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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 Link Image
SDF File Show Link Image
PDB File Show Link Image
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]
Biofluid CSF
Value 0.0243 +/- 0.0068 uM
Age N/A
Sex N/A
Patient information Normal
Comments Not Available
References
  • Linnebank M, Popp J, Smulders Y, Smith D, Semmler A, Farkas M, Kulic L, Cvetanovska G, Blom H, Stoffel-Wagner B, Kolsch H, Weller M, Jessen F: S-adenosylmethionine is decreased in the cerebrospinal fluid of patients with Alzheimer's disease. Neurodegener Dis. 2010;7(6):373-8. Epub 2010 Jun 3. [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]
Biofluid CSF
Value 0.0269 +/- 0.0062 uM
Age Adult:>18 yrs old
Sex N/A
Comments Not Available
References
  • Linnebank M, Popp J, Smulders Y, Smith D, Semmler A, Farkas M, Kulic L, Cvetanovska G, Blom H, Stoffel-Wagner B, Kolsch H, Weller M, Jessen F: S-adenosylmethionine is decreased in the cerebrospinal fluid of patients with Alzheimer's disease. Neurodegener Dis. 2010;7(6):373-8. Epub 2010 Jun 3. [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 SETD7
  7. Phenylethanolamine N-methyltransferase
  8. Arsenite methyltransferase
  9. Mitochondrial tRNA-specific 2-thiouridylase 1
  10. Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific
  11. Histone-lysine N-methyltransferase SETDB1
  12. Protein-L-isoaspartate(D-aspartate) O-methyltransferase
  13. Protein-S-isoprenylcysteine O-methyltransferase
  14. Indolethylamine N-methyltransferase
  15. DNA (cytosine-5)-methyltransferase 3A
  16. Hexaprenyldihydroxybenzoate methyltransferase, mitochondrial
  17. Histone-lysine N-methyltransferase, H3 lysine-9 specific 3
  18. Methionine synthase reductase
  19. Histone-lysine N-methyltransferase SUV39H1
  20. Nicotinamide N-methyltransferase
  21. Histone-lysine N-methyltransferase SUV39H2
  22. Guanidinoacetate N-methyltransferase
  23. Thiopurine S-methyltransferase
  24. N6-adenosine-methyltransferase 70 kDa subunit
  25. Putative adenosylhomocysteinase 3
  26. Adenosylhomocysteinase
  27. Putative adenosylhomocysteinase 2
  28. Histone-lysine N-methyltransferase SETD1A
  29. DNA (cytosine-5)-methyltransferase 1
  30. DNA (cytosine-5)-methyltransferase 3B
  31. tRNA (cytosine-5-)-methyltransferase
  32. Histone-lysine N-methyltransferase SETD8
  33. Histone-lysine N-methyltransferase SETDB2
  34. Histamine N-methyltransferase
  35. cDNA FLJ76252, highly similar to Homo sapiens S-adenosylhomocysteine hydrolase
  36. Probable histone-lysine N-methyltransferase ASH1L
  37. Histone-arginine methyltransferase CARM1
  38. Histone-lysine N-methyltransferase EZH2
  39. mRNA cap guanine-N7 methyltransferase
  40. Probable histone-lysine N-methyltransferase NSD2
  41. Histone-lysine N-methyltransferase NSD3
  42. Histone-lysine N-methyltransferase SETD1B
  43. Histone-lysine N-methyltransferase SETD2
  44. Histone-lysine N-methyltransferase SETMAR
  45. Histone-lysine N-methyltransferase SUV420H1
  46. Histone-lysine N-methyltransferase SUV420H2
  47. N(2),N(2)-dimethylguanosine tRNA methyltransferase
  48. tRNA (adenine-N(1)-)-methyltransferase catalytic subunit TRMT61A
  49. tRNA (guanine-N(7)-)-methyltransferase
  50. 5-methyltetrahydrofolate-homocysteine methyltransferase reductase
  51. DNA (cytosine-5)-methyltransferase 3-like
  52. Euchromatic histone-lysine N-methyltransferase 2 (Euchromatic histone- lysine N-methyltransferase 2, isoform CRA_c) (HLA-B associated transcript 8)
  53. Histone-lysine N-methyltransferase EZH1
  54. Enhancer of zeste homolog 2 (Drosophila) (Enhancer of zeste homolog 2 (Drosophila), isoform CRA_a)
  55. cDNA FLJ75818, highly similar to Homo sapiens PR/SET domain containing protein 8 (SET8), mRNA
  56. Wolf-Hirschhorn syndrome candidate 1 (Wolf-Hirschhorn syndrome candidate 1, isoform CRA_e)
  57. EHMT1 protein
  58. cDNA FLJ78356, highly similar to Homo sapiens PIMT isozyme I
  59. Protein arginine methyltransferase 5, isoform CRA_d
  60. Uncharacterized protein CARM1 (Coactivator-associated arginine methyltransferase 1, isoform CRA_b)
  61. 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)
  62. RNA (Guanine-7-) methyltransferase
  63. DPH5 homolog (S. cerevisiae), isoform CRA_e
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
YFGILKEARVTVFPFNILDNPMYWGSTANYLGWAIMHASPTGLLLTVLVALTYIVALLYE
EPFTAEIYRQKASGSHKRS
Enzyme 1 Number of Residues 199
Enzyme 1 Molecular Weight 22133.6
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
  • metabolic process
  • organophosphate metabolic process
  • phospholipid metabolic process
Component
Enzyme 1 General Function Involved in N-methyltransferase activity
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 [RN:R02056]
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 5459516 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
AAGCTGAGCAGGGCCTTCGGATCCCCCTACCTGGCCTGCTACTCTCTAAGCATCACCATC
CTGCTCCTGAACTTCCTGCGCTCGCACTGCTTCACGCAGGCCATGCTGAGCCAGCCCAGG
ATGGAGAGCCTGGACACCCCCGCGGCCTACAGCCTGGGCCTCGCGCTCCTGGGACTGGGC
GTCGTGCTCGTGCTCTCCAGCTTCTTTGCACTGGGGTTCGCTGGAACTTTCCTAGGTGAT
TACTTCGGGATCCTCAAGGAGGCGAGAGTGACCGTGTTCCCCTTCAACATCCTGGACAAC
CCCATGTACTGGGGAAGCACAGCCAACTACCTGGGCTGGGCCATCATGCACGCCAGCCCC
ACGGGCCTGCTCCTGACGGTGCTGGTGGCCCTCACCTACATAATGGCTCTCCTATACGAA
GAGCCCTTCACCGCTGAGATCTACCGGCAGAAAGCCTCCGGGTCCCACAAGAGGAGCTGA
Enzyme 1 GenBank Gene ID AB029821 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 1
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]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Resseguie M, Song J, Niculescu MD, da Costa KA, Randall TA, Zeisel SH: Phosphatidylethanolamine N-methyltransferase (PEMT) gene expression is induced by estrogen in human and mouse primary hepatocytes. FASEB J. 2007 Aug;21(10):2622-32. Epub 2007 Apr 24. [PubMed Link Image]
  6. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [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 38452.5
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 Involved in O-methyltransferase activity
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 [RN:R03130]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 57209912 Link Image
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 >1038 bp
ATGGGATCCTCAGAGGACCAGGCCTATCGCCTCCTTAATGACTACGCCAACGGCTTCATG
GTGTCCCAGGTTCTCTTCGCCGCCTGCGAGCTGGGCGTGTTTGACCTTCTCGCCGAGGCC
CCAGGGCCCCTGGACGTGGCGGCAGTGGCTGCAGGTGTGAGGGCCAGCGCCCATGGGACA
GAGCTCCTGCTGGACATCTGTGTGTCCCTGAAGCTGCTGAAAGTGGAGACGAGGGGAGGA
AAAGCTTTCTATCGAAACACAGAGCTGTCCAGCGACTACCTGACCACGGTCAGCCCGACG
TCACAATGCAGCATGCTGAAGTACATGGGCAGGACCAGCTACCGGTGCTGGGGCCACCTG
GCAGACGCCGTGAGAGAAGGAAGGAACCAGTACCTGGAGACGTTTGGCGTTCCCGCTGAA
GAGCTTTTTACGGCCATCTACAGGTCCGAGGGCGAGCGGCTACAGTTCATGCAAGCTCTG
CAGGAGGTCTGGAGCGTCAACGGGAGAAGCGTGCTGACCGCCTTTGACCTGTCAGTGTTC
CCACTTATGTGTGACCTTGGTGGTGGGGCTGGAGCTCTGGCTAAGGAATGCATGTCTCTG
TACCCTGGATGTAAGATCACCGTTTTTGACATCCCAGAAGTGGTGTGGACGGCAAAGCAG
CACTTCTCATTCCAGGAGGAAGAACAGATTGACTTCCAGGAAGGGGATTTCTTCAAAGAC
CCTCTTCCGGAAGCTGATCTGTACATCCTGGCCAGGGTCCTCCATGACTGGGCAGACGGA
AAGTGCTCACACCTGCTGGAGAGGATCTACCACACTTGCAAGCCAGGTGGTGGCATTCTG
GTAATTGAAAGCCTCCTGGATGAAGACAGGCGAGGTCCTCTGCTCACGCAGCTCTACTCT
CTGAACATGCTTGTGCAGACGGAAGGGCAGGAGAGGACCCCCACCCACTACCACATGCTC
CTCTCTTCTGCTGGCTTCAGAGACTTCCAGTTTAAGAAAACAGGAGCCATTTATGATGCC
ATTTTAGCCAGGAAATAA
Enzyme 2 GenBank Gene ID AL683807 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 Not Available
Enzyme 2 Locus Not Available
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]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [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 30036.8
Enzyme 3 Theoretical pI 5.15
Enzyme 3 GO Classification
Function
  • O-methyltransferase activity
  • binding
  • catalytic activity
  • catechol O-methyltransferase activity
  • cation binding
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • biological regulation
  • catecholamine metabolic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid derivative metabolic process
  • cellular biogenic amine metabolic process
  • cellular metabolic process
  • metabolic process
  • neurotransmitter catabolic process
  • neurotransmitter metabolic process
  • regulation of biological quality
  • regulation of neurotransmitter levels
Component
Enzyme 3 General Function Involved in magnesium ion binding
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 [RN:R07330]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • 7-26
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 2
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. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed Link Image]
  6. 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]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  8. Vilbois F, Caspers P, da Prada M, Lang G, Karrer C, Lahm HW, Cesura AM: Mass spectrometric analysis of human soluble catechol O-methyltransferase expressed in Escherichia coli. Identification of a product of ribosomal frameshifting and of reactive cysteines involved in S-adenosyl-L-methionine binding. Eur J Biochem. 1994 Jun 1;222(2):377-86. [PubMed Link Image]
  9. 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]
  10. 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]
  11. Rutherford K, Le Trong I, Stenkamp RE, Parson WW: Crystal structures of human 108V and 108M catechol O-methyltransferase. J Mol Biol. 2008 Jun 27;380(1):120-30. Epub 2008 Apr 23. [PubMed Link Image]
  12. 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]
  13. Tiihonen J, Hallikainen T, Lachman H, Saito T, Volavka J, Kauhanen J, Salonen JT, Ryynanen OP, Koulu M, Karvonen MK, Pohjalainen T, Syvalahti E, Hietala J: Association between the functional variant of the catechol-O-methyltransferase (COMT) gene and type 1 alcoholism. Mol Psychiatry. 1999 May;4(3):286-9. [PubMed Link Image]
  14. 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]
  15. Lee SG, Joo Y, Kim B, Chung S, Kim HL, Lee I, Choi B, Kim C, Song K: Association of Ala72Ser polymorphism with COMT enzyme activity and the risk of schizophrenia in Koreans. Hum Genet. 2005 Mar;116(4):319-28. Epub 2005 Jan 12. [PubMed Link Image]
  16. Rutherford K, Alphandery E, McMillan A, Daggett V, Parson WW: The V108M mutation decreases the structural stability of catechol O-methyltransferase. Biochim Biophys Acta. 2008 Jul-Aug;1784(7-8):1098-105. Epub 2008 Apr 24. [PubMed Link Image]
  17. Annerbrink K, Westberg L, Nilsson S, Rosmond R, Holm G, Eriksson E: Catechol O-methyltransferase val158-met polymorphism is associated with abdominal obesity and blood pressure in men. Metabolism. 2008 May;57(5):708-11. [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. DOT1-like protein
  2. Histone H3-K79 methyltransferase
  3. H3-K79-HMTase
  4. Lysine N-methyltransferase 4
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 184851.2
Enzyme 4 Theoretical pI 9.88
Enzyme 4 GO Classification
Function
  • DNA binding
  • binding
  • catalytic activity
  • histone-lysine N-methyltransferase activity
  • methyltransferase activity
  • nucleic acid binding
  • protein methyltransferase activity
  • protein-lysine N-methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
Component
Enzyme 4 General Function Involved in DNA binding
Enzyme 4 Specific Function Histone methyltransferase. Methylates 'Lys-79' of histone H3. Nucleosomes are preferred as substrate compared to free histones. Binds to DNA
Enzyme 4 Pathways
Enzyme 4 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 22094135 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 1NW3 Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence Not Available
Enzyme 4 GenBank Gene ID Not Available
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 1
Enzyme 4 Locus 19p13.3
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. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  3. 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]
  4. 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]
  5. Okada Y, Feng Q, Lin Y, Jiang Q, Li Y, Coffield VM, Su L, Xu G, Zhang Y: hDOT1L links histone methylation to leukemogenesis. Cell. 2005 Apr 22;121(2):167-78. [PubMed Link Image]
  6. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
  7. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  8. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  9. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  10. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  11. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  12. 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 32742.0
Enzyme 5 Theoretical pI 7.03
Enzyme 5 GO Classification
Function
  • N-methyltransferase activity
  • amino acid binding
  • binding
  • carboxylic acid binding
  • catalytic activity
  • folic acid binding
  • glycine N-methyltransferase activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • methionine metabolic process
  • sulfur amino acid metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 5 General Function Involved in folic acid binding
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 [RN:R00367]
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 6
Enzyme 5 Locus 6p12
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. 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]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Ogawa H, Gomi T, Fujioka M: Mammalian glycine N-methyltransferases. Comparative kinetic and structural properties of the enzymes from human, rat, rabbit and pig livers. Comp Biochem Physiol B. 1993 Nov;106(3):601-11. [PubMed Link Image]
  6. Pakhomova S, Luka Z, Grohmann S, Wagner C, Newcomer ME: Glycine N-methyltransferases: a comparison of the crystal structures and kinetic properties of recombinant human, mouse and rat enzymes. Proteins. 2004 Nov 1;57(2):331-7. [PubMed Link Image]
  7. Luka Z, Pakhomova S, Luka Y, Newcomer ME, Wagner C: Destabilization of human glycine N-methyltransferase by H176N mutation. Protein Sci. 2007 Sep;16(9):1957-64. Epub 2007 Jul 27. [PubMed Link Image]
  8. 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]
  9. Luka Z, Wagner C: Effect of naturally occurring mutations in human glycine N-methyltransferase on activity and conformation. Biochem Biophys Res Commun. 2003 Dec 26;312(4):1067-72. [PubMed Link Image]
  10. 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]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5641
Enzyme 6 Name Histone-lysine N-methyltransferase SETD7
Enzyme 6 Synonyms
  1. Histone H3-K4 methyltransferase SETD7
  2. H3-K4-HMTase SETD7
  3. Lysine N-methyltransferase 7
  4. SET domain-containing protein 7
  5. SET7/9
Enzyme 6 Gene Name SETD7
Enzyme 6 Protein Sequence >Histone-lysine N-methyltransferase SETD7
MDSDDEMVEEAVEGHLDDDGLPHGFCTVTYSSTDRFEGNFVHGEKNGRGKFFFFDGSTLE
GYYVDDALQGQGVYTYEDGGVLQGTYVDGELNGPAQEYDTDGRLIFKGQYKDNIRHGVCW
IYYPDGGSLVGEVNEDGEMTGEKIAYVYPDERTALYGKFIDGEMIEGKLATLMSTEEGRP
HFELMPGNSVYHFDKSTSSCISTNALLPDPYESERVYVAESLISSAGEGLFSKVAVGPNT
VMSFYNGVRITHQEVDSRDWALNGNTLSLDEETVIDVPEPYNHVSKYCASLGHKANHSFT
PNCIYDMFVHPRFGPIKCIRTLRAVEADEELTVAYGYDHSPPGKSGPEAPEWYQVELKAF
QATQQK
Enzyme 6 Number of Residues 366
Enzyme 6 Molecular Weight 40720.6
Enzyme 6 Theoretical pI 4.25
Enzyme 6 GO Classification
Function
  • catalytic activity
  • histone-lysine N-methyltransferase activity
  • methyltransferase activity
  • protein methyltransferase activity
  • protein-lysine N-methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • biological regulation
  • cellular component organization at cellular level
  • cellular process
  • chromatin modification
  • chromatin organization
  • chromosome organization
  • organelle organization
  • regulation of biological process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
  • chromosome
  • intracellular non-membrane-bounded organelle
  • non-membrane-bounded organelle
  • organelle
Enzyme 6 General Function Involved in histone-lysine N-methyltransferase activity
Enzyme 6 Specific Function Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes such as collagenase or insulin. Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription. Has also methyltransferase activity toward non-histone proteins such as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II. Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation. Also able to demethylated 'Lys-372' of p53/TP53 in vitro
Enzyme 6 Pathways
Enzyme 6 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein Not Available
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. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  4. 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]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Martens JH, Verlaan M, Kalkhoven E, Zantema A: Cascade of distinct histone modifications during collagenase gene activation. Mol Cell Biol. 2003 Mar;23(5):1808-16. [PubMed Link Image]
  7. Kouskouti A, Scheer E, Staub A, Tora L, Talianidis I: Gene-specific modulation of TAF10 function by SET9-mediated methylation. Mol Cell. 2004 Apr 23;14(2):175-82. [PubMed Link Image]
  8. Francis J, Chakrabarti SK, Garmey JC, Mirmira RG: Pdx-1 links histone H3-Lys-4 methylation to RNA polymerase II elongation during activation of insulin transcription. J Biol Chem. 2005 Oct 28;280(43):36244-53. Epub 2005 Sep 1. [PubMed Link Image]
  9. Huang J, Perez-Burgos L, Placek BJ, Sengupta R, Richter M, Dorsey JA, Kubicek S, Opravil S, Jenuwein T, Berger SL: Repression of p53 activity by Smyd2-mediated methylation. Nature. 2006 Nov 30;444(7119):629-32. Epub 2006 Nov 15. [PubMed Link Image]
  10. Hu P, Zhang Y: Catalytic mechanism and product specificity of the histone lysine methyltransferase SET7/9: an ab initio QM/MM-FE study with multiple initial structures. J Am Chem Soc. 2006 Feb 1;128(4):1272-8. [PubMed Link Image]
  11. 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]
  12. 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]
  13. 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]
  14. 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]
  15. Chuikov S, Kurash JK, Wilson JR, Xiao B, Justin N, Ivanov GS, McKinney K, Tempst P, Prives C, Gamblin SJ, Barlev NA, Reinberg D: Regulation of p53 activity through lysine methylation. Nature. 2004 Nov 18;432(7015):353-60. Epub 2004 Nov 3. [PubMed Link Image]
  16. Couture JF, Collazo E, Hauk G, Trievel RC: Structural basis for the methylation site specificity of SET7/9. Nat Struct Mol Biol. 2006 Feb;13(2):140-6. Epub 2006 Jan 15. [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 30854.7
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 Involved in methyltransferase activity
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 [RN:R04033]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein Not Available
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 1
Enzyme 7 Locus 17q
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]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Martin JL, Begun J, McLeish MJ, Caine JM, Grunewald GL: Getting the adrenaline going: crystal structure of the adrenaline-synthesizing enzyme PNMT. Structure. 2001 Oct;9(10):977-85. [PubMed Link Image]
  5. Gee CL, Tyndall JD, Grunewald GL, Wu Q, McLeish MJ, Martin JL: Mode of binding of methyl acceptor substrates to the adrenaline-synthesizing enzyme phenylethanolamine N-methyltransferase: implications for catalysis. Biochemistry. 2005 Dec 27;44(51):16875-85. [PubMed Link Image]
  6. Grunewald GL, Seim MR, Regier RC, Martin JL, Gee CL, Drinkwater N, Criscione KR: Comparison of the binding of 3-fluoromethyl-7-sulfonyl-1,2,3,4-tetrahydroisoquinolines with their isosteric sulfonamides to the active site of phenylethanolamine N-methyltransferase. J Med Chem. 2006 Sep 7;49(18):5424-33. [PubMed Link Image]
  7. Gee CL, Drinkwater N, Tyndall JD, Grunewald GL, Wu Q, McLeish MJ, Martin JL: Enzyme adaptation to inhibitor binding: a cryptic binding site in phenylethanolamine N-methyltransferase. J Med Chem. 2007 Oct 4;50(20):4845-53. Epub 2007 Sep 11. [PubMed Link Image]
  8. Ji Y, Salavaggione OE, Wang L, Adjei AA, Eckloff B, Wieben ED, Weinshilboum RM: Human phenylethanolamine N-methyltransferase pharmacogenomics: gene re-sequencing and functional genomics. J Neurochem. 2005 Dec;95(6):1766-76. Epub 2005 Nov 8. [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. Methylarsonite methyltransferase
  2. S-adenosyl-L-methionine:arsenic(III) methyltransferase
Enzyme 8 Gene Name AS3MT
Enzyme 8 Protein Sequence >Arsenite methyltransferase
MAALRDAEIQKDVQTYYGQVLKRSADLQTNGCVTTARPVPKHIREALQNVHEEVALRYYG
CGLVIPEHLENCWILDLGSGSGRDCYVLSQLVGEKGHVTGIDMTKGQVEVAEKYLDYHME
KYGFQASNVTFIHGYIEKLGEAGIKNESHDIVVSNCVINLVPDKQQVLQEAYRVLKHGGE
LYFSDVYTSLELPEEIRTHKVLWGECLGGALYWKELAVLAQKIGFCPPRLVTANLITIQN
KELERVIGDCRFVSATFRLFKHSKTGPTKRCQVIYNGGITGHEKELMFDANFTFKEGEIV
EVDEETAAILKNSRFAQDFLIRPIGEKLPTSGGCSALELKDIITDPFKLAEESDSMKSRC
VPDAAGGCCGTKKSC
Enzyme 8 Number of Residues 375
Enzyme 8 Molecular Weight 41747.5
Enzyme 8 Theoretical pI 6.14
Enzyme 8 GO Classification
Function
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • metabolic process
Component
Enzyme 8 General Function Involved in methyltransferase activity
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 [RN:R05755]
  • (2) S-adenosyl-L-methionine + methylarsonite = S-adenosyl-L-homocysteine + dimethylarsinate [RN:R05756]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 109389364 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 >1128 bp
ATGGCTGCACTTCGTGACGCTGAGATACAGAAGGACGTGCAGACCTACTACGGGCAGGTG
CTGAAGAGATCGGCAGACCTCCAGACCAACGGCTGTGTCACCACAGCCAGGCCGGTCCCC
AAGCACATCCGGGAAGCCTTGCAAAATGTACACGAAGAAGTAGCCCTAAGATATTATGGC
TGTGGTCTGGTGATCCCTGAGCATCTAGAAAACTGCTGGATTTTGGATCTGGGTAGTGGA
AGTGGCAGAGATTGCTATGTACTTAGCCAGCTGGTTGGTGAAAAAGGACACGTGACTGGA
ATAGACATGACCAAAGGCCAGGTGGAAGTGGCTGAAAAGTATCTTGACTATCACATGGAA
AAATATGGCTTCCAGGCATCTAATGTGACTTTTATTCATGGCTACATTGAGAAGTTGGGA
GAGGCTGGAATCAAGAATGAGAGCCATGATATTGTTGTATCAAACTGTGTTATTAACCTT
GTGCCTGATAAACAACAAGTGCTTCAGGAGGCATATCGGGTGCTGAAGCATGGTGGGGAG
TTATATTTCAGTGACGTCTATACGAGCCTTGAACTGCCAGAAGAAATCAGGACACACAAA
GTTTTATGGGGTGAGTGTCTGGGTGGTGCTTTATACTGGAAGGAACTTGCTGTCCTTGCT
CAAAAAATTGGGTTCTGCCCTCCACGTTTGGTCACTGCCAATCTCATTACAATTCAAAAC
AAGGAACTGGAAAGAGTTATCGGTGACTGTCGTTTTGTTTCTGCAACATTTCGCCTCTTC
AAACACTCTAAGACAGGACCAACCAAGAGATGCCAAGTTATTTACAATGGAGGAATTACA
GGACATGAAAAAGAACTAATGTTTGATGCCAATTTTACATTTAAGGAAGGTGAAATTGTT
GAAGTGGATGAAGAAACAGCAGCTATCTTGAAGAATTCAAGATTTGCTCAAGATTTTCTG
ATCAGACCAATTGGAGAGAAGTTGCCAACATCTGGAGGCTGTTCTGCTTTGGAGTTAAAG
GATATAATCACAGATCCATTTAAGCTTGCAGAAGAGTCTGACAGTATGAAGTCCAGATGT
GTCCCTGATGCTGCTGGAGGCTGCTGTGGCACAAAGAAAAGCTGCTAA
Enzyme 8 GenBank Gene ID NM_020682.3 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 1
Enzyme 8 Locus 10q24.32
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Wood TC, Salavagionne OE, Mukherjee B, Wang L, Klumpp AF, Thomae BA, Eckloff BW, Schaid DJ, Wieben ED, Weinshilboum RM: Human arsenic methyltransferase (AS3MT) pharmacogenetics: gene resequencing and functional genomics studies. J Biol Chem. 2006 Mar 17;281(11):7364-73. Epub 2006 Jan 6. [PubMed Link Image]
  2. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5646
Enzyme 9 Name Mitochondrial tRNA-specific 2-thiouridylase 1
Enzyme 9 Synonyms
  1. MTO2 homolog
Enzyme 9 Gene Name TRMU
Enzyme 9 Protein Sequence >Mitochondrial tRNA-specific 2-thiouridylase 1
MQALRHVVCALSGGVDSAVAALLLRRRGYQVTGVFMKNWDSLDEHGVCTADKDCEDAYRV
CQILDIPFHQVSYVKEYWNDVFSDFLNEYEKGRTPNPDIVCNKHIKFSCFFHYAVDNLGA
DAIATGHYARTSLEDEEVFEQKHVKKPEGLFRNRFEVRNAVKLLQAADSFKDQTFFLSQV
SQDALRRTIFPLGGLTKEFVKKIAAENRLHHVLQKKESMGMCFIGKRNFEHFLLQYLQPR
PGHFISIEDNKVLGTHKGWFLYTLGQRANIGGLREPWYVVEKDSVKGDVFVAPRTDHPAL
YRDLLRTSRVHWIAEEPPAALVRDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTAVQAV
RALATGQFAVFYKGDECLGSGKILRLGPSAYTLQKGQRRAGMATESPSDSPEDGPGLSPL
L
Enzyme 9 Number of Residues 421
Enzyme 9 Molecular Weight 47744.3
Enzyme 9 Theoretical pI 8.12
Enzyme 9 GO Classification
Function
  • catalytic activity
  • transferase activity
Process
  • RNA metabolic process
  • cellular macromolecule metabolic process
  • macromolecule metabolic process
  • metabolic process
  • ncRNA metabolic process
  • tRNA metabolic process
  • tRNA processing
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 9 General Function Involved in transferase activity
Enzyme 9 Specific Function Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2- thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 54633233 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID O75648 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name MTU1_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 AB178028 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 2
Enzyme 9 Locus 22q13
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Yan Q, Bykhovskaya Y, Li R, Mengesha E, Shohat M, Estivill X, Fischel-Ghodsian N, Guan MX: Human TRMU encoding the mitochondrial 5-methylaminomethyl-2-thiouridylate-methyltransferase is a putative nuclear modifier gene for the phenotypic expression of the deafness-associated 12S rRNA mutations. Biochem Biophys Res Commun. 2006 Apr 21;342(4):1130-6. Epub 2006 Feb 23. [PubMed Link Image]
  2. Umeda N, Suzuki T, Yukawa M, Ohya Y, Shindo H, Watanabe K, Suzuki T: Mitochondria-specific RNA-modifying enzymes responsible for the biosynthesis of the wobble base in mitochondrial tRNAs. Implications for the molecular pathogenesis of human mitochondrial diseases. J Biol Chem. 2005 Jan 14;280(2):1613-24. Epub 2004 Oct 26. [PubMed Link Image]
  3. Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. 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]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Yan Q, Li X, Faye G, Guan MX: Mutations in MTO2 related to tRNA modification impair mitochondrial gene expression and protein synthesis in the presence of a paromomycin resistance mutation in mitochondrial 15 S rRNA. J Biol Chem. 2005 Aug 12;280(32):29151-7. Epub 2005 Jun 8. [PubMed Link Image]
  8. Guan MX, Yan Q, Li X, Bykhovskaya Y, Gallo-Teran J, Hajek P, Umeda N, Zhao H, Garrido G, Mengesha E, Suzuki T, del Castillo I, Peters JL, Li R, Qian Y, Wang X, Ballana E, Shohat M, Lu J, Estivill X, Watanabe K, Fischel-Ghodsian N: Mutation in TRMU related to transfer RNA modification modulates the phenotypic expression of the deafness-associated mitochondrial 12S ribosomal RNA mutations. Am J Hum Genet. 2006 Aug;79(2):291-302. Epub 2006 Jun 22. [PubMed Link Image]
  9. Zeharia A, Shaag A, Pappo O, Mager-Heckel AM, Saada A, Beinat M, Karicheva O, Mandel H, Ofek N, Segel R, Marom D, Rotig A, Tarassov I, Elpeleg O: Acute infantile liver failure due to mutations in the TRMU gene. Am J Hum Genet. 2009 Sep;85(3):401-7. [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. Androgen receptor coactivator 267 kDa protein
  2. Androgen receptor-associated protein of 267 kDa
  3. H3-K36-HMTase
  4. H4-K20-HMTase
  5. Lysine N-methyltransferase 3B
  6. Nuclear receptor-binding SET domain-containing protein 1
  7. NR-binding SET domain-containing protein
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 296649.3
Enzyme 10 Theoretical pI 8.08
Enzyme 10 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • histone-lysine N-methyltransferase activity
  • ion binding
  • metal ion binding
  • methyltransferase activity
  • protein 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
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 10 General Function Involved in histone-lysine N-methyltransferase activity
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 [RN:R03938]
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 19923586 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 >8091 bp
ATGGATCAGACCTGTGAACTACCCAGAAGAAATTGTCTGCTGCCCTTTTCCAATCCAGTG
AATTTAGATGCCCCTGAAGACAAGGACAGCCCTTTCGGTAATGGTCAATCCAATTTTTCT
GAGCCACTTAATGGGTGTACTATGCAGTTATCGACTGTCAGTGGAACATCCCAAAATGCT
TATGGACAAGATTCTCCATCTTGTTACATTCCACTGCGGAGACTACAGGATTTGGCCTCC
ATGATCAATGTAGAGTATTTAAATGGGTCTGCTGATGGATCAGAATCCTTTCAAGACCCT
GAAAAAAGTGATTCAAGAGCTCAGACGCCAATTGTTTGCACTTCCTTGAGTCCTGGTGGT
CCTACAGCACTTGCTATGAAACAGGAACCCTCTTGTAATAACTCCCCTGAACTCCAGGTA
AAAGTAACAAAGACTATCAAGAATGGCTTTCTGCACTTTGAGAATTTTACTTGTGTGGAC
GATGCAGATGTAGATTCTGAAATGGACCCAGAACAGCCAGTCACAGAGGATGAGAGTATA
GAGGAGATCTTTGAGGAAACTCAGACCAATGCCACCTGCAATTATGAGACTAAATCAGAG
AATGGTGTAAAAGTGGCCATGGGAAGTGAACAAGACAGCACACCAGAGAGTAGACACGGT
GCAGTCAAATCGCCATTCTTGCCATTAGCTCCTCAGACTGAAACACAGAAAAATAAGCAA
AGAAATGAAGTGGACGGCAGCAATGAAAAAGCAGCCCTTCTCCCAGCCCCCTTTTCACTA
GGAGACACAAACATTACAATAGAAGAGCAATTAAACTCAATAAATTTATCTTTTCAGGAT
GATCCAGATTCCAGTACCAGTACATTAGGAAACATGCTAGAATTACCTGGAACTTCATCA
TCATCTACTTCACAGGAATTGCCATTTTGTCAACCTAAGAAAAAGTCTACGCCACTGAAG
TATGAAGTTGGAGATCTCATCTGGGCAAAATTCAAGAGACGCCCATGGTGGCCCTGCAGG
ATTTGTTCTGATCCGTTGATTAACACACATTCAAAAATGAAAGTTTCCAACCGGAGGCCC
TATCGGCAGTACTACGTGGAGGCTTTTGGAGATCCTTCTGAGAGAGCCTGGGTGGCTGGA
AAAGCAATCGTCATGTTTGAAGGCAGACATCAATTCGAAGAGCTACCTGTCCTTAGGAGA
AGAGGGAAACAGAAAGAAAAAGGATATAGGCATAAGGTTCCTCAGAAAATTTTGAGTAAA
TGGGAAGCCAGTGTTGGACTTGCAGAACAGTATGATGTTCCCAAGGGGTCAAAGAACCGA
AAATGTATTCCTGGTTCAATCAAGTTGGACAGTGAAGAAGATATGCCATTTGAAGACTGC
ACAAATGATCCTGAGTCAGAACATGACCTGTTGCTTAATGGCTGTTTGAAATCACTGGCT
TTTGATTCTGAACATTCTGCAGATGAGAAGGAAAAGCCTTGCGCTAAATCTCGAGCCAGA
AAGAGCTCTGATAATCCAAAAAGGACTAGTGTGAAAAAGGGCCACATACAATTTGAAGCA
CATAAAGATGAACGGAGGGGAAAGATTCCAGAGAACCTTGGCCTAAACTTTATCTCTGGG
GATATATCTGATACGCAGGCCTCTAATGAACTTTCCAGGATAGCAAATAGCCTCACAGGG
TCCAACACTGCCCCAGGAAGTTTTCTGTTTTCTTCCTGTGGAAAAAACACTGCAAAGAAA
GAATTTGAGACTTCAAATGGTGACTCTTTATTGGGCTTGCCTGAGGGTGCTTTGATCTCA
AAGTGTTCTCGAGAGAAGAATAAACCCCAACGAAGCCTGGTGTGTGGTTCAAAAGTGAAG
CTCTGCTATATTGGAGCAGGTGATGAGGAAAAGCGAAGTGATTCCATTAGTATCTGTACC
ACTTCTGATGATGGAAGCAGTGACCTGGATCCCATAGAACACAGCTCAGAGTCTGATAAC
AGTGTCCTTGAAATTCCAGATGCTTTCGATAGAACAGAGAACATGTTATCTATGCAGAAA
AATGAAAAGATAAAGTATTCTAGGTTTGCTGCCACAAACACTAGGGTAAAAGCAAAACAG
AAGCCTCTCATTAGTAACTCACATACAGACCACTTAATGGGTTGTACTAAGAGTGCAGAG
CCTGGAACCGAGACGTCTCAGGTTAATCTCTCTGATCTGAAGGCATCTACTCTTGTTCAC
AAACCCCAGTCAGATTTTACAAATGATGCTCTCTCTCCAAAATTCAACCTGTCATCAAGC
ATATCCAGTGAGAACTCGTTAATAAAGGGTGGGGCAGCAAATCAAGCTCTATTACATTCG
AAAAGCAAACAGCCCAAGTTCCGAAGTATAAAGTGCAAACACAAAGAAAATCCAGTTATG
GCAGAACCCCCAGTTATAAATGAGGAGTGCAGTTTGAAATGCTGCTCTTCTGATACCAAA
GGCTCTCCTTTGGCCAGCATTTCTAAAAGTGGGAAAGTGGATGGTCTAAAACTACTGAAC
AATATGCATGAGAAAACCAGGGATTCAAGTGACATAGAAACAGCAGTGGTGAAACATGTT
TTATCCGAGTTGAAGGAACTCTCTTACAGATCCTTAGGTGAGGATGTCAGTGACTCTGGA
ACATCAAAGCCATCAAAACCATTACTTTTCTCTTCTGCTTCTAGTCAGAATCACATACCT
ATTGAACCAGACTACAAATTCAGTACATTGCTAATGATGTTGAAAGATATGCATGATAGT
AAGACGAAGGAGCAGCGGTTGATGACTGCTCAAAACCTGGTCTCTTACCGGAGTCCTGGT
CGTGGGGACTGTTCTACTAATAGTCCTGTAGGAGTCTCTAAGGTTTTGGTTTCAGGAGGC
TCCACACACAATTCAGAGAAAAAGGGAGATGGCACTCAGAACTCCGCCAATCCTAGCCCT
AGTGGGGGTGACTCTGCATTATCTGGCGAGTTGTCTGCTTCCCTACCTGGCTTACTGTCC
GACAAGAGAGACCTCCCTGCTTCTGGTAAAAGTCGTTCAGACTGTGTTACTAGGCGCAAC
TGTGGACGATCAAAGCCTTCATCCAAATTGCGAGATGCTTTTTCAGCCCAAATGGTAAAG
AACACAGTGAACCGTAAAGCCTTAAAGACCGAGCGCAAAAGAAAACTGAATCAGCTTCCA
AGTGTGACTCTTGATGCTGTACTGCAGGGAGACCGAGAACGTGGAGGTTCATTGAGAGGT
GGGGCAGAAGATCCTAGTAAAGAGGATCCCCTTCAGATAATGGGCCACTTAACAAGTGAA
GATGGTGACCATTTTTCTGATGTGCATTTCGATAGCAAGGTTAAGCAATCTGATCCTGGT
AAAATTTCTGAAAAAGGACTCTCTTTTGAAAACGGAAAAGGCCCAGAGCTGGACTCTGTA
ATGAACAGTGAGAATGATGAACTCAATGGTGTAAATCAAGTGGTGCCTAAAAAGCGGTGG
CAGCGTTTAAACCAAAGGCGCACTAAACCTCGTAAGCGCATGAACAGATTTAAAGAGAAA
GAAAACTCTGAGTGTGCCTTTAGGGTCTTACTTCCTAGTGACCCTGTGCAGGAGGGGCGG
GATGAGTTTCCAGAGCATAGAACTCCTTCAGCAAGCATACTTGAGGAACCACTGACAGAG
CAAAATCATGCTGACTGCTTAGATTCAGCTGGGCCACGGTTAAATGTTTGTGATAAATCC
AGTGCCAGCATTGGTGACATGGAAAAGGAGCCAGGAATTCCCAGTTTGACACCACAGGCT
GAGCTCCCTGAACCAGCTGTGCGGTCAGAGAAGAAACGCCTTAGGAAGCCAAGCAAGTGG
CTTTTGGAATATACAGAAGAATATGATCAGATATTTGCTCCTAAGAAAAAACAAAAGAAG
GTACAGGAGCAGGTGCACAAGGTAAGTTCCCGCTGTGAAGAGGAAAGCCTTCTAGCCCGA
GGTCGATCTAGTGCTCAGAACAAGCAGGTGGACGAGAATTCTTTGATTTCAACCAAAGAA
GAGCCTCCAGTTCTTGAAAGGGAGGCTCCGTTTTTGGAGGGCCCCTTGGCTCAGTCAGAA
CTTGGAGGTGGACATGCTGAGTTGCCGCAGCTGACCTTGTCTGTGCCTGTGGCTCCGGAA
GTCTCTCCACGGCCTGCCCTTGAGTCTGAGGAATTGCTAGTTAAAACGCCAGGAAATTAT
GAAAGTAAACGTCAAAGAAAACCAACTAAGAAACTTCTTGAATCCAATGATTTAGACCCT
GGATTTATGCCCAAGAAGGGGGACCTTGGCCTTTCTAAAAAGTGCTATGAAGCTGGTCAC
CTGGAGAATGGCATAACTGAATCTTGTGCCACATCTTATTCAAAAGATTTTGGTGGAGGC
ACTACCAAGATATTTGACAAGCCAAGGAAGCGAAAACGACAGAGGCATGCTGCAGCCAAG
ATGCAGTGTAAAAAAGTGAAAAATGATGACTCGTCAAAAGAGATTCCAGGCTCAGAGGGA
GAACTAATGCCTCACAGGACGGCCACAAGCCCCAAGGAGACTGTTGAGGAAGGTGTAGAA
CACGATCCCGGGATGCCTGCCTCTAAAAAAATGCAGGGTGAACGCGGTGGAGGAGCTGCA
CTCAAGGAGAATGTCTGTCAGAATTGTGAAAAATTGGGTGAGCTGCTGTTATGTGAGGCT
CAGTGCTGTGGGGCTTTCCACCTGGAGTGCCTTGGATTGACTGAGATGCCAAGAGGAAAA
TTTATCTGCAATGAATGTCGCACAGGAATCCATACCTGTTTTGTATGTAAGCAGAGTGGG
GAAGATGTTAAAAGGTGCCTTCTACCCTTGTGTGGAAAGTTTTACCATGAAGAGTGTGTC
CAGAAGTACCCACCCACTGTTATGCAGAACAAGGGCTTCCGGTGCTCCCTCCACATCTGT
ATAACCTGTCATGCTGCTAATCCAGCCAATGTTTCTGCATCTAAAGGTCGGTTGATGCGC
TGTGTCCGCTGTCCTGTGGCATACCACGCCAATGACTTTTGCCTGGCTGCTGGGTCAAAG
ATCCTTGCATCTAATAGTATCATCTGCCCTAATCACTTTACCCCTAGGCGGGGCTGCCGA
AATCATGAGCATGTTAATGTTAGCTGGTGCTTTGTGTGCTCAGAAGGAGGCAGCCTTCTG
TGCTGTGATTCTTGCCCTGCTGCTTTTCATCGTGAATGCCTGAACATTGATATCCCTGAA
GGAAACTGGTATTGCAATGACTGTAAAGCAGGCAAAAAGCCACACTACAGGGAGATTGTC
TGGGTAAAAGTTGGACGATACAGGTGGTGGCCAGCTGAGATCTGCCATCCTCGAGCTGTT
CCTTCCAACATTGATAAGATGAGACATGATGTGGGAGAGTTCCCAGTCCTCTTTTTTGGA
TCTAATGACTATTTGTGGACTCACCAGGCCCGAGTCTTCCCTTACATGGAGGGTGACGTG
AGCAGCAAGGATAAGATGGGCAAAGGAGTGGATGGGACATATAAAAAAGCTCTTCAGGAA
GCTGCAGCAAGGTTTGAGGAATTAAAGGCCCAAAAAGAGCTAAGACAGCTGCAGGAAGAC
CGAAAGAATGACAAGAAGCCACCACCTTATAAACATATAAAGGTAAACCGTCCTATTGGC
AGGGTACAGATCTTCACTGCAGACTTATCTGAAATACCCCGTTGCAACTGTAAAGCTACT
GATGAGAACCCCTGTGGGATAGACTCTGAATGCATCAACCGCATGCTGCTCTATGAGTGC
CACCCCACAGTGTGTCCTGCCGGAGGGCGCTGTCAAAACCAGTGCTTTTCCAAGCGCCAA
TATCCAGAGGTTGAAATTTTCCGCACATTACAGCGGGGTTGGGGTCTACGGACAAAAACA
GATATTAAAAAGGGTGAATTTGTGAATGAGTATGTGGGTGAGCTTATAGATGAAGAAGAA
TGCAGAGCTCGAATTCGCTATGCTCAAGAACATGATATCACTAATTTCTATATGCTCACC
CTAGACAAAGACCGAATCATTGATGCTGGTCCCAAAGGAAACTATGCTCGGTTCATGAAT
CATTGCTGCCAGCCCAACTGTGAAACACAGAAGTGGTCTGTGAATGGAGATACCCGTGTA
GGCCTTTTTGCACTAAGTGACATTAAAGCAGGCACTGAACTTACCTTCAACTACAACCTA
GAATGTCTTGGGAATGGAAAGACTGTTTGCAAATGTGGAGCCCCGAACTGCAGTGGCTTC
TTGGGTGTAAGGCCAAAGAATCAACCCATTGCCACGGAAGAAAAGTCAAAGAAATTCAAG
AAGAAGCAACAGGGAAAGCGCAGGACCCAGGGTGAAATCACAAAGGAGCGAGAAGATGAG
TGTTTTAGTTGTGGGGATGCTGGCCAGCTCGTCTCCTGCAAGAAACCAGGCTGCCCAAAA
GTTTACCACGCAGACTGTCTCAATCTGACCAAGCGACCAGCAGGGAAATGGGAATGTCCG
TGGCATCAGTGTGACATCTGCGGGAAGGAAGCAGCCTCCTTCTGTGAGATGTGCCCCAGC
TCCTTTTGTAAGCAGCATCGAGAAGGGATGCTTTTCATTTCCAAACTGGATGGGCGTCTG
TCTTGTACTGAGCATGACCCCTGTGGGCCCAATCCTCTGGAACCTGGGGAGATCCGTGAG
TATGTGCCTCCCCCAGTACCGCTGCCTCCAGGGCCAAGCACTCACCTGGCAGAGCAATCA
ACAGGAATGGCTGCTCAGGCACCCAAAATGTCAGATAAACCTCCTGCTGACACCAACCAG
ATGCTGTCGCTCTCCAAAAAAGCTCTGGCAGGGACTTGTCAGAGGCCATTGCTACCTGAA
AGACCTCTTGAGAGAACTGACTCCAGGCCCCAGCCTTTAGATAAGGTCAGAGACCTCGCT
GGGTCAGGGACCAAATCCCAATCCTTGGTTTCCAGCCAGAGGCCACTGGACAGGCCACCA
GCAGTGGCAGGACCAAGACCCCAGCTAAGCGACAAACCCTCTCCAGTGACCAGCCCAAGC
TCCTCACCCTCAGTCAGGTCCCAACCACTGGAAAGACCTCTGGGGACGGCTGACCCAAGG
CTGGATAAATCCATAGGTGCTGCCAGCCCAAGGCCCCAGTCACTGGAGAAAACCTCAGTT
CCCACTGGCCTGAGACTTCCGCCGCCAGACAGACTGCTCATTACTAGCAGTCCCAAACCC
CAGACTTCAGACAGGCCTACTGACAAACCCCATGCCTCTTTGTCCCAGAGACTCCCACCT
CCTGAGAAAGTACTATCAGCTGTGGTCCAGACCCTTGTAGCTAAAGAAAAAGCACTGAGG
CCTGTGGACCAGAATACTCAGTCAAAAAATAGAGCTGCTTTGGTGATGGATCTCATAGAC
CTAACTCCTCGCCAGAAGGAGCGGGCAGCTTCACCTCATCAGGTCACACCACAGGCTGAT
GAGAAGATGCCAGTGTTGGAGTCAAGTTCATGGCCTGCCAGCAAAGGTCTGGGGCATATG
CCGAGAGCTGTTGAGAAAGGCTGTGTGTCAGATCCTCTTCAGACATCTGGGAAAGCAGCA
GCCCCTTCAGAGGACCCCTGGCAAGCTGTTAAATCACTCACCCAGGCCAGACTTCTTTCT
CAGCCTCCTGCCAAGGCCTTTTTATATGAGCCAACAACTCAGGCCTCAGGAAGAGCTTCT
GCAGGGGCTGAGCAGACCCCAGGGCCTCTTAGCCAATCCCCGGGCCTGGTGAAGCAGGCG
AAGCAGATGGTCGGAGGCCAGCAACTACCTGCACTTGCCGCCAAGAGTGGGCAATCTTTT
AGGTCTCTCGGGAAGGCCCCAGCCTCCCTCCCCACTGAAGAAAAGAAGTTGGTAACCACA
GAGCAAAGTCCCTGGGCCCTGGGAAAAGCCTCATCACGGGCAGGGCTCTGGCCCATAGTG
GCTGGACAGACACTGGCACAGTCTTGCTGGTCTGCTGGGAGCACACAGACATTGGCACAG
ACTTGCTGGTCTCTTGGAAGAGGGCAAGACCCCAAACCAGAGCAAAATACACTTCCAGCT
CTTAACCAGGCTCCTTCCAGTCACAAGTGTGCAGAATCAGAACAGAAGTAG
Enzyme 10 GenBank Gene ID NM_022455.4 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 5
Enzyme 10 Locus 5q35
