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Human Metabolome Database Version 2.5

 

Showing metabocard for S-Adenosylmethionine (HMDB01185)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:37
Accession Number HMDB01185
Secondary Accession Numbers Not Available
Common Name S-Adenosylmethionine
Description Physiologic methyl radical donor involved in enzymatic transmethylation reactions and present in all living organisms. It possesses anti-inflammatory activity and has been used in treatment of chronic liver disease. (From Merck, 11th ed)
Synonyms
  1. (3S)-5'-[(3-amino-3-carboxypropyl)methylsulfonio]-5'-deoxyadenosine
  2. 2-S-adenosyl-L-methionine
  3. 5'-Deoxyadenosine-5'-L-methionine disulfate ditosylate
  4. AdoMet
  5. S-(5'-Adenosyl)-L-methionine
  6. S-(5'-deoxyadenosin-5'-yl)-L-methionine
  7. S-Adenosyl-L-Methionine Disulfate Tosylate
  8. S-Adenosyl-L-methionine
  9. S-Adenosylmethionine
  10. S-adenosyl methionine
  11. S-adenosyl-methionine
  12. adenosylmethionine
  13. Active methionine
  14. Ademetionine
  15. Donamet
  16. L-S-Adenosylmethionine
Chemical IUPAC Name (3-amino-3-carboxy-propyl)-[[5-(6-aminopurin-9-yl)-3,4-dihydroxy-oxolan-2-yl]methyl]-methyl-sulfanium
Chemical Formula C15H23N6O5S
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Nucleoside Analogues
Sub Class
  • Methylated nucleosides
Family
  • Mammalian Metabolite
Species
  • cation
  • secondary alcohol
  • 1,2-diol
  • primary amine
  • primary aliphatic amine (alkylamine)
  • primary aromatic amine
  • carboxylic acid
  • aromatic compound
  • heterocyclic compound
  • alpha-aminoacid
Biofunction
  • Component of Aminosugars metabolism
  • 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 399.445
Monoisotopic Molecular Weight 399.145050
Isomeric SMILES C[S+](CC[C@@H](N)C(O)=O)C[C@H]1O[C@H]([C@H](O)[C@@H]1O)N1C=NC2=C(N)N=CN=C12
Canonical SMILES C[S+](CCC(N)C(O)=O)CC1OC(C(O)C1O)N1C=NC2=C(N)N=CN=C12
KEGG Compound ID C00019 Link Image
BioCyc ID S-ADENOSYLMETHIONINE Link Image
BiGG ID 33530 Link Image
Wikipedia Link S-Adenosylmethionine Link Image
NuGOwiki Link HMDB01185 Link Image
Metagene Link HMDB01185 Link Image
METLIN ID 6064 Link Image
PubChem Compound 1079 Link Image
PubChem Substance 3155 Link Image
ChEBI ID 15414 Link Image
CAS Registry Number 29908-03-0
InChI Identifier InChI=1/C15H22N6O5S/c1-27(3-2-7(16)15(24)25)4-8-10(22)11(23)14(26-8)21-6-20-9-12(17)18-5-19-13(9)21/h5-8,10-11,14,22-23H,2-4,16H2,1H3,(H2-,17,18,19,24,25)/p+1/t7-,8-,10-,11-,14-,27?/m1/s1
Synthesis Reference Lin, Jian-Ping; Tian, Jun; You, Jian-Feng; Jin, Zhi-Hua; Xu, Zhi-Nan; Cen, Pei-Lin. An effective strategy for the co-production of S-adenosyl-L-methionine and glutathione by fed-batch fermentation. Biochemical Engineering Journal (2004), 21(1), 19-25.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 0.111 mg/mL at 25 oC [MEYLAN,WM et al. (1996)]; 1.19 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.27 [MEYLAN,WM & HOWARD,PH (1995)]; -1.99 [Predicted by ALOGPS] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID 1CMC Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • endoplasmic reticulum
  • mitochondria
  • nucleus
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
Epidermis
Eye Lens
Fibroblasts
Gonads
Intestine
Kidney
Muscle
Myelin
Placenta
Skeletal Muscle
Testes
Concentrations (Normal)
Biofluid Blood
Value 2.2 +/- 0.38 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid CSF
Value 0.25 (0.14 - 0.38) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Struys EA, Jansen EE, de Meer K, Jakobs C: Determination of S-adenosylmethionine and S-adenosylhomocysteine in plasma and cerebrospinal fluid by stable-isotope dilution tandem mass spectrometry. Clin Chem. 2000 Oct;46(10):1650-6. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 0.11 (0.087-0.17) 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 Urine
Value 28.4 (25.3-31.6) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Diabetes mellitus type 2
Comments With ketoacidosis
References
  • Hoppel CL, Genuth SM: Urinary excretion of acetylcarnitine during human diabetic and fasting ketosis. Am J Physiol. 1982 Aug;243(2):E168-72. [PubMed Link Image]
Associated Disorders
Condition References
Diabetes mellitus type 2
  • Hoppel CL, Genuth SM: Urinary excretion of acetylcarnitine during human diabetic and fasting ketosis. Am J Physiol. 1982 Aug;243(2):E168-72. [PubMed Link Image]
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]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Betaine Metabolism SMP00123 Link Image map00260 Link Image
Carnitine Synthesis SMP00465 Link Image
Catecholamine Biosynthesis SMP00012 Link Image map00350 Link Image
Glycine and Serine Metabolism SMP00004 Link Image map00260 Link Image
Methionine Metabolism SMP00033 Link Image map00270 Link Image
Spermidine and Spermine Biosynthesis SMP00445 Link Image
General References
  1. Chamberlin ME, Ubagai T, Mudd SH, Wilson WG, Leonard JV, Chou JY: Demyelination of the brain is associated with methionine adenosyltransferase I/III deficiency. J Clin Invest. 1996 Aug 15;98(4):1021-7. [PubMed Link Image]
  2. Koeberl DD, Young SP, Gregersen NS, Vockley J, Smith WE, Benjamin DK Jr, An Y, Weavil SD, Chaing SH, Bali D, McDonald MT, Kishnani PS, Chen YT, Millington DS: Rare disorders of metabolism with elevated butyryl- and isobutyryl-carnitine detected by tandem mass spectrometry newborn screening. Pediatr Res. 2003 Aug;54(2):219-23. Epub 2003 May 7. [PubMed Link Image]
  3. Scalabrino G, Pigatto P, Ferioli ME, Modena D, Puerari M, Caru A: Levels of activity of the polyamine biosynthetic decarboxylases as indicators of degree of malignancy of human cutaneous epitheliomas. J Invest Dermatol. 1980 Mar;74(3):122-4. [PubMed Link Image]
  4. 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]
  5. Kaneoka H, Uesugi N, Moriguchi A, Hirose S, Takayanagi M, Yamaguchi S, Shigematsu Y, Yasuno T, Sasatomi Y, Saito T: Carnitine palmitoyltransferase II deficiency due to a novel gene variant in a patient with rhabdomyolysis and ARF. Am J Kidney Dis. 2005 Mar;45(3):596-602. [PubMed Link Image]
  6. Rosen RT, Hiserodt RD, Fukuda EK, Ruiz RJ, Zhou Z, Lech J, Rosen SL, Hartman TG: The determination of metabolites of garlic preparations in breath and human plasma. Biofactors. 2000;13(1-4):241-9. [PubMed Link Image]
  7. McFadden PN, Horwitz J, Clarke S: Protein carboxyl methyltransferase from cow eye lens. Biochem Biophys Res Commun. 1983 Jun 15;113(2):418-24. [PubMed Link Image]
  8. Garibotto G, Sofia A, Valli A, Tarroni A, Di Martino M, Cappelli V, Aloisi F, Procopio V: Causes of hyperhomocysteinemia in patients with chronic kidney diseases. Semin Nephrol. 2006 Jan;26(1):3-7. [PubMed Link Image]
  9. Spiekerkoetter U, Tokunaga C, Wendel U, Mayatepek E, Ijlst L, Vaz FM, van Vlies N, Overmars H, Duran M, Wijburg FA, Wanders RJ, Strauss AW: Tissue carnitine homeostasis in very-long-chain acyl-CoA dehydrogenase-deficient mice. Pediatr Res. 2005 Jun;57(6):760-4. Epub 2005 Mar 17. [PubMed Link Image]
  10. Jones MG, Goodwin CS, Amjad S, Chalmers RA: Plasma and urinary carnitine and acylcarnitines in chronic fatigue syndrome. Clin Chim Acta. 2005 Oct;360(1-2):173-7. [PubMed Link Image]
  11. Kelm A, Shaw L, Schauer R, Reuter G: The biosynthesis of 8-O-methylated sialic acids in the starfish Asterias rubens--isolation and characterisation of S-adenosyl-L-methionine:sialate-8-O-methyltransferase. Eur J Biochem. 1998 Feb 1;251(3):874-84. [PubMed Link Image]
  12. Solano AR, Sanchez ML, Podesta EJ, Turyn D, Dellacha JM: Membrane methylation in isolated rat testis interstitial cells unmasks functional luteinizing hormone receptors. Biochim Biophys Acta. 1987 Apr 2;928(1):107-13. [PubMed Link Image]
  13. D'Erme M, Santoro R, Allegra P, Reale A, Marenzi S, Strom R, Caiafa P: Inhibition of CpG methylation in linker DNA by H1 histone. Biochim Biophys Acta. 1993 May 28;1173(2):209-16. [PubMed Link Image]
  14. Hoppel CL, Genuth SM: Urinary excretion of acetylcarnitine during human diabetic and fasting ketosis. Am J Physiol. 1982 Aug;243(2):E168-72. [PubMed Link Image]
  15. Scott JM, Weir DG: The methyl folate trap. A physiological response in man to prevent methyl group deficiency in kwashiorkor (methionine deficiency) and an explanation for folic-acid induced exacerbation of subacute combined degeneration in pernicious anaemia. Lancet. 1981 Aug 15;2(8242):337-40. [PubMed Link Image]
  16. Wikipedia Link Image
Metabolic Enzymes
  1. Phosphatidylethanolamine N-methyltransferase
  2. Hydroxyindole O-methyltransferase
  3. Methionine synthase
  4. Catechol O-methyltransferase
  5. Histone-lysine N-methyltransferase, H3 lysine-79 specific
  6. Glycine N-methyltransferase
  7. Histone-lysine N-methyltransferase SETD7
  8. S-adenosylmethionine synthase isoform type-2
  9. Phenylethanolamine N-methyltransferase
  10. Diphthine synthase
  11. Arsenite methyltransferase
  12. Mitochondrial tRNA-specific 2-thiouridylase 1
  13. Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific
  14. Histone-lysine N-methyltransferase SETDB1
  15. Protein-L-isoaspartate(D-aspartate) O-methyltransferase
  16. Protein-S-isoprenylcysteine O-methyltransferase
  17. Indolethylamine N-methyltransferase
  18. DNA (cytosine-5)-methyltransferase 3A
  19. Hexaprenyldihydroxybenzoate methyltransferase, mitochondrial
  20. S-adenosylmethionine synthase isoform type-1
  21. Histone-lysine N-methyltransferase, H3 lysine-9 specific 3
  22. S-adenosylmethionine decarboxylase proenzyme
  23. Methionine synthase reductase
  24. Histone-lysine N-methyltransferase SUV39H1
  25. Nicotinamide N-methyltransferase
  26. Histone-lysine N-methyltransferase SUV39H2
  27. Histone-lysine N-methyltransferase, H3 lysine-9 specific 5
  28. Guanidinoacetate N-methyltransferase
  29. Histamine N-methyltransferase
  30. Thiopurine S-methyltransferase
  31. N6-adenosine-methyltransferase 70 kDa subunit
  32. Putative adenosylhomocysteinase 3
  33. Adenosylhomocysteinase
  34. Putative adenosylhomocysteinase 2
  35. Cystathionine beta-synthase
  36. Lipoyl synthase, mitochondrial
  37. Protein arginine N-methyltransferase 5
  38. Histone-lysine N-methyltransferase SETD1A
  39. rRNA 2'-O-methyltransferase fibrillarin
  40. Histone-lysine N-methyltransferase MLL
  41. Molybdenum cofactor biosynthesis protein 1 A
  42. DNA (cytosine-5)-methyltransferase 1
  43. DNA (cytosine-5)-methyltransferase 3B
  44. tRNA (cytosine-5-)-methyltransferase
  45. Histone-lysine N-methyltransferase SETD8
  46. Histone-lysine N-methyltransferase MLL3
  47. Methionine adenosyltransferase 2 subunit beta
  48. Histone-lysine N-methyltransferase SETDB2
  49. S-adenosylmethionine mitochondrial carrier protein
  50. tRNA (cytosine-5-)-methyltransferase NSUN2
  51. Histamine N-methyltransferase
  52. Adenosylmethionine decarboxylase 1
  53. Ubiquinone biosynthesis methyltransferase COQ5, mitochondrial
  54. tRNA wybutosine-synthesizing protein 1 homolog
  55. tRNA wybutosine-synthesizing protein 1 homolog B
  56. Molybdenum cofactor biosynthesis protein 1
  57. Radical S-adenosyl methionine domain-containing protein 2
  58. Probable histone-lysine N-methyltransferase ASH1L
  59. N-acetylserotonin O-methyltransferase-like protein
  60. Histone-arginine methyltransferase CARM1
  61. CDK5 regulatory subunit-associated protein 1-like 1
  62. CDK5 regulatory subunit-associated protein 1
  63. Elongator complex protein 3
  64. Histone-lysine N-methyltransferase EZH2
  65. rRNA/tRNA 2'-O-methyltransferase fibrillarin-like protein 1
  66. Leucine carboxyl methyltransferase 2
  67. mRNA cap guanine-N7 methyltransferase
  68. Probable S-adenosyl-L-methionine-dependent methyltransferase METT5D1
  69. 7SK snRNA methylphosphate capping enzyme
  70. Histone-lysine N-methyltransferase MLL2
  71. Histone-lysine N-methyltransferase MLL4
  72. Histone-lysine N-methyltransferase MLL5
  73. Probable histone-lysine N-methyltransferase NSD2
  74. Histone-lysine N-methyltransferase NSD3
  75. Putative methyltransferase NSUN5C
  76. Putative methyltransferase NSUN3
  77. Putative methyltransferase NSUN4
  78. Putative methyltransferase NSUN5
  79. Putative methyltransferase NSUN6
  80. Putative methyltransferase NSUN7
  81. Putative ribosomal RNA methyltransferase 1
  82. Putative ribosomal RNA methyltransferase 2
  83. Putative rRNA methyltransferase 3
  84. Radical S-adenosyl methionine domain-containing protein 1, mitochondrial
  85. Histone-lysine N-methyltransferase SETD1B
  86. Histone-lysine N-methyltransferase SETD2
  87. Histone-lysine N-methyltransferase SETMAR
  88. SET and MYND domain-containing protein 3
  89. Histone-lysine N-methyltransferase SUV420H1
  90. Histone-lysine N-methyltransferase SUV420H2
  91. Probable methyltransferase TARBP1
  92. Dimethyladenosine transferase 1, mitochondrial
  93. Dimethyladenosine transferase 2, mitochondrial
  94. tRNA guanosine-2'-O-methyltransferase TRM11 homolog
  95. tRNA guanosine-2'-O-methyltransferase TRM13 homolog
  96. N(2),N(2)-dimethylguanosine tRNA methyltransferase
  97. tRNA (adenine-N(1)-)-methyltransferase catalytic subunit TRMT61A
  98. tRNA (guanine-N(7)-)-methyltransferase
  99. Potential tRNA (adenine-N(1)-)-methyltransferase catalytic subunit TRMT61B
  100. tRNA (guanine-N(1)-)-methyltransferase
  101. tRNA wybutosine-synthesizing protein 2 homolog
  102. tRNA wybutosine-synthesizing protein 3 homolog
  103. Probable S-adenosyl-L-methionine-dependent methyltransferase METT5D2
  104. 5-methyltetrahydrofolate-homocysteine methyltransferase reductase
  105. DNA (cytosine-5)-methyltransferase 3-like
  106. Euchromatic histone-lysine N-methyltransferase 2 (Euchromatic histone- lysine N-methyltransferase 2, isoform CRA_c) (HLA-B associated transcript 8)
  107. Histone-lysine N-methyltransferase EZH1
  108. Enhancer of zeste homolog 2 (Drosophila) (Enhancer of zeste homolog 2 (Drosophila), isoform CRA_a)
  109. cDNA FLJ75818, highly similar to Homo sapiens PR/SET domain containing protein 8 (SET8), mRNA
  110. Wolf-Hirschhorn syndrome candidate 1 (Wolf-Hirschhorn syndrome candidate 1, isoform CRA_e)
  111. EHMT1 protein
  112. cDNA FLJ78356, highly similar to Homo sapiens PIMT isozyme I
  113. Protein arginine methyltransferase 5, isoform CRA_d
  114. Uncharacterized protein CARM1 (Coactivator-associated arginine methyltransferase 1, isoform CRA_b)
  115. Methionine adenosyltransferase II, beta, isoform CRA_a
  116. 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)
  117. RNA (Guanine-7-) methyltransferase
  118. 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 5392
Enzyme 3 Name Methionine synthase
Enzyme 3 Synonyms
  1. 5-methyltetrahydrofolate--homocysteine methyltransferase
  2. Vitamin-B12 dependent methionine synthase
  3. MS
Enzyme 3 Gene Name MTR
Enzyme 3 Protein Sequence >Methionine synthase
MSPALQDLSQPEGLKKTLRDEINAILQKRIMVLDGGMGTMIQREKLNEEHFRGQEFKDHA
RPLKGNNDILSITQPDVIYQIHKEYLLAGADIIETNTFSSTSIAQADYGLEHLAYRMNMC
SAGVARKAAEEVTLQTGIKRFVAGALGPTNKTLSVSPSVERPDYRNITFDELVEAYQEQA
KGLLDGGVDILLIETIFDTANAKAALFALQNLFEEKYAPRPIFISGTIVDKSGRTLSGQT
GEGFVISVSHGEPLCIGLNCALGAAEMRPFIEIIGKCTTAYVLCYPNAGLPNTFGDYDET
PSMMAKHLKDFAMDGLVNIVGGCCGSTPDHIREIAEAVKNCKPRVPPATAFEGHMLLSGL
EPFRIGPYTNFVNIGERCNVAGSRKFAKLIMAGNYEEALCVAKVQVEMGAQVLDVNMDDG
MLDGPSAMTRFCNLIASEPDIAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEDD
FLEKARKIKKYGAAMVVMAFDEEGQATETDTKIRVCTRAYHLLVKKLGFNPNDIIFDPNI
LTIGTGMEEHNLYAINFIHATKVIKETLPGARISGGLSNLSFSFRGMEAIREAMHGVFLY
HAIKSGMDMGIVNAGNLPVYDDIHKELLQLCEDLIWNKDPEATEKLLRYAQTQGTGGKKV
IQTDEWRNGPVEERLEYALVKGIEKHIIEDTEEARLNQKKYPRPLNIIEGPLMNGMKIVG
DLFGAGKMFLPQVIKSARVMKKAVGHLIPFMEKEREETRVLNGTVEEEDPYQGTIVLATV
KGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILKAALDHKADIIGLSGLITPSLDEM
IFVAKEMERLAIRIPLLIGGATTSKTHTAVKIAPRYSAPVIHVLDASKSVVVCSQLLDEN
LKDEYFEEIMEEYEDIRQDHYESLKERRYLPLSQARKSGFQMDWLSEPHPVKPTFIGTQV
FEDYDLQKLVDYIDWKPFFDVWQLRGKYPNRGFPKIFNDKTVGGEARKVYDDAHNMLNTL
ISQKKLRARGVVGFWPAQSIQDDIHLYAEAAVPQAAEPIATFYGLRQQAEKDSASTEPYY
CLSDFIAPLHSGIRDYLGLFAVACFGVEELSKAYEDDGDDYSSIMVKALGDRLAEAFAEE
LHERVRRELWAYCGSEQLDVADLRRLRYKGIRPAPGYPSQPDHTEKLTMWRLADIEQSTG
IRLTESLAMAPASAVSGLYFSNLKSKYFAVGKISKDQVEDYALRKNISVAEVEKWLGPIL
GYDTD
Enzyme 3 Number of Residues 1265
Enzyme 3 Molecular Weight 140525.9
Enzyme 3 Theoretical pI 5.27
Enzyme 3 GO Classification
Function
  • S-methyltransferase activity
  • binding
  • catalytic activity
  • cation binding
  • cobalamin binding
  • homocysteine S-methyltransferase activity
  • ion binding
  • metal ion binding
  • methionine synthase activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
  • transition metal ion binding
  • vitamin binding
  • zinc ion binding
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular aromatic compound metabolic process
  • cellular metabolic process
  • metabolic process
  • methionine biosynthetic process
  • pteridine and derivative metabolic process
  • sulfur amino acid biosynthetic process
  • sulfur amino acid metabolic process
Component
  • cell part
  • intracellular
Enzyme 3 General Function Involved in cobalamin binding
Enzyme 3 Specific Function Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate
Enzyme 3 Pathways
Enzyme 3 Reactions
  • 5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + L-methionine [RN:R00946]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein Not Available
Enzyme 3 UniProtKB/Swiss-Prot ID Q99707 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name METH_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >3798 bp
ATGTCACCCGCGCTCCAAGACCTGTCGCAACCCGAAGGTCTGAAGAAAACCCTGCGGGAT
GAGATCAATGCCATTCTGCAGAAGAGGATTATGGTGCTGGATGGAGGGATGGGGACCATG
ATCCAGCGGGAGAAGCTAAACGAAGAACACTTCCGAGGTCAGGAATTTAAAGATCATGCC
AGGCCGCTGAAAGGCAACAATGACATTTTAAGTATAACTCAGCCTGATGTCATTTACCAA
ATCCATAAGGAATACTTGCTGGCTGGGGCAGATATCATTGAAACAAATACTTTTAGCAGC
ACTAGTATTGCCCAAGCTGACTATGGCCTTGAACACTTGGCCTACCGGATGAACATGTGC
TCTGCAGGAGTGGCCAGAAAAGCTGCCGAGGAGGTAACTCTCCAGACAGGAATTAAGAGG
TTTGTGGCAGGGGCTCTGGGTCCGACTAATAAGACACTCTCTGTGTCCCCATCTGTGGAA
AGGCCGGATTATAGGAACATCACATTTGATGAGCTTGTTGAAGCATACCAAGAGCAGGCC
AAAGGACTTCTGGATGGCGGGGTTGATATCTTACTCATTGAAACTATTTTTGATACTGCC
AATGCCAAGGCAGCCTTGTTTGCACTCCAAAATCTTTTTGAGGAGAAATATGCTCCCCGG
CCTATCTTTATTTCAGGGACGATCGTTGATAAAAGTGGGCGGACTCTTTCCGGACAGACA
GGAGAGGGATTTGTCATCAGCGTGTCTCATGGAGAACCACTCTGCATTGGATTAAATTGT
GCTTTGGGTGCAGCTGAGATGAGACCTTTTATTGAAATAATTGGAAAATGTACAACAGCC
TATGTCCTCTGTTATCCCAATGCAGGTCTTCCCAACACCTTTGGTGACTATGATGAAACG
CCTTCTATGATGGCCAAGCACCTAAAGGATTTTGCTATGGATGGCTTGGTCAATATAGTT
GGAGGATGCTGTGGGTCAACACCAGATCATATCAGGGAAATTGCTGAAGCTGTGAAAAAT
TGTAAGCCTAGAGTTCCACCTGCCACTGCTTTTGAAGGACATATGTTACTGTCTGGTCTA
GAGCCCTTCAGGATTGGACCGTACACCAACTTTGTTAACATTGGAGAGCGCTGTAATGTT
GCAGGATCAAGGAAGTTTGCTAAACTCATCATGGCAGGAAACTATGAAGAAGCCTTGTGT
GTTGCCAAAGTGCAGGTGGAAATGGGAGCCCAGGTGTTGGATGTCAACATGGATGATGGC
ATGCTAGATGGTCCAAGTGCAATGACCAGATTTTGCAACTTAATTGCTTCCGAGCCAGAC
ATCGCAAAGGTACCTTTGTGCATCGACTCCTCCAATTTTGCTGTGATTGAAGCTGGGTTA
AAGTGCTGCCAAGGGAAGTGCATTGTCAATAGCATTAGTCTGAAGGAAGGAGAGGACGAC
TTCTTGGAGAAGGCCAGGAAGATTAAAAAGTATGGAGCTGCTATGGTGGTCATGGCTTTT
GATGAAGAAGGACAGGCAACAGAAACAGACACAAAAATCAGAGTGTGCACCCGGGCCTAC
CATCTGCTTGTGAAAAAACTGGGCTTTAATCCAAATGACATTATTTTTGACCCTAATATC
CTAACCATTGGGACTGGAATGGAGGAACACAACTTGTATGCCATTAATTTTATCCATGCA
ACAAAAGTCATTAAAGAAACATTACCTGGAGCCAGAATAAGTGGAGGTCTTTCCAACTTG
TCCTTCTCCTTCCGAGGAATGGAAGCCATTCGAGAAGCAATGCATGGGGTTTTCCTTTAC
CATGCAATCAAGTCTGGCATGGACATGGGGATAGTGAATGCTGGAAACCTCCCTGTGTAT
GATGATATCCATAAGGAACTTCTGCAGCTCTGTGAAGATCTCATCTGGAATAAAGACCCT
GAGGCCACTGAGAAGCTCTTACGTTATGCCCAGACTCAAGGCACAGGAGGGAAGAAAGTC
ATTCAGACTGATGAGTGGAGAAATGGCCCTGTCGAAGAACGCCTTGAGTATGCCCTTGTG
AAGGGCATTGAAAAACATATTATTGAGGATACTGAGGAAGCCAGGTTAAACCAAAAAAAA
TATCCCCGACCTCTCAATATAATTGAAGGACCCCTGATGAATGGAATGAAAATTGTTGGT
GATCTTTTTGGAGCTGGAAAAATGTTTCTACCTCAGGTTATAAAGTCAGCCCGGGTTATG
AAGAAGGCTGTTGGCCACCTTATCCCTTTCATGGAAAAAGAAAGAGAAGAAACCAGAGTG
CTTAACGGCACAGTAGAAGAAGAGGACCCTTACCAGGGCACCATCGTGCTGGCCACTGTT
AAAGGCGACGTGCACGACATAGGCAAGAACATAGTTGGAGTAGTCCTTGGCTGCAATAAT
TTCCGAGTTATTGATTTAGGAGTCATGACTCCATGTGATAAGATACTGAAAGCTGCTCTT
GACCACAAAGCAGATATAATTGGCCTGTCAGGACTCATCACTCCTTCCCTGGATGAAATG
ATTTTTGTTGCCAAGGAAATGGAGAGATTAGCTATAAGGATTCCATTGTTGATTGGAGGA
GCAACCACTTCAAAAACCCACACAGCAGTTAAAATAGCTCCGAGATACAGTGCACCTGTA
ATCCATGTCCTGGACGCGTCCAAGAGTGTGGTGGTGTGTTCCCAGCTGTTAGATGAAAAT
CTAAAGGATGAATACTTTGAGGAAATCATGGAAGAATATGAAGATATTAGACAGGACCAT
TATGAGTCTCTCAAGGAGAGGAGATACTTACCCTTAAGTCAAGCCAGAAAAAGTGGTTTC
CAAATGGATTGGCTGTCTGAACCTCACCCAGTGAAGCCCACGTTTATTGGGACCCAGGTC
TTTGAAGACTATGACCTGCAGAAGCTGGTGGACTACATTGACTGGAAGCCTTTCTTTGAT
GTCTGGCAGCTCCGGGGCAAGTACCCGAATCGAGGCTTCCCCAAGATATTTAACGACAAA
ACAGTAGGTGGAGAGGCCAGGAAGGTCTACGATGATGCCCACAATATGCTGAACACACTG
ATTAGTCAAAAGAAACTCCGGGCCCGGGGTGTGGTTGGGTTCTGGCCAGCACAGAGTATC
CAAGACGACATTCACCTGTACGCAGAGGCTGCTGTGCCCCAGGCTGCAGAGCCCATAGCC
ACTTTCTATGGGTTAAGGCAACAGGCTGAGAAGGACTCTGCCAGCACGGAGCCATACTAC
TGCCTCTCAGACTTCATCGCTCCCTTGCATTCTGGCATCCGTGACTACCTGGGCCTGTTT
GCCGTTGCCTGCTTTGGGGTAGAAGAGCTGAGCAAGGCCTATGAGGATGATGGTGACGAC
TACAGCAGCATCATGGTCAAGGCGCTGGGGGACCGGCTGGCAGAGGCCTTTGCAGAAGAG
CTCCATGAAAGAGTTCGCCGAGAACTGTGGGCCTACTGTGGCAGTGAGCAGCTGGACGTC
GCAGACCTGCGAAGGTTGCGGTACAAGGGCATCCGCCCGGCTCCTGGCTACCCCAGCCAG
CCCGACCACACCGAGAAGCTCACCATGTGGAGACTCGCAGACATCGAGCAGTCTACAGGC
ATTAGGTTAACAGAATCATTAGCAATGGCACCTGCTTCAGCAGTCTCAGGCCTCTACTTC
TCCAATTTGAAGTCCAAATATTTTGCTGTGGGGAAGATTTCCAAGGATCAGGTTGAGGAT
TATGCATTGAGGAAGAACATATCTGTGGCTGAGGTTGAGAAATGGCTTGGACCCATTTTG
GGATATGATACAGACTAA
Enzyme 3 GenBank Gene ID U71285 Link Image
Enzyme 3 GeneCard ID MTR Link Image
Enzyme 3 GenAtlas ID MTR Link Image
Enzyme 3 HGNC ID HGNC:7468 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 1q43
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Leclerc D, Campeau E, Goyette P, Adjalla CE, Christensen B, Ross M, Eydoux P, Rosenblatt DS, Rozen R, Gravel RA: Human methionine synthase: cDNA cloning and identification of mutations in patients of the cblG complementation group of folate/cobalamin disorders. Hum Mol Genet. 1996 Dec;5(12):1867-74. [PubMed Link Image]
  2. Li YN, Gulati S, Baker PJ, Brody LC, Banerjee R, Kruger WD: Cloning, mapping and RNA analysis of the human methionine synthase gene. Hum Mol Genet. 1996 Dec;5(12):1851-8. [PubMed Link Image]
  3. Chen LH, Liu ML, Hwang HY, Chen LS, Korenberg J, Shane B: Human methionine synthase. cDNA cloning, gene localization, and expression. J Biol Chem. 1997 Feb 7;272(6):3628-34. [PubMed Link Image]
  4. 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]
  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. Gulati S, Baker P, Li YN, Fowler B, Kruger W, Brody LC, Banerjee R: Defects in human methionine synthase in cblG patients. Hum Mol Genet. 1996 Dec;5(12):1859-65. [PubMed Link Image]
  7. 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]
  8. 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 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5504
Enzyme 4 Name Catechol O-methyltransferase
Enzyme 4 Synonyms Not Available
Enzyme 4 Gene Name COMT
Enzyme 4 Protein Sequence >Catechol O-methyltransferase
MPEAPPLLLAAVLLGLVLLVVLLLLLRHWGWGLCLIGWNEFILQPIHNLLMGDTKEQRIL
NHVLQHAEPGNAQSVLEAIDTYCEQKEWAMNVGDKKGKIVDAVIQEHQPSVLLELGAYCG
YSAVRMARLLSPGARLITIEINPDCAAITQRMVDFAGVKDKVTLVVGASQDIIPQLKKKY
DVDTLDMVFLDHWKDRYLPDTLLLEECGLLRKGTVLLADNVICPGAPDFLAHVRGSSCFE
CTHYQSFLEYREVVDGLEKAIYKGPGSEAGP
Enzyme 4 Number of Residues 271
Enzyme 4 Molecular Weight 30036.8
Enzyme 4 Theoretical pI 5.15
Enzyme 4 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 4 General Function Involved in magnesium ion binding
Enzyme 4 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 4 Pathways
Enzyme 4 Reactions
  • S-adenosyl-L-methionine + a catechol = S-adenosyl-L-homocysteine + a guaiacol [RN:R07330]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • 7-26
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 180920 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P21964 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name COMT_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >816 bp
ATGCCGGAGGCCCCGCCTCTGCTGTTGGCAGCTGTGTTGCTGGGCCTGGTGCTGCTGGTG
GTGCTGCTGCTGCTTCTGAGGCACTGGGGCTGGGGCCTGTGCCTTATCGGCTGGAACGAG
TTCATCCTGCAGCCCATCCACAACCTGCTCATGGGTGACACCAAGGAGCAGCGCATCCTG
AACCACGTGCTGCAGCATGCGGAGCCCGGGAACGCACAGAGCGTGCTGGAGGCCATTGAC
ACCTACTGCGAGCAGAAGGAGTGGGCCATGAACGTGGGCGACAAGAAAGGCAAGATCGTG
GACGCCGTGATTCAGGAGCACCAGCCCTCCGTGCTGCTGGAGCTGGGGGCCTACTGTGGC
TACTCAGCTGTGCGCATGGCCCGCCTGCTGTCACCAGGGGCGAGGCTCATCACCATCGAG
ATCAACCCCGACTGTGCCGCCATCACCCAGCGGATGGTGGATTTCGCTGGCGTGAAGGAC
AAGGTCACCCTTGTGGTTGGAGCGTCCCAGGACATCATCCCCCAGCTGAAGAAGAAGTAT
GATGTGGACACACTGGACATGGTCTTCCTCGACCACTGGAAGGACCGGTACCTGCCGGAC
ACGCTTCTCTTGGAGGAATGTGGCCTGCTGCGGAAGGGGACAGTGCTACTGGCTGACAAC
GTGATCTGCCCAGGTGCGCCAGACTTCCTAGCACACGTGCGCGGGAGCAGCTGCTTTGAG
TGCACACACTACCAATCGTTCCTGGAATACAGGGAGGTGGTGGACGGCCTGGAGAAGGCC
ATCTACAAGGGCCCAGGCAGCGAAGCAGGGCCCTGA
Enzyme 4 GenBank Gene ID M65212 Link Image
Enzyme 4 GeneCard ID COMT Link Image
Enzyme 4 GenAtlas ID COMT Link Image
Enzyme 4 HGNC ID HGNC:2228 Link Image
Enzyme 4 Chromosome Location 2
Enzyme 4 Locus 22q11.21-q11.23|22q11.21
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 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 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5639
Enzyme 5 Name Histone-lysine N-methyltransferase, H3 lysine-79 specific
Enzyme 5 Synonyms
  1. DOT1-like protein
  2. Histone H3-K79 methyltransferase
  3. H3-K79-HMTase
  4. Lysine N-methyltransferase 4
Enzyme 5 Gene Name DOT1L
Enzyme 5 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 5 Number of Residues 1739
Enzyme 5 Molecular Weight 184851.2
Enzyme 5 Theoretical pI 9.88
Enzyme 5 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 5 General Function Involved in DNA binding
Enzyme 5 Specific Function Histone methyltransferase. Methylates 'Lys-79' of histone H3. Nucleosomes are preferred as substrate compared to free histones. Binds to DNA
Enzyme 5 Pathways
Enzyme 5 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 22094135 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q8TEK3 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name DOT1L_HUMAN Link Image
Enzyme 5 PDB ID 1NW3 Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence Not Available
Enzyme 5 GenBank Gene ID Not Available
Enzyme 5 GeneCard ID DOT1L Link Image
Enzyme 5 GenAtlas ID DOT1L Link Image
Enzyme 5 HGNC ID HGNC:24948 Link Image
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 19p13.3
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 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 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5640
Enzyme 6 Name Glycine N-methyltransferase
Enzyme 6 Synonyms Not Available
Enzyme 6 Gene Name GNMT
Enzyme 6 Protein Sequence >Glycine N-methyltransferase
MVDSVYRTRSLGVAAEGLPDQYADGEAARVWQLYIGDTRSRTAEYKAWLLGLLRQHGCQR
VLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYALKERWNRRHEPAFDKWVIEEANWMT
LDKDVPQSAEGGFDAVICLGNSFAHLPDCKGDQSEHRLALKNIASMVRAGGLLVIDHRNY
DHILSTGCAPPGKNIYYKSDLTKDVTTSVLIVNNKAHMVTLDYTVQVPGAGQDGSPGLSK
FRLSYYPHCLASFTELLQAAFGGKCQHSVLGDFKPYKPGQTYIPCYFIHVLKRTD
Enzyme 6 Number of Residues 295
Enzyme 6 Molecular Weight 32742.0
Enzyme 6 Theoretical pI 7.03
Enzyme 6 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 6 General Function Involved in folic acid binding
Enzyme 6 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 6 Pathways
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
Enzyme 6 Reactions
  • S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine [RN:R00367]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 8671584 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q14749 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name GNMT_HUMAN Link Image
Enzyme 6 PDB ID 1R74 Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >888 bp
ATGGTGGACAGCGTGTACCGGACCCGCTCCCTGGGGGTGGCGGCCGAAGGGCTCCCGGAC
CAGTACGCGGACGGGGAGGCGGCGCGCGTGTGGCAGCTGTATATCGGAGACACCCGCAGC
