAGCTCCGT
GAAGCTATGGCTGCCTTAAGAAAGTCAGCTCAAGATGTTCAGAAGTTCATGGATGCTGTC
AACAAGAAGAGCAGTTCCCAGGATCTGCATAAAGGAACCTTGAGTCAGATGTCTGGAGAA
CTAAGCAAAGATGGTGACCTGATAGTCAGCATGCGAATTCTGGGCAAGAAGAGAACTAAG
ACTTGGCACAAAGGCACCCTTATTGCCATCCAGACAGTTGGGCCAGGGAAGAAATACAAG
GTGAAATTTGACAACAAAGGAAAGAGTCTACTGTCGGGGAACCATATTGCCTATGATTAC
CACCCTCCTGCTGACAAGCTGTATGTGGGCAGTCGGGTGGTCGCCAAATACAAAGATGGG
AATCAGGTCTGGCTCTATGCTGGCATTGTAGCTGAGACACCAAACGTCAAAAACAAGCTC
AGGTTTCTCATTTTCTTTGATGATGGCTATGCTTCCTATGTCACACAGTCGGAACTGTAT
CCCATTTGCCGGCCACTGAAAAAGACTTGGGAGGACATAGAAGACATCTCCTGCCGTGAC
TTCATAGAGGAGTATGTCACTGCCTACCCCAACCGCCCCATGGTACTGCTCAAGAGTGGC
CAGCTTATCAAGACTGAGTGGGAAGGCACGTGGTGGAAGTCCCGAGTTGAGGAGGTGGAT
GGCAGCCTAGTCAGGATCCTCTTCCTGGATGACAAAAGATGTGAGTGGATCTATCGAGGC
TCTACACGGCTGGAGCCCATGTTCAGCATGAAAACATCCTCAGCCTCTGCACTGGAGAAG
AAGCAAGGACAGCTCAGGACACGTCCAAATATGGGTGCTGTGAGGAGCAAAGGCCCTGTT
GTCCAGTACACACAGGATCTGACCGGTACTGGAACCCAGTTCAAGCCAGTGGAACCCCCA
CAGCCTACAGCTCCACCTGCCCCACCTTTCCCACCTGCTCCACCTCTATCCCCCCAAGCA
GGTGACAGTGACTTGGAAAGCCAGCTTGCCCAGTCACGGAAGCAGGTAGCCAAAAAGAGC
ACGTCCTTTCGACCAGGATCTGTGGGCTCTGGTCATTCCTCCCCTACATCTCCTGCACTC
AGTGAAAATGTCTCTGGTGGGAAACCTGGGATCAACCAGACATATAGATCACCTTTAGGC
TCCACAGCCTCTGCCCCAGCACCCTCAGCACTCCCGGCCCCTCCAGCACCCCCAGTCTTC
CATGGCATGCTGGAGCGGGCCCCAGCAGAGCCCTCCTACCGTGCTCCCATGGAGAAGCTT
TTCTACTTACCTCATGTCTGCAGCTATACCTGTCTGTCTCGAGTCAGACCTATGAGGAAT
GAGCAGTACCGGGGCAAGAACCCTCTGCTGGTCCCGTTACTATATGACTTCCGGCGGATG
ACAGCCCGGCGTCGAGTTAACCGCAAGATGGGCTTTCATGTTATCTATAAGACACCTTGT
GGTCTCTGCCTTCGGACAATGCAGGAGATAGAACGCTACCTTTTCGAGACTGGCTGTGAC
TTCCTCTTCCTGGAGATGTTCTGTTTGGATCCATATGTTCTTGTGGACCGAAAGTTTCAG
CCCTATAAGCCTTTTTACTATATTTTGGACATCACTTATGGGAAGGAAGATGTTCCCCTA
TCCTGTGTCAATGAGATTGACACAACCCCTCCACCCCAGGTGGCCTACAGCAAGGAACGT
ATCCCGGGCAAGGGTGTTTTCATTAACACAGGCCCTGAATTTCTGGTTGGCTGTGACTGC
AAGGATGGGTGTCGGGACAAGTCCAAGTGTGCCTGCCATCAACTAACTATCCAGGCTACA
GCCTGTACCCCAGGAGGCCAAATCAACCCTAACTCTGGCTACCAGTACAAGAGACTAGAA
GAGTGTCTACCCACAGGGGTATATGAGTGTAACAAACGCTGCAAATGTGACCCAAACATG
TGCACAAACCGGTTGGTGCAACATGGACTACAAGTTCGGCTACAGCTATTCAAGACACAG
AACAAGGGCTGGGGTATCCGCTGCTTGGATGACATTGCCAAAGGCTCTTTTGTTTGTATT
TATGCAGGCAAAATCCTGACAGATGACTTTGCAGACAAGGAGGGTCTGGAAATGGGTGAT
GAGTACTTTGCAAATCTGGACCATATCGAGAGCGTGGAGAACTTCAAAGAAGGATATGAG
AGTGATGCCCCCTGTTCCTCTGACAGCAGTGGTGTAGACTTGAAGGACCAGGAAGATGGC
AACAGCGGTACAGAGGACCCTGAAGAGTCCAATGATGATAGCTCAGATGATAACTTCTGT
AAGGATGAGGACTTCAGCACCAGTTCAGTGTGGCGGAGCTATGCTACCCGGAGGCAGACC
CGGGGCCAGAAAGAGAACGGACTCTCTGAGACAACTTCCAAGGACTCCCACCCCCCAGAT
CTTGGACCCCCACATATTCCTGTTCCTCCCTCAATCCCTGTAGGTGGCTGCAATCCACCT
TCCTCCGAAGAGACACCCAAGAACAAGGTGGCCTCATGGTTGAGCTGCAATAGTGTCAGT
GAAGGTGGTTTTGCTGACTCTGATAGCCATTCATCCTTCAAGACTAATGAAGGTGGGGAG
GGCCGGGCTGGGGGAAGCCGAATGGAGGCTGAGAAGGCCTCCACCTCAGGACTAGGCATC
AAGGATGAGGGAGACATCAAACAGGCCAAGAAAGAGGACACTGACGACCGAAACAAGATG
TCAGTAGTTACTGAAAGCTCTCGAAATTACGGTTACAATCCTTCTCCTGTGAAGCCTGAA
GGACTTCGCCGCCCACCTAGTAAGACTAGTATGCATCAAAGCCGAAGACTCATGGCTTCT
GCTCAGTCCAACCCTGATGATGTCCTGACACTGTCCAGCAGCACAGAAAGTGAGGGGGAA
AGTGGGACCAGCCGAAAGCCCACTGCTGGTCAGACTTCGGCTACAGCGGTTGACAGTGAT
GATATCCAGACCATATCCTCTGGCTCTGAAGGGGATGACTTTGAGGACAAGAAGAACATG
ACTGGTCCAATGAAGCGTCAAGTGGCAGTAAAATCAACCCGAGGCTTTGCTCTTAAATCA
ACCCATGGGATTGCAATTAAATCAACCAACATGGCCTCTGTGGACAAGGGGGAGAGCGCA
CCTGTTCGTAAGAACACACGCCAATTCTATGATGGCGAGGAGTCTTGCTACATCATTGAT
GCCAAGCTTGAAGGCAACCTGGGCCGCTACCTCAACCACAGTTGCAGCCCCAACCTGTTT
GTCCAGAATGTCTTCGTGGATACCCATGATCTTCGCTTCCCCTGGGTGGCCTTCTTTGCC
AGCAAAAGAATCCGGGCTGGGACAGAACTTACTTGGGACTACAACTACGAGGTGGGCAGT
GTGGAAGGCAAGGAGCTACTCTGTTGCTGTGGGGCCATTGAATGCAGAGGACGTCTTCTT
TAG
Enzyme 11 GenBank Gene ID D31891 Link Image
Enzyme 11 GeneCard ID SETDB1 Link Image
Enzyme 11 GenAtlas ID SETDB1 Link Image
Enzyme 11 HGNC ID HGNC:10761 Link Image
Enzyme 11 Chromosome Location Not Available
Enzyme 11 Locus Not Available
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Nomura N, Nagase T, Miyajima N, Sazuka T, Tanaka A, Sato S, Seki N, Kawarabayasi Y, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1994;1(5):223-9. [PubMed Link Image]
  2. Schultz DC, Ayyanathan K, Negorev D, Maul GG, Rauscher FJ 3rd: SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-finger proteins. Genes Dev. 2002 Apr 15;16(8):919-32. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5651
Enzyme 12 Name Protein-S-isoprenylcysteine O-methyltransferase
Enzyme 12 Synonyms
  1. Isoprenylcysteine carboxylmethyltransferase
  2. Prenylcysteine carboxyl methyltransferase
  3. pcCMT
  4. Prenylated protein carboxyl methyltransferase
  5. PPMT
Enzyme 12 Gene Name ICMT
Enzyme 12 Protein Sequence >Protein-S-isoprenylcysteine O-methyltransferase
MAGCAARAPPGSEARLSLATFLLGASVLALPLLTRAGLQGRTGLALYVAGLNALLLLLYR
PPRYQIAIRACFLGFVFGCGTLLSFSQSSWSHFGWYMCSLSLFHYSEYLVTAVNNPKSLS
LDSFLLNHSLEYTVAALSSWLEFTLENIFWPELKQITWLSVTGLLMVVFGECLRKAAMFT
AGSNFNHVVQNEKSDTHTLVTSGVYAWFRHPSYVGWFYWSIGTQVMLCNPICGVSYALTV
WRFFRDRTEEEEISLIHFFGEEYLEYKKRVPTGLPFIKGVKVDL
Enzyme 12 Number of Residues 284
Enzyme 12 Molecular Weight 31938
Enzyme 12 Theoretical pI 8.05
Enzyme 12 GO Classification
Function
  • O-methyltransferase activity
  • catalytic activity
  • methyltransferase activity
  • protein-S-isoprenylcysteine O-methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • C-terminal protein amino acid methylation
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid alkylation
  • protein amino acid methylation
  • protein modification
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 12 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 12 Specific Function Catalyzes the posttranslational methylation of isoprenylated C-terminal cysteine residues
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions
  • S-adenosyl-L-methionine + protein C-terminal S-farnesyl-L-cysteine = S-adenosyl-L-homocysteine + protein C-terminal S-farnesyl-L-cysteine methyl ester
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • 1-29
Enzyme 12 Transmembrane Regions Not Available
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 3135669 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID O60725 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name ICMT_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >855 bp
ATGGCGGGCTGCGCGGCGCGGGCTCCGCCGGGCTCTGAGGCGCGTCTCAGCCTCGCCACC
TTCCTGCTGGGCGCCTCGGTGCTCGCGCTGCCGCTGCTCACGCGCGCCGGCCTGCAGGGC
CGCACCGGGCTGGCGCTCTACGTGGCCGGGCTCAACGCGCTGCTGCTGCTGCTCTATCGG
CCGCCTCGCTACCAGATAGCCATCCGAGCTTGTTTCCTGGGGTTTGTGTTCGGCTGCGGC
ACGCTGCTAAGTTTTAGCCAGTCTTCTTGGAGTCACTTTGGCTGGTACATGTGCTCCCTG
TCATTGTTCCACTATTCTGAATACTTGGTGACAGCAGTCAATAATCCCAAAAGTCTGTCC
TTGGATTCCTTTCTCCTGAATCACAGCCTGGAGTATACAGTAGCTGCTCTTTCTTCTTGG
TTAGAGTTCACACTTGAAAATATCTTTTGGCCAGAACTGAAGCAGATTACCTGGCTCAGT
GTCACAGGGCTGCTGATGGTGGTCTTCGGAGAATGTCTGAGGAAGGCGGCCATGTTTACA
GCTGGCTCCAATTTCAACCACGTGGTACAGAATGAAAAATCAGATACACATACTCTGGTG
ACCAGTGGAGTGTACGCTTGGTTTCGGCATCCTTCTTACGTCGGGTGGTTTTACTGGAGT
ATTGGAACTCAGGTGATGCTGTGTAACCCCATCTGCGGCGTCAGCTATGCCCTGACAGTG
TGGCGATTCTTCCGCGATCGAACAGAAGAAGAAGAAATCTCACTAATTCACTTTTTTGGA
GAGGAGTACCTGGAGTATAAGAAGAGGGTGCCCACGGGCCTGCCTTTCATAAAGGGGGTC
AAGGTGGACCTGTGA
Enzyme 12 GenBank Gene ID AF064084 Link Image
Enzyme 12 GeneCard ID ICMT Link Image
Enzyme 12 GenAtlas ID ICMT Link Image
Enzyme 12 HGNC ID HGNC:5350 Link Image
Enzyme 12 Chromosome Location Not Available
Enzyme 12 Locus Not Available
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Dai Q, Choy E, Chiu V, Romano J, Slivka SR, Steitz SA, Michaelis S, Philips MR: Mammalian prenylcysteine carboxyl methyltransferase is in the endoplasmic reticulum. J Biol Chem. 1998 Jun 12;273(24):15030-4. [PubMed Link Image]
  2. Lin X, Antalffy B, Kang D, Orr HT, Zoghbi HY: Polyglutamine expansion down-regulates specific neuronal genes before pathologic changes in SCA1. Nat Neurosci. 2000 Feb;3(2):157-63. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5652
Enzyme 13 Name Indolethylamine N-methyltransferase
Enzyme 13 Synonyms
  1. Aromatic alkylamine N-methyltransferase
  2. Indolamine N-methyltransferase
  3. Arylamine N- methyltransferase
  4. Amine N-methyltransferase
Enzyme 13 Gene Name INMT
Enzyme 13 Protein Sequence >Indolethylamine N-methyltransferase
MKGGFTGGDEYQKHFLPRDYLATYYSFDGSPSPEAEMLKFNLECLHKTFGPGGLQGDTLI
DIGSGPTIYQVLAACDSFQDITLSDFTDRNREELEKWLKKEPGAYDWTPAVKFACELEGN
SGRWEEKEEKLRAAVKRVLKCDVHLGNPLAPAVLPLADCVLTLLAMECACCSLDAYRAAL
CNLASLLKPGGHLVTTVTLRLPSYVVGKREFSCVALEKEEVEQAVLDAGFDIEQLLHSPQ
SYSVTNAANNGVCCIVARKKPGP
Enzyme 13 Number of Residues 263
Enzyme 13 Molecular Weight 28815
Enzyme 13 Theoretical pI 4.92
Enzyme 13 GO Classification
Function
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
Component
Enzyme 13 General Function Not Available
Enzyme 13 Specific Function Catalyzes the N-methylation of tryptamine and structurally related compounds (Potential)
Enzyme 13 Pathways
Enzyme 13 Reactions
  • S-adenosyl-L-methionine + an amine = S-adenosyl-L-homocysteine + a methylated amine
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 6580815 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID O95050 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name INMT_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >792 bp
ATGAAGGGTGGCTTCACTGGGGGTGATGAGTACCAGAAGCACTTCCTGCCCAGGGACTAC
TTGGCTACTTACTACAGCTTCGATGGCAGCCCCTCACCCGAGGCCGAGATGCTGAAGTTT
AACTTGGAATGTCTCCACAAGACCTTCGGCCCTGGAGGCCTCCAAGGGGACACGCTGATT
GACATTGGCTCAGGTCCTACCATCTACCAAGTTCTTGCTGCCTGTGATTCCTTCCAAGAC
ATCACTCTCTCCGACTTTACCGACCGCAACCGGGAGGAGCTGGAAAAGTGGCTGAAGAAG
GAGCCGGGGGCCTATGACTGGACCCCAGCGGTGAAATTCGCCTGTGAGCTGGAAGGAAAC
AGCGGCCGATGGGAGGAGAAGGAGGAGAAGCTGCGGGCAGCGGTGAAGCGGGTGCTCAAG
TGCGATGTCCACCTGGGCAACCCGCTGGCCCCGGCTGTGTTGCCTCTCGCCGACTGTGTG
CTCACCCTGCTGGCCATGGAGTGTGCCTGCTGTAGCCTTGATGCCTACCGCGCTGCCCTG
TGCAACCTTGCCTCACTGCTCAAGCCGGGTGGCCACCTGGTGACCACTGTCACGCTTCGG
CTCCCGTCCTACGTGGTGGGGAAGCGTGAATTTTCCTGCGTGGCCCTGGAGAAAGAGGAG
GTGGAGCAGGCTGTCCTGGATGCTGGCTTTGACATTGAACAGCTCCTACACAGTCCCCAG
AGCTACTCTGTCACCAATGCTGCCAACAATGGGGTCTGCTGCATTGTGGCTCGCAAGAAG
CCTGGGCCCTGA
Enzyme 13 GenBank Gene ID AF128846 Link Image
Enzyme 13 GeneCard ID INMT Link Image
Enzyme 13 GenAtlas ID INMT Link Image
Enzyme 13 HGNC ID HGNC:6069 Link Image
Enzyme 13 Chromosome Location Not Available
Enzyme 13 Locus Not Available
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Thompson MA, Moon E, Kim UJ, Xu J, Siciliano MJ, Weinshilboum RM: Human indolethylamine N-methyltransferase: cDNA cloning and expression, gene cloning, and chromosomal localization. Genomics. 1999 Nov 1;61(3):285-97. [PubMed Link Image]
  2. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5653
Enzyme 14 Name DNA
Enzyme 14 Synonyms
  1. cytosine-5-methyltransferase 3A
  2. Dnmt3a
  3. DNA methyltransferase HsaIIIA
  4. DNA MTase HsaIIIA
  5. M.HsaIIIA
Enzyme 14 Gene Name DNMT3A
Enzyme 14 Protein Sequence >DNA
MPSSGPGDTSSSAAEREEDRKDGEEQEEPRGKEERQEPSTTARKVGRPGRKRKHPPVESG
DTPKDPAVISKSPSMAQDSGASELLPNGDLEKRSEPQPEEGSPAGGQKGGAPAEGEGAAE
TLPEASRAVENGCCTPKEGRGAPAEAGKEQKETNIESMKMEGSRGRLRGGLGWESSLRQR
PMPRLTFQAGDPYYISKRKRDEWLARWKREAEKKAKVIAGMNAVEENQGPGESQKVEEAS
PPAVQQPTDPASPTVATTPEPVGSDAGDKNATKAGDDEPEYEDGRGFGIGELVWGKLRGF
SWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNKQP
MYRKAIYEVLQVASSRAGKLFPVCHDSDESDTAKAVEVQNKPMIEWALGGFQPSGPKGLE
PPEEEKNPYKEVYTDMWVEPEAAAYAPPPPAKKPRKSTAEKPKVKEIIDERTRERLVYEV
RQKCRNIEDICISCGSLNVTLEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGG
REVLMCGNNNCCRCFCVECVDLLVGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPS
RLQMFFANNHDQEFDPPKVYPPVPAEKRKPIRVLSLFDGIATGLLVLKDLGIQVDRYIAS
EVCEDSITVGMVRHQGKIMYVGDVRSVTQKHIQEWGPFDLVIGGSPCNDLSIVNPARKGL
YEGTGRLFFEFYRLLHDARPKEGDDRPFFWLFENVVAMGVSDKRDISRFLESNPVMIDAK
EVSAAHRARYFWGNLPGMNRPLASTVNDKLELQECLEHGRIAKFSKVRTITTRSNSIKQG
KDQHFPVFMNEKEDILWCTEMERVFGFPVHYTDVSNMSRLARQRLLGRSWSVPVIRHLFA
PLKEYFACV
Enzyme 14 Number of Residues 909
Enzyme 14 Molecular Weight 101560
Enzyme 14 Theoretical pI 6.52
Enzyme 14 GO Classification
Function
  • DNA binding
  • binding
  • nucleic acid binding
Process
  • DNA alkylation
  • DNA metabolism
  • DNA methylation
  • DNA modification
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
Enzyme 14 General Function Not Available
Enzyme 14 Specific Function Required for genome wide de novo methylation and is essential for development. DNA methylation is coordinated with methylation of histones
Enzyme 14 Pathways
Enzyme 14 Reactions
  • S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 12746532 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID Q9Y6K1 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name DNM3A_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >2739 bp
ATGCCCGCCATGCCCTCCAGCGGCCCCGGGGACACCAGCAGCTCTGCTGCGGAGCGGGAG
GAGGACCGAAAGGACGGAGAGGAGCAGGAGGAGCCGCGTGGCAAGGAGGAGCGCCAAGAG
CCCAGCACCACGGCACGGAAGGTGGGGCGGCCTGGGAGGAAGCGCAAGCACCCCCCGGTG
GAAAGCGGTGACACGCCAAAGGACCCTGCGGTGATCTCCAAGTCCCCATCCATGGCCCAG
GACTCAGGCGCCTCAGAGCTATTACCCAATGGGGACTTGGAGAAGCGGAGTGAGCCCCAG
CCAGAGGAGGGGAGCCCTGCTGGGGGGCAGAAGGGCGGGGCCCCAGCAGAGGGAGAGGGT
GCAGCTGAGACCCTGCCTGAAGCCTCAAGAGCAGTGGAAAATGGCTGCTGCACCCCCAAG
GAGGGCCGAGGAGCCCCTGCAGAAGCGGGCAAAGAACAGAAGGAGACCAACATCGAATCC
ATGAAAATGGAGGGCTCCCGGGGCCGGCTGCGGGGTGGCTTGGGCTGGGAGTCCAGCCTC
CGTCAGCGGCCCATGCCGAGGCTCACCTTCCAGGCGGGGGACCCCTACTACATCAGCAAG
CGCAAGCGGGACGAGTGGCTGGCACGCTGGAAAAGGGAGGCTGAGAAGAAAGCCAAGGTC
ATTGCAGGAATGAATGCTGTGGAAGAAAACCAGGGGCCCGGGGAGTCTCAGAAGGTGGAG
GAGGCCAGCCCTCCTGCTGTGCAGCAGCCCACTGACCCCGCATCCCCCACTGTGGCTACC
ACGCCTGAGCCCGTGGGGTCCGATGCTGGGGACAAGAATGCCACCAAAGCAGGCGATGAC
GAGCCAGAGTACGAGGACGGCCGGGGCTTTGGCATTGGGGAGCTGGTGTGGGGGAAACTG
CGGGGCTTCTCCTGGTGGCCAGGCCGCATTGTGTCTTGGTGGATGACGGGCCGGAGCCGA
GCAGCTGAAGGCACCCGCTGGGTCATGTGGTTCGGAGACGGCAAATTCTCAGTGGTGTGT
GTTGAGAAGCTGATGCCGCTGAGCTCGTTTTGCAGTGCGTTCCACCAGGCCACGTACAAC
AAGCAGCCCATGTACCGCAAAGCCATCTACGAGGTCCTGCAGGTGGCCAGCAGCCGCGCG
GGGAAGCTGTTCCCGGTGTGCCACGACAGCGATGAGAGTGACACTGCCAAGGCCGTGGAG
GTGCAGAACAAGCCCATGATTGAATGGGCCCTGGGGGGCTTCCAGCCTTCTGGCCCTAAG
GGCCTGGAGCCACCAGAAGAAGAGAAGAATCCCTACAAAGAAGTGTACACGGACATGTGG
GTGGAACCTGAGGCAGCTGCCTACGCACCACCTCCACCAGCCAAAAAGCCCCGGAAGAGC
ACAGCGGAGAAGCCCAAGGTCAAGGAGATTATTGATGAGCGCACAAGAGAGCGGCTGGTG
TACGAGGTGCGGCAGAAGTGCCGGAACATTGAGGACATCTGCATCTCCTGTGGGAGCCTC
AATGTTACCCTGGAACACCCCCTCTTCGTTGGAGGAATGTGCCAAAACTGCAAGAACTGC
TTTCTGGAGTGTGCGTACCAGTACGACGACGACGGCTACCAGTCCTACTGCACCATCTGC
TGTGGGGGCCGTGAGGTGCTCATGTGCGGAAACAACAACTGCTGCAGGTGCTTTTGCGTG
GAGTGTGTGGACCTCTTGGTGGGGCCGGGGGCTGCCCAGGCAGCCATTAAGGAAGACCCC
TGGAACTGCTACATGTGCGGGCACAAGGGTACCTACGGGCTGCTGCGGCGGCGAGAGGAC
TGGCCCTCCCGGCTCCAGATGTTCTTCGCTAATAACCACGACCAGGAATTTGACCCTCCA
AAGGTTTACCCACCTGTCCCAGCTGAGAAGAGGAAGCCCATCCGGGTGCTGTCTCTCTTT
GATGGAATCGCTACAGGGCTCCTGGTGCTGAAGGACTTGGGCATTCAGGTGGACCGCTAC
ATTGCCTCGGAGGTGTGTGAGGACTCCATCACGGTGGGCATGGTGCGGCACCAGGGGAAG
ATCATGTACGTCGGGGACGTCCGCAGCGTCACACAGAAGCATATCCAGGAGTGGGGCCCA
TTCGATCTGGTGATTGGGGGCAGTCCCTGCAATGACCTCTCCATCGTCAACCCTGCTCGC
AAGGGCCTCTACGAGGGCACTGGCCGGCTCTTCTTTGAGTTCTACCGCCTCCTGCATGAT
GCGCGGCCCAAGGAGGGAGATGATCGCCCCTTCTTCTGGCTCTTTGAGAATGTGGTGGCC
ATGGGCGTTAGTGACAAGAGGGACATCTCGCGATTTCTCGAGTCCAACCCTGTGATGATT
GATGCCAAAGAAGTGTCAGCTGCACACAGGGCCCGCTACTTCTGGGGTAACCTTCCCGGT
ATGAACAGGCCGTTGGCATCCACTGTGAATGATAAGCTGGAGCTGCAGGAGTGTCTGGAG
CATGGCAGGATAGCCAAGTTCAGCAAAGTGAGGACCATTACTACGAGGTCAAACTCCATA
AAGCAGGGCAAAGACCAGCATTTTCCTGTCTTCATGAATGAGAAAGAGGACATCTTATGG
TGCACTGAAATGGAAAGGGTATTTGGTTTCCCAGTCCACTATACTGACGTCTCCAACATG
AGCCGCTTGGCGAGGCAGAGACTGCTGGGCCGGTCATGGAGCGTGCCAGTCATCCGCCAC
CTCTTCGCTCCGCTGAAGGAGTATTTTGCGTGTGTGTAA
Enzyme 14 GenBank Gene ID AF067972 Link Image
Enzyme 14 GeneCard ID DNMT3A Link Image
Enzyme 14 GenAtlas ID DNMT3A Link Image
Enzyme 14 HGNC ID HGNC:2978 Link Image
Enzyme 14 Chromosome Location Not Available
Enzyme 14 Locus Not Available
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Xie S, Wang Z, Okano M, Nogami M, Li Y, He WW, Okumura K, Li E: Cloning, expression and chromosome locations of the human DNMT3 gene family. Gene. 1999 Aug 5;236(1):87-95. [PubMed Link Image]
  2. Robertson KD, Uzvolgyi E, Liang G, Talmadge C, Sumegi J, Gonzales FA, Jones PA: The human DNA methyltransferases (DNMTs) 1, 3a and 3b: coordinate mRNA expression in normal tissues and overexpression in tumors. Nucleic Acids Res. 1999 Jun 1;27(11):2291-8. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 5654
Enzyme 15 Name Hexaprenyldihydroxybenzoate methyltransferase, mitochondrial precursor
Enzyme 15 Synonyms
  1. Dihydroxyhexaprenylbenzoate methyltransferase
  2. 3,4- dihydroxy-5-hexaprenylbenzoate methyltransferase
  3. DHHB methyltransferase
  4. DHHB-MT
  5. DHHB-MTase
Enzyme 15 Gene Name COQ3
Enzyme 15 Protein Sequence >Hexaprenyldihydroxybenzoate methyltransferase, mitochondrial precursor
MWSGRKLGSSGGWFLRVLGPGGCNTKAARPLISSAVYVKNQLSGTLQIKPGVFNEYRTIW
FKSYRTIFSCLNRIKSFRYPWARLYSTSQTTVDSGEVKTFLALAHKWWDEQGVYAPLHSM
NDLRVPFIRDNLLKTIPNHQPGKPLLGMKILDVGCGGGLLTEPLGRLGASVIGIDPVDEN
IKTAQCHKSFDPVLDKRIEYRVCSLEEIVEETAETFDAVVASEVVEHVIDLETFLQCCCQ
VLKPGGSLFITTINKTQLSYALGIVFSEQIAGIVPKGTHTWEKFVSPETLESILESNGLS
VQTVVGMLYNPFSGYWHWSENTSLNYAAHAVKSRVQEHPASAEFVLKGETEELQANACTN
PAVHEKLKK
Enzyme 15 Number of Residues 369
Enzyme 15 Molecular Weight 40998
Enzyme 15 Theoretical pI 7.50
Enzyme 15 GO Classification
Function
  • 2-polyprenyl-6-methoxy-1,4-benzoquinone methyltransferase activity
  • C-methyltransferase activity
  • catalytic activity
  • methyltransferase activity
  • quinone cofactor methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • cellular metabolism
  • coenzyme metabolism
  • cofactor metabolism
  • metabolism
  • oxidoreduction coenzyme metabolism
  • physiological process
  • ubiquinone biosynthesis
  • ubiquinone metabolism
Component
Enzyme 15 General Function Coenzyme transport and metabolism
Enzyme 15 Specific Function S-adenosyl-L-methionine + 3-hexaprenyl-4,5- dihydroxybenzoate = S-adenosyl-L-homocysteine + 3-hexaprenyl-4- hydroxy-5-methoxybenzoate
Enzyme 15 Pathways
Enzyme 15 Reactions
  • S-adenosyl-L-methionine + 3-hexaprenyl-4,5-dihydroxybenzoate = S-adenosyl-L-homocysteine + 3-hexaprenyl-4-hydroxy-5-methoxybenzoate
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 25990404 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID Q9NZJ6 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name COQ3_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >1110 bp
ATGTGGAGTGGCCGTAAGCTGGGCTCCTCCGGGGGTTGGTTTTTAAGAGTGCTGGGGCCT
GGAGGCTGTAATACAAAAGCTGCGCGTCCCTTAATTTCCTCGGCGGTTTATGTGAAGAAC
CAGCTCAGTGGGACTCTACAGATTAAACCAGGGGTTTTCAATGAATACAGAACCATATGG
TTCAAATCCTACAGGACGATCTTTTCCTGTTTGAACAGAATAAAGAGTTTCAGGTACCCT
TGGGCGAGACTGTACAGTACTTCCCAAACCACTGTCGACAGCGGTGAGGTAAAAACCTTC
TTGGCCCTGGCTCACAAATGGTGGGATGAACAAGGAGTATATGCACCTCTTCATTCCATG
AATGACCTGAGGGTGCCATTTATTAGGGACAATCTTCTGGAAACAATTCCTAATCACCAG
CCAGGAAAACCTTTGTTGGGGATGAAGATTCTTGACGTTGGCTGTGGTGGTGGGCTGTTA
ACTGAACCTCTAGGCCGGCTTGGGGCTTCAGTTATTGGAATCGACCCTGTGGATGAGAAC
ATTAAAACAGCACAATGCCATAAATCATTTGATCCAGTCCTGGATAAGAGAATAGAGTAC
AGAGTGTGTTCCCTGGAAGAGATTGTGGAAGAGACTGCAGAAACATTTGATGCTGTTGTA
GCTTCTGAAGTTGTAGAACATGTGATTGATCTAGAAACATTTTTACAGTGCTGCTGTCAA
GTGTTAAAACCCGGTGGTTCTTTATTCATTACTACAATCAACAAAACACAACTTTCCTAT
GCCTTGGGAATTGTTTTTTCAGAGCAAATTGCAGGTATTGTACCAAAAGGTACTCATACA
TGGGAGAAGTTTGTTTCACTTGAACCACTAGAGAGCATTCTGGAATCAAATGGTCTGTCA
GTTCAAACAGTGGTAGGAATGCTCTATAACCCCTTCTCAGGTTACTGGCATTGGAGTGAA
GATACCAGCCTTAACTATGCAGCTCATGCTGTGAAATCCAGGGTCCAGGAACACCCAGCC
TCTGCTGAGTTTGTTTTAAAGGGAGAAACAGAAGAGCTCCAAGCTAATGCCTGCACCAAT
CCAGCTGTGCATGAAAAGCTGAAGAAATGA
Enzyme 15 GenBank Gene ID AF351615 Link Image
Enzyme 15 GeneCard ID COQ3 Link Image
Enzyme 15 GenAtlas ID COQ3 Link Image
Enzyme 15 HGNC ID HGNC:18175 Link Image
Enzyme 15 Chromosome Location 6
Enzyme 15 Locus 6q16.3
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  2. Jonassen T, Clarke CF: Isolation and functional expression of human COQ3, a gene encoding a methyltransferase required for ubiquinone biosynthesis. J Biol Chem. 2000 Apr 28;275(17):12381-7. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 5658
Enzyme 16 Name Methionine synthase reductase, mitochondrial precursor
Enzyme 16 Synonyms
  1. MSR
Enzyme 16 Gene Name MTRR
Enzyme 16 Protein Sequence >Methionine synthase reductase, mitochondrial precursor
MGAASVRAGARLVEVALCSFTVTCLEVMRRFLLLYATQQGQAKAIAEEICEQAVVHGFSA
DLHCISESDKYDLKTETAPLVVVVSTTGTGDPPDTARKFVKEIQNQTLPVDFFAHLRYGL
LGLGDSEYTYFCNGGKIIDKRLQELGARHFYDTGHADDCVGLELVVEPWIAGLWPALRKH
FRSSRGQEEISGALPVASPASLRTDLVKSELLHIESQVELLRFDDSGRKDSEVLKQNAVN
SNQSNVVIEDFESSLTRSVPPLSQASLNIPGLPPEYLQVHLQESLGQEESQVSVTSADPV
FQVPISKAVQLTTNDAIKTTLLVELDISNTDFSYQPGDAFSVICPNSDSEVQSLLQRLQL
EDKREHCVLLKIKADTKKKGATLPQHIPAGCSLQFIFTWCLEIRAIPKKAFLRALVDYTS
DSAEKRRLQELCSKQGAADYSRFVRDACACLLDLLLAFPSCQPPLSLLLEHLPKLQPRPY
SCASSSLFHPGKLHFVFNIVEFLSTATTEVLRKGVCTGWLALLVASVLQPNIHASHEDSG
KALAPKISISPRTTNSFHLPDDPSIPIIMVGPGTGIAPFIGFLQHREKLQEQHPDGNFGA
MWLFFGCRHKDRDYLFRKELRHFLKHGILTHLKVSFSRDAPVGEEEAPAKYVQDNIQLHG
QQVARILLQENGHIYVCGDAKNMAKDVHDALVQIISKEVGVEKLEAMKTLATLKEEKRYL
QDIWS
Enzyme 16 Number of Residues 725
Enzyme 16 Molecular Weight 80437
Enzyme 16 Theoretical pI 6.47
Enzyme 16 GO Classification
Function
  • FMN binding
  • binding
  • catalytic activity
  • electron transporter activity
  • nucleotide binding
  • oxidoreductase activity
  • transporter activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
Enzyme 16 General Function Inorganic ion transport and metabolism
Enzyme 16 Specific Function Involved in the reductive regeneration of cob(I)alamin cofactor required for the maintenance of methionine synthase in a functional state
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions
  • 2 [methionine synthase]-methylcob(I)alamin + 2 S-adenosylhomocysteine + NADP+ = 2 [methionine synthase]-cob(I)alamin + NADPH + H+ + 2 S-adenosylLmethionine
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • 1-24
Enzyme 16 Transmembrane Regions Not Available
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 6572540 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID Q9UBK8 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name MTRR_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >2178 bp
ATGGGCGCTGCGTCAGTGCGCGCTGGCGCAAGGTTGGTGGAAGTCGCGTTGTGCAGTTTC
ACTGTTACATGCCTTGAAGTGATGAGGAGGTTTCTGTTACTATATGCTACACAGCAGGGA
CAGGCAAAGGCCATCGCAGAAGAAATGTGTGAGCAAGCTGTGGTACATGGATTTTCTGCA
GATCTTCACTGTATTAGTGAATCCGATAAGTATGACCTAAAAACCGAAACAGCTCCTCTT
GTTGTTGTGGTTTCTACCACGGGCACCGGAGACCCACCCGACACAGCCCGCAAGTTTGTT
AAGGAAATACAGAACCAAACACTGCCGGTTGATTTCTTTGCTCACCTGCGGTATGGGTTA
CTGGGTCTCGGTGATTCAGAATACACCTACTTTTGCAATGGGGGGAAGATAATTGATAAA
CGACTTCAAGAGCTTGGAGCCCGGCATTTCTATGACACTGGACATGCAGATGACTGTGTA
GGTTTAGAACTTGTGGTTGAGCCGTGGATTGCTGGACTCTGGCCAGCCCTCAGAAAGCAT
TTTAGGTCAAGCAGAGGACAAGAGGAGATAAGTGGCGCACTCCCGGTGGCATCACCTGCA
TCCTTGAGGACAGACCTTGTGAAGTCAGAGCTGCTACACATTGAATCTCAAGTCGAGCTT
CTGAGATTCGATGATTCAGGAAGAAAGGATTCTGAGGTTTTGAAGCAAAATGCAGTGAAC
AGCAACCAATCCAATGTTGTAATTGAAGACTTTGAGTCCTCACTTACCCGTTCGGTACCC