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. Baujat G, Rio M, Rossignol S, Sanlaville D, Lyonnet S, Le Merrer M, Munnich A, Gicquel C, Cormier-Daire V, Colleaux L: Paradoxical NSD1 mutations in Beckwith-Wiedemann syndrome and 11p15 anomalies in Sotos syndrome. Am J Hum Genet. 2004 Apr;74(4):715-20. Epub 2004 Mar 1. [PubMed Link Image]
  6. La Starza R, Gorello P, Rosati R, Riezzo A, Veronese A, Ferrazzi E, Martelli MF, Negrini M, Mecucci C: Cryptic insertion producing two NUP98/NSD1 chimeric transcripts in adult refractory anemia with an excess of blasts. Genes Chromosomes Cancer. 2004 Dec;41(4):395-9. [PubMed Link Image]
  7. Giorgianni F, Zhao Y, Desiderio DM, Beranova-Giorgianni S: Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line. Electrophoresis. 2007 Jun;28(12):2027-34. [PubMed Link Image]
  8. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  9. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  10. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  11. 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]
  12. 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]
  13. Ley TJ, Mardis ER, Ding L, Fulton B, McLellan MD, Chen K, Dooling D, Dunford-Shore BH, McGrath S, Hickenbotham M, Cook L, Abbott R, Larson DE, Koboldt DC, Pohl C, Smith S, Hawkins A, Abbott S, Locke D, Hillier LW, Miner T, Fulton L, Magrini V, Wylie T, Glasscock J, Conyers J, Sander N, Shi X, Osborne JR, Minx P, Gordon D, Chinwalla A, Zhao Y, Ries RE, Payton JE, Westervelt P, Tomasson MH, Watson M, Baty J, Ivanovich J, Heath S, Shannon WD, Nagarajan R, Walter MJ, Link DC, Graubert TA, DiPersio JF, Wilson RK: DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome. Nature. 2008 Nov 6;456(7218):66-72. [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. ERG-associated protein with SET domain
  2. ESET
  3. Histone H3-K9 methyltransferase 4
  4. H3-K9-HMTase 4
  5. Lysine N-methyltransferase 1E
  6. SET domain bifurcated 1
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 143155.6
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
  • metal 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
  • cellular component organization at cellular level
  • cellular process
  • chromatin modification
  • chromatin organization
  • chromosome organization
  • organelle organization
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 11 General Function Involved in DNA binding
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 [RN:R03938]
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 55960634 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 >3876 bp
ATGTCTTCCCTTCCTGGGTGCATTGGTTTGGATGCAGCAACAGCTACAGTGGAGTCTGAA
GAGATTGCAGAGCTGCAACAGGCAGTGGTTGAGGAACTGGGTATCTCTATGGAGGAACTT
CGGCATTTCATCGATGAGGAACTGGAGAAGATGGATTGTGTACAGCAACGCAAGAAGCAG
CTAGCAGAGTTAGAGACATGGGTAATACAGAAAGAATCTGAGGTGGCTCACGTTGACCAA
CTCTTTGATGATGCATCCAGGGCAGTGACTAATTGTGAGTCTTTGGTGAAGGACTTCTAC
TCCAAGCTGGGACTACAATACCGGGACAGTAGCTCTGAGGACGAATCTTCCCGGCCTACA
GAAATAATTGAGATTCCTGATGAAGATGATGATGTCCTCAGTATTGATTCAGGTGATGCT
GGGAGCAGAACTCCAAAAGACCAGAAGCTCCGTGAAGCTATGGCTGCCTTAAGAAAGTCA
GCTCAAGATGTTCAGAAGTTCATGGATGCTGTCAACAAGAAGAGCAGTTCCCAGGATCTG
CATAAAGGAACCTTGAGTCAGATGTCTGGAGAACTAAGCAAAGATGGTGACCTGATAGTC
AGCATGCGAATTCTGGGCAAGAAGAGAACTAAGACTTGGCACAAAGGCACCCTTATTGCC
ATCCAGACAGTTGGGCCAGGGAAGAAATACAAGGTGAAATTTGACAACAAAGGAAAGAGT
CTACTGTCGGGGAACCATATTGCCTATGATTACCACCCTCCTGCTGACAAGCTGTATGTG
GGCAGTCGGGTGGTCGCCAAATACAAAGATGGGAATCAGGTCTGGCTCTATGCTGGCATT
GTAGCTGAGACACCAAACGTCAAAAACAAGCTCAGGTTTCTCATTTTCTTTGATGATGGC
TATGCTTCCTATGTCACACAGTCGGAACTGTATCCCATTTGCCGGCCACTGAAAAAGACT
TGGGAGGACATAGAAGACATCTCCTGCCGTGACTTCATAGAGGAGTATGTCACTGCCTAC
CCCAACCGCCCCATGGTACTGCTCAAGAGTGGCCAGCTTATCAAGACTGAGTGGGAAGGC
ACGTGGTGGAAGTCCCGAGTTGAGGAGGTGGATGGCAGCCTAGTCAGGATCCTCTTCCTG
GATGACAAAAGATGTGAGTGGATCTATCGAGGCTCTACACGGCTGGAGCCCATGTTCAGC
ATGAAAACATCCTCAGCCTCTGCACTGGAGAAGAAGCAAGGACAGCTCAGGACACGTCCA
AATATGGGTGCTGTGAGGAGCAAAGGCCCTGTTGTCCAGTACACACAGGATCTGACCGGT
ACTGGAACCCAGTTCAAGCCAGTGGAACCCCCACAGCCTACAGCTCCACCTGCCCCACCT
TTCCCACCTGCTCCACCTCTATCCCCCCAAGCAGGTGACAGTGACTTGGAAAGCCAGCTT
GCCCAGTCACGGAAGCAGGTAGCCAAAAAGAGCACGTCCTTTCGACCAGGATCTGTGGGC
TCTGGTCATTCCTCCCCTACATCTCCTGCACTCAGTGAAAATGTCTCTGGTGGGAAACCT
GGGATCAACCAGACATATAGATCACCTTTAGGCTCCACAGCCTCTGCCCCAGCACCCTCA
GCACTCCCGGCCCCTCCAGCACCCCCAGTCTTCCATGGCATGCTGGAGCGGGCCCCAGCA
GAGCCCTCCTACCGTGCTCCCATGGAGAAGCTTTTCTACTTACCTCATGTCTGCAGCTAT
ACCTGTCTGTCTCGAGTCAGACCTATGAGGAATGAGCAGTACCGGGGCAAGAACCCTCTG
CTGGTCCCGTTACTATATGACTTCCGGCGGATGACAGCCCGGCGTCGAGTTAACCGCAAG
ATGGGCTTTCATGTTATCTATAAGACACCTTGTGGTCTCTGCCTTCGGACAATGCAGGAG
ATAGAACGCTACCTTTTCGAGACTGGCTGTGACTTCCTCTTCCTGGAGATGTTCTGTTTG
GATCCATATGTTCTTGTGGACCGAAAGTTTCAGCCCTATAAGCCTTTTTACTATATTTTG
GACATCACTTATGGGAAGGAAGATGTTCCCCTATCCTGTGTCAATGAGATTGACACAACC
CCTCCACCCCAGGTGGCCTACAGCAAGGAACGTATCCCGGGCAAGGGTGTTTTCATTAAC
ACAGGCCCTGAATTTCTGGTTGGCTGTGACTGCAAGGATGGGTGTCGGGACAAGTCCAAG
TGTGCCTGCCATCAACTAACTATCCAGGCTACAGCCTGTACCCCAGGAGGCCAAATCAAC
CCTAACTCTGGCTACCAGTACAAGAGACTAGAAGAGTGTCTACCCACAGGGGTATATGAG
TGTAACAAACGCTGCAAATGTGACCCAAACATGTGCACAAACCGGTTGGTGCAACATGGA
CTACAAGTTCGGCTACAGCTATTCAAGACACAGAACAAGGGCTGGGGTATCCGCTGCTTG
GATGACATTGCCAAAGGCTCTTTTGTTTGTATTTATGCAGGCAAAATCCTGACAGATGAC
TTTGCAGACAAGGAGGGTCTGGAAATGGGTGATGAGTACTTTGCAAATCTGGACCATATC
GAGAGCGTGGAGAACTTCAAAGAAGGATATGAGAGTGATGCCCCCTGTTCCTCTGACAGC
AGTGGTGTAGACTTGAAGGACCAGGAAGATGGCAACAGCGGTACAGAGGACCCTGAAGAG
TCCAATGATGATAGCTCAGATGATAACTTCTGTAAGGATGAGGACTTCAGCACCAGTTCA
GTGTGGCGGAGCTATGCTACCCGGAGGCAGACCCGGGGCCAGAAAGAGAACGGACTCTCT
GAGACAACTTCCAAGGACTCCCACCCCCCAGATCTTGGACCCCCACATATTCCTGTTCCT
CCCTCAATCCCTGTAGGTGGCTGCAATCCACCTTCCTCCGAAGAGACACCCAAGAACAAG
GTGGCCTCATGGTTGAGCTGCAATAGTGTCAGTGAAGGTGGTTTTGCTGACTCTGATAGC
CATTCATCCTTCAAGACTAATGAAGGTGGGGAGGGCCGGGCTGGGGGAAGCCGAATGGAG
GCTGAGAAGGCCTCCACCTCAGGACTAGGCATCAAGGATGAGGGAGACATCAAACAGGCC
AAGAAAGAGGACACTGACGACCGAAACAAGATGTCAGTAGTTACTGAAAGCTCTCGAAAT
TACGGTTACAATCCTTCTCCTGTGAAGCCTGAAGGACTTCGCCGCCCACCTAGTAAGACT
AGTATGCATCAAAGCCGAAGACTCATGGCTTCTGCTCAGTCCAACCCTGATGATGTCCTG
ACACTGTCCAGCAGCACAGAAAGTGAGGGGGAAAGTGGGACCAGCCGAAAGCCCACTGCT
GGTCAGACTTCGGCTACAGCGGTTGACAGTGATGATATCCAGACCATATCCTCTGGCTCT
GAAGGGGATGACTTTGAGGACAAGAAGAACATGACTGGTCCAATGAAGCGTCAAGTGGCA
GTAAAATCAACCCGAGGCTTTGCTCTTAAATCAACCCATGGGATTGCAATTAAATCAACC
AACATGGCCTCTGTGGACAAGGGGGAGAGCGCACCTGTTCGTAAGAACACACGCCAATTC
TATGATGGCGAGGAGTCTTGCTACATCATTGATGCCAAGCTTGAAGGCAACCTGGGCCGC
TACCTCAACCACAGTTGCAGCCCCAACCTGTTTGTCCAGAATGTCTTCGTGGATACCCAT
GATCTTCGCTTCCCCTGGGTGGCCTTCTTTGCCAGCAAAAGAATCCGGGCTGGGACAGAA
CTTACTTGGGACTACAACTACGAGGTGGGCAGTGTGGAAGGCAAGGAGCTACTCTGTTGC
TGTGGGGCCATTGAATGCAGAGGACGTCTTCTTTAG
Enzyme 11 GenBank Gene ID AL590133 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 1
Enzyme 11 Locus 1q21
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. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. 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]
  5. Ayyanathan K, Lechner MS, Bell P, Maul GG, Schultz DC, Yamada Y, Tanaka K, Torigoe K, Rauscher FJ 3rd: Regulated recruitment of HP1 to a euchromatic gene induces mitotically heritable, epigenetic gene silencing: a mammalian cell culture model of gene variegation. Genes Dev. 2003 Aug 1;17(15):1855-69. Epub 2003 Jul 17. [PubMed Link Image]
  6. Wang H, An W, Cao R, Xia L, Erdjument-Bromage H, Chatton B, Tempst P, Roeder RG, Zhang Y: mAM facilitates conversion by ESET of dimethyl to trimethyl lysine 9 of histone H3 to cause transcriptional repression. Mol Cell. 2003 Aug;12(2):475-87. [PubMed Link Image]
  7. Sarraf SA, Stancheva I: Methyl-CpG binding protein MBD1 couples histone H3 methylation at lysine 9 by SETDB1 to DNA replication and chromatin assembly. Mol Cell. 2004 Aug 27;15(4):595-605. [PubMed Link Image]
  8. Verschure PJ, van der Kraan I, de Leeuw W, van der Vlag J, Carpenter AE, Belmont AS, van Driel R: In vivo HP1 targeting causes large-scale chromatin condensation and enhanced histone lysine methylation. Mol Cell Biol. 2005 Jun;25(11):4552-64. [PubMed Link Image]
  9. Gevaert K, Staes A, Van Damme J, De Groot S, Hugelier K, Demol H, Martens L, Goethals M, Vandekerckhove J: Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC. Proteomics. 2005 Sep;5(14):3589-99. [PubMed Link Image]
  10. Lyst MJ, Nan X, Stancheva I: Regulation of MBD1-mediated transcriptional repression by SUMO and PIAS proteins. EMBO J. 2006 Nov 15;25(22):5317-28. Epub 2006 Oct 26. [PubMed Link Image]
  11. Ichimura T, Watanabe S, Sakamoto Y, Aoto T, Fujita N, Nakao M: Transcriptional repression and heterochromatin formation by MBD1 and MCAF/AM family proteins. J Biol Chem. 2005 Apr 8;280(14):13928-35. Epub 2005 Feb 2. [PubMed Link Image]
  12. Li H, Rauch T, Chen ZX, Szabo PE, Riggs AD, Pfeifer GP: The histone methyltransferase SETDB1 and the DNA methyltransferase DNMT3A interact directly and localize to promoters silenced in cancer cells. J Biol Chem. 2006 Jul 14;281(28):19489-500. Epub 2006 May 8. [PubMed Link Image]
  13. Rosendorff A, Sakakibara S, Lu S, Kieff E, Xuan Y, DiBacco A, Shi Y, Shi Y, Gill G: NXP-2 association with SUMO-2 depends on lysines required for transcriptional repression. Proc Natl Acad Sci U S A. 2006 Apr 4;103(14):5308-13. Epub 2006 Mar 27. [PubMed Link Image]
  14. Ryu H, Lee J, Hagerty SW, Soh BY, McAlpin SE, Cormier KA, Smith KM, Ferrante RJ: ESET/SETDB1 gene expression and histone H3 (K9) trimethylation in Huntington's disease. Proc Natl Acad Sci U S A. 2006 Dec 12;103(50):19176-81. Epub 2006 Dec 1. [PubMed Link Image]
  15. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
  16. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  17. Meierhofer D, Wang X, Huang L, Kaiser P: Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry. J Proteome Res. 2008 Oct;7(10):4566-76. Epub 2008 Sep 10. [PubMed Link Image]
  18. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5649
Enzyme 12 Name Protein-L-isoaspartate(D-aspartate) O-methyltransferase
Enzyme 12 Synonyms
  1. PIMT
  2. L-isoaspartyl protein carboxyl methyltransferase
  3. Protein L-isoaspartyl/D-aspartyl methyltransferase
  4. Protein-beta-aspartate methyltransferase
Enzyme 12 Gene Name PCMT1
Enzyme 12 Protein Sequence >Protein-L-isoaspartate(D-aspartate) O-methyltransferase
MAWKSGGASHSELIHNLRKNGIIKTDKVFEVMLATDRSHYAKCNPYMDSPQSIGFQATIS
APHMHAYALELLFDQLHEGAKALDVGSGSGILTACFARMVGCTGKVIGIDHIKELVDDSI
NNVRKDDPTLLSSGRVQLVVGDGRMGYAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLI
LPVGPAGGNQMLEQYDKLQDGSIKMKPLMGVIYVPLTDKEKQWSRWK
Enzyme 12 Number of Residues 227
Enzyme 12 Molecular Weight 24650.2
Enzyme 12 Theoretical pI 7.25
Enzyme 12 GO Classification
Function
  • S-adenosylmethionine-dependent methyltransferase activity
  • catalytic activity
  • methyltransferase activity
  • protein-L-isoaspartate (D-aspartate) O-methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein modification process
Component
Enzyme 12 General Function Involved in protein-L-isoaspartate (D-aspartate) O-methyltransferase activity
Enzyme 12 Specific Function Catalyzes the methyl esterification of L-isoaspartyl and D-aspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins. Acts on microtubule-associated protein 2, calreticulin, clathrin light chains a and b, Ubiquitin carboxyl- terminal hydrolase isozyme L1, phosphatidylethanolamine-binding protein 1, stathmin, beta-synuclein and alpha-synuclein
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions
  • S-adenosyl-L-methionine + protein L-isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester [RN:R04190]
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 158260471 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID P22061 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name PIMT_HUMAN Link Image
Enzyme 12 PDB ID 1KR5 Link Image
Enzyme 12 PDB File Show
Enzyme 12 3D Structure
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >684 bp
ATGGCCTGGAAATCCGGCGGCGCCAGCCACTCGGAGCTAATCCACAATCTCCGCAAAAAT
GGAATCATCAAGACAGATAAAGTATTTGAAGTGATGCTGGCTACAGACCGCTCCCACTAT
GCAAAATGTAACCCATACATGGATTCTCCACAATCAATAGGTTTCCAAGCAACAATCAGT
GCTCCACACATGCATGCATATGCGCTAGAACTTCTATTTGATCAGTTGCATGAAGGAGCT
AAAGCTCTTGATGTAGGATCTGGAAGTGGAATCCTTACTGCATGTTTTGCACGTATGGTT
GGATGTACTGGAAAAGTCATAGGAATTGATCACATTAAAGAGCTAGTAGATGACTCAGTA
AATAATGTCAGGAAGGACGATCCAACACTTCTGTCTTCAGGGAGAGTACAGCTTGTTGTG
GGGGATGGAAGAATGGGATATGCTGAAGAAGCCCCTTATGATGCCATTCATGTGGGAGCT
GCAGCCCCTGTTGTACCCCAGGCGCTAATAGATCAGTTAAAGCCCGGAGGAAGATTGATA
TTGCCTGTTGGTCCTGCAGGCGGAAACCAAATGTTGGAGCAGTATGACAAGCTACAAGAT
GGCAGCATCAAAATGAAGCCTCTGATGGGGGTGATATACGTGCCTTTAACAGATAAAGAA
AAGCAGTGGTCCAGGTGGAAGTGA
Enzyme 12 GenBank Gene ID AK289724 Link Image
Enzyme 12 GeneCard ID PCMT1 Link Image
Enzyme 12 GenAtlas ID PCMT1 Link Image
Enzyme 12 HGNC ID HGNC:8728 Link Image
Enzyme 12 Chromosome Location 6
Enzyme 12 Locus 6q24-q25
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Ingrosso D, Fowler AV, Bleibaum J, Clarke S: Sequence of the D-aspartyl/L-isoaspartyl protein methyltransferase from human erythrocytes. Common sequence motifs for protein, DNA, RNA, and small molecule S-adenosylmethionine-dependent methyltransferases. J Biol Chem. 1989 Nov 25;264(33):20131-9. [PubMed Link Image]
  2. MacLaren DC, Kagan RM, Clarke S: Alternative splicing of the human isoaspartyl protein carboxyl methyltransferase RNA leads to the generation of a C-terminal -RDEL sequence in isozyme II. Biochem Biophys Res Commun. 1992 May 29;185(1):277-83. [PubMed Link Image]
  3. Takeda R, Mizobuchi M, Murao K, Sato M, Takahara J: Characterization of three cDNAs encoding two isozymes of an isoaspartyl protein carboxyl methyltransferase from human erythroid leukemia cells. J Biochem (Tokyo). 1995 Apr;117(4):683-5. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. 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]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. DeVry CG, Tsai W, Clarke S: Structure of the human gene encoding the protein repair L-isoaspartyl (D-aspartyl) O-methyltransferase. Arch Biochem Biophys. 1996 Nov 15;335(2):321-32. [PubMed Link Image]
  8. Gilbert JM, Fowler A, Bleibaum J, Clarke S: Purification of homologous protein carboxyl methyltransferase isozymes from human and bovine erythrocytes. Biochemistry. 1988 Jul 12;27(14):5227-33. [PubMed Link Image]
  9. Tsai W, Clarke S: Amino acid polymorphisms of the human L-isoaspartyl/D-aspartyl methyltransferase involved in protein repair. Biochem Biophys Res Commun. 1994 Aug 30;203(1):491-7. [PubMed Link Image]
  10. Ingrosso D, Kagan RM, Clarke S: Distinct C-terminal sequences of isozymes I and II of the human erythrocyte L-isoaspartyl/D-aspartyl protein methyltransferase. Biochem Biophys Res Commun. 1991 Feb 28;175(1):351-8. [PubMed Link Image]
  11. DeVry CG, Clarke S: Polymorphic forms of the protein L-isoaspartate (D-aspartate) O-methyltransferase involved in the repair of age-damaged proteins. J Hum Genet. 1999;44(5):275-88. [PubMed Link Image]
  12. Ryttersgaard C, Griffith SC, Sawaya MR, MacLaren DC, Clarke S, Yeates TO: Crystal structure of human L-isoaspartyl methyltransferase. J Biol Chem. 2002 Mar 22;277(12):10642-6. Epub 2002 Jan 15. [PubMed Link Image]
  13. Smith CD, Carson M, Friedman AM, Skinner MM, Delucas L, Chantalat L, Weise L, Shirasawa T, Chattopadhyay D: Crystal structure of human L-isoaspartyl-O-methyl-transferase with S-adenosyl homocysteine at 1.6-A resolution and modeling of an isoaspartyl-containing peptide at the active site. Protein Sci. 2002 Mar;11(3):625-35. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5651
Enzyme 13 Name Protein-S-isoprenylcysteine O-methyltransferase
Enzyme 13 Synonyms
  1. Isoprenylcysteine carboxylmethyltransferase
  2. Prenylated protein carboxyl methyltransferase
  3. PPMT
  4. Prenylcysteine carboxyl methyltransferase
  5. pcCMT
Enzyme 13 Gene Name ICMT
Enzyme 13 Protein Sequence >Protein-S-isoprenylcysteine O-methyltransferase
MAGCAARAPPGSEARLSLATFLLGASVLALPLLTRAGLQGRTGLALYVAGLNALLLLLYR
PPRYQIAIRACFLGFVFGCGTLLSFSQSSWSHFGWYMCSLSLFHYSEYLVTAVNNPKSLS
LDSFLLNHSLEYTVAALSSWLEFTLENIFWPELKQITWLSVTGLLMVVFGECLRKAAMFT
AGSNFNHVVQNEKSDTHTLVTSGVYAWFRHPSYVGWFYWSIGTQVMLCNPICGVSYALTV
WRFFRDRTEEEEISLIHFFGEEYLEYKKRVPTGLPFIKGVKVDL
Enzyme 13 Number of Residues 284
Enzyme 13 Molecular Weight 31937.8
Enzyme 13 Theoretical pI 8.05
Enzyme 13 GO Classification
Function
  • catalytic activity
  • methyltransferase activity
  • protein C-terminal S-isoprenylcysteine carboxyl O-methyltransferase activity
  • protein C-terminal carboxyl O-methyltransferase activity
  • protein carboxyl O-methyltransferase activity
  • protein methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • C-terminal protein amino acid methylation
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • post-translational protein modification
  • protein amino acid alkylation
  • protein amino acid methylation
  • protein modification process
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 13 General Function Involved in protein C-terminal S-isoprenylcysteine carboxyl O-methyltransferase activity
Enzyme 13 Specific Function Catalyzes the post-translational methylation of isoprenylated C-terminal cysteine residues
Enzyme 13 Pathways Not Available
Enzyme 13 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 [RN:R04496]
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • 18-38 42-62 66-86 214-234
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 3135669 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID O60725 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name ICMT_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >855 bp
ATGGCGGGCTGCGCGGCGCGGGCTCCGCCGGGCTCTGAGGCGCGTCTCAGCCTCGCCACC
TTCCTGCTGGGCGCCTCGGTGCTCGCGCTGCCGCTGCTCACGCGCGCCGGCCTGCAGGGC
CGCACCGGGCTGGCGCTCTACGTGGCCGGGCTCAACGCGCTGCTGCTGCTGCTCTATCGG
CCGCCTCGCTACCAGATAGCCATCCGAGCTTGTTTCCTGGGGTTTGTGTTCGGCTGCGGC
ACGCTGCTAAGTTTTAGCCAGTCTTCTTGGAGTCACTTTGGCTGGTACATGTGCTCCCTG
TCATTGTTCCACTATTCTGAATACTTGGTGACAGCAGTCAATAATCCCAAAAGTCTGTCC
TTGGATTCCTTTCTCCTGAATCACAGCCTGGAGTATACAGTAGCTGCTCTTTCTTCTTGG
TTAGAGTTCACACTTGAAAATATCTTTTGGCCAGAACTGAAGCAGATTACCTGGCTCAGT
GTCACAGGGCTGCTGATGGTGGTCTTCGGAGAATGTCTGAGGAAGGCGGCCATGTTTACA
GCTGGCTCCAATTTCAACCACGTGGTACAGAATGAAAAATCAGATACACATACTCTGGTG
ACCAGTGGAGTGTACGCTTGGTTTCGGCATCCTTCTTACGTCGGGTGGTTTTACTGGAGT
ATTGGAACTCAGGTGATGCTGTGTAACCCCATCTGCGGCGTCAGCTATGCCCTGACAGTG
TGGCGATTCTTCCGCGATCGAACAGAAGAAGAAGAAATCTCACTAATTCACTTTTTTGGA
GAGGAGTACCTGGAGTATAAGAAGAGGGTGCCCACGGGCCTGCCTTTCATAAAGGGGGTC
AAGGTGGACCTGTGA
Enzyme 13 GenBank Gene ID AF064084 Link Image
Enzyme 13 GeneCard ID ICMT Link Image
Enzyme 13 GenAtlas ID ICMT Link Image
Enzyme 13 HGNC ID HGNC:5350 Link Image
Enzyme 13 Chromosome Location 1
Enzyme 13 Locus 1p36.21
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. 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 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5652
Enzyme 14 Name Indolethylamine N-methyltransferase
Enzyme 14 Synonyms
  1. Indolamine N-methyltransferase
  2. Aromatic alkylamine N-methyltransferase
  3. Amine N-methyltransferase
  4. Arylamine N-methyltransferase
Enzyme 14 Gene Name INMT
Enzyme 14 Protein Sequence >Indolethylamine N-methyltransferase
MKGGFTGGDEYQKHFLPRDYLATYYSFDGSPSPEAEMLKFNLECLHKTFGPGGLQGDTLI
DIGSGPTIYQVLAACDSFQDITLSDFTDRNREELEKWLKKEPGAYDWTPAVKFACELEGN
SGRWEEKEEKLRAAVKRVLKCDVHLGNPLAPAVLPLADCVLTLLAMECACCSLDAYRAAL
CNLASLLKPGGHLVTTVTLRLPSYMVGKREFSCVALEKEEVEQAVLDAGFDIEQLLHSPQ
SYSVTNAANNGVCFIVARKKPGP
Enzyme 14 Number of Residues 263
Enzyme 14 Molecular Weight 28890.8
Enzyme 14 Theoretical pI 4.92
Enzyme 14 GO Classification
Function
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
Component
Enzyme 14 General Function Involved in methyltransferase activity
Enzyme 14 Specific Function Catalyzes the N-methylation of tryptamine and structurally related compounds (Potential)
Enzyme 14 Pathways
Enzyme 14 Reactions
  • S-adenosyl-L-methionine + an amine = S-adenosyl-L-homocysteine + a methylated amine [RN:R02808]
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 66933018 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID O95050 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name INMT_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >792 bp
ATGAAGGGTGGCTTCACTGGGGGTGATGAGTACCAGAAGCACTTCCTGCCCAGGGACTAC
TTGGCTACTTACTACAGCTTCGATGGCAGCCCCTCACCCGAGGCCGAGATGCTGAAGTTT
AACTTGGAATGTCTCCACAAGACCTTCGGCCCTGGAGGCCTCCAAGGGGACACGCTGATT
GACATTGGCTCAGGTCCTACCATCTACCAAGTTCTTGCTGCCTGTGATTCCTTCCAAGAC
ATCACTCTCTCCGACTTTACCGACCGCAACCGGGAGGAGCTGGAAAAGTGGCTGAAGAAG
GAGCCGGGGGCCTATGACTGGACCCCAGCGGTGAAATTCGCCTGTGAGCTGGAAGGAAAC
AGCGGCCGATGGGAGGAGAAGGAGGAGAAGCTGCGGGCAGCGGTGAAGCGGGTGCTCAAG
TGCGATGTCCACCTGGGCAACCCGCTGGCCCCGGCTGTGTTGCCTCTCGCCGACTGTGTG
CTCACCCTGCTGGCCATGGAGTGTGCCTGCTGTAGCCTTGATGCCTACCGCGCTGCCCTG
TGCAACCTTGCCTCACTGCTCAAGCCGGGTGGCCACCTGGTGACCACTGTCACGCTTCGG
CTCCCGTCCTACATGGTGGGGAAGCGTGAATTTTCCTGCGTGGCCCTGGAGAAAGAGGAG
GTGGAGCAGGCTGTCCTGGATGCTGGCTTTGACATTGAACAGCTCCTACACAGTCCCCAG
AGCTACTCTGTCACCAATGCTGCCAACAATGGGGTCTGCTTCATTGTGGCTCGCAAGAAG
CCTGGGCCCTGA
Enzyme 14 GenBank Gene ID NM_006774.4 Link Image
Enzyme 14 GeneCard ID INMT Link Image
Enzyme 14 GenAtlas ID INMT Link Image
Enzyme 14 HGNC ID HGNC:6069 Link Image
Enzyme 14 Chromosome Location 7
Enzyme 14 Locus 7p15.1
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 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]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Kitano T, Liu YH, Ueda S, Saitou N: Human-specific amino acid changes found in 103 protein-coding genes. Mol Biol Evol. 2004 May;21(5):936-44. Epub 2004 Mar 10. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 5653
Enzyme 15 Name DNA (cytosine-5)-methyltransferase 3A
Enzyme 15 Synonyms
  1. Dnmt3a
  2. DNA methyltransferase HsaIIIA
  3. DNA MTase HsaIIIA
  4. M.HsaIIIA
Enzyme 15 Gene Name DNMT3A
Enzyme 15 Protein Sequence >DNA (cytosine-5)-methyltransferase 3A
MPAMPSSGPGDTSSSAAEREEDRKDGEEQEEPRGKEERQEPSTTARKVGRPGRKRKHPPV
ESGDTPKDPAVISKSPSMAQDSGASELLPNGDLEKRSEPQPEEGSPAGGQKGGAPAEGEG
AAETLPEASRAVENGCCTPKEGRGAPAEAGKEQKETNIESMKMEGSRGRLRGGLGWESSL
RQRPMPRLTFQAGDPYYISKRKRDEWLARWKREAEKKAKVIAGMNAVEENQGPGESQKVE
EASPPAVQQPTDPASPTVATTPEPVGSDAGDKNATKAGDDEPEYEDGRGFGIGELVWGKL
RGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYN
KQPMYRKAIYEVLQVASSRAGKLFPVCHDSDESDTAKAVEVQNKPMIEWALGGFQPSGPK
GLEPPEEEKNPYKEVYTDMWVEPEAAAYAPPPPAKKPRKSTAEKPKVKEIIDERTRERLV
YEVRQKCRNIEDICISCGSLNVTLEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTIC
CGGREVLMCGNNNCCRCFCVECVDLLVGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRRED
WPSRLQMFFANNHDQEFDPPKVYPPVPAEKRKPIRVLSLFDGIATGLLVLKDLGIQVDRY
IASEVCEDSITVGMVRHQGKIMYVGDVRSVTQKHIQEWGPFDLVIGGSPCNDLSIVNPAR
KGLYEGTGRLFFEFYRLLHDARPKEGDDRPFFWLFENVVAMGVSDKRDISRFLESNPVMI
DAKEVSAAHRARYFWGNLPGMNRPLASTVNDKLELQECLEHGRIAKFSKVRTITTRSNSI
KQGKDQHFPVFMNEKEDILWCTEMERVFGFPVHYTDVSNMSRLARQRLLGRSWSVPVIRH
LFAPLKEYFACV
Enzyme 15 Number of Residues 912
Enzyme 15 Molecular Weight 101857.6
Enzyme 15 Theoretical pI 6.52
Enzyme 15 GO Classification
Function
  • DNA binding
  • binding
  • cation binding
  • ion binding
  • metal ion binding
  • nucleic acid binding
  • transition metal ion binding
  • zinc ion binding
Process
  • DNA alkylation
  • DNA metabolic process
  • DNA methylation
  • DNA modification
  • cellular macromolecule metabolic process
  • macromolecule metabolic process
  • metabolic process
Component
Enzyme 15 General Function Involved in DNA binding
Enzyme 15 Specific Function Required for genome wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. DNA methylation is coordinated with methylation of histones. It modifies DNA in a non-processive manner and also methylates non-CpG sites. May preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1. Plays a role in paternal and maternal imprinting. Required for methylation of most imprinted loci in germ cells. Acts as a transcriptional corepressor for ZNF238. Can actively repress transcription through the recruitment of HDAC activity
Enzyme 15 Pathways
Enzyme 15 Reactions
  • S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine [RN:R00380]
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 12746532 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID Q9Y6K1 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name DNM3A_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 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 15 GenBank Gene ID AF067972 Link Image
Enzyme 15 GeneCard ID DNMT3A Link Image
Enzyme 15 GenAtlas ID DNMT3A Link Image
Enzyme 15 HGNC ID HGNC:2978 Link Image
Enzyme 15 Chromosome Location 2
Enzyme 15 Locus 2p23
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 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. Chen T, Ueda Y, Xie S, Li E: A novel Dnmt3a isoform produced from an alternative promoter localizes to euchromatin and its expression correlates with active de novo methylation. J Biol Chem. 2002 Oct 11;277(41):38746-54. Epub 2002 Jul 22. [PubMed Link Image]
  3. Kim GD, Ni J, Kelesoglu N, Roberts RJ, Pradhan S: Co-operation and communication between the human maintenance and de novo DNA (cytosine-5) methyltransferases. EMBO J. 2002 Aug 1;21(15):4183-95. [PubMed Link Image]
  4. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. 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]
  7. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  8. Li H, Rauch T, Chen ZX, Szabo PE, Riggs AD, Pfeifer GP: The histone methyltransferase SETDB1 and the DNA methyltransferase DNMT3A interact directly and localize to promoters silenced in cancer cells. J Biol Chem. 2006 Jul 14;281(28):19489-500. Epub 2006 May 8. [PubMed Link Image]
  9. Vire E, Brenner C, Deplus R, Blanchon L, Fraga M, Didelot C, Morey L, Van Eynde A, Bernard D, Vanderwinden JM, Bollen M, Esteller M, Di Croce L, de Launoit Y, Fuks F: The Polycomb group protein EZH2 directly controls DNA methylation. Nature. 2006 Feb 16;439(7078):871-4. Epub 2005 Dec 14. [PubMed Link Image]
  10. Schlesinger Y, Straussman R, Keshet I, Farkash S, Hecht M, Zimmerman J, Eden E, Yakhini Z, Ben-Shushan E, Reubinoff BE, Bergman Y, Simon I, Cedar H: Polycomb-mediated methylation on Lys27 of histone H3 pre-marks genes for de novo methylation in cancer. Nat Genet. 2007 Feb;39(2):232-6. Epub 2006 Dec 31. [PubMed Link Image]
  11. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  12. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  13. Jia D, Jurkowska RZ, Zhang X, Jeltsch A, Cheng X: Structure of Dnmt3a bound to Dnmt3L suggests a model for de novo DNA methylation. Nature. 2007 Sep 13;449(7159):248-51. Epub 2007 Aug 22. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 5654
Enzyme 16 Name Hexaprenyldihydroxybenzoate methyltransferase, mitochondrial
Enzyme 16 Synonyms
  1. 3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase
  2. DHHB methyltransferase
  3. DHHB-MT
  4. DHHB-MTase
  5. Dihydroxyhexaprenylbenzoate methyltransferase
Enzyme 16 Gene Name COQ3
Enzyme 16 Protein Sequence >Hexaprenyldihydroxybenzoate methyltransferase, mitochondrial
MWSGRKLGSSGGWFLRVLGPGGCNTKAARPLISSAVYVKNQLSGTLQIKPGVFNEYRTIW
FKSYRTIFSCLNRIKSFRYPWARLYSTSQTTVDSGEVKTFLALAHKWWDEQGVYAPLHSM
NDLRVPFIRDNLLKTIPNHQPGKPLLGMKILDVGCGGGLLTEPLGRLGASVIGIDPVDEN
IKTAQCHKSFDPVLDKRIEYRVCSLEEIVEETAETFDAVVASEVVEHVIDLETFLQCCCQ
VLKPGGSLFITTINKTQLSYALGIVFSEQIAGIVPKGTHTWEKFVSPETLESILESNGLS
VQTVVGMLYNPFSGYWHWSENTSLNYAAHAVKSRVQEHPASAEFVLKGETEELQANACTN
PAVHEKLKK
Enzyme 16 Number of Residues 369
Enzyme 16 Molecular Weight 40997.7
Enzyme 16 Theoretical pI 7.50
Enzyme 16 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 metabolic process
  • coenzyme metabolic process
  • cofactor metabolic process
  • metabolic process
  • oxidoreduction coenzyme metabolic process
  • ubiquinone biosynthetic process
  • ubiquinone metabolic process
Component
Enzyme 16 General Function Involved in methyltransferase activity
Enzyme 16 Specific Function S-adenosyl-L-methionine + 3-hexaprenyl-4,5- dihydroxybenzoate = S-adenosyl-L-homocysteine + 3-hexaprenyl-4- hydroxy-5-methoxybenzoate
Enzyme 16 Pathways
Enzyme 16 Reactions
  • S-adenosyl-L-methionine + 3-hexaprenyl-4,5-dihydroxybenzoate = S-adenosyl-L-homocysteine + 3-hexaprenyl-4-hydroxy-5-methoxybenzoate [RN:R04711]
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 118600965 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID Q9NZJ6 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name COQ3_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >1110 bp
ATGTGGAGTGGCCGTAAGCTGGGCTCCTCCGGGGGTTGGTTTTTAAGAGTGCTGGGGCCT
GGAGGCTGTAATACAAAAGCTGCGCGTCCCTTAATTTCCTCGGCGGTTTATGTGAAGAAC
CAGCTCAGTGGGACTCTACAGATTAAACCAGGGGTTTTCAATGAATACAGAACCATATGG
TTCAAATCCTACAGGACGATCTTTTCCTGTTTGAACAGAATAAAGAGTTTCAGGTACCCT
TGGGCGAGACTGTACAGTACTTCCCAAACCACTGTCGACAGCGGTGAGGTAAAAACCTTC
TTGGCCCTGGCTCACAAATGGTGGGATGAACAAGGAGTATATGCACCTCTTCATTCCATG
AATGACCTGAGGGTGCCATTTATTAGGGACAATCTTCTGAAAACAATTCCTAATCACCAG
CCAGGAAAACCTTTGTTGGGGATGAAGATTCTTGACGTTGGCTGTGGTGGTGGGCTGTTA
ACTGAACCTCTAGGGCGGCTTGGGGCTTCAGTTATTGGAATCGACCCTGTGGATGAGAAC
ATTAAAACAGCACAATGCCATAAATCATTTGATCCAGTCCTGGATAAGAGAATAGAGTAC
AGAGTGTGTTCCCTGGAAGAGATTGTGGAAGAGACTGCAGAAACATTTGATGCTGTTGTA
GCTTCTGAAGTTGTAGAACATGTGATTGATCTAGAAACATTTTTACAGTGCTGCTGTCAA
GTGTTAAAACCCGGTGGTTCTTTATTCATTACTACAATCAACAAAACACAACTTTCCTAT
GCCTTGGGAATTGTTTTTTCAGAGCAAATTGCAAGTATTGTACCAAAAGGTACTCATACA
TGGGAGAAGTTTGTTTCACCTGAAACACTAGAGAGCATTCTGGAATCAAATGGTCTGTCA
GTTCAAACAGTGGTAGGAATGCTCTATAACCCCTTCTCAGGTTACTGGCATTGGAGTGAA
AATACCAGCCTTAACTATGCAGCTTATGCTGTGAAATCCAGGGTCCAGGAACACCCAGCC
TCTGCTGAGTTTGTTTTAAAGGGAGAAACAGAAGAGCTCCAAGCTAATGCCTGCACCAAT
CCAGCTGTGCATGAAAAGCTGAAGAAATGA
Enzyme 16 GenBank Gene ID NM_017421.3 Link Image
Enzyme 16 GeneCard ID COQ3 Link Image
Enzyme 16 GenAtlas ID COQ3 Link Image
Enzyme 16 HGNC ID HGNC:18175 Link Image
Enzyme 16 Chromosome Location 6
Enzyme 16 Locus 6q16.2
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 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. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. 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]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. 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 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 5656
Enzyme 17 Name Histone-lysine N-methyltransferase, H3 lysine-9 specific 3
Enzyme 17 Synonyms
  1. Euchromatic histone-lysine N-methyltransferase 2
  2. HLA-B-associated transcript 8
  3. Histone H3-K9 methyltransferase 3
  4. H3-K9-HMTase 3
  5. Lysine N-methyltransferase 1C
  6. Protein G9a
Enzyme 17 Gene Name EHMT2
Enzyme 17 Protein Sequence >Histone-lysine N-methyltransferase, H3 lysine-9 specific 3
MAAAAGAAAAAAAEGEAPAEMGALLLEKETRGATERVHGSLGDTPRSEETLPKATPDSLE
PAGPSSPASVTVTVGDEGADTPVGATPLIGDESENLEGDGDLRGGRILLGHATKSFPSSP
SKGGSCPSRAKMSMTGAGKSPPSVQSLAMRLLSMPGAQGAAAAGSEPPPATTSPEGQPKV
HRARKTMSKPGNGQPPVPEKRPPEIQHFRMSDDVHSLGKVTSDLAKRRKLNSGGGLSEEL
GSARRSGEVTLTKGDPGSLEEWETVVGDDFSLYYDSYSVDERVDSDSKSEVEALTEQLSE
EEEEEEEEEEEEEEEEEEEEEEEDEESGNQSDRSGSSGRRKAKKKWRKDSPWVKPSRKRR
KREPPRAKEPRGVNGVGSSGPSEYMEVPLGSLELPSEGTLSPNHAGVSNDTSSLETERGF
EELPLCSCRMEAPKIDRISERAGHKCMATESVDGELSGCNAAILKRETMRPSSRVALMVL
CETHRARMVKHHCCPGCGYFCTAGTFLECHPDFRVAHRFHKACVSQLNGMVFCPHCGEDA
SEAQEVTIPRGDGVTPPAGTAAPAPPPLSQDVPGRADTSQPSARMRGHGEPRRPPCDPLA
DTIDSSGPSLTLPNGGCLSAVGLPLGPGREALEKALVIQESERRKKLRFHPRQLYLSVKQ
GELQKVILMLLDNLDPNFQSDQQSKRTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRT
PLMEAVVNNHLEVARYMVQRGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGQVDVNA
QDSGGWTPIIWAAEHKHIEVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNA
RCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTAWDLTPERSDVWFA
LQLNRKLRLGVGNRAIRTEKIICRDVARGYENVPIPCVNGVDGEPCPEDYKYISENCETS
TMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQA
CSCWRNCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVR
EDDSYLFDLDNKDGEVYCIDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFS
SRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQSRLARLDPHPELLP
ELGSLPPVNT
Enzyme 17 Number of Residues 1210
Enzyme 17 Molecular Weight 132369.2
Enzyme 17 Theoretical pI 5.14
Enzyme 17 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • histone-lysine N-methyltransferase activity
  • ion binding
  • metal 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
  • cellular component organization at cellular level
  • cellular process
  • chromatin modification
  • chromatin organization
  • chromosome organization
  • organelle organization
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 17 General Function Involved in zinc ion binding
Enzyme 17 Specific Function Histone methyltransferase. Preferentially methylates 'Lys-9' of histone H3 and 'Lys-27' of histone H3 (in vitro). H3 'Lys-9' methylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1. Also methylates histone H1
Enzyme 17 Pathways
Enzyme 17 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 15917538 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID Q96KQ7 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name EHMT2_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >3633 bp
ATGGCGGCGGCGGCGGGAGCTGCAGCGGCGGCGGCCGCCGAGGGGGAGGCCCCCGCTGAG
ATGGGGGCGCTGCTGCTGGAGAAGGAAACCAGAGGAGCCACCGAGAGAGTTCATGGCTCT
TTGGGGGACACCCCTCGTAGTGAAGAAACCCTGCCCAAGGCCAACCCCGACTCCCTGGAG
CCTGCTGGCCCCTCATCTCCAGCCTCTGTCACTGTCACTGTTGGTGATGAGGGGGCTGAC
ACCCCTGTAGGGGCTACACCACTCATTGGGGATGAATCTGAGAATCTTGAGGGAGATGGG
GACCTCCGTGGGGGCCGGATCCTGCTGGGCCATGCCACAAAGTCATTCCCCTCTTCCCCC
AGCAAGGGGGGTTCCTGTCCTAGCCGGGCCAAGATGTCAATGACAGGGGCGGGAAAATCA
CCTCCATCTGTCCAGAGTTTGGCTATGAGGCTACTGAGTATGCCAGGAGCCCAGGGAGCT
GCAGCAGCAGGGTCTGAACCCCCTCCAGCCACCACGAGCCCAGAGGGACAGTCCAAGGTC
CACCGAGCCCGCAAAACCATGTCCAAACCAGGAAATGGACAGCCCCCGGTCCCTGAGAAG
CGGCCCCCTGAAATACAGCATTTCCGCATGAGTGATGATGTCCACTCACTGGGAAAGGTG
ACCTCAGATCTGGCCAAAAGGAGGAAGCTGAACTCAGGAGGTGGCCTGTCGGAGGAGTTA
GGTTCTGCCCGGCGTTCAGGAGAAGTGACCCTGACGAAAGGGGACCCCGGGTCCCTGGAG
GAGTGGGAGACGGTGGTGGGTGATGACTTCAGTCTCTACTATGATTCCTACTCTGTGGAT
GAGCGCGTGGACTCCGACAGCAAGTCTGAAGTTGAAGCTCTAACTGAACAACTAAGTGAA
GAGGAGGAGGAGGAAGAGGAGGAAGAAGAAGAAGAGGAAGAGGAGGAGGAAGAGGAAGAA
GAAGAGGAAGATGAGGAGTCAGGGAATCAGTCAGATAGGAGTGGTTCCAGTGGCCGGCGC
AAGGCCAAGAAGAAATGGCGAAAAGACAGCCCATGGGTGAAGCCGTCTCGGAAACGGCGC
AAGCGGGAGCCTCCGCGGGCCAAGGAGCCACGAGGAGTGAATGGTGTGGGCTCCTCAGGC
CCCAGTGAGTACATGGAGGTCCCTCTGGGGTCCCTGGAGCTGCCCAGCGAGGGGACCCTC
TCCCCCAACCACGCTGGGGTGTCCAATGACACATCTTCGCTGGAGACAGAGCGAGGGTTT
GAGGAGTTGCCCCTGTGCAGCTGCCGCATGGAGGCACCCAAGATTGACCGCATCAGCGAG
AGGGCGGGGCACAAGTGCATGGCCACTGAGAGTGTGGACGGAGAGCTGTCAGGCTGCAAT
GCCGCCATCCTCAAGCGGGAGACCATGAGGCCATCCAGCCGTGTGGCCCTGATGGTGCTC
TGTGAGACCCACCGCGCCCGCATGGTCAAACACCACTGCTGCCCGGGCTGCGGCTACTTC
TGCACGGCGGGCACCTTCCTGGAGTGCCACCCTGACTTCCGTGTGGCCCACCGCTTCCAC
AAGGCCTGTGTGTCTCAGCTGAATGGGATGGTCTTCTGTCCCCACTGTGGGGAGGATGCT
TCTGAAGCTCAAGAGGTGACCATCCCCCGGGGTGACGGGGTGACCCCACCGGCCGGCACT
GCAGCTCCTGCACCCCCACCCCTGTCCCAGGATGTCCCCGGGAGAGCAGACACTTCTCAG
CCCAGTGCCCGGATGCGAGGGCATGGGGAACCCCGGCGCCCGCCCTGCGATCCCCTGGCT
GACACCATTGACAGCTCAGGGCCCTCCCTGACCCTGCCCAATGGGGGCTGCCTTTCAGCC
GTGGGGCTGCCACTGGGGCCAGGCCGGGAGGCCCTGGAAAAGGCCCTGGTCATCCAGGAG
TCAGAGAGGCGGAAGAAGCTCCGTTTCCACCCTCGGCAGTTGTACCTGTCCGTGAAGCAG
GGCGAGCTGCAGAAGGTGATCCTGATGCTGTTGGACAACCTGGACCCCAACTTCCAGAGC
GACCAGCAGAGCAAGCGCACGCCCCTGCATGCAGCCGCCCAGAAGGGCTCCGTGGAGATC
TGCCATGTGCTGCTGCAGGCTGGAGCCAACATAAATGCAGTGGACAAACAGCAGCGGACG
CCACTGATGGAGGCCGTGGTGAACAACCACCTGGAGGTAGCCCGTTACATGGTGCAGCGT
GGTGGCTGTGTCTATAGCAAGGAGGAGGACGGTTCCACCTGCCTCCACCACGCAGCCAAA
ATCGGGAACTTGGAGATGGTCAGCCTGCTGCTGAGCACAGGACAGGTGGACGTCAACGCC
CAGGACAGTGGGGGGTGGACGCCCATCATCTGGGCTGCAGAGCACAAGCACATCGAGGTG
ATCCGCATGCTACTGACGCGGGGCGCCGACGTCACCCTCACTGACAACGAGGAGAACATC
TGCCTGCACTGGGCCTCCTTCACGGGCAGCGCCGCCATCGCCGAAGTCCTTCTGAATGCG
CGCTGTGACCTCCATGCTGTCAACTACCATGGGGACACCCCCCTGCACATCGCAGCTCGG
GAGAGCTACCATGACTGCGTGCTGTTATTCCTGTCACGTGGGGCCAACCCTGAGCTGCGG
AACAAAGAGGGGGACACAGCATGGGACCTGACTCCCGAGCGCTCCGACGTGTGGTTTGCG
CTTCAACTCAACCGCAAGCTCCGACTTGGGGTGGGAAATCGGGCCATCCGCACAGAGAAG
ATCATCTGCCGGGACGTGGCTCGGGGCTATGAGAACGTGCCCATTCCCTGTGTCAACGGT
GTGGATGGGGAGCCCTGCCCTGAGGATTACAAGTACATCTCAGAGAACTGCGAGACGTCC
ACCATGAACATCGATCGCAACATCACCCACCTGCAGCACTGCACGTGTGTGGACGACTGC
TCTAGCTCCAACCGCCTGTGCGGCCAGCTCAGCATCCGGTGCTGGTATGACAAGGATGGG
CGATTGCTCCAGGAATTTAACAAGATTGAGCCTCCGCTGATTTTCGAGTGTAACCAGGCG
TGCTCATGCTGGAGAAACTGCAAGAACCGGGTCGTACAGAGTGGCATCAAGGTGCGGCTA
CAGCTCTACCGAACAGCCAAGATGGGCTGGGGGGTCCGCGCCCTGCAGACCATCCCACAG
GGGACCTTCATCTGCGAGTATGTCGGGGAGCTGATCTCTGATGCTGAGGCTGATGTGAGA