CGCACCGCCGAGTACAAGGCATGGCTGCTTGGGCTGCTGCGCCAGCACGGCTGCCAGCGG
GTGCTCGACGTAGCCTGTGGCACTGGGGTGGACTCCATTATGCTGGTGGAAGAGGGCTTC
AGTGTGACGAGTGTGGATGCCAGTGACAAGATGCTGAAGTATGCACTTAAGGAGCGCTGG
AACCGGCGGCACGAGCCCGCCTTCGACAAGTGGGTCATCGAAGAAGCCAACTGGATGACT
CTGGACAAAGATGTGCCCCAGTCAGCAGAGGGTGGCTTTGATGCTGTCATCTGCCTTGGA
AACAGTTTCGCTCACTTGCCAGACTGCAAAGGGGACCAGAGTGAGCACCGGCTGGCGCTG
AAAAACATTGCGAGCATGGTGCGGGCAGGGGGCCTACTGGTCATTGATCATCGCAACTAC
GACCACATCCTCAGTACAGGCTGTGCACCCCCAGGGAAGAACATCTACTATAAGAGTGAC
TTGACCAAGGACGTCACAACATCAGTGCTGATAGTGAACAACAAGGCCCACATGGTGACC
CTGGACTATACGGTGCAGGTGCCGGGGGCTGGCCAGGATGGCTCTCCTGGCTTGAGTAAG
TTCCGGCTCTCCTACTACCCACACTGTCTGGCATCCTTCACGGAGCTGCTCCAAGCAGCC
TTCGGAGGTAAGTGCCAGCACAGCGTCCTGGGCGACTTCAAGCCTTACAAGCCAGGCCAA
ACCTACATTCCCTGCTACTTCATCCACGTGCTCAAGAGGACAGACTGA
Enzyme 6 GenBank Gene ID AF101477 Link Image
Enzyme 6 GeneCard ID GNMT Link Image
Enzyme 6 GenAtlas ID GNMT Link Image
Enzyme 6 HGNC ID HGNC:4415 Link Image
Enzyme 6 Chromosome Location 6
Enzyme 6 Locus 6p12
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 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 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5641
Enzyme 7 Name Histone-lysine N-methyltransferase SETD7
Enzyme 7 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 7 Gene Name SETD7
Enzyme 7 Protein Sequence >Histone-lysine N-methyltransferase SETD7
MDSDDEMVEEAVEGHLDDDGLPHGFCTVTYSSTDRFEGNFVHGEKNGRGKFFFFDGSTLE
GYYVDDALQGQGVYTYEDGGVLQGTYVDGELNGPAQEYDTDGRLIFKGQYKDNIRHGVCW
IYYPDGGSLVGEVNEDGEMTGEKIAYVYPDERTALYGKFIDGEMIEGKLATLMSTEEGRP
HFELMPGNSVYHFDKSTSSCISTNALLPDPYESERVYVAESLISSAGEGLFSKVAVGPNT
VMSFYNGVRITHQEVDSRDWALNGNTLSLDEETVIDVPEPYNHVSKYCASLGHKANHSFT
PNCIYDMFVHPRFGPIKCIRTLRAVEADEELTVAYGYDHSPPGKSGPEAPEWYQVELKAF
QATQQK
Enzyme 7 Number of Residues 366
Enzyme 7 Molecular Weight 40720.6
Enzyme 7 Theoretical pI 4.25
Enzyme 7 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 7 General Function Involved in histone-lysine N-methyltransferase activity
Enzyme 7 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 7 Pathways
Enzyme 7 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
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 Q8WTS6 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name SETD7_HUMAN Link Image
Enzyme 7 PDB ID 1N6C Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1101 bp
ATGGATAGCGACGACGAGATGGTGGAGGAGGCGGTGGAAGGGCACCTGGACGATGACGGA
TTACCGCACGGGTTCTGCACAGTCACCTACTCCTCCACAGACAGATTTGAGGGGAACTTT
GTTCACGGAGAAAAGAACGGACGGGGGAAGTTCTTCTTCTTTGATGGCAGCACCCTGGAG
GGGTATTATGTGGATGATGCCTTGCAGGGCCAGGGAGTTTACACTTACGAAGATGGGGGA
GTTCTCCAGGGCACGTATGTAGACGGAGAGCTGAACGGTCCAGCCCAGGAATATGACACA
GATGGGAGACTGATCTTCAAGGGGCAGTATAAAGATAACATTCGTCATGGAGTGTGCTGG
ATATATTACCCAGATGGAGGAAGCCTTGTAGGAGAAGTAAATGAAGATGGGGAGATGACT
GGAGAGAAGATAGCCTATGTGTACCCTGATGAGAGGACCGCACTTTATGGGAAATTTATT
GATGGAGAGATGATAGAAGGCAAACTGGCTACCCTTATGTCCACTGAAGAAGGGAGGCCT
CACTTTGAACTGATGCCTGGAAATTCAGTGTACCACTTTGATAAGTCGACTTCATCTTGC
ATTTCTACCAATGCTCTTCTTCCAGATCCTTATGAATCAGAAAGGGTTTATGTTGCTGAA
TCTCTTATTTCCAGTGCTGGAGAAGGACTTTTTTCAAAGGTAGCTGTGGGACCTAATACT
GTTATGTCTTTTTATAATGGAGTTCGAATTACACACCAAGAGGTTGACAGCAGGGACTGG
GCCCTTAATGGGAACACCCTCTCCCTTGATGAAGAAACGGTCATTGATGTGCCTGAGCCC
TATAACCACGTATCCAAGTACTGTGCCTCCTTGGGACACAAGGCAAATCACTCCTTCACT
CCAAACTGCATCTACGATATGTTTGTCCACCCCCGTTTTGGGCCCATCAAATGCATCCGC
ACCCTGAGAGCAGTGGAGGCCGATGAAGAGCTCACCGTTGCCTATGGCTATGACCACAGC
CCCCCCGGGAAGAGTGGGCCTGAAGCCCCTGAGTGGTACCAGGTGGAGCTGAAGGCCTTC
CAGGCCACCCAGCAAAAGTGA
Enzyme 7 GenBank Gene ID AF448510 Link Image
Enzyme 7 GeneCard ID SETD7 Link Image
Enzyme 7 GenAtlas ID SETD7 Link Image
Enzyme 7 HGNC ID HGNC:30412 Link Image
Enzyme 7 Chromosome Location 4
Enzyme 7 Locus 4q28
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 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 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5642
Enzyme 8 Name S-adenosylmethionine synthase isoform type-2
Enzyme 8 Synonyms
  1. AdoMet synthase 2
  2. Methionine adenosyltransferase 2
  3. MAT 2
  4. Methionine adenosyltransferase II
  5. MAT-II
Enzyme 8 Gene Name MAT2A
Enzyme 8 Protein Sequence >S-adenosylmethionine synthase isoform type-2
MNGQLNGFHEAFIEEGTFLFTSESVGEGHPDKICDQISDAVLDAHLQQDPDAKVACETVA
KTGMILLAGEITSRAAVDYQKVVREAVKHIGYDDSSKGFDYKTCNVLVALEQQSPDIAQG
VHLDRNEEDIGAGDQGLMFGYATDETEECMPLTIVLAHKLNAKLAELRRNGTLPWLRPDS
KTQVTVQYMQDRGAVLPIRVHTIVISVQHDEEVCLDEMRDALKEKVIKAVVPAKYLDEDT
IYHLQPSGRFVIGGPQGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARW
VAKSLVKGGLCRRVLVQVSYAIGVSHPLSISIFHYGTSQKSERELLEIVKKNFDLRPGVI
VRDLDLKKPIYQRTAAYGHFGRDSFPWEVPKKLKY
Enzyme 8 Number of Residues 395
Enzyme 8 Molecular Weight 43660.4
Enzyme 8 Theoretical pI 6.45
Enzyme 8 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • methionine adenosyltransferase activity
  • nucleoside binding
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • cellular metabolic process
  • metabolic process
  • one-carbon metabolic process
Component
Enzyme 8 General Function Involved in methionine adenosyltransferase activity
Enzyme 8 Specific Function Catalyzes the formation of S-adenosylmethionine from methionine and ATP
Enzyme 8 Pathways
Enzyme 8 Reactions
  • ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine [RN:R00177]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 36327 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P31153 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name METK2_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1188 bp
ATGAACGGACAGCTCAACGGCTTCCACGAGGCGTTCATCGAGGAGGGCACATTCCTTTTC
ACCTCAGAGTCGGTCGGGGAAGGCCACCCAGATAAGATTTGTGACCAAATCAGTGATGCT
GTCCTTGATGCCCACCTTCAGCAGGATCCTGATGCCAAAGTAGCTTGTGAAACTGTTGCT
AAAACTGGAATGATCCTTCTTGCTGGGGAAATTACATCCAGAGCTGCTGTTGACTACCAG
AAAGTGGTTCGTGAAGCTGTTAAACACATTGGATATGATGATTCTTCCAAAGGTTTTGAC
TACAAGACTTGTAACGTGCTGGTAGCCTTGGAGCAACAGTCACCAGATATTGCTCAAGGT
GTTCATCTTGACAGAAATGAAGAAGACATTGGTGCTGGAGACCAGGGCTTAATGTTTGGC
TATGCCACTGATGAAACTGAGGAGTGTATGCCTTTAACCATTGTCTTGGCACACAAGCTA
AATGCCAAACTGGCAGAACTACGCCGTAATGGCACTTTGCCTTGGTTACGCCCTGATTCT
AAAACTCAAGTTACTGTGCAGTATATGCAGGATCGAGGTGCTGTGCTTCCCATCAGAGTC
CACACAATTGTTATATCTGTTCAGCATGATGAAGAGGTTTGTCTTGATGAAATGAGGGAT
GCCCTAAAGGAGAAAGTCATCAAAGCAGTTGTGCCTGCGAAATACCTTGATGAGGATACA
ATCTACCACCTACAGCCAAGTGGCAGATTTGTTATTGGTGGGCCTCAGGGTGATGCTGGT
TTGACTGGACGGAAAATCATTGTGGACACTTATGGCGGTTGGGGTGCTCATGGAGGAGGT
GCCTTTTCAGGAAAGGATTATACCAAGGTCGACCGTTCAGCTGCTTATGCTGCTCGTTGG
GTGGCAAAATCCCTTGTTAAAGGAGGTCTGTGCCGGAGGGTTCTTGTTCAGGTCTCTTAT
GCTATTGGAGTTTCTCATCCATTATCTATCTCCATTTTCCATTATGGTACCTCTCAGAAG
AGTGAGAGAGAGCTATTAGAGATTGTGAAGAAGAATTTCGATCTCCGCCCTGGGGTCATT
GTCAGGGATCTGGATCTGAAGAAGCCAATTTATCAGAGGACTGCAGCCTATGGCCACTTT
GGTAGGGACAGCTTCCCATGGGAAGTGCCCAAAAAGCTTAAATATTGA
Enzyme 8 GenBank Gene ID X68836 Link Image
Enzyme 8 GeneCard ID MAT2A Link Image
Enzyme 8 GenAtlas ID MAT2A Link Image
Enzyme 8 HGNC ID HGNC:6904 Link Image
Enzyme 8 Chromosome Location 2
Enzyme 8 Locus 2p11.2
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Horikawa S, Tsukada K: Molecular cloning and developmental expression of a human kidney S-adenosylmethionine synthetase. FEBS Lett. 1992 Nov 2;312(1):37-41. [PubMed Link Image]
  2. Panayiotidis MI, Stabler SP, Ahmad A, Pappa A, Legros LH Jr, Hernandez-Saavedra D, Schneider BK, Allen RH, Vasiliou V, McCord JM, Kotb M, White CW: Activation of a novel isoform of methionine adenosyl transferase 2A and increased S-adenosylmethionine turnover in lung epithelial cells exposed to hyperoxia. Free Radic Biol Med. 2006 Jan 15;40(2):348-58. Epub 2005 Nov 18. [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, 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. LeGros HL Jr, Halim AB, Geller AM, Kotb M: Cloning, expression, and functional characterization of the beta regulatory subunit of human methionine adenosyltransferase (MAT II). J Biol Chem. 2000 Jan 28;275(4):2359-66. [PubMed Link Image]
  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. 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 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5643
Enzyme 9 Name Phenylethanolamine N-methyltransferase
Enzyme 9 Synonyms
  1. PNMTase
  2. Noradrenaline N-methyltransferase
Enzyme 9 Gene Name PNMT
Enzyme 9 Protein Sequence >Phenylethanolamine N-methyltransferase
MSGADRSPNAGAAPDSAPGQAAVASAYQRFEPRAYLRNNYAPPRGDLCNPNGVGPWKLRC
LAQTFATGEVSGRTLIDIGSGPTVYQLLSACSHFEDITMTDFLEVNRQELGRWLQEEPGA
FNWSMYSQHACLIEGKGECWQDKERQLRARVKRVLPIDVHQPQPLGAGSPAPLPADALVS
AFCLEAVSPDLASFQRALDHITTLLRPGGHLLLIGALEESWYLAGEARLTVVPVSEEEVR
EALVRSGYKVRDLRTYIMPAHLQTGVDDVKGVFFAWAQKVGL
Enzyme 9 Number of Residues 282
Enzyme 9 Molecular Weight 30854.7
Enzyme 9 Theoretical pI 5.96
Enzyme 9 GO Classification
Function
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
Component
Enzyme 9 General Function Involved in methyltransferase activity
Enzyme 9 Specific Function Converts noradrenaline to adrenaline
Enzyme 9 Pathways
Enzyme 9 Reactions
  • S-adenosyl-L-methionine + phenylethanolamine = S-adenosyl-L-homocysteine + N-methylphenylethanolamine [RN:R04033]
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein Not Available
Enzyme 9 UniProtKB/Swiss-Prot ID P11086 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name PNMT_HUMAN Link Image
Enzyme 9 PDB ID 1N7J Link Image
Enzyme 9 PDB File Show
Enzyme 9 3D Structure
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >849 bp
ATGAGCGGCGCAGACCGTAGCCCCAATGCGGGCGCAGCCCCTGACTCGGCCCCGGGCCAG
GCGGCGGTGGCTTCGGCCTACCAGCGCTTCGAGCCGCGCGCCTACCTCCGCAACAACTAC
GCGCCCCCTCGCGGGGACCTGTGCAACCCGAACGGCGTCGGGCCGTGGAAGCTGCGCTGC
TTGGCGCAGACCTTCGCCACCGGTGAAGTGTCCGGACGCACCCTCATCGACATTGGTTCA
GGCCCCACCGTGTACCAGCTGCTCAGTGCCTGCAGCCACTTTGAGGACATCACCATGACA
GATTTCCTGGAGGTCAACCGCCAGGAGCTGGGGCGCTGGCTGCAGGAGGAGCCGGGGGCC
TTCAACTGGAGCATGTACAGCCAACATGCCTGCCTCATTGAGGGCAAGGGGGAATGCTGG
CAGGATAAGGAGCGCCAGCTGCGAGCCAGGGTGAAACGGGTCCTGCCCATCGACGTGCAC
CAGCCCCAGCCCCTGGGTGCTGGGAGCCCAGCTCCCCTGCCTGCTGACGCCCTGGTCTCT
GCCTTCTGCTTGGAGGCTGTGAGCCCAGATCTTGCCAGCTTTCAGCGGGCCCTGGACCAC
ATCACCACGCTGCTGAGGCCTGGGGGGCACCTCCTCCTCATCGGGGCCCTGGAGGAGTCG
TGGTACCTGGCTGGGGAGGCCAGGCTGACGGTGGTGCCAGTGTCTGAGGAGGAGGTGAGG
GAGGCCCTGGTGCGTAGTGGCTACAAGGTCCGGGACCTCCGCACCTATATCATGCCTGCC
CACCTTCAGACAGGCGTAGATGATGTCAAGGGCGTCTTCTTCGCCTGGGCTCAGAAGGTT
GGGCTGTGA
Enzyme 9 GenBank Gene ID J03727 Link Image
Enzyme 9 GeneCard ID PNMT Link Image
Enzyme 9 GenAtlas ID PNMT Link Image
Enzyme 9 HGNC ID HGNC:9160 Link Image
Enzyme 9 Chromosome Location 1
Enzyme 9 Locus 17q
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 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 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5644
Enzyme 10 Name Diphthine synthase
Enzyme 10 Synonyms
  1. Diphthamide biosynthesis methyltransferase
Enzyme 10 Gene Name DPH5
Enzyme 10 Protein Sequence >Diphthine synthase
MLYLIGLGLGDAKDITVKGLEVVRRCSRVYLEAYTSVLTVGKEALEEFYGRKLVVADREE
VEQEADNILKDADISDVAFLVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAVGCC
GLQLYKFGETVSIVFWTDTWRPESFFDKVKKNRQNGMHTLCLLDIKVKEQSLENLIKGRK
IYEPPRYMSVNQAAQQLLEIVQNQRIRGEEPAVTEETLCVGLARVGADDQKIAAGTLRQM
CTVDLGEPLHSLIITGGSIHPMEMEMLSLFSIPENSSESQSINGL
Enzyme 10 Number of Residues 285
Enzyme 10 Molecular Weight 31651.2
Enzyme 10 Theoretical pI 4.96
Enzyme 10 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 10 General Function Involved in methyltransferase activity
Enzyme 10 Specific Function Required for the trimethylation step of diphthamide biosynthesis
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions
  • S-adenosyl-L-methionine + 2-(3-carboxy-3-aminopropyl)-L-histidine = S-adenosyl-L-homocysteine + 2-[3-carboxy-3-(methylammonio)propyl]-L-histidine [RN:R04481]
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 117190326 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q9H2P9 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name DPH5_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >858 bp
ATGCTTTATCTCATCGGGTTGGGCCTGGGAGATGCCAAGGACATCACAGTCAAGGGCCTG
GAAGTTGTTAGACGCTGCAGTCGAGTGTATCTGGAAGCCTACACCTCAGTCCTAACTGTA
GGGAAGGAAGCCTTGGAAGAGTTTTATGGAAGAAAATTGGTTGTTGCTGATAGAGAAGAA
GTGGAACAAGAAGCAGATAATATTTTAAAGGATGCTGATATCAGTGATGTTGCATTCCTT
GTGGTTGGTGATCCATTTGGGGCCACAACACACAGTGATCTTGTTCTAAGAGCAACAAAG
CTGGGAATTCCTTATAGAGTTATTCACAATGCCTCCATAATGAATGCTGTAGGCTGCTGT
GGTTTACAGTTATATAAGTTTGGAGAGACAGTTTCTATTGTTTTTTGGACAGACACTTGG
AGACCAGAAAGCTTCTTTGACAAAGTGAAGAAGAACAGACAAAATGGCATGCACACATTA
TGTTTACTAGACATCAAAGTAAAGGAGCAGTCTTTGGAAAATCTAATCAAGGGAAGGAAG
ATCTATGAACCTCCACGGTATATGAGTGTAAACCAAGCAGCCCAGCAGCTTCTGGAGATT
GTTCAAAATCAAAGAATACGAGGAGAAGAACCAGCAGTTACCGAGGAGACACTTTGTGTT
GGCTTAGCCAGGGTTGGAGCCGACGACCAGAAAATTGCAGCAGGCACTTTAAGGCAAATG
TGCACTGTGGACTTGGGAGAACCATTGCATTCCTTGATCATCACAGGAGGCAGCATACAT
CCAATGGAGATGGAGATGCTAAGTCTGTTTTCCATACCAGAAAATAGCTCAGAATCTCAA
AGCATCAATGGACTTTGA
Enzyme 10 GenBank Gene ID NM_001077394.1 Link Image
Enzyme 10 GeneCard ID DPH5 Link Image
Enzyme 10 GenAtlas ID DPH5 Link Image
Enzyme 10 HGNC ID HGNC:24270 Link Image
Enzyme 10 Chromosome Location 1
Enzyme 10 Locus 1p21.2
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W: Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. Genome Res. 2000 May;10(5):703-13. [PubMed Link Image]
  2. 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]
  3. Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed Link Image]
  4. 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 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5645
Enzyme 11 Name Arsenite methyltransferase
Enzyme 11 Synonyms
  1. Methylarsonite methyltransferase
  2. S-adenosyl-L-methionine:arsenic(III) methyltransferase
Enzyme 11 Gene Name AS3MT
Enzyme 11 Protein Sequence >Arsenite methyltransferase
MAALRDAEIQKDVQTYYGQVLKRSADLQTNGCVTTARPVPKHIREALQNVHEEVALRYYG
CGLVIPEHLENCWILDLGSGSGRDCYVLSQLVGEKGHVTGIDMTKGQVEVAEKYLDYHME
KYGFQASNVTFIHGYIEKLGEAGIKNESHDIVVSNCVINLVPDKQQVLQEAYRVLKHGGE
LYFSDVYTSLELPEEIRTHKVLWGECLGGALYWKELAVLAQKIGFCPPRLVTANLITIQN
KELERVIGDCRFVSATFRLFKHSKTGPTKRCQVIYNGGITGHEKELMFDANFTFKEGEIV
EVDEETAAILKNSRFAQDFLIRPIGEKLPTSGGCSALELKDIITDPFKLAEESDSMKSRC
VPDAAGGCCGTKKSC
Enzyme 11 Number of Residues 375
Enzyme 11 Molecular Weight 41747.5
Enzyme 11 Theoretical pI 6.14
Enzyme 11 GO Classification
Function
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • metabolic process
Component
Enzyme 11 General Function Involved in methyltransferase activity
Enzyme 11 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 11 Pathways Not Available
Enzyme 11 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 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 109389364 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q9HBK9 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name AS3MT_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >1128 bp
ATGGCTGCACTTCGTGACGCTGAGATACAGAAGGACGTGCAGACCTACTACGGGCAGGTG
CTGAAGAGATCGGCAGACCTCCAGACCAACGGCTGTGTCACCACAGCCAGGCCGGTCCCC
AAGCACATCCGGGAAGCCTTGCAAAATGTACACGAAGAAGTAGCCCTAAGATATTATGGC
TGTGGTCTGGTGATCCCTGAGCATCTAGAAAACTGCTGGATTTTGGATCTGGGTAGTGGA
AGTGGCAGAGATTGCTATGTACTTAGCCAGCTGGTTGGTGAAAAAGGACACGTGACTGGA
ATAGACATGACCAAAGGCCAGGTGGAAGTGGCTGAAAAGTATCTTGACTATCACATGGAA
AAATATGGCTTCCAGGCATCTAATGTGACTTTTATTCATGGCTACATTGAGAAGTTGGGA
GAGGCTGGAATCAAGAATGAGAGCCATGATATTGTTGTATCAAACTGTGTTATTAACCTT
GTGCCTGATAAACAACAAGTGCTTCAGGAGGCATATCGGGTGCTGAAGCATGGTGGGGAG
TTATATTTCAGTGACGTCTATACGAGCCTTGAACTGCCAGAAGAAATCAGGACACACAAA
GTTTTATGGGGTGAGTGTCTGGGTGGTGCTTTATACTGGAAGGAACTTGCTGTCCTTGCT
CAAAAAATTGGGTTCTGCCCTCCACGTTTGGTCACTGCCAATCTCATTACAATTCAAAAC
AAGGAACTGGAAAGAGTTATCGGTGACTGTCGTTTTGTTTCTGCAACATTTCGCCTCTTC
AAACACTCTAAGACAGGACCAACCAAGAGATGCCAAGTTATTTACAATGGAGGAATTACA
GGACATGAAAAAGAACTAATGTTTGATGCCAATTTTACATTTAAGGAAGGTGAAATTGTT
GAAGTGGATGAAGAAACAGCAGCTATCTTGAAGAATTCAAGATTTGCTCAAGATTTTCTG
ATCAGACCAATTGGAGAGAAGTTGCCAACATCTGGAGGCTGTTCTGCTTTGGAGTTAAAG
GATATAATCACAGATCCATTTAAGCTTGCAGAAGAGTCTGACAGTATGAAGTCCAGATGT
GTCCCTGATGCTGCTGGAGGCTGCTGTGGCACAAAGAAAAGCTGCTAA
Enzyme 11 GenBank Gene ID NM_020682.3 Link Image
Enzyme 11 GeneCard ID AS3MT Link Image
Enzyme 11 GenAtlas ID AS3MT Link Image
Enzyme 11 HGNC ID HGNC:17452 Link Image
Enzyme 11 Chromosome Location 1
Enzyme 11 Locus 10q24.32
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 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 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5646
Enzyme 12 Name Mitochondrial tRNA-specific 2-thiouridylase 1
Enzyme 12 Synonyms
  1. MTO2 homolog
Enzyme 12 Gene Name TRMU
Enzyme 12 Protein Sequence >Mitochondrial tRNA-specific 2-thiouridylase 1
MQALRHVVCALSGGVDSAVAALLLRRRGYQVTGVFMKNWDSLDEHGVCTADKDCEDAYRV
CQILDIPFHQVSYVKEYWNDVFSDFLNEYEKGRTPNPDIVCNKHIKFSCFFHYAVDNLGA
DAIATGHYARTSLEDEEVFEQKHVKKPEGLFRNRFEVRNAVKLLQAADSFKDQTFFLSQV
SQDALRRTIFPLGGLTKEFVKKIAAENRLHHVLQKKESMGMCFIGKRNFEHFLLQYLQPR
PGHFISIEDNKVLGTHKGWFLYTLGQRANIGGLREPWYVVEKDSVKGDVFVAPRTDHPAL
YRDLLRTSRVHWIAEEPPAALVRDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTAVQAV
RALATGQFAVFYKGDECLGSGKILRLGPSAYTLQKGQRRAGMATESPSDSPEDGPGLSPL
L
Enzyme 12 Number of Residues 421
Enzyme 12 Molecular Weight 47744.3
Enzyme 12 Theoretical pI 8.12
Enzyme 12 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 12 General Function Involved in transferase activity
Enzyme 12 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 12 Pathways Not Available
Enzyme 12 Reactions Not Available
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 54633233 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID O75648 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name MTU1_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 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 12 GenBank Gene ID AB178028 Link Image
Enzyme 12 GeneCard ID TRMU Link Image
Enzyme 12 GenAtlas ID TRMU Link Image
Enzyme 12 HGNC ID HGNC:25481 Link Image
Enzyme 12 Chromosome Location 2
Enzyme 12 Locus 22q13
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 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 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5647
Enzyme 13 Name Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific
Enzyme 13 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 13 Gene Name NSD1
Enzyme 13 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 13 Number of Residues 2696
Enzyme 13 Molecular Weight 296649.3
Enzyme 13 Theoretical pI 8.08
Enzyme 13 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 13 General Function Involved in histone-lysine N-methyltransferase activity
Enzyme 13 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 13 Pathways
Enzyme 13 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 19923586 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q96L73 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name NSD1_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 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 13 GenBank Gene ID NM_022455.4 Link Image
Enzyme 13 GeneCard ID NSD1 Link Image
Enzyme 13 GenAtlas ID NSD1 Link Image
Enzyme 13 HGNC ID HGNC:14234 Link Image
Enzyme 13 Chromosome Location 5
Enzyme 13 Locus 5q35
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 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 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5648
Enzyme 14 Name Histone-lysine N-methyltransferase SETDB1
Enzyme 14 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 14 Gene Name SETDB1
Enzyme 14 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 14 Number of Residues 1291
Enzyme 14 Molecular Weight 143155.6
Enzyme 14 Theoretical pI 5.84
Enzyme 14 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 14 General Function Involved in DNA binding
Enzyme 14 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 14 Pathways
Enzyme 14 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 55960634 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID Q15047 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name SETB1_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 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 14 GenBank Gene ID AL590133 Link Image
Enzyme 14 GeneCard ID SETDB1 Link Image
Enzyme 14 GenAtlas ID SETDB1 Link Image
Enzyme 14 HGNC ID HGNC:10761 Link Image
Enzyme 14 Chromosome Location 1
Enzyme 14 Locus 1q21
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 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 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 5649
Enzyme 15 Name Protein-L-isoaspartate(D-aspartate) O-methyltransferase
Enzyme 15 Synonyms
  1. PIMT
  2. L-isoaspartyl protein carboxyl methyltransferase
  3. Protein L-isoaspartyl/D-aspartyl methyltransferase
  4. Protein-beta-aspartate methyltransferase
Enzyme 15 Gene Name PCMT1
Enzyme 15 Protein Sequence >Protein-L-isoaspartate(D-aspartate) O-methyltransferase
MAWKSGGASHSELIHNLRKNGIIKTDKVFEVMLATDRSHYAKCNPYMDSPQSIGFQATIS
APHMHAYALELLFDQLHEGAKALDVGSGSGILTACFARMVGCTGKVIGIDHIKELVDDSI
NNVRKDDPTLLSSGRVQLVVGDGRMGYAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLI
LPVGPAGGNQMLEQYDKLQDGSIKMKPLMGVIYVPLTDKEKQWSRWK
Enzyme 15 Number of Residues 227
Enzyme 15 Molecular Weight 24650.2
Enzyme 15 Theoretical pI 7.25
Enzyme 15 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 15 General Function Involved in protein-L-isoaspartate (D-aspartate) O-methyltransferase activity
Enzyme 15 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 15 Pathways Not Available
Enzyme 15 Reactions
  • S-adenosyl-L-methionine + protein L-isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester [RN:R04190]
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 158260471 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID P22061 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name PIMT_HUMAN Link Image
Enzyme 15 PDB ID 1KR5 Link Image
Enzyme 15 PDB File Show
Enzyme 15 3D Structure
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >684 bp
ATGGCCTGGAAATCCGGCGGCGCCAGCCACTCGGAGCTAATCCACAATCTCCGCAAAAAT
GGAATCATCAAGACAGATAAAGTATTTGAAGTGATGCTGGCTACAGACCGCTCCCACTAT
GCAAAATGTAACCCATACATGGATTCTCCACAATCAATAGGTTTCCAAGCAACAATCAGT
GCTCCACACATGCATGCATATGCGCTAGAACTTCTATTTGATCAGTTGCATGAAGGAGCT
AAAGCTCTTGATGTAGGATCTGGAAGTGGAATCCTTACTGCATGTTTTGCACGTATGGTT
GGATGTACTGGAAAAGTCATAGGAATTGATCACATTAAAGAGCTAGTAGATGACTCAGTA
AATAATGTCAGGAAGGACGATCCAACACTTCTGTCTTCAGGGAGAGTACAGCTTGTTGTG
GGGGATGGAAGAATGGGATATGCTGAAGAAGCCCCTTATGATGCCATTCATGTGGGAGCT
GCAGCCCCTGTTGTACCCCAGGCGCTAATAGATCAGTTAAAGCCCGGAGGAAGATTGATA
TTGCCTGTTGGTCCTGCAGGCGGAAACCAAATGTTGGAGCAGTATGACAAGCTACAAGAT
GGCAGCATCAAAATGAAGCCTCTGATGGGGGTGATATACGTGCCTTTAACAGATAAAGAA
AAGCAGTGGTCCAGGTGGAAGTGA
Enzyme 15 GenBank Gene ID AK289724 Link Image
Enzyme 15 GeneCard ID PCMT1 Link Image
Enzyme 15 GenAtlas ID PCMT1 Link Image
Enzyme 15 HGNC ID HGNC:8728 Link Image
Enzyme 15 Chromosome Location 6
Enzyme 15 Locus 6q24-q25
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 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 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 5651
Enzyme 16 Name Protein-S-isoprenylcysteine O-methyltransferase
Enzyme 16 Synonyms
  1. Isoprenylcysteine carboxylmethyltransferase
  2. Prenylated protein carboxyl methyltransferase
  3. PPMT
  4. Prenylcysteine carboxyl methyltransferase
  5. pcCMT
Enzyme 16 Gene Name ICMT
Enzyme 16 Protein Sequence >Protein-S-isoprenylcysteine O-methyltransferase
MAGCAARAPPGSEARLSLATFLLGASVLALPLLTRAGLQGRTGLALYVAGLNALLLLLYR
PPRYQIAIRACFLGFVFGCGTLLSFSQSSWSHFGWYMCSLSLFHYSEYLVTAVNNPKSLS
LDSFLLNHSLEYTVAALSSWLEFTLENIFWPELKQITWLSVTGLLMVVFGECLRKAAMFT
AGSNFNHVVQNEKSDTHTLVTSGVYAWFRHPSYVGWFYWSIGTQVMLCNPICGVSYALTV
WRFFRDRTEEEEISLIHFFGEEYLEYKKRVPTGLPFIKGVKVDL
Enzyme 16 Number of Residues 284
Enzyme 16 Molecular Weight 31937.8
Enzyme 16 Theoretical pI 8.05
Enzyme 16 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 16 General Function Involved in protein C-terminal S-isoprenylcysteine carboxyl O-methyltransferase activity
Enzyme 16 Specific Function Catalyzes the post-translational methylation of isoprenylated C-terminal cysteine residues
Enzyme 16 Pathways Not Available
Enzyme 16 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 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • 18-38 42-62 66-86 214-234
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 3135669 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID O60725 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name ICMT_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >855 bp
ATGGCGGGCTGCGCGGCGCGGGCTCCGCCGGGCTCTGAGGCGCGTCTCAGCCTCGCCACC
TTCCTGCTGGGCGCCTCGGTGCTCGCGCTGCCGCTGCTCACGCGCGCCGGCCTGCAGGGC
CGCACCGGGCTGGCGCTCTACGTGGCCGGGCTCAACGCGCTGCTGCTGCTGCTCTATCGG
CCGCCTCGCTACCAGATAGCCATCCGAGCTTGTTTCCTGGGGTTTGTGTTCGGCTGCGGC
ACGCTGCTAAGTTTTAGCCAGTCTTCTTGGAGTCACTTTGGCTGGTACATGTGCTCCCTG
TCATTGTTCCACTATTCTGAATACTTGGTGACAGCAGTCAATAATCCCAAAAGTCTGTCC
TTGGATTCCTTTCTCCTGAATCACAGCCTGGAGTATACAGTAGCTGCTCTTTCTTCTTGG
TTAGAGTTCACACTTGAAAATATCTTTTGGCCAGAACTGAAGCAGATTACCTGGCTCAGT
GTCACAGGGCTGCTGATGGTGGTCTTCGGAGAATGTCTGAGGAAGGCGGCCATGTTTACA
GCTGGCTCCAATTTCAACCACGTGGTACAGAATGAAAAATCAGATACACATACTCTGGTG
ACCAGTGGAGTGTACGCTTGGTTTCGGCATCCTTCTTACGTCGGGTGGTTTTACTGGAGT
ATTGGAACTCAGGTGATGCTGTGTAACCCCATCTGCGGCGTCAGCTATGCCCTGACAGTG
TGGCGATTCTTCCGCGATCGAACAGAAGAAGAAGAAATCTCACTAATTCACTTTTTTGGA
GAGGAGTACCTGGAGTATAAGAAGAGGGTGCCCACGGGCCTGCCTTTCATAAAGGGGGTC
AAGGTGGACCTGTGA
Enzyme 16 GenBank Gene ID AF064084 Link Image
Enzyme 16 GeneCard ID ICMT Link Image
Enzyme 16 GenAtlas ID ICMT Link Image
Enzyme 16 HGNC ID HGNC:5350 Link Image
Enzyme 16 Chromosome Location 1
Enzyme 16 Locus 1p36.21
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 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 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 5652
Enzyme 17 Name Indolethylamine N-methyltransferase
Enzyme 17 Synonyms
  1. Indolamine N-methyltransferase
  2. Aromatic alkylamine N-methyltransferase
  3. Amine N-methyltransferase
  4. Arylamine N-methyltransferase
Enzyme 17 Gene Name INMT
Enzyme 17 Protein Sequence >Indolethylamine N-methyltransferase
MKGGFTGGDEYQKHFLPRDYLATYYSFDGSPSPEAEMLKFNLECLHKTFGPGGLQGDTLI
DIGSGPTIYQVLAACDSFQDITLSDFTDRNREELEKWLKKEPGAYDWTPAVKFACELEGN
SGRWEEKEEKLRAAVKRVLKCDVHLGNPLAPAVLPLADCVLTLLAMECACCSLDAYRAAL
CNLASLLKPGGHLVTTVTLRLPSYMVGKREFSCVALEKEEVEQAVLDAGFDIEQLLHSPQ
SYSVTNAANNGVCFIVARKKPGP
Enzyme 17 Number of Residues 263
Enzyme 17 Molecular Weight 28890.8
Enzyme 17 Theoretical pI 4.92
Enzyme 17 GO Classification
Function
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
Component
Enzyme 17 General Function Involved in methyltransferase activity
Enzyme 17 Specific Function Catalyzes the N-methylation of tryptamine and structurally related compounds (Potential)
Enzyme 17 Pathways
Enzyme 17 Reactions
  • S-adenosyl-L-methionine + an amine = S-adenosyl-L-homocysteine + a methylated amine [RN:R02808]
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 66933018 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID O95050 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name INMT_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >792 bp
ATGAAGGGTGGCTTCACTGGGGGTGATGAGTACCAGAAGCACTTCCTGCCCAGGGACTAC
TTGGCTACTTACTACAGCTTCGATGGCAGCCCCTCACCCGAGGCCGAGATGCTGAAGTTT
AACTTGGAATGTCTCCACAAGACCTTCGGCCCTGGAGGCCTCCAAGGGGACACGCTGATT
GACATTGGCTCAGGTCCTACCATCTACCAAGTTCTTGCTGCCTGTGATTCCTTCCAAGAC
ATCACTCTCTCCGACTTTACCGACCGCAACCGGGAGGAGCTGGAAAAGTGGCTGAAGAAG
GAGCCGGGGGCCTATGACTGGACCCCAGCGGTGAAATTCGCCTGTGAGCTGGAAGGAAAC
AGCGGCCGATGGGAGGAGAAGGAGGAGAAGCTGCGGGCAGCGGTGAAGCGGGTGCTCAAG
TGCGATGTCCACCTGGGCAACCCGCTGGCCCCGGCTGTGTTGCCTCTCGCCGACTGTGTG
CTCACCCTGCTGGCCATGGAGTGTGCCTGCTGTAGCCTTGATGCCTACCGCGCTGCCCTG
TGCAACCTTGCCTCACTGCTCAAGCCGGGTGGCCACCTGGTGACCACTGTCACGCTTCGG
CTCCCGTCCTACATGGTGGGGAAGCGTGAATTTTCCTGCGTGGCCCTGGAGAAAGAGGAG
GTGGAGCAGGCTGTCCTGGATGCTGGCTTTGACATTGAACAGCTCCTACACAGTCCCCAG
AGCTACTCTGTCACCAATGCTGCCAACAATGGGGTCTGCTTCATTGTGGCTCGCAAGAAG
CCTGGGCCCTGA
Enzyme 17 GenBank Gene ID NM_006774.4 Link Image
Enzyme 17 GeneCard ID INMT Link Image
Enzyme 17 GenAtlas ID INMT Link Image
Enzyme 17 HGNC ID HGNC:6069 Link Image
Enzyme 17 Chromosome Location 7
Enzyme 17 Locus 7p15.1