CCACTCTCACAAGCCTCTCTGAATATTCCTGGTTTACCCCCAGAATATTTACAGGTACAT
CTGCAGGAGTCTCTTGGCCAGGAGGAAAGCCAAGTATCTGTGACTTCAGCAGATCCAGTT
TTTCAAGTGCCAATTTCAAAGGCAGTTCAACTTACTACGAATGATGCCATAAAAACCACT
CTGCTGGTAGAATTGGACATTTCAAATACAGACTTTTCCTATCAGCCTGGAGATGCCTTC
AGCGTGATCTGCCCTAACAGTGATTCTGAGGTACAAAGCCTACTCCAAAGACTGCAGCTT
GAAGATAAAAGAGAGCACTGCGTCCTTTTGAAAATAAAGGCAGACACAAAGAAGAAAGGA
GCTACCTTACCCCAGCATATACCTGCGGGATGTTCTCTCCAGTTCATTTTTACCTGGTGT
CTTGAAATCCGAGCAATTCCTAAAAAGGCATTTTTGCGAGCCCTTGTGGACTATACCAGT
GACAGTGCTGAAAAGCGCAGGCTACAGGAGCTGTGCAGTAAACAAGGGGCAGCCGATTAT
AGCCGCTTTGTACGAGATGCCTGTGCCTGCTTGTTGGATCTCCTCCTCGCTTTCCCTTCT
TGCCAGCCACCACTCAGTCTCCTGCTCGAACATCTTCCTAAACTTCAACCCAGACCATAT
TCGTGTGCAAGCTCAAGTTTATTTCACCCAGGAAAGCTCCATTTTGTCTTCAACATTGTG
GAATTTCTGTCTACTGCCACAACAGAGGTTCTGCGGAAGGGAGTATGTACAGGCTGGCTG
GCCTTGTTGGTTGCTTCAGTTCTTCAGCCAAACATACATGCATCCCATGAAGACAGCGGG
AAAGCCCTGGCTCCTAAGATATCCATCTCTCCTCGAACAACAAATTCTTTCCACTTACCA
GATGACCCCTCAATCCCCATCATAATGGTGGGTCCAGGAACCGGCATAGCCCCGTTTATT
GGGTTCCTACAACATAGAGAGAAACTCCAAGAACAACACCCAGATGGAAATTTTGGAGCA
ATGTGGTTGTTTTTTGGCTGCAGGCATAAGGATAGGGATTATCTATTCAGAAAAGAGCTC
AGACATTTCCTTAAGCATGGGATCTTAACTCATCTAAAGGTTTCCTTCTCAAGAGATGCT
CCTGTTGGGGAGGAGGAAGCCCCAGCAAAGTATGTACAAGACAACATCCAGCTTCATGGC
CAGCAGGTGGCGAGAATCCTCCTCCAGGAGAACGGCCATATTTATGTGTGTGGAGATGCA
AAGAATATGGCCAAGGATGTACATGATGCCCTTGTGCAAATAATAAGCAAAGAGGTTGGA
GTTGAAAAACTAGAAGCAATGAAAACCCTGGCCACTTTAAAAGAAGAAAAACGCTACCTT
CAGGATATTTGGTCATAA
Enzyme 16 GenBank Gene ID AF121213 Link Image
Enzyme 16 GeneCard ID MTRR Link Image
Enzyme 16 GenAtlas ID MTRR Link Image
Enzyme 16 HGNC ID HGNC:7473 Link Image
Enzyme 16 Chromosome Location 5
Enzyme 16 Locus 5p15.3-p15.2
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Leclerc D, Odievre M, Wu Q, Wilson A, Huizenga JJ, Rozen R, Scherer SW, Gravel RA: Molecular cloning, expression and physical mapping of the human methionine synthase reductase gene. Gene. 1999 Nov 15;240(1):75-88. [PubMed Link Image]
  2. Leclerc D, Wilson A, Dumas R, Gafuik C, Song D, Watkins D, Heng HH, Rommens JM, Scherer SW, Rosenblatt DS, Gravel RA: Cloning and mapping of a cDNA for methionine synthase reductase, a flavoprotein defective in patients with homocystinuria. Proc Natl Acad Sci U S A. 1998 Mar 17;95(6):3059-64. [PubMed Link Image]
  3. Wilson A, Leclerc D, Rosenblatt DS, Gravel RA: Molecular basis for methionine synthase reductase deficiency in patients belonging to the cblE complementation group of disorders in folate/cobalamin metabolism. Hum Mol Genet. 1999 Oct;8(11):2009-16. [PubMed Link Image]
  4. Wilson A, Platt R, Wu Q, Leclerc D, Christensen B, Yang H, Gravel RA, Rozen R: A common variant in methionine synthase reductase combined with low cobalamin (vitamin B12) increases risk for spina bifida. Mol Genet Metab. 1999 Aug;67(4):317-23. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 5660
Enzyme 17 Name Nicotinamide N-methyltransferase
Enzyme 17 Synonyms Not Available
Enzyme 17 Gene Name NNMT
Enzyme 17 Protein Sequence >Nicotinamide N-methyltransferase
MESGFTSKDTYLSHFNPRDYLEKYYKFGSRHSAESQILKHLLKNLFKIFCLDGVKGDLLI
DIGSGPTIYQLLSACESFKEIVVTDYSDQNLQELEKWLKKEPEAFDWSPVVTYVCDLEGN
RVKGPEKEEKLRQAVKQVLKCDVTQSQPLGAVPLPPADCVLSTLCLDAACPDLPTYCRAL
RNLGSLLKPGGFLVIMDALKSSYYMIGEQKFSSLPLGREAVEAAVKEAGYTIEWFEVISQ
SYSSTMANNEGLFSLVARKLSRPL
Enzyme 17 Number of Residues 264
Enzyme 17 Molecular Weight 29574
Enzyme 17 Theoretical pI 5.45
Enzyme 17 GO Classification
Function
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
Component
Enzyme 17 General Function Not Available
Enzyme 17 Specific Function Catalyzes the N-methylation of nicotinamide and other pyridines to form pyridinium ions. This activity is important for biotransformation of many drugs and xenobiotic compounds
Enzyme 17 Pathways
  • Nicotinate and Nicotinamide Metabolism (map00760 Link Image)
Enzyme 17 Reactions
  • S-adenosyl-L-methionine + nicotinamide = S-adenosyl-L-homocysteine + 1-methylnicotinamide
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 494989 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID P40261 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name NNMT_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >795 bp
ATGGAATCAGGCTTCACCTCCAAGGACACCTATCTAAGCCATTTTAACCCTCGGGATTAC
CTAGAAAAATATTACAAGTTTGGTTCTAGGCACTCTGCAGAAAGCCAGATTCTTAAGCAC
CTTCTGAAAAATCTTTTCAAGATATTCTGCCTAGACGGTGTGAAGGGAGACCTGCTGATT
GACATCGGCTCTGGCCCCACTATCTATCAGCTCCTCTCTGCTTGTGAATCCTTTAAGGAG
ATCGTCGTCACTGACTACTCAGACCAGAACCTGCAGGAGCTGGAGAAGTGGCTGAAGAAA
GAGCCAGAGGCCTTTGACTGGTCCCCAGTGGTGACCTATGTGTGTGATCTTGAAGGGAAC
AGAGTCAAGGGTCCAGAGAAGGAGGAGAAGTTGAGACAGGCGGTCAAGCAGGTGCTGAAG
TGTGATGTGACTCAGAGCCAGCCACTGGGGGCCGTCCCCTTACCCCCGGCTGACTGCGTG
CTCAGCACACTGTGTCTGGATGCCGCCTGCCCAGACCTCCCCACCTACTGCAGGGCGCTC
AGGAACCTCGGCAGCCTACTGAAGCCAGGGGGCTTCCTGGTGATCATGGATGCGCTCAAG
AGCAGCTACTACATGATTGGTGAGCAGAAGTTCTCCAGCCTCCCCCTGGGCCGGGAGGCA
GTAGAGGCTGCTGTGAAAGAGGCTGGCTACACAATCGAATGGTTTGAGGTGATCTCGCAA
AGTTATTCTTCCACCATGGCCAACAACGAAGGACTTTTCTCCCTGGTGGCGAGGAAGCTG
AGCAGACCCCTGTGA
Enzyme 17 GenBank Gene ID U08021 Link Image
Enzyme 17 GeneCard ID NNMT Link Image
Enzyme 17 GenAtlas ID NNMT Link Image
Enzyme 17 HGNC ID HGNC:7861 Link Image
Enzyme 17 Chromosome Location 11
Enzyme 17 Locus 11q23.1
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Aksoy S, Szumlanski CL, Weinshilboum RM: Human liver nicotinamide N-methyltransferase. cDNA cloning, expression, and biochemical characterization. J Biol Chem. 1994 May 20;269(20):14835-40. [PubMed Link Image]
  2. Aksoy S, Brandriff BF, Ward A, Little PF, Weinshilboum RM: Human nicotinamide N-methyltransferase gene: molecular cloning, structural characterization and chromosomal localization. Genomics. 1995 Oct 10;29(3):555-61. [PubMed Link Image]
  3. Hubbard MJ, McHugh NJ: Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping. Electrophoresis. 2000 Nov;21(17):3785-96. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 5661
Enzyme 18 Name Histone-lysine N-methyltransferase SUV39H2
Enzyme 18 Synonyms
  1. Suppressor of variegation 3-9 homolog 2
  2. Su(var3-9 homolog 2
  3. Histone H3-K9 methyltransferase 2
  4. H3-K9-HMTase 2
Enzyme 18 Gene Name SUV39H2
Enzyme 18 Protein Sequence >Histone-lysine N-methyltransferase SUV39H2
MAAVGAEARGAWCVPCLVSLDTLQELCRKEKLTCKSIGITKRNLNNYEVEYLCDYKVVKD
MEYYLVKWKGWPDSTNTWEPLQNLKCPLLLQQFSNDKHNYLSQVKKGKAITPKDNNKTLK
PAIAEYIVKKAKQRIALQRWQDELNRRKNHKGMIFVENTVDLEGPPSDFYYINEYKPAPG
ISLVNEATFGCSCTDCFFQKCCPAEAGVLLAYNKNQQIKIPPGTPIYECNSRCQCGPDCP
NRIVQKGTQYSLCIFRTSNGRGWGVKTLVKIKRMSFVMEYVGEVITSEEAERRGQFYDNK
GITYLFDLDYESDEFTVDAARYGNVSHFVNHSCDPNLQVFNVFIDNLDTRLPRIALFSTR
TINAGEELTFDYQMKGSGDISSDSIDHSPAKKRVRTVCKCGAVTCRGYLN
Enzyme 18 Number of Residues 410
Enzyme 18 Molecular Weight 46683
Enzyme 18 Theoretical pI 8.27
Enzyme 18 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • chromatin binding
  • histone-lysine N-methyltransferase activity
  • ion binding
  • methyltransferase activity
  • protein methyltransferase activity
  • protein-lysine N-methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
  • transition metal ion binding
  • zinc ion binding
Process
  • DNA metabolism
  • DNA packaging
  • cellular metabolism
  • chromatin assembly or disassembly
  • chromatin modification
  • establishment and/or maintenance of chromatin architecture
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
  • chromatin
  • chromosome
  • intracellular membrane-bound organelle
  • intracellular non-membrane-bound organelle
  • membrane-bound organelle
  • non-membrane-bound organelle
  • nucleus
  • organelle
Enzyme 18 General Function Not Available
Enzyme 18 Specific Function Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys- 9' as substrate. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as cell cycle regulation, transcriptional repression and regulation of telomere length. May participate in regulation of higher order chromatin organization during spermatogenesis
Enzyme 18 Pathways
Enzyme 18 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • 1-13
Enzyme 18 Transmembrane Regions Not Available
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 10440094 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q9H5I1 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name SUV92_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >1053 bp
ATGGAATATTATCTTGTAAAATGGAAAGGATGGCCAGATTCTACAAATACTTGGGAACCT
TTGCAAAATCTGAAGTGCCCGTTACTGCTTCAGCAATTCTCTAATGACAAGCATAATTAT
TTATCTCAGGTAAAGAAAGGCAAAGCAATAACTCCAAAAGACAATAACAAAACTTTGAAA
CCTGCCATTGCTGAGTACATTGTGAAGAAGGCTAAACAAAGGATAGCTCTGCAGAGATGG
CAAGATGAACTCAACAGAAGAAAGAATCATAAAGGAATGATATTTGTTGAAAATACTGTT
GATTTAGAGGGCCCACCTTCAGACTTCTATTACATTAACGAATACAAACCAGCTCCTGGA
ATCAGCTTAGTCAATGAAGCTACCTTTGGTTGTTCATGCACAGATTGCTTCTTTCAAAAA
TGTTGTCCTGCTGAAGCTGGAGTTCTTTTGGCTTATAATAAAAACCAACAAATTAAAATC
CCACCTGGTACTCCCATCTATGAATGCAACTCAAGGTGTCAGTGTGGTCCTGATTGTCCC
AATAGGATTGTACAAAAAGGCACACAGTATTCGCTTTGCATCTTTCGAACTAGCAATGGA
CGTGGCTGGGGTGTAAAGACCCTTGTGAAGATTAAAAGAATGAGTTTTGTCATGGAATAT
GTTGGAGAGGTAATCACAAGTGAAGAAGCTGAAAGACGAGGACAGTTCTATGACAACAAG
GGAATCACGTATCTCTTTGATCTGGACTATGAGTCTGATGAATTCACAGTGGATGCGGCT
CGATACGGCAATGTGTCTCATTTTGTGAATCACAGCTGTGACCCAAATCTTCAGGTGTTC
AATGTTTTCATTGATAACCTCGATACTCGTCTTCCCCGAATAGCATTGTTTTCCACAAGA
ACCATAAATGCTGGAGAAGAGCTGACTTTTGATTATCAAATGAAAGGTTCTGGAGATATA
TCTTCAGATTCTATTGACCACAGCCCAGCCAAAAAGAGGGTCAGAACAGTATGTAAATGT
GGAGCTGTGACTTGCAGAGGTTACCTCAACTGA
Enzyme 18 GenBank Gene ID AK027067 Link Image
Enzyme 18 GeneCard ID SUV39H2 Link Image
Enzyme 18 GenAtlas ID SUV39H2 Link Image
Enzyme 18 HGNC ID HGNC:17287 Link Image
Enzyme 18 Chromosome Location 10
Enzyme 18 Locus 10p13
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References Not Available
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 5663
Enzyme 19 Name Guanidinoacetate N-methyltransferase
Enzyme 19 Synonyms Not Available
Enzyme 19 Gene Name GAMT
Enzyme 19 Protein Sequence >Guanidinoacetate N-methyltransferase
MSAPSATPIFAPGENCSPAWGAAPAAYDAADTHLRILGKPVMERWETPYMHALAAAASSK
GGRVLEVGFGMAIAASKVQEAPIDEHWIIECNDGVFQRLRDWAPRQTHKVIPLKGLWEDV
APTLPDGHFDGILYDTYPLSEETWHTHQFNFIKNHAFRLLKPGGVLTYCNLTSWGELMKS
KYSDITIMFEETQVPALLEAGFRRENIRTEVMALVPPADCRYYAFPQMITPLVTKG
Enzyme 19 Number of Residues 236
Enzyme 19 Molecular Weight 26318
Enzyme 19 Theoretical pI 6.09
Enzyme 19 GO Classification Not Available
Enzyme 19 General Function Not Available
Enzyme 19 Specific Function S-adenosyl-L-methionine + guanidinoacetate = S-adenosyl-L-homocysteine + creatine
Enzyme 19 Pathways
  • Arginine and Proline Metabolism (map00330 Link Image)
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
Enzyme 19 Reactions
  • S-adenosyl-L-methionine + guanidinoacetate = S-adenosyl-L-homocysteine + creatine
Enzyme 19 Pfam Domain Function Not Available
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 1212946 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q14353 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name GAMT_HUMAN Link Image
Enzyme 19 PDB ID 1XCL Link Image
Enzyme 19 PDB File Show
Enzyme 19 3D Structure
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >711 bp
ATGAGCGCCCCCAGCGCGACCCCCATCTTCGCGCCCGGCGAGAACTGCAGCCCCGCGTGG
GGGGCGGCGCCCGCGGCCTACGACGCAGCGGACACGCACCTGCGCATCCTGGGCAAGCCG
GTGATGGAGCGCTGGGAGACCCCCTATATGCACGCGCTGGCCGCCGCCGCCTCCTCCAAA
GGGGGCCGGGTCCTGGAGGTGGGCTTTGGCATGGCCATCGCAGCGTCAAAGGTGCAGGAG
GCGCCCATTGATGAGCATTGGATCATCGAGTGCAATGACGGCGTCTTCCAGCGGCTCCGG
GACTGGGCCCCACGGCAGACACACAAGGTCATCCCCTTGAAAGGCCTGTGGGAGGATGTG
GCACCCACCCTGCCTGACGGTCACTTTGATGGGATCCTGTACGACACGTACCCACTCTCG
GAGGAGACCTGGCACACACACCAGTTCAACTTCATCAAGAACCACGCCTTTCGCCTGCTG
AAGCCGGGGGGCGTCCTCACCTACTGCAACCTCACCTCCTGGGGGGAGCTGATGAAGTCC
AAGTACTCAGACATCACCATCATGTTTGAGGAGACGCAGGTGCCCGCGCTGCTGGAGGCC
GGCTTCCGGAGGGAGAACATCCGTACGGAGGTGATGGCGCTGGTCCCACCGGCCGACTGC
CGCTACTACGCCTTCCCACAGATGATCACGCCCCTGGTGACCAAAGGCTGA
Enzyme 19 GenBank Gene ID Z49878 Link Image
Enzyme 19 GeneCard ID GAMT Link Image
Enzyme 19 GenAtlas ID GAMT Link Image
Enzyme 19 HGNC ID HGNC:4136 Link Image
Enzyme 19 Chromosome Location 19
Enzyme 19 Locus 19p13.3
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Isbrandt D, von Figura K: Cloning and sequence analysis of human guanidinoacetate N-methyltransferase cDNA. Biochim Biophys Acta. 1995 Dec 27;1264(3):265-7. [PubMed Link Image]
  2. Jenne DE, Olsen AS, Zimmer M: The human guanidinoacetate methyltransferase (GAMT) gene maps to a syntenic region on 19p13.3, homologous to band C of mouse chromosome 10, but GAMT is not mutated in jittery mice. Biochem Biophys Res Commun. 1997 Sep 29;238(3):723-7. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 5665
Enzyme 20 Name Thiopurine S-methyltransferase
Enzyme 20 Synonyms
  1. Thiopurine methyltransferase
Enzyme 20 Gene Name TPMT
Enzyme 20 Protein Sequence >Thiopurine S-methyltransferase
MDGTRTSLDIEEYSDTEVQKNQVLTLEEWQDKWVNGKTAFHQEQGHQLLKKHLDTFLKGK
SGLRVFFPLCGKAVEMKWFADRGHSVVGVEISELGIQEFFTEQNLSYSEEPITEIPGTKV
FKSSSGNISLYCCSIFDLPRTNIGKFDMIWDRGALVAINPGDRKCYADTMFSLLGKKFQY
LLCVLSYDPTKHPGPPFYVPHAEIERLFGKICNIRCLEKVDAFEERHKSWGIDCLFEKLY
LLTEK
Enzyme 20 Number of Residues 245
Enzyme 20 Molecular Weight 28181
Enzyme 20 Theoretical pI 6.16
Enzyme 20 GO Classification
Function
  • S-methyltransferase activity
  • catalytic activity
  • methyltransferase activity
  • thiopurine S-methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • metabolism
  • physiological process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 20 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 20 Specific Function Catalyzes the S-methylation of thiopurine drugs such as 6-mercaptopurine
Enzyme 20 Pathways Not Available
Enzyme 20 Reactions
  • S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 386420 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID P51580 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name TPMT_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >738 bp
ATGGATGGTACAAGAACTTCACTTGACATTGAAGAGTACTCGGATACTGAGGTACAGAAA
AACCAAGTACTAACTCTGGAAGAATGGCAAGACAAGTGGGTGAACGGCAAGACTGCTTTT
CATCAGGAACAAGGACATCAGCTATTAAAGAAGCATTTAGATACTTTCCTTAAAGGCAAG
AGTGGACTGAGGGTATTTTTTCCTCTTTGCGGAAAAGCGGTTGAGATGAAATGGTTTGCA
GACCGGGGACACAGTGTAGTTGGTGTGGAAATCAGTGAACTTGGGATACAAGAATTTTTT
ACAGAGCAGAATCTTTCTTACTCAGAAGAACCAATCACCGAAATTCCTGGAACCAAAGTA
TTTAAGAGTTCTTCGGGGAACATTTCATTGTACTGTTGCAGTATTTTTGATCTTCCCAGG
ACAAATATTGGCAAATTTGACATGATTTGGGATAGAGGAGCATTAGTTGCCATTAATCCA
GGTGATCGCAAATGCTATGCAGATACAATGTTTTCCCTCCTGGGAAAGAAGTTTCAGTAT
CTCCTGTGTGTTCTTTCTTATGATCCAACTAAACATCCAGGTCCACCATTTTATGTTCCA
CATGCTGAAATTGAAAGGTTGTTTGGTAAAATATGCAATATACGTTGTCTTGAGAAGGTT
GATGCTTTTGAAGAACGACATAAAAGTTGGGGAATTGACTGTCTTTTTGAAAAGTTATAT
CTACTTACAGAAAAGTAA
Enzyme 20 GenBank Gene ID S62904 Link Image
Enzyme 20 GeneCard ID TPMT Link Image
Enzyme 20 GenAtlas ID TPMT Link Image
Enzyme 20 HGNC ID HGNC:12014 Link Image
Enzyme 20 Chromosome Location 6
Enzyme 20 Locus 6p22.3
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Honchel R, Aksoy IA, Szumlanski C, Wood TC, Otterness DM, Wieben ED, Weinshilboum RM: Human thiopurine methyltransferase: molecular cloning and expression of T84 colon carcinoma cell cDNA. Mol Pharmacol. 1993 Jun;43(6):878-87. [PubMed Link Image]
  2. Lee D, Szumlanski C, Houtman J, Honchel R, Rojas K, Overhauser J, Wieben ED, Weinshilboum RM: Thiopurine methyltransferase pharmacogenetics. Cloning of human liver cDNA and a processed pseudogene on human chromosome 18q21.1. Drug Metab Dispos. 1995 Mar;23(3):398-405. [PubMed Link Image]
  3. Szumlanski C, Otterness D, Her C, Lee D, Brandriff B, Kelsell D, Spurr N, Lennard L, Wieben E, Weinshilboum R: Thiopurine methyltransferase pharmacogenetics: human gene cloning and characterization of a common polymorphism. DNA Cell Biol. 1996 Jan;15(1):17-30. [PubMed Link Image]
  4. Krynetski EY, Fessing MY, Yates CR, Sun D, Schuetz JD, Evans WE: Promoter and intronic sequences of the human thiopurine S-methyltransferase (TPMT) gene isolated from a human PAC1 genomic library. Pharm Res. 1997 Dec;14(12):1672-8. [PubMed Link Image]
  5. Otterness D, Szumlanski C, Lennard L, Klemetsdal B, Aarbakke J, Park-Hah JO, Iven H, Schmiegelow K, Branum E, O'Brien J, Weinshilboum R: Human thiopurine methyltransferase pharmacogenetics: gene sequence polymorphisms. Clin Pharmacol Ther. 1997 Jul;62(1):60-73. [PubMed Link Image]
  6. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  7. Spire-Vayron de la Moureyre C, Debuysere H, Sabbagh N, Marez D, Vinner E, Chevalier ED, Lo Guidice JM, Broly F: Detection of known and new mutations in the thiopurine S-methyltransferase gene by single-strand conformation polymorphism analysis. Hum Mutat. 1998;12(3):177-85. [PubMed Link Image]
  8. Krynetski EY, Schuetz JD, Galpin AJ, Pui CH, Relling MV, Evans WE: A single point mutation leading to loss of catalytic activity in human thiopurine S-methyltransferase. Proc Natl Acad Sci U S A. 1995 Feb 14;92(4):949-53. [PubMed Link Image]
  9. Tai HL, Krynetski EY, Yates CR, Loennechen T, Fessing MY, Krynetskaia NF, Evans WE: Thiopurine S-methyltransferase deficiency: two nucleotide transitions define the most prevalent mutant allele associated with loss of catalytic activity in Caucasians. Am J Hum Genet. 1996 Apr;58(4):694-702. [PubMed Link Image]
  10. Hon YY, Fessing MY, Pui CH, Relling MV, Krynetski EY, Evans WE: Polymorphism of the thiopurine S-methyltransferase gene in African-Americans. Hum Mol Genet. 1999 Feb;8(2):371-6. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 5666
Enzyme 21 Name N6-adenosine-methyltransferase 70 kDa subunit
Enzyme 21 Synonyms
  1. MT-A70
  2. Methyltransferase-like protein 3
Enzyme 21 Gene Name METTL3
Enzyme 21 Protein Sequence >N6-adenosine-methyltransferase 70 kDa subunit
MSDTWSSIQAHKKQLDSLRERLQRRRKQDSGHLDLRNPEAALSPTFRSDSPVPTAPTSGG
PKPSTASAVPELATDPELEKKLLHHLSDLALTLPTDAVSICLAISTPDAPATQDGVESLL
QKFAAQELIEVKRGLLQDDAHPTLVTYADHSKLSAMMGAVAEKKGPGEVAGTVTGQKRRA
EQDSTTVAAFASSLVSGLNSSASEPAKEPAKKSRKHAASDVDLEIESLLNQQSTKEQQSK
KVSQEILELLNTTTAKEQSIVEKFRSRGRAQVQEFCDYGTKEECMKASDADRPCRKLHFR
RIINKHTDESLGDCSFLNTCFHMDTCKYVHYEIDACMDSEAPGSKDHTPSQELALTQSVG
GDSSADRLFPPQWICCDIRYLDVSILGKFAVVMADPPWDIHMELPYGTLTDDEMRRLNIP
VLQDDGFLFLWVTGRAMELGRECLNLWGYERVDEIIWVKTNQLQRIIRTGRTGHWLNHGK
EHCLVGVKGNPQGFNQGLDCDVIVAEVRSTSHKPDEIYGMIERLSPGTRKIELFGRPHNV
QPNWITLGNQLDGIHLLDPDVVARFKQRYPDGIISKPKNL
Enzyme 21 Number of Residues 580
Enzyme 21 Molecular Weight 64475
Enzyme 21 Theoretical pI 6.38
Enzyme 21 GO Classification
Function
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 21 General Function Not Available
Enzyme 21 Specific Function N6-methyltransferase that methylates adenosine residues of some mRNAs. N6-methyladenosine (m6A), which is present at internal sites of some mRNAs, may play a role in the efficiency of mRNA splicing, transport or translation
Enzyme 21 Pathways Not Available
Enzyme 21 Reactions
  • S-adenosyl-L-methionine + m7G(5')pppAm = S-adenosyl-L-homocysteine + m7G(5')pppm6Am (mRNA containing an N6,2'-O-dimethyladenosine cap)
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • None
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 2460037 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q86U44 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name MTA70_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >1740 bp
ATGTCGGACACGTGGAGCTCTATCCAGGCCCACAAGAAGCAGCTGGACTCTCTGCGGGAG
AGGCTGCAGCGGAGGCGGAAGCAGGACTCGGGGCACTTGGATCTACGGAATCCAGAGGCA
GCATTGTCTCCAACCTTCCGTAGTGACAGCCCAGTGCCTACTGCACCCACCTCTGGTGGC
CCTAAGCCCAGCACAGCTTCAGCAGTTCCTGAATTAGCTACAGATCCTGAGTTAGAGAAG
AAGTTGCTACACCACCTCTCTGATCTGGCCTTAACATTGCCCACTGATGCTGTGTCCATC
TGTCTTGCCATCTCCACGCCAGATGCTCCTGCCACTCAAGATGGGGTAGAAAGCCTCCTG
CAGAAGTTTGCAGCTCAGGAGTTGATTGAGGTAAAGCGAGGTCTCCTACAAGATGATGCA
CATCCTACTCTTGTAACCTATGCTGACCATTCCAAGCTCTCTGCCATGATGGGTGCTGTG
GCAGAAAAGAAGGGCCCTGGGGAGGTAGCAGGGACTGTCACAGGGCAGAAGCGGCGTGCA
GAACAGGACTCGACTACAGTAGCTGCCTTTGCCAGTTCGTTAGTCTCTGGTCTGAACTCT
TCAGCATCGGAACCAGCAAAGGAGCCAGCCAAGAAATCAAGGAAACATGCTGCCTCAGAT
GTTGATCTGGAGATAGAGAGCCTTCTGAACCAACAGTCCACTAAGGAACAACAGAGCAAG
AAGGTCAGTCAGGAGATCCTAGAGCTATTAATTACTACAACAGCCAAGGAACAATCCATT
GTTGAAATTCGCTCTCGAGGTCGGGCCCAAGTGCAAGAATTCTGTGACTATGGAACCAAG
GAGGAGTGCATGAAAGCCAGTGATGCTGATCGACCCTGTCGCAAGCTGCACTTCAGACGA
ATTATCAATAAACACACTGATGAGTCTTTAGGTGACTGCTCTTTCCTTAATACATGTTTC
CACATGGATACCTGCAAGTATGTTCACTATGAAATTGATGCTTGCATGGATTCTGAGGCC
CCTGGCAGCAAAGACCACACGCCAAGCCAGGAGCTTGCTCTTACACAGAGTGTCGGAGGT
GATTCCAGTGCAGACCGACTCTTCCCACCTCAGTGGATCTGTTGTGATATCCGCTACCTG
GTCGTCAGTATCTTGGGCAAGTTTGCAGTTGTGATGGCTGACCCACCCTGGGATATTCAC
ATGGAACTGCCCTATGGGACCCTGACAGATGATGAGATGCGCAGGCTCAACATACCCGTA
CTACAGGATGATGGCTTTCTCTTCCTCTGGGTCACAGGCAGGGCCATGGAGTTGGGGAGA
GAATGTCTAAACCTCTGGGGGTATGAACGGGTAGATGAAATTATTTGGGTGAAGACAAAT
CAACTGCAACGCATCATTCGGACAGGCCGTACAGGTCACTGGTTGAACCATGGGAAGGAA
CACTGCTTGGTTGGTGTCAAAGGAAATCCCCAAGGCTTCAACCAGGGTCTGGATTGTGAT
GTGATCGTAGCTGAGGTTCGTTCCACCAGTCATAAACCAGATGAAATCTATGGCATGATT
GAAAGACTATCTCCTGGCACTCGCAAGATTGAGTTATTTGGACGACCACACAATGTGCAA
CCCAACTGGATCACCCTTGGAAACCAACTGGATGGGATCCACCTACTAGACCCAGATGTG
GTTGCACGGTTCAAGCAAAGGTACCCAGATGGTATCATCTCTAAACCTAAGAATTTATAG
Enzyme 21 GenBank Gene ID AF014837 Link Image
Enzyme 21 GeneCard ID METTL3 Link Image
Enzyme 21 GenAtlas ID METTL3 Link Image
Enzyme 21 HGNC ID HGNC:17563 Link Image
Enzyme 21 Chromosome Location 14
Enzyme 21 Locus 14q11.1
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Bokar JA, Shambaugh ME, Polayes D, Matera AG, Rottman FM: Purification and cDNA cloning of the AdoMet-binding subunit of the human mRNA (N6-adenosine)-methyltransferase. RNA. 1997 Nov;3(11):1233-47. [PubMed Link Image]
  2. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 5933
Enzyme 22 Name Putative adenosylhomocysteinase 3
Enzyme 22 Synonyms
  1. S-adenosyl-L- homocysteine hydrolase 3
  2. AdoHcyase 3
Enzyme 22 Gene Name KIAA0828
Enzyme 22 Protein Sequence >Putative adenosylhomocysteinase 3
MSVQVVSAAAAAKVPEVELKDLSPSEAESQLGLSTAAVGAMAPPAGGGDPEAPAPAAERP
PVPGPGSGPAAALSPAAGKVPQASAMKRSDPHHQHQRHRDGGEALVSPDGTVTEAPRTVK
KQIQFADQKQEFNKRPTKIGRRSLSRSISQSSTDSYSSAASYTDSSDDETSPRDKQQKNS
KGSSDFCVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTA
VLMETLGALGAQCRWAACNIYSTLNEVAAALAESGFPVFAWKGESEDDFWWCIDRCVNVE
GWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVN
DSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYV
TEIDPICALQACMDGFRLVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGH
SNTEIDVASLRTPELTWERVRSQVDHVIWPDGKRIVLLAEGRLLNLSCSTVPTFVLSITA
TTQALALIELYNAPEGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQAKYLGLNK
NGPFKPNYYRY
Enzyme 22 Number of Residues 611
Enzyme 22 Molecular Weight 66722
Enzyme 22 Theoretical pI 7.39
Enzyme 22 GO Classification
Function
  • adenosylhomocysteinase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ether bonds
  • trialkylsulfonium hydrolase activity
Process
  • cellular metabolism