GAGGATGATTCTTACCTCTTCGACTTAGACAACAAGGATGGAGAGGTGTACTGCATAGAT
GCCCGTTACTATGGCAACATCAGCCGCTTCATCAACCACCTGTGTGACCCCAACATCATT
CCCGTCCGGGTCTTCATGCTGCACCAAGACCTGCGATTTCCACGCATCGCCTTCTTCAGT
TCCCGAGACATCCGGACTGGGGAGGAGCTAGGGTTTGACTATGGCGACCGCTTCTGGGAC
ATCAAAAGCAAATATTTCACCTGCCAATGTGGCTCTGAGAAGTGCAAGCACTCAGCCGAA
GCCATTGCCCTGGAGCAGAGCCGTCTGGCCCGCCTGGACCCACACCCTGAGCTGCTGCCC
GAGCTCGGCTCCCTGCCCCCTGTCAACACATGA
Enzyme 17 GenBank Gene ID AJ315532 Link Image
Enzyme 17 GeneCard ID EHMT2 Link Image
Enzyme 17 GenAtlas ID EHMT2 Link Image
Enzyme 17 HGNC ID HGNC:14129 Link Image
Enzyme 17 Chromosome Location 6
Enzyme 17 Locus 6p21.31
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Brown SE, Campbell RD, Sanderson CM: Novel NG36/G9a gene products encoded within the human and mouse MHC class III regions. Mamm Genome. 2001 Dec;12(12):916-24. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Xie T, Rowen L, Aguado B, Ahearn ME, Madan A, Qin S, Campbell RD, Hood L: Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse. Genome Res. 2003 Dec;13(12):2621-36. [PubMed Link Image]
  4. 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]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Milner CM, Campbell RD: The G9a gene in the human major histocompatibility complex encodes a novel protein containing ankyrin-like repeats. Biochem J. 1993 Mar 15;290 ( Pt 3):811-8. [PubMed Link Image]
  7. Tachibana M, Sugimoto K, Fukushima T, Shinkai Y: Set domain-containing protein, G9a, is a novel lysine-preferring mammalian histone methyltransferase with hyperactivity and specific selectivity to lysines 9 and 27 of histone H3. J Biol Chem. 2001 Jul 6;276(27):25309-17. Epub 2001 Apr 20. [PubMed Link Image]
  8. Ogawa H, Ishiguro K, Gaubatz S, Livingston DM, Nakatani Y: A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells. Science. 2002 May 10;296(5570):1132-6. [PubMed Link Image]
  9. Vassen L, Fiolka K, Moroy T: Gfi1b alters histone methylation at target gene promoters and sites of gamma-satellite containing heterochromatin. EMBO J. 2006 Jun 7;25(11):2409-19. Epub 2006 May 11. [PubMed Link Image]
  10. Ueda J, Tachibana M, Ikura T, Shinkai Y: Zinc finger protein Wiz links G9a/GLP histone methyltransferases to the co-repressor molecule CtBP. J Biol Chem. 2006 Jul 21;281(29):20120-8. Epub 2006 May 15. [PubMed Link Image]
  11. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  12. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  13. Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed Link Image]
  14. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  15. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  16. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  17. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 5658
Enzyme 18 Name Methionine synthase reductase
Enzyme 18 Synonyms
  1. MSR
Enzyme 18 Gene Name MTRR
Enzyme 18 Protein Sequence >Methionine synthase reductase
MGAASVRAGARLVEVALCSFTVTCLEVMRRFLLLYATQQGQAKAIAEEICEQAVVHGFSA
DLHCISESDKYDLKTETAPLVVVVSTTGTGDPPDTARKFVKEIQNQTLPVDFFAHLRYGL
LGLGDSEYTYFCNGGKIIDKRLQELGARHFYDTGHADDCVGLELVVEPWIAGLWPALRKH
FRSSRGQEEISGALPVASPASSRTDLVKSELLHIESQVELLRFDDSGRKDSEVLKQNAVN
SNQSNVVIEDFESSLTRSVPPLSQASLNIPGLPPEYLQVHLQESLGQEESQVSVTSADPV
FQVPISKAVQLTTNDAIKTTLLVELDISNTDFSYQPGDAFSVICPNSDSEVQSLLQRLQL
EDKREHCVLLKIKADTKKKGATLPQHIPAGCSLQFIFTWCLEIRAIPKKAFLRALVDYTS
DSAEKRRLQELCSKQGAADYSRFVRDACACLLDLLLAFPSCQPPLSLLLEHLPKLQPRPY
SCASSSLFHPGKLHFVFNIVEFLSTATTEVLRKGVCTGWLALLVASVLQPNIHASHEDSG
KALAPKISISPRTTNSFHLPDDPSIPIIMVGPGTGIAPFIGFLQHREKLQEQHPDGNFGA
MWLFFGCRHKDRDYLFRKELRHFLKHGILTHLKVSFSRDAPVGEEEAPAKYVQDNIQLHG
QQVARILLQENGHIYVCGDAKNMAKDVHDALVQIISKEVGVEKLEAMKTLATLKEEKRYL
QDIWS
Enzyme 18 Number of Residues 725
Enzyme 18 Molecular Weight 80409.2
Enzyme 18 Theoretical pI 6.47
Enzyme 18 GO Classification
Function
  • FMN binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • nucleotide binding
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 18 General Function Involved in oxidoreductase activity
Enzyme 18 Specific Function Involved in the reductive regeneration of cob(I)alamin cofactor required for the maintenance of methionine synthase in a functional state
Enzyme 18 Pathways Not Available
Enzyme 18 Reactions
  • 2 [methionine synthase]-methylcob(I)alamin + 2 S-adenosylhomocysteine + NADP+ = 2 [methionine synthase]-cob(II)alamin + NADPH + H+ + 2 S-adenosyl-L-methionine [RN:R05182]
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 6561339 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q9UBK8 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name MTRR_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 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 18 GenBank Gene ID AF121214 Link Image
Enzyme 18 GeneCard ID MTRR Link Image
Enzyme 18 GenAtlas ID MTRR Link Image
Enzyme 18 HGNC ID HGNC:7473 Link Image
Enzyme 18 Chromosome Location 5
Enzyme 18 Locus 5p15.31
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 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. Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Froese DS, Wu X, Zhang J, Dumas R, Schoel WM, Amrein M, Gravel RA: Restricted role for methionine synthase reductase defined by subcellular localization. Mol Genet Metab. 2008 May;94(1):68-77. Epub 2008 Jan 24. [PubMed Link Image]
  6. 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]
  7. 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]
  8. Doolin MT, Barbaux S, McDonnell M, Hoess K, Whitehead AS, Mitchell LE: Maternal genetic effects, exerted by genes involved in homocysteine remethylation, influence the risk of spina bifida. Am J Hum Genet. 2002 Nov;71(5):1222-6. Epub 2002 Oct 9. [PubMed Link Image]
  9. O'Leary VB, Mills JL, Pangilinan F, Kirke PN, Cox C, Conley M, Weiler A, Peng K, Shane B, Scott JM, Parle-McDermott A, Molloy AM, Brody LC: Analysis of methionine synthase reductase polymorphisms for neural tube defects risk association. Mol Genet Metab. 2005 Jul;85(3):220-7. Epub 2005 Mar 17. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 5659
Enzyme 19 Name Histone-lysine N-methyltransferase SUV39H1
Enzyme 19 Synonyms
  1. Histone H3-K9 methyltransferase 1
  2. H3-K9-HMTase 1
  3. Lysine N-methyltransferase 1A
  4. Position-effect variegation 3-9 homolog
  5. Suppressor of variegation 3-9 homolog 1
  6. Su(var)3-9 homolog 1
Enzyme 19 Gene Name SUV39H1
Enzyme 19 Protein Sequence >Histone-lysine N-methyltransferase SUV39H1
MAENLKGCSVCCKSSWNQLQDLCRLAKLSCPALGISKRNLYDFEVEYLCDYKKIREQEYY
LVKWRGYPDSESTWEPRQNLKCVRILKQFHKDLERELLRRHHRSKTPRHLDPSLANYLVQ
KAKQRRALRRWEQELNAKRSHLGRITVENEVDLDGPPRAFVYINEYRVGEGITLNQVAVG
CECQDCLWAPTGGCCPGASLHKFAYNDQGQVRLRAGLPIYECNSRCRCGYDCPNRVVQKG
IRYDLCIFRTDDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFD
LDYVEDVYTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIRAGEE
LTFDYNMQVDPVDMESTRMDSNFGLAGLPGSPKKRVRIECKCGTESCRKYLF
Enzyme 19 Number of Residues 412
Enzyme 19 Molecular Weight 47907.1
Enzyme 19 Theoretical pI 8.07
Enzyme 19 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • chromatin binding
  • histone-lysine N-methyltransferase activity
  • ion binding
  • metal 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
  • cellular component organization at cellular level
  • cellular process
  • chromatin assembly or disassembly
  • chromatin modification
  • chromatin organization
  • chromosome organization
  • organelle organization
Component
  • chromatin
  • chromosomal part
  • intracellular membrane-bounded organelle
  • intracellular organelle part
  • membrane-bounded organelle
  • nucleus
  • organelle
  • organelle part
Enzyme 19 General Function Involved in chromatin binding
Enzyme 19 Specific Function Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys- 9' as substrate. Also weakly methylates histone H1 (in vitro). 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 repression of MYOD1-stimulated differentiation, regulation of the control switch for exiting the cell cycle and entering differentiaton, repression by the PML-RARA fusion protein, BMP-induced repression, repression of switch recombination to IgA and regulation of telomere length. Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone- modifying enzymes. The eNoSC complex is able to sense the energy status of cell:upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus
Enzyme 19 Pathways
Enzyme 19 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein Not Available
Enzyme 19 UniProtKB/Swiss-Prot ID O43463 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name SUV91_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >1239 bp
ATGGCGGAAAATTTAAAAGGCTGCAGCGTGTGTTGCAAGTCTTCTTGGAATCAGCTGCAG
GACCTGTGCCGCCTGGCCAAGCTCTCCTGCCCTGCCCTCGGTATCTCTAAGAGGAACCTC
TATGACTTTGAAGTCGAGTACCTGTGCGATTACAAGAAGATCCGCGAACAGGAATATTAC
CTGGTGAAATGGCGTGGATATCCAGACTCAGAGAGCACCTGGGAGCCACGGCAGAATCTC
AAGTGTGTGCGTATCCTCAAGCAGTTCCACAAGGACTTAGAAAGGGAGCTGCTCCGGCGG
CACCACCGGTCAAAGACCCCCCGGCACCTGGACCCAAGCTTGGCCAACTACCTGGTGCAG
AAGGCCAAGCAGAGGCGGGCGCTCCGTCGCTGGGAGCAGGAGCTCAATGCCAAGCGCAGC
CATCTGGGACGCATCACTGTAGAGAATGAGGTGGACCTGGACGGCCCTCCGCGGGCCTTC
GTGTACATCAATGAGTACCGTGTTGGTGAGGGCATCACCCTCAACCAGGTGGCTGTGGGC
TGCGAGTGCCAGGACTGTCTGTGGGCACCCACTGGAGGCTGCTGCCCGGGGGCGTCACTG
CACAAGTTTGCCTACAATGACCAGGGCCAGGTGCGGCTTCGAGCCGGGCTGCCCATCTAC
GAGTGCAACTCCCGCTGCCGCTGCGGCTATGACTGCCCAAATCGTGTGGTACAGAAGGGT
ATCCGATATGACCTCTGCATCTTCCGGACGGATGATGGGCGTGGCTGGGGCGTCCGCACC
CTGGAGAAGATTCGCAAGAACAGCTTCGTCATGGAGTACGTGGGAGAGATCATTACCTCA
GAGGAGGCAGAGCGGCGGGGCCAGATCTACGACCGTCAGGGCGCCACCTACCTCTTTGAC
CTGGACTACGTGGAGGACGTGTACACCGTGGATGCCGCCTACTATGGCAACATCTCCCAC
TTTGTCAACCACAGTTGTGACCCCAACCTGCAGGTGTACAACGTCTTCATAGACAACCTT
GACGAGCGGCTGCCCCGCATCGCTTTCTTTGCCACAAGAACCATCCGGGCAGGCGAGGAG
CTCACCTTTGATTACAACATGCAAGTGGACCCCGTGGACATGGAGAGCACCCGCATGGAC
TCCAACTTTGGCCTGGCTGGGCTCCCTGGCTCCCCTAAGAAGCGGGTCCGTATTGAATGC
AAGTGTGGGACTGAGTCCTGCCGCAAATACCTCTTCTAG
Enzyme 19 GenBank Gene ID AF019968 Link Image
Enzyme 19 GeneCard ID SUV39H1 Link Image
Enzyme 19 GenAtlas ID SUV39H1 Link Image
Enzyme 19 HGNC ID HGNC:11479 Link Image
Enzyme 19 Chromosome Location Not Available
Enzyme 19 Locus Not Available
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Aagaard L, Laible G, Selenko P, Schmid M, Dorn R, Schotta G, Kuhfittig S, Wolf A, Lebersorger A, Singh PB, Reuter G, Jenuwein T: Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31. EMBO J. 1999 Apr 1;18(7):1923-38. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Aagaard L, Schmid M, Warburton P, Jenuwein T: Mitotic phosphorylation of SUV39H1, a novel component of active centromeres, coincides with transient accumulation at mammalian centromeres. J Cell Sci. 2000 Mar;113 ( Pt 5):817-29. [PubMed Link Image]
  6. Rea S, Eisenhaber F, O'Carroll D, Strahl BD, Sun ZW, Schmid M, Opravil S, Mechtler K, Ponting CP, Allis CD, Jenuwein T: Regulation of chromatin structure by site-specific histone H3 methyltransferases. Nature. 2000 Aug 10;406(6796):593-9. [PubMed Link Image]
  7. Firestein R, Cui X, Huie P, Cleary ML: Set domain-dependent regulation of transcriptional silencing and growth control by SUV39H1, a mammalian ortholog of Drosophila Su(var)3-9. Mol Cell Biol. 2000 Jul;20(13):4900-9. [PubMed Link Image]
  8. Lachner M, O'Carroll D, Rea S, Mechtler K, Jenuwein T: Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature. 2001 Mar 1;410(6824):116-20. [PubMed Link Image]
  9. Nielsen SJ, Schneider R, Bauer UM, Bannister AJ, Morrison A, O'Carroll D, Firestein R, Cleary M, Jenuwein T, Herrera RE, Kouzarides T: Rb targets histone H3 methylation and HP1 to promoters. Nature. 2001 Aug 2;412(6846):561-5. [PubMed Link Image]
  10. Fujita N, Watanabe S, Ichimura T, Tsuruzoe S, Shinkai Y, Tachibana M, Chiba T, Nakao M: Methyl-CpG binding domain 1 (MBD1) interacts with the Suv39h1-HP1 heterochromatic complex for DNA methylation-based transcriptional repression. J Biol Chem. 2003 Jun 27;278(26):24132-8. Epub 2003 Apr 23. [PubMed Link Image]
  11. Sewalt RG, Lachner M, Vargas M, Hamer KM, den Blaauwen JL, Hendrix T, Melcher M, Schweizer D, Jenuwein T, Otte AP: Selective interactions between vertebrate polycomb homologs and the SUV39H1 histone lysine methyltransferase suggest that histone H3-K9 methylation contributes to chromosomal targeting of Polycomb group proteins. Mol Cell Biol. 2002 Aug;22(15):5539-53. [PubMed Link Image]
  12. Chakraborty S, Sinha KK, Senyuk V, Nucifora G: SUV39H1 interacts with AML1 and abrogates AML1 transactivity. AML1 is methylated in vivo. Oncogene. 2003 Aug 14;22(34):5229-37. [PubMed Link Image]
  13. Macaluso M, Cinti C, Russo G, Russo A, Giordano A: pRb2/p130-E2F4/5-HDAC1-SUV39H1-p300 and pRb2/p130-E2F4/5-HDAC1-SUV39H1-DNMT1 multimolecular complexes mediate the transcription of estrogen receptor-alpha in breast cancer. Oncogene. 2003 Jun 5;22(23):3511-7. [PubMed Link Image]
  14. Ait-Si-Ali S, Guasconi V, Fritsch L, Yahi H, Sekhri R, Naguibneva I, Robin P, Cabon F, Polesskaya A, Harel-Bellan A: A Suv39h-dependent mechanism for silencing S-phase genes in differentiating but not in cycling cells. EMBO J. 2004 Feb 11;23(3):605-15. Epub 2004 Feb 5. [PubMed Link Image]
  15. Frontelo P, Leader JE, Yoo N, Potocki AC, Crawford M, Kulik M, Lechleider RJ: Suv39h histone methyltransferases interact with Smads and cooperate in BMP-induced repression. Oncogene. 2004 Jul 1;23(30):5242-51. [PubMed Link Image]
  16. Krouwels IM, Wiesmeijer K, Abraham TE, Molenaar C, Verwoerd NP, Tanke HJ, Dirks RW: A glue for heterochromatin maintenance: stable SUV39H1 binding to heterochromatin is reinforced by the SET domain. J Cell Biol. 2005 Aug 15;170(4):537-49. [PubMed Link Image]
  17. Vassen L, Fiolka K, Moroy T: Gfi1b alters histone methylation at target gene promoters and sites of gamma-satellite containing heterochromatin. EMBO J. 2006 Jun 7;25(11):2409-19. Epub 2006 May 11. [PubMed Link Image]
  18. Bradley SP, Kaminski DA, Peters AH, Jenuwein T, Stavnezer J: The histone methyltransferase Suv39h1 increases class switch recombination specifically to IgA. J Immunol. 2006 Jul 15;177(2):1179-88. [PubMed Link Image]
  19. Chin HG, Patnaik D, Esteve PO, Jacobsen SE, Pradhan S: Catalytic properties and kinetic mechanism of human recombinant Lys-9 histone H3 methyltransferase SUV39H1: participation of the chromodomain in enzymatic catalysis. Biochemistry. 2006 Mar 14;45(10):3272-84. [PubMed Link Image]
  20. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  21. Mal AK: Histone methyltransferase Suv39h1 represses MyoD-stimulated myogenic differentiation. EMBO J. 2006 Jul 26;25(14):3323-34. Epub 2006 Jul 13. [PubMed Link Image]
  22. Carbone R, Botrugno OA, Ronzoni S, Insinga A, Di Croce L, Pelicci PG, Minucci S: Recruitment of the histone methyltransferase SUV39H1 and its role in the oncogenic properties of the leukemia-associated PML-retinoic acid receptor fusion protein. Mol Cell Biol. 2006 Feb;26(4):1288-96. [PubMed Link Image]
  23. Reed-Inderbitzin E, Moreno-Miralles I, Vanden-Eynden SK, Xie J, Lutterbach B, Durst-Goodwin KL, Luce KS, Irvin BJ, Cleary ML, Brandt SJ, Hiebert SW: RUNX1 associates with histone deacetylases and SUV39H1 to repress transcription. Oncogene. 2006 Sep 21;25(42):5777-86. Epub 2006 May 1. [PubMed Link Image]
  24. Kamoi K, Yamamoto K, Misawa A, Miyake A, Ishida T, Tanaka Y, Mochizuki M, Watanabe T: SUV39H1 interacts with HTLV-1 Tax and abrogates Tax transactivation of HTLV-1 LTR. Retrovirology. 2006 Jan 13;3:5. [PubMed Link Image]
  25. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
  26. Murayama A, Ohmori K, Fujimura A, Minami H, Yasuzawa-Tanaka K, Kuroda T, Oie S, Daitoku H, Okuwaki M, Nagata K, Fukamizu A, Kimura K, Shimizu T, Yanagisawa J: Epigenetic control of rDNA loci in response to intracellular energy status. Cell. 2008 May 16;133(4):627-39. [PubMed Link Image]
  27. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  28. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  29. Li Z, Chen L, Kabra N, Wang C, Fang J, Chen J: Inhibition of SUV39H1 methyltransferase activity by DBC1. J Biol Chem. 2009 Apr 17;284(16):10361-6. Epub 2009 Feb 13. [PubMed Link Image]
  30. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 5660
Enzyme 20 Name Nicotinamide N-methyltransferase
Enzyme 20 Synonyms Not Available
Enzyme 20 Gene Name NNMT
Enzyme 20 Protein Sequence >Nicotinamide N-methyltransferase
MESGFTSKDTYLSHFNPRDYLEKYYKFGSRHSAESQILKHLLKNLFKIFCLDGVKGDLLI
DIGSGPTIYQLLSACESFKEIVVTDYSDQNLQELEKWLKKEPEAFDWSPVVTYVCDLEGN
RVKGPEKEEKLRQAVKQVLKCDVTQSQPLGAVPLPPADCVLSTLCLDAACPDLPTYCRAL
RNLGSLLKPGGFLVIMDALKSSYYMIGEQKFSSLPLGREAVEAAVKEAGYTIEWFEVISQ
SYSSTMANNEGLFSLVARKLSRPL
Enzyme 20 Number of Residues 264
Enzyme 20 Molecular Weight 29573.7
Enzyme 20 Theoretical pI 5.45
Enzyme 20 GO Classification
Function
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
Component
Enzyme 20 General Function Involved in methyltransferase activity
Enzyme 20 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 20 Pathways
  • Nicotinate and Nicotinamide Metabolism (map00760 Link Image)
Enzyme 20 Reactions
  • S-adenosyl-L-methionine + nicotinamide = S-adenosyl-L-homocysteine + 1-methylnicotinamide [RN:R01269]
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 494989 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID P40261 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name NNMT_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >795 bp
ATGGAATCAGGCTTCACCTCCAAGGACACCTATCTAAGCCATTTTAACCCTCGGGATTAC
CTAGAAAAATATTACAAGTTTGGTTCTAGGCACTCTGCAGAAAGCCAGATTCTTAAGCAC
CTTCTGAAAAATCTTTTCAAGATATTCTGCCTAGACGGTGTGAAGGGAGACCTGCTGATT
GACATCGGCTCTGGCCCCACTATCTATCAGCTCCTCTCTGCTTGTGAATCCTTTAAGGAG
ATCGTCGTCACTGACTACTCAGACCAGAACCTGCAGGAGCTGGAGAAGTGGCTGAAGAAA
GAGCCAGAGGCCTTTGACTGGTCCCCAGTGGTGACCTATGTGTGTGATCTTGAAGGGAAC
AGAGTCAAGGGTCCAGAGAAGGAGGAGAAGTTGAGACAGGCGGTCAAGCAGGTGCTGAAG
TGTGATGTGACTCAGAGCCAGCCACTGGGGGCCGTCCCCTTACCCCCGGCTGACTGCGTG
CTCAGCACACTGTGTCTGGATGCCGCCTGCCCAGACCTCCCCACCTACTGCAGGGCGCTC
AGGAACCTCGGCAGCCTACTGAAGCCAGGGGGCTTCCTGGTGATCATGGATGCGCTCAAG
AGCAGCTACTACATGATTGGTGAGCAGAAGTTCTCCAGCCTCCCCCTGGGCCGGGAGGCA
GTAGAGGCTGCTGTGAAAGAGGCTGGCTACACAATCGAATGGTTTGAGGTGATCTCGCAA
AGTTATTCTTCCACCATGGCCAACAACGAAGGACTTTTCTCCCTGGTGGCGAGGAAGCTG
AGCAGACCCCTGTGA
Enzyme 20 GenBank Gene ID U08021 Link Image
Enzyme 20 GeneCard ID NNMT Link Image
Enzyme 20 GenAtlas ID NNMT Link Image
Enzyme 20 HGNC ID HGNC:7861 Link Image
Enzyme 20 Chromosome Location 1
Enzyme 20 Locus 11q23.1
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. 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]
  5. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 5661
Enzyme 21 Name Histone-lysine N-methyltransferase SUV39H2
Enzyme 21 Synonyms
  1. Histone H3-K9 methyltransferase 2
  2. H3-K9-HMTase 2
  3. Lysine N-methyltransferase 1B
  4. Suppressor of variegation 3-9 homolog 2
  5. Su(var)3-9 homolog 2
Enzyme 21 Gene Name SUV39H2
Enzyme 21 Protein Sequence >Histone-lysine N-methyltransferase SUV39H2
MAAVGAEARGAWCVPCLVSLDTLQELCRKEKLTCKSIGITKRNLNNYEVEYLCDYKVVKD
MEYYLVKWKGWPDSTNTWEPLQNLKCPLLLQQFSNDKHNYLSQVKKGKAITPKDNNKTLK
PAIAEYIVKKAKQRIALQRWQDELNRRKNHKGMIFVENTVDLEGPPSDFYYINEYKPAPG
ISLVNEATFGCSCTDCFFQKCCPAEAGVLLAYNKNQQIKIPPGTPIYECNSRCQCGPDCP
NRIVQKGTQYSLCIFRTSNGRGWGVKTLVKIKRMSFVMEYVGEVITSEEAERRGQFYDNK
GITYLFDLDYESDEFTVDAARYGNVSHFVNHSCDPNLQVFNVFIDNLDTRLPRIALFSTR
TINAGEELTFDYQMKGSGDISSDSIDHSPAKKRVRTVCKCGAVTCRGYLN
Enzyme 21 Number of Residues 410
Enzyme 21 Molecular Weight 46682.0
Enzyme 21 Theoretical pI 8.27
Enzyme 21 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • chromatin binding
  • histone-lysine N-methyltransferase activity
  • ion binding
  • metal 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
  • cellular component organization at cellular level
  • cellular process
  • chromatin assembly or disassembly
  • chromatin modification
  • chromatin organization
  • chromosome organization
  • organelle organization
Component
  • chromatin
  • chromosomal part
  • intracellular membrane-bounded organelle
  • intracellular organelle part
  • membrane-bounded organelle
  • nucleus
  • organelle
  • organelle part
Enzyme 21 General Function Involved in chromatin binding
Enzyme 21 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 21 Pathways
Enzyme 21 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • None
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 301171588 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q9H5I1 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name SUV92_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >1233 bp
ATGGCGGCGGTCGGGGCCGAGGCGCGAGGAGCTTGGTGTGTGCCTTGCCTAGTTTCACTT
GATACTCTTCAGGAATTATGTAGAAAAGAAAAGCTCACATGTAAATCGATTGGAATCACC
AAAAGGAATCTAAACAATTATGAGGTGGAATACTTGTGTGACTACAAGGTAGTAAAGGAT
ATGGAATATTATCTTGTAAAATGGAAAGGATGGCCAGATTCTACAAATACTTGGGAACCT
TTGCAAAATCTGAAGTGCCCGTTACTGCTTCAGCAATTCTCTAATGACAAGCATAATTAT
TTATCTCAGGTAAAGAAAGGCAAAGCAATAACTCCAAAAGACAATAACAAAACTTTGAAA
CCTGCCATTGCTGAGTACATTGTGAAGAAGGCTAAACAAAGGATAGCTCTGCAGAGATGG
CAAGATGAACTCAACAGAAGAAAGAATCATAAAGGAATGATATTTGTTGAAAATACTGTT
GATTTAGAGGGCCCACCTTCAGACTTCTATTACATTAACGAATACAAACCAGCTCCTGGA
ATCAGCTTAGTCAATGAAGCTACCTTTGGTTGTTCATGCACAGATTGCTTCTTTCAAAAA
TGTTGTCCTGCTGAAGCTGGAGTTCTTTTGGCTTATAATAAAAACCAACAAATTAAAATC
CCACCTGGTACTCCCATCTATGAATGCAACTCAAGGTGTCAGTGTGGTCCTGATTGTCCC
AATAGGATTGTACAAAAAGGCACACAGTATTCGCTTTGCATCTTTCGAACTAGCAATGGA
CGTGGCTGGGGTGTAAAGACCCTTGTGAAGATTAAAAGAATGAGTTTTGTCATGGAATAT
GTTGGAGAGGTAATCACAAGTGAAGAAGCTGAAAGACGAGGACAGTTCTATGACAACAAG
GGAATCACGTATCTCTTTGATCTGGACTATGAGTCTGATGAATTCACAGTGGATGCGGCT
CGATACGGCAATGTGTCTCATTTTGTGAATCACAGCTGTGACCCAAATCTTCAGGTGTTC
AATGTTTTCATTGATAACCTCGATACTCGTCTTCCCCGAATAGCATTGTTTTCCACAAGA
ACCATAAATGCTGGAGAAGAGCTGACTTTTGATTATCAAATGAAAGGTTCTGGAGATATA
TCTTCAGATTCTATTGACCACAGCCCAGCCAAAAAGAGGGTCAGAACAGTATGTAAATGT
GGAGCTGTGACTTGCAGAGGTTACCTCAACTGA
Enzyme 21 GenBank Gene ID NM_001193424.1 Link Image
Enzyme 21 GeneCard ID SUV39H2 Link Image
Enzyme 21 GenAtlas ID SUV39H2 Link Image
Enzyme 21 HGNC ID HGNC:17287 Link Image
Enzyme 21 Chromosome Location 1
Enzyme 21 Locus 10p13
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  5. Ait-Si-Ali S, Guasconi V, Fritsch L, Yahi H, Sekhri R, Naguibneva I, Robin P, Cabon F, Polesskaya A, Harel-Bellan A: A Suv39h-dependent mechanism for silencing S-phase genes in differentiating but not in cycling cells. EMBO J. 2004 Feb 11;23(3):605-15. Epub 2004 Feb 5. [PubMed Link Image]
  6. Frontelo P, Leader JE, Yoo N, Potocki AC, Crawford M, Kulik M, Lechleider RJ: Suv39h histone methyltransferases interact with Smads and cooperate in BMP-induced repression. Oncogene. 2004 Jul 1;23(30):5242-51. [PubMed Link Image]
  7. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  8. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  9. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 5663
Enzyme 22 Name Guanidinoacetate N-methyltransferase
Enzyme 22 Synonyms Not Available
Enzyme 22 Gene Name GAMT
Enzyme 22 Protein Sequence >Guanidinoacetate N-methyltransferase
MSAPSATPIFAPGENCSPAWGAAPAAYDAADTHLRILGKPVMERWETPYMHALAAAASSK
GGRVLEVGFGMAIAASKVQEAPIDEHWIIECNDGVFQRLRDWAPRQTHKVIPLKGLWEDV
APTLPDGHFDGILYDTYPLSEETWHTHQFNFIKNHAFRLLKPGGVLTYCNLTSWGELMKS
KYSDITIMFEETQVPALLEAGFRRENIRTEVMALVPPADCRYYAFPQMITPLVTKG
Enzyme 22 Number of Residues 236
Enzyme 22 Molecular Weight 26317.9
Enzyme 22 Theoretical pI 6.09
Enzyme 22 GO Classification Not Available
Enzyme 22 General Function Involved in guanidinoacetate N-methyltransferase activity
Enzyme 22 Specific Function S-adenosyl-L-methionine + guanidinoacetate = S-adenosyl-L-homocysteine + creatine
Enzyme 22 Pathways
  • Arginine and Proline Metabolism (map00330 Link Image)
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
Enzyme 22 Reactions
  • S-adenosyl-L-methionine + guanidinoacetate = S-adenosyl-L-homocysteine + creatine [RN:R01883]
Enzyme 22 Pfam Domain Function Not Available
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 3342733 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID Q14353 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name GAMT_HUMAN Link Image
Enzyme 22 PDB ID 1XCL Link Image
Enzyme 22 PDB File Show
Enzyme 22 3D Structure
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >711 bp
ATGAGCGCCCCCAGCGCGACCCCCATCTTCGCGCCCGGCGAGAACTGCAGCCCCGCGTGG
GGGGCGGCGCCCGCGGCCTACGACGCAGCGGACACGCACCTGCGCATCCTGGGCAAGCCG
GTGATGGAGCGCTGGGAGACCCCCTATATGCACGCGCTGGCCGCCGCCGCCTCCTCCAAA
GGGGGCCGGGTCCTGGAGGTGGGCTTTGGCATGGCCATCGCAGCGTCAAAGGTGCAGGAG
GCGCCCATTGATGAGCATTGGATCATCGAGTGCAATGACGGCGTCTTCCAGCGGCTCCGG
GACTGGGCCCCACGGCAGACACACAAGGTCATCCCCTTGAAAGGCCTGTGGGAGGATGTG
GCACCCACCCTGCCTGACGGTCACTTTGATGGGATCCTGTACGACACGTACCCACTCTCG
GAGGAGACCTGGCACACACACCAGTTCAACTTCATCAAGAACCACGCCTTTCGCCTGCTG
AAGCCGGGGGGCGTCCTCACCTACTGCAACCTCACCTCCTGGGGGGAGCTGATGAAGTCC
AAGTACTCAGACATCACCATCATGTTTGAGGAGACGCAGGTGCCCGCGCTGCTGGAGGCC
GGCTTCCGGAGGGAGAACATCCGTACGGAGGTGATGGCGCTGGTCCCACCGGCCGACTGC
CGCTACTACGCCTTCCCACAGATGATCACGCCCCTGGTGACCAAAGGCTGA
Enzyme 22 GenBank Gene ID AC005329 Link Image
Enzyme 22 GeneCard ID GAMT Link Image
Enzyme 22 GenAtlas ID GAMT Link Image
Enzyme 22 HGNC ID HGNC:4136 Link Image
Enzyme 22 Chromosome Location 1
Enzyme 22 Locus 19p13.3
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 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]
  3. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Stockler S, Isbrandt D, Hanefeld F, Schmidt B, von Figura K: Guanidinoacetate methyltransferase deficiency: the first inborn error of creatine metabolism in man. Am J Hum Genet. 1996 May;58(5):914-22. [PubMed Link Image]
  6. Wang Y, Du D, Fang L, Yang G, Zhang C, Zeng R, Ullrich A, Lottspeich F, Chen Z: Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling. EMBO J. 2006 Nov 1;25(21):5058-70. Epub 2006 Oct 19. [PubMed Link Image]
  7. Battini R, Leuzzi V, Carducci C, Tosetti M, Bianchi MC, Item CB, Stockler-Ipsiroglu S, Cioni G: Creatine depletion in a new case with AGAT deficiency: clinical and genetic study in a large pedigree. Mol Genet Metab. 2002 Dec;77(4):326-31. [PubMed Link Image]
  8. Item CB, Mercimek-Mahmutoglu S, Battini R, Edlinger-Horvat C, Stromberger C, Bodamer O, Muhl A, Vilaseca MA, Korall H, Stockler-Ipsiroglu S: Characterization of seven novel mutations in seven patients with GAMT deficiency. Hum Mutat. 2004 May;23(5):524. [PubMed Link Image]
  9. Caldeira Araujo H, Smit W, Verhoeven NM, Salomons GS, Silva S, Vasconcelos R, Tomas H, Tavares de Almeida I, Jakobs C, Duran M: Guanidinoacetate methyltransferase deficiency identified in adults and a child with mental retardation. Am J Med Genet A. 2005 Mar 1;133A(2):122-7. [PubMed Link Image]
  10. Leuzzi V, Carducci C, Carducci C, Matricardi M, Bianchi MC, Di Sabato ML, Artiola C, Antonozzi I: A mutation on exon 6 of guanidinoacetate methyltransferase (GAMT) gene supports a different function for isoform a and b of GAMT enzyme. Mol Genet Metab. 2006 Jan;87(1):88-90. Epub 2005 Nov 15. [PubMed Link Image]
  11. Lion-Francois L, Cheillan D, Pitelet G, Acquaviva-Bourdain C, Bussy G, Cotton F, Guibaud L, Gerard D, Rivier C, Vianey-Saban C, Jakobs C, Salomons GS, des Portes V: High frequency of creatine deficiency syndromes in patients with unexplained mental retardation. Neurology. 2006 Nov 14;67(9):1713-4. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 5665
Enzyme 23 Name Thiopurine S-methyltransferase
Enzyme 23 Synonyms
  1. Thiopurine methyltransferase
Enzyme 23 Gene Name TPMT
Enzyme 23 Protein Sequence >Thiopurine S-methyltransferase
MDGTRTSLDIEEYSDTEVQKNQVLTLEEWQDKWVNGKTAFHQEQGHQLLKKHLDTFLKGK
SGLRVFFPLCGKAVEMKWFADRGHSVVGVEISELGIQEFFTEQNLSYSEEPITEIPGTKV
FKSSSGNISLYCCSIFDLPRTNIGKFDMIWDRGALVAINPGDRKCYADTMFSLLGKKFQY
LLCVLSYDPTKHPGPPFYVPHAEIERLFGKICNIRCLEKVDAFEERHKSWGIDCLFEKLY
LLTEK
Enzyme 23 Number of Residues 245
Enzyme 23 Molecular Weight 28180.1
Enzyme 23 Theoretical pI 6.16
Enzyme 23 GO Classification
Function
  • S-methyltransferase activity
  • catalytic activity
  • methyltransferase activity
  • thiopurine S-methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 23 General Function Involved in thiopurine S-methyltransferase activity
Enzyme 23 Specific Function Catalyzes the S-methylation of thiopurine drugs such as 6-mercaptopurine
Enzyme 23 Pathways Not Available
Enzyme 23 Reactions
  • S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether [RN:R03701]
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • None
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein Not Available
Enzyme 23 UniProtKB/Swiss-Prot ID P51580 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name TPMT_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >738 bp
ATGGATGGTACAAGAACTTCACTTGACATTGAAGAGTACTCGGATACTGAGGTACAGAAA
AACCAAGTACTAACTCTGGAAGAATGGCAAGACAAGTGGGTGAACGGCAAGACTGCTTTT
CATCAGGAACAAGGACATCAGCTATTAAAGAAGCATTTAGATACTTTCCTTAAAGGCAAG
AGTGGACTGAGGGTATTTTTTCCTCTTTGCGGAAAAGCGGTTGAGATGAAATGGTTTGCA
GACCGGGGACACAGTGTAGTTGGTGTGGAAATCAGTGAACTTGGGATACAAGAATTTTTT
ACAGAGCAGAATCTTTCTTACTCAGAAGAACCAATCACCGAAATTCCTGGAACCAAAGTA
TTTAAGAGTTCTTCGGGGAACATTTCATTGTACTGTTGCAGTATTTTTGATCTTCCCAGG
ACAAATATTGGCAAATTTGACATGATTTGGGATAGAGGAGCATTAGTTGCCATTAATCCA
GGTGATCGCAAATGCTATGCAGATACAATGTTTTCCCTCCTGGGAAAGAAGTTTCAGTAT
CTCCTGTGTGTTCTTTCTTATGATCCAACTAAACATCCAGGTCCACCATTTTATGTTCCA
CATGCTGAAATTGAAAGGTTGTTTGGTAAAATATGCAATATACGTTGTCTTGAGAAGGTT
GATGCTTTTGAAGAACGACATAAAAGTTGGGGAATTGACTGTCTTTTTGAAAAGTTATAT
CTACTTACAGAAAAGTAA
Enzyme 23 GenBank Gene ID S62904 Link Image
Enzyme 23 GeneCard ID TPMT Link Image
Enzyme 23 GenAtlas ID TPMT Link Image
Enzyme 23 HGNC ID HGNC:12014 Link Image
Enzyme 23 Chromosome Location 6
Enzyme 23 Locus 6p22.3
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  8. 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]
  9. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  10. Han G, Ye M, Zhou H, Jiang X, Feng S, Jiang X, Tian R, Wan D, Zou H, Gu J: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. Proteomics. 2008 Apr;8(7):1346-61. [PubMed Link Image]
  11. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  12. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  13. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  14. 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]
  15. 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]
  16. Leipold G, Schutz E, Haas JP, Oellerich M: Azathioprine-induced severe pancytopenia due to a homozygous two-point mutation of the thiopurine methyltransferase gene in a patient with juvenile HLA-B27-associated spondylarthritis. Arthritis Rheum. 1997 Oct;40(10):1896-8. [PubMed Link Image]
  17. Tai HL, Krynetski EY, Schuetz EG, Yanishevski Y, Evans WE: Enhanced proteolysis of thiopurine S-methyltransferase (TPMT) encoded by mutant alleles in humans (TPMT*3A, TPMT*2): mechanisms for the genetic polymorphism of TPMT activity. Proc Natl Acad Sci U S A. 1997 Jun 10;94(12):6444-9. [PubMed Link Image]
  18. Ameyaw MM, Collie-Duguid ES, Powrie RH, Ofori-Adjei D, McLeod HL: Thiopurine methyltransferase alleles in British and Ghanaian populations. Hum Mol Genet. 1999 Feb;8(2):367-70. [PubMed Link Image]
  19. 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]
  20. Collie-Duguid ES, Pritchard SC, Powrie RH, Sludden J, Collier DA, Li T, McLeod HL: The frequency and distribution of thiopurine methyltransferase alleles in Caucasian and Asian populations. Pharmacogenetics. 1999 Feb;9(1):37-42. [PubMed Link Image]
  21. Hiratsuka M, Inoue T, Omori F, Agatsuma Y, Mizugaki M: Genetic analysis of thiopurine methyltransferase polymorphism in a Japanese population. Mutat Res. 2000 Mar 14;448(1):91-5. [PubMed Link Image]
  22. Kurzawski M, Dziewanowski K, Ciechanowski K, Drozdzik M: Severe azathioprine-induced myelotoxicity in a kidney transplant patient with thiopurine S-methyltransferase-deficient genotype (TPMT*3A/*3C). Transpl Int. 2005 May;18(5):623-5. [PubMed Link Image]
  23. Lu HF, Shih MC, Chang YS, Chang JY, Ko YC, Chang SJ, Chang JG: Molecular analysis of thiopurine S-methyltransferase alleles in Taiwan aborigines and Taiwanese. J Clin Pharm Ther. 2006 Feb;31(1):93-8. [PubMed Link Image]
  24. Rossino R, Vincis C, Alves S, Prata MJ, Macis MD, Nucaro AL, Schirru E, Congia M: Frequency of the thiopurine S-methyltransferase alleles in the ancient genetic population isolate of Sardinia. J Clin Pharm Ther. 2006 Jun;31(3):283-7. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 5666
Enzyme 24 Name N6-adenosine-methyltransferase 70 kDa subunit
Enzyme 24 Synonyms
  1. MT-A70
  2. Methyltransferase-like protein 3
Enzyme 24 Gene Name METTL3
Enzyme 24 Protein Sequence >N6-adenosine-methyltransferase 70 kDa subunit
MSDTWSSIQAHKKQLDSLRERLQRRRKQDSGHLDLRNPEAALSPTFRSDSPVPTAPTSGG
PKPSTASAVPELATDPELEKKLLHHLSDLALTLPTDAVSICLAISTPDAPATQDGVESLL
QKFAAQELIEVKRGLLQDDAHPTLVTYADHSKLSAMMGAVAEKKGPGEVAGTVTGQKRRA
EQDSTTVAAFASSLVSGLNSSASEPAKEPAKKSRKHAASDVDLEIESLLNQQSTKEQQSK
KVSQEILELLNTTTAKEQSIVEKFRSRGRAQVQEFCDYGTKEECMKASDADRPCRKLHFR
RIINKHTDESLGDCSFLNTCFHMDTCKYVHYEIDACMDSEAPGSKDHTPSQELALTQSVG
GDSSADRLFPPQWICCDIRYLDVSILGKFAVVMADPPWDIHMELPYGTLTDDEMRRLNIP
VLQDDGFLFLWVTGRAMELGRECLNLWGYERVDEIIWVKTNQLQRIIRTGRTGHWLNHGK
EHCLVGVKGNPQGFNQGLDCDVIVAEVRSTSHKPDEIYGMIERLSPGTRKIELFGRPHNV
QPNWITLGNQLDGIHLLDPDVVARFKQRYPDGIISKPKNL
Enzyme 24 Number of Residues 580
Enzyme 24 Molecular Weight 64473.3
Enzyme 24 Theoretical pI 6.38
Enzyme 24 GO Classification
Function
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
Component
Enzyme 24 General Function Involved in methyltransferase activity
Enzyme 24 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 24 Pathways Not Available
Enzyme 24 Reactions
  • S-adenosyl-L-methionine + m7G(5')pppAm = S-adenosyl-L-homocysteine + m7G(5')pppm6Am (mRNA containing an N6,2'-O-dimethyladenosine cap) [RN:R03788]
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 21361827 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID Q86U44 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name MTA70_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >1743 bp
ATGTCGGACACGTGGAGCTCTATCCAGGCCCACAAGAAGCAGCTGGACTCTCTGCGGGAG
AGGCTGCAGCGGAGGCGGAAGCAGGACTCGGGGCACTTGGATCTACGGAATCCAGAGGCA
GCATTGTCTCCAACCTTCCGTAGTGACAGCCCAGTGCCTACTGCACCCACCTCTGGTGGC
CCTAAGCCCAGCACAGCTTCAGCAGTTCCTGAATTAGCTACAGATCCTGAGTTAGAGAAG
AAGTTGCTACACCACCTCTCTGATCTGGCCTTAACATTGCCCACTGATGCTGTGTCCATC
TGTCTTGCCATCTCCACGCCAGATGCTCCTGCCACTCAAGATGGGGTAGAAAGCCTCCTG
CAGAAGTTTGCAGCTCAGGAGTTGATTGAGGTAAAGCGAGGTCTCCTACAAGATGATGCA
CATCCTACTCTTGTAACCTATGCTGACCATTCCAAGCTCTCTGCCATGATGGGTGCTGTG
GCAGAAAAGAAGGGCCCTGGGGAGGTAGCAGGGACTGTCACAGGGCAGAAGCGGCGTGCA
GAACAGGACTCGACTACAGTAGCTGCCTTTGCCAGTTCGTTAGTCTCTGGTCTGAACTCT
TCAGCATCGGAACCAGCAAAGGAGCCAGCCAAGAAATCAAGGAAACATGCTGCCTCAGAT
GTTGATCTGGAGATAGAGAGCCTTCTGAACCAACAGTCCACTAAGGAACAACAGAGCAAG
AAGGTCAGTCAGGAGATCCTAGAGCTATTAAATACTACAACAGCCAAGGAACAATCCATT
GTTGAAAAATTTCGCTCTCGAGGTCGGGCCCAAGTGCAAGAATTCTGTGACTATGGAACC
AAGGAGGAGTGCATGAAAGCCAGTGATGCTGATCGACCCTGTCGCAAGCTGCACTTCAGA
CGAATTATCAATAAACACACTGATGAGTCTTTAGGTGACTGCTCTTTCCTTAATACATGT
TTCCACATGGATACCTGCAAGTATGTTCACTATGAAATTGATGCTTGCATGGATTCTGAG
GCCCCTGGCAGCAAAGACCACACGCCAAGCCAGGAGCTTGCTCTTACACAGAGTGTCGGA
GGTGATTCCAGTGCAGACCGACTCTTCCCACCTCAGTGGATCTGTTGTGATATCCGCTAC
CTGGACGTCAGTATCTTGGGCAAGTTTGCAGTTGTGATGGCTGACCCACCCTGGGATATT
CACATGGAACTGCCCTATGGGACCCTGACAGATGATGAGATGCGCAGGCTCAACATACCC
GTACTACAGGATGATGGCTTTCTCTTCCTCTGGGTCACAGGCAGGGCCATGGAGTTGGGG
AGAGAATGTCTAAATCTCTGGGGGTATGAACGGGTAGATGAAATTATTTGGGTGAAGACA
AATCAACTGCAACGCATCATTCGGACAGGCCGTACAGGTCACTGGTTGAACCATGGGAAG
GAACACTGCTTGGTTGGTGTCAAAGGAAATCCCCAAGGCTTCAACCAGGGTCTGGATTGT
GATGTGATCGTAGCTGAGGTTCGTTCCACCAGTCATAAACCAGATGAAATCTATGGCATG
ATTGAAAGACTATCTCCTGGCACTCGCAAGATTGAGTTATTTGGACGACCACACAATGTG
CAACCCAACTGGATCACCCTTGGAAACCAACTGGATGGGATCCACCTACTAGACCCAGAT
GTGGTTGCACGGTTCAAGCAAAGGTACCCAGATGGTATCATCTCTAAACCTAAGAATTTA
TAG
Enzyme 24 GenBank Gene ID NM_019852.3 Link Image
Enzyme 24 GeneCard ID METTL3 Link Image
Enzyme 24 GenAtlas ID METTL3 Link Image
Enzyme 24 HGNC ID HGNC:17563 Link Image
Enzyme 24 Chromosome Location 1
Enzyme 24 Locus 14q11.1
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 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]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  5. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  6. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  7. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  8. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 5933