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 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 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 5653
Enzyme 18 Name DNA (cytosine-5)-methyltransferase 3A
Enzyme 18 Synonyms
  1. Dnmt3a
  2. DNA methyltransferase HsaIIIA
  3. DNA MTase HsaIIIA
  4. M.HsaIIIA
Enzyme 18 Gene Name DNMT3A
Enzyme 18 Protein Sequence >DNA (cytosine-5)-methyltransferase 3A
MPAMPSSGPGDTSSSAAEREEDRKDGEEQEEPRGKEERQEPSTTARKVGRPGRKRKHPPV
ESGDTPKDPAVISKSPSMAQDSGASELLPNGDLEKRSEPQPEEGSPAGGQKGGAPAEGEG
AAETLPEASRAVENGCCTPKEGRGAPAEAGKEQKETNIESMKMEGSRGRLRGGLGWESSL
RQRPMPRLTFQAGDPYYISKRKRDEWLARWKREAEKKAKVIAGMNAVEENQGPGESQKVE
EASPPAVQQPTDPASPTVATTPEPVGSDAGDKNATKAGDDEPEYEDGRGFGIGELVWGKL
RGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYN
KQPMYRKAIYEVLQVASSRAGKLFPVCHDSDESDTAKAVEVQNKPMIEWALGGFQPSGPK
GLEPPEEEKNPYKEVYTDMWVEPEAAAYAPPPPAKKPRKSTAEKPKVKEIIDERTRERLV
YEVRQKCRNIEDICISCGSLNVTLEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTIC
CGGREVLMCGNNNCCRCFCVECVDLLVGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRRED
WPSRLQMFFANNHDQEFDPPKVYPPVPAEKRKPIRVLSLFDGIATGLLVLKDLGIQVDRY
IASEVCEDSITVGMVRHQGKIMYVGDVRSVTQKHIQEWGPFDLVIGGSPCNDLSIVNPAR
KGLYEGTGRLFFEFYRLLHDARPKEGDDRPFFWLFENVVAMGVSDKRDISRFLESNPVMI
DAKEVSAAHRARYFWGNLPGMNRPLASTVNDKLELQECLEHGRIAKFSKVRTITTRSNSI
KQGKDQHFPVFMNEKEDILWCTEMERVFGFPVHYTDVSNMSRLARQRLLGRSWSVPVIRH
LFAPLKEYFACV
Enzyme 18 Number of Residues 912
Enzyme 18 Molecular Weight 101857.6
Enzyme 18 Theoretical pI 6.52
Enzyme 18 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 18 General Function Involved in DNA binding
Enzyme 18 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 18 Pathways
Enzyme 18 Reactions
  • S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine [RN:R00380]
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 12746532 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q9Y6K1 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name DNM3A_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 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 18 GenBank Gene ID AF067972 Link Image
Enzyme 18 GeneCard ID DNMT3A Link Image
Enzyme 18 GenAtlas ID DNMT3A Link Image
Enzyme 18 HGNC ID HGNC:2978 Link Image
Enzyme 18 Chromosome Location 2
Enzyme 18 Locus 2p23
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 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 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 5654
Enzyme 19 Name Hexaprenyldihydroxybenzoate methyltransferase, mitochondrial
Enzyme 19 Synonyms
  1. 3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase
  2. DHHB methyltransferase
  3. DHHB-MT
  4. DHHB-MTase
  5. Dihydroxyhexaprenylbenzoate methyltransferase
Enzyme 19 Gene Name COQ3
Enzyme 19 Protein Sequence >Hexaprenyldihydroxybenzoate methyltransferase, mitochondrial
MWSGRKLGSSGGWFLRVLGPGGCNTKAARPLISSAVYVKNQLSGTLQIKPGVFNEYRTIW
FKSYRTIFSCLNRIKSFRYPWARLYSTSQTTVDSGEVKTFLALAHKWWDEQGVYAPLHSM
NDLRVPFIRDNLLKTIPNHQPGKPLLGMKILDVGCGGGLLTEPLGRLGASVIGIDPVDEN
IKTAQCHKSFDPVLDKRIEYRVCSLEEIVEETAETFDAVVASEVVEHVIDLETFLQCCCQ
VLKPGGSLFITTINKTQLSYALGIVFSEQIAGIVPKGTHTWEKFVSPETLESILESNGLS
VQTVVGMLYNPFSGYWHWSENTSLNYAAHAVKSRVQEHPASAEFVLKGETEELQANACTN
PAVHEKLKK
Enzyme 19 Number of Residues 369
Enzyme 19 Molecular Weight 40997.7
Enzyme 19 Theoretical pI 7.50
Enzyme 19 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 19 General Function Involved in methyltransferase activity
Enzyme 19 Specific Function S-adenosyl-L-methionine + 3-hexaprenyl-4,5- dihydroxybenzoate = S-adenosyl-L-homocysteine + 3-hexaprenyl-4- hydroxy-5-methoxybenzoate
Enzyme 19 Pathways
Enzyme 19 Reactions
  • S-adenosyl-L-methionine + 3-hexaprenyl-4,5-dihydroxybenzoate = S-adenosyl-L-homocysteine + 3-hexaprenyl-4-hydroxy-5-methoxybenzoate [RN:R04711]
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 118600965 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q9NZJ6 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name COQ3_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >1110 bp
ATGTGGAGTGGCCGTAAGCTGGGCTCCTCCGGGGGTTGGTTTTTAAGAGTGCTGGGGCCT
GGAGGCTGTAATACAAAAGCTGCGCGTCCCTTAATTTCCTCGGCGGTTTATGTGAAGAAC
CAGCTCAGTGGGACTCTACAGATTAAACCAGGGGTTTTCAATGAATACAGAACCATATGG
TTCAAATCCTACAGGACGATCTTTTCCTGTTTGAACAGAATAAAGAGTTTCAGGTACCCT
TGGGCGAGACTGTACAGTACTTCCCAAACCACTGTCGACAGCGGTGAGGTAAAAACCTTC
TTGGCCCTGGCTCACAAATGGTGGGATGAACAAGGAGTATATGCACCTCTTCATTCCATG
AATGACCTGAGGGTGCCATTTATTAGGGACAATCTTCTGAAAACAATTCCTAATCACCAG
CCAGGAAAACCTTTGTTGGGGATGAAGATTCTTGACGTTGGCTGTGGTGGTGGGCTGTTA
ACTGAACCTCTAGGGCGGCTTGGGGCTTCAGTTATTGGAATCGACCCTGTGGATGAGAAC
ATTAAAACAGCACAATGCCATAAATCATTTGATCCAGTCCTGGATAAGAGAATAGAGTAC
AGAGTGTGTTCCCTGGAAGAGATTGTGGAAGAGACTGCAGAAACATTTGATGCTGTTGTA
GCTTCTGAAGTTGTAGAACATGTGATTGATCTAGAAACATTTTTACAGTGCTGCTGTCAA
GTGTTAAAACCCGGTGGTTCTTTATTCATTACTACAATCAACAAAACACAACTTTCCTAT
GCCTTGGGAATTGTTTTTTCAGAGCAAATTGCAAGTATTGTACCAAAAGGTACTCATACA
TGGGAGAAGTTTGTTTCACCTGAAACACTAGAGAGCATTCTGGAATCAAATGGTCTGTCA
GTTCAAACAGTGGTAGGAATGCTCTATAACCCCTTCTCAGGTTACTGGCATTGGAGTGAA
AATACCAGCCTTAACTATGCAGCTTATGCTGTGAAATCCAGGGTCCAGGAACACCCAGCC
TCTGCTGAGTTTGTTTTAAAGGGAGAAACAGAAGAGCTCCAAGCTAATGCCTGCACCAAT
CCAGCTGTGCATGAAAAGCTGAAGAAATGA
Enzyme 19 GenBank Gene ID NM_017421.3 Link Image
Enzyme 19 GeneCard ID COQ3 Link Image
Enzyme 19 GenAtlas ID COQ3 Link Image
Enzyme 19 HGNC ID HGNC:18175 Link Image
Enzyme 19 Chromosome Location 6
Enzyme 19 Locus 6q16.2
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 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 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 5655
Enzyme 20 Name S-adenosylmethionine synthase isoform type-1
Enzyme 20 Synonyms
  1. AdoMet synthase 1
  2. Methionine adenosyltransferase 1
  3. MAT 1
  4. Methionine adenosyltransferase I/III
  5. MAT-I/III
Enzyme 20 Gene Name MAT1A
Enzyme 20 Protein Sequence >S-adenosylmethionine synthase isoform type-1
MNGPVDGLCDHSLSEGVFMFTSESVGEGHPDKICDQISDAVLDAHLKQDPNAKVACETVC
KTGMVLLCGEITSMAMVDYQRVVRDTIKHIGYDDSAKGFDFKTCNVLVALEQQSPDIAQC
VHLDRNEEDVGAGDQGLMFGYATDETEECMPLTIILAHKLNARMADLRRSGLLPWLRPDS
KTQVTVQYMQDNGAVIPVRIHTIVISVQHNEDITLEEMRRALKEQVIRAVVPAKYLDEDT
VYHLQPSGRFVIGGPQGDAGVTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARW
VAKSLVKAGLCRRVLVQVSYAIGVAEPLSISIFTYGTSQKTERELLDVVHKNFDLRPGVI
VRDLDLKKPIYQKTACYGHFGRSEFPWEVPRKLVF
Enzyme 20 Number of Residues 395
Enzyme 20 Molecular Weight 43647.6
Enzyme 20 Theoretical pI 6.24
Enzyme 20 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • methionine adenosyltransferase activity
  • nucleoside binding
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • cellular metabolic process
  • metabolic process
  • one-carbon metabolic process
Component
Enzyme 20 General Function Involved in methionine adenosyltransferase activity
Enzyme 20 Specific Function Catalyzes the formation of S-adenosylmethionine from methionine and ATP
Enzyme 20 Pathways
Enzyme 20 Reactions
  • ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine [RN:R00177]
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 55959182 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID Q00266 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name METK1_HUMAN Link Image
Enzyme 20 PDB ID 1O9T Link Image
Enzyme 20 PDB File Show
Enzyme 20 3D Structure
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >1188 bp
ATGAATGGACCGGTGGATGGCTTGTGTGACCACTCTCTAAGTGAAGGAGTCTTCATGTTC
ACATCGGAGTCTGTGGGAGAGGGACACCCGGATAAGATCTGTGACCAGATCAGTGATGCA
GTGCTGGATGCCCATCTCAAGCAAGACCCCAATGCCAAGGTGGCCTGTGAGACAGTGTGC
AAGACCGGCATGGTGCTGCTGTGTGGTGAGATCACCTCAATGGCCATGGTGGACTACCAG
CGGGTGGTGAGGGACACCATCAAGCACATCGGCTACGATGACTCAGCCAAGGGCTTTGAC
TTCAAGACTTGCAACGTGCTGGTGGCTTTGGAGCAGCAATCCCCAGATATTGCCCAGTGC
GTCCATCTGGACAGAAATGAGGAGGATGTGGGGGCAGGAGATCAGGGTTTGATGTTCGGC
TATGCTACCGACGAGACAGAGGAGTGCATGCCCCTCACCATCATCCTTGCTCACAAGCTC
AACGCCCGGATGGCAGACCTCAGGCGCTCCGGCCTCCTCCCCTGGCTGCGGCCTGACTCT
AAGACTCAGGTGACAGTTCAGTACATGCAGGACAATGGCGCAGTCATCCCTGTGCGCATC
CACACCATCGTCATCTCTGTGCAGCACAACGAAGACATCACGCTGGAGGAGATGCGCAGG
GCCCTGAAGGAGCAAGTCATCAGGGCCGTGGTGCCGGCCAAGTACCTGGACGAAGACACC
GTCTACCACCTGCAGCCCAGTGGGCGGTTTGTCATCGGAGGTCCCCAGGGGGATGCGGGT
GTCACTGGCCGTAAGATTATTGTGGACACCTATGGCGGCTGGGGGGCTCATGGTGGTGGG
GCCTTCTCTGGGAAGGACTACACCAAGGTAGACCGCTCAGCTGCATATGCTGCCCGCTGG
GTGGCCAAGTCTCTGGTGAAAGCAGGGCTCTGCCGGAGAGTGCTTGTCCAGGTTTCCTAT
GCCATTGGTGTGGCCGAGCCGCTGTCCATTTCCATCTTCACCTACGGAACCTCTCAGAAG
ACAGAGCGAGAGCTGCTGGATGTGGTGCATAAGAACTTCGACCTCCGGCCGGGCGTCATT
GTCAGGGATTTGGACTTGAAGAAGCCCATCTACCAGAAGACAGCATGCTACGGCCATTTC
GGAAGAAGCGAGTTCCCATGGGAGGTTCCCAGGAAGCTTGTATTTTAG
Enzyme 20 GenBank Gene ID AL359195 Link Image
Enzyme 20 GeneCard ID MAT1A Link Image
Enzyme 20 GenAtlas ID MAT1A Link Image
Enzyme 20 HGNC ID HGNC:6903 Link Image
Enzyme 20 Chromosome Location 1
Enzyme 20 Locus 10q22
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Alvarez L, Corrales F, Martin-Duce A, Mato JM: Characterization of a full-length cDNA encoding human liver S-adenosylmethionine synthetase: tissue-specific gene expression and mRNA levels in hepatopathies. Biochem J. 1993 Jul 15;293 ( Pt 2):481-6. [PubMed Link Image]
  2. Horikawa S, Tsukada K: Molecular cloning and nucleotide sequence of cDNA encoding the human liver S-adenosylmethionine synthetase. Biochem Int. 1991 Sep;25(1):81-90. [PubMed Link Image]
  3. 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]
  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. Ubagai T, Lei KJ, Huang S, Mudd SH, Levy HL, Chou JY: Molecular mechanisms of an inborn error of methionine pathway. Methionine adenosyltransferase deficiency. J Clin Invest. 1995 Oct;96(4):1943-7. [PubMed Link Image]
  6. Chamberlin ME, Ubagai T, Mudd SH, Wilson WG, Leonard JV, Chou JY: Demyelination of the brain is associated with methionine adenosyltransferase I/III deficiency. J Clin Invest. 1996 Aug 15;98(4):1021-7. [PubMed Link Image]
  7. Chamberlin ME, Ubagai T, Mudd SH, Levy HL, Chou JY: Dominant inheritance of isolated hypermethioninemia is associated with a mutation in the human methionine adenosyltransferase 1A gene. Am J Hum Genet. 1997 Mar;60(3):540-6. [PubMed Link Image]
  8. Chamberlin ME, Ubagai T, Mudd SH, Thomas J, Pao VY, Nguyen TK, Levy HL, Greene C, Freehauf C, Chou JY: Methionine adenosyltransferase I/III deficiency: novel mutations and clinical variations. Am J Hum Genet. 2000 Feb;66(2):347-55. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 5656
Enzyme 21 Name Histone-lysine N-methyltransferase, H3 lysine-9 specific 3
Enzyme 21 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 21 Gene Name EHMT2
Enzyme 21 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 21 Number of Residues 1210
Enzyme 21 Molecular Weight 132369.2
Enzyme 21 Theoretical pI 5.14
Enzyme 21 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 21 General Function Involved in zinc ion binding
Enzyme 21 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 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 15917538 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q96KQ7 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name EHMT2_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 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 21 GenBank Gene ID AJ315532 Link Image
Enzyme 21 GeneCard ID EHMT2 Link Image
Enzyme 21 GenAtlas ID EHMT2 Link Image
Enzyme 21 HGNC ID HGNC:14129 Link Image
Enzyme 21 Chromosome Location 6
Enzyme 21 Locus 6p21.31
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 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 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 5657
Enzyme 22 Name S-adenosylmethionine decarboxylase proenzyme
Enzyme 22 Synonyms
  1. AdoMetDC
  2. SAMDC
  3. S-adenosylmethionine decarboxylase alpha chain
  4. S-adenosylmethionine decarboxylase beta chain
Enzyme 22 Gene Name AMD1
Enzyme 22 Protein Sequence >S-adenosylmethionine decarboxylase proenzyme
MEAAHFFEGTEKLLEVWFSRQQPDANQGSGDLRTIPRSEWDILLKDVQCSIISVTKTDKQ
EAYVLSESSMFVSKRRFILKTCGTTLLLKALVPLLKLARDYSGFDSIQSFFYSRKNFMKP
SHQGYPHRNFQEEIEFLNAIFPNGAAYCMGRMNSDCWYLYTLDFPESRVISQPDQTLEIL
MSELDPAVMDQFYMKDGVTAKDVTRESGIRDLIPGSVIDATMFNPCGYSMNGMKSDGTYW
TIHITPEPEFSYVSFETNLSQTSYDDLIRKVVEVFKPGKFVTTLFVNQSSKCRTVLASPQ
KIEGFKRLDCQSAMFNDYNFVFTSFAKKQQQQQS
Enzyme 22 Number of Residues 334
Enzyme 22 Molecular Weight 38339.3
Enzyme 22 Theoretical pI 5.78
Enzyme 22 GO Classification
Function
  • adenosylmethionine decarboxylase activity
  • carbon-carbon lyase activity
  • carboxy-lyase activity
  • catalytic activity
  • lyase activity
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid derivative metabolic process
  • cellular biogenic amine metabolic process
  • cellular metabolic process
  • metabolic process
  • polyamine biosynthetic process
  • polyamine metabolic process
  • spermidine biosynthetic process
  • spermine biosynthetic process
Component
Enzyme 22 General Function Involved in adenosylmethionine decarboxylase activity
Enzyme 22 Specific Function S-adenosyl-L-methionine = (5-deoxy-5- adenosyl)(3-aminopropyl)-methylsulfonium salt + CO(2)
Enzyme 22 Pathways
Enzyme 22 Reactions
  • S-adenosyl-L-methionine = (5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2 [RN:R00178]
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 55664717 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID P17707 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name DCAM_HUMAN Link Image
Enzyme 22 PDB ID 1MSV Link Image
Enzyme 22 PDB File Show
Enzyme 22 3D Structure
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >1005 bp
ATGGAAGCTGCACATTTTTTCGAAGGGACCGAGAAGCTGCTGGAGGTTTGGTTCTCCCGG
CAGCAGCCCGACGCAAACCAAGGATCTGGGGATCTTCGCACTATCCCAAGATCTGAGTGG
GACATACTTTTGAAGGATGTGCAATGTTCAATCATAAGTGTGACAAAAACTGACAAGCAG
GAAGCTTATGTACTCAGTGAGAGTAGCATGTTTGTCTCCAAGAGACGTTTCATTTTGAAG
ACATGTGGTACCACCCTCTTGCTGAAAGCACTGGTTCCCCTGTTGAAGCTTGCTAGGGAT
TACAGTGGGTTTGACTCAATTCAAAGCTTCTTTTATTCTCGTAAGAATTTCATGAAGCCT
TCTCACCAAGGGTACCCACACCGGAATTTCCAGGAAGAAATAGAGTTTCTTAATGCAATT
TTCCCAAATGGAGCAGCATATTGTATGGGACGTATGAATTCTGACTGTTGGTACTTATAT
ACTCTGGATTTCCCAGAGAGTCGGGTAATCAGTCAGCCAGATCAAACCTTGGAAATTCTG
ATGAGTGAGCTTGACCCAGCAGTTATGGACCAGTTCTACATGAAAGATGGTGTTACTGCA
AAGGATGTCACTCGTGAGAGTGGAATTCGTGACCTGATACCAGGTTCTGTCATTGATGCC
ACAATGTTCAATCCTTGTGGGTATTCGATGAATGGAATGAAATCGGATGGAACTTATTGG
ACTATTCACATCACTCCAGAACCAGAATTTTCTTATGTTAGCTTTGAAACAAACTTAAGT
CAGACCTCCTATGATGACCTGATCAGGAAAGTTGTAGAAGTCTTCAAGCCAGGAAAATTT
GTGACCACCTTGTTTGTTAATCAGAGTTCTAAATGTCGCACAGTGCTTGCTTCGCCCCAG
AAGATTGAAGGTTTTAAGCGTCTTGATTGCCAGAGTGCTATGTTCAATGATTACAATTTT
GTTTTTACCAGTTTTGCTAAGAAGCAGCAACAACAGCAGAGTTGA
Enzyme 22 GenBank Gene ID AL357515 Link Image
Enzyme 22 GeneCard ID AMD1 Link Image
Enzyme 22 GenAtlas ID AMD1 Link Image
Enzyme 22 HGNC ID HGNC:457 Link Image
Enzyme 22 Chromosome Location 6
Enzyme 22 Locus 6q21
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Pajunen A, Crozat A, Janne OA, Ihalainen R, Laitinen PH, Stanley B, Madhubala R, Pegg AE: Structure and regulation of mammalian S-adenosylmethionine decarboxylase. J Biol Chem. 1988 Nov 15;263(32):17040-9. [PubMed Link Image]
  2. 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]
  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. Stanley BA, Pegg AE: Amino acid residues necessary for putrescine stimulation of human S-adenosylmethionine decarboxylase proenzyme processing and catalytic activity. J Biol Chem. 1991 Oct 5;266(28):18502-6. [PubMed Link Image]
  5. Xiong H, Pegg AE: Mechanistic studies of the processing of human S-adenosylmethionine decarboxylase proenzyme. Isolation of an ester intermediate. J Biol Chem. 1999 Dec 3;274(49):35059-66. [PubMed Link Image]
  6. Xiong H, Stanley BA, Pegg AE: Role of cysteine-82 in the catalytic mechanism of human S-adenosylmethionine decarboxylase. Biochemistry. 1999 Feb 23;38(8):2462-70. [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. Ekstrom JL, Mathews II, Stanley BA, Pegg AE, Ealick SE: The crystal structure of human S-adenosylmethionine decarboxylase at 2.25 A resolution reveals a novel fold. Structure. 1999 May;7(5):583-95. [PubMed Link Image]
  9. Tolbert WD, Ekstrom JL, Mathews II, Secrist JA 3rd, Kapoor P, Pegg AE, Ealick SE: The structural basis for substrate specificity and inhibition of human S-adenosylmethionine decarboxylase. Biochemistry. 2001 Aug 14;40(32):9484-94. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 5658
Enzyme 23 Name Methionine synthase reductase
Enzyme 23 Synonyms
  1. MSR
Enzyme 23 Gene Name MTRR
Enzyme 23 Protein Sequence >Methionine synthase reductase
MGAASVRAGARLVEVALCSFTVTCLEVMRRFLLLYATQQGQAKAIAEEICEQAVVHGFSA
DLHCISESDKYDLKTETAPLVVVVSTTGTGDPPDTARKFVKEIQNQTLPVDFFAHLRYGL
LGLGDSEYTYFCNGGKIIDKRLQELGARHFYDTGHADDCVGLELVVEPWIAGLWPALRKH
FRSSRGQEEISGALPVASPASSRTDLVKSELLHIESQVELLRFDDSGRKDSEVLKQNAVN
SNQSNVVIEDFESSLTRSVPPLSQASLNIPGLPPEYLQVHLQESLGQEESQVSVTSADPV
FQVPISKAVQLTTNDAIKTTLLVELDISNTDFSYQPGDAFSVICPNSDSEVQSLLQRLQL
EDKREHCVLLKIKADTKKKGATLPQHIPAGCSLQFIFTWCLEIRAIPKKAFLRALVDYTS
DSAEKRRLQELCSKQGAADYSRFVRDACACLLDLLLAFPSCQPPLSLLLEHLPKLQPRPY
SCASSSLFHPGKLHFVFNIVEFLSTATTEVLRKGVCTGWLALLVASVLQPNIHASHEDSG
KALAPKISISPRTTNSFHLPDDPSIPIIMVGPGTGIAPFIGFLQHREKLQEQHPDGNFGA
MWLFFGCRHKDRDYLFRKELRHFLKHGILTHLKVSFSRDAPVGEEEAPAKYVQDNIQLHG
QQVARILLQENGHIYVCGDAKNMAKDVHDALVQIISKEVGVEKLEAMKTLATLKEEKRYL
QDIWS
Enzyme 23 Number of Residues 725
Enzyme 23 Molecular Weight 80409.2
Enzyme 23 Theoretical pI 6.47
Enzyme 23 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 23 General Function Involved in oxidoreductase activity
Enzyme 23 Specific Function Involved in the reductive regeneration of cob(I)alamin cofactor required for the maintenance of methionine synthase in a functional state
Enzyme 23 Pathways Not Available
Enzyme 23 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 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • None
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 6561339 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID Q9UBK8 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name MTRR_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 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 23 GenBank Gene ID AF121214 Link Image
Enzyme 23 GeneCard ID MTRR Link Image
Enzyme 23 GenAtlas ID MTRR Link Image
Enzyme 23 HGNC ID HGNC:7473 Link Image
Enzyme 23 Chromosome Location 5
Enzyme 23 Locus 5p15.31
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 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 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 5659
Enzyme 24 Name Histone-lysine N-methyltransferase SUV39H1
Enzyme 24 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 24 Gene Name SUV39H1
Enzyme 24 Protein Sequence >Histone-lysine N-methyltransferase SUV39H1
MAENLKGCSVCCKSSWNQLQDLCRLAKLSCPALGISKRNLYDFEVEYLCDYKKIREQEYY
LVKWRGYPDSESTWEPRQNLKCVRILKQFHKDLERELLRRHHRSKTPRHLDPSLANYLVQ
KAKQRRALRRWEQELNAKRSHLGRITVENEVDLDGPPRAFVYINEYRVGEGITLNQVAVG
CECQDCLWAPTGGCCPGASLHKFAYNDQGQVRLRAGLPIYECNSRCRCGYDCPNRVVQKG
IRYDLCIFRTDDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFD
LDYVEDVYTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIRAGEE
LTFDYNMQVDPVDMESTRMDSNFGLAGLPGSPKKRVRIECKCGTESCRKYLF
Enzyme 24 Number of Residues 412
Enzyme 24 Molecular Weight 47907.1
Enzyme 24 Theoretical pI 8.07
Enzyme 24 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 24 General Function Involved in chromatin binding
Enzyme 24 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 24 Pathways
Enzyme 24 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein Not Available
Enzyme 24 UniProtKB/Swiss-Prot ID O43463 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name SUV91_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 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 24 GenBank Gene ID AF019968 Link Image
Enzyme 24 GeneCard ID SUV39H1 Link Image
Enzyme 24 GenAtlas ID SUV39H1 Link Image
Enzyme 24 HGNC ID HGNC:11479 Link Image
Enzyme 24 Chromosome Location Not Available
Enzyme 24 Locus Not Available
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 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 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 5660
Enzyme 25 Name Nicotinamide N-methyltransferase
Enzyme 25 Synonyms Not Available
Enzyme 25 Gene Name NNMT
Enzyme 25 Protein Sequence >Nicotinamide N-methyltransferase
MESGFTSKDTYLSHFNPRDYLEKYYKFGSRHSAESQILKHLLKNLFKIFCLDGVKGDLLI
DIGSGPTIYQLLSACESFKEIVVTDYSDQNLQELEKWLKKEPEAFDWSPVVTYVCDLEGN
RVKGPEKEEKLRQAVKQVLKCDVTQSQPLGAVPLPPADCVLSTLCLDAACPDLPTYCRAL
RNLGSLLKPGGFLVIMDALKSSYYMIGEQKFSSLPLGREAVEAAVKEAGYTIEWFEVISQ
SYSSTMANNEGLFSLVARKLSRPL
Enzyme 25 Number of Residues 264
Enzyme 25 Molecular Weight 29573.7
Enzyme 25 Theoretical pI 5.45
Enzyme 25 GO Classification
Function
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
Component
Enzyme 25 General Function Involved in methyltransferase activity
Enzyme 25 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 25 Pathways
  • Nicotinate and Nicotinamide Metabolism (map00760 Link Image)
Enzyme 25 Reactions
  • S-adenosyl-L-methionine + nicotinamide = S-adenosyl-L-homocysteine + 1-methylnicotinamide [RN:R01269]
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 494989 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID P40261 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name NNMT_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >795 bp
ATGGAATCAGGCTTCACCTCCAAGGACACCTATCTAAGCCATTTTAACCCTCGGGATTAC
CTAGAAAAATATTACAAGTTTGGTTCTAGGCACTCTGCAGAAAGCCAGATTCTTAAGCAC
CTTCTGAAAAATCTTTTCAAGATATTCTGCCTAGACGGTGTGAAGGGAGACCTGCTGATT
GACATCGGCTCTGGCCCCACTATCTATCAGCTCCTCTCTGCTTGTGAATCCTTTAAGGAG
ATCGTCGTCACTGACTACTCAGACCAGAACCTGCAGGAGCTGGAGAAGTGGCTGAAGAAA
GAGCCAGAGGCCTTTGACTGGTCCCCAGTGGTGACCTATGTGTGTGATCTTGAAGGGAAC
AGAGTCAAGGGTCCAGAGAAGGAGGAGAAGTTGAGACAGGCGGTCAAGCAGGTGCTGAAG
TGTGATGTGACTCAGAGCCAGCCACTGGGGGCCGTCCCCTTACCCCCGGCTGACTGCGTG
CTCAGCACACTGTGTCTGGATGCCGCCTGCCCAGACCTCCCCACCTACTGCAGGGCGCTC
AGGAACCTCGGCAGCCTACTGAAGCCAGGGGGCTTCCTGGTGATCATGGATGCGCTCAAG
AGCAGCTACTACATGATTGGTGAGCAGAAGTTCTCCAGCCTCCCCCTGGGCCGGGAGGCA
GTAGAGGCTGCTGTGAAAGAGGCTGGCTACACAATCGAATGGTTTGAGGTGATCTCGCAA
AGTTATTCTTCCACCATGGCCAACAACGAAGGACTTTTCTCCCTGGTGGCGAGGAAGCTG
AGCAGACCCCTGTGA
Enzyme 25 GenBank Gene ID U08021 Link Image
Enzyme 25 GeneCard ID NNMT Link Image
Enzyme 25 GenAtlas ID NNMT Link Image
Enzyme 25 HGNC ID HGNC:7861 Link Image
Enzyme 25 Chromosome Location 1
Enzyme 25 Locus 11q23.1
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 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 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 5661
Enzyme 26 Name Histone-lysine N-methyltransferase SUV39H2
Enzyme 26 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 26 Gene Name SUV39H2
Enzyme 26 Protein Sequence >Histone-lysine N-methyltransferase SUV39H2
MAAVGAEARGAWCVPCLVSLDTLQELCRKEKLTCKSIGITKRNLNNYEVEYLCDYKVVKD
MEYYLVKWKGWPDSTNTWEPLQNLKCPLLLQQFSNDKHNYLSQVKKGKAITPKDNNKTLK
PAIAEYIVKKAKQRIALQRWQDELNRRKNHKGMIFVENTVDLEGPPSDFYYINEYKPAPG
ISLVNEATFGCSCTDCFFQKCCPAEAGVLLAYNKNQQIKIPPGTPIYECNSRCQCGPDCP
NRIVQKGTQYSLCIFRTSNGRGWGVKTLVKIKRMSFVMEYVGEVITSEEAERRGQFYDNK
GITYLFDLDYESDEFTVDAARYGNVSHFVNHSCDPNLQVFNVFIDNLDTRLPRIALFSTR
TINAGEELTFDYQMKGSGDISSDSIDHSPAKKRVRTVCKCGAVTCRGYLN
Enzyme 26 Number of Residues 410
Enzyme 26 Molecular Weight 46682.0
Enzyme 26 Theoretical pI 8.27
Enzyme 26 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 26 General Function Involved in chromatin binding
Enzyme 26 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 26 Pathways
Enzyme 26 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 301171588 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID Q9H5I1 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name SUV92_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 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 26 GenBank Gene ID NM_001193424.1 Link Image
Enzyme 26 GeneCard ID SUV39H2 Link Image
Enzyme 26 GenAtlas ID SUV39H2 Link Image
Enzyme 26 HGNC ID HGNC:17287 Link Image
Enzyme 26 Chromosome Location 1
Enzyme 26 Locus 10p13
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 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 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 5662
Enzyme 27 Name Histone-lysine N-methyltransferase, H3 lysine-9 specific 5
Enzyme 27 Synonyms
  1. Euchromatic histone-lysine N-methyltransferase 1
  2. Eu-HMTase1
  3. G9a-like protein 1
  4. GLP1
  5. Histone H3-K9 methyltransferase 5
  6. H3-K9-HMTase 5
  7. Lysine N-methyltransferase 1D
Enzyme 27 Gene Name EHMT1
Enzyme 27 Protein Sequence >Histone-lysine N-methyltransferase, H3 lysine-9 specific 5
MAADEGSAEKQAGEAHMAADGETNGSCENSDASSHANAAKHTQDSARVNPQDGTNTLTRI
AENGVSERDSEAAKQNHVTADDFVQTSVIGSNGYILNKPALQAQPLRTTSTLASSLPGHA
AKTLPGGAGKGRTPSAFPQTPAAPPATLGEGSADTEDRKLPAPGADVKVHRARKTMPKSV
VGLHAASKDPREVREARDHKEPKEEINKNISDFGRQQLLPPFPSLHQSLPQNQCYMATTK
SQTACLPFVLAAAVSRKKKRRMGTYSLVPKKKTKVLKQRTVIEMFKSITHSTVGSKGEKD
LGASSLHVNGESLEMDSDEDDSEELEEDDGHGAEQAAAFPTEDSRTSKESMSEADRAQKM
DGESEEEQESVDTGEEEEGGDESDLSSESSIKKKFLKRKGKTDSPWIKPARKRRRRSRKK
PSGALGSESYKSSAGSAEQTAPGDSTGYMEVSLDSLDLRVKGILSSQAEGLANGPDVLET
DGLQEVPLCSCRMETPKSREITTLANNQCMATESVDHELGRCTNSVVKYELMRPSNKAPL
LVLCEDHRGRMVKHQCCPGCGYFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCG
EESSKAKEVTIAKADTTSTVTPVPGQEKGSALEGRADTTTGSAAGPPLSEDDKLQGAASH
VPEGFDPTGPAGLGRPTPGLSQGPGKETLESALIALDSEKPKKLRFHPKQLYFSARQGEL
QKVLLMLVDGIDPNFKMEHQNKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLM
EAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQMDVNCQDD
GGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCD
LHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLNSQVWSALQM
SKALQDSAPDRPSPVERIVSRDIARGYERIPIPCVNAVDSEPCPSNYKYVSQNCVTSPMN
IDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSC
WRNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREED
SYLFDLDNKDGEVYCIDARFYGNVSRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRL
IEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHSSAALAQRQASAAQEAQEDGLPDTSS
AAAADPL
Enzyme 27 Number of Residues 1267
Enzyme 27 Molecular Weight 138252.4
Enzyme 27 Theoretical pI 5.78
Enzyme 27 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 27 General Function Involved in zinc ion binding
Enzyme 27 Specific Function Histone methyltransferase. Methylates 'Lys-9' 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. During G0 phase, it probably contributes to silencing of MYC- and E2F-responsive genes, suggesting a role in G0/G1 transition in cell cycle
Enzyme 27 Pathways
Enzyme 27 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 224465233 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID Q9H9B1 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name EHMT1_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >3897 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
ATGGCTACAGAGAGCGTGGACCATGAATTGGGCCGGTGCACAAACAGCGTGGTCAAGTAT
GAGCTGATGCGCCCCTCCAACAAGGCCCCGCTCCTCGTGCTGTGTGAAGACCACCGGGGC
CGCATGGTGAAGCACCAGTGCTGTCCTGGCTGTGGCTACTTCTGCACAGCGGGTAATTTT
ATGGAGTGTCAGCCCGAGAGCAGCATCTCTCACCGTTTCCACAAAGACTGTGCCTCTCGA
GTCAATAACGCCAGCTATTGTCCCCACTGTGGGGAGGAGAGCTCCAAGGCCAAAGAGGTG
ACGATAGCTAAAGCAGACACCACCTCGACCGTGACACCAGTCCCCGGGCAGGAGAAGGGC
TCGGCCCTGGAGGGCAGGGCCGACACCACAACGGGCAGTGCTGCCGGGCCACCACTCTCG
GAGGACGACAAGCTGCAGGGTGCAGCCTCCCACGTGCCCGAGGGCTTTGATCCAACGGGA
CCTGCTGGGCTTGGGAGGCCAACTCCCGGCCTTTCCCAGGGACCAGGGAAGGAAACCTTG
GAGAGCGCTCTCATCGCCCTCGACTCGGAAAAACCCAAGAAGCTTCGCTTCCACCCAAAG
CAGCTGTACTTCTCCGCCAGGCAAGGGGAGCTTCAGAAGGTGCTCCTCATGCTGGTGGAC
GGAATTGACCCCAACTTCAAAATGGAGCACCAGAATAAGCGCTCTCCACTGCACGCCGCG
GCAGAGGCTGGACACGTGGACATCTGCCACATGCTGGTTCAGGCGGGCGCTAATATTGAC
ACCTGCTCAGAAGACCAGAGGACCCCGTTGATGGAAGCAGCCGAAAACAACCATCTGGAA
GCAGTGAAGTACCTCATCAAGGCTGGGGCCCTGGTGGATCCCAAGGACGCAGAGGGCTCT
ACGTGTTTGCACCTGGCTGCCAAGAAAGGCCACTACGAAGTGGTCCAGTACCTGCTTTCA
AATGGACAGATGGACGTCAACTGTCAGGATGACGGAGGCTGGACACCCATGATCTGGGCC
ACAGAGTACAAGCACGTGGACCTCGTGAAGCTGCTGCTGTCCAAGGGCTCTGACATCAAC
ATCCGAGACAACGAGGAGAACATTTGCCTGCACTGGGCGGCGTTCTCCGGCTGCGTGGAC
ATAGCCGAGATCCTGCTGGCTGCCAAGTGCGACCTCCACGCCGTGAACATCCACGGAGAC
TCGCCACTGCACATTGCCGCCCGGGAGAACCGCTACGACTGTGTCGTCCTCTTTCTTTCT