  • metabolism
  • one-carbon compound metabolism
  • physiological process
Component
Enzyme 22 General Function Coenzyme transport and metabolism
Enzyme 22 Specific Function S-adenosyl-L-homocysteine + H(2)O = L- homocysteine + adenosine
Enzyme 22 Pathways
Enzyme 22 Reactions
  • S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 4240145 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID Q96HN2 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name SAHH3_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >1860 bp
GAGCCGGTGGTTGCAGCGGAGGCGGTGATGTCGGTGCAGGTTGTGTCAGCCGCGGCTGCC
GCCAAGGTGCCTGAGGTGGAGCTGAAGGACCTGAGCCCCTCCGAGGCGGAGTCGCAACTA
GGACTGAGCACGGCCGCCGTGGGCGCCATGGCCCCCCCGGCGGGCGGTGGAGACCCTGAG
GCTCCAGCTCCCGCCGCGGAGCGGCCCCCGGTCCCCGGCCCGGGCTCGGGGCCCGCCGCC
GCTCTCAGCCCCGCCGCCGGGAAGGTGCCTCAGGCGTCGGCCATGAAGCGGAGCGACCCA
CATCACCAGCACCAGCGGCACCGCGACGGCGGCGAGGCCCTGGTCAGCCCCGACGGCACC
GTCACCGAGGCGCCGCGCACAGTCAAGAAGATCCAGTTTGCTGACCAGAAGCAAGAATTC
AACAAACGTCCCACCAAAATTGGACGTCGCTCTTTGTCTCGTTCCATTTCTCAGTCATCT
ACTGACAGCTACAGCTCAGCGGCTTCATATACAGATAGCTCTGATGATGAGACATCGCCC
AGGGACAAGCAGCAAAAGAACTCTAAGGGAAGCAGTGACTTCTGTGTTAAGAACATCAAA
CAGGCAGAGTTTGGACGAAGAGAAATTGAAATTGCTGAACAAGAAATGCCTGCATTGATG
GCTTTGAGGAAGAGAGCTCAAGGAGAAAAGCCTTTGGCTGGAGCCAAAATCGTGGGTTGC
ACACACATCACTGCTCAGACTGCTGTGCTTATGGAAACTCTGGGTGCTCTGGGGGCCCAG
TGCCGATGGGCTGCCTGCAACATCTATTCCACTCTCAATGAAGTGGCTGCTGCTCTAGCA
GAAAGTGGATTTCCTGTTTTTGCCTGGAAGGGAGAGTCAGAAGATGACTTTTGGTGGTGT
ATCGATAGATGTGTGAATGTGGAGGGCTGGCAGCCAAACATGATCTTGGATGATGGAGGG
GATCTTACCCACTGGATTTATAAAAAGTATCCCAACATGTTTAAGAAAATCAAGGGCATA
GTAGAGGAGAGTGTTACTGGAGTTCACAGGCTGTACCAACTGTCCAAAGCTGGGAAGCTG
TGTGTTCCAGCCATGAATGTCAATGACTCAGTCACCAAACAGAAATTTGACAACCTCTAC
TGTTGCCGTGAATCAATTCTTGATGGACTTAAAAGGACAACAGACATGATGTTTGGTGGA
AAGCAAGTGGTAGTCTGTGGCTATGGAGAGGTGGGGAAAGGGTGCTGTGCTGCCCTGAAA
GCCATGGGCTCCATTGTGTATGTAACTGAAATTGACCCCATCTGTGCCCTGCAAGCCTGT
ATGGATGGATTTCGACTGGTGAAATTAAATGAGGTCATCCGACAAGTGGACATTGTTATT
ACCTGTACAGGTAACAAGAATGTGGTAACCAGAGAGCACTTGGACCGTATGAAGAATAGC
TGCATCGTTTGTAACATGGGACATTCCAACACAGAGATTGACGTGGCGAGTCTGCGGACA
CCAGAACTGACCTGGGAGCGAGTGAGATCTCAAGTTGACCATGTGATATGGCCTGATGGC
AAGAGGATAGTACTGCTGGCAGAGGGCCGCCTGCTGAACCTTAGCTGCTCCACAGTGCCT
ACATTTGTGCTCTCAATCACTGCTACTACTCAGGCTCTTGCCTTGATAGAGCTTTACAAT
GCTCCTGAGGGTCGCTATAAGCAGGATGTCTACCTGTTGCCCAAGAAGATGGATGAGTAT
GTGGCCAGCCTACACCTGCCTACCTTTGATGCCCACTTGACAGAGCTGACAGATGAACAG
GCCAAGTATCTGGGACTCAACAAGAATGGGCCCTTCAAGCCTAATTACTACAGGTATTAA
Enzyme 22 GenBank Gene ID AB020635 Link Image
Enzyme 22 GeneCard ID Not Available
Enzyme 22 GenAtlas ID Not Available
Enzyme 22 HGNC ID Not Available
Enzyme 22 Chromosome Location 7
Enzyme 22 Locus 7q32.1
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1998 Dec 31;5(6):355-64. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 5934
Enzyme 23 Name Adenosylhomocysteinase
Enzyme 23 Synonyms
  1. S-adenosyl-L-homocysteine hydrolase
  2. AdoHcyase
Enzyme 23 Gene Name AHCY
Enzyme 23 Protein Sequence >Adenosylhomocysteinase
MSDKLPYKVADIGLAAWGRKALDIAENEMPGLMRMRERYSASKPLKGARIAGCLHMTVET
AVLIETLVTLGAEVQWSSCNIFSTQDHAAAAIAKAGIPVYAWKGETDEEYLWCIEQTLYF
KDGPLNMILDDGGDLTNLIHTKYPQLLPGIRGISEETTTGVHNLYKMMANGILKVPAINV
NDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVI
ITEIDPINALQAAMEGYEVTTMDEACQEGNIFVTTTGCIDIILGRHFEQMKDDAIVCNIG
HFDVEIDVKWLNENAVEKVNIKPQVDRYRLKNGRRIILLAEGRLVNLGCAMGHPSFVMSN
SFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVAEAHLGKLNVKLTKLTEKQAQYLGMS
CDGPFKPDHYRY
Enzyme 23 Number of Residues 432
Enzyme 23 Molecular Weight 47717
Enzyme 23 Theoretical pI 6.29
Enzyme 23 GO Classification
Function
  • adenosylhomocysteinase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ether bonds
  • trialkylsulfonium hydrolase activity
Process
  • cellular metabolism
  • metabolism
  • one-carbon compound metabolism
  • physiological process
Component
Enzyme 23 General Function Coenzyme transport and metabolism
Enzyme 23 Specific Function Adenosylhomocysteine is a competitive inhibitor of S- adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine
Enzyme 23 Pathways
Enzyme 23 Reactions
  • S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • None
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 178277 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID P23526 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name SAHH_HUMAN Link Image
Enzyme 23 PDB ID 1LI4 Link Image
Enzyme 23 PDB File Show
Enzyme 23 3D Structure
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >1299 bp
ATGTCTGACAAACTGCCCTACAAAGTCGCCGACATCGGCCTGGCTGCCTGGGGACGCAAG
GCCCTGGACATTGCTGAGAACGAGATGCCGGGCCTGATGCGTATGCGGGAGCGGTACTCG
GCCTCCAAGCCACTGAAGGGCGCCCGCATCGCTGGCTGCCTGCACATGACCGTGGAGACG
GCCGTCCTCATTGAGACCCTCGTCACCCTGGGTGCTGAGGTGCAGTGGTCCAGCTGCAAC
ATCTTCTCCACCCAGAACCATGCGGCGGCTGCCATTGCCAAGGCTGGCATTCCGGTGTAT
GCCTGGAAGGGCGAAACGGACGAGGAGTACCTGTGGTGCATTGAGCAGACCCTGTACTTC
AAGGACGGGCCCCTCAACATGATTCTGGACGACGGGGGCGACCTCACCAACCTCATCCAC
ACCAAGTACCCGCAGCTTCTGCCAGGCATCCGAGGCATCTCTGAGGAGACCACGACTGGG
GTCCACAACCTCTACAAGATGATGGCCAATGGGATCCTCAAGGTGCCTGCCATCAATGTC
AATGACTCCGTCACCAAGAGCAAGTTTGACAACCTCTATGGCTGCCGGGAGTCCCTCATA
GATGGCATCAAGCGGGCCACAGATGTGATGATTGCCGGCAAGGTAGCGGTGGTAGCAGGC
TATGGTGATGTGGGCAAGGGCTGTGCCCAGGCCCTGCGGGGTTTCGGAGCCCGCGTCATC
ATCACCGAGATTGACCCCATCAACGCACTGCAGGCTGCCATGGAGGGCTATGAGGTGACC
ACCATGGATGAGGCCTGTCAGGAGGGCAACATCTTTGTCACCACCACAGGCTGTATTGAC
ATCATCCTTGGCCGGCACTTTGAGCAGATGAAGGATGATGCCATTGTGTGTAACATTGGA
CACTTTGACGTGGAGATCGATGTCAAGTGGCTCAACGAGAACGCCGTGGAGAAGGTGAAC
ATCAAGCCGCAGGTGGACCGGTATCGGTTGAAGAATGGGCGCCGCATCATCCTGCTGGCC
GAGGGTCGGCTGGTCAACCTGGGTTGTGCCATGGGCCACCCCAGCTTCGTGATGAGTAAC
TCCTTCACCAACCAGGTGATGGCGCAGATCGAGCTGTGGACCCATCCAGACAAGTACCCC
GTTGGGGTTCATTTCCTGCCCAAGAAGCTGGATGAGGCAGTGGCTGAAGCCCACCTGGGC
AAGCTGAATGTGAAGTTGACCAAGCTAACTGAGAAGCAAGCCCAGTACCTGGGCATGTCC
TGTGATGGCCCCTTCAAGCCGGATCACTACCGCTACTGA
Enzyme 23 GenBank Gene ID M61831 Link Image
Enzyme 23 GeneCard ID AHCY Link Image
Enzyme 23 GenAtlas ID AHCY Link Image
Enzyme 23 HGNC ID HGNC:343 Link Image
Enzyme 23 Chromosome Location 20
Enzyme 23 Locus 20cen-q13.1
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Coulter-Karis DE, Hershfield MS: Sequence of full length cDNA for human S-adenosylhomocysteine hydrolase. Ann Hum Genet. 1989 May;53(Pt 2):169-75. [PubMed Link Image]
  2. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  3. Turner MA, Yuan CS, Borchardt RT, Hershfield MS, Smith GD, Howell PL: Structure determination of selenomethionyl S-adenosylhomocysteine hydrolase using data at a single wavelength. Nat Struct Biol. 1998 May;5(5):369-76. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 5935
Enzyme 24 Name Putative adenosylhomocysteinase 2
Enzyme 24 Synonyms
  1. S-adenosyl-L- homocysteine hydrolase 2
  2. AdoHcyase 2
  3. S-adenosylhomocysteine hydrolase-like 1
  4. DC-expressed AHCY-like molecule
Enzyme 24 Gene Name AHCYL1
Enzyme 24 Protein Sequence >Putative adenosylhomocysteinase 2
MSMPDAMPLPGVGEELKQAKEIEDAEKYSFMATVTKAPKKQIQFADDMQEFTKFPTKTGR
RSLSRSISQSSTDSYSSAASYTDSSDDEVSPREKQQTNSKGSSNFCVKNIKQAEFGRREI
EIAEQDMSALISLRKRAQGEKPLAGAKIVGCTHITAQTAVLIETLCALGAQCRWSACNIY
STQNEVAAALAEAGVAVFAWKGESEDDFWWCIDRCVNMDGWQANMILDDGGDLTHWVYKK
YPNVFKKIRGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDG
LKRTTDVMFGGKQVVVCGYGEVGKGCCAALKALGAIVYITEIDPICALQACMDGFRVVKL
NEVIRQVDVVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVTSLRTPELTWERVR
SQVDHVIWPDGKRVVLLAEGRLLNLSCSTVPTFVLSITATTQALALIELYNAPEGRYKQD
VYLLPKKMDEYVASLHLPSFDAHLTELTDDQAKYLGLNKNGPFKPNYYRY
Enzyme 24 Number of Residues 530
Enzyme 24 Molecular Weight 58952
Enzyme 24 Theoretical pI 6.87
Enzyme 24 GO Classification
Function
  • adenosylhomocysteinase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ether bonds
  • trialkylsulfonium hydrolase activity
Process
  • cellular metabolism
  • metabolism
  • one-carbon compound metabolism
  • physiological process
Component
Enzyme 24 General Function Coenzyme transport and metabolism
Enzyme 24 Specific Function S-adenosyl-L-homocysteine + H(2)O = L- homocysteine + adenosine
Enzyme 24 Pathways
Enzyme 24 Reactions
  • S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 16588687 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID O43865 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name SAHH2_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >1593 bp
ATGTCGATGCCTGACGCGATGCCGCTGCCCGGGGTCGGGGAGGAGCTGAAGCAGGCCAAG
GAGATCGAGGACGCCGAGAAGTACTCCTTCATGGCCACCGTCACCAAGGCGCCCAAGAAG
CAAATCCAGTTTGCTGATGACATGCAGGAGTTCACCAAATTCCCCACCAAAACTGGCCGA
AGATCTTTGTCTCGCTCGATCTCACAGTCCTCCACTGACAGCTACAGTTCAGCTGCATCC
TACACAGATAGCTCTGATGATGAGGTTTCTCCCCGAGAGAAGCAGCAAACCAACTCCAAG
GGCAGCAGCAATTTCTGTGTGAAGAACATCAAGCAGGCAGAATTTGGACGCCGGGAGATT
GAGATTGCAGAGCAAGACATGTCTGCTCTGATTTCACTCAGGAAACGTGCTCAGGGGGAG
AAGCCCTTGGCTGGTGCTAAAATAGTGGGCTGTACACACATCACAGCCCAGACAGCGGTG
TTGATTGAGACACTCTGTGCCCTGGGGGCTCAGTGCCGCTGGTCTGCTTGTAACATCTAC
TCAACTCAGAATGAAGTAGCTGCAGCACTGGCTGAGGCTGGAGTTGCAGTGTTCGCTTGG
AAGGGCGAGTCAGAAGATGACTTCTGGTGGTGTATTGACCGCTGTGTGAACATGGATGGG
TGGCAGGCCAACATGATCCTGGATGATGGGGGAGACTTAACCCACTGGGTTTATAAGAAG
TATCCAAACGTGTTTAAGAAGATCCGAGGCATTGTGGAAGAGAGCGTGACTGGTGTTCAC
AGGCTGTATCAGCTCTCCAAAGCTGGGAAGCTCTGTGTTCCGGCCATGAACGTCAATGAT
TCTGTTACCAAACAGAAGTTTGATAACTTGTACTGCTGCCGAGAATCCATTTTGGATGGC
CTGAAGAGGACCACAGATGTGATGTTTGGTGGGAAACAAGTGGTGGTGTGTGGCTATGGT
GAGGTAGGCAAGGGCTGCTGTGCTGCTCTCAAAGCTCTTGGAGCAATTGTCTACATTACC
GAAATCGACCCCATCTGTGCTCTGCAGGCCTGCATGGATGGGTTCAGGGTGGTAAAGCTA
AATGAAGTCATCCGGCAAGTCGATGTCGTAATAACTTGCACAGGAAATAAGAATGTAGTG
ACACGGGAGCACTTGGATCGCATGAAAAACAGTTGTATCGTATGCAATATGGGCCACTCC
AACACAGAAATCGATGTGACCAGCCTCCGCACTCCGGAGCTGACGTGGGAGCGAGTACGT
TCTCAGGTGGACCATGTCATCTGGCCAGATGGCAAACGAGTTGTCCTCCTGGCAGAGGGT
CGTCTACTCAATTTGAGCTGCTCCACAGTTCCCACCTTTGTTCTGTCCATCACAGCCACA
ACACAGGCTTTGGCACTGATAGAACTCTATAATGCACCCGAGGGGCGATACAAGCAGGAT
GTGTACTTGCTTCCTAAGAAAATGGATGAATACGTTGCCAGCTTGCATCTGCCATCATTT
GATGCCCACCTTACAGAGCTGACAGATGACCAAGCAAAATATCTGGGACTCAACAAAAAT
GGGCCATTCAAACCTAATTATTACAGATACTAA
Enzyme 24 GenBank Gene ID AF315687 Link Image
Enzyme 24 GeneCard ID AHCYL1 Link Image
Enzyme 24 GenAtlas ID AHCYL1 Link Image
Enzyme 24 HGNC ID HGNC:344 Link Image
Enzyme 24 Chromosome Location 1
Enzyme 24 Locus 1p13.2
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. Dekker JW, Budhia S, Angel NZ, Cooper BJ, Clark GJ, Hart DN, Kato M: Identification of an S-adenosylhomocysteine hydrolase-like transcript induced during dendritic cell differentiation. Immunogenetics. 2002 Mar;53(12):993-1001. Epub 2002 Feb 13. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 7083
Enzyme 25 Name Histone-lysine N-methyltransferase, H3 lysine-4 specific SET1
Enzyme 25 Synonyms
  1. Set1/Ash2 histone methyltransferase complex subunit SET1
  2. SET domain-containing protein 1A
Enzyme 25 Gene Name SETD1A
Enzyme 25 Protein Sequence >Histone-lysine N-methyltransferase, H3 lysine-4 specific SET1
MDQEGGGDGQKAPSFQWRNYKLIVDPALDPALRRPSQKVYRYDGVHFSVNDSKYIPVEDL
QDPRCHVRSKNRDFSLPVPKFKLDEFYIGQIPLKEVTFARLNDNVRETFLKDMCRKYGEV
EEVEILLHPRTRKHLGLARVLFTSTRGAKETVKNLHLTSVMGNIIHAQLDIKGQQRMKYY
ELIVNGSYTPQTVPTGGKALSEKFQGSGAATETAESRRRSSSDTAAYPAGTTAVGTPGNG
TPCSQDTSFSSSRQDTPSSFGQFTPQSSQGTPYTSRGSTPYSQDSAYSSSTTSTSFKPRR
SENSYQDAFSRRHFSASSASTTASTAIAATTAATASSSASSSSLSSSSSSSSSSSSSQFR
SSDANYPAYYESWNRYQRHTSYPPRRATREEPPGAPFAENTAERFPPSYTSYLPPEPSRP
TDQDYRPPASEAPPPEPPEPGGGGGGGGPSPEREEVRTSPRPASPARSGSPAPETTNESV
PFAQHSSLDSRIEMLLKEQRSKFSFLASDTEEEEENSSMVLGARDTGSEVPSGSGHGPCT
PPPAPANFEDVAPTGSGEPGATRESPKANGQNQASPCSSGDDMEISDDDRGGSPPPAPTP
PQQPPPPPPPPPPPPPYLASLPLGYPPHQPAYLLPPRPDGPPPPEYPPPPPPPPHIYDFV
NSLELMDRLGAQWGGMPMSFQMQTQMLTRLHQLRQGKGLIAASAGPPGGAFGEAFLPFPP
PQEAAYGLPYALYAQGQEGRGAYSREAYHLPMPMAAEPLPSSSVSGEEARLPPREEAELA
EGKTLPTAGTVGRVLAMLVQEMKSIMQRDLNRKMVENVAFGAFDQWWESKEEKAKPFQNA
AKQQAKEEDKEKTKLKEPGLLSLVDWAKSGGTTGIEAFAFGSGLRGALRLPSFKVKRKEP
SEISEASEEKRPRPSTPAEEDEDDPEQEKEAGEPGRPGTKPPKRDEERGKTQGKHRKSFA
LDSEGEEASQESSSEKDEEDDEEDEEDEDREEAVDTTKKETEVSDGEDEESDSSSKCSLY
ADSDGENDSTSDSESSSSSSSSSSSSSSSSSSSSSSSSESSSEDEEEEERPAALPSASPP
PREVPVPTPAPVEVPVPERVAGSPVTPLPEQEASPARPAGPTEESPPSAPLRPPEPPAGP
PAPAPRPDERPSSPIPLLPPPKKRRKTVSFSAIEVVPAPEPPPATPPQAKFPGPASRKAP
RGVERTIRNLPLDHASLVKSWPEEVSRGGRSRAGGRGRLTEEEEAEPGTEVDLAVLADLA
LTPARRGLPALPAVEDSEATETSDEAERPRPLLSHILLEHNYALAVKPTPPAPALRPPEP
VPAPAALFSSPADEVLEAPEVVVAEAEEPKPQQLQQQREEGEEEGEEEGEEEEEESSDSS
SSSDGEGALRRRSLRSHARRRRPPPPPPPPPPRAYEPRSEFEQMTILYDIWNSGLDSEDM
SYLRLTYERLLQQTSGADWLNDTHWVHHTITNLTTPKRKRRPQDGPREHQTGSARSEGYY
PISKKEKDKYLDVCPVSARQLEGVDTQGTNRVLSERRSEQRRLLSAIGTSAIMDSDLLKL
NQLKFRKKKLRFGRSRIHEWGLFAMEPIAADEMVIEYVGQNIRQMVADMREKRYVQEGIG
SSYLFRVDHDTIIDATKCGNLARFINHCCTPNCYAKVITIESQKKIVIYSKQPIGVDEEI
TYDYKFPLEDNKIPCLCGTESCRGSLN
Enzyme 25 Number of Residues 1707
Enzyme 25 Molecular Weight 186035
Enzyme 25 Theoretical pI 4.79
Enzyme 25 GO Classification
Function
  • binding
  • nucleic acid binding
  • nucleotide binding
Process
Component
Enzyme 25 General Function Not Available
Enzyme 25 Specific Function Specifically methylates 'Lys-4' of histone H3, when part of the Set1/Ash2 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated
Enzyme 25 Pathways
Enzyme 25 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 6683126 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID O15047 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name SET1A_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >5130 bp
GCAAAGATGGATCAGGAAGGTGGGGGAGATGGGCAGAAGGCCCCGAGCTTCCAGTGGCGG
AACTACAAGCTCATCGTGGATCCTGCCTTGGACCCTGCCCTGCGCAGGCCTTCTCAGAAG
GTGTACCGCTATGATGGAGTCCACTTCAGTGTCAACGACTCAAAGTATATACCAGTCGAA
GACCTCCAAGACCCCCGTTGCCATGTCAGGTCCAAAAACAGAGACTTTTCCCTCCCAGTC
CCTAAGTTTAAGCTGGACGAGTTCTATATTGGACAGATTCCACTGAAGGAAGTGACTTTT
GCAAGGCTGAATGACAACGTGCGGGAGACCTTCCTGAAGGATATGTGCCGTAAGTACGGT
GAGGTGGAAGAGGTAGAGATCCTCCTTCACCCCCGTACGCGCAAGCACCTGGGCCTGGCC
CGTGTGCTCTTCACCAGCACTCGGGGCGCCAAGGAAACGGTCAAAAACCTCCACCTTACC
TCCGTCATGGGCAACATCATCCATGCCCAGCTTGACATCAAAGGACAACAACGAATGAAA
TACTATGAACTAATTGTCAATGGCTCCTACACCCCTCAGACTGTGCCCACTGGGGGCAAG
GCCCTGAGTGAGAAGTTCCAAGGCTCGGGTGCAGCCACTGAGACGGCCGAATCCCGCCGC
CGCTCTTCCTCTGACACAGCTGCCTACCCAGCAGGCACCACTGCGGTGGGCACTCCTGGC
AACGGCACCCCCTGCTCCCAGGACACAAGCTTCTCCAGCAGCCGACAAGATACCCCATCT
TCCTTTGGCCAGTTCACACCTCAGTCCTCCCAAGGAACCCCCTACACGTCTCGGGGCAGC
ACCCCCTACTCTCAGGACTCTGCCTACTCCAGCAGCACCACTTCAACCTCCTTCAAGCCC
CGGCGGTCAGAGAACAGCTACCAAGATGCCTTTTCCCGCCGCCACTTCTCTGCATCTTCA
GCCTCCACAACCGCCTCCACGGCCATCGCCGCCACCACTGCAGCCACTGCCTCATCCTCC
GCCTCTTCCTCCTCATTGTCCTCGTCCTCCTCGTCATCCTCTTCCTCCTCGTCCTCTCAG
TTTCGTAGTTCTGATGCAAACTACCCAGCGTATTATGAAAGCTGGAATCGCTACCAGCGC
CATACTTCCTACCCACCACGCCGGGCCACACGGGAGGAACCCCCTGGAGCCCCTTTTGCT
GAAAATACAGCTGAGCGCTTCCCACCTTCTTACACCTCCTACCTGCCCCCCGAGCCCAGC
CGGCCCACCGACCAGGACTACCGGCCTCCTGCCTCAGAGGCTCCACCCCCGGAGCCTCCA
GAACCTGGTGGAGGCGGGGGTGGAGGAGGGCCCAGCCCTGAGAGAGAAGAAGTTCGGACT
TCCCCCCGCCCAGCCTCCCCTGCCCGCTCTGGCTCCCCAGCCCCGGAGACCACCAATGAG
AGTGTGCCCTTCGCCCAGCACAGCAGCCTGGATTCCCGCATCGAGATGCTGCTGAAGGAG
CAGCGCTCCAAGTTTTCCTTCTTGGCCTCTGACACAGAGGAGGAGGAAGAGAACAGCAGC
ATGGTCCTTGGGGCCAGAGATACAGGGAGTGAGGTGCCTTCTGGGTCAGGGCATGGGCCC
TGCACACCCCCTCCGGCCCCAGCTAATTTTGAGGATGTGGCACCTACAGGGAGCGGGGAG
CCAGGGGCTACCCGGGAGTCTCCCAAGGCAAATGGACAGAACCAGGCTTCTCCATGCTCT
TCTGGAGACGACATGGAGATCTCCGACGACGACCGGGGTGGCTCACCCCCTCCGGCCCCG
ACGCCCCCTCAGCAGCCTCCGCCACCTCCCCCTCCCCCGCCGCCTCCTCCTCCCTACCTG
GCGTCCCTTCCTCTTGGTTATCCTCCCCACCAACCTGCCTACCTCCTCCCACCCAGACCT
GATGGGCCGCCGCCCCCTGAGTACCCCCCACCTCCTCCACCACCCCCGCACATCTATGAC
TTTGTGAACTCCTTGGAGCTCATGGACCGACTTGGGGCTCAGTGGGGAGGGATGCCCATG
TCCTTCCAGATGCAGACCCAGATGTTAACTCGGCTCCATCAGCTGCGGCAGGGCAAGGGA
TTGATTGCCGCCTCAGCTGGCCCCCCCGGTGGGGCCTTTGGGGAGGCCTTCCTCCCGTTT
CCACCCCCGCAGGAGGCAGCCTACGGCTTGCCGTATGCTCTATATGCACAGGGGCAGGAG
GGCAGAGGGGCATACTCACGGGAGGCCTACCACCTGCCCATGCCAATGGCAGCCGAGCCC
CTGCCCTCCTCCTCAGTCTCGGGAGAGGAGGCCCGGCTGCCACCCAGGGAAGAAGCAGAG
CTGGCAGAGGGCAAGACCCTCCCGACAGCAGGCACCGTGGGCCGTGTGCTCGCCATGCTG
GTCCAGGAGATGAAGAGCATCATGCAGCGAGACCTCAACCGCAAGATGGTGGAGAACGTG
GCCTTCGGAGCCTTTGACCAGTGGTGGGAGAGCAAGGAGGAGAAGGCCAAGCCATTCCAG
AACGCGGCCAAGCAGCAAGCCAAGGAGGAGGATAAAGAGAAGACGAAGCTGAAGGAGCCT
GGCCTGCTGTCCCTCGTGGACTGGGCCAAGAGCGGGGGCACTACGGGCATCGAGGCTTTC
GCCTTTGGGTCAGGGCTGAGAGGGGCCCTGCGGCTGCCTTCATTCAAGGTAAAGCGGAAA
GAGCCATCGGAAATTTCCGAGGCCAGTGAGGAAAAGAGGCCTCGTCCCTCCACTCCTGCT
GAGGAAGATGAAGACGACCCTGAACAAGAGAAGGAGGCTGGAGAGCCAGGACGTCCGGGG
ACCAAGCCCCCGAAGCGGGACGAAGAGCGAGGCAAGACCCAGGGCAAGCACCGCAAGTCC
TTTGCTCTGGACAGCGAAGGGGAGGAGGCATCCCAGGAGTCCTCCTCGGAGAAGGATGAG
GAGGATGACGAGGAAGATGAGGAAGATGAAGATCGAGAGGAAGCTGTGGATACCACAAAG
AAGGAGACAGAGGTGTCGGATGGCGAGGACGAGGAAAGCGATTCGTCTTCCAAATGTTCT
CTGTATGCTGACTCAGATGGCGAAAATGACAGCACATCAGACTCCGAGAGCAGCAGCTCT
TCCAGCTCCTCATCCTCCTCCTCCTCCTCGTCCTCATCCTCCTCGTCCTCTTCATCCTCT
GAGTCCTCCTCTGAAGATGAAGAGGAAGAGGAGCGGCCAGCAGCCCTTCCCTCAGCCTCC
CCGCCCCCCAGAGAAGTCCCAGTGCCCACGCCAGCACCTGTGGAGGTGCCAGTGCCGGAA
AGGGTTGCAGGCTCCCCAGTCACACCCCTGCCCGAACAGGAGGCGTCTCCAGCAAGGCCT
GCAGGCCCCACGGAGGAGTCACCCCCCAGTGCGCCTCTGCGTCCCCCAGAACCACCTGCT
GGGCCCCCGGCCCCTGCCCCACGCCCCGATGAGCGTCCCTCTTCTCCCATCCCCCTCCTG
CCCCCACCCAAGAAACGCCGGAAAACTGTCTCCTTCTCTGCCATCGAGGTGGTGCCAGCC
CCGGAGCCCCCTCCAGCCACACCGCCGCAGGCCAAGTTTCCCGGCCCAGCCTCCCGCAAG
GCTCCCCGGGGCGTGGAGCGGACCATCCGCAACCTGCCCCTGGACCACGCATCTCTGGTC
AAGAGTTGGCCCGAGGAGGTGTCCCGAGGAGGCCGGAGCCGGGCTGGAGGCCGAGGCCGC
CTCACCGAGGAAGAGGAGGCTGAGCCAGGGACAGAGGTGGACCTGGCGGTCCTGGCCGAC
CTGGCCCTGACCCCTGCCCGGCGCGGGCTGCCTGCCCTGCCTGCTGTTGAAGACTCAGAG
GCCACAGAGACATCGGACGAGGCCGAGCGCCCTAGGCCCCTGCTCAGCCACATCCTCCTG
GAGCACAACTATGCCCTGGCCGTCAAGCCCACGCCCCCTGCGCCAGCCCTGCGGCCCCCG
GAGCCAGTGCCCGCACCCGCCGCCCTCTTCAGTTCCCCAGCTGATGAGGTCCTGGAGGCC
CCCGAGGTGGTGGTGGCTGAGGCGGAGGAGCCCAAGCCGCAGCAACTGCAGCAGCAGCGG
GAGGAGGGCGAAGAGGAGGGGGAGGAAGAGGGGGAGGAAGAGGAGGAGGAGTCCTCTGAC
AGCAGCAGCAGCAGCGATGGGGAGGGCGCCCTCCGGAGGCGCAGCCTCCGCTCCCACGCC
CGGCGCCGCCGCCCTCCGCCCCCACCCCCGCCGCCACCGCCCCGCGCCTACGAGCCACGC
AGTGAGTTTGAACAGATGACCATCCTGTATGACATTTGGAACTCGGGCCTGGACTCAGAG
GACATGAGTTACCTGCGGCTTACGTACGAGCGGCTGCTGCAGCAGACAAGCGGGGCTGAC
TGGCTCAACGACACTCACTGGGTCCATCACACAATCACCAACCTGACCACCCCAAAACGC
AAGCGGCGGCCCCAGGATGGGCCCCGGGAGCACCAGACAGGCTCAGCCCGCAGCGAAGGC
TACTACCCCATCAGCAAGAAGGAGAAGGACAAGTACCTGGACGTGTGCCCAGTCTCGGCC
CGGCAGCTGGAGGGCGTGGACACTCAGGGGACGAACCGCGTGCTGTCCGAGCGCCGGTCC
GAGCAGCGGCGGCTGCTGAGCGCCATCGGTACCTCCGCCATCATGGACAGTGACCTGCTG
AAACTCAACCAGCTCAAGTTCCGGAAGAAGAAGCTCCGATTTGGCCGGAGCCGGATCCAC
GAGTGGGGTCTGTTTGCCATGGAACCCATTGCTGCTGACGAGATGGTCATCGAATACGTG
GGTCAGAACATCCGTCAGATGGTGGCCGACATGCGGGAGAAGCGCTACGTGCAGGAGGGC
ATTGGCAGCAGCTACCTGTTCCGGGTGGACCACGACACCATCATCGATGCCACCAAGTGT
GGCAACCTGGCCAGATTCATCAACCACTGCTGCACGCCTAACTGCTACGCCAAGGTCATC
ACCATCGAGTCCCAGAAGAAGATCGTGATCTACTCCAAGCAGCCCATTGGCGTGGACGAG
GAGATCACCTACGACTACAAGTTCCCACTGGAAGACAACAAGATCCCGTGTCTGTGTGGC
ACAGAGAGCTGCCGGGGCTCCCTAAACTGA
Enzyme 25 GenBank Gene ID AB002337 Link Image
Enzyme 25 GeneCard ID SETD1A Link Image
Enzyme 25 GenAtlas ID SETD1A Link Image
Enzyme 25 HGNC ID HGNC:29010 Link Image
Enzyme 25 Chromosome Location 16
Enzyme 25 Locus 16p11.2
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1997 Apr 28;4(2):141-50. [PubMed Link Image]
  2. Wysocka J, Myers MP, Laherty CD, Eisenman RN, Herr W: Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1. Genes Dev. 2003 Apr 1;17(7):896-911. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 7643
Enzyme 26 Name DNA
Enzyme 26 Synonyms
  1. cytosine-5-methyltransferase 1
  2. Dnmt1
  3. DNA methyltransferase HsaI
  4. DNA MTase HsaI
  5. MCMT
  6. M.HsaI
Enzyme 26 Gene Name DNMT1
Enzyme 26 Protein Sequence >DNA
MPARTAPARVPTLAVPAISLPDDVRRRLKDLERDSLTEKECVKEKLNLLHEFLQTEIKNQ
LCDLETKLRKEELSEEGYLAKVKSLLNKDLSLENGAHAYNREVNGRLENGNQARSEARRV
GMADANSPPKPLSKPRTPRRSKSDGEAKPEPSPSPRITRKSTRQTTITSHFAKGPAKRKP
QEESERAKSDESIKEEDKDQDEKRRRVTSRERVARPLPAEEPERAKSGTRTEKEEERDEK
EEKRLRSQTKEPTPKQKLKEEPDREARAGVQADEDEDGDEKDEKKHRSQPKDLAAKRRPE
EKEPEKVNPQISDEKDEDEKEEKRRKTTPKEPTEKKMARAKTVMNSKTHPPKCIQCGQYL
DDPDLKYGQHPPDAVDEPQMLTNEKLSIFDANESGFESYEALPQHKLTCFSVYCKHGHLC
PIDTGLIEKNIELFFSGSAKPIYDDDPSLEGGVNGKNLGPINEWWITGFDGGEKALIGFS
TSFAEYILMDPSPEYAPIFGLMQEKIYISKIVVEFLQSNSDSTYEDLINKIETTVPPSGL
NLNRFTEDSLLRHAQFVVEQVESYDEAGDSDEQPIFLTPCMRDLIKLAGVTLGQRRAQAR
RQTIRHSTREKDRGPTKATTTKLVYQIFDTFFAEQIEKDDREDKENAFKRRRCGVCEVCQ
QPECGKCKACKDMVKFGGSGRSKQACQERRCPNMAMKEADDDEEVDDNIPEMPSPKKMHQ
GKKKKQNKNRISWVGEAVKTDGKKSYYKKVCIDAETLEVGDCVSVIPDDSSKPLYLARVT
ALWEDSSNGQMFHAHWFCAGTDTVLGATSDPLELFLVDECEDMQLSYIHSKVKVIYKAPS
ENWAMEGGMDPESLLEGDDGKTYFYQLWYDQDYARFESPPKTQPTEDNKFKFCVSCARLA
EMRQKEIPRVLEQLEDLDSRVLYYSATKNGILYRVGDGVYLPPEAFTFNIKLSSPVKRPR
KEPVDEDLYPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIFCPKKSNGRPNETDIKIRVNK
FYRPENTHKSTPASYHADINLLYWSDEEAVVDFKAVQGRCTVEYGEDLPECVQVYSMGGP
NRFYFLEAYNAKSKSFEDPPNHARSPGNKGKGKGKGKGKPKSQACEPSEPEIEIKLPKLR
TLDVFSGCGGLSEGFHQAGISDTLWAIEMWDPAAQAFRLNNPGSTVFTEDCNILLKLVMA
GETTNSRGQRLPQKGDVEMLCGGPPCQGFSGMNRFNSRTYSKFKNSLVVSFLSYCDYYRP
RFFLLENVRNFVSFKRSMVLKLTLRCLVRMGYQCTFGVLQAGQYGVAQTRRRAIILAAAP
GEKLPLFPEPLHVFAPRACQLSVVVDDKKFVSNITRLSSGPFRTITVRDTMSDLPEVRNG
ASALEISYNGEPQSWFQRQLRGAQYQPILRDHICKDMSALVAARMRHIPLAPGSDWRDLP
NIEVRLSDGTMARKLRYTHHDRKNGRSSSGALRGVCSCVEAGKACDPAARQFNTLIPWCL
PHTGNRHNHWAGLYGRLEWDGFFSTTVTNPEPMGKQGRVLHPEQHRVVSVRECARSQGFP
DTYRLFGNILDKHRQVGNAVPPPLAKAIGLEIKLCMLAKARESASAKIKEEEAAKD
Enzyme 26 Number of Residues 1616
Enzyme 26 Molecular Weight 183167
Enzyme 26 Theoretical pI 7.81
Enzyme 26 GO Classification
Function
  • DNA binding
  • binding
  • cation binding
  • ion binding
  • nucleic acid binding
  • protein binding
  • transcription factor binding
  • transition metal ion binding
  • zinc ion binding
Process
  • DNA alkylation
  • DNA metabolism
  • DNA methylation
  • DNA modification
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 26 General Function Replication, recombination and repair
Enzyme 26 Specific Function Methylates CpG residues. Preferentially methylates hemimethylated DNA. It is responsible for maintaining methylation patterns established in development. DNA methylation is coordinated with methylation of histones. Mediates transcriptional repression by direct binding to HDAC2
Enzyme 26 Pathways
Enzyme 26 Reactions
  • S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 1632819 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID P26358 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name DNMT1_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >4851 bp
ATGCCGGCGCGTACCGCCCCAGCCCGGGTGCCCACACTGGCCGTCCCGGCCATCTCGCTG
CCCGACGATGTCCGCAGGCGGCTCAAAGATTTGGAAAGAGACAGCTTAACAGAAAAGGAA
TGTGTGAAGGAGAAATTGAATCTCTTGCACGAATTTCTGCAAACAGAAATAAAGAATCAG
TTATGTGACTTGGAAACCAAATTACGTAAAGAAGAATTATCCGAGGAGGGCTACCTGGCT
AAAGTCAAATCCCTTTTAAATAAAGATTTGTCCTTGGAGAACGGTGCTCATGCTTACAAC
CGGGAAGTGAATGGACGTCTAGAAAACGGGAACCAAGCAAGAAGTGAAGCCCGTAGAGTG
GGAATGGCAGATGCCAACAGCCCCCCCAAACCCCTTTCCAAACCTCGCACGCCCAGGAGG
AGCAAGTCCGATGGAGAGGCTAAGCCTGAACCTTCACCTAGCCCCAGGATTACAAGGAAA
AGCACCAGGCAAACCACCATCACATCTCATTTTGCAAAGGGCCCTGCCAAACGGAAACCT
CAGGAAGAGTCTGAAAGAGCCAAATCGGATGAGTCCATCAAGGAAGAAGACAAAGACCAG