Enzyme 25 Name Putative adenosylhomocysteinase 3
Enzyme 25 Synonyms
  1. AdoHcyase 3
  2. S-adenosyl-L-homocysteine hydrolase 3
  3. S-adenosylhomocysteine hydrolase-like protein 2
Enzyme 25 Gene Name AHCYL2
Enzyme 25 Protein Sequence >Putative adenosylhomocysteinase 3
MSVQVVSAAAAAKVPEVELKDLSPSEAESQLGLSTAAVGAMAPPAGGGDPEAPAPAAERP
PVPGPGSGPAAALSPAAGKVPQASAMKRSDPHHQHQRHRDGGEALVSPDGTVTEAPRTVK
KQIQFADQKQEFNKRPTKIGRRSLSRSISQSSTDSYSSAASYTDSSDDETSPRDKQQKNS
KGSSDFCVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTA
VLMETLGALGAQCRWAACNIYSTLNEVAAALAESGFPVFAWKGESEDDFWWCIDRCVNVE
GWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVN
DSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYV
TEIDPICALQACMDGFRLVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGH
SNTEIDVASLRTPELTWERVRSQVDHVIWPDGKRIVLLAEGRLLNLSCSTVPTFVLSITA
TTQALALIELYNAPEGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQAKYLGLNK
NGPFKPNYYRY
Enzyme 25 Number of Residues 611
Enzyme 25 Molecular Weight 66720.6
Enzyme 25 Theoretical pI 7.39
Enzyme 25 GO Classification
Function
  • adenosylhomocysteinase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ether bonds
  • trialkylsulfonium hydrolase activity
Process
  • cellular metabolic process
  • metabolic process
  • one-carbon metabolic process
Component
Enzyme 25 General Function Involved in adenosylhomocysteinase activity
Enzyme 25 Specific Function S-adenosyl-L-homocysteine + H(2)O = L- homocysteine + adenosine
Enzyme 25 Pathways
Enzyme 25 Reactions
  • S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine [RN:R00192]
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 24308043 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID Q96HN2 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name SAHH3_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >1836 bp
ATGTCGGTGCAGGTTGTGTCAGCCGCGGCTGCCGCCAAGGTGCCTGAGGTGGAGCTGAAG
GACCTGAGCCCCTCCGAGGCGGAGTCGCAACTAGGACTGAGCACGGCCGCCGTGGGCGCC
ATGGCCCCCCCGGCGGGCGGTGGAGACCCTGAGGCTCCAGCTCCCGCCGCGGAGCGGCCC
CCGGTCCCCGGCCCGGGCTCGGGGCCCGCCGCCGCTCTCAGCCCCGCCGCCGGGAAGGTG
CCTCAGGCGTCGGCCATGAAGCGGAGCGACCCACATCACCAGCACCAGCGGCACCGCGAC
GGCGGCGAGGCCCTGGTCAGCCCCGACGGCACCGTCACCGAGGCGCCGCGCACAGTCAAG
AAGCAGATCCAGTTTGCTGACCAGAAGCAAGAATTCAACAAACGTCCCACCAAAATTGGA
CGTCGCTCTTTGTCTCGTTCCATTTCTCAGTCATCTACTGACAGCTACAGCTCAGCGGCT
TCATATACAGATAGCTCTGATGATGAGACATCGCCCAGGGACAAGCAGCAAAAGAACTCT
AAGGGAAGCAGTGACTTCTGTGTTAAGAACATCAAACAGGCAGAGTTTGGACGAAGAGAA
ATTGAAATTGCTGAACAAGAAATGCCTGCATTGATGGCTTTGAGGAAGAGAGCTCAAGGA
GAAAAGCCTTTGGCTGGAGCCAAAATCGTGGGTTGCACACACATCACTGCTCAGACTGCT
GTGCTTATGGAAACTCTGGGTGCTCTGGGGGCCCAGTGCCGATGGGCTGCCTGCAACATC
TATTCCACTCTCAATGAAGTGGCTGCTGCTCTAGCAGAAAGTGGATTTCCTGTTTTTGCC
TGGAAGGGAGAGTCAGAAGATGACTTTTGGTGGTGTATCGATAGATGTGTGAATGTGGAG
GGCTGGCAGCCAAACATGATCTTGGATGATGGAGGGGATCTTACCCACTGGATTTATAAA
AAGTATCCCAACATGTTTAAGAAAATCAAGGGCATAGTAGAGGAGAGTGTTACTGGAGTT
CACAGGCTGTACCAACTGTCCAAAGCTGGGAAGCTGTGTGTTCCAGCCATGAATGTCAAT
GACTCAGTCACCAAACAGAAATTTGACAACCTCTACTGTTGCCGTGAATCAATTCTTGAT
GGACTTAAAAGGACAACAGACATGATGTTTGGTGGAAAGCAAGTGGTAGTCTGTGGCTAT
GGAGAGGTGGGGAAAGGGTGCTGTGCTGCCCTGAAAGCCATGGGCTCCATTGTGTATGTA
ACTGAAATTGACCCCATCTGTGCCCTGCAAGCCTGTATGGATGGATTTCGACTGGTGAAA
TTAAATGAGGTCATCCGACAAGTGGACATTGTTATTACCTGTACAGGTAACAAGAATGTG
GTAACCAGAGAGCACTTGGACCGTATGAAGAATAGCTGCATCGTTTGTAACATGGGACAT
TCCAACACAGAGATTGACGTGGCGAGTCTGCGGACACCAGAACTGACCTGGGAGCGAGTG
AGATCTCAAGTTGACCATGTGATATGGCCTGATGGCAAGAGGATAGTACTGCTGGCAGAG
GGCCGCCTGCTGAACCTTAGCTGCTCCACAGTGCCTACATTTGTGCTCTCAATCACTGCT
ACTACTCAGGCTCTTGCCTTGATAGAGCTTTACAATGCTCCTGAGGGTCGCTATAAGCAG
GATGTCTACCTGTTGCCCAAGAAGATGGATGAGTATGTGGCCAGCCTACACCTGCCTACC
TTTGATGCCCACTTGACAGAGCTGACAGATGAACAGGCCAAGTATCTGGGACTCAACAAG
AATGGGCCCTTCAAGCCTAATTACTACAGGTATTAA
Enzyme 25 GenBank Gene ID NM_015328.3 Link Image
Enzyme 25 GeneCard ID AHCYL2 Link Image
Enzyme 25 GenAtlas ID AHCYL2 Link Image
Enzyme 25 HGNC ID HGNC:22204 Link Image
Enzyme 25 Chromosome Location 7
Enzyme 25 Locus 7q32.1
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 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]
  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]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 5934
Enzyme 26 Name Adenosylhomocysteinase
Enzyme 26 Synonyms
  1. AdoHcyase
  2. S-adenosyl-L-homocysteine hydrolase
Enzyme 26 Gene Name AHCY
Enzyme 26 Protein Sequence >Adenosylhomocysteinase
MSDKLPYKVADIGLAAWGRKALDIAENEMPGLMRMRERYSASKPLKGARIAGCLHMTVET
AVLIETLVTLGAEVQWSSCNIFSTQDHAAAAIAKAGIPVYAWKGETDEEYLWCIEQTLYF
KDGPLNMILDDGGDLTNLIHTKYPQLLPGIRGISEETTTGVHNLYKMMANGILKVPAINV
NDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVI
ITEIDPINALQAAMEGYEVTTMDEACQEGNIFVTTTGCIDIILGRHFEQMKDDAIVCNIG
HFDVEIDVKWLNENAVEKVNIKPQVDRYRLKNGRRIILLAEGRLVNLGCAMGHPSFVMSN
SFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVAEAHLGKLNVKLTKLTEKQAQYLGMS
CDGPFKPDHYRY
Enzyme 26 Number of Residues 432
Enzyme 26 Molecular Weight 47715.7
Enzyme 26 Theoretical pI 6.29
Enzyme 26 GO Classification
Function
  • adenosylhomocysteinase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ether bonds
  • trialkylsulfonium hydrolase activity
Process
  • cellular metabolic process
  • metabolic process
  • one-carbon metabolic process
Component
Enzyme 26 General Function Involved in adenosylhomocysteinase activity
Enzyme 26 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 26 Pathways
Enzyme 26 Reactions
  • S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine [RN:R00192]
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 178277 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID P23526 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name SAHH_HUMAN Link Image
Enzyme 26 PDB ID 1LI4 Link Image
Enzyme 26 PDB File Show
Enzyme 26 3D Structure
Enzyme 26 Cellular Location Not Available
Enzyme 26 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 26 GenBank Gene ID M61831 Link Image
Enzyme 26 GeneCard ID AHCY Link Image
Enzyme 26 GenAtlas ID AHCY Link Image
Enzyme 26 HGNC ID HGNC:343 Link Image
Enzyme 26 Chromosome Location 2
Enzyme 26 Locus 20cen-q13.1
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 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. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Gupta RA, Yuan CS, Ault-Riche DB, Borchardt RT: Limited proteolysis of S-adenosylhomocysteine hydrolase: implications for the three-dimensional structure. Arch Biochem Biophys. 1995 Jun 1;319(2):365-71. [PubMed Link Image]
  6. Arredondo-Vega FX, Charlton JA, Edwards YH, Hopkinson DA, Whitehouse DB: Isozyme and DNA analysis of human S-adenosyl-L-homocysteine hydrolase (AHCY). Ann Hum Genet. 1989 May;53(Pt 2):157-67. [PubMed Link Image]
  7. Yuan CS, Borchardt RT: Photoaffinity labeling of human placental S-adenosylhomocysteine hydrolase with [2-3H]8-azido-adenosine. J Biol Chem. 1995 Jul 7;270(27):16140-6. [PubMed Link Image]
  8. Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J Proteome Res. 2006 Nov;5(11):3135-44. [PubMed Link Image]
  9. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  10. 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]
  11. Yang X, Hu Y, Yin DH, Turner MA, Wang M, Borchardt RT, Howell PL, Kuczera K, Schowen RL: Catalytic strategy of S-adenosyl-L-homocysteine hydrolase: transition-state stabilization and the avoidance of abortive reactions. Biochemistry. 2003 Feb 25;42(7):1900-9. [PubMed Link Image]
  12. Gellekink H, den Heijer M, Kluijtmans LA, Blom HJ: Effect of genetic variation in the human S-adenosylhomocysteine hydrolase gene on total homocysteine concentrations and risk of recurrent venous thrombosis. Eur J Hum Genet. 2004 Nov;12(11):942-8. [PubMed Link Image]
  13. Baric I, Fumic K, Glenn B, Cuk M, Schulze A, Finkelstein JD, James SJ, Mejaski-Bosnjak V, Pazanin L, Pogribny IP, Rados M, Sarnavka V, Scukanec-Spoljar M, Allen RH, Stabler S, Uzelac L, Vugrek O, Wagner C, Zeisel S, Mudd SH: S-adenosylhomocysteine hydrolase deficiency in a human: a genetic disorder of methionine metabolism. Proc Natl Acad Sci U S A. 2004 Mar 23;101(12):4234-9. Epub 2004 Mar 15. [PubMed Link Image]
  14. Buist NR, Glenn B, Vugrek O, Wagner C, Stabler S, Allen RH, Pogribny I, Schulze A, Zeisel SH, Baric I, Mudd SH: S-Adenosylhomocysteine hydrolase deficiency in a 26-year-old man. J Inherit Metab Dis. 2006 Aug;29(4):538-545. Epub 2006 May 30. [PubMed Link Image]
  15. Vugrek O, Beluzic R, Nakic N, Mudd SH: S-adenosylhomocysteine hydrolase (AHCY) deficiency: two novel mutations with lethal outcome. Hum Mutat. 2009 Apr;30(4):E555-65. [PubMed Link Image]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 5935
Enzyme 27 Name Putative adenosylhomocysteinase 2
Enzyme 27 Synonyms
  1. AdoHcyase 2
  2. DC-expressed AHCY-like molecule
  3. S-adenosyl-L-homocysteine hydrolase 2
  4. S-adenosylhomocysteine hydrolase-like protein 1
Enzyme 27 Gene Name AHCYL1
Enzyme 27 Protein Sequence >Putative adenosylhomocysteinase 2
MSMPDAMPLPGVGEELKQAKEIEDAEKYSFMATVTKAPKKQIQFADDMQEFTKFPTKTGR
RSLSRSISQSSTDSYSSAASYTDSSDDEVSPREKQQTNSKGSSNFCVKNIKQAEFGRREI
EIAEQDMSALISLRKRAQGEKPLAGAKIVGCTHITAQTAVLIETLCALGAQCRWSACNIY
STQNEVAAALAEAGVAVFAWKGESEDDFWWCIDRCVNMDGWQANMILDDGGDLTHWVYKK
YPNVFKKIRGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDG
LKRTTDVMFGGKQVVVCGYGEVGKGCCAALKALGAIVYITEIDPICALQACMDGFRVVKL
NEVIRQVDVVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVTSLRTPELTWERVR
SQVDHVIWPDGKRVVLLAEGRLLNLSCSTVPTFVLSITATTQALALIELYNAPEGRYKQD
VYLLPKKMDEYVASLHLPSFDAHLTELTDDQAKYLGLNKNGPFKPNYYRY
Enzyme 27 Number of Residues 530
Enzyme 27 Molecular Weight 58950.9
Enzyme 27 Theoretical pI 6.87
Enzyme 27 GO Classification
Function
  • adenosylhomocysteinase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ether bonds
  • trialkylsulfonium hydrolase activity
Process
  • cellular metabolic process
  • metabolic process
  • one-carbon metabolic process
Component
Enzyme 27 General Function Involved in adenosylhomocysteinase activity
Enzyme 27 Specific Function S-adenosyl-L-homocysteine + H(2)O = L- homocysteine + adenosine
Enzyme 27 Pathways
Enzyme 27 Reactions
  • S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine [RN:R00192]
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 16588687 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID O43865 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name SAHH2_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 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 27 GenBank Gene ID AF315687 Link Image
Enzyme 27 GeneCard ID AHCYL1 Link Image
Enzyme 27 GenAtlas ID AHCYL1 Link Image
Enzyme 27 HGNC ID HGNC:344 Link Image
Enzyme 27 Chromosome Location 1
Enzyme 27 Locus 1p13.2
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 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]
  2. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Imabayashi H, Mori T, Gojo S, Kiyono T, Sugiyama T, Irie R, Isogai T, Hata J, Toyama Y, Umezawa A: Redifferentiation of dedifferentiated chondrocytes and chondrogenesis of human bone marrow stromal cells via chondrosphere formation with expression profiling by large-scale cDNA analysis. Exp Cell Res. 2003 Aug 1;288(1):35-50. [PubMed Link Image]
  6. Pawlak A, Toussaint C, Levy I, Bulle F, Poyard M, Barouki R, Guellaen G: Characterization of a large population of mRNAs from human testis. Genomics. 1995 Mar 1;26(1):151-8. [PubMed Link Image]
  7. Zhang Y, Wolf-Yadlin A, Ross PL, Pappin DJ, Rush J, Lauffenburger DA, White FM: Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. Mol Cell Proteomics. 2005 Sep;4(9):1240-50. Epub 2005 Jun 11. [PubMed Link Image]
  8. Cooper BJ, Key B, Carter A, Angel NZ, Hart DN, Kato M: Suppression and overexpression of adenosylhomocysteine hydrolase-like protein 1 (AHCYL1) influences zebrafish embryo development: a possible role for AHCYL1 in inositol phospholipid signaling. J Biol Chem. 2006 Aug 11;281(32):22471-84. Epub 2006 Jun 5. [PubMed Link Image]
  9. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 7083
Enzyme 28 Name Histone-lysine N-methyltransferase SETD1A
Enzyme 28 Synonyms
  1. Lysine N-methyltransferase 2F
  2. SET domain-containing protein 1A
  3. hSET1A
  4. Set1/Ash2 histone methyltransferase complex subunit SET1
Enzyme 28 Gene Name SETD1A
Enzyme 28 Protein Sequence >Histone-lysine N-methyltransferase SETD1A
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 28 Number of Residues 1707
Enzyme 28 Molecular Weight 186032.2
Enzyme 28 Theoretical pI 4.79
Enzyme 28 GO Classification
Function
  • binding
  • nucleic acid binding
  • nucleotide binding
Process
Component
Enzyme 28 General Function Involved in nucleotide binding
Enzyme 28 Specific Function Histone methyltransferase that specifically methylates 'Lys-4' of histone H3, when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys- 9' residue is already methylated. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. The non-overalpping localization with SETD1B suggests that SETD1A and SETD1B make non-redundant contributions to the epigenetic control of chromatin structure and gene expression
Enzyme 28 Pathways
Enzyme 28 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 55741677 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID O15047 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name SET1A_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >5124 bp
ATGGATCAGGAAGGTGGGGGAGATGGGCAGAAGGCCCCGAGCTTCCAGTGGCGGAACTAC
AAGCTCATCGTGGATCCTGCCTTGGACCCTGCCCTGCGCAGGCCTTCTCAGAAGGTGTAC
CGCTATGATGGAGTCCACTTCAGTGTCAACGACTCAAAGTATATACCAGTCGAAGACCTC
CAAGACCCCCGTTGCCATGTCAGGTCCAAAAACAGAGACTTTTCCCTCCCAGTCCCTAAG
TTTAAGCTGGACGAGTTCTATATTGGACAGATTCCACTGAAGGAAGTGACTTTTGCAAGG
CTGAATGACAACGTGCGGGAGACCTTCCTGAAGGATATGTGCCGTAAGTACGGTGAGGTG
GAAGAGGTAGAGATCCTCCTTCACCCCCGTACGCGCAAGCACCTGGGCCTGGCCCGTGTG
CTCTTCACCAGCACTCGGGGCGCCAAGGAAACGGTCAAAAACCTCCACCTTACCTCCGTC
ATGGGCAACATCATCCATGCCCAGCTTGACATCAAAGGACAACAACGAATGAAATACTAT
GAACTAATTGTCAATGGCTCCTACACCCCTCAGACTGTGCCCACTGGGGGCAAGGCCCTG
AGTGAGAAGTTCCAAGGCTCGGGTGCAGCCACTGAGACGGCCGAATCCCGCCGCCGCTCT
TCCTCTGACACAGCTGCCTACCCAGCAGGCACCACTGCGGTGGGCACTCCTGGCAACGGC
ACCCCCTGCTCCCAGGACACAAGCTTCTCCAGCAGCCGACAAGATACCCCATCTTCCTTT
GGCCAGTTCACACCTCAGTCCTCCCAAGGAACCCCCTACACGTCTCGGGGCAGCACCCCC
TACTCTCAGGACTCTGCCTACTCCAGCAGCACCACTTCAACCTCCTTCAAGCCCCGGCGG
TCAGAGAACAGCTACCAAGATGCCTTTTCCCGCCGCCACTTCTCTGCATCTTCAGCCTCC
ACAACCGCCTCCACGGCCATCGCCGCCACCACTGCAGCCACTGCCTCATCCTCCGCCTCT
TCCTCCTCATTGTCCTCGTCCTCCTCGTCATCCTCTTCCTCCTCGTCCTCTCAGTTTCGT
AGTTCTGATGCAAACTACCCAGCGTATTATGAAAGCTGGAATCGCTACCAGCGCCATACT
TCCTACCCACCACGCCGGGCCACACGGGAGGAACCCCCTGGAGCCCCTTTTGCTGAAAAT
ACAGCTGAGCGCTTCCCACCTTCTTACACCTCCTACCTGCCCCCCGAGCCCAGCCGGCCC
ACCGACCAGGACTACCGGCCTCCTGCCTCAGAGGCTCCACCCCCGGAGCCTCCAGAACCT
GGTGGAGGCGGGGGTGGAGGAGGGCCCAGCCCTGAGAGAGAAGAAGTTCGGACTTCCCCC
CGCCCAGCCTCCCCTGCCCGCTCTGGCTCCCCAGCCCCGGAGACCACCAATGAGAGTGTG
CCCTTCGCCCAGCACAGCAGCCTGGATTCCCGCATCGAGATGCTGCTGAAGGAGCAGCGC
TCCAAGTTTTCCTTCTTGGCCTCTGACACAGAGGAGGAGGAAGAGAACAGCAGCATGGTC
CTTGGGGCCAGAGATACAGGGAGTGAGGTGCCTTCTGGGTCAGGGCATGGGCCCTGCACA
CCCCCTCCGGCCCCAGCTAATTTTGAGGATGTGGCACCTACAGGGAGCGGGGAGCCAGGG
GCTACCCGGGAGTCTCCCAAGGCAAATGGACAGAACCAGGCTTCTCCATGCTCTTCTGGA
GACGACATGGAGATCTCCGACGACGACCGGGGTGGCTCACCCCCTCCGGCCCCGACGCCC
CCTCAGCAGCCTCCGCCACCTCCCCCTCCCCCGCCGCCTCCTCCTCCCTACCTGGCGTCC
CTTCCTCTTGGTTATCCTCCCCACCAACCTGCCTACCTCCTCCCACCCAGACCTGATGGG
CCGCCGCCCCCTGAGTACCCCCCACCTCCTCCACCACCCCCGCACATCTATGACTTTGTG
AACTCCTTGGAGCTCATGGACCGACTTGGGGCTCAGTGGGGAGGGATGCCCATGTCCTTC
CAGATGCAGACCCAGATGTTAACTCGGCTCCATCAGCTGCGGCAGGGCAAGGGATTGATT
GCCGCCTCAGCTGGCCCCCCCGGTGGGGCCTTTGGGGAGGCCTTCCTCCCGTTTCCACCC
CCGCAGGAGGCAGCCTACGGCTTGCCGTATGCTCTATATGCACAGGGGCAGGAGGGCAGA
GGGGCATACTCACGGGAGGCCTACCACCTGCCCATGCCAATGGCAGCCGAGCCCCTGCCC
TCCTCCTCAGTCTCGGGAGAGGAGGCCCGGCTGCCACCCAGGGAAGAAGCAGAGCTGGCA
GAGGGCAAGACCCTCCCGACAGCAGGCACCGTGGGCCGTGTGCTCGCCATGCTGGTCCAG
GAGATGAAGAGCATCATGCAGCGAGACCTCAACCGCAAGATGGTGGAGAACGTGGCCTTC
GGAGCCTTTGACCAGTGGTGGGAGAGCAAGGAGGAGAAGGCCAAGCCATTCCAGAACGCG
GCCAAGCAGCAAGCCAAGGAGGAGGATAAAGAGAAGACGAAGCTGAAGGAGCCTGGCCTG
CTGTCCCTCGTGGACTGGGCCAAGAGCGGGGGCACTACGGGCATCGAGGCTTTCGCCTTT
GGGTCAGGGCTGAGAGGGGCCCTGCGGCTGCCTTCATTCAAGGTAAAGCGGAAAGAGCCA
TCGGAAATTTCCGAGGCCAGTGAGGAAAAGAGGCCTCGTCCCTCCACTCCTGCTGAGGAA
GATGAAGACGACCCTGAACAAGAGAAGGAGGCTGGAGAGCCAGGACGTCCGGGGACCAAG
CCCCCGAAGCGGGACGAAGAGCGAGGCAAGACCCAGGGCAAGCACCGCAAGTCCTTTGCT
CTGGACAGCGAAGGGGAGGAGGCATCCCAGGAGTCCTCCTCGGAGAAGGATGAGGAGGAT
GACGAGGAAGATGAGGAAGATGAAGATCGAGAGGAAGCTGTGGATACCACAAAGAAGGAG
ACAGAGGTGTCGGATGGCGAGGACGAGGAAAGCGATTCGTCTTCCAAATGTTCTCTGTAT
GCTGACTCAGATGGCGAAAATGACAGCACATCAGACTCCGAGAGCAGCAGCTCTTCCAGC
TCCTCATCCTCCTCCTCCTCCTCGTCCTCATCCTCCTCGTCCTCTTCATCCTCTGAGTCC
TCCTCTGAAGATGAAGAGGAAGAGGAGCGGCCAGCAGCCCTTCCCTCAGCCTCCCCGCCC
CCCAGAGAAGTCCCAGTGCCCACGCCAGCACCTGTGGAGGTGCCAGTGCCGGAAAGGGTT
GCAGGCTCCCCAGTCACACCCCTGCCCGAACAGGAGGCGTCTCCAGCAAGGCCTGCAGGC
CCCACGGAGGAGTCACCCCCCAGTGCGCCTCTGCGTCCCCCAGAACCACCTGCTGGGCCC
CCGGCCCCTGCCCCACGCCCCGATGAGCGTCCCTCTTCTCCCATCCCCCTCCTGCCCCCA
CCCAAGAAACGCCGGAAAACTGTCTCCTTCTCTGCCATCGAGGTGGTGCCAGCCCCGGAG
CCCCCTCCAGCCACACCGCCGCAGGCCAAGTTTCCCGGCCCAGCCTCCCGCAAGGCTCCC
CGGGGCGTGGAGCGGACCATCCGCAACCTGCCCCTGGACCACGCATCTCTGGTCAAGAGT
TGGCCCGAGGAGGTGTCCCGAGGAGGCCGGAGCCGGGCTGGAGGCCGAGGCCGCCTCACC
GAGGAAGAGGAGGCTGAGCCAGGGACAGAGGTGGACCTGGCGGTCCTGGCCGACCTGGCC
CTGACCCCTGCCCGGCGCGGGCTGCCTGCCCTGCCTGCTGTTGAAGACTCAGAGGCCACA
GAGACATCGGACGAGGCCGAGCGCCCTAGGCCCCTGCTCAGCCACATCCTCCTGGAGCAC
AACTATGCCCTGGCCGTCAAGCCCACGCCCCCTGCGCCAGCCCTGCGGCCCCCGGAGCCA
GTGCCCGCACCCGCCGCCCTCTTCAGTTCCCCAGCTGATGAGGTCCTGGAGGCCCCCGAG
GTGGTGGTGGCTGAGGCGGAGGAGCCCAAGCCGCAGCAACTGCAGCAGCAGCGGGAGGAG
GGCGAAGAGGAGGGGGAGGAAGAGGGGGAGGAAGAGGAGGAGGAGTCCTCTGACAGCAGC
AGCAGCAGCGATGGGGAGGGCGCCCTCCGGAGGCGCAGCCTCCGCTCCCACGCCCGGCGC
CGCCGCCCTCCGCCCCCACCCCCGCCGCCACCGCCCCGCGCCTACGAGCCACGCAGTGAG
TTTGAACAGATGACCATCCTGTATGACATTTGGAACTCGGGCCTGGACTCAGAGGACATG
AGTTACCTGCGGCTTACGTACGAGCGGCTGCTGCAGCAGACAAGCGGGGCTGACTGGCTC
AACGACACTCACTGGGTCCATCACACAATCACCAACCTGACCACCCCAAAACGCAAGCGG
CGGCCCCAGGATGGGCCCCGGGAGCACCAGACAGGCTCAGCCCGCAGCGAAGGCTACTAC
CCCATCAGCAAGAAGGAGAAGGACAAGTACCTGGACGTGTGCCCAGTCTCGGCCCGGCAG
CTGGAGGGCGTGGACACTCAGGGGACGAACCGCGTGCTGTCCGAGCGCCGGTCCGAGCAG
CGGCGGCTGCTGAGCGCCATCGGTACCTCCGCCATCATGGACAGTGACCTGCTGAAACTC
AACCAGCTCAAGTTCCGGAAGAAGAAGCTCCGATTTGGCCGGAGCCGGATCCACGAGTGG
GGTCTGTTTGCCATGGAACCCATTGCTGCTGACGAGATGGTCATCGAATACGTGGGTCAG
AACATCCGTCAGATGGTGGCCGACATGCGGGAGAAGCGCTACGTGCAGGAGGGCATTGGC
AGCAGCTACCTGTTCCGGGTGGACCACGACACCATCATCGATGCCACCAAGTGTGGCAAC
CTGGCCAGATTCATCAACCACTGCTGCACGCCTAACTGCTACGCCAAGGTCATCACCATC
GAGTCCCAGAAGAAGATCGTGATCTACTCCAAGCAGCCCATTGGCGTGGACGAGGAGATC
ACCTACGACTACAAGTTCCCACTGGAAGACAACAAGATCCCGTGTCTGTGTGGCACAGAG
AGCTGCCGGGGCTCCCTAAACTGA
Enzyme 28 GenBank Gene ID NM_014712.1 Link Image
Enzyme 28 GeneCard ID SETD1A Link Image
Enzyme 28 GenAtlas ID SETD1A Link Image
Enzyme 28 HGNC ID HGNC:29010 Link Image
Enzyme 28 Chromosome Location 1
Enzyme 28 Locus 16p11.2
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 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. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. 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]
  5. Lee JH, Skalnik DG: CpG-binding protein (CXXC finger protein 1) is a component of the mammalian Set1 histone H3-Lys4 methyltransferase complex, the analogue of the yeast Set1/COMPASS complex. J Biol Chem. 2005 Dec 16;280(50):41725-31. Epub 2005 Oct 26. [PubMed Link Image]
  6. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  7. Lee JH, Tate CM, You JS, Skalnik DG: Identification and characterization of the human Set1B histone H3-Lys4 methyltransferase complex. J Biol Chem. 2007 May 4;282(18):13419-28. Epub 2007 Mar 13. [PubMed Link Image]
  8. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  9. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 7643
Enzyme 29 Name DNA (cytosine-5)-methyltransferase 1
Enzyme 29 Synonyms
  1. Dnmt1
  2. CXXC-type zinc finger protein 9
  3. DNA methyltransferase HsaI
  4. DNA MTase HsaI
  5. M.HsaI
  6. MCMT
Enzyme 29 Gene Name DNMT1
Enzyme 29 Protein Sequence >DNA (cytosine-5)-methyltransferase 1
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 29 Number of Residues 1616
Enzyme 29 Molecular Weight 183163.6
Enzyme 29 Theoretical pI 7.81
Enzyme 29 GO Classification
Function
  • DNA (cytosine-5-)-methyltransferase activity
  • DNA binding
  • S-adenosylmethionine-dependent methyltransferase activity
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • methyltransferase activity
  • nucleic acid binding
  • protein binding
  • transcription factor binding
  • transferase activity
  • transferase activity, transferring one-carbon groups
  • transition metal ion binding
  • zinc ion binding
Process
  • DNA alkylation
  • DNA metabolic process
  • DNA methylation
  • DNA modification
  • cellular macromolecule metabolic process
  • macromolecule metabolic process
  • metabolic process
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 29 General Function Involved in DNA binding
Enzyme 29 Specific Function Methylates CpG residues. Preferentially methylates hemimethylated DNA. Associates with DNA replication sites in S phase maintaining the methylation pattern in the newly synthesized strand, that is essential for epigenetic inheritance. Associates with chromatin during G2 and M phases to maintain DNA methylation independently of replication. 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. In association with DNMT3B and via the recruitment of CTCFL/BORIS, involved in activation of BAG1 gene expression by modulating dimethylation of promoter histone H3 at H3K4 and H3K9
Enzyme 29 Pathways
Enzyme 29 Reactions
  • S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine [RN:R00380]
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 1632819 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID P26358 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name DNMT1_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 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 29 GenBank Gene ID X63692 Link Image
Enzyme 29 GeneCard ID DNMT1 Link Image
Enzyme 29 GenAtlas ID DNMT1 Link Image
Enzyme 29 HGNC ID HGNC:2976 Link Image
Enzyme 29 Chromosome Location 1
Enzyme 29 Locus 19p13.2
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 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. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
  12. Kim GD, Ni J, Kelesoglu N, Roberts RJ, Pradhan S: Co-operation and communication between the human maintenance and de novo DNA (cytosine-5) methyltransferases. EMBO J. 2002 Aug 1;21(15):4183-95. [PubMed Link Image]
  13. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  14. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  15. Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y: Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell. 2006 Aug;23(4):607-18. [PubMed Link Image]
  16. Vire E, Brenner C, Deplus R, Blanchon L, Fraga M, Didelot C, Morey L, Van Eynde A, Bernard D, Vanderwinden JM, Bollen M, Esteller M, Di Croce L, de Launoit Y, Fuks F: The Polycomb group protein EZH2 directly controls DNA methylation. Nature. 2006 Feb 16;439(7078):871-4. Epub 2005 Dec 14. [PubMed Link Image]
  17. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  18. Schlesinger Y, Straussman R, Keshet I, Farkash S, Hecht M, Zimmerman J, Eden E, Yakhini Z, Ben-Shushan E, Reubinoff BE, Bergman Y, Simon I, Cedar H: Polycomb-mediated methylation on Lys27 of histone H3 pre-marks genes for de novo methylation in cancer. Nat Genet. 2007 Feb;39(2):232-6. Epub 2006 Dec 31. [PubMed Link Image]
  19. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
  20. Pradhan M, Esteve PO, Chin HG, Samaranayke M, Kim GD, Pradhan S: CXXC domain of human DNMT1 is essential for enzymatic activity. Biochemistry. 2008 Sep 23;47(38):10000-9. Epub 2008 Aug 29. [PubMed Link Image]
  21. Sun L, Huang L, Nguyen P, Bisht KS, Bar-Sela G, Ho AS, Bradbury CM, Yu W, Cui H, Lee S, Trepel JB, Feinberg AP, Gius D: DNA methyltransferase 1 and 3B activate BAG-1 expression via recruitment of CTCFL/BORIS and modulation of promoter histone methylation. Cancer Res. 2008 Apr 15;68(8):2726-35. [PubMed Link Image]
  22. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  23. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  24. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  25. Lee B, Muller MT: SUMOylation enhances DNA methyltransferase 1 activity. Biochem J. 2009 Jul 15;421(3):449-61. [PubMed Link Image]
  26. Fellinger K, Rothbauer U, Felle M, Langst G, Leonhardt H: Dimerization of DNA methyltransferase 1 is mediated by its regulatory domain. J Cell Biochem. 2009 Mar 1;106(4):521-8. [PubMed Link Image]
  27. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  28. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 7736
Enzyme 30 Name DNA (cytosine-5)-methyltransferase 3B
Enzyme 30 Synonyms
  1. Dnmt3b
  2. DNA methyltransferase HsaIIIB
  3. DNA MTase HsaIIIB
  4. M.HsaIIIB
Enzyme 30 Gene Name DNMT3B
Enzyme 30 Protein Sequence >DNA (cytosine-5)-methyltransferase 3B
MKGDTRHLNGEEDAGGREDSILVNGACSDQSSDSPPILEAIRTPEIRGRRSSSRLSKREV
SSLLSYTQDLTGDGDGEDGDGSDTPVMPKLFRETRTRSESPAVRTRNNNSVSSRERHRPS
PRSTRGRQGRNHVDESPVEFPATRSLRRRATASAGTPWPSPPSSYLTIDLTDDTEDTHGT
PQSSSTPYARLAQDSQQGGMESPQVEADSGDGDSSEYQDGKEFGIGDLVWGKIKGFSWWP
AMVVSWKATSKRQAMSGMRWVQWFGDGKFSEVSADKLVALGLFSQHFNLATFNKLVSYRK
AMYHALEKARVRAGKTFPSSPGDSLEDQLKPMLEWAHGGFKPTGIEGLKPNNTQPVVNKS
KVRRAGSRKLESRKYENKTRRRTADDSATSDYCPAPKRLKTNCYNNGKDRGDEDQSREQM
ASDVANNKSSLEDGCLSCGRKNPVSFHPLFEGGLCQTCRDRFLELFYMYDDDGYQSYCTV
CCEGRELLLCSNTSCCRCFCVECLEVLVGTGTAAEAKLQEPWSCYMCLPQRCHGVLRRRK
DWNVRLQAFFTSDTGLEYEAPKLYPAIPAARRRPIRVLSLFDGIATGYLVLKELGIKVGK
YVASEVCEESIAVGTVKHEGNIKYVNDVRNITKKNIEEWGPFDLVIGGSPCNDLSNVNPA
RKGLYEGTGRLFFEFYHLLNYSRPKEGDDRPFFWMFENVVAMKVGDKRDISRFLECNPVM
IDAIKVSAAHRARYFWGNLPGMNRPVIASKNDKLELQDCLEYNRIAKLKKVQTITTKSNS
IKQGKNQLFPVVMNGKEDVLWCTELERIFGFPVHYTDVSNMGRGARQKLLGRSWSVPVIR
HLFAPLKDYFACE
Enzyme 30 Number of Residues 853
Enzyme 30 Molecular Weight 95750.2
Enzyme 30 Theoretical pI 8.52
Enzyme 30 GO Classification
Function
  • DNA binding
  • binding
  • cation binding
  • ion binding
  • metal ion binding
  • nucleic acid binding
  • transition metal ion binding
  • zinc ion binding
Process
  • DNA alkylation
  • DNA metabolic process
  • DNA methylation
  • DNA modification
  • cellular macromolecule metabolic process
  • macromolecule metabolic process
  • metabolic process
Component
Enzyme 30 General Function Involved in DNA binding
Enzyme 30 Specific Function Required for genome wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. DNA methylation is coordinated with methylation of histones. May preferentially methylates nucleosomal DNA within the nucleosome core region. May function as transcriptional co- repressor by associating with CBX4 and independently of DNA methylation. Seems to be involved in gene silencing. In association with DNMT1 and via the recruitment of CTCFL/BORIS, involved in activation of BAG1 gene expression by modulating dimethylation of promoter histone H3 at H3K4 and H3K9. Isoforms 4 and 5 are probably not functional due to the deletion of two conserved methyltransferase motifs
Enzyme 30 Pathways
Enzyme 30 Reactions
  • S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine [RN:R00380]
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • None
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 5901940 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID Q9UBC3 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name DNM3B_HUMAN Link Image
Enzyme 30 PDB ID 1KHC Link Image
Enzyme 30 PDB File Show
Enzyme 30 3D Structure
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >2562 bp
ATGAAGGGAGACACCAGGCATCTCAATGGAGAGGAGGACGCCGGCGGGAGGGAAGACTCG
ATCCTCGTCAACGGGGCCTGCAGCGACCAGTCCTCCGACTCGCCCCCAATCCTGGAGGCT
ATCCGCACCCCGGAGATCAGAGGCCGAAGATCAAGCTCGCGACTCTCCAAGAGGGAGGTG
TCCAGTCTGCTAAGCTACACACAGGACTTGACAGGCGATGGCGACGGGGAAGATGGGGAT
GGCTCTGACACCCCAGTCATGCCAAAGCTCTTCCGGGAAACCAGGACTCGTTCAGAAAGC
CCAGCTGTCCGAACTCGAAATAACAACAGTGTCTCCAGCCGGGAGAGGCACAGGCCTTCC
CCACGTTCCACCCGAGGCCGGCAGGGCCGCAACCATGTGGACGAGTCCCCCGTGGAGTTC
CCGGCTACCAGGTCCCTGAGACGGCGGGCAACAGCATCGGCAGGAACGCCATGGCCGTCC
CCTCCCAGCTCTTACCTTACCATCGACCTCACAGACGACACAGAGGACACACATGGGACG
CCCCAGAGCAGCAGTACCCCCTACGCCCGCCTAGCCCAGGACAGCCAGCAGGGGGGCATG
GAGTCCCCGCAGGTGGAGGCAGACAGTGGAGATGGAGACAGTTCAGAGTATCAGGATGGG
AAGGAGTTTGGAATAGGGGACCTCGTGTGGGGAAAGATCAAGGGCTTCTCCTGGTGGCCC
GCCATGGTGGTGTCTTGGAAGGCCACCTCCAAGCGACAGGCTATGTCTGGCATGCGGTGG
GTCCAGTGGTTTGGCGATGGCAAGTTCTCCGAGGTCTCTGCAGACAAACTGGTGGCACTG
GGGCTGTTCAGCCAGCACTTTAATTTGGCCACCTTCAATAAGCTCGTCTCCTATCGAAAA
GCCATGTACCATGCTCTGGAGAAAGCTAGGGTGCGAGCTGGCAAGACCTTCCCCAGCAGC
CCTGGAGACTCATTGGAGGACCAGCTGAAGCCCATGTTGGAGTGGGCCCACGGGGGCTTC
AAGCCCACTGGGATCGAGGGCCTCAAACCCAACAACACGCAACCAGTGGTTAATAAGTCG
AAGGTGCGTCGTGCAGGCAGTAGGAAATTAGAATCAAGGAAATACGAGAACAAGACTCGA
AGACGCACAGCTGACGACTCAGCCACCTCTGACTACTGCCCCGCACCCAAGCGCCTCAAG
ACAAATTGCTATAACAACGGCAAAGACCGAGGGGATGAAGATCAGAGCCGAGAACAAATG
GCTTCAGATGTTGCCAACAACAAGAGCAGCCTGGAAGATGGCTGTTTGTCTTGTGGCAGG
AAAAACCCCGTGTCCTTCCACCCTCTCTTTGAGGGGGGGCTCTGTCAGACATGCCGGGAT
CGCTTCCTTGAGCTGTTTTACATGTATGATGACGATGGCTATCAGTCTTACTGCACTGTG
TGCTGCGAGGGCCGAGAGCTGCTGCTTTGCAGCAACACGAGCTGCTGCCGGTGTTTCTGT
GTGGAGTGCCTGGAGGTGCTGGTGGGCACAGGCACAGCGGCCGAGGCCAAGCTTCAGGAG
CCCTGGAGCTGTTACATGTGTCTCCCGCAGCGCTGTCATGGCGTCCTGCGGCGCCGGAAG
GACTGGAACGTGCGCCTGCAGGCCTTCTTCACCAGTGACACGGGGCTTGAATATGAAGCC
CCCAAGCTGTACCCTGCCATTCCCGCAGCCCGAAGGCGGCCCATTCGAGTCCTGTCATTG
TTTGATGGCATCGCGACAGGCTACCTAGTCCTCAAAGAGTTGGGCATAAAGGTAGGAAAG
TACGTCGCTTCTGAAGTGTGTGAGGAGTCCATTGCTGTTGGAACCGTGAAGCACGAGGGG
AATATCAAATACGTGAACGACGTGAGGAACATCACAAAGAAAAATATTGAAGAATGGGGC
CCATTTGACTTGGTGATTGGCGGAAGCCCATGCAACGATCTCTCAAATGTGAATCCAGCC
AGGAAAGGCCTGTATGAGGGTACAGGCCGGCTCTTCTTCGAATTTTACCACCTGCTGAAT
TACTCACGCCCCAAGGAGGGTGATGACCGGCCGTTCTTCTGGATGTTTGAGAATGTTGTA
GCCATGAAGGTTGGCGACAAGAGGGACATCTCACGGTTCCTGGAGTGTAATCCAGTGATG
ATTGATGCCATCAAAGTTTCTGCTGCTCACAGGGCCCGATACTTCTGGGGCAACCTACCC
GGGATGAACAGGCCCGTGATAGCATCAAAGAATGATAAACTCGAGCTGCAGGACTGCTTG
GAATACAATAGGATAGCCAAGTTAAAGAAAGTACAGACAATAACCACCAAGTCGAACTCG
ATCAAACAGGGGAAAAACCAACTTTTCCCTGTTGTCATGAATGGCAAAGAAGATGTTTTG
TGGTGCACTGAGCTCGAAAGGATCTTTGGCTTTCCTGTGCACTACACAGACGTGTCCAAC
ATGGGCCGTGGTGCCCGCCAGAAGCTGCTGGGAAGGTCCTGGAGCGTGCCTGTCATCCGA
CACCTCTTCGCCCCTCTGAAGGACTACTTTGCATGTGAATAG
Enzyme 30 GenBank Gene ID NM_006892.3 Link Image
Enzyme 30 GeneCard ID DNMT3B Link Image
Enzyme 30 GenAtlas ID DNMT3B Link Image
Enzyme 30 HGNC ID HGNC:2979 Link Image
Enzyme 30 Chromosome Location 2
Enzyme 30 Locus 20q11.2
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 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. Kim GD, Ni J, Kelesoglu N, Roberts RJ, Pradhan S: Co-operation and communication between the human maintenance and de novo DNA (cytosine-5) methyltransferases. EMBO J. 2002 Aug 1;21(15):4183-95. [PubMed Link Image]
  7. Li H, Rauch T, Chen ZX, Szabo PE, Riggs AD, Pfeifer GP: The histone methyltransferase SETDB1 and the DNA methyltransferase DNMT3A interact directly and localize to promoters silenced in cancer cells. J Biol Chem. 2006 Jul 14;281(28):19489-500. Epub 2006 May 8. [PubMed Link Image]
  8. Vire E, Brenner C, Deplus R, Blanchon L, Fraga M, Didelot C, Morey L, Van Eynde A, Bernard D, Vanderwinden JM, Bollen M, Esteller M, Di Croce L, de Launoit Y, Fuks F: The Polycomb group protein EZH2 directly controls DNA methylation. Nature. 2006 Feb 16;439(7078):871-4. Epub 2005 Dec 14. [PubMed Link Image]
  9. Schlesinger Y, Straussman R, Keshet I, Farkash S, Hecht M, Zimmerman J, Eden E, Yakhini Z, Ben-Shushan E, Reubinoff BE, Bergman Y, Simon I, Cedar H: Polycomb-mediated methylation on Lys27 of histone H3 pre-marks genes for de novo methylation in cancer. Nat Genet. 2007 Feb;39(2):232-6. Epub 2006 Dec 31. [PubMed Link Image]
  10. Sun L, Huang L, Nguyen P, Bisht KS, Bar-Sela G, Ho AS, Bradbury CM, Yu W, Cui H, Lee S, Trepel JB, Feinberg AP, Gius D: DNA methyltransferase 1 and 3B activate BAG-1 expression via recruitment of CTCFL/BORIS and modulation of promoter histone methylation. Cancer Res. 2008 Apr 15;68(8):2726-35. [PubMed Link Image]
  11. Kim SH, Park J, Choi MC, Park JH, Kim HP, Lee JH, Oh DY, Im SA, Bang YJ, Kim TY: DNA methyltransferase 3B acts as a co-repressor of the human polycomb protein hPc2 to repress fibroblast growth factor receptor 3 transcription. Int J Biochem Cell Biol. 2008;40(11):2462-71. Epub 2008 May 18. [PubMed Link Image]
  12. 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]
  13. 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]
  14. 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]
  15. Jiang YL, Rigolet M, Bourc'his D, Nigon F, Bokesoy I, Fryns JP, Hulten M, Jonveaux P, Maraschio P, Megarbane A, Moncla A, Viegas-Pequignot E: DNMT3B mutations and DNA methylation defect define two types of ICF syndrome. Hum Mutat. 2005 Jan;25(1):56-63. [PubMed Link Image]
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 8577
Enzyme 31 Name tRNA (cytosine-5-)-methyltransferase
Enzyme 31 Synonyms
  1. DNA (cytosine-5)-methyltransferase-like protein 2
  2. Dnmt2
  3. DNA methyltransferase homolog HsaIIP
  4. DNA MTase homolog HsaIIP
  5. M.HsaIIP
  6. PuMet
Enzyme 31 Gene Name TRDMT1
Enzyme 31 Protein Sequence >tRNA (cytosine-5-)-methyltransferase
MEPLRVLELYSGVGGMHHALRESCIPAQVVAAIDVNTVANEVYKYNFPHTQLLAKTIEGI
TLEEFDRLSFDMILMSPPCQPFTRIGRQGDMTDSRTNSFLHILDILPRLQKLPKYILLEN
VKGFEVSSTRDLLIQTIENCGFQYQEFLLSPTSLGIPNSRLRYFLIAKLQSEPLPFQAPG
QVLMEFPKIESVHPQKYAMDVENKIQEKNVEPNISFDGSIQCSGKDAILFKLETAEEIHR
KNQQDSDLSVKMLKDFLEDDTDVNQYLLPPKSLLRYALLLDIVQPTCRRSVCFTKGYGSY
IEGTGSVLQTAEDVQVENIYKSLTNLSQEEQITKLLILKLRYFTPKEIANLLGFPPEFGF
PEKITVKQRYRLLGNSLNVHVVAKLIKILYE
Enzyme 31 Number of Residues 391
Enzyme 31 Molecular Weight 44596.2
Enzyme 31 Theoretical pI 5.95
Enzyme 31 GO Classification
Function
  • DNA binding
  • binding
  • nucleic acid binding
Process
  • DNA alkylation
  • DNA metabolic process
  • DNA methylation
  • DNA modification
  • cellular macromolecule metabolic process
  • macromolecule metabolic process
  • metabolic process
Component
Enzyme 31 General Function Involved in DNA binding
Enzyme 31 Specific Function Specifically methylates cytosine 38 in the anticodon loop of tRNA(Asp)
Enzyme 31 Pathways Not Available
Enzyme 31 Reactions
  • S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing 5-methylcytosine [RN:R00595]
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • None
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein Not Available
Enzyme 31 UniProtKB/Swiss-Prot ID O14717 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name TRDMT_HUMAN Link Image
Enzyme 31 PDB ID Not Available
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >1176 bp
ATGGAGCCCCTGCGGGTGCTGGAGCTATACAGCGGCGTGGGCGGCATGCACCACGCGCTG
AGAGAAAGCTGTATACCTGCACAAGTGGTGGCTGCCATTGATGTCAACACTGTCGCTAAT
GAAGTATACAAGTATAATTTTCCTCACACACAGTTACTTGCCAAGACGATTGAAGGCATT
ACACTCGAAGAGTTTGACAGATTATCTTTTGATATGATTTTAATGAGCCCTCCCTGCCAG
CCATTCACAAGGATTGGCCGGCAGGGTGATATGACTGATTCAAGGACGAATAGCTTCTTA
CATATTCTAGATATTCTCCCAAGATTACAAAAATTACCAAAGTATATTCTTTTGGAAAAT
GTTAAAGGTTTTGAAGTATCTTCTACAAGAGACCTCTTGATACAAACAATAGAAAATTGT
GGCTTTCAGTACCAAGAATTTCTATTATCTCCAACCTCTCTTGGCATTCCAAATTCAAGG
CTACGATATTTTCTTATTGCAAAGCTTCAGTCAGAGCCATTACCCTTTCAAGCCCCTGGT
CAGGTACTGATGGAGTTCCCCAAAATTGAATCTGTACATCCACAAAAATATGCAATGGAT
GTAGAAAATAAAATTCAAGAAAAGAACGTTGAACCAAATATTAGCTTTGATGGCAGCATA
CAGTGTTCTGGAAAAGATGCCATTCTTTTTAAGCTTGAAACTGCAGAAGAAATTCACAGG
AAAAATCAACAAGATAGTGATCTCTCTGTGAAAATGCTAAAAGATTTTCTTGAAGATGAC
ACTGACGTGAACCAGTATCTTTTACCACCAAAGTCATTGCTGCGATATGCTCTTCTGTTA
GACATTGTTCAGCCCACTTGTAGAAGGTCCGTGTGCTTTACCAAAGGATATGGAAGCTAC
ATAGAAGGGACAGGGTCTGTGTTACAGACTGCAGAGGATGTGCAGGTTGAGAATATCTAC
AAATCCCTTACCAATTTGTCACAAGAAGAACAGATAACAAAGCTGTTAATACTTAAACTG
CGATATTTCACTCCTAAAGAAATAGCAAATCTCCTTGGATTTCCTCCAGAGTTCGGATTT
CCTGAGAAGATAACAGTGAAACAGCGTTATCGCCTACTTGGAAATAGTCTCAACGTGCAT
GTAGTAGCTAAACTAATCAAAATCTTATATGAATAA
Enzyme 31 GenBank Gene ID AF012128 Link Image
Enzyme 31 GeneCard ID TRDMT1 Link Image
Enzyme 31 GenAtlas ID TRDMT1 Link Image
Enzyme 31 HGNC ID HGNC:2977 Link Image
Enzyme 31 Chromosome Location 1
Enzyme 31 Locus 10p15.1