CGGGATTCAGATGTCACCTTAAAGAACAAGGAAGGAGAGACGCCCCTGCAGTGTGCGAGC
CTCAACTCTCAGGTGTGGAGCGCTCTGCAGATGAGCAAGGCTCTGCAGGACTCGGCCCCC
GACAGGCCCAGCCCCGTGGAGAGGATAGTGAGCAGGGACATCGCTCGAGGCTACGAGCGC
ATCCCCATCCCCTGTGTCAACGCCGTGGACAGCGAGCCATGCCCCAGCAACTACAAGTAC
GTCTCTCAGAACTGCGTGACGTCCCCCATGAACATCGACAGAAATATCACTCATCTGCAG
TACTGCGTGTGCATCGACGACTGCTCCTCCAGCAACTGCATGTGCGGCCAGCTCAGCATG
CGCTGCTGGTACGACAAGGATGGCCGGCTCCTGCCAGAGTTCAACATGGCGGAGCCTCCC
TTGATCTTCGAATGCAACCACGCGTGCTCCTGCTGGAGGAACTGCCGAAATCGCGTCGTA
CAGAATGGTCTCAGGGCAAGGCTGCAGCTCTACCGGACGCGGGACATGGGCTGGGGCGTG
CGGTCCCTGCAGGACATCCCACCAGGCACCTTTGTCTGCGAGTATGTTGGGGAGCTGATT
TCAGACTCAGAAGCCGACGTTCGAGAGGAAGATTCTTACCTCTTTGATCTCGACAATAAG
GACGGGGAGGTTTACTGCATCGACGCGCGGTTCTACGGGAACGTCAGCCGGTTCATCAAC
CACCACTGCGAGCCCAACCTGGTGCCCGTGCGCGTGTTCATGGCCCACCAGGACCTGCGG
TTCCCCCGGATCGCCTTCTTCAGCACCCGCCTGATCGAGGCCGGCGAGCAGCTCGGGTTT
GACTATGGAGAGCGCTTCTGGGACATCAAAGGCAAGCTCTTCAGCTGCCGCTGCGGCTCC
CCCAAGTGCCGGCACTCGAGCGCGGCCCTGGCCCAGCGTCAGGCCAGCGCGGCCCAGGAG
GCCCAGGAGGACGGCTTGCCCGACACCAGCTCCGCGGCTGCCGCCGACCCCCTATGA
Enzyme 27 GenBank Gene ID NM_024757 Link Image
Enzyme 27 GeneCard ID EHMT1 Link Image
Enzyme 27 GenAtlas ID EHMT1 Link Image
Enzyme 27 HGNC ID HGNC:24650 Link Image
Enzyme 27 Chromosome Location 9
Enzyme 27 Locus 9q34.3
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. 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]
  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. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  4. 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]
  5. 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]
  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. 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]
  8. Kleefstra T, Brunner HG, Amiel J, Oudakker AR, Nillesen WM, Magee A, Genevieve D, Cormier-Daire V, van Esch H, Fryns JP, Hamel BC, Sistermans EA, de Vries BB, van Bokhoven H: Loss-of-function mutations in euchromatin histone methyl transferase 1 (EHMT1) cause the 9q34 subtelomeric deletion syndrome. Am J Hum Genet. 2006 Aug;79(2):370-7. Epub 2006 Jun 13. [PubMed Link Image]
  9. 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]
  10. 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]
  11. 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 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 5663
Enzyme 28 Name Guanidinoacetate N-methyltransferase
Enzyme 28 Synonyms Not Available
Enzyme 28 Gene Name GAMT
Enzyme 28 Protein Sequence >Guanidinoacetate N-methyltransferase
MSAPSATPIFAPGENCSPAWGAAPAAYDAADTHLRILGKPVMERWETPYMHALAAAASSK
GGRVLEVGFGMAIAASKVQEAPIDEHWIIECNDGVFQRLRDWAPRQTHKVIPLKGLWEDV
APTLPDGHFDGILYDTYPLSEETWHTHQFNFIKNHAFRLLKPGGVLTYCNLTSWGELMKS
KYSDITIMFEETQVPALLEAGFRRENIRTEVMALVPPADCRYYAFPQMITPLVTKG
Enzyme 28 Number of Residues 236
Enzyme 28 Molecular Weight 26317.9
Enzyme 28 Theoretical pI 6.09
Enzyme 28 GO Classification Not Available
Enzyme 28 General Function Involved in guanidinoacetate N-methyltransferase activity
Enzyme 28 Specific Function S-adenosyl-L-methionine + guanidinoacetate = S-adenosyl-L-homocysteine + creatine
Enzyme 28 Pathways
  • Arginine and Proline Metabolism (map00330 Link Image)
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
Enzyme 28 Reactions
  • S-adenosyl-L-methionine + guanidinoacetate = S-adenosyl-L-homocysteine + creatine [RN:R01883]
Enzyme 28 Pfam Domain Function Not Available
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 3342733 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID Q14353 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name GAMT_HUMAN Link Image
Enzyme 28 PDB ID 1XCL Link Image
Enzyme 28 PDB File Show
Enzyme 28 3D Structure
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >711 bp
ATGAGCGCCCCCAGCGCGACCCCCATCTTCGCGCCCGGCGAGAACTGCAGCCCCGCGTGG
GGGGCGGCGCCCGCGGCCTACGACGCAGCGGACACGCACCTGCGCATCCTGGGCAAGCCG
GTGATGGAGCGCTGGGAGACCCCCTATATGCACGCGCTGGCCGCCGCCGCCTCCTCCAAA
GGGGGCCGGGTCCTGGAGGTGGGCTTTGGCATGGCCATCGCAGCGTCAAAGGTGCAGGAG
GCGCCCATTGATGAGCATTGGATCATCGAGTGCAATGACGGCGTCTTCCAGCGGCTCCGG
GACTGGGCCCCACGGCAGACACACAAGGTCATCCCCTTGAAAGGCCTGTGGGAGGATGTG
GCACCCACCCTGCCTGACGGTCACTTTGATGGGATCCTGTACGACACGTACCCACTCTCG
GAGGAGACCTGGCACACACACCAGTTCAACTTCATCAAGAACCACGCCTTTCGCCTGCTG
AAGCCGGGGGGCGTCCTCACCTACTGCAACCTCACCTCCTGGGGGGAGCTGATGAAGTCC
AAGTACTCAGACATCACCATCATGTTTGAGGAGACGCAGGTGCCCGCGCTGCTGGAGGCC
GGCTTCCGGAGGGAGAACATCCGTACGGAGGTGATGGCGCTGGTCCCACCGGCCGACTGC
CGCTACTACGCCTTCCCACAGATGATCACGCCCCTGGTGACCAAAGGCTGA
Enzyme 28 GenBank Gene ID AC005329 Link Image
Enzyme 28 GeneCard ID GAMT Link Image
Enzyme 28 GenAtlas ID GAMT Link Image
Enzyme 28 HGNC ID HGNC:4136 Link Image
Enzyme 28 Chromosome Location 1
Enzyme 28 Locus 19p13.3
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 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 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 5664
Enzyme 29 Name Histamine N-methyltransferase
Enzyme 29 Synonyms
  1. HMT
Enzyme 29 Gene Name HNMT
Enzyme 29 Protein Sequence >Histamine N-methyltransferase
MASSMRSLFSDHGKYVESFRRFLNHSTEHQCMQEFMDKKLPGIIGRIGDTKSEIKILSIG
GGAGEIDLQILSKVQAQYPGVCINNEVVEPSAEQIAKYKELVAKTSNLENVKFAWHKETS
SEYQSRMLEKKELQKWDFIHMIQMLYYVKDIPATLKFFHSLLGTNAKMLIIVVSGSSGWD
KLWKKYGSRFPQDDLCQYITSDDLTQMLDNLGLKYECYDLLSTMDISDCFIDGNENGDLL
WDFLTETCNFNATAPPDLRAELGKDLQEPEFSAKKEGKVLFNNTLSFIVIEA
Enzyme 29 Number of Residues 292
Enzyme 29 Molecular Weight 33294.8
Enzyme 29 Theoretical pI 4.98
Enzyme 29 GO Classification Not Available
Enzyme 29 General Function Involved in histamine N-methyltransferase activity
Enzyme 29 Specific Function Inactivates histamine by N-methylation. Plays an important role in degrading histamine and in regulating the airway response to histamine
Enzyme 29 Pathways
Enzyme 29 Reactions
  • S-adenosyl-L-methionine + histamine = S-adenosyl-L-homocysteine + Ntau-methylhistamine [RN:R02155]
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 62988825 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID P50135 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name HNMT_HUMAN Link Image
Enzyme 29 PDB ID 1JQD Link Image
Enzyme 29 PDB File Show
Enzyme 29 3D Structure
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >879 bp
ATGGCATCTTCCATGAGGAGCTTGTTTTCTGACCACGGGAAATATGTTGAATCTTTCCGG
AGGTTTCTCAACCATTCCACGGAACACCAGTGCATGCAGGAATTCATGGACAAGAAGCTG
CCAGGCATAATAGGAAGGATTGGAGACACAAAATCAGAAATTAAGATTCTAAGCATAGGC
GGAGGTGCAGGTGAAATTGATCTTCAAATTCTCTCCAAAGTTCAGGCTCAATACCCAGGA
GTTTGTATCAACAATGAAGTTGTTGAGCCAAGTGCTGAACAAATTGCCAAATACAAAGAG
CTTGTAGCCAAGACATCGAACCTCGAGAACGTAAAGTTTGCTTGGCATAAGGAGACATCA
TCTGAATACCAAAGTAGAATGTTGGAGAAAAAGGAGCTTCAAAAGTGGGACTTTATTCAT
ATGATTCAAATGCTGTATTATGTAAAAGACATCCCAGCTACCCTGAAATTCTTCCATAGT
CTCTTAGGTACCAATGCTAAGATGCTCATTATTGTTGTGTCAGGAAGCAGTGGCTGGGAC
AAGCTGTGGAAAAAGTACGGATCACGCTTTCCCCAGGATGACCTCTGCCAGTATATCACA
TCAGATGACCTCACTCAGATGCTGGACAACCTAGGGCTTAAGTATGAGTGCTATGACCTT
TTGTCCACCATGGATATATCTGACTGCTTTATTGATGGTAATGAAAATGGAGACCTGCTT
TGGGATTTTTTGACTGAAACCTGCAACTTTAATGCCACAGCACCACCTGATCTCAGAGCA
GAGCTTGGGAAAGATCTACAAGAGCCTGAATTTAGTGCTAAGAAAGAGGGGAAGGTTCTT
TTTAATAATACTCTGAGTTTCATAGTGATTGAGGCATAA
Enzyme 29 GenBank Gene ID AC093674 Link Image
Enzyme 29 GeneCard ID HNMT Link Image
Enzyme 29 GenAtlas ID HNMT Link Image
Enzyme 29 HGNC ID HGNC:5028 Link Image
Enzyme 29 Chromosome Location 2
Enzyme 29 Locus 2q22.1
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References
  1. Yamauchi K, Sekizawa K, Suzuki H, Nakazawa H, Ohkawara Y, Katayose D, Ohtsu H, Tamura G, Shibahara S, Takemura M, et al.: Structure and function of human histamine N-methyltransferase: critical enzyme in histamine metabolism in airway. Am J Physiol. 1994 Sep;267(3 Pt 1):L342-9. [PubMed Link Image]
  2. Girard B, Otterness DM, Wood TC, Honchel R, Wieben ED, Weinshilboum RM: Human histamine N-methyltransferase pharmacogenetics: cloning and expression of kidney cDNA. Mol Pharmacol. 1994 Mar;45(3):461-8. [PubMed Link Image]
  3. Aksoy S, Raftogianis R, Weinshilboum R: Human histamine N-methyltransferase gene: structural characterization and chromosomal location. Biochem Biophys Res Commun. 1996 Feb 15;219(2):548-54. [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. 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]
  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. Horton JR, Sawada K, Nishibori M, Zhang X, Cheng X: Two polymorphic forms of human histamine methyltransferase: structural, thermal, and kinetic comparisons. Structure. 2001 Sep;9(9):837-49. [PubMed Link Image]
  8. Preuss CV, Wood TC, Szumlanski CL, Raftogianis RB, Otterness DM, Girard B, Scott MC, Weinshilboum RM: Human histamine N-methyltransferase pharmacogenetics: common genetic polymorphisms that alter activity. Mol Pharmacol. 1998 Apr;53(4):708-17. [PubMed Link Image]
  9. Yan L, Galinsky RE, Bernstein JA, Liggett SB, Weinshilboum RM: Histamine N-methyltransferase pharmacogenetics: association of a common functional polymorphism with asthma. Pharmacogenetics. 2000 Apr;10(3):261-6. [PubMed Link Image]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 5665
Enzyme 30 Name Thiopurine S-methyltransferase
Enzyme 30 Synonyms
  1. Thiopurine methyltransferase
Enzyme 30 Gene Name TPMT
Enzyme 30 Protein Sequence >Thiopurine S-methyltransferase
MDGTRTSLDIEEYSDTEVQKNQVLTLEEWQDKWVNGKTAFHQEQGHQLLKKHLDTFLKGK
SGLRVFFPLCGKAVEMKWFADRGHSVVGVEISELGIQEFFTEQNLSYSEEPITEIPGTKV
FKSSSGNISLYCCSIFDLPRTNIGKFDMIWDRGALVAINPGDRKCYADTMFSLLGKKFQY
LLCVLSYDPTKHPGPPFYVPHAEIERLFGKICNIRCLEKVDAFEERHKSWGIDCLFEKLY
LLTEK
Enzyme 30 Number of Residues 245
Enzyme 30 Molecular Weight 28180.1
Enzyme 30 Theoretical pI 6.16
Enzyme 30 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 30 General Function Involved in thiopurine S-methyltransferase activity
Enzyme 30 Specific Function Catalyzes the S-methylation of thiopurine drugs such as 6-mercaptopurine
Enzyme 30 Pathways Not Available
Enzyme 30 Reactions
  • S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether [RN:R03701]
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • None
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein Not Available
Enzyme 30 UniProtKB/Swiss-Prot ID P51580 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name TPMT_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >738 bp
ATGGATGGTACAAGAACTTCACTTGACATTGAAGAGTACTCGGATACTGAGGTACAGAAA
AACCAAGTACTAACTCTGGAAGAATGGCAAGACAAGTGGGTGAACGGCAAGACTGCTTTT
CATCAGGAACAAGGACATCAGCTATTAAAGAAGCATTTAGATACTTTCCTTAAAGGCAAG
AGTGGACTGAGGGTATTTTTTCCTCTTTGCGGAAAAGCGGTTGAGATGAAATGGTTTGCA
GACCGGGGACACAGTGTAGTTGGTGTGGAAATCAGTGAACTTGGGATACAAGAATTTTTT
ACAGAGCAGAATCTTTCTTACTCAGAAGAACCAATCACCGAAATTCCTGGAACCAAAGTA
TTTAAGAGTTCTTCGGGGAACATTTCATTGTACTGTTGCAGTATTTTTGATCTTCCCAGG
ACAAATATTGGCAAATTTGACATGATTTGGGATAGAGGAGCATTAGTTGCCATTAATCCA
GGTGATCGCAAATGCTATGCAGATACAATGTTTTCCCTCCTGGGAAAGAAGTTTCAGTAT
CTCCTGTGTGTTCTTTCTTATGATCCAACTAAACATCCAGGTCCACCATTTTATGTTCCA
CATGCTGAAATTGAAAGGTTGTTTGGTAAAATATGCAATATACGTTGTCTTGAGAAGGTT
GATGCTTTTGAAGAACGACATAAAAGTTGGGGAATTGACTGTCTTTTTGAAAAGTTATAT
CTACTTACAGAAAAGTAA
Enzyme 30 GenBank Gene ID S62904 Link Image
Enzyme 30 GeneCard ID TPMT Link Image
Enzyme 30 GenAtlas ID TPMT Link Image
Enzyme 30 HGNC ID HGNC:12014 Link Image
Enzyme 30 Chromosome Location 6
Enzyme 30 Locus 6p22.3
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 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 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 5666
Enzyme 31 Name N6-adenosine-methyltransferase 70 kDa subunit
Enzyme 31 Synonyms
  1. MT-A70
  2. Methyltransferase-like protein 3
Enzyme 31 Gene Name METTL3
Enzyme 31 Protein Sequence >N6-adenosine-methyltransferase 70 kDa subunit
MSDTWSSIQAHKKQLDSLRERLQRRRKQDSGHLDLRNPEAALSPTFRSDSPVPTAPTSGG
PKPSTASAVPELATDPELEKKLLHHLSDLALTLPTDAVSICLAISTPDAPATQDGVESLL
QKFAAQELIEVKRGLLQDDAHPTLVTYADHSKLSAMMGAVAEKKGPGEVAGTVTGQKRRA
EQDSTTVAAFASSLVSGLNSSASEPAKEPAKKSRKHAASDVDLEIESLLNQQSTKEQQSK
KVSQEILELLNTTTAKEQSIVEKFRSRGRAQVQEFCDYGTKEECMKASDADRPCRKLHFR
RIINKHTDESLGDCSFLNTCFHMDTCKYVHYEIDACMDSEAPGSKDHTPSQELALTQSVG
GDSSADRLFPPQWICCDIRYLDVSILGKFAVVMADPPWDIHMELPYGTLTDDEMRRLNIP
VLQDDGFLFLWVTGRAMELGRECLNLWGYERVDEIIWVKTNQLQRIIRTGRTGHWLNHGK
EHCLVGVKGNPQGFNQGLDCDVIVAEVRSTSHKPDEIYGMIERLSPGTRKIELFGRPHNV
QPNWITLGNQLDGIHLLDPDVVARFKQRYPDGIISKPKNL
Enzyme 31 Number of Residues 580
Enzyme 31 Molecular Weight 64473.3
Enzyme 31 Theoretical pI 6.38
Enzyme 31 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 31 General Function Involved in methyltransferase activity
Enzyme 31 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 31 Pathways Not Available
Enzyme 31 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 31 Pfam Domain Function
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • None
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 21361827 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID Q86U44 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name MTA70_HUMAN Link Image
Enzyme 31 PDB ID Not Available
Enzyme 31 Cellular Location Not Available
Enzyme 31 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 31 GenBank Gene ID NM_019852.3 Link Image
Enzyme 31 GeneCard ID METTL3 Link Image
Enzyme 31 GenAtlas ID METTL3 Link Image
Enzyme 31 HGNC ID HGNC:17563 Link Image
Enzyme 31 Chromosome Location 1
Enzyme 31 Locus 14q11.1
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 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 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 5933
Enzyme 32 Name Putative adenosylhomocysteinase 3
Enzyme 32 Synonyms
  1. AdoHcyase 3
  2. S-adenosyl-L-homocysteine hydrolase 3
  3. S-adenosylhomocysteine hydrolase-like protein 2
Enzyme 32 Gene Name AHCYL2
Enzyme 32 Protein Sequence >Putative adenosylhomocysteinase 3
MSVQVVSAAAAAKVPEVELKDLSPSEAESQLGLSTAAVGAMAPPAGGGDPEAPAPAAERP
PVPGPGSGPAAALSPAAGKVPQASAMKRSDPHHQHQRHRDGGEALVSPDGTVTEAPRTVK
KQIQFADQKQEFNKRPTKIGRRSLSRSISQSSTDSYSSAASYTDSSDDETSPRDKQQKNS
KGSSDFCVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTA
VLMETLGALGAQCRWAACNIYSTLNEVAAALAESGFPVFAWKGESEDDFWWCIDRCVNVE
GWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVN
DSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYV
TEIDPICALQACMDGFRLVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGH
SNTEIDVASLRTPELTWERVRSQVDHVIWPDGKRIVLLAEGRLLNLSCSTVPTFVLSITA
TTQALALIELYNAPEGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQAKYLGLNK
NGPFKPNYYRY
Enzyme 32 Number of Residues 611
Enzyme 32 Molecular Weight 66720.6
Enzyme 32 Theoretical pI 7.39
Enzyme 32 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 32 General Function Involved in adenosylhomocysteinase activity
Enzyme 32 Specific Function S-adenosyl-L-homocysteine + H(2)O = L- homocysteine + adenosine
Enzyme 32 Pathways
Enzyme 32 Reactions
  • S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine [RN:R00192]
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • None
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 24308043 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID Q96HN2 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name SAHH3_HUMAN Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 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 32 GenBank Gene ID NM_015328.3 Link Image
Enzyme 32 GeneCard ID AHCYL2 Link Image
Enzyme 32 GenAtlas ID AHCYL2 Link Image
Enzyme 32 HGNC ID HGNC:22204 Link Image
Enzyme 32 Chromosome Location 7
Enzyme 32 Locus 7q32.1
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 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 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 5934
Enzyme 33 Name Adenosylhomocysteinase
Enzyme 33 Synonyms
  1. AdoHcyase
  2. S-adenosyl-L-homocysteine hydrolase
Enzyme 33 Gene Name AHCY
Enzyme 33 Protein Sequence >Adenosylhomocysteinase
MSDKLPYKVADIGLAAWGRKALDIAENEMPGLMRMRERYSASKPLKGARIAGCLHMTVET
AVLIETLVTLGAEVQWSSCNIFSTQDHAAAAIAKAGIPVYAWKGETDEEYLWCIEQTLYF
KDGPLNMILDDGGDLTNLIHTKYPQLLPGIRGISEETTTGVHNLYKMMANGILKVPAINV
NDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVI
ITEIDPINALQAAMEGYEVTTMDEACQEGNIFVTTTGCIDIILGRHFEQMKDDAIVCNIG
HFDVEIDVKWLNENAVEKVNIKPQVDRYRLKNGRRIILLAEGRLVNLGCAMGHPSFVMSN
SFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVAEAHLGKLNVKLTKLTEKQAQYLGMS
CDGPFKPDHYRY
Enzyme 33 Number of Residues 432
Enzyme 33 Molecular Weight 47715.7
Enzyme 33 Theoretical pI 6.29
Enzyme 33 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 33 General Function Involved in adenosylhomocysteinase activity
Enzyme 33 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 33 Pathways
Enzyme 33 Reactions
  • S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine [RN:R00192]
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • None
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 178277 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID P23526 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name SAHH_HUMAN Link Image
Enzyme 33 PDB ID 1LI4 Link Image
Enzyme 33 PDB File Show
Enzyme 33 3D Structure
Enzyme 33 Cellular Location Not Available
Enzyme 33 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 33 GenBank Gene ID M61831 Link Image
Enzyme 33 GeneCard ID AHCY Link Image
Enzyme 33 GenAtlas ID AHCY Link Image
Enzyme 33 HGNC ID HGNC:343 Link Image
Enzyme 33 Chromosome Location 2
Enzyme 33 Locus 20cen-q13.1
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 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 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 5935
Enzyme 34 Name Putative adenosylhomocysteinase 2
Enzyme 34 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 34 Gene Name AHCYL1
Enzyme 34 Protein Sequence >Putative adenosylhomocysteinase 2
MSMPDAMPLPGVGEELKQAKEIEDAEKYSFMATVTKAPKKQIQFADDMQEFTKFPTKTGR
RSLSRSISQSSTDSYSSAASYTDSSDDEVSPREKQQTNSKGSSNFCVKNIKQAEFGRREI
EIAEQDMSALISLRKRAQGEKPLAGAKIVGCTHITAQTAVLIETLCALGAQCRWSACNIY
STQNEVAAALAEAGVAVFAWKGESEDDFWWCIDRCVNMDGWQANMILDDGGDLTHWVYKK
YPNVFKKIRGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDG
LKRTTDVMFGGKQVVVCGYGEVGKGCCAALKALGAIVYITEIDPICALQACMDGFRVVKL
NEVIRQVDVVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVTSLRTPELTWERVR
SQVDHVIWPDGKRVVLLAEGRLLNLSCSTVPTFVLSITATTQALALIELYNAPEGRYKQD
VYLLPKKMDEYVASLHLPSFDAHLTELTDDQAKYLGLNKNGPFKPNYYRY
Enzyme 34 Number of Residues 530
Enzyme 34 Molecular Weight 58950.9
Enzyme 34 Theoretical pI 6.87
Enzyme 34 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 34 General Function Involved in adenosylhomocysteinase activity
Enzyme 34 Specific Function S-adenosyl-L-homocysteine + H(2)O = L- homocysteine + adenosine
Enzyme 34 Pathways
Enzyme 34 Reactions
  • S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine [RN:R00192]
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • None
Enzyme 34 Transmembrane Regions
  • None
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein 16588687 Link Image
Enzyme 34 UniProtKB/Swiss-Prot ID O43865 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name SAHH2_HUMAN Link Image
Enzyme 34 PDB ID Not Available
Enzyme 34 Cellular Location Not Available
Enzyme 34 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 34 GenBank Gene ID AF315687 Link Image
Enzyme 34 GeneCard ID AHCYL1 Link Image
Enzyme 34 GenAtlas ID AHCYL1 Link Image
Enzyme 34 HGNC ID HGNC:344 Link Image
Enzyme 34 Chromosome Location 1
Enzyme 34 Locus 1p13.2
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 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 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 6059
Enzyme 35 Name Cystathionine beta-synthase
Enzyme 35 Synonyms
  1. Beta-thionase
  2. Serine sulfhydrase
Enzyme 35 Gene Name CBS
Enzyme 35 Protein Sequence >Cystathionine beta-synthase
MPSETPQAEVGPTGCPHRSGPHSAKGSLEKGSPEDKEAKEPLWIRPDAPSRCTWQLGRPA
SESPHHHTAPAKSPKILPDILKKIGDTPMVRINKIGKKFGLKCELLAKCEFFNAGGSVKD
RISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDV
LRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEI
LQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILAEPEELNQTEQTT
YEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKA
AQELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKEEDLTEKKPWWWHLRVQELGLS
APLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVG
KVIYKQFKQIRLTDTLGRLSHILEMDHFALVVHEQIQYHSTGKSSQRQMVFGVVTAIDLL
NFVAAQERDQK
Enzyme 35 Number of Residues 551
Enzyme 35 Molecular Weight 60586.0
Enzyme 35 Theoretical pI 6.63
Enzyme 35 GO Classification
Function
  • binding
  • carbon-oxygen lyase activity
  • catalytic activity
  • cofactor binding
  • cystathionine beta-synthase activity
  • hydro-lyase activity
  • lyase activity
  • pyridoxal phosphate binding
Process
  • L-serine metabolic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • cysteine biosynthetic process
  • cysteine biosynthetic process from serine
  • cysteine biosynthetic process via cystathionine
  • metabolic process
  • serine family amino acid metabolic process
  • sulfur amino acid biosynthetic process
  • sulfur amino acid metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 35 General Function Involved in cysteine biosynthetic process from serine
Enzyme 35 Specific Function Only known pyridoxal phosphate-dependent enzyme that contains heme. Important regulator of hydrogen sulfide, especially in the brain, utilizing cysteine instead of serine to catalyze the formation of hydrogen sulfide. Hydrogen sulfide is a gastratransmitter with signaling and cytoprotective effects such as acting as a neuromodulator in the brain to protect neurons against hypoxic injury
Enzyme 35 Pathways
Enzyme 35 Reactions
  • L-serine + L-homocysteine = L-cystathionine + H2O [RN:R01290]
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • None
Enzyme 35 Transmembrane Regions
  • None
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein 388716 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID P35520 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name CBS_HUMAN Link Image
Enzyme 35 PDB ID 1JBQ Link Image
Enzyme 35 PDB File Show
Enzyme 35 3D Structure
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >1656 bp
ATGCCTTCTGAGACCCCCCAGGCAGAAGTGGGGCCCACAGGCTGCCCCCACCGCTCAGGG
CCACACTCGGCGAAGGGGAGCCTGGAGAAGGGGTCCCCAGAGGATAAGGAAGCCAAGGAG
CCCCTGTGGATCCGGCCCGATGCTCCGAGCAGGTGCACCTGGCAGCTGGGCCGGCCTGCC
TCCGAGTCCCCACATCACCACACTGCCCCGGCAAAATCTCCAAAAATCTTGCCAGATATT
CTGAAGAAAATCGGGGACACCCCTATGGTCAGAATCAACAAGATTGGGAAGAAGTTCGGC
CTGAAGTGTGAGCTCTTGGCCAAGTGTGAGTTCTTCAACGCGGGCGGGAGCGTGAAGGAC
CGCATCAGCCTGCGGATGATTGAGGATGCTGAGCGCGACGGGACGCTGAAGCCCGGGGAC
ACGATTATCGAGCCGACATCCGGGAACACCGGGATCGGGCTGGCCCTGGCTGCGGCAGTG
AGGGGCTATCGCTGCATCATCGTGATGCCAGAGAAGATGAGCTCCGAGAAGGTGGACGTG
CTGCGGGCACTGGGGGCTGAGATTGTGAGGACGCCCACCAATGCCAGGTTCGACTCCCCG
GAGTCACACGTGGGGGTGGCCTGGCGGCTGAAGAACGAAATCCCCAATTCTCACATCCTA
GACCAGTACCGCAACGCCAGCAACCCCCTGGCTCACTACGACACCACCGCTGATGAGATC
CTGCAGCAGTGTGATGGGAAGCTGGACATGCTGGTGGCTTCAGTGGGCACGGGCGGCACC
ATCACGGGCATTGCCAGGAAGCTGAAGGAGAAGTGTCCTGGATGCAGGATCATTGGGGTG
GATCCCGAAGGGTCCATCCTCGCAGAGCCGGAGGAGCTGAACCAGACGGAGCAGACAACC
TACGAGGTGGAAGGGATCGGCTACGACTTCATCCCCACGGTGCTGGACAGGACGGTGGTG
GACAAGTGGTTCAAGAGCAACGATGAGGAGGCGTTCACCTTTGCCCGCATGCTGATCGCG
CAAGAGGGGCTGCTGTGCGGTGGCAGTGCTGGCAGCACGGTGGCGGTGGCCGTGAAGGCT
GCGCAGGAGCTGCAGGAGGGCCAGCGCTGCGTGGTCATTCTGCCCGACTCAGTGCGGAAC
TACATGACCAAGTTCCTGAGCGACAGGTGGATGCTGCAGAAGGGCTTTCTGAAGGAGGAG
GACCTCACGGAGAAGAAGCCCTGGTGGTGGCACCTCCGTGTTCAGGAGCTGGGCCTGTCA
GCCCCGCTGACCGTGCTCCCGACCATCACCTGTGGGCACACCATCGAGATCCTCCGGGAG
AAGGGCTTCGACCAGGCGCCCGTGGTGGATGAGGCGGGGGTAATCCTGGGAATGGTGACG
CTTGGGAACATGCTCTCGTCCCTGCTTGCCGGGAAGGTGCAGCCGTCAGACCAAGTTGGC
AAAGTCATCTACAAGCAGTTCAAACAGATCCGCCTCACGGACACGCTGGGCAGGCTCTCG
CACATCCTGGAGATGGACCACTTCGCCCTGGTGGTGCACGAGCAGATCCAGTACCACAGC
ACCGGGAAGTCCAGTCAGCGGCAGATGGTGTTCGGGGTGGTCACCGCCATTGACTTGCTG
AACTTCGTGGCCGCCCAGGAGCGGGACCAGAAGTGA
Enzyme 35 GenBank Gene ID L19501 Link Image
Enzyme 35 GeneCard ID CBS Link Image
Enzyme 35 GenAtlas ID CBS Link Image
Enzyme 35 HGNC ID HGNC:1550 Link Image
Enzyme 35 Chromosome Location 2
Enzyme 35 Locus 21q22.3
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References
  1. Kraus JP, Le K, Swaroop M, Ohura T, Tahara T, Rosenberg LE, Roper MD, Kozich V: Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells. Hum Mol Genet. 1993 Oct;2(10):1633-8. [PubMed Link Image]
  2. Chasse JF, Paly E, Paris D, Paul V, Sinet PM, Kamoun P, London J: Genomic organization of the human cystathionine beta-synthase gene: evidence for various cDNAs. Biochem Biophys Res Commun. 1995 Jun 26;211(3):826-32. [PubMed Link Image]
  3. Kruger WD, Cox DR: A yeast system for expression of human cystathionine beta-synthase: structural and functional conservation of the human and yeast genes. Proc Natl Acad Sci U S A. 1994 Jul 5;91(14):6614-8. [PubMed Link Image]
  4. Chasse JF, Paul V, Escanez R, Kamoun P, London J: Human cystathionine beta-synthase: gene organization and expression of different 5' alternative splicing. Mamm Genome. 1997 Dec;8(12):917-21. [PubMed Link Image]
  5. Kraus JP, Oliveriusova J, Sokolova J, Kraus E, Vlcek C, de Franchis R, Maclean KN, Bao L, Bukovsk, Patterson D, Paces V, Ansorge W, Kozich V: The human cystathionine beta-synthase (CBS) gene: complete sequence, alternative splicing, and polymorphisms. Genomics. 1998 Sep 15;52(3):312-24. [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. 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. Kraus J, Packman S, Fowler B, Rosenberg LE: Purification and properties of cystathionine beta-synthase from human liver. Evidence for identical subunits. J Biol Chem. 1978 Sep 25;253(18):6523-8. [PubMed Link Image]
  9. Kabil O, Zhou Y, Banerjee R: Human cystathionine beta-synthase is a target for sumoylation. Biochemistry. 2006 Nov 14;45(45):13528-36. [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. Meier M, Janosik M, Kery V, Kraus JP, Burkhard P: Structure of human cystathionine beta-synthase: a unique pyridoxal 5'-phosphate-dependent heme protein. EMBO J. 2001 Aug 1;20(15):3910-6. [PubMed Link Image]
  12. Taoka S, Lepore BW, Kabil O, Ojha S, Ringe D, Banerjee R: Human cystathionine beta-synthase is a heme sensor protein. Evidence that the redox sensor is heme and not the vicinal cysteines in the CXXC motif seen in the crystal structure of the truncated enzyme. Biochemistry. 2002 Aug 20;41(33):10454-61. [PubMed Link Image]
  13. Kraus JP, Janosik M, Kozich V, Mandell R, Shih V, Sperandeo MP, Sebastio G, de Franchis R, Andria G, Kluijtmans LA, Blom H, Boers GH, Gordon RB, Kamoun P, Tsai MY, Kruger WD, Koch HG, Ohura T, Gaustadnes M: Cystathionine beta-synthase mutations in homocystinuria. Hum Mutat. 1999;13(5):362-75. [PubMed Link Image]
  14. Kozich V, Kraus JP: Screening for mutations by expressing patient cDNA segments in E. coli: homocystinuria due to cystathionine beta-synthase deficiency. Hum Mutat. 1992;1(2):113-23. [PubMed Link Image]
  15. Kozich V, de Franchis R, Kraus JP: Molecular defect in a patient with pyridoxine-responsive homocystinuria. Hum Mol Genet. 1993 Jun;2(6):815-6. [PubMed Link Image]
  16. Hu FL, Gu Z, Kozich V, Kraus JP, Ramesh V, Shih VE: Molecular basis of cystathionine beta-synthase deficiency in pyridoxine responsive and nonresponsive homocystinuria. Hum Mol Genet. 1993 Nov;2(11):1857-60. [PubMed Link Image]
  17. de Franchis R, Kozich V, McInnes RR, Kraus JP: Identical genotypes in siblings with different homocystinuric phenotypes: identification of three mutations in cystathionine beta-synthase using an improved bacterial expression system. Hum Mol Genet. 1994 Jul;3(7):1103-8. [PubMed Link Image]
  18. Marble M, Geraghty MT, de Franchis R, Kraus JP, Valle D: Characterization of a cystathionine beta-synthase allele with three mutations in cis in a patient with B6 nonresponsive homocystinuria. Hum Mol Genet. 1994 Oct;3(10):1883-6. [PubMed Link Image]
  19. Kraus JP: Komrower Lecture. Molecular basis of phenotype expression in homocystinuria. J Inherit Metab Dis. 1994;17(4):383-90. [PubMed Link Image]