GATGAGAAGAGACGTAGAGTTACATCCAGAGAACGAGTTGCTAGACCGCTTCCTGCAGAA
GAACCTGAAAGAGCAAAATCAGGAACGCGCACTGAAAAGGAAGAAGAAAGAGATGAAAAA
GAAGAAAAGAGACTCCGAAGTCAAACCAAAGAACCAACACCCAAACAGAAACTGAAGGAG
GAGCCGGACAGAGAAGCCAGGGCAGGCGTGCAGGCTGACGAGGACGAAGATGGAGACGAG
AAAGATGAGAAGAAGCACAGAAGTCAACCCAAAGATCTAGCTGCCAAACGGAGGCCCGAA
GAAAAAGAACCTGAAAAAGTAAATCCACAGATTTCTGATGAAAAAGACGAGGATGAAAAG
GAGGAGAAGAGACGCAAAACGACCCCCAAAGAACCAACGGAGAAAAAAATGGCTCGCGCC
AAAACAGTCATGAACTCCAAGACCCACCCTCCCAAGTGCATTCAGTGCGGGCAGTACCTG
GACGACCCTGACCTCAAATATGGGCAGCACCCACCAGACGCGGTGGATGAGCCACAGATG
CTGACAAATGAGAAGCTGTCCATCTTTGATGCCAACGAGTCTGGCTTTGAGAGTTATGAG
GCGCTTCCCCAGCACAAACTGACCTGCTTCAGTGTGTACTGTAAGCACGGTCACCTGTGT
CCCATCGACACCGGCCTCATCGAGAAGAATATCGAACTCTTCTTTTCTGGTTCAGCAAAA
CCAATCTATGATGATGACCCGTCTCTTGAAGGTGGTGTTAATGGCAAAAATCTTGGCCCC
ATAAATGAATGGTGGATCACTGGCTTTGATGGAGGTGAAAAGGCCCTCATCGGCTTCAGC
ACCTCATTTGCCGAATACATTCTGATGGATCCCAGTCCCGAGTATGCGCCCATATTTGGG
CTGATGCAGGAGAAGATCTACATCAGCAAGATTGTGGTGGAGTTCCTGCAGAGCAATTCC
GACTCGACCTATGAGGACCTGATCAACAAGATCGAGACCACGGTTCCTCCTTCTGGCCTC
AACTTGAACCGCTTCACAGAGGACTCCCTCCTGCGACACGCGCAGTTTGTGGTGGAGCAG
GTGGAGAGTTATGACGAGGCCGGGGACAGTGATGAGCAGCCCATCTTCCTGACGCCCTGC
ATGCGGGACCTGATCAAGCTGGCTGGGGTCACGCTGGGACAGAGGCGAGCCCAGGCGAGG
CGGCAGACCATCAGGCATTCTACCAGGGAGAAGGACAGGGGACCCACGAAAGCCACCACC
ACCAAGCTGGTCTACCAGATCTTCGATACTTTCTTCGCAGAGCAAATTGAAAAGGATGAC
AGAGAAGACAAGGAGAACGCCTTTAAGCGCCGGCGATGTGGCGTCTGTGAGGTGTGTCAG
CAGCCTGAGTGTGGGAAATGTAAAGCCTGCAAGGACATGGTTAAATTTGGTGGCAGTGGA
CGGAGCAAGCAGGCTTGCCAAGAGCGGAGGTGTCCCAATATGGCCATGAAGGAGGCAGAT
GACGATGAGGAAGTCGATGATAACATCCCAGAGATGCCGTCACCCAAAAAAATGCACCAG
GGGAAGAAGAAGAAACAGAACAAGAATCGCATCTCTTGGGTCGGAGAAGCCGTCAAGACT
GATGGGAAGAAGAGTTACTATAAGAAGGTGTGCATTGATGCGGAAACCCTGGAAGTGGGG
GACTGTGTCTCTGTTATTCCAGATGATTCCTCAAAACCGCTGTATCTAGCAAGGGTCACG
GCGCTGTGGGAGGACAGCAGCAACGGGCAGATGTTTCACGCCCACTGGTTCTGCGCTGGG
ACAGACACAGTCCTCGGGGCCACGTCGGACCCTCTGGAGCTGTTCTTGGTGGATGAATGT
GAGGACATGCAGCTTTCATATATCCACAGCAAAGTGAAAGTCATCTACAAAGCCCCCTCC
GAAAACTGGGCCATGGAGGGAGGCATGGATCCCGAGTCCCTGCTGGAGGGGGACGACGGG
AAGACCTACTTCTACCAGCTGTGGTATGATCAAGACTACGCGAGATTCGAGTCCCCTCCA
AAAACCCAGCCAACAGAGGACAACAAGTTCAAATTCTGTGTGAGCTGTGCCCGTCTGGCT
GAGATGAGGCAAAAAGAAATCCCCAGGGTCCTGGAGCAGCTCGAGGACCTGGATAGCCGG
GTCCTCTACTACTCAGCCACCAAGAACGGCATCCTGTACCGAGTTGGTGATGGTGTGTAC
CTGCCCCCTGAGGCCTTCACGTTCAACATCAAGCTGTCCAGTCCCGTGAAACGCCCACGG
AAGGAGCCCGTGGATGAGGACCTGTACCCAGAGCACTACCGGAAATACTCCGACTACATC
AAAGGCAGCAACCTGGATGCCCCTGAGCCCTACCGAATTGGCCGGATCAAAGAGATCTTC
TGTCCCAAGAAGAGCAACGGCAGGCCCAATGAGACTGACATCAAAATCCGGGTCAACAAG
TTCTACAGGCCTGAGAACACCCACAAGTCCACTCCAGCGAGCTACCACGCAGACATCAAC
CTGCTCTACTGGAGCGACGAGGAGGCCGTGGTGGACTTCAAGGCTGTGCAGGGCCGCTGC
ACCGTGGAGTATGGGGAGGACCTGCCCGAGTGCGTCCAGGTGTACTCCATGGGCGGCCCC
AACCGCTTCTACTTCCTCGAGGCCTATAATGCAAAGAGCAAAAGCTTTGAAGATCCTCCC
AACCATGCCCGTAGCCCTGGAAACAAAGGGAAGGGCAAGGGAAAAGGGAAGGGCAAGCCC
AAGTCCCAAGCCTGTGAGCCGAGCGAGCCAGAGATAGAGATCAAGCTGCCCAAGCTGCGG
ACCCTGGATGTGTTTTCTGGCTGCGGGGGGTTGTCGGAGGGATTCCACCAAGCAGGCATC
TCTGACACGCTGTGGGCCATCGAGATGTGGGACCCTGCGGCCCAGGCGTTCCGGCTGAAC
AACCCCGGCTCCACAGTGTTCACAGAGGACTGCAACATCCTGCTGAAGCTGGTCATGGCT
GGGGAGACCACCAACTCCCGCGGCCAGCGGCTGCCCCAGAAGGGAGACGTGGAGATGCTG
TGCGGCGGGCCGCCCTGCCAGGGCTTCAGCGGCATGAACCGCTTCAATTCGCGCACCTAC
TCCAAGTTCAAAAACTCTCTGGTGGTTTCCTTCCTCAGCTACTGCGACTACTACCGGCCC
CGGTTCTTCCTCCTGGAGAATGTCAGGAACTTTGTCTCCTTCAAGCGCTCCATGGTCCTG
AAGCTCACCCTCCGCTGCCTGGTCCGCATGGGCTATCAGTGCACCTTCGGCGTGCTGCAG
GCCGGTCAGTACGGCGTGGCCCAGACTAGGAGGCGGGCCATCATCCTGGCCGCGGCCCCT
GGAGAGAAGCTCCCTCTGTTCCCGGAGCCACTGCACGTGTTTGCTCCCCGGGCCTGCCAG
CTGAGCGTGGTGGTGGATGACAAGAAGTTTGTGAGCAACATAACCAGGTTGAGCTCGGGT
CCTTTCCGGACCATCACGGTGCGAGACACGATGTCCGACCTGCCGGAGGTGCGGAATGGA
GCCTCGGCACTGGAGATCTCCTACAACGGGGAGCCTCAGTCCTGGTTCCAGAGGCAGCTC
CGGGGCGCACAGTACCAGCCCATCCTCAGGGACCACATCTGTAAGGACATGAGTGCATTG
GTGGCTGCCCGCATGCGGCACATCCCCTTGGCCCCAGGGTCAGACTGGCGCGATCTGCCC
AACATCGAGGTGCGGCTCTCAGACGGCACCATGGCCAGGAAGCTGCGGTATACCCACCAT
GACAGGAAGAACGGCCGCAGCAGCTCTGGGGCCCTCCGTGGGGTCTGCTCCTGCGTGGAA
GCCGGCAAAGCCTGCGACCCCGCAGCCAGGCAGTTCAACACCCTCATCCCCTGGTGCCTG
CCCCACACCGGGAACCGGCACAACCACTGGGCTGGCCTCTATGGAAGGCTCGAGTGGGAC
GGCTTCTTCAGCACAACCGTCACCAACCCCGAGCCCATGGGCAAGCAGGGCCGCGTGCTC
CACCCAGAGCAGCACCGTGTGGTGAGCGTGCGGGAGTGTGCCCGCTCCCAGGGCTTCCCT
GACACCTACCGGCTCTTCGGCAACATCCTGGACAAGCACCGGCAGGTGGGCAATGCCGTG
CCACCGCCCCTGGCCAAAGCCATTGGCTTGGAGATCAAGCTTTGTATGTTGGCCAAAGCC
CGAGAGAGTGCCTCAGCTAAAATAAAGGAGGAGGAAGCTGCTAAGGACTAG
Enzyme 26 GenBank Gene ID X63692 Link Image
Enzyme 26 GeneCard ID DNMT1 Link Image
Enzyme 26 GenAtlas ID DNMT1 Link Image
Enzyme 26 HGNC ID HGNC:2976 Link Image
Enzyme 26 Chromosome Location 19
Enzyme 26 Locus 19p13.2
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. Yen RW, Vertino PM, Nelkin BD, Yu JJ, el-Deiry W, Cumaraswamy A, Lennon GG, Trask BJ, Celano P, Baylin SB: Isolation and characterization of the cDNA encoding human DNA methyltransferase. Nucleic Acids Res. 1992 May 11;20(9):2287-91. [PubMed Link Image]
  2. Yoder JA, Yen RW, Vertino PM, Bestor TH, Baylin SB: New 5' regions of the murine and human genes for DNA (cytosine-5)-methyltransferase. J Biol Chem. 1996 Dec 6;271(49):31092-7. [PubMed Link Image]
  3. Hsu DW, Lin MJ, Lee TL, Wen SC, Chen X, Shen CK: Two major forms of DNA (cytosine-5) methyltransferase in human somatic tissues. Proc Natl Acad Sci U S A. 1999 Aug 17;96(17):9751-6. [PubMed Link Image]
  4. Bonfils C, Beaulieu N, Chan E, Cotton-Montpetit J, MacLeod AR: Characterization of the human DNA methyltransferase splice variant Dnmt1b. J Biol Chem. 2000 Apr 14;275(15):10754-60. [PubMed Link Image]
  5. Chuang LS, Ian HI, Koh TW, Ng HH, Xu G, Li BF: Human DNA-(cytosine-5) methyltransferase-PCNA complex as a target for p21WAF1. Science. 1997 Sep 26;277(5334):1996-2000. [PubMed Link Image]
  6. Tatematsu KI, Yamazaki T, Ishikawa F: MBD2-MBD3 complex binds to hemi-methylated DNA and forms a complex containing DNMT1 at the replication foci in late S phase. Genes Cells. 2000 Aug;5(8):677-88. [PubMed Link Image]
  7. Rountree MR, Bachman KE, Baylin SB: DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci. Nat Genet. 2000 Jul;25(3):269-77. [PubMed Link Image]
  8. Robertson KD, Ait-Si-Ali S, Yokochi T, Wade PA, Jones PL, Wolffe AP: DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses transcription from E2F-responsive promoters. Nat Genet. 2000 Jul;25(3):338-42. [PubMed Link Image]
  9. Robertson KD, Uzvolgyi E, Liang G, Talmadge C, Sumegi J, Gonzales FA, Jones PA: The human DNA methyltransferases (DNMTs) 1, 3a and 3b: coordinate mRNA expression in normal tissues and overexpression in tumors. Nucleic Acids Res. 1999 Jun 1;27(11):2291-8. [PubMed Link Image]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 7736
Enzyme 27 Name DNA
Enzyme 27 Synonyms
  1. cytosine-5-methyltransferase 3B
  2. Dnmt3b
  3. DNA methyltransferase HsaIIIB
  4. DNA MTase HsaIIIB
  5. M.HsaIIIB
Enzyme 27 Gene Name DNMT3B
Enzyme 27 Protein Sequence >DNA
MKGDTRHLNGEEDAGGREDSILVNGACSDQSSDSPPILEAIRTPEIRGRRSSSRLSKREV
SSLLSYTQDLTGDGDGEDGDGSDTPVMPKLFRETRTRSESPAVRTRNNNSVSSRERHRPS
PRSTRGRQGRNHVDESPVEFPATRSLRRRATASAGTPWPSPPSSYLTIDLTDDTEDTHGT
PQSSSTPYARLAQDSQQGGMESPQVEADSGDGDSSEYQDGKEFGIGDLVWGKIKGFSWWP
AMVVSWKATSKRQAMSGMRWVQWFGDGKFSEVSADKLVALGLFSQHFNLATFNKLVSYRK
AMYHALEKARVRAGKTFPSSPGDSLEDQLKPMLEWAHGGFKPTGIEGLKPNNTQPVVNKS
KVRRAGSRKLESRKYENKTRRRTADDSATSDYCPAPKRLKTNCYNNGKDRGDEDQSREQM
ASDVANNKSSLEDGCLSCGRKNPVSFHPLFEGGLCQTCRDRFLELFYMYDDDGYQSYCTV
CCEGRELLLCSNTSCCRCFCVECLEVLVGTGTAAEAKLQEPWSCYMCLPQRCHGVLRRRK
DWNVRLQAFFTSDTGLEYEAPKLYPAIPAARRRPIRVLSLFDGIATGYLVLKELGIKVGK
YVASEVCEESIAVGTVKHEGNIKYVNDVRNITKKNIEEWGPFDLVIGGSPCNDLSNVNPA
RKGLYEGTGRLFFEFYHLLNYSRPKEGDDRPFFWMFENVVAMKVGDKRDISRFLECNPVM
IDAIKVSAAHRARYFWGNLPGMNRPVIASKNDKLELQDCLEYNRIAKLKKVQTITTKSNS
IKQGKNQLFPVVMNGKEDVLWCTELERIFGFPVHYTDVSNMGRGARQKLLGRSWSVPVIR
HLFAPLKDYFACE
Enzyme 27 Number of Residues 853
Enzyme 27 Molecular Weight 95752
Enzyme 27 Theoretical pI 8.52
Enzyme 27 GO Classification
Function
  • DNA binding
  • binding
  • nucleic acid binding
Process
  • DNA alkylation
  • DNA metabolism
  • DNA methylation
  • DNA modification
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
Enzyme 27 General Function Not Available
Enzyme 27 Specific Function Required for genome wide de novo methylation and is essential for development. DNA methylation is coordinated with methylation of histones. Isoforms 4 and 5 are probably not functional due to the deletion of two conserved methyltransferase motifs
Enzyme 27 Pathways
Enzyme 27 Reactions
  • S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 5823166 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID Q9UBC3 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name DNM3B_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >2313 bp
ATGAAGGGAGACACCAGGCATCTCAATGGAGAGGAGGACGCCGGCGGGAGGGAAGACTCG
ATCCTCGTCAACGGGGCCTGCAGCGACCAGTCCTCCGACTCGCCCCCAATCCTGGAGGCT
ATCCGCACCCCGGAGATCAGAGGCCGAAGATCAAGCTCGCGACTCTCCAAGAGGGAGGTG
TCCAGTCTGCTAAGCTACACACAGGACTTGACAGGCGATGGCGACGGGGAAGATGGGGAT
GGCTCTGACACCCCAGTCATGCCAAAGCTCTTCCGGGAAACCAGGACTCGTTCAGAAAGC
CCAGCTGTCCGAACTCGAAATAACAACAGTGTCTCCAGCCGGGAGAGGCACAGGCCTTCC
CCACGTTCCACCCGAGGCCGGCAGGGCCGCAACCATGTGGACGAGTCCCCCGTGGAGTTC
CCGGCTACCAGGTCCCTGAGACGGCGGGCAACAGCATCGGCAGGAACGCCATGGCCGTCC
CCTCCCAGCTCTTACCTTACCATCGACCTCACAGACGACACAGAGGACACACATGGGACG
CCCCAGAGCAGCAGTACCCCCTACGCCCGCCTAGCCCAGGACAGCCAGCAGGGGGGCATG
GAGTCCCCGCAGGTGGAGGCAGACAGTGGAGATGGAGACAGTTCAGAGTATCAGGATGGG
AAGGAGTTTGGAATAGGGGACCTCGTGTGGGGAAAGATCAAGGGCTTCTCCTGGTGGCCC
GCCATGGTGGTGTCTTGGAAGGCCACCTCCAAGCGACAGGCTATGTCTGGCATGCGGTGG
GTCCAGTGGTTTGGCGATGGCAAGTTCTCCGAGGTCTCTGCAGACAAACTGGTGGCACTG
GGGCTGTTCAGCCAGCACTTTAATTTGGCCACCTTCAATAAGCTCGTCTCCTATCGAAAA
GCCATGTACCATGCTCTGGAGAAAGCTAGGGTGCGAGCTGGCAAGACCTTCCCCAGCAGC
CCTGGAGACTCATTGGAGGACCAGCTGAAGCCCATGTTGGAGTGGGCCCACGGGGGCTTC
AAGCCCACTGGGATCGAGGGCCTCAAACCCAACAACACGCAACCAGAGAACAAGACTCGA
AGACGCACAGCTGACGACTCAGCCACCTCTGACTACTGCCCCGCACCCAAGCGCCTCAAG
ACAAATTGCTATAACAACGGCAAAGACCGAGGGGATGAAGATCAGAGCCGAGAACAAATG
GCTTCAGATGTTGCCAACAACAAGAGCAGCCTGGAAGATGGCTGTTTGTCTTGTGGCAGG
AAAAACCCCGTGTCCTTCCACCCTCTCTTTGAGGGGGGGCTCTGTCAGACATGCCGGGAT
CGCTTCCTTGAGCTGTTTTACATGTATGATGACGATGGCTATCAGTCTTACTGCACTGTG
TGCTGCGAGGGCCGAGAGCTGCTGCTTTGCAGCAACACGAGCTGCTGCCGGTGTTTCTGT
GTGGAGTGCCTGGAGGTGCTGGTGGGCACAGGCACAGCGGCCGAGGCCAAGCTTCAGGAG
CCCTGGAGCTGCTACATGTGTCTCCCGCAGCGCTGTCATGGCGTCCTGCGGCGCCGGAAG
GACTGGAACGTGCGCCTGCAGGCCTTCTTCACCAGTGACACGGGGCTTGAATACGAAGCC
CCCAAGCTGTACCCTGCCATTCCCGCAGCCCGAAGGCGGCCCATTCGAGTCCTGTCATTG
TTTGATGGCATCGCGACAGGCTACCTAGTCCTCAAAGAGTTGGGCATAAAGGTAGGAAAG
TACGTCGCTTCTGAAGTGTGTGAGGAGTCCATTGCTGTTGGAACCGTGAAGCACGAGGGG
AATATCAAATACGTGAACGACGTGAGGAACATCACAAAGAAAAATATTGAAGAATGGGGC
CCATTTGACTTGGTGATTGGCGGAAGCCCATGCAACGATCTCTCAAATGTGAATCCAGCC
AGGAAAGGCCTGTATGAGGGTACAGGCCGGCTCTTCTTCGAATTTTACCACCTGCTGAAT
TACTCACGCCCCAAGGAGGGTGATGACCGGCCGTTCTTCTGGATGTTTGAGAATGTTGTA
GCCATGAAGGTTGGCGACAAGAGGGACATCTCACGGTTCCTGGAGTGTAATCCAGTGATG
ATTGATGCCATCAAAGTTTCTGCTGCTCACAGGGCCCGATACTTCTGGGGCAACCTACCC
GGGATGAACAGGATCTTTGGCTTTCCTGTGCACTACACAGACGTGTCCAACATGGGCCGT
GGTGCCCGCCAGAAGCTGCTGGGAAGGTCCTGGAGCGTGCCTGTCATCCGACACCTCTTC
GCCCCTCTGAAGGACTACTTTGCATGTGAATAG
Enzyme 27 GenBank Gene ID AF156487 Link Image
Enzyme 27 GeneCard ID DNMT3B Link Image
Enzyme 27 GenAtlas ID DNMT3B Link Image
Enzyme 27 HGNC ID HGNC:2979 Link Image
Enzyme 27 Chromosome Location 20
Enzyme 27 Locus 20q11.2
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. Xie S, Wang Z, Okano M, Nogami M, Li Y, He WW, Okumura K, Li E: Cloning, expression and chromosome locations of the human DNMT3 gene family. Gene. 1999 Aug 5;236(1):87-95. [PubMed Link Image]
  2. Xu GL, Bestor TH, Bourc'his D, Hsieh CL, Tommerup N, Bugge M, Hulten M, Qu X, Russo JJ, Viegas-Pequignot E: Chromosome instability and immunodeficiency syndrome caused by mutations in a DNA methyltransferase gene. Nature. 1999 Nov 11;402(6758):187-91. [PubMed Link Image]
  3. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  4. Robertson KD, Uzvolgyi E, Liang G, Talmadge C, Sumegi J, Gonzales FA, Jones PA: The human DNA methyltransferases (DNMTs) 1, 3a and 3b: coordinate mRNA expression in normal tissues and overexpression in tumors. Nucleic Acids Res. 1999 Jun 1;27(11):2291-8. [PubMed Link Image]
  5. Kang ES, Park CW, Chung JH: Dnmt3b, de novo DNA methyltransferase, interacts with SUMO-1 and Ubc9 through its N-terminal region and is subject to modification by SUMO-1. Biochem Biophys Res Commun. 2001 Dec 14;289(4):862-8. [PubMed Link Image]
  6. Okano M, Bell DW, Haber DA, Li E: DNA methyltransferases Dnmt3a and Dnmt3b are essential for de novo methylation and mammalian development. Cell. 1999 Oct 29;99(3):247-57. [PubMed Link Image]
  7. Hansen RS, Wijmenga C, Luo P, Stanek AM, Canfield TK, Weemaes CM, Gartler SM: The DNMT3B DNA methyltransferase gene is mutated in the ICF immunodeficiency syndrome. Proc Natl Acad Sci U S A. 1999 Dec 7;96(25):14412-7. [PubMed Link Image]
  8. Wijmenga C, Hansen RS, Gimelli G, Bjorck EJ, Davies EG, Valentine D, Belohradsky BH, van Dongen JJ, Smeets DF, van den Heuvel LP, Luyten JA, Strengman E, Weemaes C, Pearson PL: Genetic variation in ICF syndrome: evidence for genetic heterogeneity. Hum Mutat. 2000 Dec;16(6):509-17. [PubMed Link Image]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 8577
Enzyme 28 Name tRNA
Enzyme 28 Synonyms
  1. cytosine-5--methyltransferase
  2. DNA
  3. cytosine-5- methyltransferase-like protein 2
  4. Dnmt2
  5. DNA methyltransferase homolog HsaIIP
  6. DNA MTase homolog HsaIIP
  7. M.HsaIIP
  8. PuMet
Enzyme 28 Gene Name TRDMT1
Enzyme 28 Protein Sequence >tRNA
MEPLRVLELYSGVGGMHHALRESCIPAQVVAAIDVNTVANEVYKYNFPHTQLLAKTIEGI
TLEEFDRLSFDMILMSPPCQPFTRIGRQGDMTDSRTNSFLHILDILPRLQKLPKYILLEN
VKGFEVSSTRDLLIQTIENCGFQYQEFLLSPTSLGIPNSRLRYFLIAKLQSEPLPFQAPG
QVLMEFPKIESVHPQKYAMDVENKIQEKNVEPNISFDGSIQCSGKDAILFKLETAEEIHR
KNQQDSDLSVKMLKDFLEDDTDVNQYLLPPKSLLRYALLLDIVQPTCRRSVCFTKGYGSY
IEGTGSVLQTAEDVQVENIYKSLTNLSQEEQITKLLILKLRYFTPKEIANLLGFPPEFGF
PEKITVKQRYRLLGNSLNVHVVAKLIKILYE
Enzyme 28 Number of Residues 391
Enzyme 28 Molecular Weight 44597
Enzyme 28 Theoretical pI 5.95
Enzyme 28 GO Classification
Function
  • DNA binding
  • binding
  • nucleic acid binding
Process
  • DNA alkylation
  • DNA metabolism
  • DNA methylation
  • DNA modification
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
Enzyme 28 General Function Replication, recombination and repair
Enzyme 28 Specific Function Specifically methylates cytosine 38 in the anticodon loop of tRNA(Asp)
Enzyme 28 Pathways Not Available
Enzyme 28 Reactions
  • S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing 5-methylcytosine
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals Not Available
Enzyme 28 Transmembrane Regions Not Available
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein Not Available
Enzyme 28 UniProtKB/Swiss-Prot ID O14717 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name TRDMT_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence Not Available
Enzyme 28 GenBank Gene ID AF012128 Link Image
Enzyme 28 GeneCard ID TRDMT1 Link Image
Enzyme 28 GenAtlas ID TRDMT1 Link Image
Enzyme 28 HGNC ID HGNC:2977 Link Image
Enzyme 28 Chromosome Location 10
Enzyme 28 Locus 10p15.1
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References
  1. Yoder JA, Bestor TH: A candidate mammalian DNA methyltransferase related to pmt1p of fission yeast. Hum Mol Genet. 1998 Feb;7(2):279-84. [PubMed Link Image]
  2. Van den Wyngaert I, Sprengel J, Kass SU, Luyten WH: Cloning and analysis of a novel human putative DNA methyltransferase. FEBS Lett. 1998 Apr 17;426(2):283-9. [PubMed Link Image]
  3. Okano M, Xie S, Li E: Dnmt2 is not required for de novo and maintenance methylation of viral DNA in embryonic stem cells. Nucleic Acids Res. 1998 Jun 1;26(11):2536-40. [PubMed Link Image]
  4. Franchina M, Hooper J, Kay PH: Five novel alternatively spliced transcripts of DNA (cytosine-5) methyltransferase 2 in human peripheral blood leukocytes. Int J Biochem Cell Biol. 2001 Nov;33(11):1104-15. [PubMed Link Image]
  5. Dong A, Yoder JA, Zhang X, Zhou L, Bestor TH, Cheng X: Structure of human DNMT2, an enigmatic DNA methyltransferase homolog that displays denaturant-resistant binding to DNA. Nucleic Acids Res. 2001 Jan 15;29(2):439-48. [PubMed Link Image]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 11322
Enzyme 29 Name Histone-lysine N-methyltransferase SETDB2
Enzyme 29 Synonyms
  1. SET domain bifurcated 2
  2. Chronic lymphocytic leukemia deletion region gene 8 protein
Enzyme 29 Gene Name SETDB2
Enzyme 29 Protein Sequence >Histone-lysine N-methyltransferase SETDB2
MGEKNGDAKTFWMELEDDGKVDFIFEQVQNVLQSLKQKIKDGSATNKEYIQAMILVNEAT
IINSSTSIKGASQKEVNAQSSDPMPVTQKEQENKSNAFPSTSCENSFPEDCTFLTTENKE
ILSLEDKVVDFREKDSSSNLSYQSHDCSGACLMKMPLNLKGENPLQLPIKCHFQRRHAKT
NSHSSALHVSYKTPCGRSLRNVEEVFRYLLETECNFLFTDNFSFNTYVQLARNYPKQKEV
VSDVDISNGVESVPISFCNEIDSRKLPQFKYRKTVWPRAYNLTNFSSMFTDSCDCSEGCI
DITKCACLQLTARNAKTSPLSSDKITTGYKYKRLQRQIPTGIYECSLLCKCNRQLCQNRV
VQHGPQVRLQVFKTEQKGWGVRCLDDIDRGTFVCIYSGRLLSRANTEKSYGIDENGRDEN
TMKNIFSKKRKLEVACSDCEVEVLPLGLETHPRTAKTEKCPPKFSNNPKELTVETKYDNI
SRIQYHSVIRDPESKTAIFQHNGKKMEFVSSESVTPEDNDGFKPPREHLNSKTKGAQKDS
SSNHVDEFEDNLLIESDVIDITKYREETPPRSRCNQATTLDNQNIKKAIEVQIQKPQEGR
STACQRQQVFCDEELLSETKNTSSDSLTKFNKGNVFLLDATKEGNVGRFLNHSCCPNLLV
QNVFVETHNRNFPLVAFFTNRYVKARTELTWDYGYEAGTVPEKEIFCQCGVNKCRKKIL
Enzyme 29 Number of Residues 719
Enzyme 29 Molecular Weight 81895
Enzyme 29 Theoretical pI Not Available
Enzyme 29 GO Classification
Function
  • DNA binding
  • binding
  • catalytic activity
  • cation binding
  • histone-lysine N-methyltransferase activity
  • ion binding
  • methyltransferase activity
  • nucleic acid binding
  • protein methyltransferase activity
  • protein-lysine N-methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
  • transition metal ion binding
  • zinc ion binding
Process
  • DNA metabolism
  • DNA packaging
  • cellular metabolism
  • chromatin modification
  • establishment and/or maintenance of chromatin architecture
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 29 General Function Not Available
Enzyme 29 Specific Function Probable histone methyltransferase
Enzyme 29 Pathways
Enzyme 29 Reactions
  • Protein N6,N6-dimethyl-L-lysine + S-Adenosyl-L-methionine --> Protein N6,N6,N6-trimethyl-L-lysine + S-Adenosyl-L-homocysteine
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 13699244 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID Q96T68 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name SETB2_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence Not Available
Enzyme 29 GenBank Gene ID AF334407 Link Image
Enzyme 29 GeneCard ID Not Available
Enzyme 29 GenAtlas ID SETDB2 Link Image
Enzyme 29 HGNC ID HGNC:20263 Link Image
Enzyme 29 Chromosome Location Not Available
Enzyme 29 Locus Not Available
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References
  1. Mabuchi H, Fujii H, Calin G, Alder H, Negrini M, Rassenti L, Kipps TJ, Bullrich F, Croce CM: Cloning and characterization of CLLD6, CLLD7, and CLLD8, novel candidate genes for leukemogenesis at chromosome 13q14, a region commonly deleted in B-cell chronic lymphocytic leukemia. Cancer Res. 2001 Apr 1;61(7):2870-7. [PubMed Link Image]
  2. Zhang Y, Leaves NI, Anderson GG, Ponting CP, Broxholme J, Holt R, Edser P, Bhattacharyya S, Dunham A, Adcock IM, Pulleyn L, Barnes PJ, Harper JI, Abecasis G, Cardon L, White M, Burton J, Matthews L, Mott R, Ross M, Cox R, Moffatt MF, Cookson WO: Positional cloning of a quantitative trait locus on chromosome 13q14 that influences immunoglobulin E levels and asthma. Nat Genet. 2003 Jun;34(2):181-6. [PubMed Link Image]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 13061
Enzyme 30 Name Histamine N-methyltransferase
Enzyme 30 Synonyms
  1. Histamine N-methyltransferase, isoform CRA_b
Enzyme 30 Gene Name HNMT
Enzyme 30 Protein Sequence >Histamine N-methyltransferase
MASSMRSLFSDHGKYVESFRRFLNHSTEHQCMQEFMDKKLPGIIGRYQNCC
Enzyme 30 Number of Residues 51
Enzyme 30 Molecular Weight 6046
Enzyme 30 Theoretical pI 8.51
Enzyme 30 GO Classification Not Available
Enzyme 30 General Function Not Available
Enzyme 30 Specific Function Not Available
Enzyme 30 Pathways Not Available
Enzyme 30 Reactions Not Available
Enzyme 30 Pfam Domain Function Not Available
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • None
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 13543497 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID Q9BRW6 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name Q9BRW6_HUMAN Link Image
Enzyme 30 PDB ID 1JQD Link Image
Enzyme 30 PDB File Show
Enzyme 30 3D Structure
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence Not Available
Enzyme 30 GenBank Gene ID BC005907 Link Image
Enzyme 30 GeneCard ID Q9BRW6 Link Image
Enzyme 30 GenAtlas ID HNMT Link Image
Enzyme 30 HGNC ID HGNC:5028 Link Image
Enzyme 30 Chromosome Location Not Available
Enzyme 30 Locus Not Available
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 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]
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 13068
Enzyme 31 Name cDNA FLJ76252, highly similar to Homo sapiens S-adenosylhomocysteine hydrolase
Enzyme 31 Synonyms
  1. AHCY, mRNA
  2. S-adenosylhomocysteine hydrolase, isoform CRA_a
Enzyme 31 Gene Name AHCY
Enzyme 31 Protein Sequence >cDNA FLJ76252, highly similar to Homo sapiens S-adenosylhomocysteine hydrolase
MSDKLPYKVADIGLAAWGRKALDIAENEMPGLMRMRERYSASKPLKGARIAGCLHMTVET
AVLIETLVTLGAEVQWSSCNIFSTQDHAAAAIAKAGIPVYAWKGETDEEYLWCIEQTLYF
KDGPLNMILDDGGDLTNLIHTKYPQLLPGIRGISEETTTGVHNLYKMMANGILKVPAINV
NDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVI
ITEIDPINALQAAMEGYEVTTMDEACQEGNIFVTTTGCIDIILGRHFEQMKDDAIVCNIG
HFDVEIDVKWLNENAVEKVNIKPQVDRYRLKNGRRIILLAEGRLVNLGCAMGHPSFVMSN
SFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVAEAHLGKLNVKLTKLTEKQAQYLGMS
CDGPFKPDHYRY
Enzyme 31 Number of Residues 432
Enzyme 31 Molecular Weight 47717
Enzyme 31 Theoretical pI 6.29
Enzyme 31 GO Classification Not Available
Enzyme 31 General Function Coenzyme transport and metabolism
Enzyme 31 Specific Function Not Available
Enzyme 31 Pathways Not Available
Enzyme 31 Reactions Not Available
Enzyme 31 Pfam Domain Function Not Available
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • None
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 158261867 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID A8K307 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name A8K307_HUMAN Link Image
Enzyme 31 PDB ID 1LI4 Link Image
Enzyme 31 PDB File Show
Enzyme 31 3D Structure
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence Not Available
Enzyme 31 GenBank Gene ID AK290422 Link Image
Enzyme 31 GeneCard ID A8K307 Link Image
Enzyme 31 GenAtlas ID Not Available
Enzyme 31 HGNC ID Not Available