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 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. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. 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]
  7. Goll MG, Kirpekar F, Maggert KA, Yoder JA, Hsieh CL, Zhang X, Golic KG, Jacobsen SE, Bestor TH: Methylation of tRNAAsp by the DNA methyltransferase homolog Dnmt2. Science. 2006 Jan 20;311(5759):395-8. [PubMed Link Image]
  8. 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 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 8641
Enzyme 32 Name Histone-lysine N-methyltransferase SETD8
Enzyme 32 Synonyms
  1. H4-K20-HMTase SETD8
  2. Lysine N-methyltransferase 5A
  3. PR/SET domain-containing protein 07
  4. PR-Set7
  5. PR/SET07
  6. SET domain-containing protein 8
Enzyme 32 Gene Name SETD8
Enzyme 32 Protein Sequence >Histone-lysine N-methyltransferase SETD8
MGEGGAAAALVAAAAAAAAAAAAVVAGQRRRRLGRRARCHGPGRAAGGKMSKPCAVEAAA
AAVAATAPGPEMVERRGPGRPRTDGENVFTGQSKIYSYMSPNKCSGMRFPLQEENSVTHH
EVKCQGKPLAGIYRKREEKRNAGNAVRSAMKSEEQKIKDARKGPLVPFPNQKSEAAEPPK
TPPSSCDSTNAAIAKQALKKPIKGKQAPRKKAQGKTQQNRKLTDFYPVRRSSRKSKAELQ
SEERKRIDELIESGKEEGMKIDLIDGKGRGVIATKQFSRGDFVVEYHGDLIEITDAKKRE
ALYAQDPSTGCYMYYFQYLSKTYCVDATRETNRLGRLINHSKCGNCQTKLHDIDGVPHLI
LIASRDIAAGEELLYDYGDRSKASIEAHPWLKH
Enzyme 32 Number of Residues 393
Enzyme 32 Molecular Weight 42889.5
Enzyme 32 Theoretical pI 10.22
Enzyme 32 GO Classification Not Available
Enzyme 32 General Function Involved in histone-lysine N-methyltransferase activity
Enzyme 32 Specific Function Histone methyltransferase that specifically monomethylates 'Lys-20' of histone H4. H4 'Lys-20' monomethylation is enriched during mitosis and represents a specific tag for epigenetic transcriptional repression. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. Required for cell proliferation, probably by contributing to the maintenance of proper higher order structure of DNA during mitosis. Involved in chromosome condensation and proper cytokinesis. Nucleosomes are preferred as substrate compared to free histones
Enzyme 32 Pathways
Enzyme 32 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • None
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 15029567 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID Q9NQR1 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name SETD8_HUMAN Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence >1182 bp
ATGGGGGAAGGGGGCGCCGCGGCGGCGCTGGTGGCGGCGGCAGCAGCAGCAGCAGCGGCA
GCGGCAGCGGTGGTGGCCGGGCAGCGGCGGCGGCGGCTAGGGCGCAGGGCGCGCTGCCAT
GGGCCTGGCCGGGCTGCAGGCGGGAAGATGTCCAAGCCCTGCGCGGTGGAGGCGGCGGCG
GCGGCGGTGGCAGCGACGGCCCCGGGCCCGGAGATGGTGGAGCGGAGGGGCCCGGGGAGG
CCCCGCACCGACGGGGAGAACGTATTTACCGGGCAGTCAAAGATCTATTCCTACATGAGC
CCGAACAAATGCTCTGGAATGCGTTTCCCCCTTCAGGAAGAGAACTCAGTTACACATCAC
GAAGTCAAATGCCAGGGGAAACCATTAGCTGGAATCTACAGGAAACGAGAAGAGAAAAGA
AATGCTGGGAACGCAGTACGGAGCGCCATGAAGTCCGAGGAACAGAAGATCAAAGACGCC
AGGAGACGTCCCCTGGTACCTTTTCCAAACCAAAAATCTGAAGCAGCAGAACCTCCAAAA
ACTCCACCCTCATCTTGTGATTCCACCAATGCAGCCATCGCCAAGCAAGCCCTGAAAAAG
CCCATCAAGGGCAAACAGGCCCCCCGAAAAAAAGCTCAAGGAAAAACGCAACAGAATCGC
AAACTTACGGATTTCTACCCTGTCCGAAGGAGCTCCAGGAAGAGCAAAGCCGAGCTGCAG
TCTGAAGAAAGGAAAAGAATAGATGAATTGATTGAAAGTGGGAAGGAAGAAGGAATGAAG
ATCGACCTCATCGATGGCAAAGGCAGGGGTGTGATTGCCACCAAGCAGTTCTCCCGGGGT
GCCTTTGTGGTGGAATACCACGGGGACCTCATCGAGATCACCGACGCCAAGAAACGGGAG
GCTCTGTACGCACAGGACCCTTCCACGGGCTGCTACATGTACTATTTTCAGTATCTGAGC
AAAACCTACTGCGTGGATGCAACTAGAGAGACAAATCGCCTAGGAAGACTGATCAATCAC
AGCAAACGTGGGAACTGCCAAACCAAACTGCACGACATCGACGGCGTACCTCACCTCATC
CTCATCGCCTCCCGAGACATCGCGGCTGGGGAGGAGCCCCTGTATGACTATGGGGACCGC
AGCAAGGCTTCCATTGAAGCCCACCCATGGCTGAAGCATTAA
Enzyme 32 GenBank Gene ID AF287261 Link Image
Enzyme 32 GeneCard ID SETD8 Link Image
Enzyme 32 GenAtlas ID SETD8 Link Image
Enzyme 32 HGNC ID HGNC:29489 Link Image
Enzyme 32 Chromosome Location 1
Enzyme 32 Locus 12q24.31
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References
  1. Nishioka K, Rice JC, Sarma K, Erdjument-Bromage H, Werner J, Wang Y, Chuikov S, Valenzuela P, Tempst P, Steward R, Lis JT, Allis CD, Reinberg D: PR-Set7 is a nucleosome-specific methyltransferase that modifies lysine 20 of histone H4 and is associated with silent chromatin. Mol Cell. 2002 Jun;9(6):1201-13. [PubMed Link Image]
  2. Fang J, Feng Q, Ketel CS, Wang H, Cao R, Xia L, Erdjument-Bromage H, Tempst P, Simon JA, Zhang Y: Purification and functional characterization of SET8, a nucleosomal histone H4-lysine 20-specific methyltransferase. Curr Biol. 2002 Jul 9;12(13):1086-99. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Rice JC, Nishioka K, Sarma K, Steward R, Reinberg D, Allis CD: Mitotic-specific methylation of histone H4 Lys 20 follows increased PR-Set7 expression and its localization to mitotic chromosomes. Genes Dev. 2002 Sep 1;16(17):2225-30. [PubMed Link Image]
  6. Julien E, Herr W: A switch in mitotic histone H4 lysine 20 methylation status is linked to M phase defects upon loss of HCF-1. Mol Cell. 2004 Jun 18;14(6):713-25. [PubMed Link Image]
  7. Yin Y, Liu C, Tsai SN, Zhou B, Ngai SM, Zhu G: SET8 recognizes the sequence RHRK20VLRDN within the N terminus of histone H4 and mono-methylates lysine 20. J Biol Chem. 2005 Aug 26;280(34):30025-31. Epub 2005 Jun 17. [PubMed Link Image]
  8. Sims JK, Houston SI, Magazinnik T, Rice JC: A trans-tail histone code defined by monomethylated H4 Lys-20 and H3 Lys-9 demarcates distinct regions of silent chromatin. J Biol Chem. 2006 May 5;281(18):12760-6. Epub 2006 Mar 3. [PubMed Link Image]
  9. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  10. Xiao B, Jing C, Kelly G, Walker PA, Muskett FW, Frenkiel TA, Martin SR, Sarma K, Reinberg D, Gamblin SJ, Wilson JR: Specificity and mechanism of the histone methyltransferase Pr-Set7. Genes Dev. 2005 Jun 15;19(12):1444-54. Epub 2005 Jun 2. [PubMed Link Image]
  11. Couture JF, Collazo E, Brunzelle JS, Trievel RC: Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase. Genes Dev. 2005 Jun 15;19(12):1455-65. Epub 2005 Jun 2. [PubMed Link Image]
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 11322
Enzyme 33 Name Histone-lysine N-methyltransferase SETDB2
Enzyme 33 Synonyms
  1. Chronic lymphocytic leukemia deletion region gene 8 protein
  2. Lysine N-methyltransferase 1F
  3. SET domain bifurcated 2
Enzyme 33 Gene Name SETDB2
Enzyme 33 Protein Sequence >Histone-lysine N-methyltransferase SETDB2
MGEKNGDAKTFWMELEDDGKVDFIFEQVQNVLQSLKQKIKDGSATNKEYIQAMILVNEAT
IINSSTSIKGASQKEVNAQSSDPMPVTQKEQENKSNAFPSTSCENSFPEDCTFLTTENKE
ILSLEDKVVDFREKDSSSNLSYQSHDCSGACLMKMPLNLKGENPLQLPIKCHFQRRHAKT
NSHSSALHVSYKTPCGRSLRNVEEVFRYLLETECNFLFTDNFSFNTYVQLARNYPKQKEV
VSDVDISNGVESVPISFCNEIDSRKLPQFKYRKTVWPRAYNLTNFSSMFTDSCDCSEGCI
DITKCACLQLTARNAKTSPLSSDKITTGYKYKRLQRQIPTGIYECSLLCKCNRQLCQNRV
VQHGPQVRLQVFKTEQKGWGVRCLDDIDRGTFVCIYSGRLLSRANTEKSYGIDENGRDEN
TMKNIFSKKRKLEVACSDCEVEVLPLGLETHPRTAKTEKCPPKFSNNPKELTVETKYDNI
SRIQYHSVIRDPESKTAIFQHNGKKMEFVSSESVTPEDNDGFKPPREHLNSKTKGAQKDS
SSNHVDEFEDNLLIESDVIDITKYREETPPRSRCNQATTLDNQNIKKAIEVQIQKPQEGR
STACQRQQVFCDEELLSETKNTSSDSLTKFNKGNVFLLDATKEGNVGRFLNHSCCPNLLV
QNVFVETHNRNFPLVAFFTNRYVKARTELTWDYGYEAGTVPEKEIFCQCGVNKCRKKIL
Enzyme 33 Number of Residues 719
Enzyme 33 Molecular Weight 81893.7
Enzyme 33 Theoretical pI 7.54
Enzyme 33 GO Classification
Function
  • DNA binding
  • binding
  • catalytic activity
  • cation binding
  • histone-lysine N-methyltransferase activity
  • ion binding
  • metal 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
  • cellular component organization at cellular level
  • cellular process
  • chromatin modification
  • chromatin organization
  • chromosome organization
  • organelle organization
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 33 General Function Involved in DNA binding
Enzyme 33 Specific Function Histone methyltransferase involved in left-right axis specification in early development and mitosis. Specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). H3K9me3 is a specific tag for epigenetic transcriptional repression that recruits HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Contributes to H3K9me3 in both the interspersed repetitive elements and centromere-associated repeats. Plays a role in chromosome condensation and segregation during mitosis
Enzyme 33 Pathways
Enzyme 33 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • None
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 13699244 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID Q96T68 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name SETB2_HUMAN Link Image
Enzyme 33 PDB ID Not Available
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence >2160 bp
ATGGGAGAAAAAAATGGCGATGCAAAAACTTTCTGGATGGAGCTAGAAGATGATGGAAAA
GTGGACTTCATTTTTGAACAAGTACAAAATGTGCTGCAGTCACTGAAACAAAAGATCAAA
GATGGGTCTGCCACCAATAAAGAATACATCCAAGCAATGATTCTAGTGAATGAAGCAACT
ATAATTAACAGTTCAACATCAATAAAGGGAGCATCACAGAAAGAAGTGAATGCCCAAAGC
AGTGATCCTATGCCTGTGACTCAGAAGGAACAGGAAAACAAATCCAATGCATTTCCCTCT
ACATCATGTGAAAACTCCTTTCCAGAAGACTGTACATTTCTAACAACAGGAAATAAGGAA
ATTCTCTCTCTTGAAGATAAAGTTGTAGACTTTAGAGAAAAAGACTCATCTTCGAATTTA
TCTTACCAAAGTCATGACTGCTCTGGTGCTTGTCTGATGAAAATGCCACTGAACTTGAAG
GGAGAAAACCCTCTGCAGCTGCCAATCAAATGTCACTTCCAAAGACGACATGCAAAGACA
AACTCTCATTCTTCAGCACTCCACGTGAGTTATAAAACCCCTTGTGGAAGGAGTCTACGA
AACGTGGAGGAAGTTTTTCGTTACCTGCTTGAGACAGAGTGTAACTTTTTATTTACAGAT
AACTTTTCTTTCAATACCTATGTTCAGTTGGCTCGGAATTACCCAAAGCAAAAAGAAGTT
GTTTCTGATGTGGATATTAGCAATGGAGTGGAATCAGTGCCCATTTCTTTCTGTAATGAA
ATTGACAGTAGAAAGCTCCCACAGTTTAAGTACAGAAAGACTGTGTGGCCTCGAGCATAT
AATCTAACCAACTTTTCCAGCATGTTTACTGATTCCTGTGACTGCTCTGAGGGCTGCATA
GACATAACAAAATGTGCATGTCTTCAACTGACAGCAAGGAATGCCAAAACTTCCCCCTTG
TCAAGTGACAAAATAACCACTGGATATAAATATAAAAGACTACAGAGACAGATTCCTACT
GGCATTTATGAATGCAGCCTTTTGTGCAAATGTAATCGACAATTGTGTCAAAACCGAGTT
GTCCAACATGGTCCTCAAGTGAGGTTACAGGTGTTCAAAACTGAGCAGAAGGGATGGGGT
GTACGCTGTCTAGATGACATTGACAGAGGGACATTTGTTTGCATTTATTCAGGAAGATTA
CTAAGCAGAGCTAACACTGAAAAATCTTATGGTATTGATGAAAACGGGAGAGATGAGAAT
ACTATGAAAAATATATTTTCAAAAAAGAGGAAATTAGAAGTTGCATGTTCAGATTGTGAA
GTTGAAGTTCTCCCATTAGGATTGGAAACACATCCTAGAACTGCTAAAACTGAGAAATGT
CCACCAAAGTTCAGTAATAATCCCAAGGAGCTTACTATGGAAACGAAATATGATAATATT
TCAAGAATTCAATATCATTCAGTTATTAGAGATCCTGAATCCAAGACAGCCATTTTTCAA
CACAATGGGAAAAAAATGGAATTTGTTTCCTCGGAGTCTGTCACTCCAGAAGATAATGAT
GGATTTAAACCACCCCGAGAGCATCTGAACTCTAAAACCAAGGGAGCACAAAAGGACTCA
AGTTCAAACCATGTTGATGAGTTTGAAGATAATCTGCTGATTGAATCAGATGTGATAGAT
ATAACTAAATATAGAGAAGAAACTCCACCAAGGAGCAGATGTAACCAGGCGACCACATTG
GATAATCAGAATATTAAAAAGGCAATTGAGGTTCAAATTCAGAAACCCCAAGAGGGACGA
TCTACAGCATGTCAAAGACAGCAGGTATTTTGTGATGAAGAGTTGCTAAGTGAAACCAAG
AATACTTCATCTGATTCTCTAACAAAGTTCAATAAAGGGAATGTGTTTTTATTGGATGCC
ACAAAAGAAGGAAATGTCGGCCGCTTCCTTAATCATAGTTGTTGCCCAAATCTCTTGGTA
CAGAATGTTTTTGTAGAAACACACAACAGGAATTTTCCATTGGTGGCATTCTTCACCAAC
AGGTATGTGAAAGCAAGAACAGAGCTAACATGGGATTATGGCTATGAAGCTGGGACTGTG
CCTGAGAAGGAAATCTTCTGCCAATGTGGGGTTAATAAATGTAGAAAAAAAATATTATAA
Enzyme 33 GenBank Gene ID AF334407 Link Image
Enzyme 33 GeneCard ID SETDB2 Link Image
Enzyme 33 GenAtlas ID SETDB2 Link Image
Enzyme 33 HGNC ID HGNC:20263 Link Image
Enzyme 33 Chromosome Location 1
Enzyme 33 Locus 13q14
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 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. Dunham A, Matthews LH, Burton J, Ashurst JL, Howe KL, Ashcroft KJ, Beare DM, Burford DC, Hunt SE, Griffiths-Jones S, Jones MC, Keenan SJ, Oliver K, Scott CE, Ainscough R, Almeida JP, Ambrose KD, Andrews DT, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Bannerjee R, Barlow KF, Bates K, Beasley H, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burrill W, Carder C, Carter NP, Chapman JC, Clamp ME, Clark SY, Clarke G, Clee CM, Clegg SC, Cobley V, Collins JE, Corby N, Coville GJ, Deloukas P, Dhami P, Dunham I, Dunn M, Earthrowl ME, Ellington AG, Faulkner L, Frankish AG, Frankland J, French L, Garner P, Garnett J, Gilbert JG, Gilson CJ, Ghori J, Grafham DV, Gribble SM, Griffiths C, Hall RE, Hammond S, Harley JL, Hart EA, Heath PD, Howden PJ, Huckle EJ, Hunt PJ, Hunt AR, Johnson C, Johnson D, Kay M, Kimberley AM, King A, Laird GK, Langford CJ, Lawlor S, Leongamornlert DA, Lloyd DM, Lloyd C, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, McLaren SJ, McMurray A, Milne S, Moore MJ, Nickerson T, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter KM, Rice CM, Searle S, Sehra HK, Shownkeen R, Skuce CD, Smith M, Steward CA, Sycamore N, Tester J, Thomas DW, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Wilming L, Wray PW, Wright MW, Young L, Coulson A, Durbin R, Hubbard T, Sulston JE, Beck S, Bentley DR, Rogers J, Ross MT: The DNA sequence and analysis of human chromosome 13. Nature. 2004 Apr 1;428(6982):522-8. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  5. Falandry C, Fourel G, Galy V, Ristriani T, Horard B, Bensimon E, Salles G, Gilson E, Magdinier F: CLLD8/KMT1F is a lysine methyltransferase that is important for chromosome segregation. J Biol Chem. 2010 Jun 25;285(26):20234-41. Epub 2010 Apr 19. [PubMed Link Image]
  6. 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 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 13061
Enzyme 34 Name Histamine N-methyltransferase
Enzyme 34 Synonyms
  1. SubName: Histamine N-methyltransferase, isoform CRA_b
Enzyme 34 Gene Name HNMT
Enzyme 34 Protein Sequence >Histamine N-methyltransferase
MASSMRSLFSDHGKYVESFRRFLNHSTEHQCMQEFMDKKLPGIIGRYQNCC
Enzyme 34 Number of Residues 51
Enzyme 34 Molecular Weight 6045.9
Enzyme 34 Theoretical pI 8.51
Enzyme 34 GO Classification Not Available
Enzyme 34 General Function Involved in methyltransferase activity
Enzyme 34 Specific Function Not Available
Enzyme 34 Pathways Not Available
Enzyme 34 Reactions Not Available
Enzyme 34 Pfam Domain Function Not Available
Enzyme 34 Signals
  • None
Enzyme 34 Transmembrane Regions
  • None
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein 13543497 Link Image
Enzyme 34 UniProtKB/Swiss-Prot ID Q9BRW6 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name Q9BRW6_HUMAN Link Image
Enzyme 34 PDB ID 1JQD Link Image
Enzyme 34 PDB File Show
Enzyme 34 3D Structure
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >156 bp
ATGGCATCTTCCATGAGGAGCTTGTTTTCTGACCACGGGAAATATGTTGAATCTTTCCGG
AGGTTTCTCAACCATTCCACGGAACACCAGTGCATGCAGGAATTCATGGACAAGAAGCTG
CCAGGCATAATAGGAAGATACCAGAATTGCTGTTAA
Enzyme 34 GenBank Gene ID BC005907 Link Image
Enzyme 34 GeneCard ID HNMT Link Image
Enzyme 34 GenAtlas ID HNMT Link Image
Enzyme 34 HGNC ID HGNC:5028 Link Image
Enzyme 34 Chromosome Location 2
Enzyme 34 Locus 2q22.1
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  2. Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed Link Image]
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 13068
Enzyme 35 Name cDNA FLJ76252, highly similar to Homo sapiens S-adenosylhomocysteine hydrolase
Enzyme 35 Synonyms
  1. AHCY, mRNA
  2. S-adenosylhomocysteine hydrolase, isoform CRA_a
Enzyme 35 Gene Name AHCY
Enzyme 35 Protein Sequence >cDNA FLJ76252, highly similar to Homo sapiens S-adenosylhomocysteine hydrolase
MSDKLPYKVADIGLAAWGRKALDIAENEMPGLMRMRERYSASKPLKGARIAGCLHMTVET
AVLIETLVTLGAEVQWSSCNIFSTQDHAAAAIAKAGIPVYAWKGETDEEYLWCIEQTLYF
KDGPLNMILDDGGDLTNLIHTKYPQLLPGIRGISEETTTGVHNLYKMMANGILKVPAINV
NDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVI
ITEIDPINALQAAMEGYEVTTMDEACQEGNIFVTTTGCIDIILGRHFEQMKDDAIVCNIG
HFDVEIDVKWLNENAVEKVNIKPQVDRYRLKNGRRIILLAEGRLVNLGCAMGHPSFVMSN
SFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVAEAHLGKLNVKLTKLTEKQAQYLGMS
CDGPFKPDHYRY
Enzyme 35 Number of Residues 432
Enzyme 35 Molecular Weight 47717
Enzyme 35 Theoretical pI 6.29
Enzyme 35 GO Classification Not Available
Enzyme 35 General Function Coenzyme transport and metabolism
Enzyme 35 Specific Function Not Available
Enzyme 35 Pathways Not Available
Enzyme 35 Reactions Not Available
Enzyme 35 Pfam Domain Function Not Available
Enzyme 35 Signals
  • None
Enzyme 35 Transmembrane Regions
  • None
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein 158261867 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID A8K307 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name A8K307_HUMAN Link Image
Enzyme 35 PDB ID 1LI4 Link Image
Enzyme 35 PDB File Show
Enzyme 35 3D Structure
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence Not Available
Enzyme 35 GenBank Gene ID AK290422 Link Image
Enzyme 35 GeneCard ID A8K307 Link Image
Enzyme 35 GenAtlas ID Not Available
Enzyme 35 HGNC ID Not Available
Enzyme 35 Chromosome Location Not Available
Enzyme 35 Locus Not Available
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References Not Available
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 14748
Enzyme 36 Name Probable histone-lysine N-methyltransferase ASH1L
Enzyme 36 Synonyms
  1. ASH1-like protein
  2. huASH1
  3. Absent small and homeotic disks protein 1 homolog
  4. Lysine N-methyltransferase 2H
Enzyme 36 Gene Name ASH1L
Enzyme 36 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 36 Number of Residues 2969
Enzyme 36 Molecular Weight 332787.2
Enzyme 36 Theoretical pI 9.95
Enzyme 36 GO Classification
Function
  • DNA binding
  • binding
  • catalytic activity
  • cation binding
  • histone-lysine N-methyltransferase activity
  • ion binding
  • metal ion binding
  • methyltransferase activity
  • nucleic acid binding
  • protein 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
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 36 General Function Involved in DNA binding
Enzyme 36 Specific Function Histone methyltransferase. Probably methylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation
Enzyme 36 Pathways
Enzyme 36 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • None
Enzyme 36 Transmembrane Regions
  • None
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein 7739725 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID Q9NR48 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name ASH1L_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 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 36 GenBank Gene ID AF257305 Link Image
Enzyme 36 GeneCard ID ASH1L Link Image
Enzyme 36 GenAtlas ID ASH1L Link Image
Enzyme 36 HGNC ID HGNC:19088 Link Image
Enzyme 36 Chromosome Location 1
Enzyme 36 Locus 1q22
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 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. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  3. 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]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Vasilescu J, Zweitzig DR, Denis NJ, Smith JC, Ethier M, Haines DS, Figeys D: The proteomic reactor facilitates the analysis of affinity-purified proteins by mass spectrometry: application for identifying ubiquitinated proteins in human cells. J Proteome Res. 2007 Jan;6(1):298-305. [PubMed Link Image]
  6. Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed Link Image]
  7. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  8. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 14750
Enzyme 37 Name Histone-arginine methyltransferase CARM1
Enzyme 37 Synonyms
  1. Coactivator-associated arginine methyltransferase 1
  2. Protein arginine N-methyltransferase 4
Enzyme 37 Gene Name CARM1
Enzyme 37 Protein Sequence >Histone-arginine methyltransferase CARM1
MAAAAAAVGPGAGGAGSAVPGGAGPCATVSVFPGARLLTIGDANGEIQRHAEQQALRLEV
RAGPDSAGIALYSHEDVCVFKCSVSRETECSRVGKQSFIITLGCNSVLIQFATPNDFCSF
YNILKTCRGHTLERSVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNH
TDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDRIVVIPG
KVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSGNMFPTIGDVHLAPFTDE
QLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEYFRQPVVDTFDIRILMAKSVKYTVNFL
EAKEGDLHRIEIPFKFHMLHSGLVHGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRC
LFQSPLFAKAGDTLSGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYTGTT
PSPPPGSHYTSPSENMWNTGSTYNLSSGMAVAGMPTAYDLSSVIASGSSVGHNNLIPLAN
TGIVNHTHSRMGSIMSTGIVQGSSGAQGSGGGSTSAHYAVNSQFTMGGPAISMASPMSIP
TNTMHYGS
Enzyme 37 Number of Residues 608
Enzyme 37 Molecular Weight 65853.2
Enzyme 37 Theoretical pI 6.73
Enzyme 37 GO Classification
Function
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • multi-organism process
  • pathogenesis
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 37 General Function Involved in pathogenesis
Enzyme 37 Specific Function Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, and mRNA stability. Recruited to promoters upon gene activation together with histone acetyltransferases from EP300/P300 and p160 families, methylates histone H3 at 'Arg-17' and activates transcription via chromatin remodeling. During nuclear hormone receptor activation and TCF7L2/TCF4 activation, acts synergically with EP300/P300 and either one of the p160 histone acetyltransferases NCOA1/SRC1, NCOA2/GRIP1 and NCOA3/ACTR or CTNNB1/beta-catenin to activate transcription. During myogenic transcriptional activation, acts together with NCOA3/ACTR as a coactivator for MEF2C. During monocyte inflammatory stimulation, acts together with EP300/P300 as a coactivator for NF-kappa-B. Also seems to be involved in p53/TP53 transcriptional activation. Methylates EP300/P300, both at 'Arg-2142', which may loosen its interaction with NCOA2/GRIP1, and at 'Arg-580' and 'Arg-604' in the KIX domain, which impairs its interaction with CREB and inhibits CREB-dependent transcriptional activation. Also methylates arginine residues in RNA-binding proteins PABPC1, ELAVL1 and ELAV4, which may affect their mRNA-stabilizing properties and the half-life of their target mRNAs
Enzyme 37 Pathways
Enzyme 37 Reactions
  • S-adenosyl-L-methionine + histone-arginine = S-adenosyl-L-homocysteine + histone-Nomega-methyl-arginine [RN:R04718]
Enzyme 37 Pfam Domain Function
Enzyme 37 Signals
  • None
Enzyme 37 Transmembrane Regions
  • None
Enzyme 37 Essentiality Not Available
Enzyme 37 GenBank ID Protein 40288288 Link Image
Enzyme 37 UniProtKB/Swiss-Prot ID Q86X55 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name CARM1_HUMAN Link Image
Enzyme 37 PDB ID Not Available
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence >1827 bp
ATGGCAGCGGCGGCGGCGGCGGTGGGGCCGGGCGCGGGCGGCGCGGGGTCGGCGGTCCCG
GGCGGCGCGGGGCCCTGCGCTACCGTGTCGGTGTTCCCCGGCGCCCGCCTCCTCACCATC
GGCGACGCGAACGGCGAGATCCAGCGGCACGCGGAGCAGCAGGCGCTGCGCCTCGAGGTG
CGCGCCGGCCCGGACTCGGCGGGCATCGCCCTCTACAGCCATGAAGATGTGTGTGTCTTT
AAGTGCTCAGTGTCCCGAGAGACAGAGTGCAGCCGTGTGGGCAAGCAGTCCTTCATCATC
ACCCTGGGCTGCAACAGCGTCCTCATCCAGTTCGCCACACCCAACGATTTCTGTTCCTTC
TACAACATCCTGAAAACCTGCCGGGGCCACACCCTGGAGCGGTCTGTGTTCAGCGAGCGG
ACGGAGGAGTCTTCTGCCGTGCAGTACTTCCAGTTTTATGGCTACCTGTCCCAGCAGCAG
AACATGATGCAGGACTACGTGCGGACAGGCACCTACCAGCGCGCCATCCTGCAAAACCAC
ACCGACTTCAAGGACAAGATCGTTCTTGATGTTGGCTGTGGCTCTGGGATCCTGTCGTTT
TTTGCCGCCCAAGCTGGAGCACGGAAAATCTACGCGGTGGAGGCCAGCACCATGGCCCAG
CACGCTGAGGTCTTGGTGAAGAGTAACAACCTGACGGACCGCATCGTGGTCATCCCGGGC
AAGGTGGAGGAGGTGTCACTCCCCGAGCAGGTGGACATCATCATCTCGGAGCCCATGGGC
TACATGCTCTTCAACGAGCGCATGCTGGAGAGCTACCTCCACGCCAAGAAGTACCTGAAG
CCCAGCGGAAACATGTTTCCTACCATTGGTGACGTCCACCTTGCACCCTTCACGGATGAA
CAGCTCTACATGGAGCAGTTCACCAAGGCCAACTTCTGGTACCAGCCATCTTTCCATGGA
GTGGACCTGTCGGCCCTCCGAGGTGCCGCGGTGGATGAGTATTTCCGGCAGCCTGTGGTG
GACACATTTGACATCCGGATCCTGATGGCCAAGTCTGTCAAGTACACGGTGAACTTCTTA
GAAGCCAAAGAAGGAGATTTGCACAGGATAGAAATCCCATTCAAATTCCACATGCTGCAT
TCAGGGCTGGTCCACGGCCTGGCTTTCTGGTTTGACGTTGCTTTCATCGGCTCCATAATG
ACCGTGTGGCTGTCCACAGCCCCGACAGAGCCCCTGACCCACTGGTACCAGGTGCGGTGC
CTGTTCCAGTCACCACTGTTCGCCAAGGCAGGGGACACGCTCTCAGGGACATGTCTGCTT
ATTGCCAACAAAAGACAGAGCTACGACATCAGTATTGTGGCCCAGGTGGACCAGACCGGC
TCCAAGTCCAGTAACCTCCTGGATCTGAAAAACCCCTTCTTTAGATACACGGGCACAACG
CCCTCACCCCCACCCGGCTCCCACTACACATCTCCCTCGGAAAACATGTGGAACACGGGC
AGCACCTACAACCTCAGCAGCGGGATGGCCGTGGCAGGGATGCCGACCGCCTATGACTTG
AGCAGTGTTATTGCCAGTGGCTCCAGCGTGGGCCACAACAACCTGATTCCTTTAGCCAAC
ACGGGGATTGTCAATCACACCCACTCCCGGATGGGCTCCATAATGAGCACGGGGATTGTC
CAAGGGTCCTCCGGCGCCCAGGGCAGTGGTGGTGGCAGCACGAGTGCCCACTATGCAGTC
AACAGCCAGTTCACCATGGGCGGCCCCGCCATCTCCATGGCGTCGCCCATGTCCATCCCG
ACCAACACCATGCACTACGGGAGCTAG
Enzyme 37 GenBank Gene ID NM_199141.1 Link Image
Enzyme 37 GeneCard ID CARM1 Link Image
Enzyme 37 GenAtlas ID CARM1 Link Image
Enzyme 37 HGNC ID HGNC:23393 Link Image
Enzyme 37 Chromosome Location 1
Enzyme 37 Locus 19p13.2
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 General References
  1. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. Li H, Park S, Kilburn B, Jelinek MA, Henschen-Edman A, Aswad DW, Stallcup MR, Laird-Offringa IA: Lipopolysaccharide-induced methylation of HuR, an mRNA-stabilizing protein, by CARM1. Coactivator-associated arginine methyltransferase. J Biol Chem. 2002 Nov 22;277(47):44623-30. Epub 2002 Sep 16. [PubMed Link Image]
  5. Hong H, Kao C, Jeng MH, Eble JN, Koch MO, Gardner TA, Zhang S, Li L, Pan CX, Hu Z, MacLennan GT, Cheng L: Aberrant expression of CARM1, a transcriptional coactivator of androgen receptor, in the development of prostate carcinoma and androgen-independent status. Cancer. 2004 Jul 1;101(1):83-9. [PubMed Link Image]
  6. Ananthanarayanan M, Li S, Balasubramaniyan N, Suchy FJ, Walsh MJ: Ligand-dependent activation of the farnesoid X-receptor directs arginine methylation of histone H3 by CARM1. J Biol Chem. 2004 Dec 24;279(52):54348-57. Epub 2004 Oct 6. [PubMed Link Image]
  7. Lee YH, Coonrod SA, Kraus WL, Jelinek MA, Stallcup MR: Regulation of coactivator complex assembly and function by protein arginine methylation and demethylimination. Proc Natl Acad Sci U S A. 2005 Mar 8;102(10):3611-6. Epub 2005 Feb 24. [PubMed Link Image]
  8. Jeong SJ, Lu H, Cho WK, Park HU, Pise-Masison C, Brady JN: Coactivator-associated arginine methyltransferase 1 enhances transcriptional activity of the human T-cell lymphotropic virus type 1 long terminal repeat through direct interaction with Tax. J Virol. 2006 Oct;80(20):10036-44. [PubMed Link Image]
  9. Miao F, Li S, Chavez V, Lanting L, Natarajan R: Coactivator-associated arginine methyltransferase-1 enhances nuclear factor-kappaB-mediated gene transcription through methylation of histone H3 at arginine 17. Mol Endocrinol. 2006 Jul;20(7):1562-73. Epub 2006 Feb 23. [PubMed Link Image]
  10. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 14754
Enzyme 38 Name Histone-lysine N-methyltransferase EZH2
Enzyme 38 Synonyms
  1. ENX-1
  2. Enhancer of zeste homolog 2
  3. Lysine N-methyltransferase 6
Enzyme 38 Gene Name EZH2
Enzyme 38 Protein Sequence >Histone-lysine N-methyltransferase EZH2
MGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKSMFSSNRQKILERTEILNQEW
KQRRIQPVHILTSVSSLRGTRECSVTSDLDFPTQVIPLKTLNAVASVPIMYSWSPLQQNF
MVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQ
YNDDDDDDDGDDPEEREEKQKDLEDHRDDKESRPPRKFPSDKIFEAISSMFPDKGTAEEL
KEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFH
ATPNTYKRKNTETALDNKPCGPQCYQHLEGAKEFAAALTAERIKTPPKRPGGRRRGRLPN
NSSRPSTPTINVLESKDTDSDREAGTETGGENNDKEEEEKKDETSSSSEANSRCQTPIKM
KPNIEPPENVEWSGAEASMFRVLIGTYYDNFCAIARLIGTKTCRQVYEFRVKESSIIAPA
PAEDVDTPPRKKKRKHRLWAAHCRKIQLKKDGSSNHVYNYQPCDHPRQPCDSSCPCVIAQ
NFCEKFCQCSSECQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCLTCGAADHWDSKNVS
CKNCSIQRGSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDK
YMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGE
ELFFDYRYSQADALKYVGIEREMEIP
Enzyme 38 Number of Residues 746
Enzyme 38 Molecular Weight 85362.4
Enzyme 38 Theoretical pI 7.01
Enzyme 38 GO Classification
Function
  • DNA binding
  • binding
  • nucleic acid binding
Process
Component
Enzyme 38 General Function Involved in DNA binding
Enzyme 38 Specific Function Polycomb group (PcG) protein. Catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' and 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. Able to mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. Compared to EZH2-containing complexes, it is more abundant in embryonic stem cells and plays a major role in forming H3K27me3, which is required for embryonic stem cell identity and proper differentiation. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1, CDKN2A and retinoic acid target genes
Enzyme 38 Pathways Not Available
Enzyme 38 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 38 Pfam Domain Function
Enzyme 38 Signals
  • None
Enzyme 38 Transmembrane Regions
  • None
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein 1575349 Link Image
Enzyme 38 UniProtKB/Swiss-Prot ID Q15910 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name EZH2_HUMAN Link Image
Enzyme 38 PDB ID Not Available
Enzyme 38 Cellular Location Not Available
Enzyme 38 Gene Sequence >2241 bp
ATGGGCCAGACTGGGAAGAAATCTGAGAAGGGACCAGTTTGTTGGCGGAAGCGTGTAAAA
TCAGAGTACATGCGACTGAGACAGCTCAAGAGGTTCAGACGAGCTGATGAAGTAAAGAGT
ATGTTTAGTTCCAATCGTCAGAAAATTTTGGAAAGAACGGAAATCTTAAACCAAGAATGG
AAACAGCGAAGGATACAGCCTGTGCACATCCTGACTTCTGTGAGCTCATTGCGCGGGACT
AGGGAGTGTTCGGTGACCAGTGACTTGGATTTTCCAACACAAGTCATCCCATTAAAGACT
CTGAATGCAGTTGCTTCAGTACCCATAATGTATTCTTGGTCTCCCCTACAGCAGAATTTT
ATGGTGGAAGATGAAACTGTTTTACATAACATTCCTTATATGGGAGATGAAGTTTTAGAT
CAGGATGGTACTTTCATTGAAGAACTAATAAAAAATTATGATGGGAAAGTACACGGGGAT
AGAGAATGTGGGTTTATAAATGATGAAATTTTTGTGGAGTTGGTGAATGCCCTTGGTCAA
TATAATGATGATGACGATGATGATGATGGAGACGATCCTGAAGAAAGAGAAGAAAAGCAG
AAAGATCTGGAGGATCACCGAGATGATAAAGAAAGCCGCCCACCTCGGAAATTTCCTTCT
GATAAAATTTTTGAAGCCATTTCCTCAATGTTTCCAGATAAGGGCACAGCAGAAGAACTA
AAGGAAAAATATAAAGAACTCACCGAACAGCAGCTCCCAGGCGCACTTCCTCCTGAATGT
ACCCCCAACATAGATGGACCAAATGCTAAATCTGTTCAGAGAGAGCAAAGCTTACACTCC
TTTCATACGCTTTTCTGTAGGCGATGTTTTAAATATGACTGCTTCCTACATCCTTTTCAT
GCAACACCCAACACTTATAAGCGGAAGAACACAGAAACAGCTCTAGACAACAAACCTTGT
GGACCACAGTGTTACCAGCATTTGGAGGGAGCAAAGGAGTTTGCTGCTGCTCTCACCGCT
GAGCGGATAAAGACCCCACCAAAACGTCCAGGAGGCCGCAGAAGAGGACGGCTTCCCAAT
AACAGTAGCAGGCCCAGCACCCCCACCATTAATGTGCTGGAATCAAAGGATACAGACAGT
GATAGGGAAGCAGGGACTGAAACGGGGGGAGAGAACAATGATAAAGAAGAAGAAGAGAAG
AAAGATGAAACTTCGAGCTCCTCTGAAGCAAATTCTCGGTGTCAAACACCAATAAAGATG
AAGCCAAATATTGAACCTCCTGAGAATGTGGAGTGGAGTGGTGCTGAAGCCTCAATGTTT
AGAGTCCTCATTGGCACTTACTATGACAATTTCTGTGCCATTGCTAGGTTAATTGGGACC
AAAACATGTAGACAGGTGTATGAGTTTAGAGTCAAAGAATCTAGCATCATAGCTCCAGCT
CCCGCTGAGGATGTGGATACTCCTCCAAGGAAAAAGAAGAGGAAACACCGGTTGTGGGCT
GCACACTGCAGAAAGATACAGCTGAAAAAGGACGGCTCCTCTAACCATGTTTACAACTAT
CAACCCTGTGATCATCCACGGCAGCCTTGTGACAGTTCGTGCCCTTGTGTGATAGCACAA
AATTTTTGTGAAAAGTTTTGTCAATGTAGTTCAGAGTGTCAAAACCGCTTTCCGGGATGC
CGCTGCAAAGCACAGTGCAACACCAAGCAGTGCCCGTGCTACCTGGCTGTCCGAGAGTGT
GACCCTGACCTCTGTCTTACTTGTGGAGCCGCTGACCATTGGGACAGTAAAAATGTGTCC
TGCAAGAACTGCAGTATTCAGCGGGGCTCCAAAAAGCATCTATTGCTGGCACCATCTGAC
GTGGCAGGCTGGGGGATTTTTATCAAAGATCCTGTGCAGAAAAATGAATTCATCTCAGAA
TACTGTGGAGAGATTATTTCTCAAGATGAAGCTGACAGAAGAGGGAAAGTGTATGATAAA
TACATGTGCAGCTTTCTGTTCAACTTGAACAATGATTTTGTGGTGGATGCAACCCGCAAG
GGTAACAAAATTCGTTTTGCAAATCATTCGGTAAATCCAAACTGCTATGCAAAAGTTATG
ATGGTTAACGGTGATCACAGGATAGGTATTTTTGCCAAGAGAGCCATCCAGACTGGCGAA
GAGCTGTTTTTTGATTACAGATACAGCCAGGCTGATGCCCTGAAGTATGTCGGCATCGAA
AGAGAAATGGAAATCCCTTGA
Enzyme 38 GenBank Gene ID U61145 Link Image
Enzyme 38 GeneCard ID EZH2 Link Image
Enzyme 38 GenAtlas ID EZH2 Link Image
Enzyme 38 HGNC ID HGNC:3527 Link Image
Enzyme 38 Chromosome Location 7
Enzyme 38 Locus 7q35-q36
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 General References
  1. Chen H, Rossier C, Antonarakis SE: Cloning of a human homolog of the Drosophila enhancer of zeste gene (EZH2) that maps to chromosome 21q22.2. Genomics. 1996 Nov 15;38(1):30-7. [PubMed Link Image]
  2. Laible G, Wolf A, Dorn R, Reuter G, Nislow C, Lebersorger A, Popkin D, Pillus L, Jenuwein T: Mammalian homologues of the Polycomb-group gene Enhancer of zeste mediate gene silencing in Drosophila heterochromatin and at S. cerevisiae telomeres. EMBO J. 1997 Jun 2;16(11):3219-32. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. 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]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Hobert O, Jallal B, Ullrich A: Interaction of Vav with ENX-1, a putative transcriptional regulator of homeobox gene expression. Mol Cell Biol. 1996 Jun;16(6):3066-73. [PubMed Link Image]
  7. Cardoso C, Timsit S, Villard L, Khrestchatisky M, Fontes M, Colleaux L: Specific interaction between the XNP/ATR-X gene product and the SET domain of the human EZH2 protein. Hum Mol Genet. 1998 Apr;7(4):679-84. [PubMed Link Image]
  8. Sewalt RG, van der Vlag J, Gunster MJ, Hamer KM, den Blaauwen JL, Satijn DP, Hendrix T, van Driel R, Otte AP: Characterization of interactions between the mammalian polycomb-group proteins Enx1/EZH2 and EED suggests the existence of different mammalian polycomb-group protein complexes. Mol Cell Biol. 1998 Jun;18(6):3586-95. [PubMed Link Image]
  9. van der Vlag J, Otte AP: Transcriptional repression mediated by the human polycomb-group protein EED involves histone deacetylation. Nat Genet. 1999 Dec;23(4):474-8. [PubMed Link Image]
  10. Satijn DP, Hamer KM, den Blaauwen J, Otte AP: The polycomb group protein EED interacts with YY1, and both proteins induce neural tissue in Xenopus embryos. Mol Cell Biol. 2001 Feb;21(4):1360-9. [PubMed Link Image]
  11. Kuzmichev A, Nishioka K, Erdjument-Bromage H, Tempst P, Reinberg D: Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein. Genes Dev. 2002 Nov 15;16(22):2893-905. [PubMed Link Image]
  12. Sewalt RG, Lachner M, Vargas M, Hamer KM, den Blaauwen JL, Hendrix T, Melcher M, Schweizer D, Jenuwein T, Otte AP: Selective interactions between vertebrate polycomb homologs and the SUV39H1 histone lysine methyltransferase suggest that histone H3-K9 methylation contributes to chromosomal targeting of Polycomb group proteins. Mol Cell Biol. 2002 Aug;22(15):5539-53. [PubMed Link Image]
  13. Cao R, Wang L, Wang H, Xia L, Erdjument-Bromage H, Tempst P, Jones RS, Zhang Y: Role of histone H3 lysine 27 methylation in Polycomb-group silencing. Science. 2002 Nov 1;298(5595):1039-43. Epub 2002 Sep 26. [PubMed Link Image]
  14. Bracken AP, Pasini D, Capra M, Prosperini E, Colli E, Helin K: EZH2 is downstream of the pRB-E2F pathway, essential for proliferation and amplified in cancer. EMBO J. 2003 Oct 15;22(20):5323-35. [PubMed Link Image]
  15. Pasini D, Bracken AP, Jensen MR, Lazzerini Denchi E, Helin K: Suz12 is essential for mouse development and for EZH2 histone methyltransferase activity. EMBO J. 2004 Oct 13;23(20):4061-71. Epub 2004 Sep 23. [PubMed Link Image]
  16. Kirmizis A, Bartley SM, Kuzmichev A, Margueron R, Reinberg D, Green R, Farnham PJ: Silencing of human polycomb target genes is associated with methylation of histone H3 Lys 27. Genes Dev. 2004 Jul 1;18(13):1592-605. [PubMed Link Image]
  17. Kuzmichev A, Jenuwein T, Tempst P, Reinberg D: Different EZH2-containing complexes target methylation of histone H1 or nucleosomal histone H3. Mol Cell. 2004 Apr 23;14(2):183-93. [PubMed Link Image]
  18. Cao R, Zhang Y: SUZ12 is required for both the histone methyltransferase activity and the silencing function of the EED-EZH2 complex. Mol Cell. 2004 Jul 2;15(1):57-67. [PubMed Link Image]
  19. Tang X, Milyavsky M, Shats I, Erez N, Goldfinger N, Rotter V: Activated p53 suppresses the histone methyltransferase EZH2 gene. Oncogene. 2004 Jul 29;23(34):5759-69. [PubMed Link Image]
  20. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  21. Epping MT, Wang L, Edel MJ, Carlee L, Hernandez M, Bernards R: The human tumor antigen PRAME is a dominant repressor of retinoic acid receptor signaling. Cell. 2005 Sep 23;122(6):835-47. [PubMed Link Image]
  22. Kuzmichev A, Margueron R, Vaquero A, Preissner TS, Scher M, Kirmizis A, Ouyang X, Brockdorff N, Abate-Shen C, Farnham P, Reinberg D: Composition and histone substrates of polycomb repressive group complexes change during cellular differentiation. Proc Natl Acad Sci U S A. 2005 Feb 8;102(6):1859-64. Epub 2005 Jan 31. [PubMed Link Image]
  23. Cha TL, Zhou BP, Xia W, Wu Y, Yang CC, Chen CT, Ping B, Otte AP, Hung MC: Akt-mediated phosphorylation of EZH2 suppresses methylation of lysine 27 in histone H3. Science. 2005 Oct 14;310(5746):306-10. [PubMed Link Image]
  24. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  25. Bracken AP, Dietrich N, Pasini D, Hansen KH, Helin K: Genome-wide mapping of Polycomb target genes unravels their roles in cell fate transitions. Genes Dev. 2006 May 1;20(9):1123-36. Epub 2006 Apr 17. [PubMed Link Image]
  26. Martin C, Cao R, Zhang Y: Substrate preferences of the EZH2 histone methyltransferase complex. J Biol Chem. 2006 Mar 31;281(13):8365-70. Epub 2006 Jan 23. [PubMed Link Image]