  20. Shih VE, Fringer JM, Mandell R, Kraus JP, Berry GT, Heidenreich RA, Korson MS, Levy HL, Ramesh V: A missense mutation (I278T) in the cystathionine beta-synthase gene prevalent in pyridoxine-responsive homocystinuria and associated with mild clinical phenotype. Am J Hum Genet. 1995 Jul;57(1):34-9. [PubMed Link Image]
  21. Sebastio G, Sperandeo MP, Panico M, de Franchis R, Kraus JP, Andria G: The molecular basis of homocystinuria due to cystathionine beta-synthase deficiency in Italian families, and report of four novel mutations. Am J Hum Genet. 1995 Jun;56(6):1324-33. [PubMed Link Image]
  22. Kluijtmans LA, Blom HJ, Boers GH, van Oost BA, Trijbels FJ, van den Heuvel LP: Two novel missense mutations in the cystathionine beta-synthase gene in homocystinuric patients. Hum Genet. 1995 Aug;96(2):249-50. [PubMed Link Image]
  23. Kruger WD, Cox DR: A yeast assay for functional detection of mutations in the human cystathionine beta-synthase gene. Hum Mol Genet. 1995 Jul;4(7):1155-61. [PubMed Link Image]
  24. Sperandeo MP, Panico M, Pepe A, Candito M, de Franchis R, Kraus JP, Andria G, Sebastio G: Molecular analysis of patients affected by homocystinuria due to cystathionine beta-synthase deficiency: report of a new mutation in exon 8 and a deletion in intron 11. J Inherit Metab Dis. 1995;18(2):211-4. [PubMed Link Image]
  25. Kluijtmans LA, Boers GH, Stevens EM, Renier WO, Kraus JP, Trijbels FJ, van den Heuvel LP, Blom HJ: Defective cystathionine beta-synthase regulation by S-adenosylmethionine in a partially pyridoxine responsive homocystinuria patient. J Clin Invest. 1996 Jul 15;98(2):285-9. [PubMed Link Image]
  26. Sperandeo MP, Candito M, Sebastio G, Rolland MO, Turc-Carel C, Giudicelli H, Dellamonica P, Andria G: Homocysteine response to methionine challenge in four obligate heterozygotes for homocystinuria and relationship with cystathionine beta-synthase mutations. J Inherit Metab Dis. 1996;19(3):351-6. [PubMed Link Image]
  27. Dawson PA, Cox AJ, Emmerson BT, Dudman NP, Kraus JP, Gordon RB: Characterisation of five missense mutations in the cystathionine beta-synthase gene from three patients with B6-nonresponsive homocystinuria. Eur J Hum Genet. 1997 Jan-Feb;5(1):15-21. [PubMed Link Image]
  28. Kim CE, Gallagher PM, Guttormsen AB, Refsum H, Ueland PM, Ose L, Folling I, Whitehead AS, Tsai MY, Kruger WD: Functional modeling of vitamin responsiveness in yeast: a common pyridoxine-responsive cystathionine beta-synthase mutation in homocystinuria. Hum Mol Genet. 1997 Dec;6(13):2213-21. [PubMed Link Image]
  29. Aral B, Coude M, London J, Aupetit J, Chasse JF, Zabot MT, Chadefaux-Vekemans B, Kamoun P: Two novel mutations (K384E and L539S) in the C-terminal moiety of the cystathionine beta-synthase protein in two French pyridoxine-responsive homocystinuria patients. Hum Mutat. 1997;9(1):81-2. [PubMed Link Image]
  30. Kozich V, Janosik M, Sokolova J, Oliveriusova J, Orendac M, Kraus JP, Elleder D: Analysis of CBS alleles in Czech and Slovak patients with homocystinuria: report on three novel mutations E176K, W409X and 1223 + 37 del99. J Inherit Metab Dis. 1997 Jul;20(3):363-6. [PubMed Link Image]
  31. Tsai MY, Wong PW, Garg U, Hanson NQ, Schwichtenberg K: Two Novel Mutations in the Cystathionine beta-synthase Gene of Homocystinuric Patients. Mol Diagn. 1997 Jun;2(2):129-133. [PubMed Link Image]
  32. Gordon RB, Cox AJ, Dawson PA, Emmerson BT, Kraus JP, Dudman NP: Mutational analysis of the cystathionine beta-synthase gene: a splicing mutation, two missense mutations and an insertion in patients with homocystinuria. Mutations in brief no. 120. Online. Hum Mutat. 1998;11(4):332. [PubMed Link Image]
  33. Gallagher PM, Naughten E, Hanson NQ, Schwichtenberg K, Bignell M, Yuan M, Ward P, Yap S, Whitehead AS, Tsai MY: Characterization of mutations in the cystathionine beta-synthase gene in Irish patients with homocystinuria. Mol Genet Metab. 1998 Dec;65(4):298-302. [PubMed Link Image]
  34. de Franchis R, Kraus E, Kozich V, Sebastio G, Kraus JP: Four novel mutations in the cystathionine beta-synthase gene: effect of a second linked mutation on the severity of the homocystinuric phenotype. Hum Mutat. 1999;13(6):453-7. [PubMed Link Image]
  35. Gat-Yablonski G, Mandel H, Fowler B, Taleb O, Sela BA: Homocystinuria in the Arab population of Israel: identification of two novel mutations using DGGE analysis. Hum Mutat. 2000 Oct;16(4):372. [PubMed Link Image]
  36. Janosik M, Oliveriusova J, Janosikova B, Sokolova J, Kraus E, Kraus JP, Kozich V: Impaired heme binding and aggregation of mutant cystathionine beta-synthase subunits in homocystinuria. Am J Hum Genet. 2001 Jun;68(6):1506-13. Epub 2001 May 15. [PubMed Link Image]
  37. Castro R, Heil SG, Rivera I, Jakobs C, de Almeida IT, Blom HJ: Molecular genetic analysis of the cystathionine beta-synthase gene in Portuguese homocystinuria patients: three novel mutations. Clin Genet. 2001 Aug;60(2):161-3. [PubMed Link Image]
  38. Maclean KN, Gaustadnes M, Oliveriusova J, Janosik M, Kraus E, Kozich V, Kery V, Skovby F, Rudiger N, Ingerslev J, Stabler SP, Allen RH, Kraus JP: High homocysteine and thrombosis without connective tissue disorders are associated with a novel class of cystathionine beta-synthase (CBS) mutations. Hum Mutat. 2002 Jun;19(6):641-55. [PubMed Link Image]
  39. Gaustadnes M, Wilcken B, Oliveriusova J, McGill J, Fletcher J, Kraus JP, Wilcken DE: The molecular basis of cystathionine beta-synthase deficiency in Australian patients: genotype-phenotype correlations and response to treatment. Hum Mutat. 2002 Aug;20(2):117-26. [PubMed Link Image]
  40. Urreizti R, Balcells S, Rodes M, Vilarinho L, Baldellou A, Couce ML, Munoz C, Campistol J, Pinto X, Vilaseca MA, Grinberg D: Spectrum of CBS mutations in 16 homocystinuric patients from the Iberian Peninsula: high prevalence of T191M and absence of I278T or G307S. Hum Mutat. 2003 Jul;22(1):103. [PubMed Link Image]
  41. Kruger WD, Wang L, Jhee KH, Singh RH, Elsas LJ 2nd: Cystathionine beta-synthase deficiency in Georgia (USA): correlation of clinical and biochemical phenotype with genotype. Hum Mutat. 2003 Dec;22(6):434-41. [PubMed Link Image]
  42. Orendae M, Pronicka E, Kubalska J, Janosik M, Sokolova J, Linnebank M, Koch HG, Kozich V: Identification and functional analysis of two novel mutations in the CBS gene in Polish patients with homocystinuria. Hum Mutat. 2004 Jun;23(6):631. [PubMed Link Image]
  43. Linnebank M, Janosik M, Kozich V, Pronicka E, Kubalska J, Sokolova J, Linnebank A, Schmidt E, Leyendecker C, Klockgether T, Kraus JP, Koch HG: The cystathionine beta-synthase (CBS) mutation c.1224-2A>C in Central Europe: Vitamin B6 nonresponsiveness and a common ancestral haplotype. Hum Mutat. 2004 Oct;24(4):352-3. [PubMed Link Image]
  44. Porto MP, Galdieri LC, Pereira VG, Vergani N, da Rocha JC, Micheletti C, Martins AM, Perez AB, Almeida VD: Molecular analysis of homocystinuria in Brazilian patients. Clin Chim Acta. 2005 Dec;362(1-2):71-8. Epub 2005 Jul 5. [PubMed Link Image]
  45. Lee SJ, Lee DH, Yoo HW, Koo SK, Park ES, Park JW, Lim HG, Jung SC: Identification and functional analysis of cystathionine beta-synthase gene mutations in patients with homocystinuria. J Hum Genet. 2005;50(12):648-54. Epub 2005 Oct 5. [PubMed Link Image]
  46. Urreizti R, Asteggiano C, Cozar M, Frank N, Vilaseca MA, Grinberg D, Balcells S: Functional assays testing pathogenicity of 14 cystathionine-beta synthase mutations. Hum Mutat. 2006 Feb;27(2):211. [PubMed Link Image]
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 7011
Enzyme 36 Name Lipoyl synthase, mitochondrial
Enzyme 36 Synonyms
  1. Lipoate synthase
  2. LS
  3. Lip-syn
  4. Lipoic acid synthase
Enzyme 36 Gene Name LIAS
Enzyme 36 Protein Sequence >Lipoyl synthase, mitochondrial
MSLRCGDAARTLGPRVFGRYFCSPVRPLSSLPDKKKELLQNGPDLQDFVSGDLADRSTWD
EYKGNLKRQKGERLRLPPWLKTEIPMGKNYNKLKNTLRNLNLHTVCEEARCPNIGECWGG
GEYATATATIMLMGDTCTRGCRFCSVKTARNPPPLDASEPYNTAKAIAEWGLDYVVLTSV
DRDDMPDGGAEHIAKTVSYLKERNPKILVECLTPDFRGDLKAIEKVALSGLDVYAHNVET
VPELQSKVRDPRANFDQSLRVLKHAKKVQPDVISKTSIMLGLGENDEQVYATMKALREAD
VDCLTLGQYMQPTRRHLKVEEYITPEKFKYWEKVGNELGFHYTASGPLVRSSYKAGEFFL
KNLVAKRKTKDL
Enzyme 36 Number of Residues 372
Enzyme 36 Molecular Weight 41910.7
Enzyme 36 Theoretical pI 8.77
Enzyme 36 GO Classification
Function
  • 4 iron, 4 sulfur cluster binding
  • binding
  • catalytic activity
  • iron-sulfur cluster binding
  • lipoate synthase activity
  • metal cluster binding
  • sulfurtransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
  • cellular metabolic process
  • coenzyme metabolic process
  • cofactor metabolic process
  • lipoate biosynthetic process
  • lipoic acid biosynthetic process
  • lipoic acid metabolic process
  • metabolic process
Component
Enzyme 36 General Function Involved in catalytic activity
Enzyme 36 Specific Function Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives
Enzyme 36 Pathways Not Available
Enzyme 36 Reactions
  • protein N6-(octanoyl)lysine + 2 sulfur + 2 S-adenosyl-L-methionine = protein N6-(lipoyl)lysine + 2 L-methionine + 2 5'-deoxyadenosine [RN:R07767]
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • None
Enzyme 36 Transmembrane Regions
  • None
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein Not Available
Enzyme 36 UniProtKB/Swiss-Prot ID O43766 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name LIAS_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence >1119 bp
ATGTCTCTACGCTGCGGGGATGCAGCCCGCACCCTGGGGCCCCGGGTATTTGGGAGATAT
TTTTGCAGCCCAGTCAGACCGTTAAGCTCCTTGCCAGATAAAAAAAAGGAACTCCTACAG
AATGGACCAGACCTTCAAGATTTTGTATCTGGTGATCTTGCAGACAGGAGCACCTGGGAT
GAATATAAAGGAAACCTAAAACGCCAGAAAGGAGAAAGGTTAAGACTACCTCCATGGCTA
AAGACAGAGATTCCCATGGGGAAAAATTACAATAAACTGAAAAATACTTTGCGGAATTTA
AATCTCCATACAGTATGTGAGGAAGCTCGATGTCCCAATATTGGAGAGTGTTGGGGAGGT
GGAGAATATGCCACCGCCACAGCCACGATCATGTTGATGGGTGACACATGTACAAGAGGT
TGCAGATTTTGTTCTGTTAAGACTGCAAGAAATCCTCCTCCACTGGATGCCAGTGAGCCC
TACAATACTGCAAAGGCAATTGCAGAATGGGGTCTGGATTATGTTGTCCTGACGTCTGTG
GATCGAGATGATATGCCTGATGGGGGAGCTGAACACATTGCAAAGACCGTATCATATTTA
AAGGAAAGGAATCCAAAAATCCTTGTGGAGTGTCTTACTCCTGATTTTCGAGGTGATCTC
AAAGCAATAGAAAAAGTTGCTCTGTCAGGATTAGATGTGTATGCACATAATGTAGAAACA
GTCCCGGAATTACAGAGTAAGGTTCGTGATCCTCGGGCCAATTTTGATCAGTCCCTACGT
GTACTGAAACATGCCAAGAAGGTTCAGCCTGATGTTATTTCTAAAACATCTATAATGTTG
GGTTTAGGCGAGAATGATGAGCAAGTATATGCAACAATGAAAGCACTTCGTGAGGCAGAT
GTAGACTGCTTGACTTTAGGACAATATATGCAGCCAACAAGGCGTCACCTTAAGGTTGAA
GAATATATTACTCCTGAAAAATTCAAATACTGGGAAAAAGTAGGAAATGAACTTGGATTT
CATTATACTGCAAGTGGCCCTTTGGTGCGTTCTTCATATAAAGCAGGTGAATTTTTCCTG
AAAAATCTAGTGGCTAAAAGAAAAACAAAAGACCTCTAA
Enzyme 36 GenBank Gene ID AK292238 Link Image
Enzyme 36 GeneCard ID LIAS Link Image
Enzyme 36 GenAtlas ID LIAS Link Image
Enzyme 36 HGNC ID HGNC:16429 Link Image
Enzyme 36 Chromosome Location 4
Enzyme 36 Locus 4p14
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 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. 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. Stanchi F, Bertocco E, Toppo S, Dioguardi R, Simionati B, Cannata N, Zimbello R, Lanfranchi G, Valle G: Characterization of 16 novel human genes showing high similarity to yeast sequences. Yeast. 2001 Jan 15;18(1):69-80. [PubMed Link Image]
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 7065
Enzyme 37 Name Protein arginine N-methyltransferase 5
Enzyme 37 Synonyms
  1. 72 kDa ICln-binding protein
  2. Histone-arginine N-methyltransferase PRMT5
  3. Jak-binding protein 1
  4. Shk1 kinase-binding protein 1 homolog
  5. SKB1 homolog
  6. SKB1Hs
Enzyme 37 Gene Name PRMT5
Enzyme 37 Protein Sequence >Protein arginine N-methyltransferase 5
MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVAKQGFDFLCMPVFHPRFKREFIQEPAK
NRPGPQTRSDLLLSGRDWNTLIVGKLSPWIRPDSKVEKIRRNSEAAMLQELNFGAYLGLP
AFLLPLNQEDNTNLARVLTNHIHTGHHSSMFWMRVPLVAPEDLRDDIIENAPTTHTEEYS
GEEKTWMWWHNFRTLCDYSKRIAVALEIGADLPSNHVIDRWLGEPIKAAILPTSIFLTNK
KGFPVLSKMHQRLIFRLLKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELF
AKGYEDYLQSPLQPLMDNLESQTYEVFEKDPIKYSQYQQAIYKCLLDRVPEEEKDTNVQV
LMVLGAGRGPLVNASLRAAKQADRRIKLYAVEKNPNAVVTLENWQFEEWGSQVTVVSSDM
REWVAPEKADIIVSELLGSFADNELSPECLDGAQHFLKDDGVSIPGEYTSFLAPISSSKL
YNEVRACREKDRDPEAQFEMPYVVRLHNFHQLSAPQPCFTFSHPNRDPMIDNNRYCTLEF
PVEVNTVLHGFAGYFETVLYQDITLSIRPETHSPGMFSWFPILFPIKQPITVREGQTICV
RFWRCSNSKKVWYEWAVTAPVCSAIHNPTGRSYTIGL
Enzyme 37 Number of Residues 637
Enzyme 37 Molecular Weight 72683.2
Enzyme 37 Theoretical pI 6.24
Enzyme 37 GO Classification
Function
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 37 General Function Involved in histone-arginine N-methyltransferase activity
Enzyme 37 Specific Function Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Methylates SUPT5H. Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. Plays a role in the assembly of snRNP core particles. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. May regulate the SUPT5H transcriptional elongation properties. May be part of a pathway that is connected to a chloride current, possibly through cytoskeletal rearrangement. Methylates histone H2A and H4 'Arg-3' during germ cell development. Methylates histone H3 'Arg-8', which may repress transcription. Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage. Methylates RPS10
Enzyme 37 Pathways Not Available
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 197692193 Link Image
Enzyme 37 UniProtKB/Swiss-Prot ID O14744 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name ANM5_HUMAN Link Image
Enzyme 37 PDB ID Not Available
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence >1914 bp
ATGGCGGCGATGGCGGTCGGGGGTGCTGGTGGGAGCCGCGTGTCCAGCGGGAGGGACCTG
AATTGCGTCCCCGAAATAGCTGACACACTAGGGGCTGTGGCCAAGCAGGGGTTTGATTTC
CTCTGCATGCCTGTCTTCCATCCGCGTTTCAAGAGGGAGTTCATTCAGGAACCTGCTAAG
AATCGGCCCGGTCCCCAGACACGATCAGACCTACTGCTGTCAGGAAGGGACTGGAATACG
CTAATTGTGGGAAAGCTTTCTCCATGGATTCGTCCAGACTCAAAAGTGGAGAAGATTCGC
AGGAACTCCGAGGCGGCCATGTTACAGGAGCTGAATTTTGGTGCATATTTGGGTCTTCCA
GCTTTCCTGCTGCCCCTTAATCAGGAAGATAACACCAACCTGGCCAGAGTTTTGACCAAC
CACATCCACACTGGCCATCACTCTTCCATGTTCTGGATGCGGGTACCCTTGGTGGCACCA
GAGGACCTGAGAGATGATATAATTGAGAATGCACCAACTACACACACAGAGGAGTACAGT
GGGGAGGAGAAAACGTGGATGTGGTGGCACAACTTCCGGACTTTGTGTGACTATAGTAAG
AGGATTGCAGTGGCTCTTGAAATTGGGGCTGACCTCCCATCTAATCATGTCATTGATCGC
TGGCTTGGGGAGCCCATCAAAGCAGCCATTCTCCCCACTAGCATTTTCCTGACCAATAAG
AAGGGATTTCCTGTTCTTTCTAAGATGCACCAGAGGCTCATCTTCCGGCTCCTCAAGTTG
GAGGTGCAGTTCATCATCACAGGCACCAACCACCACTCAGAGAAGGAGTTCTGCTCCTAC
CTCCAATACCTGGAATACTTAAGCCAGAACCGTCCTCCACCTAATGCCTATGAACTCTTT
GCCAAGGGCTATGAAGACTATCTGCAGTCCCCGCTTCAGCCACTGATGGACAATCTGGAA
TCTCAGACATATGAAGTGTTTGAAAAGGACCCCATCAAATACTCTCAGTACCAGCAGGCC
ATCTATAAATGTCTGCTAGACCGAGTACCAGAAGAGGAGAAGGATACCAATGTCCAGGTA
CTGATGGTGCTGGGAGCAGGACGGGGACCCCTGGTGAACGCTTCCCTGCGGGCAGCCAAG
CAGGCCGACCGGCGGATAAAGCTGTATGCTGTGGAGAAAAACCCAAATGCCGTGGTGACG
CTAGAGAACTGGCAGTTTGAAGAATGGGGAAGCCAAGTGACCGTAGTCTCATCAGACATG
AGGGAATGGGTGGCTCCAGAGAAAGCAGACATCATTGTCAGTGAGCTTCTGGGCTCATTT
GCTGACAATGAATTGTCGCCTGAGTGCCTGGATGGAGCCCAGCACTTCCTAAAAGATGAT
GGTGTGAGCATCCCCGGGGAGTACACTTCCTTTCTGGCTCCCATCTCTTCCTCCAAGCTG
TACAATGAGGTCCGAGCCTGTAGGGAGAAGGACCGTGACCCTGAGGCCCAGTTTGAGATG
CCTTATGTGGTACGGCTGCACAACTTCCACCAGCTCTCTGCACCCCAGCCCTGTTTCACC
TTCAGCCATCCCAACAGAGATCCTATGATTGACAACAACCGCTATTGCACCTTGGAATTT
CCTGTGGAGGTGAACACAGTACTACATGGCTTTGCCGGCTACTTTGAGACTGTGCTTTAT
CAGGACATCACTCTGAGTATCCGTCCAGAGACTCACTCTCCCGGGATGTTCTCATGGTTT
CCCATCCTCTTCCCTATTAAGCAGCCCATAACGGTACGTGAAGGCCAAACCATCTGTGTG
CGTTTCTGGCGATGCAGCAATTCCAAGAAGGTGTGGTATGAGTGGGCTGTGACAGCACCA
GTCTGTTCTGCTATTCATAACCCCACAGGCCGCTCATATACCATTGGCCTCTAA
Enzyme 37 GenBank Gene ID AB451246 Link Image
Enzyme 37 GeneCard ID PRMT5 Link Image
Enzyme 37 GenAtlas ID Not Available
Enzyme 37 HGNC ID Not Available
Enzyme 37 Chromosome Location 1
Enzyme 37 Locus 14q11.2
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 General References
  1. Krapivinsky G, Pu W, Wickman K, Krapivinsky L, Clapham DE: pICln binds to a mammalian homolog of a yeast protein involved in regulation of cell morphology. J Biol Chem. 1998 May 1;273(18):10811-4. [PubMed Link Image]
  2. Gilbreth M, Yang P, Bartholomeusz G, Pimental RA, Kansra S, Gadiraju R, Marcus S: Negative regulation of mitosis in fission yeast by the shk1 interacting protein skb1 and its human homolog, Skb1Hs. Proc Natl Acad Sci U S A. 1998 Dec 8;95(25):14781-6. [PubMed Link Image]
  3. Pollack BP, Kotenko SV, He W, Izotova LS, Barnoski BL, Pestka S: The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity. J Biol Chem. 1999 Oct 29;274(44):31531-42. [PubMed Link Image]
  4. Goshima N, Kawamura Y, Fukumoto A, Miura A, Honma R, Satoh R, Wakamatsu A, Yamamoto J, Kimura K, Nishikawa T, Andoh T, Iida Y, Ishikawa K, Ito E, Kagawa N, Kaminaga C, Kanehori K, Kawakami B, Kenmochi K, Kimura R, Kobayashi M, Kuroita T, Kuwayama H, Maruyama Y, Matsuo K, Minami K, Mitsubori M, Mori M, Morishita R, Murase A, Nishikawa A, Nishikawa S, Okamoto T, Sakagami N, Sakamoto Y, Sasaki Y, Seki T, Sono S, Sugiyama A, Sumiya T, Takayama T, Takayama Y, Takeda H, Togashi T, Yahata K, Yamada H, Yanagisawa Y, Endo Y, Imamoto F, Kisu Y, Tanaka S, Isogai T, Imai J, Watanabe S, Nomura N: Human protein factory for converting the transcriptome into an in vitro-expressed proteome,. Nat Methods. 2008 Dec;5(12):1011-7. [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. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  7. Azzouz TN, Pillai RS, Dapp C, Chari A, Meister G, Kambach C, Fischer U, Schumperli D: Toward an assembly line for U7 snRNPs: interactions of U7-specific Lsm proteins with PRMT5 and SMN complexes. J Biol Chem. 2005 Oct 14;280(41):34435-40. Epub 2005 Aug 8. [PubMed Link Image]
  8. Schwarzler A, Kreienkamp HJ, Richter D: Interaction of the somatostatin receptor subtype 1 with the human homolog of the Shk1 kinase-binding protein from yeast. J Biol Chem. 2000 Mar 31;275(13):9557-62. [PubMed Link Image]
  9. Rho J, Choi S, Seong YR, Cho WK, Kim SH, Im DS: Prmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family. J Biol Chem. 2001 Apr 6;276(14):11393-401. Epub 2001 Jan 10. [PubMed Link Image]
  10. Meister G, Eggert C, Buhler D, Brahms H, Kambach C, Fischer U: Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln. Curr Biol. 2001 Dec 11;11(24):1990-4. [PubMed Link Image]
  11. Fabbrizio E, El Messaoudi S, Polanowska J, Paul C, Cook JR, Lee JH, Negre V, Rousset M, Pestka S, Le Cam A, Sardet C: Negative regulation of transcription by the type II arginine methyltransferase PRMT5. EMBO Rep. 2002 Jul;3(7):641-5. [PubMed Link Image]
  12. Kwak YT, Guo J, Prajapati S, Park KJ, Surabhi RM, Miller B, Gehrig P, Gaynor RB: Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties. Mol Cell. 2003 Apr;11(4):1055-66. [PubMed Link Image]
  13. Pal S, Vishwanath SN, Erdjument-Bromage H, Tempst P, Sif S: Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes. Mol Cell Biol. 2004 Nov;24(21):9630-45. [PubMed Link Image]
  14. Gonsalvez GB, Tian L, Ospina JK, Boisvert FM, Lamond AI, Matera AG: Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins. J Cell Biol. 2007 Aug 27;178(5):733-40. Epub 2007 Aug 20. [PubMed Link Image]
  15. Lacroix M, El Messaoudi S, Rodier G, Le Cam A, Sardet C, Fabbrizio E: The histone-binding protein COPR5 is required for nuclear functions of the protein arginine methyltransferase PRMT5. EMBO Rep. 2008 May;9(5):452-8. Epub 2008 Apr 11. [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. 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]
  18. Ren J, Wang Y, Liang Y, Zhang Y, Bao S, Xu Z: Methylation of ribosomal protein S10 by protein-arginine methyltransferase 5 regulates ribosome biogenesis. J Biol Chem. 2010 Apr 23;285(17):12695-705. Epub 2010 Feb 16. [PubMed Link Image]
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 7083
Enzyme 38 Name Histone-lysine N-methyltransferase SETD1A
Enzyme 38 Synonyms
  1. Lysine N-methyltransferase 2F
  2. SET domain-containing protein 1A
  3. hSET1A
  4. Set1/Ash2 histone methyltransferase complex subunit SET1
Enzyme 38 Gene Name SETD1A
Enzyme 38 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 38 Number of Residues 1707
Enzyme 38 Molecular Weight 186032.2
Enzyme 38 Theoretical pI 4.79
Enzyme 38 GO Classification
Function
  • binding
  • nucleic acid binding
  • nucleotide binding
Process
Component
Enzyme 38 General Function Involved in nucleotide binding
Enzyme 38 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 38 Pathways
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 55741677 Link Image
Enzyme 38 UniProtKB/Swiss-Prot ID O15047 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name SET1A_HUMAN Link Image
Enzyme 38 PDB ID Not Available
Enzyme 38 Cellular Location Not Available
Enzyme 38 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 38 GenBank Gene ID NM_014712.1 Link Image
Enzyme 38 GeneCard ID SETD1A Link Image
Enzyme 38 GenAtlas ID SETD1A Link Image
Enzyme 38 HGNC ID HGNC:29010 Link Image
Enzyme 38 Chromosome Location 1
Enzyme 38 Locus 16p11.2
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 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 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 7234
Enzyme 39 Name rRNA 2'-O-methyltransferase fibrillarin
Enzyme 39 Synonyms
  1. 34 kDa nucleolar scleroderma antigen
Enzyme 39 Gene Name FBL
Enzyme 39 Protein Sequence >rRNA 2'-O-methyltransferase fibrillarin
MKPGFSPRGGGFGGRGGFGDRGGRGGRGGFGGGRGRGGGFRGRGRGGGGGGGGGGGGGRG
GGGFHSGGNRGRGRGGKRGNQSGKNVMVEPHRHEGVFICRGKEDALVTKNLVPGESVYGE
KRVSISEGDDKIEYRAWNPFRSKLAAAILGGVDQIHIKPGAKVLYLGAASGTTVSHVSDI
VGPDGLVYAVEFSHRSGRDLINLAKKRTNIIPVIEDARHPHKYRMLIAMVDVIFADVAQP
DQTRIVALNAHTFLRNGGHFVISIKANCIDSTASAEAVFASEVKKMQQENMKPQEQLTLE
PYERDHAVVVGVYRPPPKVKN
Enzyme 39 Number of Residues 321
Enzyme 39 Molecular Weight 33784.1
Enzyme 39 Theoretical pI 10.81
Enzyme 39 GO Classification
Function
  • RNA binding
  • binding
  • catalytic activity
  • methyltransferase activity
  • nucleic acid binding
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • RNA metabolic process
  • cellular macromolecule metabolic process
  • macromolecule metabolic process
  • metabolic process
  • ncRNA metabolic process
  • rRNA metabolic process
  • rRNA processing
  • tRNA metabolic process
  • tRNA processing
Component
Enzyme 39 General Function Involved in RNA binding
Enzyme 39 Specific Function Involved in pre-rRNA processing. Utilizes the methyl donor S-adenosyl-L-methionine to catalyze the site-specific 2'- hydroxyl methylation of ribose moieties in pre-ribosomal RNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA
Enzyme 39 Pathways Not Available
Enzyme 39 Reactions Not Available
Enzyme 39 Pfam Domain Function
Enzyme 39 Signals
  • None
Enzyme 39 Transmembrane Regions
  • None
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein 197692469 Link Image
Enzyme 39 UniProtKB/Swiss-Prot ID P22087 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name FBRL_HUMAN Link Image
Enzyme 39 PDB ID Not Available
Enzyme 39 Cellular Location Not Available
Enzyme 39 Gene Sequence >963 bp
ATGAAGCCAGGATTCAGTCCCCGTGGGGGTGGCTTTGGCGGCCGAGGGGGCTTTGGTGAC
CGTGGTGGTCGTGGAGGCCGAGGGGGCTTTGGCGGGGGCCGAGGTCGAGGCGGAGGCTTT
AGAGGTCGTGGACGAGGAGGAGGTGGAGGCGGCGGCGGCGGTGGAGGAGGAGGAAGAGGT
GGTGGAGGCTTCCATTCTGGTGGCAACCGGGGTCGTGGTCGGGGAGGAAAAAGAGGAAAC
CAGTCGGGGAAGAATGTGATGGTGGAGCCGCATCGGCATGAGGGTGTCTTCATTTGTCGA
GGAAAGGAAGATGCACTGGTCACCAAGAACCTGGTCCCTGGGGAATCAGTTTATGGAGAG
AAGAGAGTCTCGATTTCGGAAGGAGATGACAAAATTGAGTACCGAGCCTGGAACCCCTTC
CGCTCCAAGCTAGCAGCAGCAATCCTGGGTGGTGTGGACCAGATCCACATCAAACCGGGG
GCTAAGGTTCTCTACCTCGGGGCTGCCTCGGGCACCACGGTCTCCCATGTCTCTGACATC
GTTGGTCCGGATGGTCTAGTCTATGCAGTCGAGTTCTCCCACCGCTCTGGCCGTGACCTC
ATTAACTTGGCCAAGAAGAGGACCAACATCATTCCTGTGATCGAGGATGCTCGACACCCA
CACAAATACCGCATGCTCATCGCAATGGTGGATGTGATCTTTGCTGATGTGGCCCAGCCA
GACCAGACCCGGATTGTGGCCCTGAATGCCCACACCTTCCTGCGTAATGGAGGACACTTT
GTGATTTCCATTAAGGCCAACTGCATTGACTCCACAGCCTCAGCCGAGGCCGTGTTTGCC
TCCGAAGTGAAAAAGATGCAACAGGAGAACATGAAGCCGCAGGAGCAGTTGACCCTTGAG
CCATATGAAAGAGACCATGCCGTGGTCGTGGGAGTGTACAGGCCACCCCCCAAGGTGAAG
AAC
Enzyme 39 GenBank Gene ID AB451384 Link Image
Enzyme 39 GeneCard ID FBL Link Image
Enzyme 39 GenAtlas ID FBL Link Image
Enzyme 39 HGNC ID HGNC:3599 Link Image
Enzyme 39 Chromosome Location 1
Enzyme 39 Locus 19q13.1
Enzyme 39 SNPs SNPJam Report Link Image
Enzyme 39 General References
  1. Aris JP, Blobel G: cDNA cloning and sequencing of human fibrillarin, a conserved nucleolar protein recognized by autoimmune antisera. Proc Natl Acad Sci U S A. 1991 Feb 1;88(3):931-5. [PubMed Link Image]
  2. Jansen RP, Hurt EC, Kern H, Lehtonen H, Carmo-Fonseca M, Lapeyre B, Tollervey D: Evolutionary conservation of the human nucleolar protein fibrillarin and its functional expression in yeast. J Cell Biol. 1991 May;113(4):715-29. [PubMed Link Image]
  3. Goshima N, Kawamura Y, Fukumoto A, Miura A, Honma R, Satoh R, Wakamatsu A, Yamamoto J, Kimura K, Nishikawa T, Andoh T, Iida Y, Ishikawa K, Ito E, Kagawa N, Kaminaga C, Kanehori K, Kawakami B, Kenmochi K, Kimura R, Kobayashi M, Kuroita T, Kuwayama H, Maruyama Y, Matsuo K, Minami K, Mitsubori M, Mori M, Morishita R, Murase A, Nishikawa A, Nishikawa S, Okamoto T, Sakagami N, Sakamoto Y, Sasaki Y, Seki T, Sono S, Sugiyama A, Sumiya T, Takayama T, Takayama Y, Takeda H, Togashi T, Yahata K, Yamada H, Yanagisawa Y, Endo Y, Imamoto F, Kisu Y, Tanaka S, Isogai T, Imai J, Watanabe S, Nomura N: Human protein factory for converting the transcriptome into an in vitro-expressed proteome,. Nat Methods. 2008 Dec;5(12):1011-7. [PubMed Link Image]
  4. 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]
  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. Lischwe MA, Ochs RL, Reddy R, Cook RG, Yeoman LC, Tan EM, Reichlin M, Busch H: Purification and partial characterization of a nucleolar scleroderma antigen (Mr = 34,000; pI, 8.5) rich in NG,NG-dimethylarginine. J Biol Chem. 1985 Nov 15;260(26):14304-10. [PubMed Link Image]
  7. Baserga SJ, Yang XD, Steitz JA: An intact Box C sequence in the U3 snRNA is required for binding of fibrillarin, the protein common to the major family of nucleolar snRNPs. EMBO J. 1991 Sep;10(9):2645-51. [PubMed Link Image]
  8. Yanagida M, Hayano T, Yamauchi Y, Shinkawa T, Natsume T, Isobe T, Takahashi N: Human fibrillarin forms a sub-complex with splicing factor 2-associated p32, protein arginine methyltransferases, and tubulins alpha 3 and beta 1 that is independent of its association with preribosomal ribonucleoprotein complexes. J Biol Chem. 2004 Jan 16;279(3):1607-14. Epub 2003 Oct 28. [PubMed Link Image]
  9. Wang Y, Liu J, Zhao H, Lu W, Zhao J, Yang L, Li N, Du X, Ke Y: Human 1A6/DRIM, the homolog of yeast Utp20, functions in the 18S rRNA processing. Biochim Biophys Acta. 2007 Jun;1773(6):863-8. Epub 2007 Apr 12. [PubMed Link Image]
  10. 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]
  11. 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 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 7398
Enzyme 40 Name Histone-lysine N-methyltransferase MLL
Enzyme 40 Synonyms
  1. ALL-1
  2. CXXC-type zinc finger protein 7
  3. Lysine N-methyltransferase 2A
  4. KMT2A
  5. Trithorax-like protein
  6. Zinc finger protein HRX
  7. MLL cleavage product N320
  8. N-terminal cleavage product of 320 kDa
  9. p320
  10. MLL cleavage product C180
  11. C-terminal cleavage product of 180 kDa
  12. p180
Enzyme 40 Gene Name MLL
Enzyme 40 Protein Sequence >Histone-lysine N-methyltransferase MLL
MAHSCRWRFPARPGTTGGGGGGGRRGLGGAPRQRVPALLLPPGPPVGGGGPGAPPSPPAV
AAAAAAAGSSGAGVPGGAAAASAASSSSASSSSSSSSSASSGPALLRVGPGFDAALQVSA
AIGTNLRRFRAVFGESGGGGGSGEDEQFLGFGSDEEVRVRSPTRSPSVKTSPRKPRGRPR
SGSDRNSAILSDPSVFSPLNKSETKSGDKIKKKDSKSIEKKRGRPPTFPGVKIKITHGKD
ISELPKGNKEDSLKKIKRTPSATFQQATKIKKLRAGKLSPLKSKFKTGKLQIGRKGVQIV
RRRGRPPSTERIKTPSGLLINSELEKPQKVRKDKEGTPPLTKEDKTVVRQSPRRIKPVRI
IPSSKRTDATIAKQLLQRAKKGAQKKIEKEAAQLQGRKVKTQVKNIRQFIMPVVSAISSR
IIKTPRRFIEDEDYDPPIKIARLESTPNSRFSAPSCGSSEKSSAASQHSSQMSSDSSRSS
SPSVDTSTDSQASEEIQVLPEERSDTPEVHPPLPISQSPENESNDRRSRRYSVSERSFGS
RTTKKLSTLQSAPQQQTSSSPPPPLLTPPPPLQPASSISDHTPWLMPPTIPLASPFLPAS
TAPMQGKRKSILREPTFRWTSLKHSRSEPQYFSSAKYAKEGLIRKPIFDNFRPPPLTPED