Enzyme 31 Chromosome Location Not Available
Enzyme 31 Locus Not Available
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 General References Not Available
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 14748
Enzyme 32 Name Probable histone-lysine N-methyltransferase ASH1L
Enzyme 32 Synonyms
  1. ASH1- like protein
  2. Absent small and homeotic disks protein 1 homolog
  3. huASH1
Enzyme 32 Gene Name ASH1L
Enzyme 32 Protein Sequence >Probable histone-lysine N-methyltransferase ASH1L
MDPRNTAMLGLGSDSEGFSRKSPSAISTGTLVSKREVELEKNTKEEEDLRKRNRERNIEA
GKDDGLTDAQQQFSVKETNFSEGNLKLKIGLQAKRTKKPPKNLENYVCRPAIKTTIKHPR
KALKSGKMTDEKNEHCPSKRDPSKLYKKADDVAAIECQSEEVIRLHSQGENNPLSKKLSP
VHSEMADYINATPSTLLGSRDPDLKDRALLNGGTSVTEKLAQLIATCPPSKSSKTKPKKL
GTGTTAGLVSKDLIRKAGVGSVAGIIHKDLIKKPTISTAVGLVTKDPGKKPVFNAAVGLV
NKDSVKKLGTGTTAVFINKNLGKKPGTITTVGLLSKDSGKKLGIGIVPGLVHKESGKKLG
LGTVVGLVNKDLGKKLGSTVGLVAKDCAKKIVASSAMGLVNKDIGKKLMSCPLAGLISKD
AINLKAEALLPTQEPLKASCSTNINNQESQELSESLKDSATSKTFEKNVVRQNKESILEK
FSVRKEIINLEKEMFNEGTCIQQDSFSSSEKGSYETSKHEKQPPVYCTSPDFKMGGASDV
STAKSPFSAVGESNLPSPSPTVSVNPLTRSPPETSSQLAPNPLLLSSTTELIEEISESVG
KNQFTSESTHLNVGHRSVGHSISIECKGIDKEVNDSKTTHIDIPRISSSLGKKPSLTSES
SIHTITPSVVNFTSLFSNKPFLKLGAVSASDKHCQVAESLSTSLQSKPLKKRKGRKPRWT
KVVARSTCRSPKGLELERSELFKNVSCSSLSNSNSEPAKFMKNIGPPSFVDHDFLKRRLP
KLSKSTAPSLALLADSEKPSHKSFATHKLSSSMCVSSDLLSDIYKPKRGRPKSKEMPQLE
GPPKRTLKIPASKVFSLQSKEEQEPPILQPEIEIPSFKQGLSVSPFPKKRGRPKRQMRSP
VKMKPPVLSVAPFVATESPSKLESESDNHRSSSDFFESEDQLQDPDDLDDSHRPSVCSMS
DLEMEPDKKITKRNNGQLMKTIIRKINKMKTLKRKKLLNQILSSSVESSNKGKVQSKLHN
TVSSLAATFGSKLGQQINVSKKGTIYIGKRRGRKPKTVLNGILSGSPTSLAVLEQTAQQA
AGSALGQILPPLLPSSASSSEILPSPICSQSSGTSGGQSPVSSDAGFVEPSSVPYLHLHS
RQGSMIQTLAMKKASKGRRRLSPPTLLPNSPSHLSELTSLKEATPSPISESHSDETIPSD
SGIGTDNNSTSDRAEKFCGQKKRRHSFEHVSLIPPETSTVLSSLKEKHKHKCKRRNHDYL
SYDKMKRQKRKRKKKYPQLRNRQDPDFIAELEELISRLSEIRITHRSHHFIPRDLLPTIF
RINFNSFYTHPSFPLDPLHYIRKPDLKKKRGRPPKMREAMAEMPFMHSLSFPLSSTGFYP
SYGMPYSPSPLTAAPIGLGYYGRYPPTLYPPPPSPSFTTPLPPPSYMHAGHLLLNPAKYH
KKKHKLLRQEAFLTTSRTPLLSMSTYPSVPPEMAYGWMVEHKHRHRHKHREHRSSEQPQV
SMDTGSSRSVLESLKRYRFGKDAVGERYKHKEKHRCHMSCPHLSPSKSLINREEQWVHRE
PSESSPLALGLQTPLQIDCSESSPSLSLGGFTPNSEPASSDEHTNLFTSAIGSCRVSNPN
SSGRKKLTDSPGLFSAQDTSLNRLHRKESLPSNERAVQTLAGSQPTSDKPSQRPSESTNC
SPTRKRSSSESTSSTVNGVPSRSPRLVASGDDSVDSLLQRMVQNEDQEPMEKSIDAVIAT
ASAPPSSSPGRSHSKDRTLGKPDSLLVPAVTSDSCNNSISLLSEKLTSSCSPHHIKRSVV
EAMQRQARKMCNYDKILATKKNLDHVNKILKAKKLQRQARTGNNFVKRRPGRPRKCPLQA
VVSMQAFQAAQFVNPELNRDEEGAALHLSPDTVTDVIEAVVQSVNLNPEHKKGLKRKGWL
LEEQTRKKQKPLPEEEEQENNKSFNEAPVEIPSPSETPAKPSEPESTLQPVLSLIPREKK
PPRPPKKKYQKAGLYSDVYKTTDPKSRLIQLKKEKLEYTPGEHEYGLFPAPIHVVFFVSG
KYLRQKRIDFQLPYDILWQWKHNQLYKKPDVPLYKKIRSNVYVDVKPLSGYEATTCNCKK
PDDDTRKGCVDDCLNRMIFAECSPNTCPCGEQCCNQRIQRHEWVQCLERFRAEEKGWGIR
TKEPLKAGQFIIEYLGEVVSEQEFRNRMIEQYHNHSDHYCLNLDSGMVIDSYRMGNEARF
INHSCDPNCEMQKWSVNGVYRIGLYALKDMPAGTELTYDYNFHSFNVEKQQLCKCGFEKC
RGIIGGKSQRVNGLTSSKNSQPMATHKKSGRSKEKRKSKHKLKKRRGHLSEEPSENINTP
TRLTPQLQMKPMSNRERNFVLKHHVFLVRNWEKIRQKQEEVKHTSDNIHSASLYTRWNGI
CRDDGNIKSDVFMTQFSALQTARSVRTRRLAAAEENIEVARAARLAQIFKEICDGIISYK
DSSRQALAAPLLNLPPKKKNADYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFR
NAEKYYGRKSPVGRDVCRLRKAYYNARHEASAQIDEIVGETASEADSSETSVSEKENGHE
KDDDVIRCICGLYKDEGLMIQCDKCMVWQHCDCMGVNSDVEHYLCEQCDPRPVDREVPMI
PRPHYAQPGCVYFICLLRDDLLLRQGDCVYLMRDSRRTPDGHPVRQSYRLLSHINRDKLD
IFRIEKLWKNEKEERFAFGHHYFRPHETHHSPSRRFYHNELFRVPLYEIIPLEAVVGTCC
VLDLYTYCKGRPKGVKEQDVYICDYRLDKSAHLFYKIHRNRYPVCTKPYAFDHFPKKLTP
KKDFSPHYVPDNYKRNGGRSSWKSERSKPPLKDLGQEDDALPLIEEVLASQEQAANEIPS
LEEPEREGATANVSEGEKKTEESSQEPQSTCTPEERRHNQRERLNQILLNLLEKIPGKNA
IDVTYLLEEGSGRKLRRRTLFIPENSFRK
Enzyme 32 Number of Residues 2969
Enzyme 32 Molecular Weight 332793
Enzyme 32 Theoretical pI 9.95
Enzyme 32 GO Classification
Function
  • DNA binding
  • binding
  • cation binding
  • ion binding
  • nucleic acid binding
  • protein binding
  • transition metal ion binding
  • zinc ion binding
Process
  • regulation of biological process
  • regulation of cellular metabolism
  • regulation of metabolism
  • regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • regulation of physiological process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
Enzyme 32 General Function Not Available
Enzyme 32 Specific Function Histone methyltransferase. Probably methylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation
Enzyme 32 Pathways
Enzyme 32 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938] ALL_REAC R03938
  • (other) R03875 R04866 R04867
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • None
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 7739725 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID Q9NR48 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name ASH1L_HUMAN Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence >8910 bp
ATGGACCCTAGAAATACTGCTATGTTAGGATTGGGTTCTGATTCCGAAGGTTTTTCAAGA
AAGAGTCCTTCTGCCATCAGTACTGGCACATTGGTCAGTAAGAGAGAAGTAGAGCTAGAA
AAAAACACAAAGGAGGAAGAGGACCTTCGCAAACGGAATCGAGAAAGAAACATCGAAGCT
GGGAAAGATGATGGTTTGACTGATGCACAGCAACAGTTTTCAGTGAAAGAAACAAACTTT
TCAGAGGGAAATTTAAAATTGAAAATTGGCCTCCAGGCTAAGAGAACTAAAAAACCTCCA
AAGAACTTGGAGAACTATGTATGTCGACCTGCCATAAAAACAACTATTAAGCACCCAAGG
AAAGCACTTAAAAGTGGAAAGATGACGGATGAAAAGAATGAACACTGTCCTTCAAAACGA
GACCCTTCAAAGTTGTACAAGAAAGCAGATGATGTTGCAGCCATTGAATGCCAGTCTGAA
GAAGTCATCCGTCTTCATTCACAGGGAGAAAACAATCCTTTGTCTAAGAAGCTGTCTCCA
GTACACTCAGAAATGGCAGATTATATTAATGCAACGCCATCTACTCTTCTTGGTAGCCGG
GATCCTGATTTAAAGGACAGAGCATTACTTAATGGAGGAACTAGTGTAACAGAAAAGTTG
GCACAGCTGATTGCTACCTGTCCTCCTTCCAAGTCTTCCAAGACAAAACCGAAGAAGTTA
GGAACTGGCACTACAGCAGGATTGGTTAGCAAGGATTTGATCAGGAAAGCAGGTGTTGGC
TCTGTAGCTGGAATAATACATAAGGACTTAATAAAAAAGCCAACCATCAGCACAGCAGTT
GGATTGGTAACTAAAGATCCTGGGAAAAAGCCAGTGTTTAATGCAGCAGTAGGATTGGTC
AATAAGGACTCTGTGAAAAAACTGGGAACTGGCACTACAGCGGTATTCATTAATAAAAAC
TTAGGCAAAAAGCCAGGAACTATCACTACAGTAGGACTGCTAAGCAAAGATTCAGGAAAG
AAGCTAGGAATTGGTATTGTTCCAGGTTTAGTGCATAAAGAGTCTGGCAAGAAGTTAGGA
CTTGGCACTGTGGTTGGACTGGTTAATAAAGATTTGGGAAAGAAATTGGGTTCTACTGTT
GGCCTAGTGGCCAAGGACTGTGCAAAGAAGATTGTAGCAAGTTCAGCAATGGGATTGGTT
AATAAGGACATTGGAAAGAAACTAATGAGTTGTCCTTTGGCAGGTCTGATCAGTAAAGAT
GCCATAAACCTTAAAGCCGAAGCACTGCTCCCCACTCAGGAACCGCTTAAGGCTTCTTGT
AGTACAAACATCAATAATCAGGAAAGTCAGGAACTTTCTGAATCCCTGAAAGATAGTGCC
ACCAGCAAAACTTTTGAAAAGAATGTTGTACGGCAGAATAAAGAAAGCATATTGGAAAAG
TTCTCAGTACGAAAAGAAATCATTAATTTGGAGAAAGAAATGTTTAATGAAGGAACATGC
ATTCAGCAAGACAGTTTCTCATCCAGTGAAAAGGGATCTTATGAAACCTCAAAGCATGAA
AAGCAGCCTCCTGTATATTGCACTTCTCCGGACTTTAAAATGGGAGGTGCTTCTGATGTA
TCTACCGCTAAATCCCCATTCAGTGCAGTAGGAGAAAGCAATCTCCCTTCCCCATCACCT
ACTGTATCTGTTAATCCTTTAACCAGAAGTCCCCCTGAAACTTCTTCACAGTTGGCTCCT
AATCCATTACTTTTAAGTTCTACTACAGAACTAATCGAAGAAATTTCTGAATCTGTTGGA
AAGAACCAGTTTACTTCTGAAAGTACCCACTTGAACGTTGGTCATAGGTCAGTTGGTCAT
AGTATAAGTATTGAATGTAAAGGGATTGATAAAGAGGTAAATGATTCAAAAACTACCCAT
ATAGATATTCCAAGAATAAGCTCTTCCCTTGGAAAAAAGCCAAGTTTGACTTCTGAATCC
AGCATTCATACTATTACTCCTTCAGTTGTTAACTTCACTAGTTTATTTAGTAATAAGCCT
TTTTTAAAACTGGGTGCAGTATCTGCATCAGACAAACACTGCCAAGTTGCTGAAAGCCTA
AGTACTAGTTTGCAGTCCAAACCATTAAAAAAAAGAAAAGGAAGAAAACCTCGGTGGACT
AAAGTGGTGGCAAGAAGCACATGCCGGTCTCCAAAAGGGCTAGAATTAGAAAGATCAGAG
CTTTTTAAAAACGTTTCATGTAGCTCACTATCAAATAGTAATTCTGAGCCAGCCAAGTTT
ATGAAAAACATTGGACCCCCTTCATTTGTAGATCATGACTTCCTTAAACGCCGATTGCCA
AAGTTGAGCAAATCCACAGCTCCATCTCTTGCTCTCTTAGCTGATAGTGAAAAACCATCT
CATAAGTCTTTTGCTACTCACAAACTATCCTCCAGTATGTGTGTCTCTAGTGACCTTTTG
TCTGATATTTATAAGCCCAAAAGAGGAAGGCCTAAATCTAAGGAGATGCCTCAACTGGAA
GGGCCACCTAAAAGGACTTTAAAAATCCCTGCTTCTAAAGTGTTTTCTTTACAGTCTAAG
GAAGAACAAGAACCCCCAATTTTACAGCCAGAAATTGAAATCCCTTCCTTCAAACAAGGT
CTGTCTGTGTCTCCTTTTCCAAAAAAGAGAGGCAGGCCTAAGAGGCAAATGAGGTCACCA
GTCAAGATGAAGCCACCTGTACTGTCAGTGGCTCCATTTGTTGCCACTGAAAGTCCAAGC
AAGCTAGAATCTGAAAGTGACAACCATAGAAGTAGCAGTGATTTCTTTGAGAGCGAGGAT
CAACTTCAGGATCCAGATGACCTAGATGACAGTCATAGGCCAAGTGTCTGTAGTATGAGT
GACCTTGAGATGGAACCAGATAAAAAAATTACCAAGAGAAACAATGGACAATTAATGAAA
ACAATTATCCGCAAAATAAATAAAATGAAGACTTTAAAGAGAAAGAAACTGTTGAATCAG
ATTCTTTCAAGTTCTGTAGAATCAAGTAATAAAGGGAAAGTGCAATCCAAACTCCATAAT
ACGGTATCAAGTCTTGCTGCCACATTTGGCTCTAAATTGGGCCAACAGATAAATGTCAGC
AAGAAAGGAACCATTTATATAGGAAAGAGAAGAGGTCGCAAACCAAAAACTGTCTTAAAT
GGTATTCTTTCTGGTAGTCCTACTAGCCTTGCTGTTCTTGAGCAAACAGCTCAACAGGCA
GCTGGGTCAGCATTAGGACAGATTCTTCCCCCATTACTGCCTTCATCTGCTAGTAGTTCT
GAGATTCTTCCATCACCTATTTGCTCTCAGTCTTCTGGGACTAGTGGAGGTCAGAGCCCT
GTAAGTAGTGATGCAGGTTTTGTTGAACCCAGTTCAGTGCCATATTTGCATTTACACTCC
AGACAGGGCAGTATGATTCAGACTCTTGCAATGAAGAAGGCCTCAAAGGGGAGGAGGCGG
TTATCTCCTCCTACTTTGTTGCCAAATTCTCCTTCGCACTTGAGTGAACTCACATCTCTA
AAAGAAGCTACTCCTTCCCCAATCAGTGAGTCTCATAGTGATGAGACCATTCCCAGTGAT
AGTGGAATTGGAACAGATAATAACAGCACATCAGACAGGGCAGAGAAATTTTGTGGGCAA
AAAAAGAGGAGGCATTCTTTTGAGCATGTTTCTCTGATTCCCCCTGAAACCTCTACAGTG
CTAAGCAGTCTTAAAGAAAAACATAAACACAAATGTAAGCGCAGGAATCATGATTACCTC
AGCTATGACAAGATGAAAAGGCAGAAACGAAAACGGAAAAAGAAATATCCCCAGCTTCGA
AATAGACAGGATCCAGACTTTATTGCAGAGCTGGAGGAACTAATAAGTCGCCTAAGTGAA
ATTCGGATCACTCATCGAAGTCATCATTTTATCCCCCGAGATCTTCTGCCAACTATCTTT
CGAATCAACTTTAATAGTTTCTATACACATCCTTCTTTCCCCTTAGACCCTTTGCACTAC
ATTCGAAAACCTGACTTAAAAAAGAAAAGAGGGAGACCCCCTAAGATGAGGGAGGCAATG
GCTGAAATGCCTTTTATGCACAGCCTTAGTTTTCCTCTTTCTAGTACTGGATTCTATCCA
TCTTATGGTATGCCTTACTCTCCTTCACCCCTTACAGCTGCTCCCATAGGATTAGGTTAC
TATGGAAGGTATCCTCCCACTCTTTATCCACCTCCTCCATCTCCTTCTTTCACCACGCCA
CTTCCACCTCCTTCCTATATGCATGCTGGTCATTTACTTCTCAATCCTGCCAAATACCAT
AAGAAAAAGCATAAGCTACTTCGACAGGAGGCCTTTCTTACAACCAGCAGGACTCCCCTC
CTTTCCATGAGTACCTACCCCAGTGTTCCTCCTGAGATGGCCTATGGTTGGATGGTTGAG
CACAAACACAGGCACCGTCACAAACACAGAGAACACCGTTCTTCTGAACAACCCCAGGTT
TCTATGGACACTGGCTCTTCCCGATCTGTCCTGGAATCTTTGAAGCGCTATAGATTTGGA
AAGGATGCTGTTGGAGAGCGATATAAGCATAAGGAAAAGCACCGTTGTCACATGTCCTGC
CCTCATCTCTCTCCTTCAAAAAGCTTAATAAACAGAGAGGAACAGTGGGTCCACCGAGAG
CCTTCAGAATCTAGTCCATTGGCCTTGGGATTGCAGACACCTTTACAGATTGACTGTTCA
GAAAGTTCTCCAAGCTTATCCCTTGGAGGATTCACTCCCAACTCTGAGCCAGCCAGCAGT
GATGAACATACAAACCTTTTCACAAGTGCAATAGGCAGCTGCAGAGTTTCAAACCCTAAC
TCCAGTGGCCGGAAGAAATTAACTGACAGCCCTGGACTCTTTTCTGCACAGGACACTTCA
CTAAATCGGCTTCACAGAAAGGAGTCACTGCCTTCTAACGAAAGGGCAGTACAGACTTTG
GCAGGCTCCCAGCCAACCTCTGATAAACCCTCCCAGCGGCCATCAGAGAGCACAAATTGT
AGCCCTACCCGGAAAAGGTCTTCATCTGAGAGTACTTCTTCAACAGTAAACGGAGTTCCC
TCTCGAAGTCCAAGATTAGTTGCTTCTGGGGATGACTCTGTGGATAGTCTGCTGCAGCGG
ATGGTACAAAATGAGGACCAAGAGCCCATGGAGAAAAGTATTGATGCTGTGATTGCAACT
GCCTCTGCACCACCTTCTTCCAGTCCAGGCCGTAGCCACAGCAAGGACCGAACCCTGGGA
AAACCAGACAGCCTTTTAGTGCCTGCAGTCGCAAGTGACTCTTGCAATAATAGCATCTCA
CTCCTATCTGAAAAGTTGACAAGCAGCTGTTCCCCCCATCATATCAAGAGAAGTGTAGTG
GAAGCTATGCAACGCCAAGCTCGGAAAATGTGCAATTACGACAAAATCTTGGCCACAAAG
AAAAACCTAGACCATGTCAATAAAATCTTAAAAGCCAAAAAACTTCAAAGGCAGGCCAGG
ACAGGGAATAACTTTGTGAAACGTAGGCCAGGTCGACCTCGGAAATGTCCCCTTCAGGCT
GTCGTATCAATGCAAGCATTCCAGGCTGCTCAGTTTGTCAACCCAGAATTGAACAGAGAC
GAGGAAGGAGCAGCACTGCACCTCAGTCCTGACACAGTTACAGATGTAATTGAGGCTGTT
GTTCAGAGTGTAAATCTGAACCCAGAACATAAAAAGGGGTTGAAGAGAAAAGGTTGGCTA
TTGGAAGAACAGACCAGAAAAAAGCAGAAGCCATTACCAGAGGAAGAAGAGCAAGAGAAT
AATAAAAGCTTTAATGAAGCACCAGTTGAGATTCCCAGTCCTTCTGAAACCCCAGCTAAA
CCTTCTGAACCTGAAAGTACCTTGCAGCCTGTGCTTTCTCTCATCCCAAGGGAAAAGAAG
CCCCCACGTCCCCCAAAGAAGAAGTATCAGAAAGCAGGGCTGTATTCTGACGTTTACAAA
ACTACAGACCCAAAGAGTCGATTGATCCAATTAAAGAAAGAGAAGCTGGAGTATACTCCA
GGAGAGCATGAATATGGATTATTTCCAGCGCCCATTCATGTTGTGTTTTTTGTTTCAGGA
AAGTATCTAAGACAAAAGAGAATTGACTTCCAGCTTCCTTATGATATCCTTTGGCAGTGG
AAACACAATCAGCTATACAAAAAGCCAGATGTCCCACTATATAAGAAAATTCGTTCAAAT
GTCTACGTTGATGTCAAACCCCTTTCTGGTTACGAAGCTACCACCTGTAACTGTAAGAAG
CCAGATGATGACACCAGGAAGGGCTGTGTTGATGACTGCCTCAATAGAATGATCTTTGCT
GAGTGTTCCCCCAACACTTGCCCATGTGGCGAGCAATGCTGTAACCAGAGGATACAGAGG
CATGAATGGGTGCAATGTCTAGAACGATTTCGAGCTGAGGAAAAAGGTTGGGGAATCAGA
ACCAAAGAGCCCCTAAAAGCTGGGCAGTTCATCATTGAATACCTAGGGGAGGTCGTCAGT
GAACAGGAGTTCAGGAACAGGATGATTGAGCAGTATCATAATCACAGTGACCACTACTGC
CTGAACCTGGATAGTGGGATGGTGATTGACAGTTACCGCATGGGAAATGAGGCCCGATTC
ATCAACCATAGCTGTGACCCAAATTGTGAAATGCAGAAATGGTCTGTTAATGGAGTATAC
CGGATTGGACTCTATGCTCTTAAAGACATGCCAGCTGGGACTGAACTCACTTATGATTAT
AACTTTCATTCCTTCAATGTGGAAAAACAGCAACTTTGTAAGTGTGGCTTTGAGAAATGT
CGAGGAATCATCGGAGGCAAGAGTCAGCGTGTGAATGGACTCACCAGCAGCAAAAACAGC
CAGCCCATGGCCACACACAAAAAATCTGGACGGTCAAAAGAGAAGAGAAAGTCTAAGCAC
AAGCTGAAGAAAAGGAGAGGCCATCTCTCTGAGGAACCCAGTGAAAATATCAACACCCCA
ACTAGATTGACCCCCCAATTACAGATGAAGCCAATGTCCAATCGTGAAAGGAACTTTGTG
TTAAAGCATCATGTATTCTTGGTCCGAAACTGGGAGAAGATTCGTCAAAAACAGGAGGAA
GTAAAGCACACCAGTGATAATATTCACTCAGCATCATTATATACCCGTTGGAATGGGATC
TGCCGAGATGATGGGAATATCAAGTCTGATGTCTTCATGACCCAGTTCTCTGCCCTGCAG
ACAGCTCGATCTGTTCGAACAAGACGGTTGGCAGCTGCAGAGGAAAATATTGAAGTGGCT
CGGGCAGCCCGCCTAGCCCAGATCTTCAAAGAAATTTGTGATGGTATCATCTCTTATAAA
GATTCTTCCCGGCAAGCACTGGCAGCTCCACTTTTGAACCTTCCCCCAAAGAAAAAGAAT
GCTGATTATTATGAGAAGATCTCTGATCCCCTAGATCTTATCACCATAGAGAAGCAGATC
CTCACTGGTTACTATAAGACAGTGGAAGCTTTTGATGCTGACATGCTCAAAGTCTTTCGG
AATGCTGAGAAGTACTATGGGCGTAAATCCCCAGTTGGGAGAGATGTTTGTCGTCTACGA
AAGGCCTATTACAATGCCCGGCATGAGGCATCAGCCCAGATTGATGAGATTGTGGGAGAG
ACAGCAAGTGAGGCAGACAGCAGTGAGACCTCAGTCTCTGAAAAGGAGAATGGGCATGAG
AAGGACGACGATGTTATTCGCTGTATCTGTGGCCTCTACAACGATGAAGGTCTCATGATC
CAGTGTGACAAGTGCATGGTATGGCAGCACTGTGATTGTATGGGAGTGAACTCAGATGTG
GAGCACTACCTTTGTGAGCAGTGTGACCCAAGGCCTGTGGACAGGGAGGTTCCCATGATC
CCTCGGCCCCACTATGCCCAACCTGGCTGTGTCTACTTCATCTGTTTGCTCCGAGATGAC
TTGCTGCTTCGTCAGGGTGACTGTGTGTATCTGATGAGGGATAGTCGGCGCACCCCTGAT
GGCCACCCGGTCCGTCAGTCCTATCGACTGTTATCTCACATTAACCGACATAAACTTGAC
ATCTTTCGCATTGAGAAGCTTTGGAAGAATGAAAAAGAGGAACGGTTTGCCTTTGGTCAC
CATTATTTCCGTCCCCACGAAACACACCACTCTCCATCCCGTCGGTTCTATCATAATGAA
CTATTTCGGGTGCCACTCTATGAGATCATTCCCTTGGAGGCTGTAGTGGGGACCTGCTGT
GTGTTGGACCTTTATACGTATTGTAAAGGGAGACCCAAAGGAGTAAAGGAGCAAGATGTG
TACATCTGTGATTATCGGCTTGACAAGTCAGCACACCTGTTTTACAAGATCCACCGGAAC
CGCTATCCTGTCTGCACCAAACCCTATGCTTTTGATCACTTCCCCAAGAAGCTCACTCCC
AAAAAAGATTTCTCGCCTCATTACGTCCCAGACAACTACAAGAGGAATGGAGGACGATCA
TCCTGGAAGTCTGAGCGCTCAAAGCCACCCCTAAAAGACTTGGGCCAGGAGGATGATGCT
CTACCCTTGATTGAAGAGGTTCTAGCCAGTCAAGAGCAAGCAGCCAATGAGATACCCAGC
CTGGAGGAGCCAGAACGGGAAGGGGCCACTGCTAACGTCAGTGAGGGTGAAAAAAAAACA
GAGGAAAGTAGTCAAGAACCCCAGTCAACCTGTACCCCTGAGGAACGACGGCATAACCAA
CGGGAACGACTCAACCAGATCTTGCTCAATCTCCTTGAAAAAATCCCTGGAAAAAATGCC
ATTGATGTGACCTACTTGCTGGAGGAAGGATCAGGCAGGAAACTGCGAAGGCGTACTTTG
TTTATCCCAGAAAACAGCTTTCGAAAGTGA
Enzyme 32 GenBank Gene ID AF257305 Link Image
Enzyme 32 GeneCard ID Q9NR48 Link Image
Enzyme 32 GenAtlas ID ASH1L Link Image
Enzyme 32 HGNC ID HGNC:19088 Link Image
Enzyme 32 Chromosome Location Not Available
Enzyme 32 Locus Not Available
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References
  1. Nakamura T, Blechman J, Tada S, Rozovskaia T, Itoyama T, Bullrich F, Mazo A, Croce CM, Geiger B, Canaani E: huASH1 protein, a putative transcription factor encoded by a human homologue of the Drosophila ash1 gene, localizes to both nuclei and cell-cell tight junctions. Proc Natl Acad Sci U S A. 2000 Jun 20;97(13):7284-9. [PubMed Link Image]
  2. Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Feb 28;7(1):65-73. [PubMed Link Image]
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 14765
Enzyme 33 Name Histone-lysine N-methyltransferase NSD3
Enzyme 33 Synonyms
  1. Nuclear SET domain-containing protein 3
  2. WHSC1-like protein 1
  3. Wolf-Hirschhorn syndrome candidate 1-like protein 1
  4. Whistle
  5. WHSC1-like 1 isoform 9 with methyltransferase activity to lysine
Enzyme 33 Gene Name WHSC1L1
Enzyme 33 Protein Sequence >Histone-lysine N-methyltransferase NSD3
MDFSFSFMQGIMGNTIQQPPQLIDSANIRQEDAFDNNSDIAEDGGQTPYEATLQQGFQYP
ATTEDLPPLTNGYPSSISVYETQTKYQSYNQYPNGSANGFGAVRNFSPTDYYHSEIPNTR
PHEILEKPSPPQPPPPPSVPQTVIPKKTGSPEIKLKITKTIQNGRELFESSLCGDLLNEV
QASEHTKSKHESRKEKRKKSNKHDSSRSEERKSHKIPKLEPEEQNRPNERVDTVSEKPRE
EPVLKEEAPVQPILSSVPTTEVSTGVKFQVGDLVWSKVGTYPWWPCMVSSDPQLEVHTKI
NTRGAREYHVQFFSNQPERAWVHEKRVREYKGHKQYEELLAEATKQASNHSEKQKIRKPR
PQRERAQWDIGIAHAEKALKMTREERIEQYTFIYIDKQPEEALSQAKKSVASKTEVKKTR
RPRSVLNTQPEQTNAGEVASSLSSTEIRRHSQRRHTSAEEEEPPPVKIAWKTAAARKSLP
ASITMHKGSLDLQKCNMSPVVKIEQVFALQNATGDGKFIDQFVYSTKGIGNKTEISVRGQ
DRLIISTPNQRNEKPTQSVSSPEATSGSTGSVEKKQQRRSIRTRSESEKSTEVVPKKKIK
KEQVETVPQATVKTGLQKGASEISDSCKPLKKRSRASTDVEMTSSAYRDTSDSDSRGLSD
LQVGFGKQVDSPSATADADVSDVQSMDSSLSRRGTGMSKKDTVCQICESSGDSLIPCEGE
CCKHFHLECLGLASLPDSKFICMECKTGQHPCFSCKVSGKDVKRCSVGACGKFYHEACVR
KFPTAIFESKGFRCPQHCCSACSMEKDIHKASKGRMMRCLRCPVAYHSGDACIAAGSMLV
SSYILICSNHSKRSSNSSAVNVGFCFVCARGLIVQDHSDPMFSSYAYKSHYLLNESNRAE
LMKLPMIPSSSASKKKCEKGGRLLCCESCPASFHPECLSIEMPEGCWNCNDCKAGKKLHY
KQIVWVKLGNYRWWPAEICNPRSVPLNIQGLKHDLGDFPVFFFGSHDYYWVHQGRVFPYV
EGDKSFAEGQTSINKTFKKALEEAAKRFQELKAQRESKEALEIEKNSRKPPPYKHIKANK
VIGKVQIQVADLSEIPRCNCKPADENPCGLESECLNRMLQYECHPQVCPAGDRCQNQCFT
KRLYPDAEIIKTERRGWGLRTKRSIKKGEFVNEYVGELIDEEECRLRIKRAHENSVTNFY
MLTVTKDRIIDAGPKGNYSRFMNHSCNPNCETQKWTVNGDVRVGLFALCDIPAGMELTFN
YNLDCLGNGRTECHCGADNCSGFLGVRPKSACASTNEEKAKNAKLKQKRRKIKTEPKQMH
EDYCFQCGDGGELVMCDKKDCPKAYHLLCLNLTQPPYGKWECPWHQCDECSSAAVSFCEF
CPHSFCKDHEKGALVPSALEGRLCCSEHDPMAPVSPEYWSKIKCKWESQDHGEEVKE
Enzyme 33 Number of Residues 1437
Enzyme 33 Molecular Weight 161614
Enzyme 33 Theoretical pI 8.26
Enzyme 33 GO Classification
Function
  • acid-amino acid ligase activity
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • protein binding
  • transition metal ion binding
  • ubiquitin-protein ligase activity
  • zinc ion binding
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein modification
  • protein ubiquitination
  • regulation of biological process
  • regulation of cellular metabolism
  • regulation of metabolism
  • regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • regulation of physiological process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
  • ubiquitin cycle
Component
  • protein complex
  • ubiquitin ligase complex
Enzyme 33 General Function Not Available
Enzyme 33 Specific Function Histone methyltransferase. Preferentially methylates 'Lys-4' and 'Lys-27' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation, while 'Lys-27' is a mark for transcriptional repression
Enzyme 33 Pathways
Enzyme 33 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938] ALL_REAC R03938
  • (other) R03875 R04866 R04867
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • None
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 12642815 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID Q9BZ95 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name NSD3_HUMAN Link Image
Enzyme 33 PDB ID Not Available
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence >1938 bp
ATGGATTTCTCTTTCTCTTTCATGCAAGGGATCATGGGAAACACAATTCAGCAACCACCT
CAACTCATTGACTCCGCCAACATCCGTCAGGAGGATGCCTTTGATAACAACAGTGACATT
GCTGAAGATGGTGGCCAGACACCATATGAAGCTACTTTGCAGCAAGGCTTTCAGTACCCA
GCTACAACAGAAGATCTTCCTCCACTCACAAATGGGTATCCATCATCAATCAGTGTGTAT
GAAACTCAAACCAAATACCAGTCATATAATCAGTATCCTAATGGGTCAGCCAATGGCTTT
GGTGCAGTTAGAAACTTTAGCCCCACTGACTATTATCATTCAGAAATTCCAAACACAAGA
CCACATGAAATTCTGGAAAAACCTTCCCCTCCACAGCCACCACCTCCTCCTTCGGTACCA
CAAACTGTGATTCCAAAGAAGACTGGCTCACCTGAAATTAAACTAAAAATAACCAAAACT
ATCCAGAATGGCAGGGAATTGTTTGAGTCTTCCCTTTGTGGAGACCTTTTAAATGAAGTA
CAGGCAAGTGAGCACACGAAATCAAAGCATGAAAGCAGAAAAGAAAAGAGGAAAAAAAGC
AACAAGCATGACTCATCAAGATCTGAAGAGCGCAAGTCACACAAAATCCCCAAATTAGAA
CCAGAGGAACAAAATAGACCAAATGAGAGGGTTGACACTGTATCAGAAAAACCAAGGGAA
GAACCAGTACTAAAAGAGGAAGCCCCAGTTCAGCCAATACTATCTTCTGTTCCAACAACG
GAAGTGTCCACTGGTGTTAAGTTTCAGGTTGGCGATCTTGTGTGGTCCAAGGTGGGAACC
TATCCTTGGTGGCCTTGTATGGTTTCAAGTGATCCCCAGCTTGAGGTTCATACTAAAATT
AACACAAGAGGTGCCCGAGAATATCATGTCCAGTTTTTTAGCAACCAGCCAGAGAGGGCG
TGGGTTCATGAAAAACGGGTACGAGAGTATAAAGGTCATAAACAGTATGAAGAATTACTG
GCTGAGGCAACCAAACAAGCCAGCAATCACTCTGAGAAACAAAAGATTCGGAAACCCCGA
CCTCAGAGAGAACGTGCTCAGTGGGATATTGGCATTGCCCATGCAGAGAAAGCATTGAAA
ATGACTCGAGAAGAAAGAATAGAACAGTATACTTTTATTTACATTGATAAACAGCCTGAA
GAGGCTTTATCCCAAGCAAAAAAGAGTGTTGCCTCCAAAACCGAAGTTAAAAAAACCCGA
CGACCAAGATCTGTGCTGAATACTCAGCCAGAACAGACCAATGCAGGGGAGGTGGCCTCC
TCACTCTCAAGTACTGAAATTCGGAGACATAGCCAGAGGCGGCACACAAGTGCGGAAGAG
GAAGAGCCACCGCCTGTTAAAATAGCCTGGAAAACTGCGGCAGCAAGGAAATCCTTACCA
GCTTCCATTACGATGCACAAAGGGAGCCTGGATTTGCAGAAGTGTAACATGTCTCCAGTT
GTGAAAATTGAACAAGTGTTTGCTCTTCAGAATGCTACAGGGGATGGGAAATTTATCGAT
CAATTTGTTTATTCAACAAAGGGAATTGGTAACAAAACAGAAATAAGTGTCAGGGGGCAA
GACAGGCTTATAATTTCTACACCAAACCAGAGAAATGAAAAGCCAACGCAGAGTGTATCA
TCTCCTGAAGCAACATCTGGTTCTACAGGCTCAGTAGAAAAGAAGCAACAGAGAAGATCA
ATTAGAACTCGTTCTGAATCAGAGAAATCCACTGAGGTTGTGCCAAAGAAGAAGATCAAA
AAGGAGCAGGTTGAAACAGTTCCTCAGGCTACAGTGAAGACTGGATTACAGAAAGGGTCG
GCGGACCGGGGAGTGCAGGGCTCTGTCAGATTCAGTGACAGCTCCGTCTCCGCAGCGATT
GAGGAAACTGTGGACTGA
Enzyme 33 GenBank Gene ID AF332468 Link Image
Enzyme 33 GeneCard ID Q9BZ95 Link Image
Enzyme 33 GenAtlas ID WHSC1L1 Link Image
Enzyme 33 HGNC ID HGNC:12767 Link Image
Enzyme 33 Chromosome Location Not Available
Enzyme 33 Locus Not Available
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References
  1. Stec I, van Ommen GJ, den Dunnen JT: WHSC1L1, on human chromosome 8p11.2, closely resembles WHSC1 and maps to a duplicated region shared with 4p16.3. Genomics. 2001 Aug;76(1-3):5-8. [PubMed Link Image]
  2. Angrand PO, Apiou F, Stewart AF, Dutrillaux B, Losson R, Chambon P: NSD3, a new SET domain-containing gene, maps to 8p12 and is amplified in human breast cancer cell lines. Genomics. 2001 May 15;74(1):79-88. [PubMed Link Image]
Enzyme 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 14776
Enzyme 34 Name SET domain-containing protein 1B
Enzyme 34 Synonyms Not Available
Enzyme 34 Gene Name KIAA1076
Enzyme 34 Protein Sequence >SET domain-containing protein 1B
EFESSSESSPSSSEDEEEVVAREEEEEEEEEEMVAEESMASAGPEDFEQDGEEAALAPGA
PAVDSLGMEEEVDIETEAVAPEERPSMLDEPPLPVGVEEPADSREPPEEPGLSQEGAMLL
SPEPPAKEVEARPPLSPERAPEHDLEVEPEPPMMLPLPLQPPLPPPRPPRPPSPPPEPET
TDASHPSVPPEPLAEDHPPHTPGLCGSLAKSQSTETVPATPGGEPPLSGGSSGLSLSSPQ
VPGSPFSYPAPSPSLSSGGLPRTPGRDFSFTPTFSEPSGPLLLPVCPLPTGRRDERSGPL
ASPVLLETGLPLPLPLPLPLPLALPAVLRAQARAPTPLPPLLPAPLASCPPPMKRKPGRP
RRSPPSMLSLDGPLVRPPAGAALGRELLLLPGQPQTPVFPSTHDPRTVTLDFRNAGIPAP
PPPLPPQPPPPPPPPPVEPTKLPFKELDNQWPSEAIPPGPRGRDEVTEEYMELAKSRGPW
RRPPKKRHEDLVPPAGSPELSPPQPLFRPRSEFEEMTILYDIWNGGIDEEDIRFLCVTYE
RLLQQDNGMDWLNDTLWVYHPSTSLSSAKKKKRDDGIREHVTGCARSEGFYTIDKKDKLR
YLNSSRASTDEPPADTQGMSIPAQPHASTRAGSERRSEQRRLLSSFTGSCDSDLLKFNQL
KFRKKKLKFCKSHIHDWGLFAMEPIAADEMVIEYVGQNIRQVIADMREKRYEDEGIGSSY
MFRVDHDTIIDATKCGNFARFINHSCNPNCYAKVITVESQKKIVIYSKQHINVNEEITYD
YKFPIEDVKIPCLCGSENCRGTLN
Enzyme 34 Number of Residues 804
Enzyme 34 Molecular Weight 87999
Enzyme 34 Theoretical pI 4.49
Enzyme 34 GO Classification Not Available
Enzyme 34 General Function Not Available
Enzyme 34 Specific Function Not Available
Enzyme 34 Pathways Not Available
Enzyme 34 Reactions Not Available
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • None
Enzyme 34 Transmembrane Regions
  • None
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein 5689489 Link Image
Enzyme 34 UniProtKB/Swiss-Prot ID Q9UPS6 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name Q9UPS6_HUMAN Link Image
Enzyme 34 PDB ID Not Available
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >2416 bp
TGAGTTTGAGTCAAGCTCCGAGTCCTCGCCCTCATCCTCGGAGGATGAGGAGGAGGTAGT
GGCCAGGGAAGAGGAGGAAGAAGAGGAGGAGGAGGAGATGGTGGCCGAGGAAAGCATGGC
TTCTGCAGGCCCTGAGGACTTTGAGCAGGACGGGGAGGAAGCGGCTCTGGCCCCGGGGGC