  27. Vire E, Brenner C, Deplus R, Blanchon L, Fraga M, Didelot C, Morey L, Van Eynde A, Bernard D, Vanderwinden JM, Bollen M, Esteller M, Di Croce L, de Launoit Y, Fuks F: The Polycomb group protein EZH2 directly controls DNA methylation. Nature. 2006 Feb 16;439(7078):871-4. Epub 2005 Dec 14. [PubMed Link Image]
  28. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  29. Kim DH, Villeneuve LM, Morris KV, Rossi JJ: Argonaute-1 directs siRNA-mediated transcriptional gene silencing in human cells. Nat Struct Mol Biol. 2006 Sep;13(9):793-7. Epub 2006 Aug 27. [PubMed Link Image]
  30. Nousiainen M, Sillje HH, Sauer G, Nigg EA, Korner R: Phosphoproteome analysis of the human mitotic spindle. Proc Natl Acad Sci U S A. 2006 Apr 4;103(14):5391-6. Epub 2006 Mar 24. [PubMed Link Image]
  31. Kotake Y, Cao R, Viatour P, Sage J, Zhang Y, Xiong Y: pRB family proteins are required for H3K27 trimethylation and Polycomb repression complexes binding to and silencing p16INK4alpha tumor suppressor gene. Genes Dev. 2007 Jan 1;21(1):49-54. [PubMed Link Image]
  32. Bracken AP, Kleine-Kohlbrecher D, Dietrich N, Pasini D, Gargiulo G, Beekman C, Theilgaard-Monch K, Minucci S, Porse BT, Marine JC, Hansen KH, Helin K: The Polycomb group proteins bind throughout the INK4A-ARF locus and are disassociated in senescent cells. Genes Dev. 2007 Mar 1;21(5):525-30. [PubMed Link Image]
  33. Schlesinger Y, Straussman R, Keshet I, Farkash S, Hecht M, Zimmerman J, Eden E, Yakhini Z, Ben-Shushan E, Reubinoff BE, Bergman Y, Simon I, Cedar H: Polycomb-mediated methylation on Lys27 of histone H3 pre-marks genes for de novo methylation in cancer. Nat Genet. 2007 Feb;39(2):232-6. Epub 2006 Dec 31. [PubMed Link Image]
  34. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
  35. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  36. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  37. Margueron R, Li G, Sarma K, Blais A, Zavadil J, Woodcock CL, Dynlacht BD, Reinberg D: Ezh1 and Ezh2 maintain repressive chromatin through different mechanisms. Mol Cell. 2008 Nov 21;32(4):503-18. [PubMed Link Image]
  38. Cao R, Wang H, He J, Erdjument-Bromage H, Tempst P, Zhang Y: Role of hPHF1 in H3K27 methylation and Hox gene silencing. Mol Cell Biol. 2008 Mar;28(5):1862-72. Epub 2007 Dec 17. [PubMed Link Image]
  39. Sarma K, Margueron R, Ivanov A, Pirrotta V, Reinberg D: Ezh2 requires PHF1 to efficiently catalyze H3 lysine 27 trimethylation in vivo. Mol Cell Biol. 2008 Apr;28(8):2718-31. Epub 2008 Feb 19. [PubMed Link Image]
  40. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  41. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  42. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 14757
Enzyme 39 Name mRNA cap guanine-N7 methyltransferase
Enzyme 39 Synonyms
  1. RG7MT1
  2. mRNA (guanine-N(7)-)-methyltransferase
  3. mRNA cap methyltransferase
  4. hCMT1
  5. hMet
  6. hcm1p
Enzyme 39 Gene Name RNMT
Enzyme 39 Protein Sequence >mRNA cap guanine-N7 methyltransferase
MANSAKAEEYEKMSLEQAKASVNSETESSFNINENTTASGTGLSEKTSVCRQVDIARKRK
EFEDDLVKESSSCGKDTPSKKRKLDPEIVPEEKDCGDAEGNSKKRKRETEDVPKDKSSTG
DGTQNKRKIALEDVPEKQKNLEEGHSSTVAAHYNELQEVGLEKRSQSRIFYLRNFNNWMK
SVLIGEFLEKVRQKKKRDITVLDLGCGKGGDLLKWKKGRINKLVCTDIADVSVKQCQQRY
EDMKNRRDSEYIFSAEFITADSSKELLIDKFRDPQMCFDICSCQFVCHYSFESYEQADMM
LRNACERLSPGGYFIGTTPNSFELIRRLEASETESFGNEIYTVKFQKKGDYPLFGCKYDF
NLEGVVDVPEFLVYFPLLNEMAKKYNMKLVYKKTFLEFYEEKIKNNENKMLLKRMQALEP
YPANESSKLVSEKVDDYEHAAKYMKNSQVRLPLGTLSKSEWEATSIYLVFAFEKQQ
Enzyme 39 Number of Residues 476
Enzyme 39 Molecular Weight 54843.7
Enzyme 39 Theoretical pI 6.54
Enzyme 39 GO Classification
Function
Process
  • RNA metabolic process
  • RNA processing
  • cellular macromolecule metabolic process
  • mRNA capping
  • mRNA processing
  • macromolecule metabolic process
  • metabolic process
Component
Enzyme 39 General Function Involved in mRNA capping
Enzyme 39 Specific Function mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC
Enzyme 39 Pathways Not Available
Enzyme 39 Reactions
  • S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA (mRNA containing an N7-methylguanine cap) [RN:R03805]
Enzyme 39 Pfam Domain Function
Enzyme 39 Signals
  • None
Enzyme 39 Transmembrane Regions
  • None
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein 2662077 Link Image
Enzyme 39 UniProtKB/Swiss-Prot ID O43148 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name MCES_HUMAN Link Image
Enzyme 39 PDB ID Not Available
Enzyme 39 Cellular Location Not Available
Enzyme 39 Gene Sequence >1431 bp
ATGGCAAATTCTGCAAAAGCAGAAGAATATGAAAAGATGTCTCTTGAACAGGCAAAAGCG
TCAGTGAATTCTGAAACAGAGTCTTCATTCAATATTAATGAAAACACAACAGCTTCTGGG
ACTGGGCTTTCTGAAAAGACTTCTGTCTGTAGGCAAGTAGACATAGCAAGAAAGAGAAAA
GAGTTTGAAGATGATCTTGTAAAGGAAAGTTCTAGTTGTGGGAAAGACACTCCATCCAAG
AAGAGAAAACTTGATCCTGAAATTGTCCCAGAGGAAAAAGATTGTGGTGATGCTGAAGGC
AATTCAAAGAAAAGAAAAAGAGAAACTGAGGATGTTCCAAAAGATAAATCTTCTACTGGA
GATGGCACTCAAAATAAGAGAAAAATAGCACTTGAGGATGTTCCTGAAAAGCAGAAAAAT
CTGGAAGAAGGACACAGCTCAACAGTGGCTGCCCATTACAATGAACTTCAGGAAGTTGGT
TTGGAGAAGCGTAGTCAAAGTCGTATTTTTTACCTAAGAAACTTTAATAATTGGATGAAA
AGTGTTCTCATTGGAGAATTTTTGGAAAAGGTACGACAGAAGAAAAAACGTGATATCACT
GTTTTGGACCTGGGATGTGGTAAAGGTGGAGATTTGCTGAAATGGAAAAAAGGAAGAATT
AACAAGCTAGTTTGTACTGATATTGCCGATGTTTCTGTCAAACAGTGTCAGCAGCGGTAT
GAGGACATGAAAAATCGTCGTGATAGTGAATATATTTTCAGTGCAGAATTTATAACTGCT
GACAGCTCAAAGGAACTTCTGATTGACAAATTTCGTGACCCACAAATGTGTTTTGACATC
TGCAGTTGTCAGTTTGTCTGTCATTACTCATTTGAGTCTTATGAGCAGGCTGACATGATG
CTGAGAAATGCGTGTGAGAGACTTAGCCCTGGGGGCTATTTTATTGGTACTACTCCCAAT
AGCTTTGAATTGATAAGACGCCTTGAAGCTTCAGAAACAGAATCATTTGGAAATGAAATA
TATACTGTGAAATTTCAGAAGAAAGGAGATTATCCTTTATTTGGCTGCAAATATGACTTC
AACTTGGAAGGTGTTGTGGATGTTCCTGAATTCTTGGTCTATTTTCCATTGCTAAATGAA
ATGGCAAAGAAGTACAATATGAAACTAGTCTACAAAAAAACATTTCTGGAATTCTACGAA
GAAAAGATTAAGAACAATGAAAATAAAATGCTCTTAAAACGAATGCAGGCCTTGGAGCCA
TATCCTGCAAATGAGAGTTCTAAACTTGTCTCTGAGAAGGTGGATGACTATGAACATGCA
GCAAAGTACATGAAGAACAGTCAAGTAAGGTTACCTTTGGGAACCTTAAGTAAATCAGAA
TGGGAAGCTACAAGTATTTACTTGGTGTTTGCCTTTGAGAAACAGCAGTGA
Enzyme 39 GenBank Gene ID AB007858 Link Image
Enzyme 39 GeneCard ID RNMT Link Image
Enzyme 39 GenAtlas ID RNMT Link Image
Enzyme 39 HGNC ID HGNC:10075 Link Image
Enzyme 39 Chromosome Location 1
Enzyme 39 Locus 18p11.21
Enzyme 39 SNPs SNPJam Report Link Image
Enzyme 39 General References
  1. Tsukamoto T, Shibagaki Y, Niikura Y, Mizumoto K: Cloning and characterization of three human cDNAs encoding mRNA (guanine-7-)-methyltransferase, an mRNA cap methylase. Biochem Biophys Res Commun. 1998 Oct 9;251(1):27-34. [PubMed Link Image]
  2. Pillutla RC, Yue Z, Maldonado E, Shatkin AJ: Recombinant human mRNA cap methyltransferase binds capping enzyme/RNA polymerase IIo complexes. J Biol Chem. 1998 Aug 21;273(34):21443-6. [PubMed Link Image]
  3. Yamada-Okabe T, Mio T, Kashima Y, Matsui M, Arisawa M, Yamada-Okabe H: The Candida albicans gene for mRNA 5-cap methyltransferase: identification of additional residues essential for catalysis. Microbiology. 1999 Nov;145 ( Pt 11):3023-33. [PubMed Link Image]
  4. Ishikawa K, Nagase T, Nakajima D, Seki N, Ohira M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1997 Oct 31;4(5):307-13. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Saha N, Schwer B, Shuman S: Characterization of human, Schizosaccharomyces pombe, and Candida albicans mRNA cap methyltransferases and complete replacement of the yeast capping apparatus by mammalian enzymes. J Biol Chem. 1999 Jun 4;274(23):16553-62. [PubMed Link Image]
  7. Wen Y, Shatkin AJ: Cap methyltransferase selective binding and methylation of GpppG-RNA are stimulated by importin-alpha. Genes Dev. 2000 Dec 1;14(23):2944-9. [PubMed Link Image]
  8. Shafer B, Chu C, Shatkin AJ: Human mRNA cap methyltransferase: alternative nuclear localization signal motifs ensure nuclear localization required for viability. Mol Cell Biol. 2005 Apr;25(7):2644-9. [PubMed Link Image]
Enzyme 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 14764
Enzyme 40 Name Probable histone-lysine N-methyltransferase NSD2
Enzyme 40 Synonyms
  1. Multiple myeloma SET domain-containing protein
  2. Nuclear SET domain-containing protein 2
  3. Protein trithorax-5
  4. Wolf-Hirschhorn syndrome candidate 1 protein
Enzyme 40 Gene Name WHSC1
Enzyme 40 Protein Sequence >Probable histone-lysine N-methyltransferase NSD2
MEFSIKQSPLSVQSVVKCIKMKQAPEILGSANGKTPSCEVNRECSVFLSKAQLSSSLQEG
VMQKFNGHDALPFIPADKLKDLTSRVFNGEPGAHDAKLRFESQEMKGIGTPPNTTPIKNG
SPEIKLKITKTYMNGKPLFESSICGDSAADVSQSEENGQKPENKARRNRKRSIKYDSLLE
QGLVEAALVSKISSPSDKKIPAKKESCPNTGRDKDHLLKYNVGDLVWSKVSGYPWWPCMV
SADPLLHSYTKLKGQKKSARQYHVQFFGDAPERAWIFEKSLVAFEGEGQFEKLCQESAKQ
APTKAEKIKLLKPISGKLRAQWEMGIVQAEEAASMSVEERKAKFTFLYVGDQLHLNPQVA
KEAGIAAESLGEMAESSGVSEEAAENPKSVREECIPMKRRRRAKLCSSAETLESHPDIGK
STPQKTAEADPRRGVGSPPGRKKTTVSMPRSRKGDAASQFLVFCQKHRDEVVAEHPDASG
EEIEELLRSQWSLLSEKQRARYNTKFALVAPVQAEEDSGNVNGKKRNHTKRIQDPTEDAE
AEDTPRKRLRTDKHSLRKRDTITDKTARTSSYKAMEAASSLKSQAATKNLSDACKPLKKR
NRASTAASSALGFSKSSSPSASLTENEVSDSPGDEPSESPYESADETQTEVSVSSKKSER
GVTAKKEYVCQLCEKPGSLLLCEGPCCGAFHLACLGLSRRPEGRFTCSECASGIHSCFVC
KESKTDVKRCVVTQCGKFYHEACVKKYPLTVFESRGFRCPLHSCVSCHASNPSNPRPSKG
KMMRCVRCPVAYHSGDACLAAGCSVIASNSIICTAHFTARKGKRHHAHVNVSWCFVCSKG
GSLLCCESCPAAFHPDCLNIEMPDGSWFCNDCRAGKKLHFQDIIWVKLGNYRWWPAEVCH
PKNVPPNIQKMKHEIGEFPVFFFGSKDYYWTHQARVFPYMEGDRGSRYQGVRGIGRVFKN
ALQEAEARFREIKLQREARETQESERKPPPYKHIKVNKPYGKVQIYTADISEIPKCNCKP
TDENPCGFDSECLNRMLMFECHPQVCPAGEFCQNQCFTKRQYPETKIIKTDGKGWGLVAK
RDIRKGEFVNEYVGELIDEEECMARIKHAHENDITHFYMLTIDKDRIIDAGPKGNYSRFM
NHSCQPNCETLKWTVNGDTRVGLFAVCDIPAGTELTFNYNLDCLGNEKTVCRCGASNCSG
FLGDRPKTSTTLSSEEKGKKTKKKTRRRRAKGEGKRQSEDECFRCGDGGQLVLCDRKFCT
KAYHLSCLGLGKRPFGKWECPWHHCDVCGKPSTSFCHLCPNSFCKEHQDGTAFSCTPDGR
SYCCEHDLGAASVRSTKTEKPPPEPGKPKGKRRRRRGWRRVTEGK
Enzyme 40 Number of Residues 1365
Enzyme 40 Molecular Weight 152257.0
Enzyme 40 Theoretical pI 8.81
Enzyme 40 GO Classification
Function
  • DNA binding
  • binding
  • catalytic activity
  • cation binding
  • histone-lysine N-methyltransferase activity
  • ion binding
  • metal ion binding
  • methyltransferase activity
  • nucleic acid binding
  • protein 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
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 40 General Function Involved in histone-lysine N-methyltransferase activity
Enzyme 40 Specific Function Probable histone methyltransferase. May act as a transcription regulator that binds DNA and suppresses IL5 transcription
Enzyme 40 Pathways
Enzyme 40 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 40 Pfam Domain Function
Enzyme 40 Signals
  • None
Enzyme 40 Transmembrane Regions
  • None
Enzyme 40 Essentiality Not Available
Enzyme 40 GenBank ID Protein 109633019 Link Image
Enzyme 40 UniProtKB/Swiss-Prot ID O96028 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name NSD2_HUMAN Link Image
Enzyme 40 PDB ID Not Available
Enzyme 40 Cellular Location Not Available
Enzyme 40 Gene Sequence >4098 bp
ATGGAATTTAGCATCAAGCAGAGTCCCCTTTCTGTTCAGAGTGTTGTAAAGTGCATAAAG
ATGAAGCAGGCACCAGAAATCCTCGGCAGTGCCAACGGGAAGACTCCGAGCTGCGAGGTG
AACCGCGAGTGTTCTGTGTTCCTCAGCAAAGCCCAGCTCTCCAGTAGCCTGCAGGAGGGG
GTCATGCAGAAGTTTAACGGCCACGACGCCCTGCCCTTTATTCCAGCCGACAAGCTGAAA
GATCTTACTTCCCGGGTGTTTAATGGAGAACCCGGCGCACACGATGCCAAACTGCGTTTT
GAGTCCCAGGAAATGAAAGGGATTGGGACACCCCCTAACACTACCCCTATCAAAAATGGC
TCTCCAGAAATTAAGCTGAAAATCACCAAAACATACATGAATGGGAAGCCTCTCTTTGAA
TCTTCCATTTGTGGTGACAGTGCTGCTGATGTGTCTCAGTCAGAAGAAAATGGACAAAAA
CCAGAAAACAAGGCGAGAAGGAACAGGAAGAGGAGCATAAAATATGACTCCTTGCTGGAG
CAGGGCCTTGTCGAAGCAGCTCTTGTGTCTAAGATCTCAAGTCCTTCAGATAAAAAGATT
CCAGCTAAGAAAGAGTCTTGTCCAAACACTGGAAGAGACAAAGACCACCTGTTGAAATAC
AACGTTGGTGATTTGGTGTGGTCCAAAGTGTCGGGTTACCCTTGGTGGCCTTGCATGGTT
TCTGCAGATCCACTCCTTCACAGCTATACCAAACTTAAAGGTCAGAAAAAGAGTGCACGC
CAGTATCACGTACAGTTCTTTGGTGACGCCCCAGAAAGAGCTTGGATATTTGAGAAGAGC
CTCGTAGCTTTTGAAGGAGAAGGACAGTTTGAAAAATTATGCCAGGAAAGTGCCAAGCAG
GCACCCACGAAAGCTGAGAAAATTAAGCTATTGAAACCAATTTCAGGGAAATTGAGGGCC
CAGTGGGAAATGGGCATTGTTCAAGCAGAAGAAGCTGCAAGCATGTCAGTGGAGGAGCGG
AAAGCCAAGTTCACCTTTCTCTATGTGGGGGACCAGCTTCATCTCAACCCTCAAGTAGCC
AAGGAGGCTGGCATTGCTGCAGAGTCTTTGGGAGAAATGGCAGAATCCTCAGGAGTCAGT
GAAGAAGCTGCTGAAAACCCCAAGTCTGTGAGAGAAGAGTGCATTCCCATGAAGAGAAGG
CGGAGGGCCAAACTGTGTAGCTCTGCAGAGACCCTGGAGAGTCACCCCGACATAGGGAAG
AGTACTCCTCAAAAGACGGCAGAGGCTGACCCCAGAAGAGGAGTAGGGTCTCCTCCTGGG
AGGAAGAAGACCACAGTCTCCATGCCACGAAGCAGGAAGGGAGATGCAGCATCCCAGTTT
TTGGTCTTCTGTCAAAAACACAGGGATGAGGTGGTAGCTGAGCACCCAGATGCTTCAGGT
GAGGAGATTGAAGAGCTGCTCAGGTCACAGTGGAGTCTGCTGAGTGAGAAGCAGAGAGCA
CGCTACAACACCAAGTTTGCCCTGGTGGCCCCTGTCCAGGCTGAAGAAGACTCTGGTAAT
GTAAATGGGAAAAAAAGAAACCACACAAAGAGGATACAGGACCCTACAGAAGATGCTGAA
GCTGAGGACACACCCAGGAAAAGACTCAGGACGGACAAGCACAGTCTTCGGAAGAGAGAC
ACAATCACTGACAAAACGGCCAGAACAAGCTCTTACAAGGCCATGGAGGCAGCCTCCTCG
CTCAAGAGCCAGGCAGCAACGAAAAATCTGTCTGATGCATGTAAACCACTGAAGAAGCGA
AATCGGGCTTCCACGGCAGCATCTTCAGCTCTTGGGTTTAGCAAAAGTTCATCTCCTTCT
GCATCCTTAACTGAGAATGAGGTCTCGGACAGCCCGGGAGACGAGCCCTCGGAGTCCCCA
TACGAAAGTGCAGACGAAACACAAACTGAAGTATCTGTCTCATCCAAAAAGTCTGAGCGA
GGAGTGACTGCCAAAAAGGAGTATGTGTGCCAGCTGTGTGAGAAGCCGGGCAGCCTCCTG
CTCTGTGAAGGACCCTGCTGCGGAGCTTTCCACCTCGCCTGCCTTGGGCTTTCCCGGAGG
CCAGAAGGGAGGTTCACCTGCAGCGAGTGTGCCTCAGGGATTCACTCATGTTTCGTGTGT
AAAGAGAGCAAGACAGATGTTAAGCGCTGTGTGGTAACTCAGTGTGGAAAATTTTACCAT
GAGGCTTGTGTGAAAAAATACCCTCTGACTGTATTTGAGAGCCGAGGTTTCCGCTGCCCC
CTCCACAGCTGTGTGAGCTGCCATGCTTCCAACCCTTCAAACCCAAGGCCGTCAAAAGGT
AAAATGATGCGGTGTGTCCGCTGCCCCGTTGCCTATCACAGCGGGGATGCTTGTCTGGCA
GCAGGATGCTCAGTGATCGCCTCCAACAGCATCATCTGCACTGCCCACTTCACTGCTCGG
AAGGGGAAGCGACACCACGCCCACGTCAACGTGAGCTGGTGCTTCGTGTGCTCCAAAGGG
GGGAGCCTTCTGTGCTGTGAGTCCTGCCCAGCGGCCTTCCACCCTGACTGCCTGAACATC
GAGATGCCTGACGGCAGCTGGTTCTGCAATGACTGCAGGGCTGGGAAGAAGCTGCACTTC
CAGGATATCATTTGGGTGAAACTTGGGAACTACAGATGGTGGCCGGCAGAAGTTTGCCAT
CCCAAAAATGTTCCCCCAAATATTCAGAAAATGAAGCACGAGATTGGAGAATTCCCTGTG
TTTTTCTTTGGGTCTAAAGATTATTACTGGACGCATCAGGCGCGAGTGTTCCCGTACATG
GAGGGGGACCGGGGCAGCCGCTACCAGGGGGTCAGAGGGATCGGAAGAGTCTTCAAAAAC
GCACTGCAAGAAGCTGAAGCTCGTTTTCGTGAAATTAAGCTTCAGAGGGAAGCCCGAGAA
ACACAGGAGAGCGAGCGCAAGCCCCCACCATACAAGCACATCAAGGTGAATAAGCCTTAC
GGGAAAGTCCAGATCTACACAGCGGATATTTCAGAAATCCCTAAGTGCAACTGCAAGCCC
ACAGATGAGAATCCTTGTGGCTTTGATTCGGAGTGTCTGAACAGGATGCTGATGTTTGAG
TGCCACCCGCAGGTGTGTCCCGCGGGCGAGTTCTGCCAGAACCAGTGCTTCACCAAGCGC
CAGTACCCAGAGACCAAGATCATCAAGACAGATGGCAAAGGGTGGGGCCTGGTCGCCAAG
AGGGACATCAGAAAGGGAGAATTTGTTAACGAGTACGTTGGGGAGCTGATCGACGAGGAG
GAGTGCATGGCGAGAATCAAGCACGCACACGAGAACGACATCACCCACTTCTACATGCTC
ACTATAGACAAGGACCGTATAATAGACGCTGGCCCCAAAGGAAACTACTCTCGATTTATG
AATCACAGCTGCCAGCCCAACTGTGAGACCCTCAAGTGGACAGTGAATGGGGACACTCGT
GTGGGCCTGTTTGCCGTCTGTGACATTCCTGCAGGGACGGAGCTGACTTTTAACTACAAC
CTCGATTGTCTGGGCAATGAAAAAACGGTCTGCCGGTGTGGAGCCTCCAATTGCAGTGGA
TTCCTCGGGGATAGACCAAAGACCTCGACGACCCTTTCATCAGAGGAAAAGGGCAAAAAG
ACCAAGAAGAAAACGAGGCGGCGCAGAGCAAAAGGGGAAGGGAAGAGGCAGTCAGAGGAC
GAGTGCTTCCGCTGCGGTGATGGCGGGCAGCTGGTGCTGTGTGACCGCAAGTTCTGCACC
AAGGCCTACCACCTGTCCTGCCTGGGCCTTGGCAAGCGGCCCTTCGGGAAGTGGGAATGT
CCTTGGCATCATTGTGACGTGTGTGGCAAACCTTCGACTTCATTTTGCCACCTCTGCCCC
AATTCGTTCTGTAAGGAGCACCAGGACGGGACAGCCTTCAGCTGCACCCCGGACGGGCGG
TCCTACTGCTGTGAGCATGACTTAGGGGCGGCATCGGTCAGAAGCACCAAGACTGAGAAG
CCCCCCCCAGAGCCAGGGAAGCCGAAGGGGAAGAGGCGGCGGCGGAGGGGCTGGCGGAGA
GTCACAGAGGGCAAATAG
Enzyme 40 GenBank Gene ID NM_001042424.2 Link Image
Enzyme 40 GeneCard ID WHSC1 Link Image
Enzyme 40 GenAtlas ID WHSC1 Link Image
Enzyme 40 HGNC ID HGNC:12766 Link Image
Enzyme 40 Chromosome Location 4
Enzyme 40 Locus 4p16.3
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 General References
  1. Chesi M, Nardini E, Lim RS, Smith KD, Kuehl WM, Bergsagel PL: The t(4;14) translocation in myeloma dysregulates both FGFR3 and a novel gene, MMSET, resulting in IgH/MMSET hybrid transcripts. Blood. 1998 Nov 1;92(9):3025-34. [PubMed Link Image]
  2. Stec I, Wright TJ, van Ommen GJ, de Boer PA, van Haeringen A, Moorman AF, Altherr MR, den Dunnen JT: WHSC1, a 90 kb SET domain-containing gene, expressed in early development and homologous to a Drosophila dysmorphy gene maps in the Wolf-Hirschhorn syndrome critical region and is fused to IgH in t(4;14) multiple myeloma. Hum Mol Genet. 1998 Jul;7(7):1071-82. [PubMed Link Image]
  3. Garlisi CG, Uss AS, Xiao H, Tian F, Sheridan KE, Wang L, Motasim Billah M, Egan RW, Stranick KS, Umland SP: A unique mRNA initiated within a middle intron of WHSC1/MMSET encodes a DNA binding protein that suppresses human IL-5 transcription. Am J Respir Cell Mol Biol. 2001 Jan;24(1):90-98. [PubMed Link Image]
  4. Keats JJ, Maxwell CA, Taylor BJ, Hendzel MJ, Chesi M, Bergsagel PL, Larratt LM, Mant MJ, Reiman T, Belch AR, Pilarski LM: Overexpression of transcripts originating from the MMSET locus characterizes all t(4;14)(p16;q32)-positive multiple myeloma patients. Blood. 2005 May 15;105(10):4060-9. Epub 2005 Jan 27. [PubMed Link Image]
  5. 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]
  6. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  7. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  8. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  9. Malgeri U, Baldini L, Perfetti V, Fabris S, Vignarelli MC, Colombo G, Lotti V, Compasso S, Bogni S, Lombardi L, Maiolo AT, Neri A: Detection of t(4;14)(p16.3;q32) chromosomal translocation in multiple myeloma by reverse transcription-polymerase chain reaction analysis of IGH-MMSET fusion transcripts. Cancer Res. 2000 Aug 1;60(15):4058-61. [PubMed Link Image]
  10. Perfetti V, Coluccia AM, Intini D, Malgeri U, Vignarelli MC, Casarini S, Merlini G, Neri A: Translocation T(4;14)(p16.3;q32) is a recurrent genetic lesion in primary amyloidosis. Am J Pathol. 2001 May;158(5):1599-603. [PubMed Link Image]
  11. Santra M, Zhan F, Tian E, Barlogie B, Shaughnessy J Jr: A subset of multiple myeloma harboring the t(4;14)(p16;q32) translocation lacks FGFR3 expression but maintains an IGH/MMSET fusion transcript. Blood. 2003 Mar 15;101(6):2374-6. Epub 2002 Nov 14. [PubMed Link Image]
  12. Intini D, Fabris S, Storlazzi T, Otsuki T, Ciceri G, Verdelli D, Lombardi L, Rocchi M, Neri A: Identification of a novel IGH-MMSET fusion transcript in a human myeloma cell line with the t(4;14)(p16.3;q32) chromosomal translocation. Br J Haematol. 2004 Aug;126(3):437-9. [PubMed Link Image]
  13. Hudlebusch HR, Theilgaard-Monch K, Lodahl M, Johnsen HE, Rasmussen T: Identification of ID-1 as a potential target gene of MMSET in multiple myeloma. Br J Haematol. 2005 Sep;130(5):700-8. [PubMed Link Image]
  14. Todoerti K, Ronchetti D, Agnelli L, Castellani S, Marelli S, Deliliers GL, Zanella A, Lombardi L, Neri A: Transcription repression activity is associated with the type I isoform of the MMSET gene involved in t(4;14) in multiple myeloma. Br J Haematol. 2005 Oct;131(2):214-8. [PubMed Link Image]
  15. Bergemann AD, Cole F, Hirschhorn K: The etiology of Wolf-Hirschhorn syndrome. Trends Genet. 2005 Mar;21(3):188-95. [PubMed Link Image]
  16. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  17. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  18. Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed Link Image]
  19. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  20. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  21. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  22. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 14765
Enzyme 41 Name Histone-lysine N-methyltransferase NSD3
Enzyme 41 Synonyms
  1. Nuclear SET domain-containing protein 3
  2. Protein whistle
  3. WHSC1-like 1 isoform 9 with methyltransferase activity to lysine
  4. Wolf-Hirschhorn syndrome candidate 1-like protein 1
  5. WHSC1-like protein 1
Enzyme 41 Gene Name WHSC1L1
Enzyme 41 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 41 Number of Residues 1437
Enzyme 41 Molecular Weight 161611.8
Enzyme 41 Theoretical pI 8.26
Enzyme 41 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • histone-lysine N-methyltransferase activity
  • ion binding
  • metal ion binding
  • methyltransferase activity
  • protein 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
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 41 General Function Involved in histone-lysine N-methyltransferase activity
Enzyme 41 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 41 Pathways
Enzyme 41 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 41 Pfam Domain Function
Enzyme 41 Signals
  • None
Enzyme 41 Transmembrane Regions
  • None
Enzyme 41 Essentiality Not Available
Enzyme 41 GenBank ID Protein 13699811 Link Image
Enzyme 41 UniProtKB/Swiss-Prot ID Q9BZ95 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name NSD3_HUMAN Link Image
Enzyme 41 PDB ID Not Available
Enzyme 41 Cellular Location Not Available
Enzyme 41 Gene Sequence >4314 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
AAGGAGCAGGTTGAAACAGTTCCTCAGGCTACAGTGAAGACTGGATTACAGAAAGGTGCC
AGCGAGATTTCAGATTCCTGTAAACCTCTAAAGAAAAGGAGTCGCGCCTCAACTGATGTA
GAAATGACTAGTTCAGCATACAGAGACACATCTGACTCCGATTCTAGAGGACTGAGTGAC
CTGCAGGTAGGCTTTGGAAAGCAAGTAGATAGCCCTTCAGCTACTGCAGATGCAGACGTT
TCTGATGTGCAGTCCATGGATTCAAGTTTGTCGAGAAGAGGCACTGGAATGAGTAAGAAG
GACACTGTATGTCAGATTTGTGAAAGCTCTGGTGACTCTCTGATTCCTTGTGAGGGAGAG
TGCTGCAAACACTTTCACCTGGAGTGCCTGGGATTGGCATCACTTCCTGATAGCAAGTTC
ATCTGCATGGAATGTAAAACTGGGCAGCACCCATGTTTTTCGTGTAAAGTGTCTGGTAAA
GATGTGAAGCGTTGTTCTGTTGGTGCTTGTGGGAAATTTTATCATGAAGCCTGTGTCCGC
AAATTCCCCACTGCCATCTTTGAATCAAAAGGATTCCGCTGTCCTCAGCACTGCTGCTCT
GCCTGCTCTATGGAGAAAGATATCCACAAAGCAAGTAAAGGCCGCATGATGAGATGTTTA
AGATGTCCAGTTGCCTATCACTCTGGAGATGCTTGCATTGCGGCCGGAAGCATGTTAGTA
TCCTCCTACATTCTCATCTGTAGTAATCATTCCAAACGGAGCAGTAATTCTTCTGCTGTA
AATGTAGGCTTTTGTTTCGTTTGTGCCAGAGGGCTGATAGTTCAGGACCATTCAGACCCC
ATGTTCAGTTCATATGCCTATAAGTCCCACTACCTACTGAATGAATCAAATCGTGCTGAG
TTGATGAAATTACCTATGATTCCTTCTTCGTCAGCTTCCAAAAAGAAATGTGAGAAAGGT
GGAAGATTGCTCTGCTGTGAATCGTGCCCAGCTTCCTTCCACCCGGAATGCCTAAGCATA
GAAATGCCAGAAGGCTGCTGGAATTGTAATGACTGTAAAGCTGGCAAGAAACTACATTAC
AAGCAGATTGTTTGGGTCAAATTGGGAAATTACAGATGGTGGCCAGCAGAGATCTGCAAC
CCCAGGTCTGTGCCACTGAACATCCAGGGCCTTAAACATGACTTGGGGGACTTCCCTGTA
TTCTTCTTTGGTTCTCATGACTACTACTGGGTACACCAGGGCAGAGTGTTCCCTTATGTT
GAAGGAGACAAAAGCTTTGCTGAAGGGCAGACTAGTATTAACAAGACCTTCAAAAAGGCA
CTGGAAGAAGCTGCAAAACGTTTCCAGGAATTGAAAGCACAAAGAGAAAGTAAAGAAGCC
CTAGAGATTGAAAAAAACTCAAGAAAACCCCCTCCCTACAAACACATCAAAGCTAACAAA
GTAATAGGAAAGGTGCAGATCCAGGTTGCTGACCTGTCAGAGATTCCCCGCTGTAACTGC
AAGCCAGCTGATGAAAACCCTTGTGGCTTGGAATCGGAGTGCCTGAACAGAATGTTGCAG
TATGAATGCCACCCGCAGGTGTGCCCAGCTGGAGATCGTTGTCAGAACCAGTGCTTTACA
AAGAGACTATACCCTGATGCAGAGATCATCAAAACGGAGCGGAGAGGCTGGGGCCTCAGG
ACCAAAAGGAGCATTAAGAAGGGTGAATTTGTAAATGAATACGTCGGTGAATTAATTGAT
GAAGAAGAATGCAGATTGCGAATCAAGCGAGCCCACGAGAACAGTGTAACTAATTTTTAT
ATGTTAACTGTTACCAAGGACCGTATAATTGATGCCGGCCCAAAAGGAAATTATTCTCGC
TTCATGAACCACAGTTGTAATCCCAACTGTGAAACACAAAAGTGGACAGTGAATGGAGAT
GTTCGAGTGGGACTATTTGCTCTCTGTGATATTCCTGCAGGGATGGAGTTAACATTTAAT
TATAACCTAGATTGTCTGGGCAACGGCAGAACGGAGTGCCACTGTGGAGCAGATAACTGC
AGTGGTTTTCTAGGAGTGCGGCCAAAGTCGGCATGTGCGTCAACAAATGAAGAGAAGGCA
AAAAATGCTAAGTTAAAACAGAAGAGACGAAAGATCAAAACAGAACCAAAGCAGATGCAT
GAAGATTACTGTTTTCAATGTGGAGATGGTGGAGAGCTGGTCATGTGTGACAAAAAAGAC
TGTCCCAAAGCATACCACCTCCTATGCCTTAACCTGACTCAGCCACCATATGGAAAGTGG
GAGTGTCCGTGGCATCAGTGCGATGAGTGCAGCAGTGCAGCTGTTTCCTTCTGTGAATTC
TGTCCACATTCATTTTGTAAAGATCATGAAAAGGGGGCCCTGGTTCCCTCTGCACTGGAA
GGCCGCCTCTGCTGCTCGGAACATGACCCCATGGCTCCTGTGTCACCAGAATACTGGAGC
AAGATAAAATGTAAATGGGAATCACAAGATCATGGAGAAGAAGTAAAAGAATAA
Enzyme 41 GenBank Gene ID NM_023034.1 Link Image
Enzyme 41 GeneCard ID WHSC1L1 Link Image
Enzyme 41 GenAtlas ID WHSC1L1 Link Image
Enzyme 41 HGNC ID HGNC:12767 Link Image
Enzyme 41 Chromosome Location 8
Enzyme 41 Locus 8p11.2
Enzyme 41 SNPs SNPJam Report Link Image
Enzyme 41 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]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Rosati R, La Starza R, Veronese A, Aventin A, Schwienbacher C, Vallespi T, Negrini M, Martelli MF, Mecucci C: NUP98 is fused to the NSD3 gene in acute myeloid leukemia associated with t(8;11)(p11.2;p15). Blood. 2002 May 15;99(10):3857-60. [PubMed Link Image]
  6. Tonon G, Wong KK, Maulik G, Brennan C, Feng B, Zhang Y, Khatry DB, Protopopov A, You MJ, Aguirre AJ, Martin ES, Yang Z, Ji H, Chin L, Depinho RA: High-resolution genomic profiles of human lung cancer. Proc Natl Acad Sci U S A. 2005 Jul 5;102(27):9625-30. Epub 2005 Jun 27. [PubMed Link Image]
  7. Kim SM, Kee HJ, Eom GH, Choe NW, Kim JY, Kim YS, Kim SK, Kook H, Kook H, Seo SB: Characterization of a novel WHSC1-associated SET domain protein with H3K4 and H3K27 methyltransferase activity. Biochem Biophys Res Commun. 2006 Jun 23;345(1):318-23. Epub 2006 Apr 27. [PubMed Link Image]
  8. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  9. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 41 Metabolite References Not Available
Enzyme 42 [top]
Enzyme 42 ID 14776
Enzyme 42 Name Histone-lysine N-methyltransferase SETD1B
Enzyme 42 Synonyms
  1. Lysine N-methyltransferase 2G
  2. SET domain-containing protein 1B
  3. hSET1B
Enzyme 42 Gene Name SETD1B
Enzyme 42 Protein Sequence >Histone-lysine N-methyltransferase SETD1B
MENSHPPHHHHQQPPPQPGPSGERRNHHWRSYKLMIDPALKKGHHKLYRYDGQHFSLAMS
SNRPVEIVEDPRVVGIWTKNKELELSVPKFKIDEFYVGPVPPKQVTFAKLNDNIRENFLR
DMCKKYGEVEEVEILYNPKTKKHLGIAKVVFATVRGAKDAVQHLHSTSVMGNIIHVELDT
KGETRMRFYELLVTGRYTPQTLPVGELDAVSPIVNETLQLSDALKRLKDGGLSAGCGSGS
SSVTPNSGGTPFSQDTAYSSCRLDTPNSYGQGTPLTPRLGTPFSQDSSYSSRQPTPSYLF
SQDPAVTFKARRHESKFTDAYNRRHEHHYVHNSPAVTAVAGATAAFRGSSDLPFGAVGGT
GGSSGPPFKAQPQDSATFAHTPPPAQATPAPGFKSAFSPYQTPVAHFPPPPEEPTATAAF
GARDSGEFRRAPAPPPLPPAEPLAKEKPGTPPGPPPPDTNSMELGGRPTFGWSPEPCDSP
GTPTLESSPAGPEKPHDSLDSRIEMLLKEQRTKLLFLREPDSDTELQMEGSPISSSSSQL
SPLAPFGTNSQPGFRGPTPPSSRPSSTGLEDISPTPLPDSDEDEELDLGLGPRPPPEPGP
PDPAGLLSQTAEVALDLVGDRTPTSEKMDEGQQSSGEDMEISDDEMPSAPITSADCPKPM
VVTPGAAAVAAPSVLAPTLPLPPPPGFPPLPPPPPPPPPQPGFPMPPPLPPPPPPPPPAH
PAVTVPPPPLPAPPGVPPPPILPPLPPFPPGLFPVMQVDMSHVLGGQWGGMPMSFQMQTQ
VLSRLMTGQGACPYPPFMAAAAAAASAGLQFVNLPPYRGPFSLSNSGPGRGQHWPPLPKF
DPSVPPPGYMPRQEDPHKATVDGVLLVVLKELKAIMKRDLNRKMVEVVAFRAFDEWWDKK
ERMAKASLTPVKSGEHKDEDRPKPKDRIASCLLESWGKGEGLGYEGLGLGIGLRGAIRLP
SFKVKRKEPPDTTSSGDQKRLRPSTSVDEEDEESERERDRDMADTPCELAKRDPKGVGVR
RRPARPLELDSGGEEDEKESLSEEQESTEEEEEAEEEEEEEDDDDDDSDDRDESENDDED
TALSEASEKDEGDSDEEETVSIVTSKAEATSSSESSESSEFESSSESSPSSSEDEEEVVA
REEEEEEEEEEMVAEESMASAGPEDFEQDGEEAALAPGAPAVDSLGMEEEVDIETEAVAP
EERPSMLDEPPLPVGVEEPADSREPPEEPGLSQEGAMLLSPEPPAKEVEARPPLSPERAP
EHDLEVEPEPPMMLPLPLQPPLPPPRPPRPPSPPPEPETTDASHPSVPPEPLAEDHPPHT
PGLCGSLAKSQSTETVPATPGGEPPLSGGSSGLSLSSPQVPGSPFSYPAPSPSLSSGGLP
RTPGRDFSFTPTFSEPSGPLLLPVCPLPTGRRDERSGPLASPVLLETGLPLPLPLPLPLP
LALPAVLRAQARAPTPLPPLLPAPLASCPPPMKRKPGRPRRSPPSMLSLDGPLVRPPAGA
ALGRELLLLPGQPQTPVFPSTHDPRTVTLDFRNAGIPAPPPPLPPQPPPPPPPPPVEPTK
LPFKELDNQWPSEAIPPGPRGRDEVTEEYMELAKSRGPWRRPPKKRHEDLVPPAGSPELS
PPQPLFRPRSEFEEMTILYDIWNGGIDEEDIRFLCVTYERLLQQDNGMDWLNDTLWVYHP
STSLSSAKKKKRDDGIREHVTGCARSEGFYTIDKKDKLRYLNSSRASTDEPPADTQGMSI
PAQPHASTRAGSERRSEQRRLLSSFTGSCDSDLLKFNQLKFRKKKLKFCKSHIHDWGLFA
MEPIAADEMVIEYVGQNIRQVIADMREKRYEDEGIGSSYMFRVDHDTIIDATKCGNFARF
INHSCNPNCYAKVITVESQKKIVIYSKQHINVNEEITYDYKFPIEDVKIPCLCGSENCRG
TLN
Enzyme 42 Number of Residues 1923
Enzyme 42 Molecular Weight 208729.7
Enzyme 42 Theoretical pI 4.59
Enzyme 42 GO Classification
Function
  • binding
  • nucleic acid binding
  • nucleotide binding
Process
Component
Enzyme 42 General Function Involved in nucleotide binding
Enzyme 42 Specific Function Histone methyltransferase that specifically methylates 'Lys-4' of histone H3, when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys- 9' residue is already methylated. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. The non-overalpping localization with SETD1A suggests that SETD1A and SETD1B make non-redundant contributions to the epigenetic control of chromatin structure and gene expression. Specifically tri-methylates 'Lys-4' of histone H3 in vitro
Enzyme 42 Pathways Not Available
Enzyme 42 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 42 Pfam Domain Function
Enzyme 42 Signals
  • None
Enzyme 42 Transmembrane Regions
  • None
Enzyme 42 Essentiality Not Available
Enzyme 42 GenBank ID Protein 210032580 Link Image
Enzyme 42 UniProtKB/Swiss-Prot ID Q9UPS6 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name SET1B_HUMAN Link Image
Enzyme 42 PDB ID Not Available
Enzyme 42 Cellular Location Not Available
Enzyme 42 Gene Sequence >5772 bp
ATGGAGAACAGTCACCCCCCCCACCACCACCACCAGCAGCCCCCGCCGCAGCCCGGCCCT
TCGGGCGAGAGGAGGAACCACCATTGGAGAAGTTACAAGTTGATGATTGACCCGGCTCTG
AAAAAGGGGCATCATAAACTGTACCGCTACGATGGGCAGCATTTCAGCCTGGCGATGTCC
AGCAACCGCCCGGTGGAAATTGTCGAAGATCCCCGGGTCGTCGGGATCTGGACCAAAAAC
AAGGAGCTGGAGCTGTCGGTGCCCAAATTCAAGATCGATGAGTTCTACGTGGGCCCGGTG
CCTCCGAAGCAGGTGACATTTGCCAAGCTGAATGATAACATCCGTGAAAACTTCCTGAGG
GACATGTGCAAGAAGTATGGGGAGGTGGAGGAGGTGGAGATTTTGTACAACCCCAAGACC
AAGAAGCACCTGGGCATCGCCAAGGTGGTCTTTGCCACGGTCCGGGGAGCCAAGGATGCC
GTTCAGCACTTGCACAGCACTTCCGTCATGGGCAACATTATCCACGTGGAGCTGGACACC
AAAGGGGAAACCCGAATGCGGTTCTATGAACTGTTGGTCACTGGCCGATACACCCCCCAG
ACCCTCCCAGTGGGCGAGCTGGACGCTGTCTCTCCAATCGTGAATGAGACCCTGCAGCTG
TCAGATGCCCTGAAGCGCCTCAAGGATGGAGGCCTGTCTGCAGGCTGTGGCTCCGGCTCC
TCCTCTGTCACCCCCAATAGCGGTGGGACACCCTTCTCCCAGGACACAGCTTATTCCAGC
TGCCGCCTGGACACACCCAACTCCTATGGACAGGGCACCCCGCTCACACCGCGCCTGGGC
ACCCCTTTCTCACAGGACTCCAGCTACTCCAGCCGCCAGCCCACACCCTCATACCTCTTC
AGCCAGGACCCTGCAGTGACCTTCAAGGCCCGGCGCCACGAGAGCAAGTTCACGGACGCC
TACAACCGCCGCCACGAACATCATTATGTACACAATTCTCCCGCGGTCACTGCGGTGGCC
GGGGCCACAGCCGCTTTCCGGGGTTCCTCGGACCTCCCGTTCGGAGCAGTCGGCGGCACT
GGGGGCAGCAGCGGTCCCCCGTTCAAGGCTCAACCACAGGATTCAGCCACATTTGCCCAC
ACTCCACCACCCGCCCAAGCAACCCCTGCTCCTGGATTCAAGTCTGCTTTCTCTCCGTAT
CAGACCCCAGTGGCCCACTTCCCTCCACCCCCGGAAGAGCCCACCGCCACAGCCGCTTTT
GGGGCCCGCGACAGTGGGGAGTTCCGGAGGGCACCGGCGCCCCCACCCCTGCCACCTGCT
GAGCCTCTGGCCAAGGAGAAGCCAGGCACGCCACCCGGCCCGCCGCCCCCCGACACCAAC
AGCATGGAGCTGGGCGGCCGGCCCACCTTCGGCTGGAGTCCTGAGCCCTGTGACAGCCCT
GGCACGCCCACGCTGGAGTCGTCCCCTGCAGGGCCAGAGAAACCCCACGACAGCCTGGAC
TCGCGCATCGAGATGCTGCTGAAGGAGCAGCGCACCAAGCTGCTCTTCCTGAGGGAGCCG
GACTCGGACACCGAGCTGCAGATGGAGGGCAGCCCCATCTCCTCCTCCTCCTCCCAGCTC
TCCCCACTGGCCCCCTTTGGCACCAACTCCCAGCCAGGCTTCCGGGGCCCCACGCCCCCC
TCGTCACGCCCCTCCAGCACCGGCCTGGAGGATATCAGCCCAACACCCCTCCCAGACTCC
GACGAGGACGAGGAGCTCGACCTGGGCCTTGGGCCTCGGCCTCCACCTGAGCCAGGCCCC
CCGGACCCTGCTGGGCTTCTGAGCCAGACAGCTGAGGTGGCCTTGGACCTGGTTGGAGAC
AGAACCCCGACCTCAGAGAAGATGGATGAGGGCCAGCAGTCCTCAGGCGAGGACATGGAG
ATCTCGGATGACGAGATGCCCTCGGCCCCCATCACCAGCGCTGACTGCCCCAAGCCCATG
GTGGTGACCCCAGGAGCGGCAGCCGTGGCAGCCCCTTCTGTGCTAGCCCCAACCCTGCCG
CTGCCCCCGCCACCTGGCTTCCCCCCGCTGCCCCCCCCACCACCACCACCCCCACCGCAG
CCTGGCTTCCCCATGCCCCCACCGCTGCCCCCACCGCCGCCCCCACCCCCTCCAGCCCAC
CCTGCTGTGACAGTGCCCCCACCACCCTTGCCAGCGCCGCCTGGAGTCCCGCCCCCACCC
ATCCTGCCACCACTGCCCCCCTTTCCGCCGGGCCTGTTCCCTGTGATGCAGGTGGACATG
AGCCACGTGCTGGGTGGCCAGTGGGGCGGCATGCCCATGTCCTTCCAGATGCAAACGCAG
GTGCTCAGCCGGCTGATGACGGGCCAGGGCGCCTGCCCCTACCCGCCCTTCATGGCCGCT
GCGGCCGCCGCTGCCTCAGCTGGGCTCCAGTTTGTCAACCTGCCGCCCTACCGGGGCCCC
TTCTCCCTGAGCAACTCCGGCCCAGGCCGCGGGCAGCACTGGCCACCACTGCCCAAGTTT
GACCCGTCAGTGCCTCCACCAGGCTACATGCCACGCCAGGAGGACCCACACAAAGCCACG
GTGGATGGCGTCCTGCTGGTGGTCCTCAAAGAACTCAAGGCCATCATGAAGCGTGACCTG
AACCGCAAGATGGTGGAAGTGGTGGCTTTCCGGGCCTTTGACGAGTGGTGGGACAAGAAG
GAGCGGATGGCCAAGGCCTCGCTGACCCCGGTGAAGTCGGGCGAGCACAAGGACGAGGAC
AGGCCGAAGCCCAAGGACCGCATCGCCTCGTGCCTGCTGGAGTCATGGGGCAAGGGCGAG
GGCCTGGGCTACGAGGGCCTGGGCCTGGGCATTGGGCTGCGTGGGGCCATTCGCCTGCCC
TCCTTCAAGGTCAAGAGGAAGGAGCCACCAGACACCACCTCATCTGGCGACCAGAAGCGG
CTGCGGCCCTCGACCTCTGTGGATGAGGAAGATGAAGAGTCCGAGCGAGAGCGAGACCGG
GATATGGCAGACACCCCCTGTGAGCTCGCCAAGCGGGACCCCAAGGGCGTGGGTGTGCGG
CGGCGGCCGGCGCGGCCTCTGGAGCTGGACAGTGGTGGGGAGGAGGACGAGAAGGAGTCA
TTGTCGGAGGAACAGGAGAGCACCGAGGAGGAAGAGGAGGCGGAGGAGGAGGAGGAGGAG
GAAGATGACGACGATGACGACAGTGATGACCGGGACGAGTCTGAGAACGATGACGAGGAC
ACAGCCCTGTCAGAGGCGAGTGAGAAGGACGAAGGGGACTCGGATGAAGAGGAGACAGTG
AGCATTGTAACCTCCAAGGCCGAAGCCACGTCGTCCAGTGAGAGTTCCGAGTCTTCTGAG
TTTGAGTCAAGCTCCGAGTCCTCGCCCTCATCCTCGGAGGATGAGGAGGAGGTAGTGGCC
AGGGAAGAGGAGGAAGAAGAGGAGGAGGAGGAGATGGTGGCCGAGGAAAGCATGGCTTCT
GCAGGCCCTGAGGACTTTGAGCAGGACGGGGAGGAAGCGGCTCTGGCCCCGGGGGCACCT
GCAGTGGACTCGTTGGGCATGGAAGAGGAGGTGGACATCGAGACTGAGGCTGTGGCCCCT
GAGGAGCGGCCCTCCATGCTGGACGAGCCCCCCTTGCCTGTGGGTGTTGAAGAGCCAGCG
GACTCCAGGGAGCCGCCTGAGGAACCAGGCCTGAGCCAGGAAGGGGCCATGTTGCTGTCT
CCAGAGCCCCCTGCCAAGGAGGTGGAGGCTCGACCCCCATTGTCCCCTGAGCGAGCTCCA
GAACATGACCTGGAAGTGGAGCCGGAGCCCCCTATGATGCTCCCCTTGCCGCTGCAACCA
CCATTGCCGCCCCCACGACCACCCCGGCCACCCAGCCCACCGCCGGAGCCTGAGACCACA
GATGCCTCACACCCATCTGTCCCTCCGGAGCCCCTTGCCGAGGACCACCCCCCGCATACT
CCAGGCCTCTGTGGCAGCCTGGCCAAGTCGCAGAGCACAGAGACGGTGCCAGCCACACCA
GGCGGGGAGCCCCCGCTATCAGGGGGCAGCAGTGGCCTGTCCCTGAGCTCTCCGCAAGTG
CCCGGCAGCCCCTTCTCCTACCCAGCCCCGTCCCCTAGCTTGAGCAGTGGGGGCCTCCCT
CGGACACCTGGCCGGGACTTCAGCTTCACACCCACCTTCTCCGAGCCCAGCGGGCCCTTG
CTCCTGCCCGTCTGCCCACTCCCCACTGGCCGACGCGATGAACGCTCCGGGCCCCTGGCC
TCCCCGGTGCTCCTGGAGACGGGCCTGCCCCTCCCTCTGCCCCTTCCCCTGCCCTTGCCC
TTGGCATTGCCCGCCGTCTTGCGGGCCCAGGCTCGTGCGCCCACCCCGCTGCCACCCCTG
CTGCCCGCCCCCCTGGCCTCTTGCCCTCCCCCAATGAAGAGGAAGCCGGGCCGGCCCCGG
CGATCCCCACCATCTATGCTCTCCTTGGATGGGCCCTTGGTCCGACCACCAGCAGGGGCC
GCCCTTGGAAGGGAACTCCTGCTCCTGCCGGGCCAGCCACAGACCCCCGTCTTCCCCAGC
ACCCATGACCCCCGGACGGTGACCCTGGACTTCCGGAACGCGGGGATCCCAGCCCCTCCA
CCACCCCTTCCCCCCCAGCCACCCCCACCCCCACCTCCCCCACCTGTAGAGCCCACCAAG
CTGCCCTTTAAGGAGCTAGACAACCAGTGGCCCTCCGAGGCCATTCCTCCGGGCCCCCGT
GGGCGCGATGAGGTCACTGAGGAATACATGGAGTTGGCCAAGAGCCGGGGGCCGTGGCGC
CGGCCACCTAAGAAGCGCCATGAGGACCTGGTGCCACCTGCGGGCTCGCCCGAACTCTCG
CCACCCCAGCCCCTCTTCCGGCCCCGCTCGGAGTTTGAGGAGATGACCATCCTGTATGAC
ATCTGGAACGGTGGCATCGATGAGGAGGACATCCGCTTCCTGTGTGTCACCTACGAGCGA
CTGCTACAGCAGGACAATGGCATGGACTGGCTTAACGACACGCTCTGGGTCTACCATCCC
TCCACCAGCCTCTCTTCAGCTAAGAAGAAGAAACGGGACGATGGCATCCGCGAGCACGTG
ACGGGCTGTGCCCGCAGTGAGGGCTTCTACACCATCGACAAGAAGGACAAGCTCAGATAC
CTCAACAGCAGCCGTGCCAGCACCGATGAGCCCCCCGCAGACACCCAGGGCATGAGCATC
CCAGCACAGCCCCACGCCTCCACCCGGGCAGGCTCGGAGCGGCGTTCGGAGCAGCGCCGC
CTGCTGTCCTCCTTCACTGGCAGCTGTGACAGTGACCTGCTCAAGTTCAACCAGCTCAAG
TTCCGGAAGAAAAAGCTCAAGTTCTGCAAGAGCCACATTCACGACTGGGGCTTGTTCGCC
ATGGAGCCCATCGCGGCTGACGAGATGGTCATCGAGTACGTGGGCCAGAATATCCGTCAG
GTGATCGCAGACATGCGGGAGAAGCGTTATGAGGACGAGGGCATCGGGAGCAGCTACATG
TTCCGGGTGGACCATGACACCATCATCGACGCCACCAAGTGCGGCAACTTCGCGCGCTTC
ATCAACCACAGCTGCAACCCCAACTGCTATGCCAAGGTGATCACGGTGGAGTCACAGAAG
AAGATAGTCATCTACTCGAAGCAGCACATTAACGTCAATGAGGAGATTACCTATGACTAT
AAGTTCCCCATCGAGGACGTCAAGATCCCCTGCCTCTGTGGCTCCGAGAACTGCCGGGGG
ACCCTCAACTAG
Enzyme 42 GenBank Gene ID NM_015048.1 Link Image
Enzyme 42 GeneCard ID SETD1B Link Image
Enzyme 42 GenAtlas ID SETD1B Link Image
Enzyme 42 HGNC ID HGNC:29187 Link Image
Enzyme 42 Chromosome Location 1
Enzyme 42 Locus 12q24.31
Enzyme 42 SNPs SNPJam Report Link Image
Enzyme 42 General References
  1. Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed Link Image]
  2. 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]
  3. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  4. Lee JH, Tate CM, You JS, Skalnik DG: Identification and characterization of the human Set1B histone H3-Lys4 methyltransferase complex. J Biol Chem. 2007 May 4;282(18):13419-28. Epub 2007 Mar 13. [PubMed Link Image]
  5. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 14777
Enzyme 43 Name Histone-lysine N-methyltransferase SETD2
Enzyme 43 Synonyms
  1. HIF-1
  2. Huntingtin yeast partner B
  3. Huntingtin-interacting protein 1
  4. HIP-1
  5. Huntingtin-interacting protein B
  6. Lysine N-methyltransferase 3A
  7. SET domain-containing protein 2
  8. hSET2
  9. p231HBP
Enzyme 43 Gene Name SETD2
Enzyme 43 Protein Sequence >Histone-lysine N-methyltransferase SETD2
MKQLQPQPPPKMGDFYDPEHPTPEEEENEAKIENVQKTGFIKGPMFKGVASSRFLPKGTK
TKVNLEEQGRQKVSFSFSLTKKTLQNRFLTALGNEKQSDTPNPPAVPLQVDSTPKMKMEI
GDTLSTAEESSPPKSRVELGKIHFKKHLLHVTSRPLLATTTAVASPPTHAAPLPAVIAES
TTVDSPPSSPPPPPPPAQATTLSSPAPVTEPVALPHTPITVLMAAPVPLPVDVAVRSLKE
PPIIIVPESLEADTKQDTISNSLEEHVTQILNEQADISSKKEDSHIGKDEEIPDSSKISL
SCKKTGSKKKSSQSEGIFLGSESDEDSVRTSSSQRSHDLKFSASIEKERDFKKSSAPLKS
EDLGKPSRSKTDRDDKYFSYSKLERDTRYVSSRCRSERERRRSRSHSRSERGSRTNLSYS
RSERSHYYDSDRRYHRSSPYRERTRYSRPYTDNRARESSDSEEEYKKTYSRRTSSHSSSY
RDLRTSSYSKSDRDCKTETSYLEMERRGKYSSKLERESKRTSENEAIKRCCSPPNELGFR
RGSSYSKHDSSASRYKSTLSKPIPKSDKFKNSFCCTELNEEIKQSHSFSLQTPCSKGSEL
RMINKNPEREKAGSPAPSNRLNDSPTLKKLDELPIFKSEFITHDSHDSIKELDSLSKVKN
DQLRSFCPIELNINGSPGAESDLATFCTSKTDAVLMTSDDSVTGSELSPLVKACMLSSNG
FQNISRCKEKDLDDTCMLHKKSESPFRETEPLVSPHQDKLMSMPVMTVDYSKTVVKEPVD
TRVSCCKTKDSDIYCTLNDSNPSLCNSEAENIEPSVMKISSNSFMNVHLESKPVICDSRN
LTDHSKFACEEYKQSIGSTSSASVNHFDDLYQPIGSSGIASSLQSLPPGIKVDSLTLLKC
GENTSPVLDAVLKSKKSSEFLKHAGKETIVEVGSDLPDSGKGFASRENRRNNGLSGKCLQ
EAQEEGNSILPERRGRPEISLDERGEGGHVHTSDDSEVVFSSCDLNLTMEDSDGVTYALK