VGFASGFSASGTAASARLFSPLHSGTRFDMHKRSPLLRAPRFTPSEAHSRIFESVTLPSN
RTSAGTSSSGVSNRKRKRKVFSPIRSEPRSPSHSMRTRSGRLSSSELSPLTPPSSVSSSL
SISVSPLATSALNPTFTFPSHSLTQSGESAEKNQRPRKQTSAPAEPFSSSSPTPLFPWFT
PGSQTERGRNKDKAPEELSKDRDADKSVEKDKSRERDREREKENKRESRKEKRKKGSEIQ
SSSALYPVGRVSKEKVVGEDVATSSSAKKATGRKKSSSHDSGTDITSVTLGDTTAVKTKI
LIKKGRGNLEKTNLDLGPTAPSLEKEKTLCLSTPSSSTVKHSTSSIGSMLAQADKLPMTD
KRVASLLKKAKAQLCKIEKSKSLKQTDQPKAQGQESDSSETSVRGPRIKHVCRRAAVALG
RKRAVFPDDMPTLSALPWEEREKILSSMGNDDKSSIAGSEDAEPLAPPIKPIKPVTRNKA
PQEPPVKKGRRSRRCGQCPGCQVPEDCGVCTNCLDKPKFGGRNIKKQCCKMRKCQNLQWM
PSKAYLQKQAKAVKKKEKKSKTSEKKDSKESSVVKNVVDSSQKPTPSAREDPAPKKSSSE
PPPRKPVEEKSEEGNVSAPGPESKQATTPASRKSSKQVSQPALVIPPQPPTTGPPRKEVP
KTTPSEPKKKQPPPPESGPEQSKQKKVAPRPSIPVKQKPKEKEKPPPVNKQENAGTLNIL
STLSNGNSSKQKIPADGVHRIRVDFKEDCEAENVWEMGGLGILTSVPITPRVVCFLCASS
GHVEFVYCQVCCEPFHKFCLEENERPLEDQLENWCCRRCKFCHVCGRQHQATKQLLECNK
CRNSYHPECLGPNYPTKPTKKKKVWICTKCVRCKSCGSTTPGKGWDAQWSHDFSLCHDCA
KLFAKGNFCPLCDKCYDDDDYESKMMQCGKCDRWVHSKCENLSDEMYEILSNLPESVAYT
CVNCTERHPAEWRLALEKELQISLKQVLTALLNSRTTSHLLRYRQAAKPPDLNPETEESI
PSRSSPEGPDPPVLTEVSKQDDQQPLDLEGVKRKMDQGNYTSVLEFSDDIVKIIQAAINS
DGGQPEIKKANSMVKSFFIRQMERVFPWFSVKKSRFWEPNKVSSNSGMLPNAVLPPSLDH
NYAQWQEREENSHTEQPPLMKKIIPAPKPKGPGEPDSPTPLHPPTPPILSTDRSREDSPE
LNPPPGIEDNRQCALCLTYGDDSANDAGRLLYIGQNEWTHVNCALWSAEVFEDDDGSLKN
VHMAVIRGKQLRCEFCQKPGATVGCCLTSCTSNYHFMCSRAKNCVFLDDKKVYCQRHRDL
IKGEVVPENGFEVFRRVFVDFEGISLRRKFLNGLEPENIHMMIGSMTIDCLGILNDLSDC
EDKLFPIGYQCSRVYWSTTDARKRCVYTCKIVECRPPVVEPDINSTVEHDENRTIAHSPT
SFTESSSKESQNTAEIISPPSPDRPPHSQTSGSCYYHVISKVPRIRTPSYSPTQRSPGCR
PLPSAGSPTPTTHEIVTVGDPLLSSGLRSIGSRRHSTSSLSPQRSKLRIMSPMRTGNTYS
RNNVSSVSTTGTATDLESSAKVVDHVLGPLNSSTSLGQNTSTSSNLQRTVVTVGNKNSHL
DGSSSSEMKQSSASDLVSKSSSLKGEKTKVLSSKSSEGSAHNVAYPGIPKLAPQVHNTTS
RELNVSKIGSFAEPSSVSFSSKEALSFPHLHLRGQRNDRDQHTDSTQSANSSPDEDTEVK
TLKLSGMSNRSSIINEHMGSSSRDRRQKGKKSCKETFKEKHSSKSFLEPGQVTTGEEGNL
KPEFMDEVLTPEYMGQRPCNNVSSDKIGDKGLSMPGVPKAPPMQVEGSAKELQAPRKRTV
KVTLTPLKMENESQSKNALKESSPASPLQIESTSPTEPISASENPGDGPVAQPSPNNTSC
QDSQSNNYQNLPVQDRNLMLPDGPKPQEDGSFKRRYPRRSARARSNMFFGLTPLYGVRSY
GEEDIPFYSSSTGKKRGKRSAEGQVDGADDLSTSDEDDLYYYNFTRTVISSGGEERLASH
NLFREEEQCDLPKISQLDGVDDGTESDTSVTATTRKSSQIPKRNGKENGTENLKIDRPED
AGEKEHVTKSSVGHKNEPKMDNCHSVSRVKTQGQDSLEAQLSSLESSRRVHTSTPSDKNL
LDTYNTELLKSDSDNNNSDDCGNILPSDIMDFVLKNTPSMQALGESPESSSSELLNLGEG
LGLDSNREKDMGLFEVFSQQLPTTEPVDSSVSSSISAEEQFELPLELPSDLSVLTTRSPT
VPSQNPSRLAVISDSGEKRVTITEKSVASSESDPALLSPGVDPTPEGHMTPDHFIQGHMD
ADHISSPPCGSVEQGHGNNQDLTRNSSTPGLQVPVSPTVPIQNQKYVPNSTDSPGPSQIS
NAAVQTTPPHLKPATEKLIVVNQNMQPLYVLQTLPNGVTQKIQLTSSVSSTPSVMETNTS
VLGPMGGGLTLTTGLNPSLPTSQSLFPSASKGLLPMSHHQHLHSFPAATQSSFPPNISNP
PSGLLIGVQPPPDPQLLVSESSQRTDLSTTVATPSSGLKKRPISRLQTRKNKKLAPSSTP
SNIAPSDVVSNMTLINFTPSQLPNHPSLLDLGSLNTSSHRTVPNIIKRSKSSIMYFEPAP
LLPQSVGGTAATAAGTSTISQDTSHLTSGSVSGLASSSSVLNVVSMQTTTTPTSSASVPG
HVTLTNPRLLGTPDIGSISNLLIKASQQSLGIQDQPVALPPSSGMFPQLGTSQTPSTAAI
TAASSICVLPSTQTTGITAASPSGEADEHYQLQHVNQLLASKTGIHSSQRDLDSASGPQV
SNFTQTVDAPNSMGLEQNKALSSAVQASPTSPGGSPSSPSSGQRSASPSVPGPTKPKPKT
KRFQLPLDKGNGKKHKVSHLRTSSSEAHIPDQETTSLTSGTGTPGAEAEQQDTASVEQSS
QKECGQPAGQVAVLPEVQVTQNPANEQESAEPKTVEEEESNFSSPLMLWLQQEQKRKESI
TEKKPKKGLVFEISSDDGFQICAESIEDAWKSLTDKVQEARSNARLKQLSFAGVNGLRML
GILHDAVVFLIEQLSGAKHCRNYKFRFHKPEEANEPPLNPHGSARAEVHLRKSAFDMFNF
LASKHRQPPEYNPNDEEEEEVQLKSARRATSMDLPMPMRFRHLKKTSKEAVGVYRSPIHG
RGLFCKRNIDAGEMVIEYAGNVIRSIQTDKREKYYDSKGIGCYMFRIDDSEVVDATMHGN
AARFINHSCEPNCYSRVINIDGQKHIVIFAMRKIYRGEELTYDYKFPIEDASNKLPCNCG
AKKCRKFLN
Enzyme 40 Number of Residues 3969
Enzyme 40 Molecular Weight 431760.5
Enzyme 40 Theoretical pI 9.56
Enzyme 40 GO Classification
Function
  • DNA binding
  • binding
  • catalytic activity
  • cation binding
  • histone methyltransferase activity (H3-K4 specific)
  • 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
  • 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
  • histone methyltransferase complex
  • intracellular membrane-bounded organelle
  • macromolecular complex
  • membrane-bounded organelle
  • methyltransferase complex
  • nucleus
  • organelle
  • protein complex
Enzyme 40 General Function Involved in DNA binding
Enzyme 40 Specific Function Histone methyltransferase that plays an essential role in early development and hematopoiesis. Catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of 'Lys-4' of histone H3 (H3K4me) complex and acetylation of 'Lys-16' of histone H4 (H4K16ac). In the MLL1/MLL complex, it specifically mediates H3K4me, a specific tag for epigenetic transcriptional activation. Has weak methyltransferase activity by itself, and requires other component of the MLL1/MLL complex to obtain full methyltransferase activity. Has no activity toward histone H3 phosphorylated on 'Thr-3', less activity toward H3 dimethylated on 'Arg-8' or 'Lys-9', while it has higher activity toward H3 acetylated on 'Lys-9'. Required for transcriptional activation of HOXA9. Promotes PPP1R15A-induced apoptosis
Enzyme 40 Pathways Not Available
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 34305635 Link Image
Enzyme 40 UniProtKB/Swiss-Prot ID Q03164 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name MLL1_HUMAN Link Image
Enzyme 40 PDB ID Not Available
Enzyme 40 Cellular Location Not Available
Enzyme 40 Gene Sequence >11910 bp
ATGGCGCACAGCTGTCGGTGGCGCTTCCCCGCCCGACCCGGGACCACCGGGGGCGGCGGC
GGCGGGGGGCGCCGGGGCCTAGGGGGCGCCCCGCGGCAACGCGTCCCGGCCCTGCTGCTT
CCCCCCGGGCCCCCGGTCGGCGGTGGCGGCCCCGGGGCGCCCCCCTCCCCCCCGGCTGTG
GCGGCCGCGGCGGCGGCGGCGGGAAGCAGCGGGGCTGGGGTTCCAGGGGGAGCGGCCGCC
GCCTCAGCAGCCTCCTCGTCGTCCGCCTCGTCTTCGTCTTCGTCATCGTCCTCAGCCTCT
TCAGGGCCGGCCCTGCTCCGGGTGGGCCCGGGCTTCGACGCGGCGCTGCAGGTCTCGGCC
GCCATCGGCACCAACCTGCGCCGGTTCCGGGCCGTGTTTGGGGAGAGCGGCGGGGGAGGC
GGCAGCGGAGAGGATGAGCAATTCTTAGGTTTTGGCTCAGATGAAGAAGTCAGAGTGCGA
AGTCCCACAAGGTCTCCTTCAGTTAAAACTAGTCCTCGAAAACCTCGTGGGAGACCTAGA
AGTGGCTCTGACCGAAATTCAGCTATCCTCTCAGATCCATCTGTGTTTTCCCCTCTAAAT
AAATCAGAGACCAAATCTGGAGATAAGATCAAGAAGAAAGATTCTAAAAGTATAGAAAAG
AAGAGAGGAAGACCTCCCACCTTCCCTGGAGTAAAAATCAAAATAACACATGGAAAGGAC
ATTTCAGAGTTACCAAAGGGAAACAAAGAAGATAGCCTGAAAAAAATTAAAAGGACACCT
TCTGCTACGTTTCAGCAAGCCACAAAGATTAAAAAATTAAGAGCAGGTAAACTCTCTCCT
CTCAAGTCTAAGTTTAAGACAGGGAAGCTTCAAATAGGAAGGAAGGGGGTACAAATTGTA
CGACGGAGAGGAAGGCCTCCATCAACAGAAAGGATAAAGACCCCTTCGGGTCTCCTCATT
AATTCTGAACTGGAAAAGCCCCAGAAAGTCCGGAAAGACAAGGAAGGAACACCTCCACTT
ACAAAAGAAGATAAGACAGTTGTCAGACAAAGCCCTCGAAGGATTAAGCCAGTTAGGATT
ATTCCTTCTTCAAAAAGGACAGATGCAACCATTGCTAAGCAACTCTTACAGAGGGCAAAA
AAGGGGGCTCAAAAGAAAATTGAAAAAGAAGCAGCTCAGCTGCAGGGAAGAAAGGTGAAG
ACACAGGTCAAAAATATTCGACAGTTCATCATGCCTGTTGTCAGTGCTATCTCCTCGCGG
ATCATTAAGACCCCTCGGCGGTTTATAGAGGATGAGGATTATGACCCTCCAATTAAAATT
GCCCGATTAGAGTCTACACCGAATAGTAGATTCAGTGCCCCGTCCTGTGGATCTTCTGAA
AAATCAAGTGCAGCTTCTCAGCACTCCTCTCAAATGTCTTCAGACTCCTCTCGATCTAGT
AGCCCCAGTGTTGATACCTCCACAGACTCTCAGGCTTCTGAGGAGATTCAGGTACTTCCT
GAGGAGCGGAGCGATACCCCTGAAGTTCATCCTCCACTGCCCATTTCCCAGTCCCCAGAA
AATGAGAGTAATGATAGGAGAAGCAGAAGGTATTCAGTGTCGGAGAGAAGTTTTGGATCT
AGAACGACGAAAAAATTATCAACTCTACAAAGTGCCCCCCAGCAGCAGACCTCCTCGTCT
CCACCTCCACCTCTGCTGACTCCACCGCCACCACTGCAGCCAGCCTCCAGTATCTCTGAC
CACACACCTTGGCTTATGCCTCCAACAATCCCCTTAGCATCACCATTTTTGCCTGCTTCC
ACTGCTCCTATGCAAGGGAAGCGAAAATCTATTTTGCGAGAACCGACATTTAGGTGGACT
TCTTTAAAGCATTCTAGGTCAGAGCCACAATACTTTTCCTCAGCAAAGTATGCCAAAGAA
GGTCTTATTCGCAAACCAATATTTGATAATTTCCGACCCCCTCCACTAACTCCCGAGGAC
GTTGGCTTTGCATCTGGTTTTTCTGCATCTGGTACCGCTGCTTCAGCCCGATTGTTTTCG
CCACTCCATTCTGGAACAAGGTTTGATATGCACAAAAGGAGCCCTCTTCTGAGAGCTCCA
AGATTTACTCCAAGTGAGGCTCACTCTAGAATATTTGAGTCTGTAACCTTGCCTAGTAAT
CGAACTTCTGCTGGAACATCTTCTTCAGGAGTATCCAATAGAAAAAGGAAAAGAAAAGTG
TTTAGTCCTATTCGATCTGAACCAAGATCTCCTTCTCACTCCATGAGGACAAGAAGTGGA
AGGCTTAGTAGTTCTGAGCTCTCACCTCTCACCCCCCCGTCTTCTGTCTCTTCCTCGTTA
AGCATTTCTGTTAGTCCTCTTGCCACTAGTGCCTTAAACCCAACTTTTACTTTTCCTTCT
CATTCCCTGACTCAGTCTGGGGAATCTGCAGAGAAAAATCAGAGACCAAGGAAGCAGACT
AGTGCTCCGGCAGAGCCATTTTCATCAAGTAGTCCTACTCCTCTCTTCCCTTGGTTTACC
CCAGGCTCTCAGACTGAAAGAGGGAGAAATAAAGACAAGGCCCCCGAGGAGCTGTCCAAA
GATCGAGATGCTGACAAGAGCGTGGAGAAGGACAAGAGTAGAGAGAGAGACCGGGAGAGA
GAAAAGGAGAATAAGCGGGAGTCAAGGAAAGAGAAAAGGAAAAAGGGATCAGAAATTCAG
AGTAGTTCTGCTTTGTATCCTGTGGGTAGGGTTTCCAAAGAGAAGGTTGTTGGTGAAGAT
GTTGCCACTTCATCTTCTGCCAAAAAAGCAACAGGGCGGAAGAAGTCTTCATCACATGAT
TCTGGGACTGATATTACTTCTGTGACTCTTGGGGATACAACAGCTGTCAAAACCAAAATA
CTTATAAAGAAAGGGAGAGGAAATCTGGAAAAAACCAACTTGGACCTCGGCCCAACTGCC
CCATCCCTGGAGAAGGAGAAAACCCTCTGCCTTTCCACTCCTTCATCTAGCACTGTTAAA
CATTCCACTTCCTCCATAGGCTCCATGTTGGCTCAGGCAGACAAGCTTCCAATGACTGAC
AAGAGGGTTGCCAGCCTCCTAAAAAAGGCCAAAGCTCAGCTCTGCAAGATTGAGAAGAGT
AAGAGTCTTAAACAAACCGACCAGCCCAAAGCACAGGGTCAAGAAAGTGACTCATCAGAG
ACCTCTGTGCGAGGACCCCGGATTAAACATGTCTGCAGAAGAGCAGCTGTTGCCCTTGGC
CGAAAACGAGCTGTGTTTCCTGATGACATGCCCACCCTGAGTGCCTTACCATGGGAAGAA
CGAGAAAAGATTTTGTCTTCCATGGGGAATGATGACAAGTCATCAATTGCTGGCTCAGAA
GATGCTGAACCTCTTGCTCCACCCATCAAACCAATTAAACCTGTCACTAGAAACAAGGCA
CCCCAGGAACCTCCAGTAAAGAAAGGACGTCGATCGAGGCGGTGTGGGCAGTGTCCCGGC
TGCCAGGTGCCTGAGGACTGTGGTGTTTGTACTAATTGCTTAGATAAGCCCAAGTTTGGT
GGTCGCAATATAAAGAAGCAGTGCTGCAAGATGAGAAAATGTCAGAATCTACAATGGATG
CCTTCCAAAGCCTACCTGCAGAAGCAAGCTAAAGCTGTGAAAAAGAAAGAGAAAAAGTCT
AAGACCAGTGAAAAGAAAGACAGCAAAGAGAGCAGTGTTGTGAAGAACGTGGTGGACTCT
AGTCAGAAACCTACCCCATCAGCAAGAGAGGATCCTGCCCCAAAGAAAAGCAGTAGTGAG
CCTCCTCCACGAAAGCCCGTCGAGGAAAAGAGTGAAGAAGGGAATGTCTCGGCCCCTGGG
CCTGAATCCAAACAGGCCACCACTCCAGCTTCCAGGAAGTCAAGCAAGCAGGTCTCCCAG
CCAGCACTGGTCATCCCGCCTCAGCCACCTACTACAGGACCGCCAAGAAAAGAAGTTCCC
AAAACCACTCCTAGTGAGCCCAAGAAAAAGCAGCCTCCACCACCAGAATCAGGTCCAGAG
CAGAGCAAACAGAAAAAAGTGGCTCCCCGCCCAAGTATCCCTGTAAAACAAAAACCAAAA
GAAAAGGAAAAACCACCTCCGGTCAATAAGCAGGAGAATGCAGGCACTTTGAACATCCTC
AGCACTCTCTCCAATGGCAATAGTTCTAAGCAAAAAATTCCAGCAGATGGAGTCCACAGG
ATCAGAGTGGACTTTAAGGAGGATTGTGAAGCAGAAAATGTGTGGGAGATGGGAGGCTTA
GGAATCTTGACTTCTGTTCCTATAACACCCAGGGTGGTTTGCTTTCTCTGTGCCAGTAGT
GGGCATGTAGAGTTTGTGTATTGCCAAGTCTGTTGTGAGCCCTTCCACAAGTTTTGTTTA
GAGGAGAACGAGCGCCCTCTGGAGGACCAGCTGGAAAATTGGTGTTGTCGTCGTTGCAAA
TTCTGTCACGTTTGTGGAAGGCAACATCAGGCTACAAAGCAGCTGCTGGAGTGTAATAAG
TGCCGAAACAGCTATCACCCTGAGTGCCTGGGACCAAACTACCCCACCAAACCCACAAAG
AAGAAGAAAGTCTGGATCTGTACCAAGTGTGTTCGCTGTAAGAGCTGTGGATCCACAACT
CCAGGCAAAGGGTGGGATGCACAGTGGTCTCATGATTTCTCACTGTGTCATGATTGCGCC
AAGCTCTTTGCTAAAGGAAACTTCTGCCCTCTCTGTGACAAATGTTATGATGATGATGAC
TATGAGAGTAAGATGATGCAATGTGGAAAGTGTGATCGCTGGGTCCATTCCAAATGTGAG
AATCTTTCAGATGAGATGTATGAGATTCTATCTAATCTGCCAGAAAGTGTGGCCTACACT
TGTGTGAACTGTACTGAGCGGCACCCTGCAGAGTGGCGACTGGCCCTTGAAAAAGAGCTG
CAGATTTCTCTGAAGCAAGTTCTGACAGCTTTGTTGAATTCTCGGACTACCAGCCATTTG
CTACGCTACCGGCAGGCTGCCAAGCCTCCAGACTTAAATCCCGAGACAGAGGAGAGTATA
CCTTCCCGCAGCTCCCCCGAAGGACCTGATCCACCAGTTCTTACTGAGGTCAGCAAACAG
GATGATCAGCAGCCTTTAGATCTAGAAGGAGTCAAGAGGAAGATGGACCAAGGGAATTAC
ACATCTGTGTTGGAGTTCAGTGATGATATTGTGAAGATCATTCAAGCAGCCATTAATTCA
GATGGAGGACAGCCAGAAATTAAAAAAGCCAACAGCATGGTCAAGTCCTTCTTCATTCGG
CAAATGGAACGTGTTTTTCCATGGTTCAGTGTCAAAAAGTCCAGGTTTTGGGAGCCAAAT
AAAGTATCAAGCAACAGTGGGATGTTACCAAACGCAGTGCTTCCACCTTCACTTGACCAT
AATTATGCTCAGTGGCAGGAGCGAGAGGAAAACAGCCACACTGAGCAGCCTCCTTTAATG
AAGAAAATCATTCCAGCTCCCAAACCCAAAGGTCCTGGAGAACCAGACTCACCAACTCCT
CTGCATCCTCCTACACCACCAATTTTGAGTACTGATAGGAGTCGAGAAGACAGTCCAGAG
CTGAACCCACCCCCAGGCATAGAAGACAATAGACAGTGTGCGTTATGTTTGACTTATGGT
GATGACAGTGCTAATGATGCTGGTCGTTTACTATATATTGGCCAAAATGAGTGGACACAT
GTAAATTGTGCTTTGTGGTCAGCGGAAGTGTTTGAAGATGATGACGGATCACTAAAGAAT
GTGCATATGGCTGTGATCAGGGGCAAGCAGCTGAGATGTGAATTCTGCCAAAAGCCAGGA
GCCACCGTGGGTTGCTGTCTCACATCCTGCACCAGCAACTATCACTTCATGTGTTCCCGA
GCCAAGAACTGTGTCTTTCTGGATGATAAAAAAGTATATTGCCAACGACATCGGGATTTG
ATCAAAGGCGAAGTGGTTCCTGAGAATGGATTTGAAGTTTTCAGAAGAGTGTTTGTGGAC
TTTGAAGGAATCAGCTTGAGAAGGAAGTTTCTCAATGGCTTGGAACCAGAAAATATCCAC
ATGATGATTGGGTCTATGACAATCGACTGCTTAGGAATTCTAAATGATCTCTCCGACTGT
GAAGATAAGCTCTTTCCTATTGGATATCAGTGTTCCAGGGTATACTGGAGCACCACAGAT
GCTCGCAAGCGCTGTGTATATACATGCAAGATAGTGGAGTGCCGTCCTCCAGTCGTAGAG
CCGGATATCAACAGCACTGTTGAACATGATGAAAACAGGACCATTGCCCATAGTCCAACA
TCTTTTACAGAAAGTTCATCAAAAGAGAGTCAAAACACAGCTGAAATTATAAGTCCTCCA
TCACCAGACCGACCTCCTCATTCACAAACCTCTGGCTCCTGTTATTATCATGTCATCTCA
AAGGTCCCCAGGATTCGAACACCCAGTTATTCTCCAACACAGAGATCCCCTGGCTGTCGA
CCGTTGCCTTCTGCAGGAAGTCCTACCCCAACCACTCATGAAATAGTCACAGTAGGTGAT
CCTTTACTCTCCTCTGGACTTCGAAGCATTGGCTCCAGGCGTCACAGTACCTCTTCCTTA
TCACCCCAGCGGTCCAAACTCCGGATAATGTCTCCAATGAGAACTGGGAATACTTACTCT
AGGAATAATGTTTCCTCAGTCTCCACCACCGGGACCGCTACTGATCTTGAATCAAGTGCC
AAAGTAGTTGATCATGTCTTAGGGCCACTGAATTCAAGTACTAGTTTAGGGCAAAACACT
TCCACCTCTTCAAATTTGCAAAGGACAGTGGTTACTGTAGGCAATAAAAACAGTCACTTG
GATGGATCTTCATCTTCAGAAATGAAGCAGTCCAGTGCTTCAGACTTGGTGTCCAAGAGC
TCCTCTTTAAAGGGAGAGAAGACCAAAGTGCTGAGTTCCAAGAGCTCAGAGGGATCTGCA
CATAATGTGGCTTACCCTGGAATTCCTAAACTGGCCCCACAGGTTCATAACACAACATCT
AGAGAACTGAATGTTAGTAAAATCGGCTCCTTTGCTGAACCCTCTTCAGTGTCGTTTTCT
TCTAAAGAGGCCCTCTCCTTCCCACACCTCCATTTGAGAGGGCAAAGGAATGATCGAGAC
CAACACACAGATTCTACCCAATCAGCAAACTCCTCTCCAGATGAAGATACTGAAGTCAAA
ACCTTGAAGCTATCTGGAATGAGCAACAGATCATCCATTATCAACGAACATATGGGATCT
AGTTCCAGAGATAGGAGACAGAAAGGGAAAAAATCCTGTAAAGAAACTTTCAAAGAAAAG
CATTCCAGTAAATCTTTTTTGGAACCTGGTCAGGTGACAACTGGTGAGGAAGGAAACTTG
AAGCCAGAGTTTATGGATGAGGTTTTGACTCCTGAGTATATGGGCCAACGACCATGTAAC
AATGTTTCTTCTGATAAGATTGGTGATAAAGGCCTTTCTATGCCAGGAGTCCCCAAAGCT
CCACCCATGCAAGTAGAAGGATCTGCCAAGGAATTACAGGCACCACGGAAACGCACAGTC
AAAGTGACACTGACACCTCTAAAAATGGAAAATGAGAGTCAATCCAAAAATGCCCTGAAA
GAAAGTAGTCCTGCTTCCCCTTTGCAAATAGAGTCAACATCTCCCACAGAACCAATTTCA
GCCTCTGAAAATCCAGGAGATGGTCCAGTGGCCCAACCAAGCCCCAATAATACCTCATGC
CAGGATTCTCAAAGTAACAACTATCAGAATCTTCCAGTACAGGACAGAAACCTAATGCTT
CCAGATGGCCCCAAACCTCAGGAGGATGGCTCTTTTAAAAGGAGGTATCCCCGTCGCAGT
GCCCGTGCACGTTCTAACATGTTTTTTGGGCTTACCCCACTCTATGGAGTAAGATCCTAT
GGTGAAGAAGACATTCCATTCTACAGCAGCTCAACTGGGAAGAAGCGAGGCAAGAGATCA
GCTGAAGGACAGGTGGATGGGGCCGATGACTTAAGCACTTCAGATGAAGACGACTTATAC
TATTACAACTTCACTAGAACAGTGATTTCTTCAGGTGGAGAGGAACGACTGGCATCCCAT
AATTTATTTCGGGAGGAGGAACAGTGTGATCTTCCAAAAATCTCACAGTTGGATGGTGTT
GATGATGGGACAGAGAGTGATACTAGTGTCACAGCCACAACAAGGAAAAGCAGCCAGATT
CCAAAAAGAAATGGTAAAGAAAATGGAACAGAGAACTTAAAGATTGATAGACCTGAAGAT
GCTGGGGAGAAAGAACATGTCACTAAGAGTTCTGTTGGCCACAAAAATGAGCCAAAGATG
GATAACTGCCATTCTGTAAGCAGAGTTAAAACACAGGGACAAGATTCCTTGGAAGCTCAG
CTCAGCTCATTGGAGTCAAGCCGCAGAGTCCACACAAGTACCCCCTCCGACAAAAATTTA
CTGGACACCTATAATACTGAGCTCCTGAAATCAGATTCAGACAATAACAACAGTGATGAC
TGTGGGAATATCCTGCCTTCAGACATTATGGACTTTGTACTAAAGAATACTCCATCCATG
CAGGCTTTGGGTGAGAGCCCAGAGTCATCTTCATCAGAACTCCTGAATCTTGGTGAAGGA
TTGGGTCTTGACAGTAATCGTGAAAAAGACATGGGTCTTTTTGAAGTATTTTCTCAGCAG
CTGCCTACAACAGAACCTGTGGATAGTAGTGTCTCTTCCTCTATCTCAGCAGAGGAACAG
TTTGAGTTGCCTCTAGAGCTACCATCTGATCTGTCTGTCTTGACCACCCGGAGTCCCACT
GTCCCCAGCCAGAATCCCAGTAGACTAGCTGTTATCTCAGACTCAGGGGAGAAGAGAGTA
ACCATCACAGAAAAATCTGTAGCCTCCTCTGAAAGTGACCCAGCACTGCTGAGCCCAGGA
GTAGATCCAACTCCTGAAGGCCACATGACTCCTGATCATTTTATCCAAGGACACATGGAT
GCAGACCACATCTCTAGCCCTCCTTGTGGTTCAGTAGAGCAAGGTCATGGCAACAATCAG
GATTTAACTAGGAACAGTAGCACCCCTGGCCTTCAGGTACCTGTTTCCCCAACTGTTCCC
ATCCAGAACCAGAAGTATGTGCCCAATTCTACTGATAGTCCTGGCCCGTCTCAGATTTCC
AATGCAGCTGTCCAGACCACTCCACCCCACCTGAAGCCAGCCACTGAGAAACTCATAGTT
GTTAACCAGAACATGCAGCCACTTTATGTTCTCCAAACTCTTCCAAATGGAGTGACCCAA
AAAATCCAATTGACCTCTTCTGTTAGTTCTACACCCAGTGTGATGGAGACAAATACTTCA
GTATTGGGACCCATGGGAGGTGGTCTCACCCTTACCACAGGACTAAATCCAAGCTTGCCA
ACTTCTCAATCTTTGTTCCCTTCTGCTAGCAAAGGATTGCTACCCATGTCTCATCACCAG
CACTTACATTCCTTCCCTGCAGCTACTCAAAGTAGTTTCCCACCAAACATCAGCAATCCT
CCTTCAGGCCTGCTTATTGGGGTTCAGCCTCCTCCGGATCCCCAACTTTTGGTTTCAGAA
TCCAGCCAGAGGACAGACCTCAGTACCACAGTAGCCACTCCATCCTCTGGACTCAAGAAA
AGACCCATATCTCGTCTACAGACCCGAAAGAATAAAAAACTTGCTCCCTCTAGTACCCCT
TCAAACATTGCCCCTTCTGATGTGGTTTCTAATATGACATTGATTAACTTCACACCCTCC
CAGCTTCCTAATCATCCAAGTCTGTTAGATTTGGGGTCACTTAATACTTCATCTCACCGA
ACTGTCCCCAACATCATAAAAAGATCTAAATCTAGCATCATGTATTTTGAACCGGCACCC
CTGTTACCACAGAGTGTGGGAGGAACTGCTGCCACAGCGGCAGGCACATCAACAATAAGC
CAGGATACTAGCCACCTCACATCAGGGTCTGTGTCTGGCTTGGCATCCAGTTCCTCTGTC
TTGAATGTTGTATCCATGCAAACTACCACAACCCCTACAAGTAGTGCGTCAGTTCCAGGA
CACGTCACCTTAACCAACCCAAGGTTGCTTGGTACCCCAGATATTGGCTCAATAAGCAAT
CTTTTAATCAAAGCTAGCCAGCAGAGCCTGGGGATTCAGGACCAGCCTGTGGCTTTACCG
CCAAGTTCAGGAATGTTTCCACAACTGGGGACATCACAGACCCCCTCTACTGCTGCAATA
ACAGCGGCATCTAGCATCTGTGTGCTCCCCTCCACTCAGACTACGGGCATAACAGCCGCT
TCACCTTCTGGGGAAGCAGACGAACACTATCAGCTTCAGCATGTGAACCAGCTCCTTGCC
AGCAAAACTGGGATTCATTCTTCCCAGCGTGATCTTGATTCTGCTTCAGGGCCCCAGGTA
TCCAACTTTACCCAGACGGTAGACGCTCCTAATAGCATGGGACTGGAGCAGAACAAGGCT
TTATCCTCAGCTGTGCAAGCCAGCCCCACCTCTCCTGGGGGTTCTCCATCCTCTCCATCT
TCTGGACAGCGGTCAGCAAGCCCTTCAGTGCCGGGTCCCACTAAACCCAAACCAAAAACC
AAACGGTTTCAGCTGCCTCTAGACAAAGGGAATGGCAAGAAGCACAAAGTTTCCCATTTG
CGGACCAGTTCTTCTGAAGCACACATTCCAGACCAAGAAACGACATCCCTGACCTCAGGC
ACAGGGACTCCAGGAGCAGAGGCTGAGCAGCAGGATACAGCTAGCGTGGAGCAGTCCTCC
CAGAAGGAGTGTGGGCAACCTGCAGGGCAAGTCGCTGTTCTTCCGGAAGTTCAGGTGACC
CAAAATCCAGCAAATGAACAAGAAAGTGCAGAACCTAAAACAGTGGAAGAAGAGGAAAGT
AATTTCAGCTCCCCACTGATGCTTTGGCTTCAGCAAGAACAAAAGCGGAAGGAAAGCATT
ACTGAGAAAAAACCCAAGAAAGGACTTGTTTTTGAAATTTCCAGTGATGATGGCTTTCAG
ATCTGTGCAGAAAGTATTGAAGATGCCTGGAAGTCATTGACAGATAAAGTCCAGGAAGCT
CGATCAAATGCCCGCCTAAAGCAGCTCTCATTTGCAGGTGTTAACGGTTTGAGGATGCTG
GGGATTCTCCATGATGCAGTTGTGTTCCTCATTGAGCAGCTGTCTGGTGCCAAGCACTGT
CGAAATTACAAATTCCGTTTCCACAAGCCAGAGGAGGCCAATGAACCCCCCTTGAACCCT
CACGGCTCAGCCAGGGCTGAAGTCCACCTCAGGAAGTCAGCATTTGACATGTTTAACTTC
CTGGCTTCTAAACATCGTCAGCCTCCTGAATACAACCCCAATGATGAAGAAGAGGAGGAG
GTACAGCTGAAGTCAGCTCGGAGGGCAACTAGCATGGATCTGCCAATGCCCATGCGCTTC
CGGCACTTAAAAAAGACTTCTAAGGAGGCAGTTGGTGTCTACAGGTCTCCCATCCATGGC
CGGGGTCTTTTCTGTAAGAGAAACATTGATGCAGGTGAGATGGTGATTGAGTATGCCGGC
AACGTCATCCGCTCCATCCAGACTGACAAGCGGGAAAAGTATTACGACAGCAAGGGCATT
GGTTGCTATATGTTCCGAATTGATGACTCAGAGGTAGTGGATGCCACCATGCATGGAAAT
GCTGCACGCTTCATCAATCACTCGTGTGAGCCTAACTGCTATTCTCGGGTCATCAATATT
GATGGGCAGAAGCACATTGTCATCTTTGCCATGCGTAAGATCTACCGAGGAGAGGAACTC
ACTTACGACTATAAGTTCCCCATTGAGGATGCCAGCAACAAGCTGCCCTGCAACTGTGGC
GCCAAGAAATGCCGGAAGTTCCTAAACTAA
Enzyme 40 GenBank Gene ID AY373585 Link Image
Enzyme 40 GeneCard ID MLL Link Image
Enzyme 40 GenAtlas ID MLL Link Image
Enzyme 40 HGNC ID HGNC:7132 Link Image
Enzyme 40 Chromosome Location 1
Enzyme 40 Locus 11q23
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 General References
  1. Tkachuk DC, Kohler S, Cleary ML: Involvement of a homolog of Drosophila trithorax by 11q23 chromosomal translocations in acute leukemias. Cell. 1992 Nov 13;71(4):691-700. [PubMed Link Image]
  2. Nilson I, Lochner K, Siegler G, Greil J, Beck JD, Fey GH, Marschalek R: Exon/intron structure of the human ALL-1 (MLL) gene involved in translocations to chromosomal region 11q23 and acute leukaemias. Br J Haematol. 1996 Jun;93(4):966-72. [PubMed Link Image]
  3. Yamamoto K, Seto M, Komatsu H, Iida S, Akao Y, Kojima S, Kodera Y, Nakazawa S, Ariyoshi Y, Takahashi T, et al.: Two distinct portions of LTG19/ENL at 19p13 are involved in t(11;19) leukemia. Oncogene. 1993 Oct;8(10):2617-25. [PubMed Link Image]
  4. Gu Y, Nakamura T, Alder H, Prasad R, Canaani O, Cimino G, Croce CM, Canaani E: The t(4;11) chromosome translocation of human acute leukemias fuses the ALL-1 gene, related to Drosophila trithorax, to the AF-4 gene. Cell. 1992 Nov 13;71(4):701-8. [PubMed Link Image]
  5. Djabali M, Selleri L, Parry P, Bower M, Young BD, Evans GA: A trithorax-like gene is interrupted by chromosome 11q23 translocations in acute leukaemias. Nat Genet. 1992 Oct;2(2):113-8. [PubMed Link Image]
  6. Djabali M, Selleri L, Parry P, Bower M, Young B, Evans GA: A trithorax-like gene is interrupted by chromosome 11q23 translocations in acute leukaemias. Nat Genet. 1993 Aug;4(4):431. [PubMed Link Image]
  7. Marschalek R, Greil J, Lochner K, Nilson I, Siegler G, Zweckbronner I, Beck JD, Fey GH: Molecular analysis of the chromosomal breakpoint and fusion transcripts in the acute lymphoblastic SEM cell line with chromosomal translocation t(4;11). Br J Haematol. 1995 Jun;90(2):308-20. [PubMed Link Image]
  8. Mbangkollo D, Burnett R, McCabe N, Thirman M, Gill H, Yu H, Rowley JD, Diaz MO: The human MLL gene: nucleotide sequence, homology to the Drosophila trx zinc-finger domain, and alternative splicing. DNA Cell Biol. 1995 Jun;14(6):475-83. [PubMed Link Image]
  9. Gu Y, Alder H, Nakamura T, Schichman SA, Prasad R, Canaani O, Saito H, Croce CM, Canaani E: Sequence analysis of the breakpoint cluster region in the ALL-1 gene involved in acute leukemia. Cancer Res. 1994 May 1;54(9):2326-30. [PubMed Link Image]
  10. Forster A, Rabbitts TH: A method for identifying genes within yeast artificial chromosomes: application to isolation of MLL fusion cDNAs from acute leukaemia translocations. Oncogene. 1993 Nov;8(11):3157-60. [PubMed Link Image]
  11. Hsieh JJ, Ernst P, Erdjument-Bromage H, Tempst P, Korsmeyer SJ: Proteolytic cleavage of MLL generates a complex of N- and C-terminal fragments that confers protein stability and subnuclear localization. Mol Cell Biol. 2003 Jan;23(1):186-94. [PubMed Link Image]
  12. Taki T, Hayashi Y, Taniwaki M, Seto M, Ueda R, Hanada R, Suzukawa K, Yokota J, Morishita K: Fusion of the MLL gene with two different genes, AF-6 and AF-5alpha, by a complex translocation involving chromosomes 5, 6, 8 and 11 in infant leukemia. Oncogene. 1996 Nov 21;13(10):2121-30. [PubMed Link Image]
  13. Taki T, Shibuya N, Taniwaki M, Hanada R, Morishita K, Bessho F, Yanagisawa M, Hayashi Y: ABI-1, a human homolog to mouse Abl-interactor 1, fuses the MLL gene in acute myeloid leukemia with t(10;11)(p11.2;q23). Blood. 1998 Aug 15;92(4):1125-30. [PubMed Link Image]
  14. Cui X, De Vivo I, Slany R, Miyamoto A, Firestein R, Cleary ML: Association of SET domain and myotubularin-related proteins modulates growth control. Nat Genet. 1998 Apr;18(4):331-7. [PubMed Link Image]
  15. Adler HT, Chinery R, Wu DY, Kussick SJ, Payne JM, Fornace AJ Jr, Tkachuk DC: Leukemic HRX fusion proteins inhibit GADD34-induced apoptosis and associate with the GADD34 and hSNF5/INI1 proteins. Mol Cell Biol. 1999 Oct;19(10):7050-60. [PubMed Link Image]
  16. Taki T, Kano H, Taniwaki M, Sako M, Yanagisawa M, Hayashi Y: AF5q31, a newly identified AF4-related gene, is fused to MLL in infant acute lymphoblastic leukemia with ins(5;11)(q31;q13q23). Proc Natl Acad Sci U S A. 1999 Dec 7;96(25):14535-40. [PubMed Link Image]
  17. Sano K, Hayakawa A, Piao JH, Kosaka Y, Nakamura H: Novel SH3 protein encoded by the AF3p21 gene is fused to the mixed lineage leukemia protein in a therapy-related leukemia with t(3;11) (p21;q23). Blood. 2000 Feb 1;95(3):1066-8. [PubMed Link Image]
  18. Pegram LD, Megonigal MD, Lange BJ, Nowell PC, Rowley JD, Rappaport EF, Felix CA: t(3;11) translocation in treatment-related acute myeloid leukemia fuses MLL with the GMPS (GUANOSINE 5' MONOPHOSPHATE SYNTHETASE) gene. Blood. 2000 Dec 15;96(13):4360-2. [PubMed Link Image]
  19. Megonigal MD, Cheung NK, Rappaport EF, Nowell PC, Wilson RB, Jones DH, Addya K, Leonard DG, Kushner BH, Williams TM, Lange BJ, Felix CA: Detection of leukemia-associated MLL-GAS7 translocation early during chemotherapy with DNA topoisomerase II inhibitors. Proc Natl Acad Sci U S A. 2000 Mar 14;97(6):2814-9. [PubMed Link Image]
  20. Daheron L, Veinstein A, Brizard F, Drabkin H, Lacotte L, Guilhot F, Larsen CJ, Brizard A, Roche J: Human LPP gene is fused to MLL in a secondary acute leukemia with a t(3;11) (q28;q23). Genes Chromosomes Cancer. 2001 Aug;31(4):382-9. [PubMed Link Image]
  21. Ono R, Taki T, Taketani T, Taniwaki M, Kobayashi H, Hayashi Y: LCX, leukemia-associated protein with a CXXC domain, is fused to MLL in acute myeloid leukemia with trilineage dysplasia having t(10;11)(q22;q23). Cancer Res. 2002 Jul 15;62(14):4075-80. [PubMed Link Image]
  22. Nakamura T, Mori T, Tada S, Krajewski W, Rozovskaia T, Wassell R, Dubois G, Mazo A, Croce CM, Canaani E: ALL-1 is a histone methyltransferase that assembles a supercomplex of proteins involved in transcriptional regulation. Mol Cell. 2002 Nov;10(5):1119-28. [PubMed Link Image]
  23. Hsieh JJ, Cheng EH, Korsmeyer SJ: Taspase1: a threonine aspartase required for cleavage of MLL and proper HOX gene expression. Cell. 2003 Oct 31;115(3):293-303. [PubMed Link Image]
  24. Chinwalla V, Chien A, Odero M, Neilly MB, Zeleznik-Le NJ, Rowley JD: A t(11;15) fuses MLL to two different genes, AF15q14 and a novel gene MPFYVE on chromosome 15. Oncogene. 2003 Mar 6;22(9):1400-10. [PubMed Link Image]
  25. Kuefer MU, Chinwalla V, Zeleznik-Le NJ, Behm FG, Naeve CW, Rakestraw KM, Mukatira ST, Raimondi SC, Morris SW: Characterization of the MLL partner gene AF15q14 involved in t(11;15)(q23;q14). Oncogene. 2003 Mar 6;22(9):1418-24. [PubMed Link Image]
  26. von Bergh AR, Wijers PM, Groot AJ, van Zelderen-Bhola S, Falkenburg JH, Kluin PM, Schuuring E: Identification of a novel RAS GTPase-activating protein (RASGAP) gene at 9q34 as an MLL fusion partner in a patient with de novo acute myeloid leukemia. Genes Chromosomes Cancer. 2004 Apr;39(4):324-34. [PubMed Link Image]
  27. Kojima K, Sakai I, Hasegawa A, Niiya H, Azuma T, Matsuo Y, Fujii N, Tanimoto M, Fujita S: FLJ10849, a septin family gene, fuses MLL in a novel leukemia cell line CNLBC1 derived from chronic neutrophilic leukemia in transformation with t(4;11)(q21;q23). Leukemia. 2004 May;18(5):998-1005. [PubMed Link Image]
  28. Yokoyama A, Wang Z, Wysocka J, Sanyal M, Aufiero DJ, Kitabayashi I, Herr W, Cleary ML: Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression. Mol Cell Biol. 2004 Jul;24(13):5639-49. [PubMed Link Image]
  29. 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]
  30. Hayette S, Cornillet-Lefebvre P, Tigaud I, Struski S, Forissier S, Berchet A, Doll D, Gillot L, Brahim W, Delabesse E, Magaud JP, Rimokh R: AF4p12, a human homologue to the furry gene of Drosophila, as a novel MLL fusion partner. Cancer Res. 2005 Aug 1;65(15):6521-5. [PubMed Link Image]
  31. Dou Y, Milne TA, Tackett AJ, Smith ER, Fukuda A, Wysocka J, Allis CD, Chait BT, Hess JL, Roeder RG: Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF. Cell. 2005 Jun 17;121(6):873-85. [PubMed Link Image]
  32. 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]
  33. 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]
  34. Cho YW, Hong T, Hong S, Guo H, Yu H, Kim D, Guszczynski T, Dressler GR, Copeland TD, Kalkum M, Ge K: PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex. J Biol Chem. 2007 Jul 13;282(28):20395-406. Epub 2007 May 11. [PubMed Link Image]
  35. 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]
  36. 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]
  37. 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]
  38. 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]
  39. 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]
  40. 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]
  41. Patel A, Dharmarajan V, Vought VE, Cosgrove MS: On the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complex. J Biol Chem. 2009 Sep 4;284(36):24242-56. Epub 2009 Jun 25. [PubMed Link Image]
  42. 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]
  43. 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]
  44. 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]
  45. Allen MD, Grummitt CG, Hilcenko C, Min SY, Tonkin LM, Johnson CM, Freund SM, Bycroft M, Warren AJ: Solution structure of the nonmethyl-CpG-binding CXXC domain of the leukaemia-associated MLL histone methyltransferase. EMBO J. 2006 Oct 4;25(19):4503-12. Epub 2006 Sep 21. [PubMed Link Image]
  46. De Guzman RN, Goto NK, Dyson HJ, Wright PE: Structural basis for cooperative transcription factor binding to the CBP coactivator. J Mol Biol. 2006 Feb 3;355(5):1005-13. Epub 2005 Oct 5. [PubMed Link Image]
  47. Patel A, Dharmarajan V, Cosgrove MS: Structure of WDR5 bound to mixed lineage leukemia protein-1 peptide. J Biol Chem. 2008 Nov 21;283(47):32158-61. Epub 2008 Oct 1. [PubMed Link Image]
  48. Southall SM, Wong PS, Odho Z, Roe SM, Wilson JR: Structural basis for the requirement of additional factors for MLL1 SET domain activity and recognition of epigenetic marks. Mol Cell. 2009 Jan 30;33(2):181-91. [PubMed Link Image]
Enzyme 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 7474
Enzyme 41 Name Molybdenum cofactor biosynthesis protein 1 A
Enzyme 41 Synonyms
  1. MOCS1A
Enzyme 41 Gene Name MOCS1
Enzyme 41 Protein Sequence >Molybdenum cofactor biosynthesis protein 1 A
MAARPLSRMLRRLLRSSARSCSSGAPVTQPCPGESARAASEEVSRRRQFLREHAAPFSAF
LTDSFGRQHSYLRISLTEKCNLRCQYCMPEEGVPLTPKANLLTTEEILTLARLFVKEGID
KIRLTGGEPLIRPDVVDIVAQLQRLEGLRTIGVTTNGINLARLLPQLQKAGLSAINISLD