ACCTGCAGTGGACTCGTTGGGCATGGAAGAGGAGGTGGACATCGAGACTGAGGCTGTGGC
CCCTGAGGAGCGGCCCTCCATGCTGGACGAGCCCCCCTTGCCTGTGGGTGTTGAAGAGCC
AGCGGACTCCAGGGAGCCGCCTGAGGAACCAGGCCTGAGCCAGGAAGGGGCCATGTTGCT
GTCTCCAGAGCCCCCTGCCAAGGAGGTGGAGGCTCGACCCCCATTGTCCCCTGAGCGAGC
TCCAGAACATGACCTGGAAGTGGAGCCGGAGCCCCCTATGATGCTCCCCTTGCCGCTGCA
ACCACCATTGCCGCCCCCACGACCACCCCGGCCACCCAGCCCACCGCCGGAGCCTGAGAC
CACAGATGCCTCACACCCATCTGTCCCTCCGGAGCCCCTTGCCGAGGACCACCCCCCGCA
TACTCCAGGCCTCTGTGGCAGCCTGGCCAAGTCGCAGAGCACAGAGACGGTGCCAGCCAC
ACCAGGCGGGGAGCCCCCGCTATCAGGGGGCAGCAGTGGCCTGTCCCTGAGCTCTCCGCA
AGTGCCCGGCAGCCCCTTCTCCTACCCAGCCCCGTCCCCTAGCTTGAGCAGTGGGGGCCT
CCCTCGGACACCTGGCCGGGACTTCAGCTTCACACCCACCTTCTCCGAGCCCAGCGGGCC
CTTGCTCCTGCCCGTCTGCCCACTCCCCACTGGCCGACGCGATGAACGCTCCGGGCCCCT
GGCCTCCCCGGTGCTCCTGGAGACGGGCCTGCCCCTCCCTCTGCCCCTTCCCCTGCCCTT
GCCCTTGGCATTGCCCGCCGTCTTGCGGGCCCAGGCTCGTGCGCCCACCCCGCTGCCACC
CCTGCTGCCCGCCCCCCTGGCCTCTTGCCCTCCCCCAATGAAGAGGAAGCCGGGCCGGCC
CCGGCGATCCCCACCATCTATGCTCTCCTTGGATGGGCCCTTGGTCCGACCACCAGCAGG
GGCCGCCCTTGGAAGGGAACTCCTGCTCCTGCCGGGCCAGCCACAGACCCCCGTCTTCCC
CAGCACCCATGACCCCCGGACGGTGACCCTGGACTTCCGGAACGCGGGGATCCCAGCCCC
TCCACCACCCCTTCCCCCCCAGCCACCCCCACCCCCACCTCCCCCACCTGTAGAGCCCAC
CAAGCTGCCCTTTAAGGAGCTAGACAACCAGTGGCCCTCCGAGGCCATTCCTCCGGGCCC
CCGTGGGCGCGATGAGGTCACTGAGGAATACATGGAGTTGGCCAAGAGCCGGGGGCCGTG
GCGCCGGCCACCTAAGAAGCGCCATGAGGACCTGGTGCCACCTGCAGGCTCGCCCGAACT
CTCGCCACCCCAGCCCCTCTTCCGGCCCCGCTCGGAGTTTGAGGAGATGACCATCCTGTA
TGACATCTGGAACGGTGGCATCGATGAGGAGGACATCCGCTTCCTGTGTGTCACCTACGA
GCGACTGCTACAGCAGGACAATGGCATGGACTGGCTTAACGACACGCTCTGGGTCTACCA
TCCCTCCACCAGCCTCTCTTCAGCTAAGAAGAAGAAACGGGACGATGGCATCCGCGAGCA
CGTGACGGGCTGTGCCCGCAGTGAGGGCTTCTACACCATCGACAAGAAGGACAAGCTCAG
ATACCTCAACAGCAGCCGTGCCAGCACCGATGAGCCCCCCGCAGACACCCAGGGCATGAG
CATCCCAGCACAGCCCCACGCCTCCACCCGGGCAGGCTCGGAGCGGCGTTCGGAGCAGCG
CCGCCTGCTGTCCTCCTTCACTGGCAGCTGTGACAGTGACCTGCTCAAGTTCAACCAGCT
CAAGTTCCGGAAGAAAAAGCTCAAGTTCTGCAAGAGCCACATTCACGACTGGGGCTTGTT
CGCCATGGAGCCCATCGCGGCTGACGAGATGGTCATCGAGTACGTGGGCCAGAATATCCG
TCAGGTGATCGCAGACATGCGGGAGAAGCGTTATGAGGACGAGGGCATCGGGAGCAGCTA
CATGTTCCGGGTGGACCATGACACCATCATCGACGCCACCAAGTGCGGCAACTTCGCGCG
CTTCATCAACCACAGCTGCAACCCCAACTGCTATGCCAAGGTGATCACGGTGGAGTCACA
GAAGAAGATAGTCATCTACTCGAAGCAGCACATTAACGTCAATGAGGAGATTACCTATGA
CTATAAGTTCCCCATCGAGGACGTCAAGATCCCCTGCCTCTGTGGCTCCGAGAACTGCCG
GGGGACCCTCAACTAG
Enzyme 34 GenBank Gene ID AB028999 Link Image
Enzyme 34 GeneCard ID Q9UPS6 Link Image
Enzyme 34 GenAtlas ID SETD1B Link Image
Enzyme 34 HGNC ID HGNC:29187 Link Image
Enzyme 34 Chromosome Location Not Available
Enzyme 34 Locus Not Available
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 General References
  1. Kikuno R, Nagase T, Ishikawa K, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Jun 30;6(3):197-205. [PubMed Link Image]
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 14777
Enzyme 35 Name Histone-lysine N-methyltransferase SETD2
Enzyme 35 Synonyms
  1. SET domain- containing protein 2
  2. hSET2
  3. Huntingtin-interacting protein HYPB
  4. Huntingtin yeast partner B
  5. Huntingtin-interacting protein 1
  6. HIF- 1
  7. p231HBP
Enzyme 35 Gene Name SETD2
Enzyme 35 Protein Sequence >Histone-lysine N-methyltransferase SETD2
MKQLQPQPPPKMGDFYDPEHPTPEEEENEAKIENVQKTGFIKGPMFKGVASSRFLPKGTK
TKVNLEEQGRQKVSFSFSLTKKTLQNRFLTALGNEKQSDTPNPPAVPLQVDSTPKMKMEI
GDTLSTAEESSPPKSRVELGKIHFKKHLLHVTSRPLLATTTAVASPPTHAAPLPAVIAES
TTVDSPPSSPPPPPPPAQATTLSSPAPVTEPVALPHTPITVLMAAPVPLPVDVAVRSLKE
PPIIIVPESLEADTKQDTISNSLEEHVTQILNEQADISSKKEDSHIGKDEEIPDSSKISL
SCKKTGSKKKSSQSEGIFLGSESDEDSVRTSSSQRSHDLKFSASIEKERDFKKSSAPLKS
EDLGKPSRSKTDRDDKYFSYSKLERDTRYVSSRCRSERERRRSRSHSRSERGSRTNLSYS
RSERSHYYDSDRRYHRSSPYRERTRYSRPYTDNRARESSDSEEEYKKTYSRRTSSHSSSY
RDLRTSSYSKSDRDCKTETSYLEMERRGKYSSKLERESKRTSENEAIKRCCSPPNELGFR
RGSSYSKHDSSASRYKSTLSKPIPKSDKFKNSFCCTELNEEIKQSHSFSLQTPCSKGSEL
RMINKNPEREKAGSPAPSNRLNDSPTLKKLDELPIFKSEFITHDSHDSIKELDSLSKVKN
DQLRSFCPIELNINGSPGAESDLATFCTSKTDAVLMTSDDSVTGSELSPLVKACMLSSNG
FQNISRCKEKDLDDTCMLHKKSESPFRETEPLVSPHQDKLMSMPVMTVDYSKTVVKEPVD
TRVSCCKTKDSDIYCTLNDSNPSLCNSEAENIEPSVMKISSNSFMNVHLESKPVICDSRN
LTDHSKFACEEYKQSIGSTSSASVNHFDDLYQPIGSSGIASSLQSLPPGIKVDSLTLLKC
GENTSPVLDAVLKSKKSSEFLKHAGKETIVEVGSDLPDSGKGFASRENRRNNGLSGKCLQ
EAQKEGNSILPERRGRPEISLDERGEGGHVHTSDDSEVVFSSCDLNLTMEDSDGVTYALK
CDSSGHAPEIVSTVHEDYSGSSESSNDESDSEDTDSDDSSIPRNRLQSVVVVPKNSTLPM
EETSPCSSRSSQSYRHYSDHWEDERLESRRHLYEEKFESIASKACPQTDKFFLHKGTEKN
PEISFTQSSRKQIDNRLPELSHPQSDGVDSTSHTDVKSDPLGHPNSEETVKAKIPSRQQE
ELPIYSSDFEDVPNKSWQQTTFQNRPDSRLGKTELSFSSSCEIPHVDGLHSSEELRNLGW
DFSQEKPSATYQQPDSSYGACGGHKYQQNAEQYGGTRDYWQGNGYWDPRSGRPPGTGVVY
DRTQGQVPDSLTDDREEEENWDQQDGSHFSDQSDKFLLSLQKDKGSVQAPEISSNSIKDT
LAVNEKKDFSKNLEKNDIKDRGPLKKRRQEIESDSESDGELQDRKKVRVEVEQGETSVPP
GSALVGPSCVMDDFRDPQRWKECAKQGKMPCYFDLIEENVYLTERKKNKSHRDIKRMQCE
CTPLSKDERAQGEIACGEDCLNRLLMIECSSRCPNGDYCSNRRFQRKQHADVEVILTEKK
GWGLRAAKDLPSNTFVLEYCGEVLDHKEFKARVKEYARNKNIHYYFMALKNDEIIDATQK
GNCSRFMNHSCEPNCETQKWTVNGQLRVGFFTTKLVPSGSELTFDYQFQRYGKEAQKCFC
GSANCRGYLGGENRVSIRAAGGKMKKERSRKKDSVDGELEALMENGEGLSDKNQVPSLSR
LMVRIETLEQKLTCLELIQNTHSQSCLKSFLERHGLSLLWIWMAELGDGRESNQKLQEEI
IKTLEHLPIPTKNMLEESKVLPIIQRWSQTKTAVPPLSEGDGYSSENTSRAHTPLNTPDP
STKLSTEADTDTPKKLMFRRLKIISENSMDSAISDATSELEGKDGKEDLDQLENVPVEEE
EELQSQQLLPQQLPECKVDSETNIEASKLPTSEPEADAEIEPKESNGTKLEEPINEETPS
QDEEEGVSDVESERSQEQPDKTVDISDLATKLLDSWKDLKEVYRIPKKSQTEKENTTTER
GRDAVGFRDQTPAPKTPNRSRERDPDKQTQNKEKRKRRSSLSPPSSAYERGTKRPDDRYD
TPTSKKKVRIKDRNKLSTEERRKLFEQEVAQREAQKQQQQMQNLGMTSPLPYDSLGYNAP
HHPFAGYPPGYPMQAYVDPSNPNAGKVLLPTPSMDPVCSPAPYDHAQPLVGHSTEPLSAP
PPVPVVPHVAAPVEVSSSQYVAQSDGVVHQDSSVAVLPVPAPGPVQGQNYSVWDSNQQSV
SVQQQYSPAQSQATIYYQGQTCPTVYGVTSPYSQTTPPIVQSYAQPSLQYIQGQQIFTAH
PQGVVVQPAAAVTTIVAPGQPQPLQPSEMVVTNNLLDLPPPSPPKPKTIVLPPNWKTARD
PEGKIYYYHVITRQTQWDPPTWESPGDDASLEHEAEMDLGTPTYDENPMKASKKPKTAEA
DTSSELAKKSKEVFRKEMSQFIVQCLNPYRKPDCKVGRITTTEDFKHLARKLTHGVMNKE
LKYCKNPEDLECNENVKHKTKEYIKKYMQKFGAVYKPKEDTELE
Enzyme 35 Number of Residues 2564
Enzyme 35 Molecular Weight 287551
Enzyme 35 Theoretical pI 6.08
Enzyme 35 GO Classification Not Available
Enzyme 35 General Function Not Available
Enzyme 35 Specific Function Histone methyltransferase that methylates 'Lys-36' of histone H3. H3 'Lys-36' methylation represents a specific tag for epigenetic transcriptional activation. Probably plays a role in chromatin structure modulation during elongation via its interaction with hyperphosphorylated POLR2A. Binds DNA at promoters. May also act as a transcription activator that binds to promoters. Binds to the promoters of adenovirus 12 E1A gene in case of infection, possibly leading to regulate its expression
Enzyme 35 Pathways
Enzyme 35 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938] ALL_REAC R03938
  • (other) R03875 R04866 R04867
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • None
Enzyme 35 Transmembrane Regions
  • None
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein 10438874 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID Q9BYW2 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name SETD2_HUMAN Link Image
Enzyme 35 PDB ID Not Available
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >1984 bp
ATGCTGCATAAGAAGTCAGAAAGCCCATTTAGAGAAACAGAACCTCTGGTGTCACCACAC
CAAGATAAACTCATGTCTATGCCAGTTATGACTGTGGATTATTCCAAAACAGTAGTTAAA
GAACCAGTTGATACGAGGGTTTCTTGCTGCAAAACCAAAGATTCAGACATATACTGTACT
TTGAACGATAGCAACCCTTCTTTGTGTAACTCTGAAGCTGAAAATATTGAGCCTTCAGTT
ATGAAGATTTCTTCAAATAGCTTTATGAATGTGCATTTGGAATCAAAACCAGTTATATGT
GATAGTAGAAATTTGACAGATCACTCAAAATTTGCATGTGAAGAATATAAGCAGAGCATC
GGTAGCACTAGTTCAGCTTCTGTTAATCATTTTGATGATTTATATCAACCTATTGGGAGT
TCAGGTATTGCTTCATCTCTTCAGAGTCTTCCACCAGGAATAAAGGTGGACAGTCTAACT
CTCTTGAAATGCGGAGAGAACACATCTCCAGTTCTGGATGCAGTGCCAAAGAGTAAAAAA
AGTTCAGAGTTTTTAAAGCATGCAGGGAAAGAAACAATAGTAGAAGTAGGTAGTGACCTT
CCTGATTCAGGAAAGGGATTTGCTTCCAGGGAGAACAGGCGTAATAATGGGTTATCTGGG
AAATGTTTGCAAGAGGCTCAAGAAGAAGGGAATTCCATATTGCCTGAAAGAAGAGGAAGA
CCAGAAATCTCTTTAGATGAAAGAGGAGAAGGAGGACATGTGCATACTTCTGATGACTCA
GAAGTTGTATTTTCTTCTTGTGATTTGAATTTAACCATGGAAGACAGTGATGGTGTAACT
TATGCATTAAAGTGTGACAGTAGTGGTCATGCCCCAGAAATTGTGTCTACAGTTCATGAA
GATTATTCTGGCTCTTCTGAAAGTTCAAATGATGAAAGTGATTCAGAAGATACAGATTCG
GATGATAGCAGTATTCCAAGAAACCGTCTCCAGTCTGTTGTGGTTGTGCCAAAGAATTCT
ACTTTGCCCATGGAAGAAACAAGTCCTTGTTCTTCTCGGAGCAGTCAAAGTTATAGACAC
TATTCTGACCATTGGGAAGATGAGAGATTGGAGTCAAGGAGACATTTGTATGAGGAAAAA
TTTGAAAGTATAGCAAGTAAAGCCTGTCCTCAAACTGATAAGTTTTTCCTTCATAAAGGA
ACAGAGAAGAATCCGGAAATTTCTTTTACACAGTCCAGTAGAAAACAAATAGATAACCGC
CTGCCTGAACTTTCTCATCCTCAGAGTGATGGGGTTGATAGTACAAGTCATACAGATGTG
AAATCTGACCCTCTGGGTCACCCAAATTCAGAGGAAACCGTGAAAGCCAAAATACCTTCT
AGGCAGCAAGAAGAGCTGCCAATTTATTCTTCTGATTTTGAAGATGTCCCAAATAAGTCT
TGGCAACAGACCACTTTCCAAAACAGGCCAGATAGTAGACTGGGAAAAACAGAATTGAGT
TTTTCTTCCTCTTGTGAGATACCACATGTGGATGGCTTGCACTCATCAGAAGAGCTCAGA
AACTTAGGTTGGGACTTCTCTCAAGAAAAGCCTTCTACCACGTATCAGCAACCTGACAGT
AGCTATGGAGCTTGTGGTGGACACAAGTATCAGCAAAATGCAGAACAGTATGGTGGGACA
CGTGATTACTGGCAAGGCAATGGTTACTGGGATCCAAGATCAGGTAGACCTCCTGGAACT
GGGGTTGTGTATGATCGAACTCAAGGACAAGTACCAGATTCCCTAACAGATGATCGTGAA
GAAGGGGAGAATTGGGATCAACAGGATGGATCCCATTTTTCAGACCAGTCCGATAAATTT
CTTCTATCCCTTCAGAAAGACAAGGGGTCAGTGCAAGCACCTGAAATAAGCAGCAATTCC
ATTAAGGACACTTTAGCTGTGAATGAAAAGAAAGATTTTTCAAAAAAAAAAAAAAAAAAA
AAAA
Enzyme 35 GenBank Gene ID AK026125 Link Image
Enzyme 35 GeneCard ID Q9BYW2 Link Image
Enzyme 35 GenAtlas ID SETD2 Link Image
Enzyme 35 HGNC ID HGNC:18420 Link Image
Enzyme 35 Chromosome Location Not Available
Enzyme 35 Locus Not Available
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References
  1. Nagase T, Kikuno R, Hattori A, Kondo Y, Okumura K, Ohara O: Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Dec 31;7(6):347-55. [PubMed Link Image]
  2. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed Link Image]
  3. Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed Link Image]
  4. Faber PW, Barnes GT, Srinidhi J, Chen J, Gusella JF, MacDonald ME: Huntingtin interacts with a family of WW domain proteins. Hum Mol Genet. 1998 Sep;7(9):1463-74. [PubMed Link Image]
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 14778
Enzyme 36 Name Histone-lysine N-methyltransferase SETMAR
Enzyme 36 Synonyms
  1. SET domain and mariner transposase fusion gene-containing protein
  2. Metnase
  3. Hsmar1[Includes: Histone-lysine N-methyltransferase
  4. Mariner transposase Hsmar1]
Enzyme 36 Gene Name SETMAR
Enzyme 36 Protein Sequence >Histone-lysine N-methyltransferase SETMAR
MAEFKEKPEAPTEQLDVACGQENLPVGAWPPGAAPAPFQYTPDHVVGPGADIDPTQITFP
GCICVKTPCLPGTCSCLRHGENYDDNSCLRDIGSGGKYAEPVFECNVLCRCSDHCRNRVV
QKGLQFHFQVFKTHKKGWGLRTLEFIPKGRFVCEYAGEVLGFSEVQRRIHLQTKSDSNYI
IAIREHVYNGQVMETFVDPTYIGNIGRFLNHSCEPNLLMIPVRIDSMVPKLALFAAKDIV
PEEELSYDYSGRYLNLTVSEDKERLDHGKLRKPCYCGAKSCTAFLPFDSSLYCPVEKSNI
SCGNEKEPSMCGSAPSVFPSCKRLTLETMKMMLDKKQIRAIFLFEFKMGRKAAETTRNIN
NAFGPGTANERTVQWWFKKFCKGDESLEDEERSGRPSEVDNDQLRAIIEADPLTTTREVA
EELNVNHSTVVRHLKQIGKVKKLDKWVPHELTENQKNRRFEVSSSLILRNHNEPFLDRIV
TCDEKWILYDNRRRSAQWLDQEEAPKHFPKPILHPKKVMVTIWWSAAGLIHYSFLNPGET
ITSEKYAQEIDEMNQKLQRLQLALVNRKGPILLHDNARPHVAQPTLQKLNELGYEVLPHP
PYSPDLLPTNYHVFKHLNNFLQGKRFHNQQDAENAFQEFVESQSTDFYATGINQLISRWQ
KCVDCNGSYFD
Enzyme 36 Number of Residues 671
Enzyme 36 Molecular Weight 76670
Enzyme 36 Theoretical pI 7.05
Enzyme 36 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • histone-lysine N-methyltransferase activity
  • ion binding
  • methyltransferase activity
  • protein methyltransferase activity
  • protein-lysine N-methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
  • transition metal ion binding
  • zinc ion binding
Process
  • DNA metabolism
  • DNA packaging
  • cellular metabolism
  • chromatin modification
  • establishment and/or maintenance of chromatin architecture
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 36 General Function Not Available
Enzyme 36 Specific Function Histone methyltransferase that methylates 'Lys-4' and 'Lys-36' of histone H3, 2 specific tags for epigenetic transcriptional activation. Specifically mediates dimethylation of H3 'Lys-36'. Binds DNA. May play a role in non-homologous end- joining repair
Enzyme 36 Pathways
Enzyme 36 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938] ALL_REAC R03938
  • (other) R03875 R04866 R04867
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • None
Enzyme 36 Transmembrane Regions
  • None
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein 63079013 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID Q53H47 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name SETMR_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence >2016 bp
ATGGCGGAGTTTAAGGAGAAGCCTGAGGCCCCGACTGAGCAGCTGGATGTCGCGTGCGGC
CAGGAAAACTTGCCGGTGGGCGCGTGGCCCCCGGGGGCCGCGCCGGCGCCCTTCCAGTAC
ACTCCTGATCATGTAGTTGGACCTGGAGCAGACATTGATCCCACTCAAATAACCTTTCCC
GGATGCATTTGTGTCAAAACTCCCTGCCTCCCTGGCACTTGCTCCTGTCTCCGCCATGGA
GAGAACTATGATGATAACTCATGCCTTAGAGATATAGGATCTGGAGGAAAGTATGCAGAG
CCTGTTTTTGAATGCAATGTCCTGTGCCGATGCAGTGACCACTGCAGAAACAGAGTGGTC
CAGAAAGGTCTACAGTTCCACTTCCAAGTGTTCAAGACGCATAAAAAAGGCTGGGGACTT
CGTACCTTGGAATTTATACCGAAAGGAAGGTTTGTCTGTGAATATGCTGGTGAGGTTTTA
GGATTCTCTGAAGTTCAGAGAAGAATTCACTTACAAACAAAATCCGACTCCAATTACATT
ATAGCCATCAGGGAACATGTTTATAATGGGCAGGTAATGGAAACATTTGTTGACCCTACT
TATATAGGAAATATTGGAAGATTCCTTAATCATTCTTGTGAGCCAAACCTTTTGATGATT
CCTGTCCGAATTGACTCAATGGTACCTAAGTTGGCACTTTTTGCAGCCAAAGATATTGTG
CCAGAAGAAGAACTCTCTTATGATTATTCAGGAAGATATCTTAATCTAACAGTCAGTGAA
GACAAAGAAAGGCTAGATCATGGGAAACTAAGGAAACCTTGTTACTGTGGTGCCAAATCA
TGTACTGCTTTCCTGCCTTTTGACAGTTCTCTGTACTGCCCCGTAGAAAAGTCGAACATC
AGTTGTGGAAATGAGAAGGAACCCAGCATGTGTGGCTCGGCCCCTTCTGTGTTCCCCTCC
TGCAAGCGATTGACCCTTGAGACTATGAAAATGATGTTAGACAAAAAGCAAATTCGAGCA
ATTTTCTTATTCGAGTTCAAAATGGGTCGTAAAGCAGCAGAAACAACTCGCAACATCAAC
AATGCATTTGGCCCAGGAACTGCTAACGAACGTACAGTGCAGTGGTGGTTCAAGAAGTTT
TGCAAAGGAGATGAGAGCCTTGAAGATGAGGAGCGTAGTGGCCGGCCATCAGAAGTTGAC
AACGACCAGTTGAGAGCAATCATCGAAGCTGATCCCCTTACAACTACACGAGAAGTTGCT
GAAGAACTCAATGTCAACCATTCTACGGTCGTTCGGCATTTGAAGCAAATTGGAAAGGTG
AAAAAGCTCGATAAGTGGGTGCCTCATGAGCTGACTGAAAATCAAAAAAATCGTCGTTTT
GAAGTGTCATCTTCTCTTATTCTACGCAACCACAACGAACCATTTCTCGATCGGATTGTG
ACGTGTGATGAAAAGTGGATTTTATATGACAACCGGCGACGATCAGCTCAGTGGTTGGAT
CAAGAAGAAGCTCCAAAGCACTTCCCAAAGCCAATCTTGCACCCAAAAAAGGTCATGGTC
ACTATTTGGTGGTCTGCTGCTGGTCTGATCCACTACAGCTTTCTGAATCCCGGTGAAACC
ATTACATCTGAGAAGTATGCTCAGGAAATCGATGAGATGAACCAAAAACTGCAACGCCTG
CAGCTGGCATTGGTCAACAGAAAGGGCCCAATTCTTCTCCACGACAATGCCCGACCGCAT
GTTGCACAACCCACACTTCAAAAGTTGAATGAATTGGGCTATGAAGTTTTGCCTCATCCA
CCGTATTCACCTGACCTCTTGCCAACCAACTACCACGTCTTTAAGCATCTCAACAACTTT
TTGCAGGGAAAACGCTTCCACAACCAGCAGGATGCAGAAAATGCTTTCCAAGAGTTCGTC
GAATCCCAAAGCACGGATTTTTACGCTACAGGAATAAACCAACTTATTTCTCGTTGGCAA
AAATGTGTTGATTGTAATGGTTCCTATTTTGATTAA
Enzyme 36 GenBank Gene ID AY952295 Link Image
Enzyme 36 GeneCard ID Q53H47 Link Image
Enzyme 36 GenAtlas ID SETMAR Link Image
Enzyme 36 HGNC ID HGNC:10762 Link Image
Enzyme 36 Chromosome Location Not Available
Enzyme 36 Locus Not Available
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 General References
  1. Robertson HM, Zumpano KL: Molecular evolution of an ancient mariner transposon, Hsmar1, in the human genome. Gene. 1997 Dec 31;205(1-2):203-17. [PubMed Link Image]
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 14780
Enzyme 37 Name Histone-lysine N-methyltransferase SUV420H1
Enzyme 37 Synonyms
  1. Suppressor of variegation 4-20 homolog 1
  2. Suv4-20h1
  3. Su(var4-20 homolog 1
Enzyme 37 Gene Name SUV420H1
Enzyme 37 Protein Sequence >Histone-lysine N-methyltransferase SUV420H1
MKWLGESKNMVVNGRRNGGKLSNDHQQNQSKLQHTGKDTLKAGKNAVERRSNRCNGNSGF
EGQSRYVPSSGMSAKELCENDDLATSLVLDPYLGFQTHKMNTSAFPSRSSRHFSKSDSFS
HNNPVRFRPIKGRQEELKEVIERFKKDEHLEKAFKCLTSGEWARHYFLNKNKMQEKLFKE
HVFIYLRMFATDSGFEILPCNRYSSEQNGAKIVATKEWKRNDKIELLVGCIAELSEIEEN
MLLRHGENDFSVMYSTRKNCAQLWLGPAAFINHDCRPNCKFVSTGRDTACVKALRDIEPG
EEISCYYGDGFFGENNEFCECYTCERRGTGAFKSRVGLPAPAPVINSKYGLRETDKRLNR
LKKLGDSSKNSDSQSVSSNTDADTTQEKNNATSNRKSSVGVKKNSKSRTLTRQSMSRIPA
SSNSTSSKLTHINNSRVPKKLKKPAKPLLSKIKLRNHCKRLEQKNASRKLEMGNLVLKEP
KVVLYKNLPIKKDKEPEGPAQAAVASGCLTRHAAREHRQNPVRGAHSQGESSPCTYITRR
SVRTRTNLKEASDIKLEPNTLNGYKSSVTEPCPDSGEQLQPAPVLQEEELAHETAQKGEA
KCHKSDTGMSKKKSRQGKLVKQFAKIEESTPVHDSPGKDDAVPDLMGPHSDQGEHSGTVG
VPVSYTDCAPSPVGCSVVTSDSFKTKDSFRTAKSKKKRRITRYDAQLILENNSGIPKLTL
RRRHDSSSKTNDQENDGMNSSKISIKLSKDHDNDNNLYVAKLNNGFNSGSGSSSTKLKIQ
LKRDEENRGSYTEGLHENGVCCSDPLSLLESRMEVDDYSQYEEESTDDSSSSEGDEEEDD
YDDDFEDDFIPLPPAKRLRLIVGKDSIDIDISSRRREDQSLRLNA
Enzyme 37 Number of Residues 885
Enzyme 37 Molecular Weight 99189
Enzyme 37 Theoretical pI 9.05
Enzyme 37 GO Classification Not Available
Enzyme 37 General Function Not Available
Enzyme 37 Specific Function Histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4. H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions. SUV420H1 is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2)
Enzyme 37 Pathways
Enzyme 37 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938] ALL_REAC R03938
  • (other) R03875 R04866 R04867
Enzyme 37 Pfam Domain Function
Enzyme 37 Signals
  • None
Enzyme 37 Transmembrane Regions
  • None
Enzyme 37 Essentiality Not Available
Enzyme 37 GenBank ID Protein 51574062 Link Image
Enzyme 37 UniProtKB/Swiss-Prot ID Q4FZB7 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name SUV41_HUMAN Link Image
Enzyme 37 PDB ID Not Available
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence >1182 bp
ATGAAGTGGTTGGGAGAATCCAAGAACATGGTGGTGAATGGCAGGAGAAATGGAGGCAAG
TTGTCTAATGACCATCAGCAGAATCAATCAAAATTACAGCACACGGGGAAGGACACCCTG
AAGGCTGGCAAAAATGCAGTCGAGAGGAGGTCGAACAGATGTAATGGTAACTCGGGATTT
GAAGGACAGAGTCGCTATGTACCATCCTCTGGAATGTCCGCCAAGGAACTCTGTGAAAAT
GATGACCTAGCAACCAGTTTGGTTCTTGATCCCTATTTAGGTTTTCAAACACACAAAATG
AATACTAGCGCCTTTCCTTCGAGGAGCTCAAGGCATTTTTCAAAATCTGACAGTTTTTCT
CACAACAACCCTGTGAGATTTAGGCCTATTAAAGGAAGGCAGGAAGAACTAAAGGAAGTA
ATTGAACGTTTTAAGAAAGATGAACACTTGGAGAAAGCCTTCAAATGTTTGACTTCAGGC
GAATGGGCACGGCACTATTTTCTCAACAAGAATAAAATGCAGGAGAAATTATTCAAAGAA
CATGTATTTATTTATTTGCGAATGTTTGCAACTGACAGTGGATTTGAAATATTGCCATGT
AATAGATACTCATCAGAACAAAATGGAGCCAAAATAGTTGCAACAAAAGAGTGGAAACGA
AATGACAAAATAGAATTACTGGTGGGTTGTATTGCCGAACTTTCAGAAATTGAGGAGAAC
ATGCTACTTAGACATGGAGAAAACGACTTCAGTGTCATGTACTCCACAAGGAAAAACTGT
GCTCAACTCTGGCTGGGTCCTGCTGCGTTTATAAACCATGATTGCAGACCTAATTGTAAG
TTTGTGTCAACTGGTCGAGATACAGCATGTGTGAAGGCTCTAAGAGACATTGAACCTGGA
GAAGAAATTTCTTGTTATTATGGAGATGGGTTCTTTGGAGAAAATAATGAGTTCTGCGAG
TGTTACACTTGCGAAAGACGGGGCACTGGTGCTTTTAAATCCAGAGTGGGACTGCCTGCG
CCTGCTCCTGTTATCAATAGCAAATATGGACTCAGAGAAACAGATAAACGTTTAAATAGG
CTTAAAAAGTTAGGTGACAGCAGCAAAAATTCAGACAGTCAATCTGTCAGCTCTAACACT
GATGCAGATACCACTCAGGAAAAAAACAATGCAAGTAAGTAA
Enzyme 37 GenBank Gene ID BC002522 Link Image
Enzyme 37 GeneCard ID Q4FZB7 Link Image
Enzyme 37 GenAtlas ID SUV420H1 Link Image
Enzyme 37 HGNC ID HGNC:24283 Link Image
Enzyme 37 Chromosome Location 11
Enzyme 37 Locus 11q13.2
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 General References
  1. Twells RC, Metzker ML, Brown SD, Cox R, Garey C, Hammond H, Hey PJ, Levy E, Nakagawa Y, Philips MS, Todd JA, Hess JF: The sequence and gene characterization of a 400-kb candidate region for IDDM4 on chromosome 11q13. Genomics. 2001 Mar 15;72(3):231-42. [PubMed Link Image]
  2. Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W: Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. Genome Res. 2000 May;10(5):703-13. [PubMed Link Image]
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 14781
Enzyme 38 Name Histone-lysine N-methyltransferase SUV420H2
Enzyme 38 Synonyms
  1. Suppressor of variegation 4-20 homolog 2
  2. Suv4-20h2
  3. Su(var4-20 homolog 2
Enzyme 38 Gene Name SUV420H2
Enzyme 38 Protein Sequence >Histone-lysine N-methyltransferase SUV420H2
MGPDRVTARELCENDDLATSLVLDPYLGFRTHKMNVSPVPPLRRQQHLRSALETFLRQRD
LEAAYRALTLGGWTARYFQSRGPRQEAALKTHVYRYLRAFLPESGFTILPCTRYSMETNG
AKIVSTRAWKKNEKLELLVGCIAELREADEGLLRAGENDFSIMYSTRKRSAQLWLGPAAF
INHDCKPNCKFVPADGNAACVKVLRDIEPGDEVTCFYGEGFFGEKNEHCECHTCERKGEG
AFRTRPREPALPPRPLDKYQLRETKRRLQQGLDSGSRQGLLGPRACVHPSPLRRDPFCAA
CQPLRLPACSARPDTSPLWLQWLPQPQPRVRPRKRRRPRPRRAPVLSTHHAARVSLHRWG
GCGPHCRLRGEALVALGQPPHARWAPQQDWHWARRYGLPYVVRVDLRRLAPAPPATPAPA
GTPGPILIPKQALAFAPFSPPKRLRLVVSHGSIDLDVGGEEL
Enzyme 38 Number of Residues 462
Enzyme 38 Molecular Weight 52114
Enzyme 38 Theoretical pI 10.31
Enzyme 38 GO Classification Not Available
Enzyme 38 General Function Not Available
Enzyme 38 Specific Function Histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4. H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions. SUV420H1 is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2)
Enzyme 38 Pathways
Enzyme 38 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938] ALL_REAC R03938
  • (other) R03875 R04866 R04867
Enzyme 38 Pfam Domain Function
Enzyme 38 Signals
  • None
Enzyme 38 Transmembrane Regions
  • None
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein 18027368 Link Image
Enzyme 38 UniProtKB/Swiss-Prot ID Q86Y97 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name SUV42_HUMAN Link Image
Enzyme 38 PDB ID Not Available
Enzyme 38 Cellular Location Not Available
Enzyme 38 Gene Sequence >390 bp
ATGGGGCCCGACAGAGTGACAGCACGAGAACTGTGCGAGAACGACGACCTGGCCACCAGC
CTCGTCCTGGACCCCTACCTCGGTTTCCGCACCCATAAGATGAACGTCAGCCCTGTGCCC
CCCCTGCGGCGACAGCAGCACCTGCGCTCAGCGCTGGAAACTTTCCTGAGGCAGCGGGAC
CTGGAGGCTGCGTACCGGGCCCTGACGCTGGGAGGCTGGACGGCCCGCTACTTCCAGAGC
CGGGGCCCGCGGCAGGAGGCTGCCCTCAAGACCCACGTCTATCGCTACCTCCGTGCCTTC
CTGCCGGAAAGTGGCTTTACCATCCTGCCCTGCACGCGCTACTCCATGGAGACCAACGGG
GCCAAGATCGTGTCCACTCGTGCTTGGTAA
Enzyme 38 GenBank Gene ID AF289582 Link Image
Enzyme 38 GeneCard ID Q86Y97 Link Image
Enzyme 38 GenAtlas ID SUV420H2 Link Image
Enzyme 38 HGNC ID HGNC:28405 Link Image
Enzyme 38 Chromosome Location 19
Enzyme 38 Locus 19q13.42
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 General References Not Available
Enzyme 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 14787
Enzyme 39 Name N(2),N(2)-dimethylguanosine tRNA methyltransferase
Enzyme 39 Synonyms
  1. tRNA(guanine-26,N(2-N(2methyltransferase
  2. tRNA 2,2- dimethylguanosine-26 methyltransferase
  3. tRNA(m(2,2G26dimethyltransferase
Enzyme 39 Gene Name TRMT1
Enzyme 39 Protein Sequence >N(2),N(2)-dimethylguanosine tRNA methyltransferase
MQGSSLWLSLTFRSARVLSRARFFEWQSPGLPNTAAMENGTGPYGEERPREVQETTVTEG
AAKIAFPSANEVFYNPVQEFNRDLTCAVITEFARIQLGAKGIQIKVPGEKDTQKVVVDLS
EQEEEKVELKESENLASGDQPRTAAVGEICEEGLHVLEGLAASGLRSIRFALEVPGLRSV
VANDASTRAVDLIRRNVQLNDVAHLVQPSQADARMLMYQHQRVSERFDVIDLDPYGSPAT
FLDAAVQAVSEGGLLCVTCTDMAVLAGNSGETCYSKYGAMALKSRACHEMALRIVLHSLD
LRANCYQRFVVPLLSISADFYVRVFVRVFTGQAKVKASASKQALVFQCVGCGAFHLQRLG
KASGVPSGRAKFSAACGPPVTPECEHCGQRHQLGGPMWAEPIHDLDFVGRVLEAVSANPG
RFHTSERIRGVLSVITEELPDVPLYYTLDQLSSTIHCNTPSLLQLRSALLHADFRVSLSH
ACKNAVKTDAPASALWDIMRCWEKECPVKRERLSETSPAFRILSVEPRLQANFTIREDAN
PSSRQRGLKRFQANPEANWGPRPRARPGGKAADEAMEERRRLLQNKRKEPPEDVAQRAAR
LKTFPCKRFKEGTCQRGDQCCYSHSPPTPRVSADAAPDCPETSNQTPPGPGAAAGPGID
Enzyme 39 Number of Residues 659
Enzyme 39 Molecular Weight 72235
Enzyme 39 Theoretical pI 7.67