CDSSGHAPEIVSTVHEDYSGSSESSNDESDSEDTDSDDSSIPRNRLQSVVVVPKNSTLPM
EETSPCSSRSSQSYRHYSDHWEDERLESRRHLYEEKFESIASKACPQTDKFFLHKGTEKN
PEISFTQSSRKQIDNRLPELSHPQSDGVDSTSHTDVKSDPLGHPNSEETVKAKIPSRQQE
ELPIYSSDFEDVPNKSWQQTTFQNRPDSRLGKTELSFSSSCEIPHVDGLHSSEELRNLGW
DFSQEKPSTTYQQPDSSYGACGGHKYQQNAEQYGGTRDYWQGNGYWDPRSGRPPGTGVVY
DRTQGQVPDSLTDDREEEENWDQQDGSHFSDQSDKFLLSLQKDKGSVQAPEISSNSIKDT
LAVNEKKDFSKNLEKNDIKDRGPLKKRRQEIESDSESDGELQDRKKVRVEVEQGETSVPP
GSALVGPSCVMDDFRDPQRWKECAKQGKMPCYFDLIEENVYLTERKKNKSHRDIKRMQCE
CTPLSKDERAQGEIACGEDCLNRLLMIECSSRCPNGDYCSNRRFQRKQHADVEVILTEKK
GWGLRAAKDLPSNTFVLEYCGEVLDHKEFKARVKEYARNKNIHYYFMALKNDEIIDATQK
GNCSRFMNHSCEPNCETQKWTVNGQLRVGFFTTKLVPSGSELTFDYQFQRYGKEAQKCFC
GSANCRGYLGGENRVSIRAAGGKMKKERSRKKDSVDGELEALMENGEGLSDKNQVLSLSR
LMVRIETLEQKLTCLELIQNTHSQSCLKSFLERHGLSLLWIWMAELGDGRESNQKLQEEI
IKTLEHLPIPTKNMLEESKVLPIIQRWSQTKTAVPPLSEGDGYSSENTSRAHTPLNTPDP
STKLSTEADTDTPKKLMFRRLKIISENSMDSAISDATSELEGKDGKEDLDQLENVPVEEE
EELQSQQLLPQQLPECKVDSETNIEASKLPTSEPEADAEIEPKESNGTKLEEPINEETPS
QDEEEGVSDVESERSQEQPDKTVDISDLATKLLDSWKDLKEVYRIPKKSQTEKENTTTER
GRDAVGFRDQTPAPKTPNRSRERDPDKQTQNKEKRKRRSSLSPPSSAYERGTKRPDDRYD
TPTSKKKVRIKDRNKLSTEERRKLFEQEVAQREAQKQQQQMQNLGMTSPLPYDSLGYNAP
HHPFAGYPPGYPMQAYVDPSNPNAGKVLLPTPSMDPVCSPAPYDHAQPLVGHSTEPLSAP
PPVPVVPHVAAPVEVSSSQYVAQSDGVVHQDSSVAVLPVPAPGPVQGQNYSVWDSNQQSV
SVQQQYSPAQSQATIYYQGQTCPTVYGVTSPYSQTTPPIVQSYAQPSLQYIQGQQIFTAH
PQGVVVQPAAAVTTIVAPGQPQPLQPSEMVVTNNLLDLPPPSPPKPKTIVLPPNWKTARD
PEGKIYYYHVITRQTQWDPPTWESPGDDASLEHEAEMDLGTPTYDENPMKASKKPKTAEA
DTSSELAKKSKEVFRKEMSQFIVQCLNPYRKPDCKVGRITTTEDFKHLARKLTHGVMNKE
LKYCKNPEDLECNENVKHKTKEYIKKYMQKFGAVYKPKEDTELE
Enzyme 43 Number of Residues 2564
Enzyme 43 Molecular Weight 287594.2
Enzyme 43 Theoretical pI 6.02
Enzyme 43 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • histone-lysine N-methyltransferase activity
  • ion binding
  • metal ion binding
  • methyltransferase activity
  • oxidoreductase activity
  • protein binding
  • protein methyltransferase activity
  • protein-lysine N-methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
  • transition metal ion binding
Process
  • biological regulation
  • metabolic process
  • oxidation reduction
  • regulation of biological process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
  • chromosome
  • intracellular membrane-bounded organelle
  • intracellular non-membrane-bounded organelle
  • membrane-bounded organelle
  • non-membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 43 General Function Involved in histone-lysine N-methyltransferase activity
Enzyme 43 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 43 Pathways
Enzyme 43 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 43 Pfam Domain Function
Enzyme 43 Signals
  • None
Enzyme 43 Transmembrane Regions
  • None
Enzyme 43 Essentiality Not Available
Enzyme 43 GenBank ID Protein 197313748 Link Image
Enzyme 43 UniProtKB/Swiss-Prot ID Q9BYW2 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name SETD2_HUMAN Link Image
Enzyme 43 PDB ID Not Available
Enzyme 43 Cellular Location Not Available
Enzyme 43 Gene Sequence >7695 bp
ATGAAGCAGCTGCAGCCGCAGCCGCCTCCGAAGATGGGGGATTTCTACGACCCGGAGCAC
CCGACCCCTGAAGAAGAAGAAAATGAGGCAAAGATTGAAAATGTGCAGAAAACAGGTTTC
ATCAAAGGACCAATGTTCAAAGGTGTTGCTTCTAGTCGATTTTTGCCCAAAGGCACCAAA
ACAAAAGTTAATTTGGAAGAACAGGGACGACAGAAGGTGTCATTCAGCTTCAGCCTTACA
AAGAAAACTTTGCAGAATAGGTTTCTCACTGCACTTGGCAATGAAAAGCAAAGTGATACT
CCAAACCCTCCAGCTGTACCTCTTCAGGTAGACTCGACTCCTAAAATGAAAATGGAAATT
GGTGATACCTTATCTACTGCAGAAGAATCTTCCCCACCAAAGTCAAGGGTGGAATTGGGC
AAAATTCATTTTAAGAAACATCTGCTTCATGTAACATCCAGGCCACTGCTGGCTACTACC
ACAGCAGTAGCATCTCCACCTACTCATGCAGCACCATTACCAGCAGTGATAGCAGAATCA
ACAACTGTAGACTCACCGCCCTCATCTCCGCCTCCACCGCCTCCACCTGCCCAAGCCACA
ACACTCTCATCACCAGCACCAGTAACAGAGCCAGTGGCCTTGCCACATACACCAATAACA
GTTCTAATGGCAGCACCAGTACCCTTACCAGTAGATGTAGCAGTTAGATCTCTGAAAGAA
CCACCAATTATAATTGTACCAGAATCTTTAGAAGCAGATACTAAGCAGGACACTATATCT
AATAGTTTAGAAGAACACGTAACTCAAATATTGAATGAGCAAGCAGATATTTCCTCAAAA
AAAGAAGATTCCCATATTGGGAAGGATGAAGAAATTCCAGATAGTTCTAAGATTAGTCTG
AGCTGTAAAAAAACAGGTTCTAAGAAGAAATCCTCACAATCTGAAGGCATCTTTCTTGGT
TCAGAATCTGATGAAGATTCTGTACGGACTTCTTCAAGTCAAAGATCACATGATTTAAAA
TTTTCAGCAAGCATTGAAAAGGAAAGAGATTTTAAAAAGAGCTCAGCACCTTTAAAAAGT
GAGGATCTAGGGAAACCTTCACGATCTAAAACAGACAGAGATGATAAATATTTTAGCTAT
TCAAAACTTGAAAGAGATACTCGGTATGTATCTTCCCGATGTAGATCAGAAAGAGAGCGA
CGGCGGAGCAGATCTCACTCTAGGTCTGAGAGAGGCTCTAGAACTAATTTATCCTATTCC
AGGTCAGAACGATCTCATTATTATGACTCTGATCGTCGCTACCATAGGAGCTCCCCTTAT
CGAGAGAGGACGCGCTATTCTCGGCCATACACAGATAACAGAGCACGAGAGAGTTCTGAC
TCAGAAGAAGAGTATAAGAAGACATACTCAAGGCGTACCTCATCTCATTCCTCTTCTTAC
AGAGACCTAAGGACATCATCCTATTCTAAATCTGATCGGGACTGTAAAACTGAGACCTCT
TACTTAGAGATGGAAAGAAGAGGCAAGTATTCTTCAAAACTAGAAAGAGAATCTAAAAGG
ACTTCAGAAAATGAAGCAATTAAAAGATGTTGTTCTCCCCCTAATGAACTGGGATTCCGA
CGAGGGTCATCATATTCTAAGCATGACAGTAGTGCTTCCCGTTATAAATCTACCCTTTCA
AAACCTATACCCAAGTCTGATAAATTTAAAAATTCTTTCTGTTGTACAGAATTAAATGAA
GAAATCAAACAGTCTCATTCTTTTAGTTTACAGACACCTTGTTCAAAAGGTAGTGAATTA
AGAATGATTAATAAAAATCCTGAAAGAGAAAAGGCTGGGTCTCCAGCTCCATCAAATCGA
TTAAATGATTCACCTACTTTAAAAAAGCTAGATGAATTGCCTATTTTTAAGTCCGAATTT
ATAACACATGATAGCCATGATAGTATTAAGGAATTAGACTCTTTATCTAAAGTGAAGAAT
GATCAATTAAGAAGTTTTTGTCCCATAGAATTAAATATAAATGGATCTCCTGGGGCAGAA
TCTGATTTGGCAACATTTTGCACTTCTAAAACTGATGCTGTTTTAATGACTTCTGATGAT
AGTGTGACTGGATCGGAATTATCCCCTTTGGTCAAAGCATGCATGCTTTCATCAAATGGA
TTTCAGAATATTAGTAGGTGCAAAGAAAAAGACTTGGATGATACCTGCATGCTGCATAAG
AAGTCAGAAAGCCCATTTAGAGAAACAGAACCTCTGGTGTCACCACACCAAGATAAACTC
ATGTCTATGCCAGTTATGACTGTGGATTATTCCAAAACAGTAGTTAAAGAACCAGTTGAT
ACGAGGGTTTCTTGCTGCAAAACCAAAGATTCAGACATATACTGTACTTTGAACGATAGC
AACCCTTCTTTGTGTAACTCTGAAGCTGAAAATATTGAGCCTTCAGTTATGAAGATTTCT
TCAAATAGCTTTATGAATGTGCATTTGGAATCAAAACCAGTTATATGTGATAGTAGAAAT
TTGACAGATCACTCAAAATTTGCATGTGAAGAATATAAGCAGAGCATCGGTAGCACTAGT
TCAGCTTCTGTTAATCATTTTGATGATTTATATCAACCTATTGGGAGTTCAGGTATTGCT
TCATCTCTTCAGAGTCTTCCACCAGGAATAAAGGTGGACAGTCTAACTCTCTTGAAATGC
GGAGAGAACACATCTCCAGTTCTGGATGCAGTGCTAAAGAGTAAAAAAAGTTCAGAGTTT
TTAAAGCATGCAGGGAAAGAAACAATAGTAGAAGTAGGTAGTGACCTTCCTGATTCAGGA
AAGGGATTTGCTTCCAGGGAGAACAGGCGTAATAATGGGTTATCTGGGAAATGTTTGCAA
GAGGCTCAAGAAGAAGGGAATTCCATATTGCCTGAAAGAAGAGGAAGACCAGAAATCTCT
TTAGATGAAAGAGGAGAAGGAGGACATGTGCATACTTCTGATGACTCAGAAGTTGTATTT
TCTTCTTGTGATTTGAATTTAACCATGGAAGACAGTGATGGTGTAACTTATGCATTAAAG
TGTGACAGTAGTGGTCATGCCCCAGAAATTGTGTCTACAGTTCATGAAGATTATTCTGGC
TCTTCTGAAAGTTCAAATGATGAAAGTGATTCAGAAGATACAGATTCGGATGATAGCAGT
ATTCCAAGAAACCGTCTCCAGTCTGTTGTGGTTGTGCCAAAGAATTCTACTTTGCCCATG
GAAGAAACAAGTCCTTGTTCTTCTCGGAGCAGTCAAAGTTATAGACACTATTCTGACCAT
TGGGAAGATGAGAGATTGGAGTCAAGGAGACATTTGTATGAGGAAAAATTTGAAAGTATA
GCAAGTAAAGCCTGTCCTCAAACTGATAAGTTTTTCCTTCATAAAGGAACAGAGAAGAAT
CCGGAAATTTCTTTTACACAGTCCAGTAGAAAACAAATAGATAATCGCCTGCCTGAACTT
TCTCATCCTCAGAGTGATGGGGTTGATAGTACAAGTCATACAGATGTGAAATCTGACCCT
CTGGGTCACCCAAATTCAGAGGAAACCGTGAAAGCCAAAATACCTTCTAGGCAGCAAGAA
GAGCTGCCAATTTATTCTTCTGATTTTGAAGATGTCCCAAATAAGTCTTGGCAACAGACC
ACTTTCCAAAACAGGCCAGATAGTAGACTGGGAAAAACAGAATTGAGTTTTTCTTCCTCT
TGTGAGATACCACATGTGGATGGCTTGCACTCATCAGAAGAGCTCAGAAACTTAGGTTGG
GACTTCTCTCAAGAAAAGCCTTCTACCACGTATCAGCAACCTGACAGTAGCTATGGAGCT
TGTGGTGGACACAAGTATCAGCAAAATGCAGAACAGTATGGTGGGACACGTGATTACTGG
CAAGGCAATGGTTACTGGGATCCAAGATCAGGTAGACCTCCTGGAACTGGGGTTGTGTAT
GATCGAACTCAAGGACAAGTACCAGATTCCCTAACAGATGATCGTGAAGAAGAGGAGAAT
TGGGATCAACAGGATGGATCCCATTTTTCAGACCAGTCCGATAAATTTCTTCTATCCCTT
CAGAAAGACAAGGGGTCAGTGCAAGCACCTGAAATAAGCAGCAATTCCATTAAGGACACT
TTAGCTGTGAATGAAAAGAAAGATTTTTCAAAAAACTTAGAAAAAAATGATATCAAAGAT
AGAGGGCCTCTTAAAAAAAGGAGGCAGGAAATAGAGAGTGATTCTGAAAGTGATGGTGAG
CTTCAGGACAGAAAGAAAGTTAGAGTGGAGGTAGAGCAGGGAGAGACATCAGTGCCCCCA
GGTTCAGCACTGGTTGGGCCCTCCTGTGTCATGGATGACTTCAGGGACCCACAGCGATGG
AAGGAATGTGCCAAGCAAGGGAAAATGCCATGTTACTTTGATCTTATTGAAGAAAATGTT
TATTTAACAGAAAGAAAGAAGAATAAATCTCATCGAGATATTAAGCGAATGCAGTGTGAG
TGTACACCTCTTTCTAAAGATGAAAGAGCTCAAGGTGAAATAGCATGTGGGGAAGATTGT
CTTAATCGTCTTCTCATGATTGAATGTTCTTCTCGGTGTCCAAATGGGGATTATTGTTCC
AATAGACGGTTTCAGAGAAAACAGCATGCAGATGTGGAAGTCATACTCACAGAAAAGAAA
GGCTGGGGCTTGAGAGCTGCCAAAGACCTTCCTTCGAACACCTTTGTCCTAGAATATTGT
GGAGAGGTACTCGATCATAAAGAGTTTAAAGCTCGAGTGAAGGAGTATGCACGAAACAAA
AACATCCATTACTATTTCATGGCCCTGAAGAATGATGAGATAATAGATGCCACTCAAAAA
GGAAATTGCTCTCGTTTCATGAATCACAGCTGTGAACCAAATTGTGAAACCCAAAAATGG
ACTGTGAACGGACAACTGAGGGTTGGGTTTTTTACCACCAAACTGGTTCCTTCAGGCTCA
GAGTTAACGTTTGACTATCAGTTCCAGAGATATGGAAAAGAAGCCCAGAAATGTTTCTGC
GGATCAGCCAATTGCCGGGGTTACCTGGGAGGAGAAAACAGAGTCAGCATCAGAGCAGCA
GGAGGGAAAATGAAGAAGGAACGATCTCGTAAGAAGGATTCAGTGGATGGAGAGCTAGAA
GCTCTGATGGAAAATGGTGAGGGTCTCTCTGATAAAAACCAGGTGCTCAGCTTATCCCGG
CTAATGGTTAGAATTGAAACTTTGGAGCAGAAACTTACCTGTCTGGAACTCATACAGAAC
ACACACTCACAGTCCTGCCTGAAGTCCTTTCTGGAACGTCATGGGCTGTCTTTGTTGTGG
ATCTGGATGGCAGAGCTAGGTGACGGCCGGGAAAGTAACCAGAAGCTTCAGGAAGAGATT
ATAAAGACTTTGGAACACTTGCCCATTCCTACTAAAAATATGTTGGAGGAAAGCAAAGTA
CTTCCAATTATTCAACGCTGGTCTCAGACTAAGACTGCTGTCCCTCCGTTGAGTGAAGGA
GATGGGTATTCTAGTGAGAATACATCGCGTGCTCATACACCACTCAACACACCTGATCCT
TCCACCAAGCTGAGCACAGAAGCTGACACAGACACTCCCAAGAAACTAATGTTTCGCAGA
CTGAAAATTATAAGTGAAAATAGCATGGACAGTGCAATCTCTGATGCAACCAGTGAGCTA
GAAGGCAAGGATGGCAAAGAGGATCTTGATCAATTAGAAAATGTCCCTGTAGAGGAAGAG
GAAGAATTGCAGTCACAACAGCTACTCCCACAACAGCTGCCTGAATGCAAAGTTGATAGT
GAAACCAACATAGAAGCTAGTAAGCTACCTACATCTGAACCAGAAGCTGACGCTGAAATA
GAGCCCAAAGAGAGCAACGGCACAAAACTAGAAGAACCTATTAATGAAGAAACACCATCC
CAAGATGAAGAGGAGGGTGTGTCTGATGTGGAGAGTGAAAGGAGCCAAGAACAGCCAGAT
AAAACAGTGGATATAAGTGATTTGGCCACCAAACTCCTGGACAGTTGGAAAGACCTAAAG
GAGGTATATCGAATTCCAAAGAAAAGTCAAACTGAAAAGGAAAACACAACAACTGAACGA
GGAAGGGATGCTGTTGGCTTCAGAGATCAAACACCTGCCCCGAAGACTCCTAATAGGTCA
AGAGAGAGAGACCCAGACAAGCAAACTCAAAATAAAGAGAAAAGGAAACGAAGAAGCTCC
CTCTCACCACCCTCTTCTGCCTATGAGCGGGGAACAAAAAGGCCAGATGACAGATATGAT
ACACCAACTTCTAAAAAGAAAGTACGAATTAAAGACCGCAATAAACTTTCTACAGAGGAA
CGCCGGAAGTTGTTTGAGCAAGAGGTGGCTCAACGGGAGGCTCAGAAACAACAGCAACAG
ATGCAGAACCTGGGAATGACATCACCACTGCCCTATGACTCTCTTGGTTATAATGCCCCG
CATCATCCCTTTGCTGGTTACCCACCAGGTTATCCCATGCAGGCCTATGTGGATCCCAGC
AACCCTAATGCTGGAAAGGTGCTCCTGCCCACACCCAGCATGGACCCAGTGTGTTCTCCT
GCTCCTTATGATCATGCTCAGCCCTTGGTGGGACATTCTACAGAACCCCTTTCTGCCCCT
CCACCAGTACCAGTGGTGCCACATGTGGCAGCTCCTGTGGAAGTTTCCAGTTCCCAGTAT
GTGGCCCAGAGTGATGGTGTAGTACACCAAGACTCCAGCGTTGCTGTCTTGCCAGTGCCG
GCCCCCGGCCCAGTTCAGGGACAGAATTATAGTGTTTGGGATTCAAACCAACAGTCTGTC
AGTGTACAGCAGCAGTACTCTCCTGCACAGTCTCAAGCAACCATATATTATCAAGGACAG
ACATGTCCAACAGTCTATGGTGTGACATCACCTTATTCACAGACAACTCCACCAATTGTA
CAGAGTTATGCCCAGCCAAGTCTTCAGTATATCCAGGGGCAACAGATTTTCACAGCTCAT
CCACAAGGAGTGGTGGTACAGCCAGCCGCAGCAGTGACTACAATAGTTGCACCAGGGCAG
CCTCAGCCCTTGCAGCCATCTGAAATGGTTGTGACAAATAATCTCTTGGATCTGCCGCCC
CCCTCTCCTCCCAAACCAAAAACCATTGTCTTACCTCCCAACTGGAAGACAGCTCGAGAT
CCAGAAGGGAAGATTTATTACTACCATGTGATCACAAGGCAGACTCAGTGGGATCCTCCT
ACTTGGGAAAGCCCAGGAGATGATGCCAGCCTTGAGCATGAAGCTGAGATGGACCTGGGA
ACTCCAACATATGATGAAAACCCCATGAAGGCCTCGAAAAAGCCCAAGACAGCAGAAGCA
GACACCTCCAGTGAACTAGCAAAGAAAAGCAAAGAAGTATTCAGAAAAGAGATGTCCCAG
TTCATCGTCCAGTGCCTGAACCCTTACCGGAAACCTGACTGCAAAGTGGGAAGAATTACC
ACAACTGAAGACTTTAAACATCTGGCTCGCAAGCTGACTCACGGTGTTATGAATAAGGAG
CTGAAGTACTGTAAGAATCCTGAGGACCTGGAGTGCAATGAGAATGTGAAACACAAAACC
AAGGAGTACATTAAGAAGTACATGCAGAAGTTTGGGGCTGTTTACAAACCCAAAGAGGAC
ACTGAATTAGAGTGA
Enzyme 43 GenBank Gene ID NM_014159.6 Link Image
Enzyme 43 GeneCard ID SETD2 Link Image
Enzyme 43 GenAtlas ID SETD2 Link Image
Enzyme 43 HGNC ID HGNC:18420 Link Image
Enzyme 43 Chromosome Location 3
Enzyme 43 Locus 3p21.31
Enzyme 43 SNPs SNPJam Report Link Image
Enzyme 43 General References
  1. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. Rega S, Stiewe T, Chang DI, Pollmeier B, Esche H, Bardenheuer W, Marquitan G, Putzer BM: Identification of the full-length huntingtin- interacting protein p231HBP/HYPB as a DNA-binding factor. Mol Cell Neurosci. 2001 Jul;18(1):68-79. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Sun XJ, Wei J, Wu XY, Hu M, Wang L, Wang HH, Zhang QH, Chen SJ, Huang QH, Chen Z: Identification and characterization of a novel human histone H3 lysine 36-specific methyltransferase. J Biol Chem. 2005 Oct 21;280(42):35261-71. Epub 2005 Aug 22. [PubMed Link Image]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. Passani LA, Bedford MT, Faber PW, McGinnis KM, Sharp AH, Gusella JF, Vonsattel JP, MacDonald ME: Huntingtin's WW domain partners in Huntington's disease post-mortem brain fulfill genetic criteria for direct involvement in Huntington's disease pathogenesis. Hum Mol Genet. 2000 Sep 1;9(14):2175-82. [PubMed Link Image]
  12. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  13. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  14. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  15. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  16. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  17. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  18. Li M, Phatnani HP, Guan Z, Sage H, Greenleaf AL, Zhou P: Solution structure of the Set2-Rpb1 interacting domain of human Set2 and its interaction with the hyperphosphorylated C-terminal domain of Rpb1. Proc Natl Acad Sci U S A. 2005 Dec 6;102(49):17636-41. Epub 2005 Nov 28. [PubMed Link Image]
Enzyme 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 14778
Enzyme 44 Name Histone-lysine N-methyltransferase SETMAR
Enzyme 44 Synonyms
  1. SET domain and mariner transposase fusion gene-containing protein
  2. HsMar1
  3. Metnase
  4. Histone-lysine N-methyltransferase
  5. Mariner transposase Hsmar1
Enzyme 44 Gene Name SETMAR
Enzyme 44 Protein Sequence >Histone-lysine N-methyltransferase SETMAR
MAEFKEKPEAPTEQLDVACGQENLPVGAWPPGAAPAPFQYTPDHVVGPGADIDPTQITFP
GCICVKTPCLPGTCSCLRHGENYDDNSCLRDIGSGGKYAEPVFECNVLCRCSDHCRNRVV
QKGLQFHFQVFKTHKKGWGLRTLEFIPKGRFVCEYAGEVLGFSEVQRRIHLQTKSDSNYI
IAIREHVYNGQVMETFVDPTYIGNIGRFLNHSCEPNLLMIPVRIDSMVPKLALFAAKDIV
PEEELSYDYSGRYLNLTVSEDKERLDHGKLRKPCYCGAKSCTAFLPFDSSLYCPVEKSNI
SCGNEKEPSMCGSAPSVFPSCKRLTLETMKMMLDKKQIRAIFLFEFKMGRKAAETTRNIN
NAFGPGTANERTVQWWFKKFCKGDESLEDEERSGRPSEVDNDQLRAIIEADPLTTTREVA
EELNVNHSTVVRHLKQIGKVKKLDKWVPHELTENQKNRRFEVSSSLILRNHNEPFLDRIV
TCDEKWILYDNRRRSAQWLDQEEAPKHFPKPILHPKKVMVTIWWSAAGLIHYSFLNPGET
ITSEKYAQEIDEMNQKLQRLQLALVNRKGPILLHDNARPHVAQPTLQKLNELGYEVLPHP
PYSPDLLPTNYHVFKHLNNFLQGKRFHNQQDAENAFQEFVESQSTDFYATGINQLISRWQ
KCVDCNGSYFD
Enzyme 44 Number of Residues 671
Enzyme 44 Molecular Weight 76668.7
Enzyme 44 Theoretical pI 7.05
Enzyme 44 GO Classification
Function
  • DNA binding
  • binding
  • catalytic activity
  • cation binding
  • histone-lysine N-methyltransferase activity
  • ion binding
  • metal 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
  • transposase activity
  • zinc ion binding
Process
  • DNA integration
  • DNA metabolic process
  • DNA recombination
  • cellular component organization at cellular level
  • cellular macromolecule metabolic process
  • cellular process
  • chromatin modification
  • chromatin organization
  • chromosome organization
  • macromolecule metabolic process
  • metabolic process
  • organelle organization
  • transposition, DNA-mediated
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 44 General Function Involved in zinc ion binding
Enzyme 44 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'. Has sequence-specific DNA-binding activity and recognizes the 19-mer core of the 5'-terminal inverted repeats (TIRs) of the Hsmar1 element. Has DNA nicking activity. Has in vivo end joining activity and may mediate genomic integration of foreign DNA
Enzyme 44 Pathways
Enzyme 44 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 44 Pfam Domain Function
Enzyme 44 Signals
  • None
Enzyme 44 Transmembrane Regions
  • None
Enzyme 44 Essentiality Not Available
Enzyme 44 GenBank ID Protein 62897027 Link Image
Enzyme 44 UniProtKB/Swiss-Prot ID Q53H47 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name SETMR_HUMAN Link Image
Enzyme 44 PDB ID Not Available
Enzyme 44 Cellular Location Not Available
Enzyme 44 Gene Sequence >2016 bp
ATGGCGGAGTTTAAGGAGAAGCCTGAGGCCCCGACTGAGCAGCTGGATGTCGCGTGCGGC
CAGGAAAACTTGCCGGTGGGCGCGTGGCCCCCGGGGGCCGCGCCGGCGCCCTTCCAGTAC
ACTCCTGATCATGTAGTTGGACCTGGAGCAGACATTGATCCCACTCAAATAACCTTTCCC
GGATGCATTTGTGTCAAAACTCCCTGCCTCCCTGGCACTTGCTCCTGTCTCCGCCATGGA
GAGAACTATGATGATAACTCATGCCTTAGAGATATAGGATCTGGAGGAAAGTATGCAGAG
CCTGTTTTTGAATGCAATGTCCTGTGCCGATGCAGTGACCACTGCAGAAACAGAGTGGTC
CAGAAAGGTCTACAGTTCCACTTCCAAGTGTTCAAGACGCATAAAAAAGGCTGGGGACTT
CGTACCTTGGAATTTATACCGAAAGGAAGGTTTGTCTGTGAATATGCTGGTGAGGTTTTA
GGATTCTCTGAAGTTCAGAGAAGAATTCACTTACAAACAAAATCCGACTCCAATTACATT
ATAGCCATCAGGGAACATGTTTATAATGGGCAGGTAATGGAAACATTTGTTGACCCTACT
TATATAGGAAATATTGGAAGATTCCTTAATCATTCTTGTGAGCCAAACCTTTTGATGATT
CCTGTCCGAATTGACTCAATGGTACCTAAGTTGGCACTTTTTGCAGCCAAAGATATTGTG
CCAGAAGAAGAACTCTCTTATGATTATTCAGGAAGATATCTTAATCTAACAGTCAGTGAA
GACAAAGAAAGGCTAGATCATGGGAAACTAAGGAAACCTTGTTACTGTGGTGCCAAATCA
TGTACTGCTTTCCTGCCTTTTGACAGTTCTCTGTACTGCCCCGTAGAAAAGTCGAACATC
AGTTGTGGAAATGAGAAGGAACCCAGCATGTGTGGCTCAGCCCCTTCTGTGTTCCCCTCC
TGCAAGCGATTGACCCTTGAGACTATGAAAATGATGTTAGACAAAAAGCAAATTCGAGCA
ATTTTCTTATTCGAGTTCAAAATGGGTCGTAAAGCAGCAGAAACAACTCGCAACATCAAC
AATGCATTTGGCCCAGGAACTGCTAACGAACGTACAGTGCAGTGGTGGTTCAAGAAGTTT
TGCAAAGGAGATGAGAGCCTTGAAGATGAGGAGCGTAGTGGCCGGCCATCAGAAGTTGAC
AACGACCAGTTGAGAGCAATCATCGAAGCTGATCCCCTTACAACTACACGAGAAGTTGCT
GAAGAACTCAATGTCAACCATTCTACGGTCGTTCGACATTTGAAGCAAATTGGAAAGGTG
AAAAAGCTCGATAAGTGGGTGCCTCATGAGCTGACTGAAAATCAAAAAAATCGTCGTTTT
GAAGTGTCATCTTCTCTTATTCTACGCAACCACAACGAACCATTTCTCGATCGGATTGTG
ACGTGTGATGAAAAGTGGATTTTATATGACAACCGGCGACGATCAGCTCAGTGGTTGGAT
CAAGAAGAAGCTCCAAAGCACTTCCCAAAGCCAATCTTGCACCCAAAAAAGGTCATGGTC
ACTATTTGGTGGTCTGCTGCTGGTCTGATCCACTACAGCTTTCTGAATCCCGGTGAAACC
ATTACATCTGAGAAGTATGCTCAGGAAATCGATGAGATGAACCAAAAACTGCAACGCCTG
CAGCTGGCATTGGTCAACAGAAAGGGCCCAATTCTTCTCCACGACAATGCCCGACCGCAT
GTTGCACAACCCACACTTCAAAAGTTGAATGAATTGGGCTATGAAGTTTTGCCTCATCCA
CCGTATTCACCTGACCTCTTGCCAACCAACTACCACGTCTTTAAGCATCTCAACAACTTT
TTGCAGGGAAAACGCTTCCACAACCAGCAGGATGCAGAAAATGCTTTCCAAGAGTTCGTC
GAATCCCAAAGCACGGATTTTTACGCTACAGGAATAAACCAACTTATTTCTCGTTGGCAA
AAATGTGTTGATTGTAATGGTTCCTATTTTGATTAA
Enzyme 44 GenBank Gene ID AK222734 Link Image
Enzyme 44 GeneCard ID SETMAR Link Image
Enzyme 44 GenAtlas ID SETMAR Link Image
Enzyme 44 HGNC ID HGNC:10762 Link Image
Enzyme 44 Chromosome Location 3
Enzyme 44 Locus 3p26.1
Enzyme 44 SNPs SNPJam Report Link Image
Enzyme 44 General References
  1. Lee SH, Oshige M, Durant ST, Rasila KK, Williamson EA, Ramsey H, Kwan L, Nickoloff JA, Hromas R: The SET domain protein Metnase mediates foreign DNA integration and links integration to nonhomologous end-joining repair. Proc Natl Acad Sci U S A. 2005 Dec 13;102(50):18075-80. Epub 2005 Dec 6. [PubMed Link Image]
  2. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Cordaux R, Udit S, Batzer MA, Feschotte C: Birth of a chimeric primate gene by capture of the transposase gene from a mobile element. Proc Natl Acad Sci U S A. 2006 May 23;103(21):8101-6. Epub 2006 May 3. [PubMed Link Image]
  5. 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]
  6. Roman Y, Oshige M, Lee YJ, Goodwin K, Georgiadis MM, Hromas RA, Lee SH: Biochemical characterization of a SET and transposase fusion protein, Metnase: its DNA binding and DNA cleavage activity. Biochemistry. 2007 Oct 9;46(40):11369-76. Epub 2007 Sep 18. [PubMed Link Image]
  7. Miskey C, Papp B, Mates L, Sinzelle L, Keller H, Izsvak Z, Ivics Z: The ancient mariner sails again: transposition of the human Hsmar1 element by a reconstructed transposase and activities of the SETMAR protein on transposon ends. Mol Cell Biol. 2007 Jun;27(12):4589-600. Epub 2007 Apr 2. [PubMed Link Image]
  8. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
Enzyme 44 Metabolite References Not Available
Enzyme 45 [top]
Enzyme 45 ID 14780
Enzyme 45 Name Histone-lysine N-methyltransferase SUV420H1
Enzyme 45 Synonyms
  1. Lysine N-methyltransferase 5B
  2. Suppressor of variegation 4-20 homolog 1
  3. Su(var)4-20 homolog 1
  4. Suv4-20h1
Enzyme 45 Gene Name SUV420H1
Enzyme 45 Protein Sequence >Histone-lysine N-methyltransferase SUV420H1
MKWLGESKIMVVNGRRNGGKLSNDHQQNQSKLQHTGKDTLKAGKNAVERRSNRCNGNSGF
EGQSRYVPSSGMSAKELCENDDLATSLVLDPYLGFQTHKMNTSAFPSRSSRHFSKSDSFS
HNNPVRFRPIKGRQEELKEVIERFKKDEHLEKAFKCLTSGEWARHYFLNKNKMQEKLFKE
HVFIYLRMFATDSGFEILPCNRYSSEQNGAKIVATKEWKRNDKIELLVGCIAELSEIEEN
MLLRHGENDFSVMYSTRKNCAQLWLGPAAFINHDCRPNCKFVSTGRDTACVKALRDIEPG
EEISCYYGDGFFGENNEFCECYTCERRGTGAFKSRVGLPAPAPVINSKYGLRETDKRLNR
LKKLGDSSKNSDSQSVSSNTDADTTQEKNNATSNRKSSVGVKKNSKSRTLTRQSMSRIPA
SSNSTSSKLTHINNSRVPKKLKKPAKPLLSKIKLRNHCKRLEQKNASRKLEMGNLVLKEP
KVVLYKNLPIKKDKEPEGPAQAAVASGCLTRHAAREHRQNPVRGAHSQGESSPCTYITRR
SVRTRTNLKEASDIKLEPNTLNGYKSSVTEPCPDSGEQLQPAPVLQEEELAHETAQKGEA
KCHKSDTGMSKKKSRQGKLVKQFAKIEESTPVHDSPGKDDAVPDLMGPHSDQGEHSGTVG
VPVSYTDCAPSPVGCSVVTSDSFKTKDSFRTAKSKKKRRITRYDAQLILENNSGIPKLTL
RRRHDSSSKTNDQENDGMNSSKISIKLSKDHDNDNNLYVAKLNNGFNSGSGSSSTKLKIQ
LKRDEENRGSYTEGLHENGVCCSDPLSLLESRMEVDDYSQYEEESTDDSSSSEGDEEEDD
YDDDFEDDFIPLPPAKRLRLIVGKDSIDIDISSRRREDQSLRLNA
Enzyme 45 Number of Residues 885
Enzyme 45 Molecular Weight 99186.1
Enzyme 45 Theoretical pI 9.05
Enzyme 45 GO Classification Not Available
Enzyme 45 General Function Involved in protein binding
Enzyme 45 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 45 Pathways
Enzyme 45 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 45 Pfam Domain Function
Enzyme 45 Signals
  • None
Enzyme 45 Transmembrane Regions
  • None
Enzyme 45 Essentiality Not Available
Enzyme 45 GenBank ID Protein 50659082 Link Image
Enzyme 45 UniProtKB/Swiss-Prot ID Q4FZB7 Link Image
Enzyme 45 UniProtKB/Swiss-Prot Entry Name SV421_HUMAN Link Image
Enzyme 45 PDB ID Not Available
Enzyme 45 Cellular Location Not Available
Enzyme 45 Gene Sequence >2658 bp
ATGAAGTGGTTGGGAGAATCCAAGAACATGGTGGTGAATGGCAGGAGAAATGGAGGCAAG
TTGTCTAATGACCATCAGCAGAATCAATCAAAATTACAGCACACGGGGAAGGACACCCTG
AAGGCTGGCAAAAATGCAGTCGAGAGGAGGTCGAACAGATGTAATGGTAACTCGGGATTT
GAAGGACAGAGTCGCTATGTACCATCCTCTGGAATGTCCGCCAAGGAACTCTGTGAAAAT
GATGACCTAGCAACCAGTTTGGTTCTTGATCCCTATTTAGGTTTTCAAACACACAAAATG
AATACTAGCGCCTTTCCTTCGAGGAGCTCAAGGCATTTTTCAAAATCTGACAGTTTTTCT
CACAACAACCCTGTGAGATTTAGGCCTATTAAAGGAAGGCAGGAAGAACTAAAGGAAGTA
ATTGAACGTTTTAAGAAAGATGAACACTTGGAGAAAGCCTTCAAATGTTTGACTTCAGGC
GAATGGGCACGGCACTATTTTCTCAACAAGAATAAAATGCAGGAGAAATTATTCAAAGAA
CATGTATTTATTTATTTGCGAATGTTTGCAACTGACAGTGGATTTGAAATATTGCCATGT
AATAGATACTCATCAGAACAAAATGGAGCCAAAATAGTTGCAACAAAAGAGTGGAAACGA
AATGACAAAATAGAATTACTGGTGGGTTGTATTGCCGAACTTTCAGAAATTGAGGAGAAC
ATGCTACTTAGACATGGAGAAAACGACTTCAGTGTCATGTACTCCACAAGGAAAAACTGT
GCTCAACTCTGGCTGGGTCCTGCTGCGTTTATAAACCATGATTGCAGACCTAATTGTAAG
TTTGTGTCAACTGGTCGAGATACAGCATGTGTGAAGGCTCTAAGAGACATTGAACCTGGA
GAAGAAATTTCTTGTTATTATGGAGATGGGTTCTTTGGAGAAAATAATGAGTTCTGCGAG
TGTTACACTTGCGAAAGACGGGGCACTGGTGCTTTTAAATCCAGAGTGGGACTGCCTGCG
CCTGCTCCTGTTATCAATAGCAAATATGGACTCAGAGAAACAGATAAACGTTTAAATAGG
CTTAAAAAGTTAGGTGACAGCAGCAAAAATTCAGACAGTCAATCTGTCAGCTCTAACACT
GATGCAGATACCACTCAGGAAAAAAACAATGCAACTTCTAACCGAAAATCTTCAGTTGGC
GTAAAAAAGAATAGCAAGAGCAGAACGTTAACGAGGCAATCTATGTCAAGAATTCCAGCT
TCTTCCAACTCTACCTCATCTAAGCTAACTCATATAAATAATTCCAGGGTACCAAAGAAA
CTGAAGAAGCCTGCAAAGCCTTTACTTTCAAAGATAAAATTGAGAAATCATTGCAAGCGG
CTGGAGCAAAAGAATGCTTCAAGAAAACTCGAAATGGGAAACTTAGTACTGAAAGAGCCT
AAAGTAGTTCTGTATAAAAATTTGCCCATTAAAAAAGATAAGGAGCCAGAGGGACCAGCC
CAAGCCGCAGTTGCCAGCGGGTGCTTGACTAGACACGCGGCGAGAGAACACAGACAGAAT
CCTGTGAGAGGTGCTCATTCGCAGGGGGAGAGCTCGCCCTGCACCTACATAACTCGGCGG
TCAGTGAGGACAAGAACAAATCTGAAGGAGGCCTCTGACATCAAGCTTGAACCAAATACG
TTGAATGGCTATAAAAGCAGTGTGACGGAACCTTGCCCCGACAGTGGTGAACAGCTGCAG
CCAGCTCCTGTGCTGCAGGAGGAAGAACTGGCTCATGAGACTGCACAAAAAGGGGAGGCA
AAGTGTCATAAGAGTGACACAGGCATGTCCAAAAAGAAGTCACGACAAGGAAAACTTGTG
AAACAGTTTGCAAAAATAGAGGAATCTACTCCAGTGCACGATTCTCCTGGAAAAGACGAC
GCGGTACCAGATTTGATGGGTCCCCATTCTGACCAGGGTGAGCACAGTGGCACTGTGGGC
GTGCCTGTGAGCTACACAGACTGTGCTCCTTCACCCGTCGGTTGTTCAGTTGTGACATCA
GATAGCTTCAAAACAAAAGACAGCTTTAGAACTGCAAAAAGTAAAAAGAAGAGGCGAATC
ACAAGGTATGATGCACAGTTAATCCTAGAAAATAACTCTGGGATTCCCAAATTGACTCTT
CGTAGGCGTCATGATAGCAGCAGCAAAACAAATGACCAAGAGAATGATGGAATGAACTCT
TCCAAAATAAGCATCAAGTTAAGCAAAGACCATGACAACGATAACAATCTCTATGTAGCA
AAGCTTAATAATGGATTTAACTCAGGATCAGGCAGTAGTTCTACAAAATTAAAAATCCAG
CTAAAACGAGATGAGGAAAATAGGGGGTCTTATACAGAGGGGCTTCATGAAAATGGGGTG
TGCTGCAGTGATCCTCTTTCTCTCTTGGAGTCTCGAATGGAGGTGGATGACTATAGTCAG
TATGAGGAAGAAAGTACAGATGATTCCTCCTCTTCTGAGGGCGATGAAGAGGAGGATGAC
TATGATGATGACTTTGAAGACGATTTTATTCCTCTTCCTCCAGCTAAGCGCTTGAGGTTA
ATAGTTGGAAAAGACTCTATAGATATTGACATTTCTTCAAGGAGAAGAGAAGATCAGTCT
TTAAGGCTTAATGCCTAA
Enzyme 45 GenBank Gene ID NM_017635.3 Link Image
Enzyme 45 GeneCard ID SUV420H1 Link Image
Enzyme 45 GenAtlas ID SUV420H1 Link Image
Enzyme 45 HGNC ID HGNC:24283 Link Image
Enzyme 45 Chromosome Location 1
Enzyme 45 Locus 11q13.2
Enzyme 45 SNPs SNPJam Report Link Image
Enzyme 45 General References
  1. Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. 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]
  4. 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]
  5. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  6. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  7. Tryndyak VP, Kovalchuk O, Pogribny IP: Loss of DNA methylation and histone H4 lysine 20 trimethylation in human breast cancer cells is associated with aberrant expression of DNA methyltransferase 1, Suv4-20h2 histone methyltransferase and methyl-binding proteins. Cancer Biol Ther. 2006 Jan;5(1):65-70. [PubMed Link Image]
Enzyme 45 Metabolite References Not Available
Enzyme 46 [top]
Enzyme 46 ID 14781
Enzyme 46 Name Histone-lysine N-methyltransferase SUV420H2
Enzyme 46 Synonyms
  1. Lysine N-methyltransferase 5C
  2. Suppressor of variegation 4-20 homolog 2
  3. Su(var)4-20 homolog 2
  4. Suv4-20h2
Enzyme 46 Gene Name SUV420H2
Enzyme 46 Protein Sequence >Histone-lysine N-methyltransferase SUV420H2
MGPDRVTARELCENDDLATSLVLDPYLGFRTHKMNVSPVPPLRRQQHLRSALETFLRQRD
LEAAYRALTLGGWTARYFQSRGPRQEAALKTHVYRYLRAFLPESGFTILPCTRYSMETNG
AKIVSTRAWKKNEKLELLVGCIAELREADEGLLRAGENDFSIMYSTRKRSAQLWLGPAAF
INHDCKPNCKFVPADGNAACVKVLRDIEPGDEVTCFYGEGFFGEKNEHCECHTCERKGEG
AFRTRPREPALPPRPLDKYQLRETKRRLQQGLDSGSRQGLLGPRACVHPSPLRRDPFCAA
CQPLRLPACSARPDTSPLWLQWLPQPQPRVRPRKRRRPRPRRAPVLSTHHAARVSLHRWG
GCGPHCRLRGEALVALGQPPHARWAPQQDWHWARRYGLPYVVRVDLRRLAPAPPATPAPA
GTPGPILIPKQALAFAPFSPPKRLRLVVSHGSIDLDVGGEEL
Enzyme 46 Number of Residues 462
Enzyme 46 Molecular Weight 52112.4
Enzyme 46 Theoretical pI 10.31
Enzyme 46 GO Classification Not Available
Enzyme 46 General Function Involved in protein binding
Enzyme 46 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 46 Pathways
Enzyme 46 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 46 Pfam Domain Function
Enzyme 46 Signals
  • None
Enzyme 46 Transmembrane Regions
  • None
Enzyme 46 Essentiality Not Available
Enzyme 46 GenBank ID Protein 31543169 Link Image
Enzyme 46 UniProtKB/Swiss-Prot ID Q86Y97 Link Image
Enzyme 46 UniProtKB/Swiss-Prot Entry Name SV422_HUMAN Link Image
Enzyme 46 PDB ID Not Available
Enzyme 46 Cellular Location Not Available
Enzyme 46 Gene Sequence >1389 bp
ATGGGGCCCGACAGAGTGACAGCACGAGAACTGTGCGAGAACGACGACCTGGCCACCAGC
CTCGTCCTGGACCCCTACCTCGGTTTCCGCACCCATAAGATGAACGTCAGCCCTGTGCCC
CCCCTGCGGCGACAGCAGCACCTGCGCTCAGCGCTGGAAACTTTCCTGAGGCAGCGGGAC
CTGGAGGCTGCGTACCGGGCCCTGACGCTGGGAGGCTGGACGGCCCGCTACTTCCAGAGC
CGGGGCCCGCGGCAGGAGGCTGCCCTCAAGACCCACGTCTATCGCTACCTCCGTGCCTTC
CTGCCGGAAAGTGGCTTTACCATCCTGCCCTGCACGCGCTACTCCATGGAGACCAACGGG
GCCAAGATCGTGTCCACTCGTGCTTGGAAAAAGAATGAGAAGCTGGAGCTGCTGGTGGGC
TGCATTGCAGAGCTGCGGGAGGCAGATGAGGGGCTGCTGAGGGCCGGTGAGAATGACTTC
AGCATCATGTACTCAACCCGCAAGCGGAGTGCTCAGCTGTGGCTGGGCCCAGCCGCCTTC
ATCAACCATGACTGCAAACCCAACTGCAAGTTTGTGCCTGCAGATGGGAACGCAGCCTGC
GTGAAGGTGCTCCGGGACATTGAGCCTGGGGACGAGGTGACATGCTTCTACGGCGAGGGC
TTCTTCGGCGAGAAGAATGAGCACTGTGAATGCCACACCTGTGAGAGGAAAGGTGAAGGA
GCTTTCCGAACCAGGCCTAGGGAGCCCGCGTTGCCACCACGGCCCCTGGACAAGTACCAG
CTGCGTGAGACCAAGCGGCGGCTGCAGCAAGGCCTGGACAGTGGCAGCCGACAGGGCCTG
CTGGGCCCTCGGGCCTGCGTGCACCCATCCCCGCTGCGCCGGGACCCATTCTGCGCCGCC
TGCCAGCCCCTGCGCCTGCCAGCCTGCAGCGCCCGCCCAGACACCTCACCCCTCTGGCTC
CAGTGGCTGCCTCAGCCCCAGCCCCGAGTGCGGCCCCGGAAGCGCCGACGCCCCCGGCCC
CGGAGGGCCCCAGTGCTCTCCACCCACCACGCTGCCCGCGTCTCCCTGCACCGATGGGGA
GGCTGTGGCCCCCACTGCCGCCTGCGAGGAGAGGCCCTGGTGGCCCTGGGCCAGCCCCCC
CACGCCCGCTGGGCCCCTCAGCAGGACTGGCACTGGGCCCGGCGCTATGGGCTGCCTTAC
GTGGTGCGTGTGGACCTTCGTCGCCTGGCCCCAGCCCCACCAGCTACCCCAGCCCCTGCT
GGGACCCCAGGCCCCATCCTGATCCCGAAGCAGGCCCTCGCCTTCGCCCCCTTCTCCCCA
CCCAAGCGCCTACGGCTGGTGGTCAGCCACGGCTCCATCGACCTGGATGTCGGCGGTGAA
GAGCTGTGA
Enzyme 46 GenBank Gene ID NM_032701.3 Link Image
Enzyme 46 GeneCard ID SUV420H2 Link Image
Enzyme 46 GenAtlas ID SUV420H2 Link Image
Enzyme 46 HGNC ID HGNC:28405 Link Image
Enzyme 46 Chromosome Location 1
Enzyme 46 Locus 19q13.42
Enzyme 46 SNPs SNPJam Report Link Image
Enzyme 46 General References
  1. Wan D, Gong Y, Qin W, Zhang P, Li J, Wei L, Zhou X, Li H, Qiu X, Zhong F, He L, Yu J, Yao G, Jiang H, Qian L, Yu Y, Shu H, Chen X, Xu H, Guo M, Pan Z, Chen Y, Ge C, Yang S, Gu J: Large-scale cDNA transfection screening for genes related to cancer development and progression. Proc Natl Acad Sci U S A. 2004 Nov 2;101(44):15724-9. Epub 2004 Oct 21. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 46 Metabolite References Not Available
Enzyme 47 [top]
Enzyme 47 ID 14787
Enzyme 47 Name N(2),N(2)-dimethylguanosine tRNA methyltransferase
Enzyme 47 Synonyms
  1. tRNA 2,2-dimethylguanosine-26 methyltransferase
  2. tRNA(guanine-26,N(2)-N(2)) methyltransferase
  3. tRNA(m(2,2)G26)dimethyltransferase
Enzyme 47 Gene Name TRMT1
Enzyme 47 Protein Sequence >N(2),N(2)-dimethylguanosine tRNA methyltransferase
MQGSSLWLSLTFRSARVLSRARFFEWQSPGLPNTAAMENGTGPYGEERPREVQETTVTEG
AAKIAFPSANEVFYNPVQEFNRDLTCAVITEFARIQLGAKGIQIKVPGEKDTQKVVVDLS
EQEEEKVELKESENLASGDQPRTAAVGEICEEGLHVLEGLAASGLRSIRFALEVPGLRSV
VANDASTRAVDLIRRNVQLNDVAHLVQPSQADARMLMYQHQRVSERFDVIDLDPYGSPAT
FLDAAVQAVSEGGLLCVTCTDMAVLAGNSGETCYSKYGAMALKSRACHEMALRIVLHSLD
LRANCYQRFVVPLLSISADFYVRVFVRVFTGQAKVKASASKQALVFQCVGCGAFHLQRLG
KASGVPSGRAKFSAACGPPVTPECEHCGQRHQLGGPMWAEPIHDLDFVGRVLEAVSANPG
RFHTSERIRGVLSVITEELPDVPLYYTLDQLSSTIHCNTPSLLQLRSALLHADFRVSLSH
ACKNAVKTDAPASALWDIMRCWEKECPVKRERLSETSPAFRILSVEPRLQANFTIREDAN
PSSRQRGLKRFQANPEANWGPRPRARPGGKAADEAMEERRRLLQNKRKEPPEDVAQRAAR
LKTFPCKRFKEGTCQRGDQCCYSHSPPTPRVSADAAPDCPETSNQTPPGPGAAAGPGID
Enzyme 47 Number of Residues 659
Enzyme 47 Molecular Weight 72233.4
Enzyme 47 Theoretical pI 7.67
Enzyme 47 GO Classification
Function
  • N-methyltransferase activity
  • RNA binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • methyltransferase activity
  • nucleic acid binding
  • tRNA (guanine-N2-)-methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
  • transition metal ion binding
  • zinc ion binding
Process
  • RNA metabolic process
  • cellular macromolecule metabolic process
  • macromolecule metabolic process
  • metabolic process
  • ncRNA metabolic process
  • tRNA metabolic process
  • tRNA processing
Component
Enzyme 47 General Function Involved in RNA binding
Enzyme 47 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 47 Pathways Not Available
Enzyme 47 Reactions
  • S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N2-methylguanine [RN:R00598]
Enzyme 47 Pfam Domain Function
Enzyme 47 Signals
  • None
Enzyme 47 Transmembrane Regions
  • None
Enzyme 47 Essentiality Not Available
Enzyme 47 GenBank ID Protein 209862871 Link Image
Enzyme 47 UniProtKB/Swiss-Prot ID Q9NXH9 Link Image
Enzyme 47 UniProtKB/Swiss-Prot Entry Name TRM1_HUMAN Link Image
Enzyme 47 PDB ID Not Available
Enzyme 47 Cellular Location Not Available
Enzyme 47 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 47 GenBank Gene ID NM_001136035.2 Link Image
Enzyme 47 GeneCard ID TRMT1 Link Image
Enzyme 47 GenAtlas ID TRMT1 Link Image
Enzyme 47 HGNC ID HGNC:25980 Link Image
Enzyme 47 Chromosome Location 1
Enzyme 47 Locus 19p13.2
Enzyme 47 SNPs SNPJam Report Link Image
Enzyme 47 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]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  6. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  7. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  8. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
Enzyme 47 Metabolite References Not Available
Enzyme 48 [top]
Enzyme 48 ID 14788
Enzyme 48 Name tRNA (adenine-N(1)-)-methyltransferase catalytic subunit TRMT61A
Enzyme 48 Synonyms
  1. tRNA(m1A58)-methyltransferase subunit TRMT61A
  2. tRNA(m1A58)MTase subunit TRMT61A
Enzyme 48 Gene Name TRMT61A
Enzyme 48 Protein Sequence >tRNA (adenine-N(1)-)-methyltransferase catalytic subunit TRMT61A
MSFVAYEELIKEGDTAILSLGHGAMVAVRVQRGAQTQTRHGVLRHSVDLIGRPFGSKVTC
GRGGWVYVLHPTPELWTLNLPHRTQILYSTDIALITMMLELRPGSVVCESGTGSGSVSHA
IIRTIAPTGHLHTVEFHQQRAEKAREEFQEHRVGRWVTVRTQDVCRSGFGVSHVADAVFL
DIPSPWEAVGHAWDALKVEGGRFCSFSPCIEQVQRTCQALAARGFSELSTLEVLPQVYNV
RTVSLPPPDLGTGTDGPAGSDTSPFRSGTPMKEAVGHTGYLTFATKTPG
Enzyme 48 Number of Residues 289
Enzyme 48 Molecular Weight 31381.5
Enzyme 48 Theoretical pI 7.39
Enzyme 48 GO Classification
Function
  • RNA methyltransferase activity
  • catalytic activity
  • methyltransferase activity
  • tRNA (adenine) methyltransferase activity
  • tRNA (adenine-N1-)-methyltransferase activity
  • tRNA methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • RNA metabolic process
  • RNA methylation
  • RNA modification
  • cellular macromolecule metabolic process
  • macromolecule metabolic process
  • metabolic process
  • tRNA methylation
Component
Enzyme 48 General Function Involved in tRNA (adenine-N1-)-methyltransferase activity
Enzyme 48 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 48 Pathways Not Available
Enzyme 48 Reactions
  • S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N1-methyladenine [RN:R00596]
Enzyme 48 Pfam Domain Function
Enzyme 48 Signals
  • None
Enzyme 48 Transmembrane Regions
  • None
Enzyme 48 Essentiality Not Available
Enzyme 48 GenBank ID Protein 123173772 Link Image
Enzyme 48 UniProtKB/Swiss-Prot ID Q96FX7 Link Image
Enzyme 48 UniProtKB/Swiss-Prot Entry Name TRM61_HUMAN Link Image
Enzyme 48 PDB ID Not Available
Enzyme 48 Cellular Location Not Available
Enzyme 48 Gene Sequence >870 bp
ATGAGCTTCGTGGCATACGAGGAGCTGATCAAGGAGGGTGACACGGCCATCCTGTCACTG
GGCCATGGTGCAATGGTGGCAGTGCGTGTGCAGCGTGGGGCACAGACCCAGACCCGGCAT
GGTGTCCTGCGGCACTCAGTTGACCTTATCGGCCGCCCCTTCGGCTCCAAGGTGACGTGC
GGCCGAGGTGGCTGGGTGTATGTGCTGCACCCCACGCCCGAGCTCTGGACGCTGAACCTG
CCGCACCGCACGCAGATCCTCTACTCCACAGACATCGCCCTCATCACCATGATGTTGGAG
CTTCGGCCCGGCTCTGTGGTCTGTGAGTCTGGCACCGGCAGTGGCTCTGTGTCCCACGCC
ATCATCCGCACCATTGCACCCACGGGTCACCTGCACACGGTGGAGTTCCACCAGCAGCGG
GCAGAGAAGGCCCGGGAGGAGTTCCAGGAGCACCGTGTGGGCCGCTGGGTGACTGTGCGC
ACCCAGGACGTGTGCCGCAGTGGCTTTGGCGTGAGCCACGTGGCCGACGCCGTCTTCCTG
GACATCCCATCACCCTGGGAGGCCGTGGGCCACGCCTGGGACGCCCTCAAGGTCGAAGGC
GGGCGCTTCTGCTCCTTCTCACCGTGCATCGAGCAGGTGCAACGCACATGCCAGGCGCTG
GCAGCGCGCGGCTTCTCAGAGCTGAGCACCCTGGAGGTGCTGCCACAGGTCTACAACGTG
CGCACTGTCAGCCTGCCACCGCCCGACCTGGGCACAGGCACAGATGGCCCTGCCGGCTCC
GACACCAGCCCCTTCCGCAGCGGCACGCCCATGAAGGAGGCCGTGGGCCACACCGGCTAC
CTGACCTTCGCCACCAAGACCCCAGGCTAG
Enzyme 48 GenBank Gene ID NM_152307.2 Link Image
Enzyme 48 GeneCard ID TRMT61A Link Image
Enzyme 48 GenAtlas ID TRMT61A Link Image
Enzyme 48 HGNC ID HGNC:23790 Link Image
Enzyme 48 Chromosome Location 1
Enzyme 48 Locus 14q32
Enzyme 48 SNPs SNPJam Report Link Image
Enzyme 48 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [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]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Ozanick S, Krecic A, Andersland J, Anderson JT: The bipartite structure of the tRNA m1A58 methyltransferase from S. cerevisiae is conserved in humans. RNA. 2005 Aug;11(8):1281-90. [PubMed Link Image]
  5. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  6. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 48 Metabolite References Not Available
Enzyme 49 [top]
Enzyme 49 ID 14789
Enzyme 49 Name tRNA (guanine-N(7)-)-methyltransferase
Enzyme 49 Synonyms
  1. Methyltransferase-like protein 1
  2. tRNA(m7G46)-methyltransferase
Enzyme 49 Gene Name METTL1
Enzyme 49 Protein Sequence >tRNA (guanine-N(7)-)-methyltransferase
MAAETRNVAGAEAPPPQKRYYRQRAHSNPMADHTLRYPVKPEEMDWSELYPEFFAPLTQN
QSHDDPKDKKEKRAQAQVEFADIGCGYGGLLVELSPLFPDTLILGLEIRVKVSDYVQDRI
RALRAAPAGGFQNIACLRSNAMKHLPNFFYKGQLTKMFFLFPDPHFKRTKHKWRIISPTL
LAEYAYVLRVGGLVYTITDVLELHDWMCTHFEEHPLFERVPLEDLSEDPVVGHLGTSTEE
GKKVLRNGGKNFPAIFRRIQDPVLQAVTSQTSLPGH
Enzyme 49 Number of Residues 276
Enzyme 49 Molecular Weight 31470.8
Enzyme 49 Theoretical pI 7.73
Enzyme 49 GO Classification
Function
  • RNA methyltransferase activity
  • catalytic activity
  • methyltransferase activity
  • tRNA (guanine) methyltransferase activity
  • tRNA (guanine-N7-)-methyltransferase activity
  • tRNA methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • RNA metabolic process