TLVPAKFEFIVRRKGFHKVMEGIHKAIELGYNPVKVNCVVMRGLNEDELLDFAALTEGLP
LDVRFIEYMPFDGNKWNFKKMVSYKEMLDTVRQQWPELEKVPEEESSTAKAFKIPGFQGQ
ISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEQELLRIIGAAVG
RKKRQHAGMFSISQMKNRPMILIGG
Enzyme 41 Number of Residues 385
Enzyme 41 Molecular Weight 43089
Enzyme 41 Theoretical pI 9.78
Enzyme 41 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • transition metal ion binding
Process
  • Mo-molybdopterin cofactor biosynthesis
  • cellular metabolism
  • coenzyme biosynthesis
  • coenzyme metabolism
  • cofactor metabolism
  • metabolism
  • physiological process
Component
  • molybdopterin synthase complex
  • protein complex
  • unlocalized protein complex
Enzyme 41 General Function Coenzyme transport and metabolism
Enzyme 41 Specific Function Involved in the biosynthesis of molybdopterin precursor Z from guanosine
Enzyme 41 Pathways Not Available
Enzyme 41 Reactions Not Available
Enzyme 41 Pfam Domain Function
Enzyme 41 Signals
  • None
Enzyme 41 Transmembrane Regions
  • None
Enzyme 41 Essentiality Not Available
Enzyme 41 GenBank ID Protein 2645879 Link Image
Enzyme 41 UniProtKB/Swiss-Prot ID O14940 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name MOS1A_HUMAN Link Image
Enzyme 41 PDB ID Not Available
Enzyme 41 Cellular Location Not Available
Enzyme 41 Gene Sequence >1158 bp
ATGGCGGCGCGGCCACTGTCCCGGATGCTGCGGCGGCTTCTGAGGTCCAGCGCCCGGAGC
TGCAGCTCAGGGGCTCCGGTGACCCAGCCCTGCCCCGGGGAGTCCGCGCGAGCTGCCTCG
GAGGAGGTGTCCAGGCGGAGGCAGTTCCTGCGGGAGCATGCGGCCCCCTTCTCCGCCTTC
CTCACAGACAGCTTCGGCCGGCAGCACAGCTACCTGCGGATCTCCCTCACAGAGAAGTGC
AACCTCAGATGTCAGTACTGCATGCCCGAGGAGGGGGTCCCGCTGACCCCCAAAGCCAAC
CTGCTGACCACAGAGGAGATCCTGACCCTCGCCCGGCTCTTTGTGAAGGAAGGCATCGAC
AAGATCCGGCTCACAGGTGGAGAGCCGCTTATCCGGCCGGACGTGGTGGACATTGTGGCC
CAGCTCCAGCGGCTGGAAGGGCTGAGAACCATAGGTGTTACCACCAATGGCATCAACCTG
GCCCGGCTACTGCCCCAGCTTCAGAAGGCTGGTCTCAGTGCCATCAACATCAGCCTGGAC
ACCCTGGTGCCTGCCAAGTTTGAGTTCATTGTCCGCAGGAAAGGCTTCCACAAGGTCATG
GAGGGCATCCACAAGGCCATCGAGCTGGGCTACAACCCTGTGAAGGTGAACTGTGTGGTG
ATGCGAGGCCTTAACGAGGATGAACTCCTGGACTTTGCGGCCTTGACTGAGGGCCACCCC
CTGGATGTGCGCTTCATAGAGTATATGCCCTTTGATGGCAACAAGTGGAACTTCAAGAAG
ATGGTCAGCTATAAGGAGATGCTAGACACTGTCCGGCAGCAGTGGCCAGAGCTGGAGAAG
GTGCCAGAGGAGGAATCCAGCACAGCCAAGGCCTTTAAAATCCCTGGCTTCCAAGGCCAG
ATCAGCTTCATCACATCCATGTCTGAGCATTTCTGTGGGACCTGCAACCGCCTGCGAATC
ACAGCTGATGGGAACCTCAAGGTCTGCCTCTTTGGAAACTCTGAGGTATCCCTGCGGGAT
CACCTGCGAGCTGGGGCCTCTGAGCAGGAGCTGCTGAGAATCATTGGGGCTGCTGTGGGC
AGGAAGAAGCGGCAGCATGCAGGCATGTTCAGTATTTCCCAGATGAAGAACCGGCCCATG
ATCCTCATCGGTGGGTGA
Enzyme 41 GenBank Gene ID AF034374 Link Image
Enzyme 41 GeneCard ID MOCS1 Link Image
Enzyme 41 GenAtlas ID MOCS1 Link Image
Enzyme 41 HGNC ID HGNC:7190 Link Image
Enzyme 41 Chromosome Location 6
Enzyme 41 Locus 6p21.3
Enzyme 41 SNPs SNPJam Report Link Image
Enzyme 41 General References
  1. Reiss J, Cohen N, Dorche C, Mandel H, Mendel RR, Stallmeyer B, Zabot MT, Dierks T: Mutations in a polycistronic nuclear gene associated with molybdenum cofactor deficiency. Nat Genet. 1998 Sep;20(1):51-3. [PubMed Link Image]
  2. 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]
  3. Gross-Hardt S, Reiss J: The bicistronic MOCS1 gene has alternative start codons on two mutually exclusive exons. Mol Genet Metab. 2002 Aug;76(4):340-3. [PubMed Link Image]
  4. Hanzelmann P, Schwarz G, Mendel RR: Functionality of alternative splice forms of the first enzymes involved in human molybdenum cofactor biosynthesis. J Biol Chem. 2002 May 24;277(21):18303-12. Epub 2002 Mar 12. [PubMed Link Image]
  5. Reiss J, Christensen E, Kurlemann G, Zabot MT, Dorche C: Genomic structure and mutational spectrum of the bicistronic MOCS1 gene defective in molybdenum cofactor deficiency type A. Hum Genet. 1998 Dec;103(6):639-44. [PubMed Link Image]
Enzyme 41 Metabolite References Not Available
Enzyme 42 [top]
Enzyme 42 ID 7643
Enzyme 42 Name DNA (cytosine-5)-methyltransferase 1
Enzyme 42 Synonyms
  1. Dnmt1
  2. CXXC-type zinc finger protein 9
  3. DNA methyltransferase HsaI
  4. DNA MTase HsaI
  5. M.HsaI
  6. MCMT
Enzyme 42 Gene Name DNMT1
Enzyme 42 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 42 Number of Residues 1616
Enzyme 42 Molecular Weight 183163.6
Enzyme 42 Theoretical pI 7.81
Enzyme 42 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 42 General Function Involved in DNA binding
Enzyme 42 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 42 Pathways
Enzyme 42 Reactions
  • S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine [RN:R00380]
Enzyme 42 Pfam Domain Function
Enzyme 42 Signals
  • None
Enzyme 42 Transmembrane Regions
  • None
Enzyme 42 Essentiality Not Available
Enzyme 42 GenBank ID Protein 1632819 Link Image
Enzyme 42 UniProtKB/Swiss-Prot ID P26358 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name DNMT1_HUMAN Link Image
Enzyme 42 PDB ID Not Available
Enzyme 42 Cellular Location Not Available
Enzyme 42 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 42 GenBank Gene ID X63692 Link Image
Enzyme 42 GeneCard ID DNMT1 Link Image
Enzyme 42 GenAtlas ID DNMT1 Link Image
Enzyme 42 HGNC ID HGNC:2976 Link Image
Enzyme 42 Chromosome Location 1
Enzyme 42 Locus 19p13.2
Enzyme 42 SNPs SNPJam Report Link Image
Enzyme 42 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 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 7736
Enzyme 43 Name DNA (cytosine-5)-methyltransferase 3B
Enzyme 43 Synonyms
  1. Dnmt3b
  2. DNA methyltransferase HsaIIIB
  3. DNA MTase HsaIIIB
  4. M.HsaIIIB
Enzyme 43 Gene Name DNMT3B
Enzyme 43 Protein Sequence >DNA (cytosine-5)-methyltransferase 3B
MKGDTRHLNGEEDAGGREDSILVNGACSDQSSDSPPILEAIRTPEIRGRRSSSRLSKREV
SSLLSYTQDLTGDGDGEDGDGSDTPVMPKLFRETRTRSESPAVRTRNNNSVSSRERHRPS
PRSTRGRQGRNHVDESPVEFPATRSLRRRATASAGTPWPSPPSSYLTIDLTDDTEDTHGT
PQSSSTPYARLAQDSQQGGMESPQVEADSGDGDSSEYQDGKEFGIGDLVWGKIKGFSWWP
AMVVSWKATSKRQAMSGMRWVQWFGDGKFSEVSADKLVALGLFSQHFNLATFNKLVSYRK
AMYHALEKARVRAGKTFPSSPGDSLEDQLKPMLEWAHGGFKPTGIEGLKPNNTQPVVNKS
KVRRAGSRKLESRKYENKTRRRTADDSATSDYCPAPKRLKTNCYNNGKDRGDEDQSREQM
ASDVANNKSSLEDGCLSCGRKNPVSFHPLFEGGLCQTCRDRFLELFYMYDDDGYQSYCTV
CCEGRELLLCSNTSCCRCFCVECLEVLVGTGTAAEAKLQEPWSCYMCLPQRCHGVLRRRK
DWNVRLQAFFTSDTGLEYEAPKLYPAIPAARRRPIRVLSLFDGIATGYLVLKELGIKVGK
YVASEVCEESIAVGTVKHEGNIKYVNDVRNITKKNIEEWGPFDLVIGGSPCNDLSNVNPA
RKGLYEGTGRLFFEFYHLLNYSRPKEGDDRPFFWMFENVVAMKVGDKRDISRFLECNPVM
IDAIKVSAAHRARYFWGNLPGMNRPVIASKNDKLELQDCLEYNRIAKLKKVQTITTKSNS
IKQGKNQLFPVVMNGKEDVLWCTELERIFGFPVHYTDVSNMGRGARQKLLGRSWSVPVIR
HLFAPLKDYFACE
Enzyme 43 Number of Residues 853
Enzyme 43 Molecular Weight 95750.2
Enzyme 43 Theoretical pI 8.52
Enzyme 43 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 43 General Function Involved in DNA binding
Enzyme 43 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 43 Pathways
Enzyme 43 Reactions
  • S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine [RN:R00380]
Enzyme 43 Pfam Domain Function
Enzyme 43 Signals
  • None
Enzyme 43 Transmembrane Regions
  • None
Enzyme 43 Essentiality Not Available
Enzyme 43 GenBank ID Protein 5901940 Link Image
Enzyme 43 UniProtKB/Swiss-Prot ID Q9UBC3 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name DNM3B_HUMAN Link Image
Enzyme 43 PDB ID 1KHC Link Image
Enzyme 43 PDB File Show
Enzyme 43 3D Structure
Enzyme 43 Cellular Location Not Available
Enzyme 43 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 43 GenBank Gene ID NM_006892.3 Link Image
Enzyme 43 GeneCard ID DNMT3B Link Image
Enzyme 43 GenAtlas ID DNMT3B Link Image
Enzyme 43 HGNC ID HGNC:2979 Link Image
Enzyme 43 Chromosome Location 2
Enzyme 43 Locus 20q11.2
Enzyme 43 SNPs SNPJam Report Link Image
Enzyme 43 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 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 8577
Enzyme 44 Name tRNA (cytosine-5-)-methyltransferase
Enzyme 44 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 44 Gene Name TRDMT1
Enzyme 44 Protein Sequence >tRNA (cytosine-5-)-methyltransferase
MEPLRVLELYSGVGGMHHALRESCIPAQVVAAIDVNTVANEVYKYNFPHTQLLAKTIEGI
TLEEFDRLSFDMILMSPPCQPFTRIGRQGDMTDSRTNSFLHILDILPRLQKLPKYILLEN
VKGFEVSSTRDLLIQTIENCGFQYQEFLLSPTSLGIPNSRLRYFLIAKLQSEPLPFQAPG
QVLMEFPKIESVHPQKYAMDVENKIQEKNVEPNISFDGSIQCSGKDAILFKLETAEEIHR
KNQQDSDLSVKMLKDFLEDDTDVNQYLLPPKSLLRYALLLDIVQPTCRRSVCFTKGYGSY
IEGTGSVLQTAEDVQVENIYKSLTNLSQEEQITKLLILKLRYFTPKEIANLLGFPPEFGF
PEKITVKQRYRLLGNSLNVHVVAKLIKILYE
Enzyme 44 Number of Residues 391
Enzyme 44 Molecular Weight 44596.2
Enzyme 44 Theoretical pI 5.95
Enzyme 44 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 44 General Function Involved in DNA binding
Enzyme 44 Specific Function Specifically methylates cytosine 38 in the anticodon loop of tRNA(Asp)
Enzyme 44 Pathways Not Available
Enzyme 44 Reactions
  • S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing 5-methylcytosine [RN:R00595]
Enzyme 44 Pfam Domain Function
Enzyme 44 Signals
  • None
Enzyme 44 Transmembrane Regions
  • None
Enzyme 44 Essentiality Not Available
Enzyme 44 GenBank ID Protein Not Available
Enzyme 44 UniProtKB/Swiss-Prot ID O14717 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name TRDMT_HUMAN Link Image
Enzyme 44 PDB ID Not Available
Enzyme 44 Cellular Location Not Available
Enzyme 44 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 44 GenBank Gene ID AF012128 Link Image
Enzyme 44 GeneCard ID TRDMT1 Link Image
Enzyme 44 GenAtlas ID TRDMT1 Link Image
Enzyme 44 HGNC ID HGNC:2977 Link Image
Enzyme 44 Chromosome Location 1
Enzyme 44 Locus 10p15.1
Enzyme 44 SNPs SNPJam Report Link Image
Enzyme 44 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 44 Metabolite References Not Available
Enzyme 45 [top]
Enzyme 45 ID 8641
Enzyme 45 Name Histone-lysine N-methyltransferase SETD8
Enzyme 45 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 45 Gene Name SETD8
Enzyme 45 Protein Sequence >Histone-lysine N-methyltransferase SETD8
MGEGGAAAALVAAAAAAAAAAAAVVAGQRRRRLGRRARCHGPGRAAGGKMSKPCAVEAAA
AAVAATAPGPEMVERRGPGRPRTDGENVFTGQSKIYSYMSPNKCSGMRFPLQEENSVTHH
EVKCQGKPLAGIYRKREEKRNAGNAVRSAMKSEEQKIKDARKGPLVPFPNQKSEAAEPPK
TPPSSCDSTNAAIAKQALKKPIKGKQAPRKKAQGKTQQNRKLTDFYPVRRSSRKSKAELQ
SEERKRIDELIESGKEEGMKIDLIDGKGRGVIATKQFSRGDFVVEYHGDLIEITDAKKRE
ALYAQDPSTGCYMYYFQYLSKTYCVDATRETNRLGRLINHSKCGNCQTKLHDIDGVPHLI
LIASRDIAAGEELLYDYGDRSKASIEAHPWLKH
Enzyme 45 Number of Residues 393
Enzyme 45 Molecular Weight 42889.5
Enzyme 45 Theoretical pI 10.22
Enzyme 45 GO Classification Not Available
Enzyme 45 General Function Involved in histone-lysine N-methyltransferase activity
Enzyme 45 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 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 15029567 Link Image
Enzyme 45 UniProtKB/Swiss-Prot ID Q9NQR1 Link Image
Enzyme 45 UniProtKB/Swiss-Prot Entry Name SETD8_HUMAN Link Image
Enzyme 45 PDB ID Not Available
Enzyme 45 Cellular Location Not Available
Enzyme 45 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 45 GenBank Gene ID AF287261 Link Image
Enzyme 45 GeneCard ID SETD8 Link Image
Enzyme 45 GenAtlas ID SETD8 Link Image
Enzyme 45 HGNC ID HGNC:29489 Link Image
Enzyme 45 Chromosome Location 1
Enzyme 45 Locus 12q24.31
Enzyme 45 SNPs SNPJam Report Link Image
Enzyme 45 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 45 Metabolite References Not Available
Enzyme 46 [top]
Enzyme 46 ID 8738
Enzyme 46 Name Histone-lysine N-methyltransferase MLL3
Enzyme 46 Synonyms
  1. Homologous to ALR protein
  2. Lysine N-methyltransferase 2C
  3. KMT2C
  4. Myeloid/lymphoid or mixed-lineage leukemia protein 3
Enzyme 46 Gene Name MLL3
Enzyme 46 Protein Sequence >Histone-lysine N-methyltransferase MLL3
MSSEEDKSVEQPQPPPPPPEEPGAPAPSPAAADKRPRGRPRKDGASPFQRARKKPRSRGK
TAVEDEDSMDGLETTETETIVETEIKEQSAEEDAEAEVDNSKQLIPTLQRSVSEESANSL
VSVGVEAKISEQLCAFCYCGEKSSLGQGDLKQFRITPGFILPWRNQPSNKKDIDDNSNGT
YEKMQNSAPRKQRGQRKERSPQQNIVSCVSVSTQTASDDQAGKLWDELSLVGLPDAIDIQ
ALFDSTGTCWAHHRCVEWSLGVCQMEEPLLVNVDKAVVSGSTERCAFCKHLGATIKCCEE
KCTQMYHYPCAAGAGTFQDFSHIFLLCPEHIDQAPERSKEDANCAVCDSPGDLLDQFFCT
TCGQHYHGMCLDIAVTPLKRAGWQCPECKVCQNCKQSGEDSKMLVCDTCDKGYHTFCLQP
VMKSVPTNGWKCKNCRICIECGTRSSSQWHHNCLICDNCYQQQDNLCPFCGKCYHPELQK
DMLHCNMCKRWVHLECDKPTDHELDTQLKEEYICMYCKHLGAEMDRLQPGEEVEIAELTT
DYNNEMEVEGPEDQMVFSEQAANKDVNGQESTPGIVPDAVQVHTEEQQKSHPSESLDTDS
LLIAVSSQHTVNTELEKQISNEVDSEDLKMSSEVKHICGEDQIEDKMEVTENIEVVTHQI
TVQQEQLQLLEEPETVVSREESRPPKLVMESVTLPLETLVSPHEESISLCPEEQLVIERL
QGEKEQKENSELSTGLMDSEMTPTIEGCVKDVSYQGGKSIKLSSETESSFSSSADISKAD
VSSSPTPSSDLPSHDMLHNYPSALSSSAGNIMPTTYISVTPKIGMGKPAITKRKFSPGRP
RSKQGAWSTHNTVSPPSWSPDISEGREIFKPRQLPGSAIWSIKVGRGSGFPGKRRPRGAG
LSGRGGRGRSKLKSGIGAVVLPGVSTADISSNKDDEENSMHNTVVLFSSSDKFTLNQDMC
VVCGSFGQGAEGRLLACSQCGQCYHPYCVSIKITKVVLSKGWRCLECTVCEACGKATDPG
RLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWCVWCRHCGATSAGLRCEWQNNYTQCAP
CASLSSCPVCYRNYREEDLILQCRQCDRWMHAVCQNLNTEEEVENVADIGFDCSMCRPYM
PASNVPSSDCCESSLVAQIVTKVKELDPPKTYTQDGVCLTESGMTQLQSLTVTVPRRKRS
KPKLKLKIINQNSVAVLQTPPDIQSEHSRDGEMDDSREGELMDCDGKSESSPEREAVDDE
TKGVEGTDGVKKRKRKPYRPGIGGFMVRQRSRTGQGKTKRSVIRKDSSGSISEQLPCRDD
GWSEQLPDTLVDESVSVTESTEKIKKRYRKRKNKLEETFPAYLQEAFFGKDLLDTSRQSK
ISLDNLSEDGAQLLYKTNMNTGFLDPSLDPLLSSSSAPTKSGTHGPADDPLADISEVLNT
DDDILGIISDDLAKSVDHSDIGPVTDDPSSLPQPNVNQSSRPLSEEQLDGILSPELDKMV
TDGAILGKLYKIPELGGKDVEDLFTAVLSPANTQPTPLPQPPPPTQLLPIHNQDAFSRMP
LMNGLIGSSPHLPHNSLPPGSGLGTFSAIAQSSYPDARDKNSAFNPMASDPNNSWTSSAP
TVEGENDTMSNAQRSTLKWEKEEALGEMATVAPVLYTNINFPNLKEEFPDWTTRVKQIAK
LWRKASSQERAPYVQKARDNRAALRINKVQMSNDSMKRQQQQDSIDPSSRIDSELFKDPL
KQRESEHEQEWKFRQQMRQKSKQQAKIEATQKLEQVKNEQQQQQQQQFGSQHLLVQSGSD
TPSSGIQSPLTPQPGNGNMSPAQSFHKELFTKQPPSTPTSTSSDDVFVKPQAPPPPPAPS
RIPIQDSLSQAQTSQPPSPQVFSPGSSNSRPPSPMDPYAKMVGTPRPPPVGHSFSRRNSA
APVENCTPLSSVSRPLQMNETTANRPSPVRDLCSSSTTNNDPYAKPPDTPRPVMTDQFPK
SLGLSRSPVVSEQTAKGPIAAGTSDHFTKPSPRADVFQRQRIPDSYARPLLTPAPLDSGP
GPFKTPMQPPPSSQDPYGSVSQASRRLSVDPYERPALTPRPIDNFSHNQSNDPYSQPPLT
PHPAVNESFAHPSRAFSQPGTISRPTSQDPYSQPPGTPRPVVDSYSQSSGTARSNTDPYS
QPPGTPRPTTVDPYSQQPQTPRPSTQTDLFVTPVTNQRHSDPYAHPPGTPRPGISVPYSQ
PPATPRPRISEGFTRSSMTRPVLMPNQDPFLQAAQNRGPALPGPLVRPPDTCSQTPRPPG
PGLSDTFSRVSPSAARDPYDQSPMTPRSQSDSFGTSQTAHDVADQPRPGSEGSFCASSNS
PMHSQGQQFSGVSQLPGPVPTSGVTDTQNTVNMAQADTEKLRQRQKLREIILQQQQQKKI
AGRQEKGSQDSPAVPHPGPLQHWQPENVNQAFTRPPPPYPGNIRSPVAPPLGPRYAVFPK
DQRGPYPPDVASMGMRPHGFRFGFPGGSHGTMPSQERFLVPPQQIQGSGVSPQLRRSVSV
DMPRPLNNSQMNNPVGLPQHFSPQSLPVQQHNILGQAYIELRHRAPDGRQRLPFSAPPGS
VVEASSNLRHGNFIPRPDFPGPRHTDPMRRPPQGLPNQLPVHPDLEQVPPSQQEQGHSVH
SSSMVMRTLNHPLGGEFSEAPLSTSVPSETTSDNLQITTQPSDGLEEKLDSDDPSVKELD
VKDLEGVEVKDLDDEDLENLNLDTEDGKVVELDTLDNLETNDPNLDDLLRSGEFDIIAYT
DPELDMGDKKSMFNEELDLPIDDKLDNQCVSVEPKKKEQENKTLVLSDKHSPQKKSTVTN
EVKTEVLSPNSKVESKCETEKNDENKDNVDTPCSQASAHSDLNDGEKTSLHPCDPDLFEK
RTNRETAGPSANVIQASTQLPAQDVINSCGITGSTPVLSSLLANEKSDNSDIRPSGSPPP
PTLPASPSNHVSSLPPFIAPPGRVLDNAMNSNVTVVSRVNHVFSQGVQVNPGLIPGQSTV
NHSLGTGKPATQTGPQTSQSGTSSMSGPQQLMIPQTLAQQNRERPLLLEEQPLLLQDLLD
QERQEQQQQRQMQAMIRQRSEPFFPNIDFDAITDPIMKAKMVALKGINKVMAQNNLGMPP
MVMSRFPFMGQVVTGTQNSEGQNLGPQAIPQDGSITHQISRPNPPNFGPGFVNDSQRKQY
EEWLQETQQLLQMQQKYLEEQIGAHRKSKKALSAKQRTAKKAGREFPEEDAEQLKHVTEQ
QSMVQKQLEQIRKQQKEHAELIEDYRIKQQQQCAMAPPTMMPSVQPQPPLIPGATPPTMS
QPTFPMVPQQLQHQQHTTVISGHTSPVRMPSLPGWQPNSAPAHLPLNPPRIQPPIAQLPI
KTCTPAPGTVSNANPQSGPPPRVEFDDNNPFSESFQERERKERLREQQERQRIQLMQEVD
RQRALQQRMEMEQHGMVGSEISSSRTSVSQIPFYSSDLPCDFMQPLGPLQQSPQHQQQMG
QVLQQQNIQQGSINSPSTQTFMQTNERRQVGPPSFVPDSPSIPVGSPNFSSVKQGHGNLS
GTSFQQSPVRPSFTPALPAAPPVANSSLPCGQDSTITHGHSYPGSTQSLIQLYSDIIPEE
KGKKKRTRKKKRDDDAESTKAPSTPHSDITAPPTPGISETTSTPAVSTPSELPQQADQES
VEPVGPSTPNMAAGQLCTELENKLPNSDFSQATPNQQTYANSEVDKLSMETPAKTEEIKL
EKAETESCPGQEEPKLEEQNGSKVEGNAVACPVSSAQSPPHSAGAPAAKGDSGNELLKHL
LKNKKSSSLLNQKPEGSICSEDDCTKDNKLVEKQNPAEGLQTLGAQMQGGFGCGNQLPKT
DGGSETKKQRSKRTQRTGEKAAPRSKKRKKDEEEKQAMYSSTDTFTHLKQQNNLSNPPTP
PASLPPTPPPMACQKMANGFATTEELAGKAGVLVSHEVTKTLGPKPFQLPFRPQDDLLAR
ALAQGPKTVDVPASLPTPPHNNQEELRIQDHCGDRDTPDSFVPSSSPESVVGVEVSRYPD
LSLVKEEPPEPVPSPIIPILPSTAGKSSESRRNDIKTEPGTLYFASPFGPSPNGPRSGLI
SVAITLHPTAAENISSVVAAFSDLLHVRIPNSYEVSSAPDVPSMGLVSSHRINPGLEYRQ
HLLLRGPPPGSANPPRLVSSYRLKQPNVPFPPTSNGLSGYKDSSHGIAESAALRPQWCCH
CKVVILGSGVRKSFKDLTLLNKDSRESTKRVEKDIVFCSNNCFILYSSTAQAKNSENKES
IPSLPQSPMRETPSKAFHQYSNNISTLDVHCLPQLPEKASPPASPPIAFPPAFEAAQVEA
KPDELKVTVKLKPRLRAVHGGFEDCRPLNKKWRGMKWKKWSIHIVIPKGTFKPPCEDEID
EFLKKLGTSLKPDPVPKDYRKCCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVY
ETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRFRCTNIYHFTCAIKAQCMFFKDKT
MLCPMHKPKGIHEQELSYFAVFRRVYVQRDEVRQIASIVQRGERDHTFRVGSLIFHTIGQ
LLPQQMQAFHSPKALFPVGYEASRLYWSTRYANRRCRYLCSIEEKDGRPVFVIRIVEQGH
EDLVLSDISPKGVWDKILEPVACVRKKSEMLQLFPAYLKGEDLFGLTVSAVARIAESLPG
VEACENYTFRYGRNPLMELPLAVNPTGCARSEPKMSAHVKRFVLRPHTLNSTSTSKSFQS
TVTGELNAPYSKQFVHSKSSQYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEY
IGTIIRNEVANRKEKLYESQNRGVYMFRMDNDHVIDATLTGGPARYINHSCAPNCVAEVV
TFERGHKIIISSSRRIQKGEELCYDYKFDFEDDQHKIPCHCGAVNCRKWMN
Enzyme 46 Number of Residues 4911
Enzyme 46 Molecular Weight 541365.6
Enzyme 46 Theoretical pI 6.46
Enzyme 46 GO Classification
Function
  • DNA binding
  • binding
  • cation binding
  • ion binding
  • metal ion binding
  • nucleic acid binding
  • protein binding
  • transition metal ion binding
  • zinc ion binding
Process
  • biological regulation
  • intracellular signaling pathway
  • 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
  • signaling
  • signaling pathway
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 46 General Function Involved in DNA binding
Enzyme 46 Specific Function Histone methyltransferase. Methylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Central component of the MLL2/MLL3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation. MLL3 may be a catalytic subunit of this complex. May be involved in leukemogenesis and developmental disorder
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 91718902 Link Image
Enzyme 46 UniProtKB/Swiss-Prot ID Q8NEZ4 Link Image
Enzyme 46 UniProtKB/Swiss-Prot Entry Name MLL3_HUMAN Link Image
Enzyme 46 PDB ID Not Available
Enzyme 46 Cellular Location Not Available
Enzyme 46 Gene Sequence >14736 bp
ATGTCGTCGGAGGAGGACAAGAGCGTGGAGCAGCCGCAGCCGCCGCCACCACCCCCCGAG
GAGCCTGGAGCCCCGGCCCCGAGCCCCGCAGCCGCAGACAAAAGACCTCGGGGCCGGCCT
CGCAAAGATGGCGCTTCCCCTTTCCAGAGAGCCAGAAAGAAACCTCGAAGTAGGGGGAAA
ACTGCAGTGGAAGATGAGGACAGCATGGATGGGCTGGAGACAACAGAAACAGAAACGATT
GTGGAAACAGAAATCAAAGAACAATCTGCAGAAGAGGATGCTGAAGCAGAAGTGGATAAC
AGCAAACAGCTAATTCCAACTCTTCAGCGATCTGTGTCTGAGGAATCGGCAAACTCCCTG
GTCTCTGTTGGTGTAGAAGCCAAAATCAGTGAACAGCTCTGCGCTTTTTGTTACTGTGGG
GAAAAAAGTTCCTTAGGACAAGGAGACTTAAAACAATTCAGAATAACGCCTGGATTTATC
TTGCCATGGAGAAACCAACCTTCTAACAAGAAGGACATTGATGACAACAGCAATGGAACC
TATGAGAAAATGCAAAACTCAGCACCACGAAAACAAAGAGGACAGAGAAAAGAACGATCT
CCTCAGCAGAATATAGTATCTTGTGTAAGTGTAAGCACCCAGACAGCTTCAGATGATCAA
GCTGGTAAACTGTGGGATGAACTCAGTCTGGTTGGGCTTCCAGATGCCATTGATATCCAA
GCCTTATTTGATTCTACAGGCACTTGTTGGGCTCATCACCGTTGTGTGGAGTGGTCACTA
GGAGTATGCCAGATGGAAGAACCATTGTTAGTGAACGTGGACAAAGCTGTTGTCTCAGGG
AGCACAGAACGATGTGCATTTTGTAAGCACCTTGGAGCCACTATCAAATGCTGTGAAGAG
AAATGTACCCAGATGTATCATTATCCTTGTGCTGCAGGAGCCGGCACCTTTCAGGATTTC
AGTCACATCTTCCTGCTTTGTCCAGAACACATTGACCAAGCTCCTGAAAGATCGAAGGAA
GATGCAAACTGTGCAGTGTGCGACAGCCCGGGAGACCTCTTAGATCAGTTCTTTTGTACT
ACTTGTGGTCAGCACTATCATGGAATGTGCCTGGATATAGCGGTTACTCCATTAAAACGT
GCAGGTTGGCAATGTCCTGAGTGCAAAGTGTGCCAGAACTGCAAACAATCGGGAGAAGAT
AGCAAGATGCTAGTGTGTGATACGTGTGACAAAGGGTATCATACTTTTTGTCTTCAACCA
GTTATGAAATCAGTACCAACCAATGGCTGGAAATGCAAAAATTGCAGAATATGTATAGAG
TGTGGCACACGGTCTAGTTCTCAGTGGCACCACAATTGCCTGATATGTGACAATTGTTAC
CAACAGCAGGATAACTTATGTCCCTTCTGTGGGAAGTGTTATCATCCAGAATTGCAGAAA
GACATGCTTCATTGTAATATGTGCAAAAGGTGGGTTCACCTAGAGTGTGACAAACCAACA
GATCATGAACTGGATACTCAGCTCAAAGAAGAGTATATCTGCATGTATTGTAAACACCTG
GGAGCTGAGATGGATCGTTTACAGCCAGGTGAGGAAGTGGAGATAGCTGAGCTCACTACA
GATTATAACAATGAAATGGAAGTTGAAGGCCCTGAAGATCAAATGGTATTCTCAGAGCAG
GCAGCTAATAAAGATGTCAACGGTCAGGAGTCCACTCCTGGAATTGTTCCAGATGCGGTT
CAAGTCCACACTGAAGAGCAACAGAAGAGTCATCCCTCAGAAAGTCTTGACACAGATAGT
CTTCTTATTGCTGTATCATCCCAACATACAGTGAATACTGAATTGGAAAAACAGATTTCT
AATGAAGTTGATAGTGAAGACCTGAAAATGTCTTCTGAAGTGAAGCATATTTGTGGCGAA
GATCAAATTGAAGATAAAATGGAAGTGACAGAAAACATTGAAGTCGTTACACACCAGATC
ACTGTGCAGCAAGAACAACTGCAGTTGTTAGAGGAACCTGAAACAGTGGTATCCAGAGAA
GAATCAAGGCCTCCAAAATTAGTCATGGAATCTGTCACTCTTCCACTAGAAACCTTAGTG
TCCCCACATGAGGAAAGTATTTCATTATGTCCTGAGGAACAGTTGGTTATAGAAAGGCTA
CAAGGAGAAAAGGAACAGAAAGAAAATTCTGAACTTTCTACTGGATTGATGGACTCTGAA
ATGACTCCTACAATTGAGGGTTGTGTGAAAGATGTTTCATACCAAGGAGGCAAATCTATA
AAGTTATCATCTGAGACAGAGTCATCATTTTCATCATCAGCAGACATAAGCAAGGCAGAT
GTGTCTTCCTCCCCAACACCTTCTTCAGACTTGCCTTCGCATGACATGCTGCATAATTAC
CCTTCAGCTCTTAGTTCCTCTGCTGGAAACATCATGCCAACAACTTACATCTCAGTCACT
CCAAAAATTGGCATGGGTAAACCAGCTATTACTAAGAGAAAATTTTCTCCTGGTAGACCT
CGGTCCAAACAGGGGGCTTGGAGTACCCATAATACAGTGAGCCCACCTTCCTGGTCCCCA
GACATTTCAGAAGGTCGGGAAATTTTTAAACCCAGGCAGCTTCCTGGCAGTGCCATTTGG
AGCATCAAAGTGGGCCGTGGGTCTGGATTTCCAGGAAAGCGGAGACCTCGAGGTGCAGGA
CTGTCGGGGCGAGGTGGCCGAGGCAGGTCAAAGCTGAAAAGTGGAATCGGAGCTGTTGTA
TTACCTGGGGTGTCTACTGCAGATATTTCATCAAATAAGGATGATGAAGAAAACTCTATG
CACAATACAGTTGTGTTGTTTTCTAGCAGTGACAAGTTCACTTTGAATCAGGATATGTGT
GTAGTTTGTGGCAGTTTTGGCCAAGGAGCAGAAGGAAGATTACTTGCCTGTTCTCAGTGT
GGTCAGTGTTACCATCCATACTGTGTCAGTATTAAGATCACTAAAGTGGTTCTTAGCAAA
GGTTGGAGGTGTCTTGAGTGCACTGTGTGTGAGGCCTGTGGGAAGGCAACTGACCCAGGA
AGACTCCTGCTGTGTGATGACTGTGACATAAGTTATCACACCTACTGCCTAGACCCTCCA
TTGCAGACAGTTCCCAAAGGAGGCTGGAAGTGCAAATGGTGTGTTTGGTGCAGACACTGT
GGAGCAACATCTGCAGGTCTAAGATGTGAATGGCAGAACAATTACACACAGTGCGCTCCT
TGTGCAAGCTTATCTTCCTGTCCAGTCTGCTATCGAAACTATAGAGAAGAAGATCTTATT
CTGCAATGTAGACAATGTGATAGATGGATGCATGCAGTTTGTCAGAACTTAAATACTGAG
GAAGAAGTGGAAAATGTAGCAGACATTGGTTTTGATTGTAGCATGTGCAGACCCTATATG
CCTGCGTCTAATGTGCCTTCCTCAGACTGCTGTGAATCTTCACTTGTAGCACAAATTGTC
ACAAAAGTAAAAGAGCTAGACCCACCCAAGACTTATACCCAGGATGGTGTGTGTTTGACT
GAATCAGGGATGACTCAGTTACAGAGCCTCACAGTTACAGTTCCAAGAAGAAAACGGTCA
AAACCAAAATTGAAATTGAAGATTATAAATCAGAATAGCGTGGCCGTCCTTCAGACCCCT
CCAGACATCCAATCAGAGCATTCAAGGGATGGTGAAATGGATGATAGTCGAGAAGGAGAA
CTTATGGATTGTGATGGAAAATCAGAATCTAGTCCTGAGCGGGAAGCTGTGGATGATGAA
ACTAAGGGAGTGGAAGGAACAGATGGTGTCAAAAAGAGAAAAAGGAAACCATACAGACCA
GGTATTGGTGGATTTATGGTGCGGCAAAGAAGTCGAACTGGGCAAGGGAAAACCAAAAGA
TCTGTGATCAGAAAAGATTCCTCAGGCTCTATTTCCGAGCAGTTACCTTGCAGAGATGAT
GGCTGGAGTGAGCAGTTACCAGATACTTTAGTTGATGAATCTGTTTCTGTTACTGAAAGC
ACTGAAAAAATAAAGAAGAGATACCGAAAAAGGAAAAATAAGCTTGAAGAAACTTTCCCT
GCCTATTTACAAGAAGCTTTCTTTGGAAAAGATCTTCTAGATACAAGTAGACAAAGCAAG
ATAAGTTTAGATAATCTGTCAGAAGATGGAGCTCAGCTTTTATATAAAACAAACATGAAC
ACAGGTTTCTTGGATCCTTCCTTAGATCCACTACTTAGTTCATCCTCGGCTCCAACAAAA
TCTGGAACTCACGGTCCTGCTGATGACCCATTAGCTGATATTTCTGAAGTTTTAAACACA
GATGATGACATTCTTGGAATAATTTCAGATGATCTAGCAAAATCAGTTGATCATTCAGAT
ATTGGTCCTGTCACTGATGATCCTTCCTCTTTGCCTCAGCCAAATGTCAATCAGAGTTCA
CGACCATTAAGTGAAGAACAGCTAGATGGGATCCTCAGTCCTGAACTAGACAAAATGGTC
ACAGATGGAGCAATTCTTGGAAAATTATATAAAATTCCAGAGCTTGGCGGAAAAGATGTT
GAAGACTTATTTACAGCTGTACTTAGTCCTGCGAACACTCAGCCAACTCCATTGCCACAG
CCTCCCCCACCAACACAGCTGTTGCCAATACACAATCAGGATGCTTTTTCACGGATGCCT
CTCATGAATGGCCTTATTGGATCCAGTCCTCATCTCCCACATAATTCTTTGCCACCTGGA
AGCGGACTGGGAACTTTCTCTGCAATTGCACAATCCTCTTATCCTGATGCCAGGGATAAA
AATTCAGCCTTTAATCCAATGGCAAGTGATCCTAACAACTCTTGGACATCATCAGCTCCC
ACTGTGGAAGGAGAAAATGACACAATGTCGAATGCCCAGAGAAGCACGCTTAAGTGGGAG
AAAGAGGAGGCTCTGGGTGAAATGGCAACTGTTGCCCCAGTTCTCTACACCAATATTAAT
TTCCCCAACTTAAAGGAAGAATTCCCTGATTGGACTACTAGAGTGAAGCAAATTGCCAAA
TTGTGGAGAAAAGCAAGCTCACAAGAAAGAGCACCATATGTGCAAAAAGCCAGAGATAAC
AGAGCTGCTTTACGCATTAATAAAGTACAGATGTCAAATGATTCCATGAAAAGGCAGCAA
CAGCAAGATAGCATTGATCCCAGCTCTCGTATTGATTCGGAGCTTTTTAAAGATCCTTTA
AAGCAAAGAGAATCAGAACATGAACAGGAATGGAAATTTAGACAGCAAATGCGTCAGAAA
AGTAAGCAGCAAGCTAAAATTGAAGCCACACAGAAACTTGAACAGGTGAAAAATGAGCAG
CAGCAGCAGCAACAACAGCAATTTGGTTCTCAGCATCTTCTGGTGCAGTCTGGTTCAGAT
ACACCAAGTAGTGGGATACAGAGTCCCTTGACACCTCAGCCTGGCAATGGAAATATGTCT
CCTGCACAGTCATTCCATAAAGAACTGTTTACAAAACAGCCACCCAGTACCCCTACGTCT
ACATCTTCAGATGATGTGTTTGTAAAGCCACAAGCTCCACCTCCTCCTCCAGCCCCATCC
CGGATTCCCATCCAGGATAGTCTTTCTCAGGCTCAGACTTCTCAGCCACCCTCACCGCAA
GTGTTTTCACCTGGGTCCTCTAACTCACGACCACCATCTCCAATGGATCCATATGCAAAA
ATGGTTGGTACCCCTCGACCACCTCCTGTGGGCCATAGTTTTTCCAGAAGAAATTCTGCT
GCACCAGTGGAAAACTGTACACCTTTATCATCGGTATCTAGGCCCCTTCAAATGAATGAG
ACAACAGCAAATAGGCCATCCCCTGTCAGAGATTTATGTTCTTCTTCCACGACAAATAAT
GACCCCTATGCAAAACCTCCAGACACACCTAGGCCTGTGATGACAGATCAATTTCCCAAA
TCCTTGGGCCTATCCCGGTCTCCTGTAGTTTCAGAACAAACTGCAAAAGGCCCTATAGCA
GCTGGAACCAGTGATCACTTTACTAAACCATCTCCTAGGGCAGATGTGTTTCAAAGACAA
AGGATACCTGACTCATATGCACGACCCTTGTTGACACCTGCACCTCTTGATAGTGGTCCT
GGACCTTTTAAGACTCCAATGCAACCTCCTCCATCCTCTCAGGATCCTTATGGATCAGTG
TCACAGGCATCAAGGCGATTGTCTGTTGACCCTTATGAAAGGCCTGCTTTGACACCAAGA
CCTATAGATAATTTTTCTCATAATCAGTCAAATGATCCATATAGTCAGCCTCCCCTTACC
CCACATCCAGCAGTGAATGAATCTTTTGCCCATCCTTCAAGGGCTTTTTCCCAGCCTGGA
ACCATATCAAGGCCAACATCTCAGGACCCATACTCCCAACCCCCAGGAACTCCACGACCT
GTTGTAGATTCTTATTCCCAATCTTCAGGAACAGCTAGGTCCAATACAGACCCTTACTCT
CAACCTCCTGGAACTCCCCGGCCTACTACTGTTGACCCATATAGTCAGCAGCCCCAAACC
CCAAGACCATCTACACAAACTGACTTGTTTGTTACACCTGTAACAAATCAGAGGCATTCT
GATCCATATGCTCATCCTCCTGGAACACCAAGACCTGGAATTTCTGTCCCTTACTCTCAG
CCACCAGCAACACCAAGGCCAAGGATTTCAGAGGGTTTTACTAGGTCCTCAATGACAAGA
CCAGTCCTCATGCCAAATCAGGATCCTTTCCTGCAAGCAGCACAAAACCGAGGACCAGCT
TTACCTGGCCCGTTGGTAAGGCCACCTGATACATGTTCCCAGACACCTAGGCCCCCTGGA
CCTGGTCTTTCAGACACATTTAGCCGTGTTTCCCCATCTGCTGCCCGTGATCCCTATGAT
CAGTCTCCAATGACTCCAAGATCTCAGTCTGACTCTTTTGGAACAAGTCAAACTGCCCAT
GATGTTGCTGATCAGCCAAGGCCTGGATCAGAGGGGAGCTTCTGTGCATCTTCAAACTCT
CCAATGCACTCCCAAGGCCAGCAGTTCTCTGGTGTCTCCCAACTTCCTGGACCTGTGCCA
ACTTCAGGAGTAACTGATACACAGAATACTGTAAATATGGCCCAAGCAGATACAGAGAAA
TTGAGACAGCGGCAGAAGTTACGTGAAATCATTCTCCAGCAGCAACAGCAGAAGAAGATT
GCAGGTCGACAGGAGAAGGGGTCACAGGACTCACCCGCAGTGCCTCATCCAGGGCCTCTT
CAACACTGGCAACCAGAGAATGTTAACCAGGCTTTCACCAGACCCCCACCTCCCTATCCT
GGGAACATTAGGTCTCCTGTTGCCCCTCCTTTAGGACCTAGATATGCTGTTTTCCCAAAA
GATCAGCGTGGACCCTATCCTCCTGATGTTGCTAGTATGGGGATGAGACCTCATGGATTT
AGATTTGGATTTCCAGGAGGTAGTCATGGTACCATGCCGAGTCAAGAGCGCTTCCTTGTG
CCTCCTCAGCAAATACAGGGATCTGGAGTTTCTCCACAGCTAAGAAGATCAGTATCTGTA
GATATGCCTAGGCCTTTAAATAACTCACAAATGAATAATCCAGTTGGACTTCCTCAGCAT
TTTTCACCACAGAGCTTGCCAGTTCAGCAGCACAACATACTGGGCCAAGCATATATTGAA
CTGAGACATAGGGCTCCTGACGGAAGGCAACGGCTGCCTTTCAGTGCTCCACCTGGCAGC
GTTGTAGAGGCATCTTCTAATCTGAGACATGGAAACTTCATTCCCCGGCCAGACTTTCCG
GGCCCTAGACACACAGACCCCATGCGACGACCTCCCCAGGGTCTACCTAATCAGCTACCT
GTGCACCCAGATTTGGAACAAGTGCCACCATCTCAACAAGAGCAAGGTCATTCTGTCCAT
TCATCTTCTATGGTCATGAGGACTCTGAACCATCCACTAGGTGGTGAATTTTCAGAAGCT
CCTTTGTCAACATCTGTACCGTCTGAAACAACGTCTGATAATTTACAGATAACCACCCAG
CCTTCTGATGGTCTAGAGGAAAAACTTGATTCTGATGACCCTTCTGTGAAGGAACTGGAT
GTTAAAGACCTTGAGGGGGTTGAAGTCAAAGACTTAGATGATGAAGATCTTGAAAACTTA
AATTTAGATACAGAGGATGGCAAGGTAGTTGAATTGGATACTTTAGATAATTTGGAAACT
AATGATCCCAACCTGGATGACCTCTTAAGGTCAGGAGAGTTTGATATCATTGCATATACA
GATCCAGAACTTGACATGGGAGATAAGAAAAGCATGTTTAATGAGGAACTAGACCTTCCA
ATTGATGATAAGTTAGATAATCAGTGTGTATCTGTTGAACCAAAAAAAAAGGAACAAGAA
AACAAAACTCTGGTTCTCTCTGATAAACATTCACCACAGAAAAAATCCACTGTTACCAAT
GAGGTAAAAACGGAAGTACTGTCTCCAAATTCTAAGGTGGAATCCAAATGTGAAACTGAA
AAAAATGATGAGAATAAAGATAATGTTGACACTCCTTGCTCACAGGCTTCTGCTCACTCA
GACCTAAATGATGGAGAAAAGACTTCTTTGCATCCTTGTGATCCAGATCTATTTGAGAAA
AGAACCAATCGAGAAACTGCTGGCCCCAGTGCAAATGTCATTCAGGCATCCACTCAACTA
CCTGCTCAAGATGTAATAAACTCTTGTGGCATAACTGGATCAACTCCAGTTCTCTCAAGT
TTACTTGCTAATGAGAAATCTGATAATTCAGACATTAGGCCATCGGGGTCTCCACCACCA
CCAACTCTGCCGGCCTCCCCATCCAATCATGTGTCAAGTTTGCCTCCTTTCATAGCACCG
CCTGGCCGTGTTTTGGATAATGCCATGAATTCTAATGTGACAGTAGTCTCTAGGGTAAAC
CATGTTTTTTCTCAGGGTGTGCAGGTAAACCCAGGGCTCATTCCAGGTCAATCAACAGTT
AACCACAGTCTGGGGACAGGAAAACCTGCAACTCAAACTGGGCCTCAAACAAGTCAGTCT
GGTACCAGTAGCATGTCTGGACCCCAACAGCTAATGATTCCTCAAACATTAGCACAGCAG
AATAGAGAGAGGCCCCTTCTTCTAGAAGAACAGCCTCTACTTCTACAGGATCTTTTGGAT
CAAGAAAGGCAAGAACAGCAGCAGCAAAGACAGATGCAAGCCATGATTCGTCAGCGATCA
GAACCGTTCTTCCCTAATATTGATTTTGATGCAATTACAGATCCTATAATGAAAGCCAAA
ATGGTGGCCCTTAAAGGTATAAATAAAGTGATGGCACAAAACAATCTGGGCATGCCACCA
ATGGTGATGAGCAGGTTCCCTTTTATGGGCCAGGTGGTAACTGGAACACAGAACAGTGAA
GGACAGAACCTTGGACCACAGGCCATTCCTCAGGATGGCAGTATAACACATCAGATTTCT
AGGCCTAATCCTCCAAATTTTGGTCCAGGCTTTGTCAATGATTCACAGCGTAAGCAGTAT
GAAGAGTGGCTCCAGGAGACCCAACAGCTGCTTCAAATGCAGCAGAAGTATCTTGAAGAA
CAAATTGGTGCTCACAGAAAATCTAAGAAGGCCCTTTCAGCTAAACAACGTACTGCCAAG
AAAGCTGGGCGTGAATTTCCAGAGGAAGATGCAGAACAACTCAAGCATGTTACTGAACAG
CAAAGCATGGTTCAGAAACAGCTAGAACAGATTCGTAAACAACAGAAAGAACATGCTGAA
TTGATTGAAGATTATCGGATCAAACAGCAGCAGCAATGTGCAATGGCCCCACCTACCATG
ATGCCCAGTGTCCAGCCCCAGCCACCCCTAATTCCAGGTGCCACTCCACCCACCATGAGC
CAACCCACCTTTCCCATGGTGCCACAGCAGCTTCAGCACCAGCAGCACACAACAGTTATT