Enzyme 39 GO Classification
Function
  • N-methyltransferase activity
  • RNA binding
  • binding
  • catalytic activity
  • methyltransferase activity
  • nucleic acid binding
  • tRNA (guanine-N2-)-methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • RNA metabolism
  • RNA processing
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • tRNA processing
Component
Enzyme 39 General Function Translation, ribosomal structure and biogenesis
Enzyme 39 Specific Function Dimethylates a single guanine residue at position 26 of most tRNAs using S-adenosyl-L-methionine as donor of the methyl groups
Enzyme 39 Pathways Not Available
Enzyme 39 Reactions
  • S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N2-methylguanine [RN:R00598] ALL_REAC R00598
Enzyme 39 Pfam Domain Function
Enzyme 39 Signals
  • 1-21
Enzyme 39 Transmembrane Regions
  • None
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein 11066198 Link Image
Enzyme 39 UniProtKB/Swiss-Prot ID Q9NXH9 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name TRM1_HUMAN Link Image
Enzyme 39 PDB ID Not Available
Enzyme 39 Cellular Location Not Available
Enzyme 39 Gene Sequence >1980 bp
ATGCAAGGATCGTCTCTGTGGCTAAGCCTCACTTTCCGCTCCGCCCGGGTGCTCTCTAGA
GCCCGGTTTTTCGAGTGGCAGTCTCCAGGGCTGCCGAATACAGCAGCGATGGAGAACGGC
ACCGGGCCCTACGGAGAAGAACGTCCACGTGAAGTCCAGGAGACGACAGTCACCGAGGGG
GCTGCCAAAATCGCCTTTCCCAGTGCCAACGAGGTCTTTTATAACCCGGTGCAGGAATTC
AATCGGGACCTGACATGTGCTGTGATCACCGAGTTTGCTCGCATTCAGCTTGGGGCCAAA
GGAATCCAGATCAAGGTTCCAGGAGAGAAGGACACGCAAAAAGTGGTCGTGGACTTGTCA
GAGCAAGAGGAGGAAAAGGTTGAACTGAAAGAGAGTGAAAACCTGGCCTCAGGAGACCAA
CCTCGCACAGCGGCCGTGGGGGAGATCTGTGAGGAAGGCCTGCATGTGCTGGAAGGCCTG
GCAGCTTCAGGCCTACGTTCCATTCGATTTGCCCTAGAGGTGCCTGGGCTCAGATCTGTG
GTTGCAAACGATGCCTCCACCCGGGCTGTGGATCTCATACGCCGGAATGTCCAGCTCAAT
GACGTGGCCCACCTGGTACAGCCGAGCCAAGCAGATGCCCGGATGCTGATGTACCAGCAC
CAGAGGGTGTCGGAGAGGTTTGACGTCATCGATCTGGACCCCTATGGCAGCCCAGCCACC
TTCCTGGATGCAGCTGTGCAGGCTGTGAGTGAAGGAGGGTTGCTGTGTGTGACCTGCACA
GACATGGCGGTGTTGGCGGGGAACAGCGGGGAGACGTGCTACAGCAAGTACGGGGCCATG
GCCCTCAAGAGCCGGGCCTGCCACGAGATGGCCCTGAGAATCGTCCTGCACAGCCTGGAC
CTCCGCGCCAACTGCTACCAGCGCTTCGTGGTGCCGCTGCTCAGCATCAGCGCTGACTTC
TACGTGCGTGTTTTTGTCCGTGTCTTCACCGGCCAGGCCAAGGTCAAGGCCTCAGCCAGC
AAGCAGGCGCTGGTGTTCCAGTGTGTGGGCTGCGGGGCCTTCCACCTTCAGCGTCTCGGC
AAAGCGTCAGGAGTCCCCAGCGGCCGGGCCAAGTTCTCTGCAGCCTGTGGTCCCCCTGTG
ACCCCCGAGTGTGAACACTGTGGGCAACGACACCAGCTTGGTGGCCCCATGTGGGCAGAG
CCCATCCATGACCTGGATTTTGTGGGCCGTGTCCTGGAGGCTGTGAGCGCTAACCCCGGC
CGCTTCCACACCTCGGAGCGGATCCGAGGGGTCCTGAGCGTCATCACTGAGGAGCTCCCG
GACGTGCCTCTGTACTACACCCTGGACCAGCTGAGCAGCACCATCCACTGCAACACACCA
AGCCTCCTGCAGTTGCGGTCGGCCCTCCTCCACGCTGACTTCCGGGTCTCACTCTCCCAC
GCCTGTAAGAACGCTGTGAAGACGGATGCCCCTGCCTCTGCCCTCTGGGACATCATGCGT
TGCTGGGAGAAGGAATGTCCGGTGAAACGGGAGCGACTATCAGAGACTAGCCCAGCGTTC
CGCATTCTCAGTGTGGAGCCCAGGCTGCAGGCCAACTTCACCATCCGGGAAGATGCCAAC
CCCAGCTCCCGACAGCGAGGACTCAAGCGCTTCCAGGCTAACCCGGAGGCCAACTGGGGT
CCCCGGCCTCGTGCCCGGCCAGGGGGCAAGGCGGCCGACGAAGCTATGGAGGAGAGACGC
AGGCTGCTTCAGAACAAGCGGAAGGAGCCGCCGGAAGATGTGGCCCAGCGGGCTGCCCGG
CTCAAGACATTTCCTTGCAAGAGGTTTAAGGAGGGCACCTGTCAACGCGGGGACCAGTGC
TGCTACTCCCACAGCCCCCCGACACCCAGGGTTTCTGCTGATGCTGCCCCTGACTGTCCA
GAGACCTCCAACCAGACCCCCCCTGGACCTGGGGCTGCCGCTGGGCCAGGCATAGACTGA
Enzyme 39 GenBank Gene ID AF196479 Link Image
Enzyme 39 GeneCard ID Q9NXH9 Link Image
Enzyme 39 GenAtlas ID TRMT1 Link Image
Enzyme 39 HGNC ID HGNC:25980 Link Image
Enzyme 39 Chromosome Location 19
Enzyme 39 Locus 19p13.13
Enzyme 39 SNPs SNPJam Report Link Image
Enzyme 39 General References
  1. Liu J, Straby KB: The human tRNA(m(2)(2)G(26))dimethyltransferase: functional expression and characterization of a cloned hTRM1 gene. Nucleic Acids Res. 2000 Sep 15;28(18):3445-51. [PubMed Link Image]
Enzyme 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 14788
Enzyme 40 Name tRNA
Enzyme 40 Synonyms
  1. adenine-N(1--methyltransferase catalytic subunit TRM61
  2. tRNA(m1A58-methyltransferase subunit TRM61
  3. tRNA(m1A58MTase subunit TRM61
Enzyme 40 Gene Name TRM61
Enzyme 40 Protein Sequence >tRNA
MSFVAYEELIKEGDTAILSLGHGAMVAVRVQRGAQTQTRHGVLRHSVDLIGRPFGSKVTC
GRGGWVYVLHPTPELWTLNLPHRTQILYSTDIALITMMLELRPGSVVCESGTGSGSVSHA
IIRTIAPTGHLHTVEFHQQRAEKAREEFQEHRVGRWVTVRTQDVCRSGFGVSHVADAVFL
DIPSPWEAVGHAWDALKVEGGRFCSFSPCIEQVQRTCQALAARGFSELSTLEVLPQVYNV
RTVSLPPPDLGTGTDGPAGSDTSPFRSGTPMKEAVGHTGYLTFATKTPG
Enzyme 40 Number of Residues 289
Enzyme 40 Molecular Weight 31382
Enzyme 40 Theoretical pI 7.39
Enzyme 40 GO Classification Not Available
Enzyme 40 General Function Translation, ribosomal structure and biogenesis
Enzyme 40 Specific Function Catalytic subunit of tRNA (adenine-N(1)-)- methyltransferase, which catalyzes the formation of N(1)- methyladenine at position 58 (m1A58) in initiator methionyl-tRNA
Enzyme 40 Pathways Not Available
Enzyme 40 Reactions
  • S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N1-methyladenine [RN:R00596] ALL_REAC R00596
Enzyme 40 Pfam Domain Function
Enzyme 40 Signals
  • None
Enzyme 40 Transmembrane Regions
  • None
Enzyme 40 Essentiality Not Available
Enzyme 40 GenBank ID Protein 21757646 Link Image
Enzyme 40 UniProtKB/Swiss-Prot ID Q96FX7 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name TRM61_HUMAN Link Image
Enzyme 40 PDB ID Not Available
Enzyme 40 Cellular Location Not Available
Enzyme 40 Gene Sequence >963 bp
ATGAGCTTCGTGGCATACGAGGAGCTGATCAAGGAGGGTGACACGGCCATCCTGTCACTG
GGCCATGGTGCAATGGTGGCAGTGCGTGTGCAGCGTGGGGCACAGACCCAGACCCGGCAT
GGTGTCCTGCGGCACTCAGTTGACCTTATCGGCCGCCCCTTCGGCTCCAAGGTGACGTGC
GGCCGAGGTGGCTGGGTGTATGTGCTGCACCCCACGCCCGAGCTCTGGACGCTGAACCTG
CCGCACCGCACGCAGATCCTCTACTCCACAGACATCGCCCTCATCACCATGATGTTGGAG
CTTCGGCCCGGCTCTGTGGTCTGTGAGTCTGGCACCGGCAGTGGCTCTGTGTCCCACGCC
ATCATCCGCACCATTGCACCCACGGGTCACCTGCACACGGTGGAGTTCCACCAGCAGCGG
GCAGAGAAGGCCCGGGAGGAGTTCCAGGAGCACCGTGTGGGCCGCTGGGTGACTGTGCGC
ACCCAGGACGTGTGCCGCAGTGGCTTTGGCGTGAGCCACGTGGCCGACGCCGTCTTCCTG
GACATCCCATCACCCTGGGAGGCCGTGGGCCACGCCTGGGACGCCCTCAAGGTCGAAGGC
GGGCGCTTCTGCTCCTTCTCACCGTGCATCGAGCAGGTGCAACGCACATGCCAGGCGCTG
GCAGCGCGCGGCTTCTCAGAGCTGAGCACCCTGGAGGTGCTGCCACAGGTCTACAACGTG
CGCACTGTCAGCCTGCCACCGCCCGACCTGGGCACAGGCACAGATGGCCCTGCCGGCTCC
GACACCAGCCCCTTCCGCAGCGGCACGCCCATGAAGGAGGCCGTGGGCCACACCGGCTAC
CTGACCTTGGCCAGAAGCTGGGGTGAGCTGACCCAGAATCCCTGCCCTGCTCTCCCCAGC
GCTAGGAGACCAGGCCAGCCCAGGAACCAGGGAGGTGACCCTGCTCTCTGGCCTCCTGGC
TGA
Enzyme 40 GenBank Gene ID AK097771 Link Image
Enzyme 40 GeneCard ID Q96FX7 Link Image
Enzyme 40 GenAtlas ID TRM61 Link Image
Enzyme 40 HGNC ID HGNC:23790 Link Image
Enzyme 40 Chromosome Location Not Available
Enzyme 40 Locus Not Available
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 General References Not Available
Enzyme 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 14789
Enzyme 41 Name tRNA
Enzyme 41 Synonyms
  1. guanine-N(7--methyltransferase
  2. tRNA(m7G46- methyltransferase
  3. Methyltransferase-like protein 1
Enzyme 41 Gene Name METTL1
Enzyme 41 Protein Sequence >tRNA
MAAETRNVAGAEAPPPQKRYYRQRAHSNPMADHTLRYPVKPEEMDWSELYPEFFAPLTQN
QSHDDPKDKKEKRAQAQVEFADIGCGYGGLLVELSPLFPDTLILGLEIRVKVSDYVQDRI
RALRAAPAGGFQNIACLRSNAMKHLPNFFYKGQLTKMFFLFPDPHFKRTKHKWRIISPTL
LAEYAYVLRVGGLVYTITDVLELHDWMCTHFEEHPLFERVPLEDLSEDPVVGHLGTSTEE
GKKVLRNGGKNFPAIFRRIQDPVLQAVTSQTSLPGH
Enzyme 41 Number of Residues 276
Enzyme 41 Molecular Weight 31471
Enzyme 41 Theoretical pI 7.73
Enzyme 41 GO Classification
Function
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
Component
Enzyme 41 General Function Not Available
Enzyme 41 Specific Function Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA
Enzyme 41 Pathways Not Available
Enzyme 41 Reactions
  • S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N7-methylguanine [RN:R00600] ALL_REAC R00600
Enzyme 41 Pfam Domain Function
Enzyme 41 Signals
  • None
Enzyme 41 Transmembrane Regions
  • None
Enzyme 41 Essentiality Not Available
Enzyme 41 GenBank ID Protein 4160184 Link Image
Enzyme 41 UniProtKB/Swiss-Prot ID Q9UBP6 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name TRMB_HUMAN Link Image
Enzyme 41 PDB ID Not Available
Enzyme 41 Cellular Location Not Available
Enzyme 41 Gene Sequence >831 bp
ATGGCAGCCGAGACTCGGAACGTGGCCGGAGCAGAGGCCCCACCGCCCCAGAAGCGCTAC
TACCGGCAACGTGCTCACTCCAACCCCATGGCGGACCACACGCTGCGCTACCCTGTGAAG
CCAGAGGAGATGGACTGGTCTGAGCTATACCCAGAGTTCTTCGCTCCACTCACTCAAAAT
CAGAGCCACGATGACCCAAAGGATAAGAAAGAAAAGAGAGCTCAGGCCCAAGTGGAGTTT
GCAGACATAGGCTGTGGCTATGGTGGCCTGTTAGTGGAACTGTCACCGCTGTTCCCAGAC
ACACTTATTCTGGGTCTGGAGATCCGGGTGAAGGTCTCAGACTATGTACAAGACCGGATT
CGGGCCCTACGCGCAGCTCCTGCAGGTGGCTTCCAGAACATCGCCTGTCTCCGTAGCAAT
GCCATGAAGCACCTTCCTAACTTCTTCTACAAGGGCCAGCTGACAAAGATGTTCTTCCTC
TTCCCCGACCCACATTTCAAGCGGACAAAGCACAAGTGGCGAATCATCAGTCCCACCCTG
CTAGCAGAATATGCCTACGTGCTAAGAGTTGGGGGGCTGGTGTATACCATAACCGATGTG
CTGGAGCTACACGACTGGATGTGCACTCATTTCGAAGAGCACCCACTGTTTGAGCGTGTG
CCTCTGGAGGACCTGAGTGAAGACCCCGTTGTGGGACATCTAGGCACCTCAACTGAGGAG
GGGAAGAAAGTTCTACGTAATGGAGGGAAGAATTTCCCAGCCATCTTCCGAAGAATACAA
GATCCCGTCCTCCAGGCAGTGACCTCCCAAACCAGCCTGCCTGGTCACTGA
Enzyme 41 GenBank Gene ID Y18643 Link Image
Enzyme 41 GeneCard ID Q9UBP6 Link Image
Enzyme 41 GenAtlas ID METTL1 Link Image
Enzyme 41 HGNC ID HGNC:7030 Link Image
Enzyme 41 Chromosome Location 12
Enzyme 41 Locus 12q13
Enzyme 41 SNPs SNPJam Report Link Image
Enzyme 41 General References
  1. Bahr A, Hankeln T, Fiedler T, Hegemann J, Schmidt ER: Molecular analysis of METTL1, a novel human methyltransferase-like gene with a high degree of phylogenetic conservation. Genomics. 1999 May 1;57(3):424-8. [PubMed Link Image]
  2. Alexandrov A, Martzen MR, Phizicky EM: Two proteins that form a complex are required for 7-methylguanosine modification of yeast tRNA. RNA. 2002 Oct;8(10):1253-66. [PubMed Link Image]
Enzyme 41 Metabolite References Not Available
Enzyme 42 [top]
Enzyme 42 ID 15244
Enzyme 42 Name 5-methyltetrahydrofolate-homocysteine methyltransferase reductase
Enzyme 42 Synonyms Not Available
Enzyme 42 Gene Name MTRR
Enzyme 42 Protein Sequence >5-methyltetrahydrofolate-homocysteine methyltransferase reductase
MRRFLLLYATQQGQAKAIAEEICEQAVVHGFSADLHCISESDKYDLKTETAPLVVVVSTT
GTGDPPDTARKFVKEIQNQTLPVDFFAHLRYGLLGLGDSEYTYFCNGGKIIDKRLQELGA
RHFYDTGHADDCVGLELVVEPWIAGLWPALRKHFRSSRGQEEISGALPVASPASSRTDLV
KSELLHIESQVELLRFDDSGRKDSEVLKQNAVNSNQSNVVIEDFESSLTRSVPPLSQASL
NIPGLPPEYLQVHLQESLGQEESQVSVTSADPVFQVPISKAVQLTTNDAIKTTLLVELDI
SNTDFSYQPGDAFSVICPNSDSEVQSLLQRLQLEDKREHCVLLKIKADTKKKGATLPQHI
PAGCSLQFIFTWCLEIRAIPKKAFLRALVDYTSDSAEKRRLQELCSKQGAADYSRFVRDA
CACLLDLLLAFPSCQPPLSLLLEHLPKLQPRPYSCASSSLFHPGKLHFVFNIVEFLSTAT
TEVLRKGVCTGWLALLVASVLQPNIHASHEDSGKALAPKISISPRTTNSFHLPDDPSIPI
IMVGPGTGIAPFIGFLQHREKLQEQHPDGNFGAMWLFFGCRHKDRDYLFRKELRHFLKHG
ILTHLKVSFSRDAPVGEEEAPAKYVQDNIQLHGQQVARILLQENGHIYVCGDAKNMAKDV
HDALVQIISKEVGVEKLEAMKTLATLKEEKRYLQDIWS
Enzyme 42 Number of Residues 698
Enzyme 42 Molecular Weight 77675
Enzyme 42 Theoretical pI 6.47
Enzyme 42 GO Classification
Function
  • FMN binding
  • binding
  • catalytic activity
  • electron transporter activity
  • nucleotide binding
  • oxidoreductase activity
  • transporter activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
Enzyme 42 General Function Inorganic ion transport and metabolism
Enzyme 42 Specific Function Not Available
Enzyme 42 Pathways Not Available
Enzyme 42 Reactions Not Available
Enzyme 42 Pfam Domain Function
Enzyme 42 Signals
  • None
Enzyme 42 Transmembrane Regions
  • None
Enzyme 42 Essentiality Not Available
Enzyme 42 GenBank ID Protein 127798340 Link Image
Enzyme 42 UniProtKB/Swiss-Prot ID Q7Z4M8 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name Q7Z4M8_HUMAN Link Image
Enzyme 42 PDB ID Not Available
Enzyme 42 Cellular Location Not Available
Enzyme 42 Gene Sequence >2097 bp
ATGAGGAGGTTTCTGTTACTATATGCTACACAGCAGGGACAGGCAAAGGCCATCGCAGAA
GAAATATGTGAGCAAGCTGTGGTACATGGATTTTCTGCAGATCTTCACTGTATTAGTGAA
TCCGATAAGTATGACCTAAAAACCGAAACAGCTCCTCTTGTTGTTGTGGTTTCTACCACG
GGCACCGGAGACCCACCCGACACAGCCCGCAAGTTTGTTAAGGAAATACAGAACCAAACA
CTGCCGGTTGATTTCTTTGCTCACCTGCGGTATGGGTTACTGGGTCTCGGTGATTCAGAA
TACACCTACTTTTGCAATGGGGGGAAGATAATTGATAAACGACTTCAAGAGCTTGGAGCC
CGGCATTTCTATGACACTGGACATGCAGATGACTGTGTAGGTTTAGAACTTGTGGTTGAG
CCGTGGATTGCTGGACTCTGGCCAGCCCTCAGAAAGCATTTTAGGTCAAGCAGAGGACAA
GAGGAGATAAGTGGCGCACTCCCGGTGGCATCACCTGCATCCTCGAGGACAGACCTTGTG
AAGTCAGAGCTGCTACACATTGAATCTCAAGTCGAGCTTCTGAGATTCGATGATTCAGGA
AGAAAGGATTCTGAGGTTTTGAAGCAAAATGCAGTGAACAGCAACCAATCCAATGTTGTA
ATTGAAGACTTTGAGTCCTCACTTACCCGTTCGGTACCCCCACTCTCACAAGCCTCTCTG
AATATTCCTGGTTTACCCCCAGAATATTTACAGGTACATCTGCAGGAGTCTCTTGGCCAG
GAGGAAAGCCAAGTATCTGTGACTTCAGCAGATCCAGTTTTTCAAGTGCCAATTTCAAAG
GCAGTTCAACTTACTACGAATGATGCCATAAAAACCACTCTGCTGGTAGAATTGGACATT
TCAAATACAGACTTTTCCTATCAGCCTGGAGATGCCTTCAGCGTGATCTGCCCTAACAGT
GATTCTGAGGTACAAAGCCTACTCCAAAGACTGCAGCTTGAAGATAAAAGAGAGCACTGC
GTCCTTTTGAAAATAAAGGCAGACACAAAGAAGAAAGGAGCTACCTTACCCCAGCATATA
CCTGCGGGATGTTCTCTCCAGTTCATTTTTACCTGGTGTCTTGAAATCCGAGCAATTCCT
AAAAAGGCATTTTTGCGAGCCCTTGTGGACTATACCAGTGACAGTGCTGAAAAGCGCAGG
CTACAGGAGCTGTGCAGTAAACAAGGGGCAGCCGATTATAGCCGCTTTGTACGAGATGCC
TGTGCCTGCTTGTTGGATCTCCTCCTCGCTTTCCCTTCTTGCCAGCCACCACTCAGTCTC
CTGCTCGAACATCTTCCTAAACTTCAACCCAGACCATATTCGTGTGCAAGCTCAAGTTTA
TTTCACCCAGGAAAGCTCCATTTTGTCTTCAACATTGTGGAATTTCTGTCTACTGCCACA
ACAGAGGTTCTGCGGAAGGGAGTATGTACAGGCTGGCTGGCCTTGTTGGTTGCTTCAGTT
CTTCAGCCAAACATACATGCATCCCATGAAGACAGCGGGAAAGCCCTGGCTCCTAAGATA
TCCATCTCTCCTCGAACAACAAATTCTTTCCACTTACCAGATGACCCCTCAATCCCCATC
ATAATGGTGGGTCCAGGAACCGGCATAGCCCCGTTTATTGGGTTCCTACAACATAGAGAG
AAACTCCAAGAACAACACCCAGATGGAAATTTTGGAGCAATGTGGTTGTTTTTTGGCTGC
AGGCATAAGGATAGGGATTATCTATTCAGAAAAGAGCTCAGACATTTCCTTAAGCATGGG
ATCTTAACTCATCTAAAGGTTTCCTTCTCAAGAGATGCTCCTGTTGGGGAGGAGGAAGCC
CCAGCAAAGTATGTGCAAGACAACATCCAGCTTCATGGCCAGCAGGTGGCGAGAATCCTC
CTCCAGGAGAACGGCCATATTTATGTGTGTGGAGATGCAAAGAATATGGCCAAGGATGTA
CATGATGCCCTTGTGCAAATAATAAGCAAAGAGGTTGGAGTTGAAAAACTAGAAGCAATG
AAAACCCTGGCCACTTTAAAAGAAGAAAAACGCTACCTTCAGGATATTTGGTCATAA
Enzyme 42 GenBank Gene ID BC054816 Link Image
Enzyme 42 GeneCard ID Q7Z4M8 Link Image
Enzyme 42 GenAtlas ID Not Available
Enzyme 42 HGNC ID Not Available
Enzyme 42 Chromosome Location Not Available
Enzyme 42 Locus Not Available
Enzyme 42 SNPs SNPJam Report Link Image
Enzyme 42 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]
Enzyme 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 15862
Enzyme 43 Name DNA (cytosine-5)-methyltransferase 3-like
Enzyme 43 Synonyms Not Available
Enzyme 43 Gene Name DNMT3L
Enzyme 43 Protein Sequence >DNA (cytosine-5)-methyltransferase 3-like
MAAIPALDPEAEPSMDVILVGSSELSSSVSPGTGRDLIAYEVKANQRNIEDICICCGSLQ
VHTQHPLFEGGICAPCKDKFLDALFLYDDDGYQSYCSICCSGETLLICGNPDCTRCYCFE
CVDSLVGPGTSGKVHAMSNWVCYLCLPSSRSGLLQRRRKWRSQLKAFYDRESENPLEMFE
TVPVWRRQPVRVLSLFEDIKKELTSLGFLESGSDPGQLKHVVDVTDTVRKDVEEWGPFDL
VYGATPPLGHTCDRPPSWYLFQFHRLLQYARPKPGSPRPFFWMFVDNLVLNKEDLDVASR
FLEMEPVTIPDVHGGSLQNAVRVWSNIPAIRSSRHWALVSEEELSLLAQNKQSSKLAAKW
PTKLVKNCFLPLREYFKYFSTELTSSL
Enzyme 43 Number of Residues 387
Enzyme 43 Molecular Weight 43670
Enzyme 43 Theoretical pI 5.67
Enzyme 43 GO Classification Not Available
Enzyme 43 General Function Not Available
Enzyme 43 Specific Function Probably not catalytically active as it has lost the active site residues. May function not directly as a DNA methyltransferase but as a regulator of methylation at imprinted loci. It is required specifically for the establishment of genomic imprints but is dispensable for their propagation. It is essential for the de novo methylation of single-copy DNA sequences
Enzyme 43 Pathways Not Available
Enzyme 43 Reactions Not Available
Enzyme 43 Pfam Domain Function Not Available
Enzyme 43 Signals
  • None
Enzyme 43 Transmembrane Regions
  • None
Enzyme 43 Essentiality Not Available
Enzyme 43 GenBank ID Protein Not Available
Enzyme 43 UniProtKB/Swiss-Prot ID Q9UJW3 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name DNM3L_HUMAN Link Image
Enzyme 43 PDB ID Not Available
Enzyme 43 Cellular Location Not Available
Enzyme 43 Gene Sequence Not Available
Enzyme 43 GenBank Gene ID AF194032 Link Image
Enzyme 43 GeneCard ID Q9UJW3 Link Image
Enzyme 43 GenAtlas ID DNMT3L Link Image
Enzyme 43 HGNC ID HGNC:2980 Link Image
Enzyme 43 Chromosome Location 21
Enzyme 43 Locus 21q22.3
Enzyme 43 SNPs SNPJam Report Link Image
Enzyme 43 General References
  1. Aapola U, Kawasaki K, Scott HS, Ollila J, Vihinen M, Heino M, Shintani A, Kawasaki K, Minoshima S, Krohn K, Antonarakis SE, Shimizu N, Kudoh J, Peterson P: Isolation and initial characterization of a novel zinc finger gene, DNMT3L, on 21q22.3, related to the cytosine-5-methyltransferase 3 gene family. Genomics. 2000 May 1;65(3):293-8. [PubMed Link Image]
  2. Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [PubMed Link Image]
Enzyme 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 15863
Enzyme 44 Name Euchromatic histone-lysine N-methyltransferase 2 (Euchromatic histone- lysine N-methyltransferase 2, isoform CRA_c) (HLA-B associated transcript 8)
Enzyme 44 Synonyms Not Available
Enzyme 44 Gene Name EHMT2
Enzyme 44 Protein Sequence >Euchromatic histone-lysine N-methyltransferase 2 (Euchromatic histone- lysine N-methyltransferase 2, isoform CRA_c) (HLA-B associated transcript 8)
MAAAAGAAAAAAAEGEAPAEMGALLLEKETRGATERVHGSLGDTPRSEETLPKATPDSLE
PAGPSSPASVTVTVGDEGADTPVGATPLIGDESENLEGDGDLRGGRILLGHATKSFPSSP
SKGGSCPSRAKMSMTGAGKSPPSVQSLAMRLLSMPGAQGAAAAGSEPPPATTSPEGQPKV
HRARKTMSKPGNGQPPVPEKRPPEIQHFRMSDDVHSLGKVTSDLAKRRKLNSGGGLSEEL
GSARRSGEVTLTKGDPGSLEEWETVVGDDFSLYYDSYSVDERVDSDSKSEVEALTEQLSE
EEEEEEEEEEEEEEEEEEEEEEEDEESGNQSDRSGSSGRRKAKKKWRKDSPWVKPSRKRR
KREPPRAKEPRGVNGVGSSGPSEYMEVPLGSLELPSEGTLSPNHAGVSNDTSSLETERGF
EELPLCSCRMEAPKIDRISERAGHKCMATESVDGELSGCNAAILKRETMRPSSRVALMVL
CETHRARMVKHHCCPGCGYFCTAGTFLECHPDFRVAHRFHKACVSQLNGMVFCPHCGEDA
SEAQEVTIPRGDGVTPPAGTAAPAPPPLSQDVPGRADTSQPSARMRGHGEPRRPPCDPLA
DTIDSSGPSLTLPNGGCLSAVGLPLGPGREALEKALVIQESERRKKLRFHPRQLYLSVKQ
GELQKVILMLLDNLDPNFQSDQQSKRTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRT
PLMEAVVNNHLEVARYMVQRGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGQVDVNA
QDSGGWTPIIWAAEHKHIEVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNA
RCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTAWDLTPERSDVWFA
LQLNRKLRLGVGNRAIRTEKIICRDVARGYENVPIPCVNGVDGEPCPEDYKYISENCETS
TMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQA
CSCWRNCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVR
EDDSYLFDLDNKDGEVYCIDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFS
SRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQSRLARLDPHPELLP
ELGSLPPVNT
Enzyme 44 Number of Residues 1210
Enzyme 44 Molecular Weight 132372
Enzyme 44 Theoretical pI 5.14
Enzyme 44 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • histone-lysine N-methyltransferase activity
  • ion binding
  • methyltransferase activity
  • protein methyltransferase activity
  • protein-lysine N-methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
  • transition metal ion binding
  • zinc ion binding
Process
  • DNA metabolism
  • DNA packaging
  • cellular metabolism
  • chromatin modification
  • establishment and/or maintenance of chromatin architecture
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 44 General Function Not Available
Enzyme 44 Specific Function S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N(6)-methyl-L-lysine
Enzyme 44 Pathways Not Available
Enzyme 44 Reactions Not Available
Enzyme 44 Pfam Domain Function
Enzyme 44 Signals
  • None
Enzyme 44 Transmembrane Regions
  • None
Enzyme 44 Essentiality Not Available
Enzyme 44 GenBank ID Protein Not Available
Enzyme 44 UniProtKB/Swiss-Prot ID Q5JQ92 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name Q5JQ92_HUMAN Link Image
Enzyme 44 PDB ID Not Available
Enzyme 44 Cellular Location Not Available
Enzyme 44 Gene Sequence Not Available
Enzyme 44 GenBank Gene ID AL662834 Link Image
Enzyme 44 GeneCard ID Q5JQ92 Link Image
Enzyme 44 GenAtlas ID EHMT2 Link Image
Enzyme 44 HGNC ID HGNC:14129 Link Image
Enzyme 44 Chromosome Location Not Available
Enzyme 44 Locus Not Available
Enzyme 44 SNPs SNPJam Report Link Image
Enzyme 44 General References Not Available
Enzyme 44 Metabolite References Not Available
Enzyme 45 [top]
Enzyme 45 ID 15864
Enzyme 45 Name Enhancer of zeste homolog 1
Enzyme 45 Synonyms
  1. ENX-2
Enzyme 45 Gene Name EZH1
Enzyme 45 Protein Sequence >Enhancer of zeste homolog 1
MEIPNPPTSKCITYWKRKVKSEYMRLRQLKRLQANMGAKALYVANFAKVQEKTQILNEEW
KKLRVQPVQSMKPVSGHPFLKKCTIESIFPGFASQHMLMRSLNTVALVPIMYSWSPLQQN
FMVEDETVLCNIPYMGDEVKEEDETFIEELINNYDGKVHGEEEMIPGSVLISDAVFLELV
DALNQYSDEEEEGHNDTSDGKQDDSKEDLPVTRKRKRHAIEGNKKSSKKQFPNDMIFSAI
ASMFPENGVPDDMKERYRELTEMSDPNALPPQCTPNIDGPNAKSVQREQSLHSFHTLFCR
RCFKYDCFLHPFHATPNVYKRKNKEIKIEPEPCGTDCFLLLEGAKEYAMLHNPRSKCSGR
RRRRHHIVSASCSNASASAVAETKEGDSDRDTGNDWASSSSEANSRCQTPTKQKASPAPP
QLCVVEAPSEPVEWTGAEESLFRVFHGTYFNNFCSIARLLGTKTCKQVFQFAVKESLILK
LPTDELMNPSQKKKRKHRLWAAHCRKIQLKKDNSSTQVYNYQPCDHPDRPCDSTCPCIMT
QNFCEKFCQCNPDCQNRFPGCRCKTQCNTKQCPCYLAVRECDPDLCLTCGASEHWDCKVV
SCKNCSIQRGLKKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKVYD
KYMSSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVVMVNGDHRIGIFAKRAIQAG
EELFFDYRYSQADALKYVGIERETDVL
Enzyme 45 Number of Residues 747
Enzyme 45 Molecular Weight 85272
Enzyme 45 Theoretical pI 7.77
Enzyme 45 GO Classification
Function
  • DNA binding
  • binding
  • nucleic acid binding
Process
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 45 General Function Not Available
Enzyme 45 Specific Function May be involved in the regulation of gene transcription and chromatin structure
Enzyme 45 Pathways Not Available
Enzyme 45 Reactions Not Available
Enzyme 45 Pfam Domain Function
Enzyme 45 Signals
  • None
Enzyme 45 Transmembrane Regions
  • None
Enzyme 45 Essentiality Not Available
Enzyme 45 GenBank ID Protein Not Available
Enzyme 45 UniProtKB/Swiss-Prot ID Q92800 Link Image
Enzyme 45 UniProtKB/Swiss-Prot Entry Name EZH1_HUMAN Link Image
Enzyme 45 PDB ID Not Available
Enzyme 45 Cellular Location Not Available
Enzyme 45 Gene Sequence Not Available
Enzyme 45 GenBank Gene ID U50315 Link Image
Enzyme 45 GeneCard ID Q92800 Link Image
Enzyme 45 GenAtlas ID EZH1 Link Image
Enzyme 45 HGNC ID HGNC:3526 Link Image
Enzyme 45 Chromosome Location 17
Enzyme 45 Locus 17q21.1-q21.3
Enzyme 45 SNPs SNPJam Report Link Image
Enzyme 45 General References
  1. Abel KJ, Brody LC, Valdes JM, Erdos MR, McKinley DR, Castilla LH, Merajver SD, Couch FJ, Friedman LS, Ostermeyer EA, Lynch ED, King MC, Welcsh PL, Osborne-Lawrence S, Spillman M, Bowcock AM, Collins FS, Weber BL: Characterization of EZH1, a human homolog of Drosophila Enhancer of zeste near BRCA1. Genomics. 1996 Oct 15;37(2):161-71. [PubMed Link Image]
  2. Ogawa M, Hiraoka Y, Taniguchi K, Aiso S: Cloning and expression of a human/mouse Polycomb group gene, ENX-2/Enx-2. Biochim Biophys Acta. 1998 Jan 21;1395(2):151-8. [PubMed Link Image]
  3. Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1997 Apr 28;4(2):141-50. [PubMed Link Image]