  • cellular macromolecule metabolic process
  • macromolecule metabolic process
  • metabolic process
  • ncRNA metabolic process
  • tRNA metabolic process
  • tRNA modification
  • tRNA processing
Component
Enzyme 49 General Function Involved in tRNA (guanine-N7-)-methyltransferase activity
Enzyme 49 Specific Function Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA
Enzyme 49 Pathways Not Available
Enzyme 49 Reactions
  • S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N7-methylguanine [RN:R00600]
Enzyme 49 Pfam Domain Function
Enzyme 49 Signals
  • None
Enzyme 49 Transmembrane Regions
  • None
Enzyme 49 Essentiality Not Available
Enzyme 49 GenBank ID Protein 189054580 Link Image
Enzyme 49 UniProtKB/Swiss-Prot ID Q9UBP6 Link Image
Enzyme 49 UniProtKB/Swiss-Prot Entry Name TRMB_HUMAN Link Image
Enzyme 49 PDB ID Not Available
Enzyme 49 Cellular Location Not Available
Enzyme 49 Gene Sequence >831 bp
ATGGCAGCCGAGACTCGGAACGTGGCCGGAGCAGAGGCCCCACCGCCCCAGAAGCGCTAC
TACCGGCAACGTGCTCACTCCAACCCCATGGCGGACCACACGCTGCGCTACCCTGTGAAG
CCAGAGGAGATGGACTGGTCTGAGCTATACCCAGAGTTCTTCGCTCCACTCACTCAAAAT
CAGAGCCACGATGACCCAAAGGATAAGAAAGAAAAGAGAGCTCAGGCCCAAGTGGAGTTT
GCAGACATAGGCTGTGGCTATGGTGGCCTGTTAGTGGAACTGTCACCGCTGTTCCCAGAC
ACACTTATTCTGGGTCTGGAGATCCGGGTGAAGGTCTCAGACTATGTACAAGACCGGATT
CGGGCCCTACGCGCAGCTCCTGCAGGTGGCTTCCAGAACATCGCCTGTCTCCGTAGCAAT
GCCATGAAGCACCTTCCTAACTTCTTCTACAAGGGCCAGCTGACAAAGATGTTCTTCCTC
TTCCCCGACCCACATTTCAAGCGGACAAAGCACAAGTGGCGAATCATCAGTCCCACCCTG
CTAGCAGAATATGCCTACGTGCTAAGAGTTGGGGGGCTGGTGTATACCATAACCGATGTG
CTGGAGCTACACGACTGGATGTGCACTCATTTCGAAGAGCACCCACTGTTTGAGCGTGTG
CCTCTGGAGGACCTGAGTGAAGACCCCGTTGTGGGACATCTAGGCACCTCAACTGAGGAG
GGGAAGAAAGTTCTACGTAATGGAGGGAAGAATTTCCCAGCCATCTTCCGAAGAATACAA
GATCCCGTCCTCCAGGCAGTGACCTCCCAAACCAGCCTGCCTGGTCACTGA
Enzyme 49 GenBank Gene ID AK314851 Link Image
Enzyme 49 GeneCard ID METTL1 Link Image
Enzyme 49 GenAtlas ID METTL1 Link Image
Enzyme 49 HGNC ID HGNC:7030 Link Image
Enzyme 49 Chromosome Location 1
Enzyme 49 Locus 12q13
Enzyme 49 SNPs SNPJam Report Link Image
Enzyme 49 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. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. 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]
  5. Cartlidge RA, Knebel A, Peggie M, Alexandrov A, Phizicky EM, Cohen P: The tRNA methylase METTL1 is phosphorylated and inactivated by PKB and RSK in vitro and in cells. EMBO J. 2005 May 4;24(9):1696-705. Epub 2005 Apr 14. [PubMed Link Image]
  6. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
Enzyme 49 Metabolite References Not Available
Enzyme 50 [top]
Enzyme 50 ID 15244
Enzyme 50 Name 5-methyltetrahydrofolate-homocysteine methyltransferase reductase
Enzyme 50 Synonyms Not Available
Enzyme 50 Gene Name MTRR
Enzyme 50 Protein Sequence >5-methyltetrahydrofolate-homocysteine methyltransferase reductase
MRRFLLLYATQQGQAKAIAEEICEQAVVHGFSADLHCISESDKYDLKTETAPLVVVVSTT
GTGDPPDTARKFVKEIQNQTLPVDFFAHLRYGLLGLGDSEYTYFCNGGKIIDKRLQELGA
RHFYDTGHADDCVGLELVVEPWIAGLWPALRKHFRSSRGQEEISGALPVASPASSRTDLV
KSELLHIESQVELLRFDDSGRKDSEVLKQNAVNSNQSNVVIEDFESSLTRSVPPLSQASL
NIPGLPPEYLQVHLQESLGQEESQVSVTSADPVFQVPISKAVQLTTNDAIKTTLLVELDI
SNTDFSYQPGDAFSVICPNSDSEVQSLLQRLQLEDKREHCVLLKIKADTKKKGATLPQHI
PAGCSLQFIFTWCLEIRAIPKKAFLRALVDYTSDSAEKRRLQELCSKQGAADYSRFVRDA
CACLLDLLLAFPSCQPPLSLLLEHLPKLQPRPYSCASSSLFHPGKLHFVFNIVEFLSTAT
TEVLRKGVCTGWLALLVASVLQPNIHASHEDSGKALAPKISISPRTTNSFHLPDDPSIPI
IMVGPGTGIAPFIGFLQHREKLQEQHPDGNFGAMWLFFGCRHKDRDYLFRKELRHFLKHG
ILTHLKVSFSRDAPVGEEEAPAKYVQDNIQLHGQQVARILLQENGHIYVCGDAKNMAKDV
HDALVQIISKEVGVEKLEAMKTLATLKEEKRYLQDIWS
Enzyme 50 Number of Residues 698
Enzyme 50 Molecular Weight 77673.0
Enzyme 50 Theoretical pI 6.47
Enzyme 50 GO Classification
Function
  • FMN binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • nucleotide binding
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 50 General Function Involved in oxidoreductase activity
Enzyme 50 Specific Function Not Available
Enzyme 50 Pathways Not Available
Enzyme 50 Reactions Not Available
Enzyme 50 Pfam Domain Function
Enzyme 50 Signals
  • None
Enzyme 50 Transmembrane Regions
  • None
Enzyme 50 Essentiality Not Available
Enzyme 50 GenBank ID Protein 127798340 Link Image
Enzyme 50 UniProtKB/Swiss-Prot ID Q7Z4M8 Link Image
Enzyme 50 UniProtKB/Swiss-Prot Entry Name Q7Z4M8_HUMAN Link Image
Enzyme 50 PDB ID Not Available
Enzyme 50 Cellular Location Not Available
Enzyme 50 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 50 GenBank Gene ID BC054816 Link Image
Enzyme 50 GeneCard ID MTRR Link Image
Enzyme 50 GenAtlas ID MTRR Link Image
Enzyme 50 HGNC ID HGNC:7473 Link Image
Enzyme 50 Chromosome Location 5
Enzyme 50 Locus 5p15.31
Enzyme 50 SNPs SNPJam Report Link Image
Enzyme 50 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 50 Metabolite References Not Available
Enzyme 51 [top]
Enzyme 51 ID 15862
Enzyme 51 Name DNA (cytosine-5)-methyltransferase 3-like
Enzyme 51 Synonyms Not Available
Enzyme 51 Gene Name DNMT3L
Enzyme 51 Protein Sequence >DNA (cytosine-5)-methyltransferase 3-like
MAAIPALDPEAEPSMDVILVGSSELSSSVSPGTGRDLIAYEVKANQRNIEDICICCGSLQ
VHTQHPLFEGGICAPCKDKFLDALFLYDDDGYQSYCSICCSGETLLICGNPDCTRCYCFE
CVDSLVGPGTSGKVHAMSNWVCYLCLPSSRSGLLQRRRKWRSQLKAFYDRESENPLEMFE
TVPVWRRQPVRVLSLFEDIKKELTSLGFLESGSDPGQLKHVVDVTDTVRKDVEEWGPFDL
VYGATPPLGHTCDRPPSWYLFQFHRLLQYARPKPGSPRPFFWMFVDNLVLNKEDLDVASR
FLEMEPVTIPDVHGGSLQNAVRVWSNIPAIRSSRHWALVSEEELSLLAQNKQSSKLAAKW
PTKLVKNCFLPLREYFKYFSTELTSSL
Enzyme 51 Number of Residues 387
Enzyme 51 Molecular Weight 43669.5
Enzyme 51 Theoretical pI 5.67
Enzyme 51 GO Classification
Function
  • binding
  • cation binding
  • ion binding
  • metal ion binding
  • transition metal ion binding
  • zinc ion binding
Process
Component
Enzyme 51 General Function Involved in zinc ion binding
Enzyme 51 Specific Function Catalytically inactive regulatory factor of DNA methyltransferases. It is essential for the function of DNMT3A and DNMT3B. Activates DNMT3A and DNMT3B by binding to their catalytic domain. Accelerates the binding of DNA and AdoMet to the methyltransferases and dissociates from the complex after DNA binding to the methyltransferases. Recognizes unmethylated histone H3 lysine 4 (H3K4) and induces de novo DNA methylation by recruitment or activation of DNMT3
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 6180116 Link Image
Enzyme 51 UniProtKB/Swiss-Prot ID Q9UJW3 Link Image
Enzyme 51 UniProtKB/Swiss-Prot Entry Name DNM3L_HUMAN Link Image
Enzyme 51 PDB ID Not Available
Enzyme 51 Cellular Location Not Available
Enzyme 51 Gene Sequence >1164 bp
ATGGCGGCCATCCCAGCCCTGGACCCAGAGGCCGAGCCCAGCATGGACGTGATTTTGGTG
GGATCCAGTGAGCTCTCAAGCTCCGTTTCACCCGGGACAGGCAGAGATCTTATTGCATAT
GAAGTCAAGGCTAACCAGCGAAATATAGAAGACATCTGCATCTGCTGCGGAAGTCTCCAG
GTTCACACACAGCACCCTCTGTTTGAGGGAGGGATCTGCGCCCCATGTAAGGACAAGTTC
CTGGATGCCCTCTTCCTGTACGACGATGACGGGTACCAATCCTACTGCTCCATCTGCTGC
TCCGGAGAGACGCTGCTCATCTGCGGAAACCCTGATTGCACCCGATGCTACTGCTTCGAG
TGTGTGGATAGCCTGGTCGGCCCCGGGACCTCGGGGAAGGTGCACGCCATGAGCAACTGG
GTGTGCTACCTGTGCCTGCCGTCCTCCCGAAGCGGGCTGCTGCAGCGTCGGAGGAAGTGG
CGCAGCCAGCTCAAGGCCTTCTACGACCGAGAGTCGGAGAATCCCCTTGAGATGTTCGAA
ACCGTGCCTGTGTGGAGGAGACAGCCAGTCCGGGTGCTGTCCCTTTTTGAAGACATCAAG
AAAGAGCTGACGAGTTTGGGCTTTTTGGAAAGTGGTTCTGACCCGGGACAACTGAAGCAT
GTGGTTGATGTCACAGACACAGTGAGGAAGGATGTGGAGGAGTGGGGACCCTTCGATCTT
GTGTACGGCGCCACAGCTCCCCTGGGCCACACCTGTGACCGTCCTCCCAGCTGGTACCTG
TTCCAGTTCCACCGGTTCCTGCAGTACGCACGGCCCAAGCCAGGCAGCCCCAGGCCCTTC
TTCTGGATGTTCGTGGACAATCTGGTGCTGAACAAGGAAGACCTGGACGTCGCATCTCGC
TTCCTGGAGATGGAGCCAGTCACCATCCCAGATGTCCACGGCGGATCCTTGCAGAATGCT
GTCCGCGTGTGGAGCAACATCCCAGCCATAAGGAGCAGCAGGCACTGGGCTCTGGTTTCG
GAAGAAGAATTGTCCCTGCTGGCCCAGAACAAGCAGAGCTCGAAGCTCGCGGCCAAGTGG
CCCACCAAGCTGGTGAAGAACTGCTTTCTCCCCCTAAGAGAATATTTCAAGTATTTTTCA
ACAGAACTCACTTCCTCTTTATAA
Enzyme 51 GenBank Gene ID AF194032 Link Image
Enzyme 51 GeneCard ID DNMT3L Link Image
Enzyme 51 GenAtlas ID DNMT3L Link Image
Enzyme 51 HGNC ID HGNC:2980 Link Image
Enzyme 51 Chromosome Location 2
Enzyme 51 Locus 21q22.3
Enzyme 51 SNPs SNPJam Report Link Image
Enzyme 51 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]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Ooi SK, Qiu C, Bernstein E, Li K, Jia D, Yang Z, Erdjument-Bromage H, Tempst P, Lin SP, Allis CD, Cheng X, Bestor TH: DNMT3L connects unmethylated lysine 4 of histone H3 to de novo methylation of DNA. Nature. 2007 Aug 9;448(7154):714-7. [PubMed Link Image]
  5. Jia D, Jurkowska RZ, Zhang X, Jeltsch A, Cheng X: Structure of Dnmt3a bound to Dnmt3L suggests a model for de novo DNA methylation. Nature. 2007 Sep 13;449(7159):248-51. Epub 2007 Aug 22. [PubMed Link Image]
Enzyme 51 Metabolite References Not Available
Enzyme 52 [top]
Enzyme 52 ID 15863
Enzyme 52 Name Euchromatic histone-lysine N-methyltransferase 2 (Euchromatic histone- lysine N-methyltransferase 2, isoform CRA_c) (HLA-B associated transcript 8)
Enzyme 52 Synonyms Not Available
Enzyme 52 Gene Name EHMT2
Enzyme 52 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 52 Number of Residues 1210
Enzyme 52 Molecular Weight 132372
Enzyme 52 Theoretical pI 5.14
Enzyme 52 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 52 General Function Not Available
Enzyme 52 Specific Function S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N(6)-methyl-L-lysine
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 Q5JQ92 Link Image
Enzyme 52 UniProtKB/Swiss-Prot Entry Name Q5JQ92_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 AL662834 Link Image
Enzyme 52 GeneCard ID Q5JQ92 Link Image
Enzyme 52 GenAtlas ID EHMT2 Link Image
Enzyme 52 HGNC ID HGNC:14129 Link Image
Enzyme 52 Chromosome Location Not Available
Enzyme 52 Locus Not Available
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 15864
Enzyme 53 Name Histone-lysine N-methyltransferase EZH1
Enzyme 53 Synonyms
  1. ENX-2
  2. Enhancer of zeste homolog 1
Enzyme 53 Gene Name EZH1
Enzyme 53 Protein Sequence >Histone-lysine N-methyltransferase EZH1
MEIPNPPTSKCITYWKRKVKSEYMRLRQLKRLQANMGAKALYVANFAKVQEKTQILNEEW
KKLRVQPVQSMKPVSGHPFLKKCTIESIFPGFASQHMLMRSLNTVALVPIMYSWSPLQQN
FMVEDETVLCNIPYMGDEVKEEDETFIEELINNYDGKVHGEEEMIPGSVLISDAVFLELV
DALNQYSDEEEEGHNDTSDGKQDDSKEDLPVTRKRKRHAIEGNKKSSKKQFPNDMIFSAI
ASMFPENGVPDDMKERYRELTEMSDPNALPPQCTPNIDGPNAKSVQREQSLHSFHTLFCR
RCFKYDCFLHPFHATPNVYKRKNKEIKIEPEPCGTDCFLLLEGAKEYAMLHNPRSKCSGR
RRRRHHIVSASCSNASASAVAETKEGDSDRDTGNDWASSSSEANSRCQTPTKQKASPAPP
QLCVVEAPSEPVEWTGAEESLFRVFHGTYFNNFCSIARLLGTKTCKQVFQFAVKESLILK
LPTDELMNPSQKKKRKHRLWAAHCRKIQLKKDNSSTQVYNYQPCDHPDRPCDSTCPCIMT
QNFCEKFCQCNPDCQNRFPGCRCKTQCNTKQCPCYLAVRECDPDLCLTCGASEHWDCKVV
SCKNCSIQRGLKKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKVYD
KYMSSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVVMVNGDHRIGIFAKRAIQAG
EELFFDYRYSQADALKYVGIERETDVL
Enzyme 53 Number of Residues 747
Enzyme 53 Molecular Weight 85270.4
Enzyme 53 Theoretical pI 7.77
Enzyme 53 GO Classification
Function
  • DNA binding
  • binding
  • nucleic acid binding
Process
Component
Enzyme 53 General Function Involved in DNA binding
Enzyme 53 Specific Function Polycomb group (PcG) protein. Catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. Able to mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. Required for embryonic stem cell derivation and self-renewal, suggesting that it is involved in safeguarding embryonic stem cell identity. Compared to EZH1-containing complexes, it is less abundant in embryonic stem cells and plays a less critical role in forming H3K27me3, which is required for embryonic stem cell identity and proper differentiation
Enzyme 53 Pathways Not Available
Enzyme 53 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 53 Pfam Domain Function
Enzyme 53 Signals
  • None
Enzyme 53 Transmembrane Regions
  • None
Enzyme 53 Essentiality Not Available
Enzyme 53 GenBank ID Protein 19923202 Link Image
Enzyme 53 UniProtKB/Swiss-Prot ID Q92800 Link Image
Enzyme 53 UniProtKB/Swiss-Prot Entry Name EZH1_HUMAN Link Image
Enzyme 53 PDB ID Not Available
Enzyme 53 Cellular Location Not Available
Enzyme 53 Gene Sequence >2244 bp
ATGGAAATACCAAATCCCCCTACCTCCAAATGTATCACTTACTGGAAAAGAAAAGTGAAA
TCTGAATACATGCGACTTCGACAACTTAAACGGCTTCAGGCAAATATGGGTGCAAAGGCT
TTGTATGTGGCAAATTTTGCAAAGGTTCAAGAAAAAACCCAGATCCTCAATGAAGAATGG
AAGAAGCTTCGTGTCCAACCTGTTCAGTCAATGAAGCCTGTGAGTGGACACCCTTTTCTC
AAAAAGTGTACCATAGAGAGCATTTTCCCGGGATTTGCAAGCCAACATATGTTAATGAGG
TCACTGAACACAGTTGCATTGGTTCCCATCATGTATTCCTGGTCCCCTCTCCAACAGAAC
TTTATGGTAGAAGATGAGACGGTTTTGTGCAATATTCCCTACATGGGAGATGAAGTGAAA
GAAGAAGATGAGACTTTTATTGAGGAGCTGATCAATAACTATGATGGGAAAGTCCATGGT
GAAGAAGAGATGATCCCTGGATCCGTTCTGATTAGTGATGCTGTTTTTCTGGAGTTGGTC
GATGCCCTGAATCAGTACTCAGATGAGGAGGAGGAAGGGCACAATGACACCTCAGATGGA
AAGCAGGATGACAGCAAAGAAGATCTGCCAGTAACAAGAAAGAGAAAGCGACATGCTATT
GAAGGCAACAAAAAGAGTTCCAAGAAACAGTTCCCAAATGACATGATCTTCAGTGCAATT
GCCTCAATGTTCCCTGAGAATGGTGTCCCAGATGACATGAAGGAGAGGTATCGAGAACTA
ACAGAGATGTCAGACCCCAATGCACTTCCCCCTCAGTGCACACCCAACATCGATGGCCCC
AATGCCAAGTCTGTGCAGCGGGAGCAATCTCTGCACTCCTTCCACACACTTTTTTGCCGG
CGCTGCTTTAAATACGACTGCTTCCTTCACCCTTTTCATGCCACCCCTAATGTATATAAA
CGCAAGAATAAAGAAATCAAGATTGAACCAGAACCATGTGGCACAGACTGCTTCCTTTTG
CTGGAAGGAGCAAAGGAGTATGCCATGCTCCACAACCCCCGCTCCAAGTGCTCTGGTCGT
CGCCGGAGAAGGCACCACATAGTCAGTGCTTCCTGCTCCAATGCCTCAGCCTCTGCTGTG
GCTGAGACTAAAGAAGGAGACAGTGACAGGGACACAGGCAATGACTGGGCCTCCAGTTCT
TCAGAGGCTAACTCTCGCTGTCAGACTCCCACAAAACAGAAGGCTAGTCCAGCCCCACCT
CAACTCTGCGTAGTGGAAGCACCCTCGGAGCCTGTGGAATGGACTGGGGCTGAAGAATCT
CTTTTTCGAGTCTTCCATGGCACCTACTTCAACAACTTCTGTTCAATAGCCAGGCTTCTG
GGGACCAAGACGTGCAAGCAGGTCTTTCAGTTTGCAGTCAAAGAATCACTTATCCTGAAG
CTGCCAACAGATGAGCTCATGAACCCCTCACAGAAGAAGAAAAGAAAGCACAGATTGTGG
GCTGCACACTGCAGGAAGATTCAGCTGAAGAAAGATAACTCTTCCACACAAGTGTACAAC
TACCAACCCTGCGACCACCCAGACCGCCCCTGTGACAGCACCTGCCCCTGCATCATGACT
CAGAATTTCTGTGAGAAGTTCTGCCAGTGCAACCCAGACTGTCAGAATCGTTTCCCTGGC
TGTCGCTGTAAGACCCAGTGCAATACCAAGCAATGTCCTTGCTATCTGGCAGTGCGAGAA
TGTGACCCTGACCTGTGTCTCACCTGTGGGGCCTCAGAGCACTGGGACTGCAAGGTGGTT
TCCTGTAAAAACTGCAGCATCCAGCGTGGACTTAAGAAGCACCTGCTGCTGGCCCCCTCT
GATGTGGCCGGATGGGGCACCTTCATAAAGGAGTCTGTGCAGAAGAACGAATTCATTTCT
GAATACTGTGGTGAGCTCATCTCTCAGGATGAGGCTGATCGACGCGGAAAGGTCTATGAC
AAATACATGTCCAGCTTCCTCTTCAACCTCAATAATGATTTTGTAGTGGATGCTACTCGG
AAAGGAAACAAAATTCGATTTGCAAATCATTCAGTGAATCCCAACTGTTATGCCAAAGTG
GTCATGGTGAATGGAGACCATCGGATTGGGATCTTTGCCAAGAGGGCAATTCAAGCTGGC
GAAGAGCTCTTCTTTGATTACAGGTACAGCCAAGCTGATGCTCTCAAGTACGTGGGGATC
GAGAGGGAGACCGACGTCCTTTAG
Enzyme 53 GenBank Gene ID NM_001991.3 Link Image
Enzyme 53 GeneCard ID EZH1 Link Image
Enzyme 53 GenAtlas ID EZH1 Link Image
Enzyme 53 HGNC ID HGNC:3526 Link Image
Enzyme 53 Chromosome Location 1
Enzyme 53 Locus 17q21.1-q21.3
Enzyme 53 SNPs SNPJam Report Link Image
Enzyme 53 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. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. 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]
  8. Margueron R, Li G, Sarma K, Blais A, Zavadil J, Woodcock CL, Dynlacht BD, Reinberg D: Ezh1 and Ezh2 maintain repressive chromatin through different mechanisms. Mol Cell. 2008 Nov 21;32(4):503-18. [PubMed Link Image]
Enzyme 53 Metabolite References Not Available
Enzyme 54 [top]
Enzyme 54 ID 15865
Enzyme 54 Name Enhancer of zeste homolog 2 (Drosophila) (Enhancer of zeste homolog 2 (Drosophila), isoform CRA_a)
Enzyme 54 Synonyms Not Available
Enzyme 54 Gene Name EZH2
Enzyme 54 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 54 Number of Residues 751
Enzyme 54 Molecular Weight 86019
Enzyme 54 Theoretical pI 7.22
Enzyme 54 GO Classification
Function
  • DNA binding
  • binding
  • nucleic acid binding
Process
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 54 General Function Not Available
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 Q96FI6 Link Image
Enzyme 54 UniProtKB/Swiss-Prot Entry Name Q96FI6_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 BC010858 Link Image
Enzyme 54 GeneCard ID Q96FI6 Link Image
Enzyme 54 GenAtlas ID EZH2 Link Image
Enzyme 54 HGNC ID HGNC:3527 Link Image
Enzyme 54 Chromosome Location Not Available
Enzyme 54 Locus Not Available
Enzyme 54 SNPs SNPJam Report Link Image
Enzyme 54 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 54 Metabolite References Not Available
Enzyme 55 [top]
Enzyme 55 ID 15866
Enzyme 55 Name cDNA FLJ75818, highly similar to Homo sapiens PR/SET domain containing protein 8 (SET8), mRNA
Enzyme 55 Synonyms Not Available
Enzyme 55 Gene Name Not Available
Enzyme 55 Protein Sequence >cDNA FLJ75818, highly similar to Homo sapiens PR/SET domain containing protein 8 (SET8), mRNA
MARGRKMSKPRAVEAAAAAAAVAATAPGPEMVERRGPGRPRTDGENVFTGQSKIYSYMSP
NKCSGMRFPLQEENSVTHHEVKCQGKPLAGIYRKREEKRNAGNAVRSAMKSEEQKIKDAR
KGPLVPFPNQKSEAAEPPKTPPSSCDSTNAAIAKQALKKPIKGKQAPRKKAQGKTQQNRK
LTDFYPVRRSSRKSKAELQSEERKRIDELIESGKEEGMKIDLIDGKGRGVIATKQFSRGD
FVVEYHGDLIEITDAKKREALYAQDPSTGCYMYYFQYLSKTYCVDATRETNRLGRLINHS
KCGNCQTKLHDIDGVPHLILIASRDIAAGEELLYDYGDRSKASIEAHPWLKH
Enzyme 55 Number of Residues 352
Enzyme 55 Molecular Weight 39223
Enzyme 55 Theoretical pI 10.12
Enzyme 55 GO Classification Not Available
Enzyme 55 General Function Not Available
Enzyme 55 Specific Function Not Available
Enzyme 55 Pathways Not Available
Enzyme 55 Reactions Not Available
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 A8K9D0 Link Image
Enzyme 55 UniProtKB/Swiss-Prot Entry Name A8K9D0_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 AK292645 Link Image
Enzyme 55 GeneCard ID A8K9D0 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 Not Available
Enzyme 55 General References Not Available
Enzyme 55 Metabolite References Not Available
Enzyme 56 [top]
Enzyme 56 ID 15867
Enzyme 56 Name Wolf-Hirschhorn syndrome candidate 1 (Wolf-Hirschhorn syndrome candidate 1, isoform CRA_e)
Enzyme 56 Synonyms Not Available
Enzyme 56 Gene Name WHSC1
Enzyme 56 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 56 Number of Residues 1365
Enzyme 56 Molecular Weight 152259
Enzyme 56 Theoretical pI 8.81
Enzyme 56 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 56 General Function Not Available
Enzyme 56 Specific Function Not Available
Enzyme 56 Pathways Not Available
Enzyme 56 Reactions Not Available
Enzyme 56 Pfam Domain Function
Enzyme 56 Signals
  • None
Enzyme 56 Transmembrane Regions
  • None
Enzyme 56 Essentiality Not Available
Enzyme 56 GenBank ID Protein Not Available
Enzyme 56 UniProtKB/Swiss-Prot ID A2A2T3 Link Image
Enzyme 56 UniProtKB/Swiss-Prot Entry Name A2A2T3_HUMAN Link Image
Enzyme 56 PDB ID Not Available
Enzyme 56 Cellular Location Not Available
Enzyme 56 Gene Sequence Not Available
Enzyme 56 GenBank Gene ID AL132868 Link Image
Enzyme 56 GeneCard ID A2A2T3 Link Image
Enzyme 56 GenAtlas ID Not Available
Enzyme 56 HGNC ID Not Available
Enzyme 56 Chromosome Location Not Available
Enzyme 56 Locus Not Available
Enzyme 56 SNPs SNPJam Report Link Image
Enzyme 56 General References Not Available
Enzyme 56 Metabolite References Not Available
Enzyme 57 [top]
Enzyme 57 ID 15868
Enzyme 57 Name EHMT1 protein
Enzyme 57 Synonyms Not Available
Enzyme 57 Gene Name EHMT1
Enzyme 57 Protein Sequence >EHMT1 protein
MAAADAEAVPARGEPQQDCCVKTELLGEETPMAADEGSAEKQAGEAHMAADGETNGSCEN
SDASSHANAAKHTQDSARVNPQDGTNTLTRIAENGVSERDSEAAKQNHVTADDFVQTSVI
GSNGYILNKPALQAQPLRTTSTLASSLPGHAAKTLPGGAGKGRTPSAFPQTPAAPPATLG
EGSADTEDRKLPAPGADVKVHRARKTMPKSVVGLHAASKDPREVREARDHKEPKEEINKN
ISDFGRQQLLPPFPSLHQSLPQNQCYMATTKSQTACLPFVLAAAVSRKKKRRMGTYSLVP
KKKTKVLKQRTVIEMFKSITHSTVGSKGEKDLGASSLHVNGESLEMDSDEDDSEELEEDD
GHGAEQAAAFPTEDSRTSKESMSEADRAQKMDGESEEEQESVDTGEEEEGGDESDLSSES
SIKKKFLKRKGKTDSPWIKPARKRRRRSRKKPSGALGSESYKSSAGSAEQTAPGDSTGYM
EVSLDSLDLRVKGILSSQAEGLANGPDVLETDGLQEVPLCSCRMETPKSREITTLANNQC
MATESVDHELGRCTDSVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCGYFCTAGNF
MECQPESSISHRFHKDCASRVNNASYCPHCGEESSKAKEVTIAKADTTSTVTPVPGQEKG
SALEGRADTTTGSAAGPPLSEDDKLQGAASHVPEGFDPTGPAGLGRPTPGLSQGPGKETL
ESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQNKRSPLHAA
AEAGHVDICHMLVQFCRLGSPRSRGCLW
Enzyme 57 Number of Residues 808
Enzyme 57 Molecular Weight 86703.8
Enzyme 57 Theoretical pI 6.18
Enzyme 57 GO Classification Not Available
Enzyme 57 General Function Not Available
Enzyme 57 Specific Function Not Available
Enzyme 57 Pathways Not Available
Enzyme 57 Reactions Not Available
Enzyme 57 Pfam Domain Function Not Available
Enzyme 57 Signals
  • None
Enzyme 57 Transmembrane Regions
  • None
Enzyme 57 Essentiality Not Available
Enzyme 57 GenBank ID Protein 28704074 Link Image
Enzyme 57 UniProtKB/Swiss-Prot ID Q86X08 Link Image
Enzyme 57 UniProtKB/Swiss-Prot Entry Name Q86X08_HUMAN Link Image
Enzyme 57 PDB ID Not Available
Enzyme 57 Cellular Location Not Available
Enzyme 57 Gene Sequence >2427 bp
ATGGCCGCCGCCGATGCCGAGGCAGTTCCGGCGAGGGGGGAGCCTCAGCAGGATTGCTGT
GTGAAAACCGAGCTGCTGGGAGAAGAGACACCTATGGCTGCCGATGAAGGCTCAGCAGAG
AAACAGGCAGGAGAGGCCCACATGGCTGCGGACGGTGAGACCAATGGGTCTTGTGAAAAC
AGCGATGCCAGCAGTCATGCAAATGCTGCAAAGCACACTCAGGACAGCGCAAGGGTCAAC
CCCCAGGATGGCACCAACACACTAACTCGGATAGCGGAAAATGGGGTTTCAGAAAGAGAC
TCAGAAGCGGCGAAGCAAAACCACGTCACTGCCGACGACTTTGTGCAGACTTCTGTCATC
GGCAGCAACGGATACATCTTAAATAAGCCGGCCCTACAGGCACAGCCCTTGAGGACTACC
AGCACTCTGGCCTCTTCGCTGCCTGGCCATGCTGCAAAAACCCTTCCTGGAGGGGCTGGC
AAAGGCAGGACTCCAAGCGCTTTTCCCCAGACGCCAGCCGCCCCACCAGCCACCCTTGGG
GAGGGGAGTGCTGACACAGAGGACAGGAAGCTCCCGGCCCCTGGCGCCGACGTCAAGGTC
CACAGGGCACGCAAGACCATGCCGAAGTCCGTCGTGGGCCTGCATGCAGCCAGTAAAGAT
CCCAGAGAAGTTCGAGAAGCTAGAGATCATAAGGAACCAAAAGAGGAGATCAACAAAAAC
ATTTCTGACTTTGGACGACAGCAGCTTTTACCCCCCTTCCCATCCCTTCATCAGTCGCTA
CCTCAGAACCAGTGCTACATGGCCACCACAAAATCACAGACAGCTTGCTTGCCTTTTGTT
TTAGCAGCTGCAGTATCTCGGAAGAAAAAACGAAGAATGGGAACCTATAGCCTGGTTCCT
AAGAAAAAGACCAAAGTATTAAAACAGAGGACGGTGATTGAGATGTTTAAGAGCATAACT
CATTCCACTGTGGGTTCCAAGGGGGAGAAGGACCTGGGCGCCAGCAGCCTGCACGTGAAT
GGGGAGAGCCTGGAGATGGACTCGGATGAGGACGACTCAGAGGAGCTCGAGGAGGACGAC
GGCCATGGTGCAGAGCAGGCGGCCGCGTTCCCCACAGAGGACAGCAGGACTTCCAAGGAG
AGCATGTCGGAGGCTGATCGCGCCCAGAAGATGGACGGGGAGTCCGAGGAGGAGCAGGAG
TCCGTGGACACCGGGGAGGAGGAGGAAGGCGGTGACGAGTCTGACCTGAGTTCGGAATCC
AGCATTAAGAAGAAATTTCTCAAGAGGAAAGGAAAGACCGACAGTCCCTGGATCAAGCCA
GCCAGGAAAAGGAGGCGGAGAAGTAGAAAGAAGCCCAGCGGTGCCCTCGGTTCTGAGTCG
TATAAGTCATCTGCAGGAAGCGCTGAGCAGACGGCACCAGGAGACAGCACAGGGTACATG
GAAGTTTCTCTGGACTCCCTGGATCTCCGAGTCAAAGGAATTCTGTCTTCACAAGCAGAA
GGGTTGGCCAACGGTCCAGATGTGCTGGAGACAGACGGCCTCCAGGAAGTGCCTCTCTGC
AGCTGCCGGATGGAAACACCGAAGAGTCGAGAGATCACCACACTGGCCAACAACCAGTGC
ATGGCTACAGAGAGCGTGGACCATGAATTGGGCCGGTGCACAGACAGCGTGGTCAAGTAT
GAGCTGATGCGCCCCTCCAACAAGGCCCCGCTCCTCGTGCTGTGTGAAGACCACCGGGGC
CGCATGGTGAAGCACCAGTGCTGTCCTGGCTGTGGCTACTTCTGCACAGCGGGTAATTTT
ATGGAGTGTCAGCCCGAGAGCAGCATCTCTCACCGTTTCCACAAAGACTGTGCCTCTCGA
GTCAATAACGCCAGCTATTGTCCCCACTGTGGGGAGGAGAGCTCCAAGGCCAAAGAGGTG
ACGATAGCTAAAGCAGACACCACCTCGACCGTGACACCAGTCCCCGGGCAGGAGAAGGGC
TCGGCCCTGGAGGGCAGGGCCGACACCACAACGGGCAGTGCTGCCGGGCCACCACTCTCG
GAGGACGACAAGCTGCAGGGTGCAGCCTCCCACGTGCCCGAGGGCTTTGATCCAACGGGA
CCTGCTGGGCTTGGGAGGCCAACTCCCGGCCTTTCCCAGGGACCAGGGAAGGAAACCTTG
GAGAGCGCTCTCATCGCCCTCGACTCGGAAAAACCCAAGAAGCTTCGCTTCCACCCAAAG
CAGCTGTACTTCTCCGCCAGGCAAGGGGAGCTTCAGAAGGTGCTCCTCATGCTGGTGGAC
GGAATTGACCCCAACTTCAAAATGGAGCACCAGAATAAGCGCTCTCCACTGCACGCCGCG
GCAGAGGCTGGACACGTGGACATCTGCCACATGCTGGTTCAGTTCTGCAGGCTGGGAAGC
CCAAGGTCGAGGGGCTGCCTTTGGTGA
Enzyme 57 GenBank Gene ID BC047504 Link Image
Enzyme 57 GeneCard ID EHMT1 Link Image
Enzyme 57 GenAtlas ID EHMT1 Link Image
Enzyme 57 HGNC ID HGNC:24650 Link Image
Enzyme 57 Chromosome Location 9
Enzyme 57 Locus 9q34.3
Enzyme 57 SNPs SNPJam Report Link Image
Enzyme 57 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 57 Metabolite References Not Available
Enzyme 58 [top]
Enzyme 58 ID 15869
Enzyme 58 Name cDNA FLJ78356, highly similar to Homo sapiens PIMT isozyme I
Enzyme 58 Synonyms Not Available
Enzyme 58 Gene Name Not Available
Enzyme 58 Protein Sequence >cDNA FLJ78356, highly similar to Homo sapiens PIMT isozyme I
MAWKSGGASHSELIHNLRKNGIIKTDKVFEVMLATDRSHYAKCNPYMDSPQSIGFQATIS
APHMHAYALELLFDQLHEGAKALDVGSGSGILTACFARMVGCTGKVIGIDHIKELVDDSV
NNVRKDDPTLLSSGRVQLVVGDGRMGYAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLI
LPVGPAGGNQMLEQYDKLQDGSIKMKPLMGVIYVPLTDKEKQWSRWK
Enzyme 58 Number of Residues 227
Enzyme 58 Molecular Weight 24637
Enzyme 58 Theoretical pI 7.25
Enzyme 58 GO Classification Not Available
Enzyme 58 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 58 Specific Function Not Available
Enzyme 58 Pathways Not Available
Enzyme 58 Reactions Not Available
Enzyme 58 Pfam Domain Function Not Available
Enzyme 58 Signals
  • None
Enzyme 58 Transmembrane Regions
  • None
Enzyme 58 Essentiality Not Available
Enzyme 58 GenBank ID Protein Not Available
Enzyme 58 UniProtKB/Swiss-Prot ID A8K109 Link Image
Enzyme 58 UniProtKB/Swiss-Prot Entry Name A8K109_HUMAN Link Image
Enzyme 58 PDB ID 1KR5 Link Image
Enzyme 58 PDB File Show
Enzyme 58 3D Structure
Enzyme 58 Cellular Location Not Available
Enzyme 58 Gene Sequence Not Available
Enzyme 58 GenBank Gene ID AK289724 Link Image
Enzyme 58 GeneCard ID A8K109 Link Image
Enzyme 58 GenAtlas ID Not Available
Enzyme 58 HGNC ID Not Available
Enzyme 58 Chromosome Location Not Available
Enzyme 58 Locus Not Available
Enzyme 58 SNPs Not Available
Enzyme 58 General References Not Available
Enzyme 58 Metabolite References Not Available
Enzyme 59 [top]
Enzyme 59 ID 15870
Enzyme 59 Name Protein arginine methyltransferase 5, isoform CRA_d
Enzyme 59 Synonyms
  1. SubName: Putative uncharacterized protein PRMT5
  2. SubName: cDNA FLJ90770 fis, clone THYRO1000866, highly similar to Protein arginine N-methyltransferase 5 (EC 2.1.1.-)
Enzyme 59 Gene Name PRMT5
Enzyme 59 Protein Sequence >Protein arginine methyltransferase 5, isoform CRA_d
MRGPNSGTEKGRLVIPEKQGFDFLCMPVFHPRFKREFIQEPAKNRPGPQTRSDLLLSGRD
WNTLIVGKLSPWIRPDSKVEKIRRNSEAAMLQELNFGAYLGLPAFLLPLNQEDNTNLARV
LTNHIHTGHHSSMFWMRVPLVAPEDLRDDIIENAPTTHTEEYSGEEKTWMWWHNFRTLCD
YSKRIAVALEIGADLPSNHVIDRWLGEPIKAAILPTSIFLTNKKGFPVLSKMHQRLIFRL
LKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELFAKGYEDYLQSPLQPLMD
NLESQTYEVFEKDPIKYSQYQQAIYKCLLDRVPEEEKDTNVQVLMVLGAGRGPLVNASLR
AAKQADRRIKLYAVEKNPNAVVTLENWQFEEWGSQVTVVSSDMREWVAPEKADIIVSELL
GSFADNELSPECLDGAQHFLKDDGVSIPGEYTSFLAPISSSKLYNEVRACREKDRDPEAQ
FEMPYVVRLHNFHQLSAPQPCFTFSHPNRDPMIDNNRYCTLEFPVEVNTVLHGFAGYFET
VLYQDITLSIRPETHSPGMFSWFPILFPIKQPITVREGQTICVRFWRCSNSKKVWYEWAV
TAPVCSAIHNPTGRSYTIGL
Enzyme 59 Number of Residues 620
Enzyme 59 Molecular Weight 71319.8
Enzyme 59 Theoretical pI 6.42
Enzyme 59 GO Classification
Function
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 59 General Function Involved in methyltransferase activity
Enzyme 59 Specific Function Not Available
Enzyme 59 Pathways Not Available
Enzyme 59 Reactions Not Available
Enzyme 59 Pfam Domain Function
Enzyme 59 Signals
  • None
Enzyme 59 Transmembrane Regions
  • None
Enzyme 59 Essentiality Not Available
Enzyme 59 GenBank ID Protein 193786772 Link Image
Enzyme 59 UniProtKB/Swiss-Prot ID A8MZ91 Link Image
Enzyme 59 UniProtKB/Swiss-Prot Entry Name A8MZ91_HUMAN Link Image
Enzyme 59 PDB ID Not Available
Enzyme 59 Cellular Location Not Available
Enzyme 59 Gene Sequence >1863 bp
ATGCGGGGTCCGAACTCGGGGACGGAGAAGGGCAGACTAGTCATCCCGGAGAAGCAGGGG
TTTGATTTCCTCTGCATGCCTGTCTTCCATCCGCGTTTCAAGAGGGAGTTCATTCAGGAA
CCTGCTAAGAATCGGCCCGGTCCCCAGACACGATCAGACCTACTGCTGTCAGGAAGGGAC
TGGAATACGCTAATTGTGGGAAAGCTTTCTCCATGGATTCGTCCAGACTCAAAAGTGGAG
AAGATTCGCAGGAACTCCGAGGCGGCCATGTTACAGGAGCTGAATTTTGGTGCATATTTG
GGTCTTCCAGCTTTCCTGCTGCCCCTTAATCAGGAAGATAACACCAACCTGGCCAGAGTT
TTGACCAACCACATCCACACTGGCCATCACTCTTCCATGTTCTGGATGCGGGTACCCTTG
GTGGCACCAGAGGACCTGAGAGATGATATAATTGAGAATGCACCAACTACACACACAGAG
GAGTACAGTGGGGAGGAGAAAACGTGGATGTGGTGGCACAACTTCCGGACTTTGTGTGAC
TATAGTAAGAGGATTGCAGTGGCTCTTGAAATTGGGGCTGACCTCCCATCTAATCATGTC
ATTGATCGCTGGCTTGGGGAGCCCATCAAAGCAGCCATTCTCCCCACTAGCATTTTCCTG
ACCAATAAGAAGGGATTTCCTGTTCTTTCTAAGATGCACCAGAGGCTCATCTTCCGGCTC
CTCAAGTTGGAGGTGCAGTTCATCATCACAGGCACCAACCACCACTCAGAGAAGGAGTTC
TGCTCCTACCTCCAATACCTGGAATACTTAAGCCAGAACCGTCCTCCACCTAATGCCTAT
GAACTCTTTGCCAAGGGCTATGAAGACTATCTGCAGTCCCCGCTTCAGCCACTGATGGAC
AATCTGGAATCTCAGACATATGAAGTGTTTGAAAAGGACCCCATCAAATACTCTCAGTAC
CAGCAGGCCATCTATAAATGTCTGCTAGACCGAGTACCAGAAGAGGAGAAGGATACCAAT
GTCCAGGTACTGATGGTGCTGGGAGCAGGACGGGGACCCCTGGTGAACGCTTCCCTGCGG
GCAGCCAAGCAGGCCGACCGGCGGATAAAGCTGTATGCTGTGGAGAAAAACCCAAATGCC
GTGGTGACGCTAGAGAACTGGCAGTTTGAAGAATGGGGAAGCCAAGTGACCGTAGTCTCA
TCAGACATGAGGGAATGGGTGGCTCCAGAGAAAGCAGACATCATTGTCAGTGAGCTTCTG
GGCTCATTTGCTGACAATGAATTGTCGCCTGAGTGCCTGGATGGAGCCCAGCACTTCCTA
AAAGATGATGGTGTGAGCATCCCCGGGGAGTACACTTCCTTTCTGGCTCCCATCTCTTCC
TCCAAGCTGTACAATGAGGTCCGAGCCTGTAGGGAGAAGGACCGTGACCCTGAGGCCCAG
TTTGAGATGCCTTATGTGGTACGGCTGCACAACTTCCACCAGCTCTCTGCACCCCAGCCC
TGTTTCACCTTCAGCCATCCCAACAGAGATCCTATGATTGACAACAACCGCTATTGCACC
TTGGAATTTCCTGTGGAGGTGAACACAGTACTACATGGCTTTGCCGGCTACTTTGAGACT
GTGCTTTATCAGGACATCACTCTGAGTATCCGTCCAGAGACTCACTCTCCTGGGATGTTC
TCATGGTTTCCCATCCTCTTCCCTATTAAGCAGCCCATAACGGTACGTGAAGGCCAAACC
ATCTGTGTGCGTTTCTGGCGATGCAGCAATTCCAAGAAGGTGTGGTATGAGTGGGCTGTG
ACAGCACCAGTCTGTTCTGCTATTCATAACCCCACAGGCCGCTCATATACCATTGGCCTC
TAG
Enzyme 59 GenBank Gene ID AK075251 Link Image
Enzyme 59 GeneCard ID PRMT5 Link Image
Enzyme 59 GenAtlas ID PRMT5 Link Image
Enzyme 59 HGNC ID HGNC:10894 Link Image
Enzyme 59 Chromosome Location 1
Enzyme 59 Locus 14q11.2
Enzyme 59 SNPs SNPJam Report Link Image
Enzyme 59 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]
  2. Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed Link Image]
Enzyme 59 Metabolite References Not Available
Enzyme 60 [top]
Enzyme 60 ID 15871
Enzyme 60 Name Uncharacterized protein CARM1 (Coactivator-associated arginine methyltransferase 1, isoform CRA_b)
Enzyme 60 Synonyms Not Available
Enzyme 60 Gene Name CARM1
Enzyme 60 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 60 Number of Residues 608
Enzyme 60 Molecular Weight 65854
Enzyme 60 Theoretical pI 6.73
Enzyme 60 GO Classification Not Available
Enzyme 60 General Function Not Available
Enzyme 60 Specific Function Not Available
Enzyme 60 Pathways Not Available
Enzyme 60 Reactions Not Available
Enzyme 60 Pfam Domain Function
Enzyme 60 Signals
  • None
Enzyme 60 Transmembrane Regions
  • None
Enzyme 60 Essentiality Not Available
Enzyme 60 GenBank ID Protein Not Available
Enzyme 60 UniProtKB/Swiss-Prot ID A6NN38 Link Image
Enzyme 60 UniProtKB/Swiss-Prot Entry Name A6NN38_HUMAN Link Image
Enzyme 60 PDB ID Not Available
Enzyme 60 Cellular Location Not Available
Enzyme 60 Gene Sequence Not Available
Enzyme 60 GenBank Gene ID AC011442 Link Image
Enzyme 60 GeneCard ID A6NN38 Link Image
Enzyme 60 GenAtlas ID CARM1 Link Image
Enzyme 60 HGNC ID HGNC:23393 Link Image
Enzyme 60 Chromosome Location 19
Enzyme 60 Locus 19p13.2
Enzyme 60 SNPs SNPJam Report Link Image
Enzyme 60 General References Not Available
Enzyme 60 Metabolite References Not Available
Enzyme 61 [top]
Enzyme 61 ID 16701
Enzyme 61 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 61 Synonyms Not Available
Enzyme 61 Gene Name SUV39H1
Enzyme 61 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 61 Number of Residues 412
Enzyme 61 Molecular Weight 47908
Enzyme 61 Theoretical pI 8.07
Enzyme 61 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 61 General Function Not Available
Enzyme 61 Specific Function S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N(6)-methyl-L-lysine
Enzyme 61 Pathways Not Available
Enzyme 61 Reactions Not Available
Enzyme 61 Pfam Domain Function
Enzyme 61 Signals
  • None
Enzyme 61 Transmembrane Regions
  • None
Enzyme 61 Essentiality Not Available
Enzyme 61 GenBank ID Protein Not Available
Enzyme 61 UniProtKB/Swiss-Prot ID B2R6E8 Link Image
Enzyme 61 UniProtKB/Swiss-Prot Entry Name B2R6E8_HUMAN Link Image
Enzyme 61 PDB ID Not Available
Enzyme 61 Cellular Location Not Available
Enzyme 61 Gene Sequence Not Available
Enzyme 61 GenBank Gene ID AK312547 Link Image
Enzyme 61 GeneCard ID B2R6E8 Link Image
Enzyme 61 GenAtlas ID Not Available
Enzyme 61 HGNC ID Not Available
Enzyme 61 Chromosome Location Not Available
Enzyme 61 Locus Not Available
Enzyme 61 SNPs SNPJam Report Link Image
Enzyme 61 General References Not Available
Enzyme 61 Metabolite References Not Available
Enzyme 62 [top]
Enzyme 62 ID 16702
Enzyme 62 Name RNA (Guanine-7-) methyltransferase
Enzyme 62 Synonyms
  1. SubName: RNA (Guanine-7-) methyltransferase, isoform CRA_a
Enzyme 62 Gene Name RNMT
Enzyme 62 Protein Sequence >RNA (Guanine-7-) methyltransferase
MANSAKAEEYEKMSLEQAKASVNSETESSFNINENTTASGTGLSEKTSVCRQVDIARKRK
EFEDDLVKESSSCGKDTPSKKRKLDPEIVPEEKDCGDAEGNSKKRKRETEDVPKDKSSTG
DGTQNKRKIALEDVPEKQKNLEEGHSSTVAAHYNELQEVGLEKRSQSRIFYLRNFNNWMK
SVLIGEFLEKVRQKKKRDITVLDLGCGKGGDLLKWKKGRINKLVCTDIADVSVKQCQQRY
EDMKNRRDSEYIFSAEFITADSSKELLIDKFRDPQMCFDICSCQFVCHYSFESYEQADMM
LRNACERLSPGGYFIGTTPNSFELIRRLEASETESFGNEIYTVKFQKKGDYPLFGCKYDF
NLEGVVDVPEFLVYFPLLNEMAKKYNMKLVYKKTFLEFYEEKIKNNENKMLLKRMQALEP
YPANESSKLVSEKVDDYEHAAKYMKNSQVRLPLGTLSKSEWEATSIYLVFAFEKQQ
Enzyme 62 Number of Residues 476
Enzyme 62 Molecular Weight 54845
Enzyme 62 Theoretical pI 6.54
Enzyme 62 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 62 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 62 Specific Function Not Available
Enzyme 62 Pathways Not Available
Enzyme 62 Reactions Not Available
Enzyme 62 Pfam Domain Function
Enzyme 62 Signals
  • None
Enzyme 62 Transmembrane Regions
  • None
Enzyme 62 Essentiality Not Available
Enzyme 62 GenBank ID Protein Not Available
Enzyme 62 UniProtKB/Swiss-Prot ID B0YJ90 Link Image
Enzyme 62 UniProtKB/Swiss-Prot Entry Name B0YJ90_HUMAN Link Image
Enzyme 62 PDB ID Not Available
Enzyme 62 Cellular Location Not Available
Enzyme 62 Gene Sequence Not Available
Enzyme 62 GenBank Gene ID EF445026 Link Image
Enzyme 62 GeneCard ID B0YJ90 Link Image
Enzyme 62 GenAtlas ID Not Available
Enzyme 62 HGNC ID Not Available
Enzyme 62 Chromosome Location 18
Enzyme 62 Locus 18p11.22-p11.23
Enzyme 62 SNPs SNPJam Report Link Image
Enzyme 62 General References Not Available
Enzyme 62 Metabolite References Not Available
Enzyme 63 [top]
Enzyme 63 ID 16703
Enzyme 63 Name DPH5 homolog (S. cerevisiae), isoform CRA_e
Enzyme 63 Synonyms
  1. SubName: cDNA FLJ43496 fis, clone PEBLM2001465, highly similar to Probable diphthine synthase (EC 2.1.1.98)
Enzyme 63 Gene Name DPH5
Enzyme 63 Protein Sequence >DPH5 homolog (S. cerevisiae), isoform CRA_e
MNAVGCCGLQLYKFGETVSIVFWTDTWRPESFFDKVKKNRQNGMHTLCLLDIKVKEQSLE
NLIKGRKIYEPPRYMSVNQAAQQLLEIVQNQRIRGEEPAVTEETLCVGLARVGADDQKIA
AGTLRQMCTVDLGEPLHSLIITGGSIHPMEMEMLSLFSIPENSSESQSINGL
Enzyme 63 Number of Residues 172
Enzyme 63 Molecular Weight 19244.0
Enzyme 63 Theoretical pI 5.29
Enzyme 63 GO Classification
Function
  • S-adenosylmethionine-dependent methyltransferase activity
  • catalytic activity
  • diphthine synthase activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • peptidyl-amino acid modification
  • peptidyl-diphthamide biosynthetic process from peptidyl-histidine
  • peptidyl-diphthamide metabolic process
  • peptidyl-histidine modification
  • protein modification process
Component
Enzyme 63 General Function Involved in methyltransferase activity
Enzyme 63 Specific Function Not Available
Enzyme 63 Pathways Not Available
Enzyme 63 Reactions Not Available
Enzyme 63 Pfam Domain Function Not Available
Enzyme 63 Signals
  • None
Enzyme 63 Transmembrane Regions
  • None
Enzyme 63 Essentiality Not Available
Enzyme 63 GenBank ID Protein 193785050 Link Image
Enzyme 63 UniProtKB/Swiss-Prot ID B3KWP1 Link Image
Enzyme 63 UniProtKB/Swiss-Prot Entry Name B3KWP1_HUMAN Link Image
Enzyme 63 PDB ID Not Available
Enzyme 63 Cellular Location Not Available
Enzyme 63 Gene Sequence >519 bp
ATGAATGCTGTAGGCTGCTGTGGTTTACAGTTATATAAGTTTGGAGAGACAGTTTCTATT
GTTTTTTGGACAGACACTTGGAGACCAGAAAGCTTCTTTGACAAAGTGAAGAAGAACAGA
CAAAATGGCATGCACACATTATGTTTACTAGACATCAAAGTAAAGGAGCAGTCTTTGGAA
AATCTAATCAAGGGAAGGAAGATCTATGAACCTCCACGGTATATGAGTGTAAACCAAGCA
GCCCAGCAGCTTCTGGAGATTGTTCAAAATCAAAGAATACGAGGAGAAGAACCAGCAGTT
ACCGAGGAGACACTTTGTGTTGGCTTAGCCAGGGTTGGAGCCGACGACCAGAAAATTGCA
GCAGGCACTTTAAGGCAAATGTGCACTGTGGACTTGGGAGAACCATTGCATTCCTTGATC
ATCACAGGAGGCAGCATACATCCAATGGAGATGGAGATGCTAAGTCTGTTTTCCATACCA
GAAAATAGCTCAGAATCTCAAAGCATCAATGGACTTTGA
Enzyme 63 GenBank Gene ID AK125485 Link Image
Enzyme 63 GeneCard ID DPH5 Link Image
Enzyme 63 GenAtlas ID DPH5 Link Image
Enzyme 63 HGNC ID HGNC:24270 Link Image
Enzyme 63 Chromosome Location 1
Enzyme 63 Locus 1p21.2
Enzyme 63 SNPs SNPJam Report Link Image
Enzyme 63 General References
  1. Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed Link Image]
Enzyme 63 Metabolite References Not Available