  4. Rommens JM, Durocher F, McArthur J, Tonin P, LeBlanc JF, Allen T, Samson C, Ferri L, Narod S, Morgan K, et al.: Generation of a transcription map at the HSD17B locus centromeric to BRCA1 at 17q21. Genomics. 1995 Aug 10;28(3):530-42. [PubMed Link Image]
Enzyme 45 Metabolite References Not Available
Enzyme 46 [top]
Enzyme 46 ID 15865
Enzyme 46 Name Enhancer of zeste homolog 2 (Drosophila) (Enhancer of zeste homolog 2 (Drosophila), isoform CRA_a)
Enzyme 46 Synonyms Not Available
Enzyme 46 Gene Name EZH2
Enzyme 46 Protein Sequence >Enhancer of zeste homolog 2 (Drosophila) (Enhancer of zeste homolog 2 (Drosophila), isoform CRA_a)
MGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKSMFSSNRQKILERTEILNQEW
KQRRIQPVHILTSVSSLRGTRECSVTSDLDFPTQVIPLKTLNAVASVPIMYSWSPLQQNF
MVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQ
YNDDDDDDDGDDPEEREEKQKDLEDHRDDKESRPPRKFPSDKIFEAISSMFPDKGTAEEL
KEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHRKC
NYSFHATPNTYKRKNTETALDNKPCGPQCYQHLEGAKEFAAALTAERIKTPPKRPGGRRR
GRLPNNSSRPSTPTINVLESKDTDSDREAGTETGGENNDKEEEEKKDETSSSSEANSRCQ
TPIKMKPNIEPPENVEWSGAEASMFRVLIGTYYDNFCAIARLIGTKTCRQVYEFRVKESS
IIAPAPAEDVDTPPRKKKRKHRLWAAHCRKIQLKKDGSSNHVYNYQPCDHPRQPCDSSCP
CVIAQNFCEKFCQCSSECQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCLTCGAADHWD
SKNVSCKNCSIQRGSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRG
KVYDKYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHRIGIFAKRA
IQTGEELFFDYRYSQADALKYVGIEREMEIP
Enzyme 46 Number of Residues 751
Enzyme 46 Molecular Weight 86019
Enzyme 46 Theoretical pI 7.22
Enzyme 46 GO Classification
Function
  • DNA binding
  • binding
  • nucleic acid binding
Process
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 46 General Function Not Available
Enzyme 46 Specific Function Not Available
Enzyme 46 Pathways Not Available
Enzyme 46 Reactions Not Available
Enzyme 46 Pfam Domain Function
Enzyme 46 Signals
  • None
Enzyme 46 Transmembrane Regions
  • None
Enzyme 46 Essentiality Not Available
Enzyme 46 GenBank ID Protein Not Available
Enzyme 46 UniProtKB/Swiss-Prot ID Q96FI6 Link Image
Enzyme 46 UniProtKB/Swiss-Prot Entry Name Q96FI6_HUMAN Link Image
Enzyme 46 PDB ID Not Available
Enzyme 46 Cellular Location Not Available
Enzyme 46 Gene Sequence Not Available
Enzyme 46 GenBank Gene ID BC010858 Link Image
Enzyme 46 GeneCard ID Q96FI6 Link Image
Enzyme 46 GenAtlas ID EZH2 Link Image
Enzyme 46 HGNC ID HGNC:3527 Link Image
Enzyme 46 Chromosome Location Not Available
Enzyme 46 Locus Not Available
Enzyme 46 SNPs SNPJam Report Link Image
Enzyme 46 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]
Enzyme 46 Metabolite References Not Available
Enzyme 47 [top]
Enzyme 47 ID 15866
Enzyme 47 Name cDNA FLJ75818, highly similar to Homo sapiens PR/SET domain containing protein 8 (SET8), mRNA
Enzyme 47 Synonyms Not Available
Enzyme 47 Gene Name Not Available
Enzyme 47 Protein Sequence >cDNA FLJ75818, highly similar to Homo sapiens PR/SET domain containing protein 8 (SET8), mRNA
MARGRKMSKPRAVEAAAAAAAVAATAPGPEMVERRGPGRPRTDGENVFTGQSKIYSYMSP
NKCSGMRFPLQEENSVTHHEVKCQGKPLAGIYRKREEKRNAGNAVRSAMKSEEQKIKDAR
KGPLVPFPNQKSEAAEPPKTPPSSCDSTNAAIAKQALKKPIKGKQAPRKKAQGKTQQNRK
LTDFYPVRRSSRKSKAELQSEERKRIDELIESGKEEGMKIDLIDGKGRGVIATKQFSRGD
FVVEYHGDLIEITDAKKREALYAQDPSTGCYMYYFQYLSKTYCVDATRETNRLGRLINHS
KCGNCQTKLHDIDGVPHLILIASRDIAAGEELLYDYGDRSKASIEAHPWLKH
Enzyme 47 Number of Residues 352
Enzyme 47 Molecular Weight 39223
Enzyme 47 Theoretical pI 10.12
Enzyme 47 GO Classification Not Available
Enzyme 47 General Function Not Available
Enzyme 47 Specific Function Not Available
Enzyme 47 Pathways Not Available
Enzyme 47 Reactions Not Available
Enzyme 47 Pfam Domain Function Not Available
Enzyme 47 Signals
  • None
Enzyme 47 Transmembrane Regions
  • None
Enzyme 47 Essentiality Not Available
Enzyme 47 GenBank ID Protein Not Available
Enzyme 47 UniProtKB/Swiss-Prot ID A8K9D0 Link Image
Enzyme 47 UniProtKB/Swiss-Prot Entry Name A8K9D0_HUMAN Link Image
Enzyme 47 PDB ID Not Available
Enzyme 47 Cellular Location Not Available
Enzyme 47 Gene Sequence Not Available
Enzyme 47 GenBank Gene ID AK292645 Link Image
Enzyme 47 GeneCard ID A8K9D0 Link Image
Enzyme 47 GenAtlas ID Not Available
Enzyme 47 HGNC ID Not Available
Enzyme 47 Chromosome Location Not Available
Enzyme 47 Locus Not Available
Enzyme 47 SNPs Not Available
Enzyme 47 General References Not Available
Enzyme 47 Metabolite References Not Available
Enzyme 48 [top]
Enzyme 48 ID 15867
Enzyme 48 Name Wolf-Hirschhorn syndrome candidate 1 (Wolf-Hirschhorn syndrome candidate 1, isoform CRA_e)
Enzyme 48 Synonyms Not Available
Enzyme 48 Gene Name WHSC1
Enzyme 48 Protein Sequence >Wolf-Hirschhorn syndrome candidate 1 (Wolf-Hirschhorn syndrome candidate 1, isoform CRA_e)
MEFSIKQSPLSVQSVVKCIKMKQAPEILGSANGKTPSCEVNRECSVFLSKAQLSSSLQEG
VMQKFNGHDALPFIPADKLKDLTSRVFNGEPGAHDAKLRFESQEMKGIGTPPNTTPIKNG
SPEIKLKITKTYMNGKPLFESSICGDSAADVSQSEENGQKPENKARRNRKRSIKYDSLLE
QGLVEAALVSKISSPSDKKIPAKKESCPNTGRDKDHLLKYNVGDLVWSKVSGYPWWPCMV
SADPLLHSYTKLKGQKKSARQYHVQFFGDAPERAWIFEKSLVAFEGEGQFEKLCQESAKQ
APTKAEKIKLLKPISGKLRAQWEMGIVQAEEAASMSVEERKAKFTFLYVGDQLHLNPQVA
KEAGIAAESLGEMAESSGVSEEAAENPKSVREECIPMKRRRRAKLCSSAETLESHPDIGK
STPQKTAEADPRRGVGSPPGRKKTTVSMPRSRKGDAASQFLVFCQKHRDEVVAEHPDASG
EEIEELLRSQWSLLSEKQRARYNTKFALVAPVQAEEDSGNVNGKKRNHTKRIQDPTEDAE
AEDTPRKRLRTDKHSLRKRDTITDKTARTSSYKAMEAASSLKSQAATKNLSDACKPLKKR
NRASTAASSALGFSKSSSPSASLTENEVSDSPGDEPSESPYESADETQTEVSVSSKKSER
GVTAKKEYVCQLCEKPGSLLLCEGPCCGAFHLACLGLSRRPEGRFTCSECASGIHSCFVC
KESKTDVKRCVVTQCGKFYHEACVKKYPLTVFESRGFRCPLHSCVSCHASNPSNPRPSKG
KMMRCVRCPVAYHSGDACLAAGCSVIASNSIICTAHFTARKGKRHHAHVNVSWCFVCSKG
GSLLCCESCPAAFHPDCLNIEMPDGSWFCNDCRAGKKLHFQDIIWVKLGNYRWWPAEVCH
PKNVPPNIQKMKHEIGEFPVFFFGSKDYYWTHQARVFPYMEGDRGSRYQGVRGIGRVFKN
ALQEAEARFREIKLQREARETQESERKPPPYKHIKVNKPYGKVQIYTADISEIPKCNCKP
TDENPCGFDSECLNRMLMFECHPQVCPAGEFCQNQCFTKRQYPETKIIKTDGKGWGLVAK
RDIRKGEFVNEYVGELIDEEECMARIKHAHENDITHFYMLTIDKDRIIDAGPKGNYSRFM
NHSCQPNCETLKWTVNGDTRVGLFAVCDIPAGTELTFNYNLDCLGNEKTVCRCGASNCSG
FLGDRPKTSTTLSSEEKGKKTKKKTRRRRAKGEGKRQSEDECFRCGDGGQLVLCDRKFCT
KAYHLSCLGLGKRPFGKWECPWHHCDVCGKPSTSFCHLCPNSFCKEHQDGTAFSCTPDGR
SYCCEHDLGAASVRSTKTEKPPPEPGKPKGKRRRRRGWRRVTEGK
Enzyme 48 Number of Residues 1365
Enzyme 48 Molecular Weight 152259
Enzyme 48 Theoretical pI 8.81
Enzyme 48 GO Classification
Function
  • DNA binding
  • acid-amino acid ligase activity
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • nucleic acid binding
  • protein binding
  • transition metal ion binding
  • ubiquitin-protein ligase activity
  • zinc ion binding
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein modification
  • protein ubiquitination
  • regulation of biological process
  • regulation of cellular metabolism
  • regulation of metabolism
  • regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • regulation of physiological process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
  • ubiquitin cycle
Component
  • protein complex
  • ubiquitin ligase complex
Enzyme 48 General Function Not Available
Enzyme 48 Specific Function Not Available
Enzyme 48 Pathways Not Available
Enzyme 48 Reactions Not Available
Enzyme 48 Pfam Domain Function
Enzyme 48 Signals
  • None
Enzyme 48 Transmembrane Regions
  • None
Enzyme 48 Essentiality Not Available
Enzyme 48 GenBank ID Protein Not Available
Enzyme 48 UniProtKB/Swiss-Prot ID A2A2T3 Link Image
Enzyme 48 UniProtKB/Swiss-Prot Entry Name A2A2T3_HUMAN Link Image
Enzyme 48 PDB ID Not Available
Enzyme 48 Cellular Location Not Available
Enzyme 48 Gene Sequence Not Available
Enzyme 48 GenBank Gene ID AL132868 Link Image
Enzyme 48 GeneCard ID A2A2T3 Link Image
Enzyme 48 GenAtlas ID Not Available
Enzyme 48 HGNC ID Not Available
Enzyme 48 Chromosome Location Not Available
Enzyme 48 Locus Not Available
Enzyme 48 SNPs SNPJam Report Link Image
Enzyme 48 General References Not Available
Enzyme 48 Metabolite References Not Available
Enzyme 49 [top]
Enzyme 49 ID 15868
Enzyme 49 Name EHMT1 protein
Enzyme 49 Synonyms Not Available
Enzyme 49 Gene Name EHMT1
Enzyme 49 Protein Sequence >EHMT1 protein
MAAADAEAVPARGEPQQDCCVKTELLGEETPMAADEGSAEKQAGEAHMAADGETNGSCEN
SDASSHANAAKHTQDSARVNPQDGTNTLTRIAENGVSERDSEAAKQNHVTADDFVQTSVI
GSNGYILNKPALQAQPLRTTSTLASSLPGHAAKTLPGGAGKGRTPSAFPQTPAAPPATLG
EGSADTEDRKLPAPGADVKVHRARKTMPKSVVGLHAASKDPREVREARDHKEPKEEINKN
ISDFGRQQLLPPFPSLHQSLPQNQCYMATTKSQTACLPFVLAAAVSRKKKRRMGTYSLVP
KKKTKVLKQRTVIEMFKSITHSTVGSKGEKDLGASSLHVNGESLEMDSDEDDSEELEEDD
GHGAEQAAAFPTEDSRTSKESMSEADRAQKMDGESEEEQESVDTGEEEEGGDESDLSSES
SIKKKFLKRKGKTDSPWIKPARKRRRRSRKKPSGALGSESYKSSAGSAEQTAPGDSTGYM
EVSLDSLDLRVKGILSSQAEGLANGPDVLETDGLQEVPLCSCRMETPKSREITTLANNQC
MATESVDHELGRCTDSVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCGYFCTAGNF
MECQPESSISHRFHKDCASRVNNASYCPHCGEESSKAKEVTIAKADTTSTVTPVPGQEKG
SALEGRADTTTGSAAGPPLSEDDKLQGAASHVPEGFDPTGPAGLGRPTPGLSQGPGKETL
ESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQNKRSPLHAA
AEAGHVDICHMLVQFCRLGSPRSRGCLW
Enzyme 49 Number of Residues 808
Enzyme 49 Molecular Weight 86705
Enzyme 49 Theoretical pI 6.18
Enzyme 49 GO Classification Not Available
Enzyme 49 General Function Not Available
Enzyme 49 Specific Function Not Available
Enzyme 49 Pathways Not Available
Enzyme 49 Reactions Not Available
Enzyme 49 Pfam Domain Function Not Available
Enzyme 49 Signals
  • None
Enzyme 49 Transmembrane Regions
  • None
Enzyme 49 Essentiality Not Available
Enzyme 49 GenBank ID Protein Not Available
Enzyme 49 UniProtKB/Swiss-Prot ID Q86X08 Link Image
Enzyme 49 UniProtKB/Swiss-Prot Entry Name Q86X08_HUMAN Link Image
Enzyme 49 PDB ID Not Available
Enzyme 49 Cellular Location Not Available
Enzyme 49 Gene Sequence Not Available
Enzyme 49 GenBank Gene ID BC047504 Link Image
Enzyme 49 GeneCard ID Q86X08 Link Image
Enzyme 49 GenAtlas ID EHMT1 Link Image
Enzyme 49 HGNC ID HGNC:24650 Link Image
Enzyme 49 Chromosome Location Not Available
Enzyme 49 Locus Not Available
Enzyme 49 SNPs SNPJam Report Link Image
Enzyme 49 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]
Enzyme 49 Metabolite References Not Available
Enzyme 50 [top]
Enzyme 50 ID 15869
Enzyme 50 Name cDNA FLJ78356, highly similar to Homo sapiens PIMT isozyme I
Enzyme 50 Synonyms Not Available
Enzyme 50 Gene Name Not Available
Enzyme 50 Protein Sequence >cDNA FLJ78356, highly similar to Homo sapiens PIMT isozyme I
MAWKSGGASHSELIHNLRKNGIIKTDKVFEVMLATDRSHYAKCNPYMDSPQSIGFQATIS
APHMHAYALELLFDQLHEGAKALDVGSGSGILTACFARMVGCTGKVIGIDHIKELVDDSV
NNVRKDDPTLLSSGRVQLVVGDGRMGYAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLI
LPVGPAGGNQMLEQYDKLQDGSIKMKPLMGVIYVPLTDKEKQWSRWK
Enzyme 50 Number of Residues 227
Enzyme 50 Molecular Weight 24637
Enzyme 50 Theoretical pI 7.25
Enzyme 50 GO Classification Not Available
Enzyme 50 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 50 Specific Function Not Available
Enzyme 50 Pathways Not Available
Enzyme 50 Reactions Not Available
Enzyme 50 Pfam Domain Function Not Available
Enzyme 50 Signals
  • None
Enzyme 50 Transmembrane Regions
  • None
Enzyme 50 Essentiality Not Available
Enzyme 50 GenBank ID Protein Not Available
Enzyme 50 UniProtKB/Swiss-Prot ID A8K109 Link Image
Enzyme 50 UniProtKB/Swiss-Prot Entry Name A8K109_HUMAN Link Image
Enzyme 50 PDB ID 1KR5 Link Image
Enzyme 50 PDB File Show
Enzyme 50 3D Structure
Enzyme 50 Cellular Location Not Available
Enzyme 50 Gene Sequence Not Available
Enzyme 50 GenBank Gene ID AK289724 Link Image
Enzyme 50 GeneCard ID A8K109 Link Image
Enzyme 50 GenAtlas ID Not Available
Enzyme 50 HGNC ID Not Available
Enzyme 50 Chromosome Location Not Available
Enzyme 50 Locus Not Available
Enzyme 50 SNPs Not Available
Enzyme 50 General References Not Available
Enzyme 50 Metabolite References Not Available
Enzyme 51 [top]
Enzyme 51 ID 15870
Enzyme 51 Name Uncharacterized protein PRMT5 (Protein arginine methyltransferase 5, isoform CRA_d)
Enzyme 51 Synonyms Not Available
Enzyme 51 Gene Name PRMT5
Enzyme 51 Protein Sequence >Uncharacterized protein PRMT5 (Protein arginine methyltransferase 5, isoform CRA_d)
MRGPNSGTEKGRLVIPEKQGFDFLCMPVFHPRFKREFIQEPAKNRPGPQTRSDLLLSGRD
WNTLIVGKLSPWIRPDSKVEKIRRNSEAAMLQELNFGAYLGLPAFLLPLNQEDNTNLARV
LTNHIHTGHHSSMFWMRVPLVAPEDLRDDIIENAPTTHTEEYSGEEKTWMWWHNFRTLCD
YSKRIAVALEIGADLPSNHVIDRWLGEPIKAAILPTSIFLTNKKGFPVLSKMHQRLIFRL
LKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELFAKGYEDYLQSPLQPLMD
NLESQTYEVFEKDPIKYSQYQQAIYKCLLDRVPEEEKDTNVQVLMVLGAGRGPLVNASLR
AAKQADRRIKLYAVEKNPNAVVTLENWQFEEWGSQVTVVSSDMREWVAPEKADIIVSELL
GSFADNELSPECLDGAQHFLKDDGVSIPGEYTSFLAPISSSKLYNEVRACREKDRDPEAQ
FEMPYVVRLHNFHQLSAPQPCFTFSHPNRDPMIDNNRYCTLEFPVEVNTVLHGFAGYFET
VLYQDITLSIRPETHSPGMFSWFPILFPIKQPITVREGQTICVRFWRCSNSKKVWYEWAV
TAPVCSAIHNPTGRSYTIGL
Enzyme 51 Number of Residues 620
Enzyme 51 Molecular Weight 71321
Enzyme 51 Theoretical pI 6.42
Enzyme 51 GO Classification Not Available
Enzyme 51 General Function Not Available
Enzyme 51 Specific Function Not Available
Enzyme 51 Pathways Not Available
Enzyme 51 Reactions Not Available
Enzyme 51 Pfam Domain Function Not Available
Enzyme 51 Signals
  • None
Enzyme 51 Transmembrane Regions
  • None
Enzyme 51 Essentiality Not Available
Enzyme 51 GenBank ID Protein Not Available
Enzyme 51 UniProtKB/Swiss-Prot ID A8MZ91 Link Image
Enzyme 51 UniProtKB/Swiss-Prot Entry Name A8MZ91_HUMAN Link Image
Enzyme 51 PDB ID Not Available
Enzyme 51 Cellular Location Not Available
Enzyme 51 Gene Sequence Not Available
Enzyme 51 GenBank Gene ID AL132780 Link Image
Enzyme 51 GeneCard ID A8MZ91 Link Image
Enzyme 51 GenAtlas ID PRMT5 Link Image
Enzyme 51 HGNC ID HGNC:10894 Link Image
Enzyme 51 Chromosome Location 14
Enzyme 51 Locus 14q11.2-q21
Enzyme 51 SNPs SNPJam Report Link Image
Enzyme 51 General References
  1. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed Link Image]
Enzyme 51 Metabolite References Not Available
Enzyme 52 [top]
Enzyme 52 ID 15871
Enzyme 52 Name Uncharacterized protein CARM1 (Coactivator-associated arginine methyltransferase 1, isoform CRA_b)
Enzyme 52 Synonyms Not Available
Enzyme 52 Gene Name CARM1
Enzyme 52 Protein Sequence >Uncharacterized protein CARM1 (Coactivator-associated arginine methyltransferase 1, isoform CRA_b)
MAAAAAAVGPGAGGAGSAVPGGAGPCATVSVFPGARLLTIGDANGEIQRHAEQQALRLEV
RAGPDSAGIALYSHEDVCVFKCSVSRETECSRVGKQSFIITLGCNSVLIQFATPNDFCSF
YNILKTCRGHTLERSVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNH
TDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDRIVVIPG
KVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSGNMFPTIGDVHLAPFTDE
QLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEYFRQPVVDTFDIRILMAKSVKYTVNFL
EAKEGDLHRIEIPFKFHMLHSGLVHGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRC
LFQSPLFAKAGDTLSGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYTGTT
PSPPPGSHYTSPSENMWNTGSTYNLSSGMAVAGMPTAYDLSSVIASGSSVGHNNLIPLAN
TGIVNHTHSRMGSIMSTGIVQGSSGAQGSGGGSTSAHYAVNSQFTMGGPAISMASPMSIP
TNTMHYGS
Enzyme 52 Number of Residues 608
Enzyme 52 Molecular Weight 65854
Enzyme 52 Theoretical pI 6.73
Enzyme 52 GO Classification Not Available
Enzyme 52 General Function Not Available
Enzyme 52 Specific Function Not Available
Enzyme 52 Pathways Not Available
Enzyme 52 Reactions Not Available
Enzyme 52 Pfam Domain Function
Enzyme 52 Signals
  • None
Enzyme 52 Transmembrane Regions
  • None
Enzyme 52 Essentiality Not Available
Enzyme 52 GenBank ID Protein Not Available
Enzyme 52 UniProtKB/Swiss-Prot ID A6NN38 Link Image
Enzyme 52 UniProtKB/Swiss-Prot Entry Name A6NN38_HUMAN Link Image
Enzyme 52 PDB ID Not Available
Enzyme 52 Cellular Location Not Available
Enzyme 52 Gene Sequence Not Available
Enzyme 52 GenBank Gene ID AC011442 Link Image
Enzyme 52 GeneCard ID A6NN38 Link Image
Enzyme 52 GenAtlas ID CARM1 Link Image
Enzyme 52 HGNC ID HGNC:23393 Link Image
Enzyme 52 Chromosome Location 19
Enzyme 52 Locus 19p13.2
Enzyme 52 SNPs SNPJam Report Link Image
Enzyme 52 General References Not Available
Enzyme 52 Metabolite References Not Available
Enzyme 53 [top]
Enzyme 53 ID 16701
Enzyme 53 Name cDNA, FLJ92918, Homo sapiens suppressor of variegation 3-9 homolog 1 (Drosophila)(SUV39H1), mRNA (Suppressor of variegation 3-9 homolog 1 (Drosophila), isoform CRA_a)
Enzyme 53 Synonyms Not Available
Enzyme 53 Gene Name SUV39H1
Enzyme 53 Protein Sequence >cDNA, FLJ92918, Homo sapiens suppressor of variegation 3-9 homolog 1 (Drosophila)(SUV39H1), mRNA (Suppressor of variegation 3-9 homolog 1 (Drosophila), isoform CRA_a)
MAENLKGCSVCCKSSWNQLQDLCRLAKLSCPALGISKRNLYDFEVEYLCDYKKIREQEYY
LVKWRGYPDSESTWEPRQNLKCVRILKQFHKDLERELLRRHHRSKTPRHLDPSLANYLVQ
KAKQRRALRRWEQELNAKRSHLGRITVENEVDLDGPPRAFVYINEYRVGEGITLNQVAVG
CECQDCLWAPTGGCCPGASLHKFAYNDQGQVRLRAGLPIYECNSRCRCGYDCPNRVVQKG
IRYDLCIFRTDDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFD
LDYVEDVYTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIRAGEE
LTFDYNMQVDPVDMESTRMDSNFGLAGLPGSPKKRVRIECKCGTESCRKYLF
Enzyme 53 Number of Residues 412
Enzyme 53 Molecular Weight 47908
Enzyme 53 Theoretical pI 8.07
Enzyme 53 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • chromatin binding
  • histone-lysine N-methyltransferase activity
  • ion binding
  • methyltransferase activity
  • protein methyltransferase activity
  • protein-lysine N-methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
  • transition metal ion binding
  • zinc ion binding
Process
  • DNA metabolism
  • DNA packaging
  • cellular metabolism
  • chromatin assembly or disassembly
  • chromatin modification
  • establishment and/or maintenance of chromatin architecture
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
  • chromatin
  • chromosome
  • intracellular membrane-bound organelle
  • intracellular non-membrane-bound organelle
  • membrane-bound organelle
  • non-membrane-bound organelle
  • nucleus
  • organelle
Enzyme 53 General Function Not Available
Enzyme 53 Specific Function S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N(6)-methyl-L-lysine
Enzyme 53 Pathways Not Available
Enzyme 53 Reactions Not Available
Enzyme 53 Pfam Domain Function
Enzyme 53 Signals
  • None
Enzyme 53 Transmembrane Regions
  • None
Enzyme 53 Essentiality Not Available
Enzyme 53 GenBank ID Protein Not Available
Enzyme 53 UniProtKB/Swiss-Prot ID B2R6E8 Link Image
Enzyme 53 UniProtKB/Swiss-Prot Entry Name B2R6E8_HUMAN Link Image
Enzyme 53 PDB ID Not Available
Enzyme 53 Cellular Location Not Available
Enzyme 53 Gene Sequence Not Available
Enzyme 53 GenBank Gene ID AK312547 Link Image
Enzyme 53 GeneCard ID B2R6E8 Link Image
Enzyme 53 GenAtlas ID Not Available
Enzyme 53 HGNC ID Not Available
Enzyme 53 Chromosome Location Not Available
Enzyme 53 Locus Not Available
Enzyme 53 SNPs SNPJam Report Link Image
Enzyme 53 General References Not Available
Enzyme 53 Metabolite References Not Available
Enzyme 54 [top]
Enzyme 54 ID 16702
Enzyme 54 Name RNA (Guanine-7-) methyltransferase
Enzyme 54 Synonyms
  1. SubName: RNA (Guanine-7-) methyltransferase, isoform CRA_a
Enzyme 54 Gene Name RNMT
Enzyme 54 Protein Sequence >RNA (Guanine-7-) methyltransferase
MANSAKAEEYEKMSLEQAKASVNSETESSFNINENTTASGTGLSEKTSVCRQVDIARKRK
EFEDDLVKESSSCGKDTPSKKRKLDPEIVPEEKDCGDAEGNSKKRKRETEDVPKDKSSTG
DGTQNKRKIALEDVPEKQKNLEEGHSSTVAAHYNELQEVGLEKRSQSRIFYLRNFNNWMK
SVLIGEFLEKVRQKKKRDITVLDLGCGKGGDLLKWKKGRINKLVCTDIADVSVKQCQQRY
EDMKNRRDSEYIFSAEFITADSSKELLIDKFRDPQMCFDICSCQFVCHYSFESYEQADMM
LRNACERLSPGGYFIGTTPNSFELIRRLEASETESFGNEIYTVKFQKKGDYPLFGCKYDF
NLEGVVDVPEFLVYFPLLNEMAKKYNMKLVYKKTFLEFYEEKIKNNENKMLLKRMQALEP
YPANESSKLVSEKVDDYEHAAKYMKNSQVRLPLGTLSKSEWEATSIYLVFAFEKQQ
Enzyme 54 Number of Residues 476
Enzyme 54 Molecular Weight 54845
Enzyme 54 Theoretical pI 6.54
Enzyme 54 GO Classification
Function
Process
  • RNA metabolism
  • RNA processing
  • cellular metabolism
  • mRNA capping
  • mRNA processing
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
Enzyme 54 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 54 Specific Function Not Available
Enzyme 54 Pathways Not Available
Enzyme 54 Reactions Not Available
Enzyme 54 Pfam Domain Function
Enzyme 54 Signals
  • None
Enzyme 54 Transmembrane Regions
  • None
Enzyme 54 Essentiality Not Available
Enzyme 54 GenBank ID Protein Not Available
Enzyme 54 UniProtKB/Swiss-Prot ID B0YJ90 Link Image
Enzyme 54 UniProtKB/Swiss-Prot Entry Name B0YJ90_HUMAN Link Image
Enzyme 54 PDB ID Not Available
Enzyme 54 Cellular Location Not Available
Enzyme 54 Gene Sequence Not Available
Enzyme 54 GenBank Gene ID EF445026 Link Image
Enzyme 54 GeneCard ID B0YJ90 Link Image
Enzyme 54 GenAtlas ID Not Available
Enzyme 54 HGNC ID Not Available
Enzyme 54 Chromosome Location 18
Enzyme 54 Locus 18p11.22-p11.23
Enzyme 54 SNPs SNPJam Report Link Image
Enzyme 54 General References Not Available
Enzyme 54 Metabolite References Not Available
Enzyme 55 [top]
Enzyme 55 ID 16703
Enzyme 55 Name cDNA FLJ43496 fis, clone PEBLM2001465, highly similar to Probable diphthine synthase (EC 2.1.1.98)
Enzyme 55 Synonyms
  1. SubName: DPH5 homolog (S. cerevisiae), isoform CRA_e
Enzyme 55 Gene Name DPH5
Enzyme 55 Protein Sequence >cDNA FLJ43496 fis, clone PEBLM2001465, highly similar to Probable diphthine synthase (EC 2.1.1.98)
MNAVGCCGLQLYKFGETVSIVFWTDTWRPESFFDKVKKNRQNGMHTLCLLDIKVKEQSLE
NLIKGRKIYEPPRYMSVNQAAQQLLEIVQNQRIRGEEPAVTEETLCVGLARVGADDQKIA
AGTLRQMCTVDLGEPLHSLIITGGSIHPMEMEMLSLFSIPENSSESQSINGL
Enzyme 55 Number of Residues 172
Enzyme 55 Molecular Weight 19244
Enzyme 55 Theoretical pI 5.29
Enzyme 55 GO Classification
Function
  • S-adenosylmethionine-dependent methyltransferase activity
  • catalytic activity
  • diphthine synthase activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • biosynthesis
  • metabolism
  • peptidyl-diphthamide biosynthesis from peptidyl-histidine
  • physiological process
Component
Enzyme 55 General Function Translation, ribosomal structure and biogenesis
Enzyme 55 Specific Function Not Available
Enzyme 55 Pathways Not Available
Enzyme 55 Reactions
  • S-adenosyl-L-methionine + 2-(3-carboxy-3-aminopropyl)-L-histidine = S-adenosyl-L-homocysteine + 2-[3-carboxy-3-(methylammonio)propyl]-L-histidine [RN:R04481] ALL_REAC R04481
Enzyme 55 Pfam Domain Function Not Available
Enzyme 55 Signals
  • None
Enzyme 55 Transmembrane Regions
  • None
Enzyme 55 Essentiality Not Available
Enzyme 55 GenBank ID Protein Not Available
Enzyme 55 UniProtKB/Swiss-Prot ID B3KWP1 Link Image
Enzyme 55 UniProtKB/Swiss-Prot Entry Name B3KWP1_HUMAN Link Image
Enzyme 55 PDB ID Not Available
Enzyme 55 Cellular Location Not Available
Enzyme 55 Gene Sequence Not Available
Enzyme 55 GenBank Gene ID AK125485 Link Image
Enzyme 55 GeneCard ID B3KWP1 Link Image
Enzyme 55 GenAtlas ID Not Available
Enzyme 55 HGNC ID Not Available
Enzyme 55 Chromosome Location Not Available
Enzyme 55 Locus Not Available
Enzyme 55 SNPs SNPJam Report Link Image
Enzyme 55 General References Not Available
Enzyme 55 Metabolite References Not Available