TCTGGCCATACTAGCCCTGTTAGAATGCCCAGTTTACCTGGATGGCAACCCAACAGTGCT
CCTGCCCACCTGCCCCTCAATCCTCCTAGAATTCAGCCCCCAATTGCCCAGTTACCAATA
AAAACTTGTACACCAGCCCCAGGGACAGTCTCAAATGCAAATCCACAGAGTGGACCACCA
CCTCGGGTAGAATTTGATGACAACAATCCCTTTAGTGAAAGTTTTCAAGAACGGGAACGT
AAGGAACGTTTACGAGAACAGCAAGAGAGACAACGGATCCAACTCATGCAGGAGGTAGAT
AGACAAAGAGCTTTGCAGCAGAGGATGGAAATGGAGCAGCATGGTATGGTGGGCTCTGAG
ATAAGTAGTAGTAGGACATCTGTGTCCCAGATTCCCTTCTACAGTTCCGACTTACCTTGT
GATTTTATGCAACCTCTAGGACCCCTTCAGCAGTCTCCACAACACCAACAGCAAATGGGG
CAGGTTTTACAGCAGCAGAATATACAACAAGGATCAATTAATTCACCCTCCACCCAAACT
TTCATGCAGACTAATGAGCGAAGGCAGGTAGGCCCTCCTTCATTTGTTCCTGATTCACCA
TCAATCCCTGTTGGAAGCCCAAATTTTTCTTCTGTGAAGCAGGGACATGGAAATCTTTCT
GGGACCAGCTTCCAGCAGTCCCCAGTGAGGCCTTCTTTTACACCTGCTTTACCAGCAGCA
CCTCCAGTAGCTAATAGCAGTCTCCCATGTGGCCAAGATTCTACTATAACCCATGGACAC
AGTTATCCGGGATCAACCCAATCGCTCATTCAGTTGTATTCTGATATAATCCCAGAGGAA
AAAGGGAAAAAGAAAAGAACAAGAAAGAAGAAAAGAGATGATGATGCAGAATCCACCAAG
GCTCCATCAACTCCCCATTCAGATATAACTGCCCCACCGACTCCAGGCATCTCAGAAACT
ACCTCTACTCCTGCAGTGAGCACACCCAGTGAGCTTCCTCAACAAGCCGACCAAGAGTCG
GTGGAACCAGTCGGCCCATCCACTCCCAATATGGCAGCAGGCCAGCTATGTACAGAATTA
GAGAACAAACTGCCCAATAGTGATTTCTCACAAGCAACTCCAAATCAACAGACGTATGCA
AATTCAGAAGTAGACAAGCTCTCCATGGAAACCCCTGCCAAAACAGAAGAGATAAAACTG
GAAAAGGCTGAGACAGAGTCCTGCCCAGGCCAAGAGGAGCCTAAATTGGAGGAACAGAAT
GGTAGTAAGGTAGAAGGAAACGCTGTAGCCTGTCCTGTCTCCTCAGCACAGAGTCCTCCC
CATTCTGCTGGGGCCCCTGCTGCCAAAGGAGACTCAGGGAATGAACTTCTGAAACACTTG
TTGAAAAATAAAAAGTCATCTTCTCTTTTGAATCAAAAACCTGAGGGCAGTATTTGTTCA
GAAGATGACTGTACAAAGGATAATAAACTAGTTGAGAAGCAGAACCCAGCTGAAGGACTG
CAAACTTTGGGGGCTCAAATGCAAGGTGGTTTTGGATGTGGCAACCAGTTGCCAAAAACA
GATGGAGGAAGTGAAACCAAGAAACAGCGAAGCAAACGGACTCAGAGGACGGGTGAGAAA
GCAGCACCTCGCTCAAAGAAAAGGAAAAAGGACGAAGAGGAGAAACAAGCTATGTACTCT
AGCACTGACACGTTTACCCACTTGAAACAGCAGAATAATTTAAGTAATCCTCCAACACCC
CCTGCCTCTCTTCCTCCTACACCACCTCCTATGGCTTGTCAGAAGATGGCCAATGGTTTT
GCAACAACTGAAGAACTTGCTGGAAAAGCCGGAGTGTTAGTGAGCCATGAAGTTACCAAA
ACTCTAGGACCTAAACCATTTCAGCTGCCCTTCAGACCCCAGGACGACTTGTTGGCCCGA
GCTCTTGCTCAGGGCCCCAAGACAGTTGATGTGCCAGCCTCCCTCCCAACACCACCTCAT
AACAATCAGGAAGAATTAAGGATACAGGATCACTGTGGTGATCGAGATACTCCTGACAGT
TTTGTTCCCTCATCCTCTCCTGAGAGTGTGGTTGGGGTAGAAGTGAGCAGGTATCCAGAT
CTGTCATTGGTCAAGGAGGAGCCTCCAGAACCGGTGCCGTCCCCCATCATTCCAATTCTT
CCTAGCACTGCTGGGAAAAGTTCAGAATCAAGAAGGAATGACATCAAAACTGAGCCAGGC
ACTTTATATTTTGCGTCACCTTTTGGTCCTTCCCCAAATGGTCCCAGATCAGGTCTTATA
TCTGTAGCAATTACTCTGCATCCTACAGCTGCTGAGAACATTAGCAGTGTTGTGGCTGCA
TTTTCCGACCTTCTTCACGTCCGAATCCCTAACAGCTATGAGGTTAGCAGTGCTCCAGAT
GTCCCATCCATGGGTTTGGTCAGTAGCCACAGAATCAACCCGGGTTTGGAGTATCGACAG
CATTTACTTCTCCGTGGGCCTCCGCCAGGATCTGCAAACCCTCCCAGATTAGTGAGCTCT
TACCGGCTGAAGCAGCCTAATGTACCATTTCCTCCAACAAGCAATGGTCTTTCTGGATAT
AAGGATTCTAGTCATGGTATTGCAGAAAGCGCAGCACTCAGACCACAGTGGTGTTGTCAT
TGTAAAGTGGTTATTCTTGGAAGTGGTGTGCGGAAATCTTTCAAAGATCTGACCCTTTTG
AACAAGGATTCCCGAGAAAGCACCAAGAGGGTAGAGAAGGACATTGTCTTCTGTAGTAAT
AACTGCTTTATTCTTTATTCATCAACTGCACAAGCGAAAAACTCAGAAAACAAGGAATCC
ATTCCTTCATTGCCACAATCACCTATGAGAGAAACGCCTTCCAAAGCATTTCATCAGTAC
AGCAACAACATCTCCACTTTGGATGTGCACTGTCTCCCCCAGCTCCCAGAGAAAGCTTCT
CCCCCTGCCTCACCACCCATCGCCTTCCCTCCTGCTTTTGAAGCAGCCCAAGTCGAGGCC
AAGCCAGATGAGCTGAAGGTGACAGTCAAGCTGAAGCCTCGGCTAAGAGCTGTCCATGGT
GGGTTTGAAGATTGCAGGCCGCTCAATAAAAAATGGAGAGGAATGAAATGGAAGAAGTGG
AGCATTCATATTGTAATCCCTAAGGGGACATTTAAACCACCTTGTGAGGATGAAATAGAT
GAATTTCTAAAGAAATTGGGCACTTCCCTTAAACCTGATCCTGTGCCCAAAGACTATCGG
AAATGTTGCTTTTGTCATGAAGAAGGTGATGGATTGACAGATGGACCAGCAAGGCTACTC
AACCTTGACTTGGATCTGTGGGTCCACTTGAACTGCGCTCTGTGGTCCACGGAGGTCTAT
GAGACTCAGGCTGGTGCCTTAATAAATGTGGAGCTAGCTCTGAGGAGAGGCCTACAAATG
AAATGTGTCTTCTGTCACAAGACGGGTGCCACTAGTGGATGCCACAGATTTCGATGCACC
AACATTTATCACTTCACTTGCGCCATTAAAGCACAATGCATGTTTTTTAAGGACAAAACT
ATGCTTTGCCCCATGCACAAACCAAAGGGAATTCATGAGCAAGAATTAAGTTACTTTGCA
GTCTTCAGGAGGGTCTATGTTCAGCGTGATGAGGTGCGACAGATTGCTAGCATCGTGCAA
CGAGGAGAACGGGACCATACCTTTCGCGTGGGTAGCCTCATCTTCCACACAATTGGTCAG
CTGCTTCCACAGCAGATGCAAGCATTCCATTCTCCTAAAGCACTCTTCCCTGTGGGCTAT
GAAGCCAGCCGGCTGTACTGGAGCACTCGCTATGCCAATAGGCGCTGCCGCTACCTGTGC
TCCATTGAGGAGAAGGATGGGCGCCCAGTGTTTGTCATCAGGATTGTGGAACAAGGCCAT
GAAGACCTGGTTCTAAGTGACATCTCACCTAAAGGTGTCTGGGATAAGATTTTGGAGCCT
GTGGCATGTGTGAGAAAAAAGTCTGAAATGCTCCAGCTTTTCCCAGCGTATTTAAAAGGA
GAGGATCTGTTTGGCCTGACCGTCTCTGCAGTGGCACGCATAGCGGAATCACTTCCTGGG
GTTGAGGCATGTGAAAATTATACCTTCCGATACGGCCGAAATCCTCTCATGGAACTTCCT
CTTGCCGTTAACCCCACAGGTTGTGCCCGTTCTGAACCTAAAATGAGTGCCCATGTCAAG
AGGTTTGTGTTAAGGCCTCACACCTTAAACAGCACCAGCACCTCAAAGTCATTTCAGAGC
ACAGTCACTGGAGAACTGAACGCACCTTATAGTAAACAGTTTGTTCACTCCAAGTCATCG
CAGTACCGGAAGATGAAAACTGAATGGAAATCCAATGTGTATCTGGCACGGTCTCGGATT
CAGGGGCTGGGCCTGTATGCTGCTCGAGACATTGAGAAACACACCATGGTCATTGAGTAC
ATCGGGACTATCATTCGAAACGAAGTAGCCAACAGGAAAGAGAAGCTTTATGAGTCTCAG
AACCGTGGTGTGTACATGTTCCGCATGGATAACGACCATGTGATTGACGCGACGCTCACA
GGAGGGCCCGCAAGGTATATCAACCATTCGTGTGCACCTAATTGTGTGGCTGAAGTGGTG
ACTTTTGAGAGAGGACACAAAATTATCATCAGCTCCAGTCGGAGAATCCAGAAAGGAGAA
GAGCTCTGCTATGACTATAAGTTTGACTTTGAAGATGACCAGCACAAGATTCCGTGTCAC
TGTGGAGCTGTGAACTGCCGGAAGTGGATGAACTGA
Enzyme 46 GenBank Gene ID NM_170606.2 Link Image
Enzyme 46 GeneCard ID MLL3 Link Image
Enzyme 46 GenAtlas ID MLL3 Link Image
Enzyme 46 HGNC ID HGNC:13726 Link Image
Enzyme 46 Chromosome Location 7
Enzyme 46 Locus 7q36.1
Enzyme 46 SNPs SNPJam Report Link Image
Enzyme 46 General References
  1. Ruault M, Brun ME, Ventura M, Roizes G, De Sario A: MLL3, a new human member of the TRX/MLL gene family, maps to 7q36, a chromosome region frequently deleted in myeloid leukaemia. Gene. 2002 Feb 6;284(1-2):73-81. [PubMed Link Image]
  2. Tan YC, Chow VT: Novel human HALR (MLL3) gene encodes a protein homologous to ALR and to ALL-1 involved in leukemia, and maps to chromosome 7q36 associated with leukemia and developmental defects. Cancer Detect Prev. 2001;25(5):454-69. [PubMed Link Image]
  3. 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]
  4. Nagase T, Kikuno R, Ishikawa K, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Apr 28;7(2):143-50. [PubMed Link Image]
  5. 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]
  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. 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]
  8. Goo YH, Sohn YC, Kim DH, Kim SW, Kang MJ, Jung DJ, Kwak E, Barlev NA, Berger SL, Chow VT, Roeder RG, Azorsa DO, Meltzer PS, Suh PG, Song EJ, Lee KJ, Lee YC, Lee JW: Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins. Mol Cell Biol. 2003 Jan;23(1):140-9. [PubMed Link Image]
  9. 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]
  10. 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]
  11. 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]
  12. 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]
  13. 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]
  14. Cho YW, Hong T, Hong S, Guo H, Yu H, Kim D, Guszczynski T, Dressler GR, Copeland TD, Kalkum M, Ge K: PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex. J Biol Chem. 2007 Jul 13;282(28):20395-406. Epub 2007 May 11. [PubMed Link Image]
Enzyme 46 Metabolite References Not Available
Enzyme 47 [top]
Enzyme 47 ID 9553
Enzyme 47 Name Methionine adenosyltransferase 2 subunit beta
Enzyme 47 Synonyms
  1. DTDP-4-keto-6-deoxy-D-glucose 4-reductase
  2. Methionine adenosyltransferase II beta
  3. MAT II beta
Enzyme 47 Gene Name MAT2B
Enzyme 47 Protein Sequence >Methionine adenosyltransferase 2 subunit beta
MVGREKELSIHFVPGSCRLVEEEVNIPNRRVLVTGATGLLGRAVHKEFQQNNWHAVGCGF
RRARPKFEQVNLLDSNAVHHIIHDFQPHVIVHCAAERRPDVVENQPDAASQLNVDASGNL
AKEAAAVGAFLIYISSDYVFDGTNPPYREEDIPAPLNLYGKTKLDGEKAVLENNLGAAVL
RIPILYGEVEKLEESAVTVMFDKVQFSNKSANMDHWQQRFPTHVKDVATVCRQLAEKRML
DPSIKGTFHWSGNEQMTKYEMACAIADAFNLPSSHLRPITDSPVLGAQRPRNAQLDCSKL
ETLGIGQRTPFRIGIKESLWPFLIDKRWRQTVFH
Enzyme 47 Number of Residues 334
Enzyme 47 Molecular Weight 37551.5
Enzyme 47 Theoretical pI 7.39
Enzyme 47 GO Classification
Function
  • binding
  • catalytic activity
  • dTDP-4-dehydrorhamnose reductase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • carbohydrate metabolic process
  • cellular polysaccharide biosynthetic process
  • extracellular polysaccharide biosynthetic process
  • metabolic process
  • polysaccharide biosynthetic process
  • polysaccharide metabolic process
  • primary metabolic process
Component
Enzyme 47 General Function Involved in dTDP-4-dehydrorhamnose reductase activity
Enzyme 47 Specific Function Non-catalytic regulatory subunit of S-adenosylmethionine synthetase 2 (MAT2A), an enzyme that catalyzes the formation of S- adenosylmethionine from methionine and ATP. Regulates the activity of S-adenosylmethionine synthetase 2 by changing its kinetic properties, rendering the enzyme more susceptible to S- adenosylmethionine inhibition
Enzyme 47 Pathways Not Available
Enzyme 47 Reactions Not Available
Enzyme 47 Pfam Domain Function
Enzyme 47 Signals
  • None
Enzyme 47 Transmembrane Regions
  • None
Enzyme 47 Essentiality Not Available
Enzyme 47 GenBank ID Protein Not Available
Enzyme 47 UniProtKB/Swiss-Prot ID Q9NZL9 Link Image
Enzyme 47 UniProtKB/Swiss-Prot Entry Name MAT2B_HUMAN Link Image
Enzyme 47 PDB ID Not Available
Enzyme 47 Cellular Location Not Available
Enzyme 47 Gene Sequence >1005 bp
ATGGTGGGGAGGGAGAAAGAACTGTCTATACACTTTGTTCCCGGGAGCTGTCGGCTGGTG
GAGGAGGAAGTTAACATCCCTAATAGGAGGGTTCTGGTTACTGGTGCCACTGGGCTTCTT
GGCAGAGCTGTACACAAAGAATTTCAGCAGAATAATTGGCATGCAGTTGGCTGTGGTTTC
AGAAGAGCAAGACCAAAATTTGAACAGGTTAATCTGTTGGATTCTAATGCAGTTCATCAC
ATCATTCATGATTTTCAGCCCCATGTTATAGTACATTGTGCAGCAGAGAGAAGACCAGAT
GTTGTAGAAAATCAGCCAGATGCTGCCTCTCAACTTAATGTGGATGCTTCTGGGAATTTA
GCAAAGGAAGCAGCTGCTGTTGGAGCATTTCTCATCTACATTAGCTCAGATTATGTATTT
GATGGAACAAATCCACCTTACAGAGAGGAAGACATACCAGCTCCCCTAAATTTGTATGGC
AAAACAAAATTAGATGGAGAAAAGGCTGTCCTGGAGAACAATCTAGGAGCTGCTGTTTTG
AGGATTCCTATTCTGTATGGGGAAGTTGAAAAGCTCGAAGAAAGTGCTGTGACTGTTATG
TTTGATAAAGTGCAGTTCAGCAACAAGTCAGCAAACATGGATCACTGGCAGCAGAGGTTC
CCCACACATGTCAAAGATGTGGCCACTGTGTGCCGGCAGCTAGCAGAGAAGAGAATGCTG
GATCCATCAATTAAGGGAACCTTTCACTGGTCTGGCAATGAACAGATGACTAAGTATGAA
ATGGCATGTGCAATTGCAGATGCCTTCAACCTCCCCAGCAGTCACTTAAGACCTATTACT
GACAGCCCTGTCCTAGGAGCACAACGTCCGAGAAATGCTCAGCTTGACTGCTCCAAATTG
GAGACCTTGGGCATTGGCCAACGAACACCATTTCGAATTGGAATCAAAGAATCACTTTGG
CCTTTCCTCATTGACAAGAGATGGAGACAAACGGTCTTTCATTAG
Enzyme 47 GenBank Gene ID AF182814 Link Image
Enzyme 47 GeneCard ID MAT2B Link Image
Enzyme 47 GenAtlas ID MAT2B Link Image
Enzyme 47 HGNC ID HGNC:6905 Link Image
Enzyme 47 Chromosome Location 5
Enzyme 47 Locus 5q34-q35
Enzyme 47 SNPs SNPJam Report Link Image
Enzyme 47 General References
  1. LeGros HL Jr, Halim AB, Geller AM, Kotb M: Cloning, expression, and functional characterization of the beta regulatory subunit of human methionine adenosyltransferase (MAT II). J Biol Chem. 2000 Jan 28;275(4):2359-66. [PubMed Link Image]
  2. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  3. Ohira M, Morohashi A, Nakamura Y, Isogai E, Furuya K, Hamano S, Machida T, Aoyama M, Fukumura M, Miyazaki K, Suzuki Y, Sugano S, Hirato J, Nakagawara A: Neuroblastoma oligo-capping cDNA project: toward the understanding of the genesis and biology of neuroblastoma. Cancer Lett. 2003 Jul 18;197(1-2):63-8. [PubMed Link Image]
  4. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  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. 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. LeGros L, Halim AB, Chamberlin ME, Geller A, Kotb M: Regulation of the human MAT2B gene encoding the regulatory beta subunit of methionine adenosyltransferase, MAT II. J Biol Chem. 2001 Jul 6;276(27):24918-24. Epub 2001 May 3. [PubMed Link Image]
  8. Martinez-Chantar ML, Garcia-Trevijano ER, Latasa MU, Martin-Duce A, Fortes P, Caballeria J, Avila MA, Mato JM: Methionine adenosyltransferase II beta subunit gene expression provides a proliferative advantage in human hepatoma. Gastroenterology. 2003 Apr;124(4):940-8. [PubMed Link Image]
Enzyme 47 Metabolite References Not Available
Enzyme 48 [top]
Enzyme 48 ID 11322
Enzyme 48 Name Histone-lysine N-methyltransferase SETDB2
Enzyme 48 Synonyms
  1. Chronic lymphocytic leukemia deletion region gene 8 protein
  2. Lysine N-methyltransferase 1F
  3. SET domain bifurcated 2
Enzyme 48 Gene Name SETDB2
Enzyme 48 Protein Sequence >Histone-lysine N-methyltransferase SETDB2
MGEKNGDAKTFWMELEDDGKVDFIFEQVQNVLQSLKQKIKDGSATNKEYIQAMILVNEAT
IINSSTSIKGASQKEVNAQSSDPMPVTQKEQENKSNAFPSTSCENSFPEDCTFLTTENKE
ILSLEDKVVDFREKDSSSNLSYQSHDCSGACLMKMPLNLKGENPLQLPIKCHFQRRHAKT
NSHSSALHVSYKTPCGRSLRNVEEVFRYLLETECNFLFTDNFSFNTYVQLARNYPKQKEV
VSDVDISNGVESVPISFCNEIDSRKLPQFKYRKTVWPRAYNLTNFSSMFTDSCDCSEGCI
DITKCACLQLTARNAKTSPLSSDKITTGYKYKRLQRQIPTGIYECSLLCKCNRQLCQNRV
VQHGPQVRLQVFKTEQKGWGVRCLDDIDRGTFVCIYSGRLLSRANTEKSYGIDENGRDEN
TMKNIFSKKRKLEVACSDCEVEVLPLGLETHPRTAKTEKCPPKFSNNPKELTVETKYDNI
SRIQYHSVIRDPESKTAIFQHNGKKMEFVSSESVTPEDNDGFKPPREHLNSKTKGAQKDS
SSNHVDEFEDNLLIESDVIDITKYREETPPRSRCNQATTLDNQNIKKAIEVQIQKPQEGR
STACQRQQVFCDEELLSETKNTSSDSLTKFNKGNVFLLDATKEGNVGRFLNHSCCPNLLV
QNVFVETHNRNFPLVAFFTNRYVKARTELTWDYGYEAGTVPEKEIFCQCGVNKCRKKIL
Enzyme 48 Number of Residues 719
Enzyme 48 Molecular Weight 81893.7
Enzyme 48 Theoretical pI 7.54
Enzyme 48 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 48 General Function Involved in DNA binding
Enzyme 48 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 48 Pathways
Enzyme 48 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 48 Pfam Domain Function
Enzyme 48 Signals
  • None
Enzyme 48 Transmembrane Regions
  • None
Enzyme 48 Essentiality Not Available
Enzyme 48 GenBank ID Protein 13699244 Link Image
Enzyme 48 UniProtKB/Swiss-Prot ID Q96T68 Link Image
Enzyme 48 UniProtKB/Swiss-Prot Entry Name SETB2_HUMAN Link Image
Enzyme 48 PDB ID Not Available
Enzyme 48 Cellular Location Not Available
Enzyme 48 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 48 GenBank Gene ID AF334407 Link Image
Enzyme 48 GeneCard ID SETDB2 Link Image
Enzyme 48 GenAtlas ID SETDB2 Link Image
Enzyme 48 HGNC ID HGNC:20263 Link Image
Enzyme 48 Chromosome Location 1
Enzyme 48 Locus 13q14
Enzyme 48 SNPs SNPJam Report Link Image
Enzyme 48 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 48 Metabolite References Not Available
Enzyme 49 [top]
Enzyme 49 ID 11328
Enzyme 49 Name S-adenosylmethionine mitochondrial carrier protein
Enzyme 49 Synonyms
  1. Mitochondrial S-adenosylmethionine transporter
  2. Solute carrier family 25 member 26
Enzyme 49 Gene Name SLC25A26
Enzyme 49 Protein Sequence >S-adenosylmethionine mitochondrial carrier protein
MDRPGFVAALVAGGVAGVSVDLILFPLDTIKTRLQSPQGFNKAGGFHGIYAGVPSAAIGS
FPNAAAFFITYEYVKWFLHADSSSYLTPMKHMLAASAGEVVACLIRVPSEVVKQRAQVSA
STRTFQIFSNILYEEGIQGLYRGYKSTVLREIPFSLVQFPLWESLKALWSWRQDHVVDSW
QSAVCGAFAGGFAAAVTTPLDVAKTRITLAKAGSSTADGNVLSVLHGVWRSQGLAGLFAG
VFPRMAAISLGGFIFLGAYDRTHSLLLEVGRKSP
Enzyme 49 Number of Residues 274
Enzyme 49 Molecular Weight 29380.6
Enzyme 49 Theoretical pI 9.73
Enzyme 49 GO Classification
Function
  • binding
Process
  • establishment of localization
  • transmembrane transport
  • transport
Component
  • cell part
  • membrane
Enzyme 49 General Function Involved in binding
Enzyme 49 Specific Function Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. Specifically mediates the transport of S- adenosylmethionine (SAM) into the mitochondria
Enzyme 49 Pathways Not Available
Enzyme 49 Reactions Not Available
Enzyme 49 Pfam Domain Function
Enzyme 49 Signals
  • None
Enzyme 49 Transmembrane Regions
  • 5-25 49-69 85-105 142-162 182-202 238-258
Enzyme 49 Essentiality Not Available
Enzyme 49 GenBank ID Protein 41351486 Link Image
Enzyme 49 UniProtKB/Swiss-Prot ID Q70HW3 Link Image
Enzyme 49 UniProtKB/Swiss-Prot Entry Name SAMC_HUMAN Link Image
Enzyme 49 PDB ID Not Available
Enzyme 49 Cellular Location Not Available
Enzyme 49 Gene Sequence >825 bp
ATGGACCGGCCGGGGTTCGTGGCAGCGCTGGTGGCTGGTGGGGTAGCAGGTGTTTCTGTT
GACTTGATATTATTTCCTCTGGATACCATTAAAACCAGGCTGCAGAGTCCCCAAGGATTT
AATAAGGCTGGTGGTTTTCATGGAATATATGCTGGCGTTCCTTCTGCTGCTATTGGATCC
TTTCCTAATGCTGCTGCATTTTTTATCACCTATGAATATGTGAAGTGGTTTTTGCATGCT
GATTCATCTTCATATTTGACACCTATGAAACATATGTTGGCTGCCTCTGCTGGAGAAGTG
GTTGCCTGCCTGATTCGAGTTCCATCTGAAGTGGTTAAGCAGAGGGCACAGGTATCTGCT
TCTACAAGAACATTTCAGATTTTCTCTAACATCTTATATGAAGAGGGTATCCAAGGGTTG
TATCGAGGCTATAAAAGCACAGTTTTAAGAGAGATTCCTTTTTCTTTGGTCCAGTTTCCC
TTATGGGAGTCCTTAAAAGCCCTCTGGTCCTGGAGGCAGGATCATGTGGTGGATTCTTGG
CAGTCAGCAGTCTGTGGAGCTTTTGCAGGTGGATTTGCCGCTGCAGTCACCACCCCTCTA
GACGTGGCAAAGACAAGAATTACGCTGGCAAAGGCTGGCTCCAGCACTGCTGATGGGAAT
GTGCTCTCTGTCCTGCATGGGGTCTGGCGGTCACAGGGGCTGGCAGGATTATTTGCAGGT
GTCTTCCCTCGAATGGCAGCCATCAGTCTGGGAGGTTTCATCTTTCTGGGGGCTTATGAC
CGAACGCACAGCTTGCTGTTGGAAGTTGGCAGAAAGAGTCCTTGA
Enzyme 49 GenBank Gene ID AJ580932 Link Image
Enzyme 49 GeneCard ID SLC25A26 Link Image
Enzyme 49 GenAtlas ID SLC25A26 Link Image
Enzyme 49 HGNC ID HGNC:20661 Link Image
Enzyme 49 Chromosome Location 3
Enzyme 49 Locus 3p14.1
Enzyme 49 SNPs SNPJam Report Link Image
Enzyme 49 General References
  1. Agrimi G, Di Noia MA, Marobbio CM, Fiermonte G, Lasorsa FM, Palmieri F: Identification of the human mitochondrial S-adenosylmethionine transporter: bacterial expression, reconstitution, functional characterization and tissue distribution. Biochem J. 2004 Apr 1;379(Pt 1):183-90. [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]
Enzyme 49 Metabolite References Not Available
Enzyme 50 [top]
Enzyme 50 ID 12870
Enzyme 50 Name tRNA (cytosine-5-)-methyltransferase NSUN2
Enzyme 50 Synonyms
  1. NOL1/NOP2/Sun domain family member 2
  2. Substrate of AIM1/Aurora kinase B
  3. tRNA (cytosine-5-)-methyltransferase
  4. tRNA methyltransferase 4 homolog
  5. hTrm4
Enzyme 50 Gene Name NSUN2
Enzyme 50 Protein Sequence >tRNA (cytosine-5-)-methyltransferase NSUN2
MGRRSRGRRLQQQQRPEDAEDGAEGGGKRGEAGWEGGYPEIVKENKLFEHYYQELKIVPE
GEWGQFMDALREPLPATLRITGYKSHAKEILHCLKNKYFKELEDLEVDGQKVEVPQPLSW
YPEELAWHTNLSRKILRKSPHLEKFHQFLVSETESGNISRQEAVSMIPPLLLNVRPHHKI
LDMCAAPGSKTTQLIEMLHADMNVPFPEGFVIANDVDNKRCYLLVHQAKRLSSPCIMVVN
HDASSIPRLQIDVDGRKEILFYDRILCDVPCSGDGTMRKNIDVWKKWTTLNSLQLHGLQL
RIATRGAEQLAEGGRMVYSTCSLNPIEDEAVIASLLEKSEGALELADVSNELPGLKWMPG
ITQWKVMTKDGQWFTDWDAVPHSRHTQIRPTMFPPKDPEKLQAMHLERCLRILPHHQNTG
GFFVAVLVKKSSMPWNKRQPKLQGKSAETRESTQLSPADLTEGKPTDPSKLESPSFTGTG
DTEIAHATEDLENNGSKKDGVCGPPPSKKMKLFGFKEDPFVFIPEDDPLFPPIEKFYALD
PSFPRMNLLTRTTEGKKRQLYMVSKELRNVLLNNSEKMKVINTGIKVWCRNNSGEEFDCA
FRLAQEGIYTLYPFINSRIITVSMEDVKILLTQENPFFRKLSSETYSQAKDLAKGSIVLK
YEPDSANPDALQCPIVLCGWRGKASIRTFVPKNERLHYLRMMGLEVLGEKKKEGVILTNE
SAASTGQPDNDVTEGQRAGEPNSPDAEEANSPDVTAGCDPAGVHPPR
Enzyme 50 Number of Residues 767
Enzyme 50 Molecular Weight 86470.1
Enzyme 50 Theoretical pI 6.76
Enzyme 50 GO Classification Not Available
Enzyme 50 General Function Involved in tRNA (cytosine-5-)-methyltransferase activity
Enzyme 50 Specific Function RNA methyltransferase that methylates tRNAs, and possibly RNA polymerase III transcripts. Methylates cytosine to 5- methylcytosine (m5C) at position 34 of intron-containing tRNA(Leu)(CAA) precursors. Not able to modify tRNAs at positions 48 or 49. May act downstream of Myc to regulate epidermal cell growth and proliferation
Enzyme 50 Pathways Not Available
Enzyme 50 Reactions
  • S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing 5-methylcytosine [RN:R00595]
Enzyme 50 Pfam Domain Function
Enzyme 50 Signals
  • None
Enzyme 50 Transmembrane Regions
  • None
Enzyme 50 Essentiality Not Available
Enzyme 50 GenBank ID Protein 115501316 Link Image
Enzyme 50 UniProtKB/Swiss-Prot ID Q08J23 Link Image
Enzyme 50 UniProtKB/Swiss-Prot Entry Name NSUN2_HUMAN Link Image
Enzyme 50 PDB ID Not Available
Enzyme 50 Cellular Location Not Available
Enzyme 50 Gene Sequence >2304 bp
ATGGGGCGGCGGTCGCGGGGTCGGCGGCTCCAGCAACAGCAGCGGCCGGAGGACGCGGAG
GATGGCGCCGAGGGTGGTGGAAAGCGCGGCGAGGCGGGCTGGGAAGGAGGCTACCCCGAG
ATCGTCAAGGAGAACAAGCTGTTCGAGCACTACTACCAGGAGCTCAAGATCGTGCCCGAG
GGCGAGTGGGGCCAGTTCATGGACGCTCTCAGGGAGCCGCTCCCGGCCACTTTAAGAATT
ACTGGTTACAAAAGCCACGCAAAAGAGATTCTCCATTGCTTAAAGAACAAATATTTTAAG
GAATTGGAGGACCTGGAGGTGGACGGTCAGAAAGTTGAAGTTCCACAGCCACTGAGTTGG
TATCCTGAAGAACTTGCCTGGCACACAAATTTAAGTCGAAAAATCTTGAGAAAATCGCCA
CACTTGGAAAAGTTTCATCAGTTTCTAGTTAGTGAAACAGAATCTGGAAATATTAGTCGT
CAAGAAGCTGTTAGCATGATCCCACCACTGCTCCTCAACGTGCGGCCTCATCATAAGATC
TTAGATATGTGTGCAGCACCTGGCTCAAAGACCACACAGTTAATTGAAATGCTACATGCC
GACATGAATGTCCCCTTTCCAGAGGGATTTGTTATTGCGAATGATGTGGACAACAAGCGC
TGCTACCTGCTCGTCCATCAAGCCAAGAGGCTGAGCAGCCCCTGCATCATGGTGGTCAAC
CATGATGCCTCCAGCATACCCAGGCTCCAGATAGATGTGGACGGCAGGAAAGAGATCCTC
TTCTATGATCGAATTTTATGTGATGTCCCTTGCAGTGGAGACGGCACTATGAGAAAAAAC
ATTGATGTTTGGAAAAAGTGGACCACCTTAAATAGCTTGCAGCTACATGGCTTACAGCTG
CGGATTGCAACACGCGGGGCTGAACAGCTGGCTGAAGGTGGAAGGATGGTGTATTCCACG
TGTTCACTAAACCCTATTGAGGATGAAGCAGTCATAGCATCTTTACTGGAAAAAAGTGAA
GGTGCTTTGGAGCTTGCTGATGTGTCTAATGAACTGCCAGGGCTGAAGTGGATGCCTGGA
ATCACACAGTGGAAGGTAATGACGAAAGATGGGCAGTGGTTTACAGACTGGGACGCTGTT
CCTCACAGCAGACACACCCAGATCCGACCTACCATGTTCCCTCCGAAGGACCCAGAAAAG
CTGCAGGCCATGCACCTGGAGCGATGCCTTAGGATATTACCCCATCATCAGAATACTGGA
GGGTTTTTTGTGGCAGTATTGGTGAAAAAATCTTCAATGCCGTGGAATAAACGTCAGCCA
AAGCTTCAGGGTAAATCTGCAGAGACCAGAGAAAGCACACAGCTGAGCCCTGCAGATCTC
ACAGAAGGGAAACCCACAGATCCCTCTAAGCTGGAAAGTCCGTCATTCACAGGAACTGGT
GACACAGAAATAGCTCATGCAACTGAGGATTTAGAGAATAATGGCAGTAAGAAAGATGGC
GTGTGTGGTCCTCCTCCATCAAAGAAAATGAAGTTATTTGGATTTAAAGAAGATCCATTT
GTATTTATTCCTGAAGATGACCCATTATTTCCACCTATTGAGAAATTTTATGCTTTGGAT
CCTTCATTCCCAAGGATGAATTTGTTAACTCGGACTACAGAAGGGAAGAAAAGGCAGCTC
TACATGGTTTCTAAGGAGTTGCGGAATGTGCTGCTGAATAACAGTGAGAAGATGAAGGTT
ATTAACACGGGGATCAAAGTCTGGTGTAGAAATAACAGCGGTGAAGAGTTTGACTGTGCT
TTCCGGCTGGCACGGGAGGGAATATATACATTGTATCCATTTATTAACTCAAGAATTATT
ACTGTATCAATGGAAGATGTTAAGATACTGTTGACCCAGGAAAATCCCTTTTTTAGAAAA
CTCAGCAGTGAGACCTACAGTCAAGCAAAGGACCTGGCAAAGGGAAGCATCGTGCTGAAG
TATGAACCAGATTCTGCGAATCCAGACGCTCTGCAGTGTCCCATCGTCTTATGCGGATGG
CGGGGAAAGGCCTCCATTCGAACTTTTGTGCCCAAGAATGAACGGCTTCATTATCTCAGG
ATGATGGGGCTGGAGGTATTGGGAGAAAAGAAGAAGGAAGGGGTTATCCTCACAAATGAG
AGTGCAGCCAGCACCGGACAGCCAGACAATGACGTGACTGAGGGACAGAGAGCAGGAGAG
CCCAACAGCCCAGATGCAGAAGAGGCCAACAGTCCAGACGTGACAGCAGGCTGTGACCCG
GCGGGGGTCCATCCACCCCGGTGA
Enzyme 50 GenBank Gene ID AB255451 Link Image
Enzyme 50 GeneCard ID NSUN2 Link Image
Enzyme 50 GenAtlas ID NSUN2 Link Image
Enzyme 50 HGNC ID HGNC:25994 Link Image
Enzyme 50 Chromosome Location 5
Enzyme 50 Locus 5p15.31
Enzyme 50 SNPs SNPJam Report Link Image
Enzyme 50 General References
  1. Sakita-Suto S, Kanda A, Suzuki F, Sato S, Takata T, Tatsuka M: Aurora-B regulates RNA methyltransferase NSUN2. Mol Biol Cell. 2007 Mar;18(3):1107-17. Epub 2007 Jan 10. [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. 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. 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]
  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. Brzezicha B, Schmidt M, Makalowska I, Jarmolowski A, Pienkowska J, Szweykowska-Kulinska Z: Identification of human tRNA:m5C methyltransferase catalysing intron-dependent m5C formation in the first position of the anticodon of the pre-tRNA Leu (CAA). Nucleic Acids Res. 2006;34(20):6034-43. Epub 2006 Oct 27. [PubMed Link Image]
  7. 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]
  8. 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]
  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]
Enzyme 50 Metabolite References Not Available
Enzyme 51 [top]
Enzyme 51 ID 13061
Enzyme 51 Name Histamine N-methyltransferase
Enzyme 51 Synonyms
  1. SubName: Histamine N-methyltransferase, isoform CRA_b
Enzyme 51 Gene Name HNMT
Enzyme 51 Protein Sequence >Histamine N-methyltransferase
MASSMRSLFSDHGKYVESFRRFLNHSTEHQCMQEFMDKKLPGIIGRYQNCC
Enzyme 51 Number of Residues 51
Enzyme 51 Molecular Weight 6045.9
Enzyme 51 Theoretical pI 8.51
Enzyme 51 GO Classification Not Available
Enzyme 51 General Function Involved in methyltransferase activity
Enzyme 51 Specific Function Not Available
Enzyme 51 Pathways Not Available
Enzyme 51 Reactions Not Available
Enzyme 51 Pfam Domain Function Not Available
Enzyme 51 Signals
  • None
Enzyme 51 Transmembrane Regions
  • None
Enzyme 51 Essentiality Not Available
Enzyme 51 GenBank ID Protein 13543497 Link Image
Enzyme 51 UniProtKB/Swiss-Prot ID Q9BRW6 Link Image
Enzyme 51 UniProtKB/Swiss-Prot Entry Name Q9BRW6_HUMAN Link Image
Enzyme 51 PDB ID 1JQD Link Image
Enzyme 51 PDB File Show
Enzyme 51 3D Structure
Enzyme 51 Cellular Location Not Available
Enzyme 51 Gene Sequence >156 bp
ATGGCATCTTCCATGAGGAGCTTGTTTTCTGACCACGGGAAATATGTTGAATCTTTCCGG
AGGTTTCTCAACCATTCCACGGAACACCAGTGCATGCAGGAATTCATGGACAAGAAGCTG
CCAGGCATAATAGGAAGATACCAGAATTGCTGTTAA
Enzyme 51 GenBank Gene ID BC005907 Link Image
Enzyme 51 GeneCard ID HNMT Link Image
Enzyme 51 GenAtlas ID HNMT Link Image
Enzyme 51 HGNC ID HGNC:5028 Link Image
Enzyme 51 Chromosome Location 2
Enzyme 51 Locus 2q22.1
Enzyme 51 SNPs SNPJam Report Link Image
Enzyme 51 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 51 Metabolite References Not Available
Enzyme 52 [top]
Enzyme 52 ID 13069
Enzyme 52 Name Adenosylmethionine decarboxylase 1
Enzyme 52 Synonyms
  1. SubName: Adenosylmethionine decarboxylase 1, isoform CRA_b
  2. SubName: Putative uncharacterized protein DKFZp313L1234
Enzyme 52 Gene Name AMD1
Enzyme 52 Protein Sequence >Adenosylmethionine decarboxylase 1
MGRMNSDCWYLYTLDFPESRVISQPDQTLEILMSELDPAVMDQFYMKDGVTAKDVTRESG
IRDLIPGSVIDATMFNPCGYSMNGMKSDGTYWTIHITPEPEFSYVSFETNLSQTSYDDLI
RKVVEVFKPGKFVTTLFVNQSSKCRTVLASPQKIEGFKRLDCQSAMFNDYNFVFTSFAKK
QQQQQS
Enzyme 52 Number of Residues 186
Enzyme 52 Molecular Weight 21301.0
Enzyme 52 Theoretical pI 4.67
Enzyme 52 GO Classification
Function
  • adenosylmethionine decarboxylase activity
  • carbon-carbon lyase activity
  • carboxy-lyase activity
  • catalytic activity
  • lyase activity
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid derivative metabolic process
  • cellular biogenic amine metabolic process
  • cellular metabolic process
  • metabolic process
  • polyamine biosynthetic process
  • polyamine metabolic process
  • spermidine biosynthetic process
  • spermine biosynthetic process
Component
Enzyme 52 General Function Involved in adenosylmethionine decarboxylase activity
Enzyme 52 Specific Function Not Available
Enzyme 52 Pathways Not Available
Enzyme 52 Reactions Not Available
Enzyme 52 Pfam Domain Function
Enzyme 52 Signals
  • None
Enzyme 52 Transmembrane Regions
  • None
Enzyme 52 Essentiality Not Available
Enzyme 52 GenBank ID Protein 55664719 Link Image
Enzyme 52 UniProtKB/Swiss-Prot ID Q5VXN4 Link Image
Enzyme 52 UniProtKB/Swiss-Prot Entry Name Q5VXN4_HUMAN Link Image
Enzyme 52 PDB ID 1MSV Link Image
Enzyme 52 PDB File Show
Enzyme 52 3D Structure
Enzyme 52 Cellular Location Not Available
Enzyme 52 Gene Sequence >561 bp
ATGGGACGTATGAATTCTGACTGTTGGTACTTATATACTCTGGATTTCCCAGAGAGTCGG
GTAATCAGTCAGCCAGATCAAACCTTGGAAATTCTGATGAGTGAGCTTGACCCAGCAGTT
ATGGACCAGTTCTACATGAAAGATGGTGTTACTGCAAAGGATGTCACTCGTGAGAGTGGA
ATTCGTGACCTGATACCAGGTTCTGTCATTGATGCCACAATGTTCAATCCTTGTGGGTAT
TCGATGAATGGAATGAAATCGGATGGAACTTATTGGACTATTCACATCACTCCAGAACCA
GAATTTTCTTATGTTAGCTTTGAAACAAACTTAAGTCAGACCTCCTATGATGACCTGATC
AGGAAAGTTGTAGAAGTCTTCAAGCCAGGAAAATTTGTGACCACCTTGTTTGTTAATCAG
AGTTCTAAATGTCGCACAGTGCTTGCTTCGCCCCAGAAGATTGAAGGTTTTAAGCGTCTT
GATTGCCAGAGTGCTATGTTCAATGATTACAATTTTGTTTTTACCAGTTTTGCTAAGAAG
CAGCAACAACAGCAGAGTTGA
Enzyme 52 GenBank Gene ID AL357515 Link Image
Enzyme 52 GeneCard ID AMD1 Link Image
Enzyme 52 GenAtlas ID AMD1 Link Image
Enzyme 52 HGNC ID HGNC:457 Link Image
Enzyme 52 Chromosome Location 6
Enzyme 52 Locus 6q21
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 13121
Enzyme 53 Name Ubiquinone biosynthesis methyltransferase COQ5, mitochondrial
Enzyme 53 Synonyms Not Available
Enzyme 53 Gene Name COQ5
Enzyme 53 Protein Sequence >Ubiquinone biosynthesis methyltransferase COQ5, mitochondrial
MAAPGSCALWSYCGRGWSRAMRGCQLLGLRSSWPGDLLSARLLSQEKRAAETHFGFETVS
EEEKGGKVYQVFESVAKKYDVMNDMMSLGIHRVWKDLLLWKMHPLPGTQLLDVAGGTGDI
AFRFLNYVQSQHQRKQKRQLRAQQNLSWEEIAKEYQNEEDSLGGSRVVVCDINKEMLKVG
KQKALAQGYRAGLAWVLGDAEELPFDDDKFDIYTIAFGIRNVTHIDQALQEAHRVLKPGG
RFLCLEFSQVNNPLISRLYDLYSFQVIPVLGEVIAGDWKSYQYLVESIRRFPSQEEFKDM
IEDAGFHKVTYESLTSGIVAIHSGFKL
Enzyme 53 Number of Residues 327
Enzyme 53 Molecular Weight 37140.2
Enzyme 53 Theoretical pI 6.94
Enzyme 53 GO Classification
Function
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
Component
Enzyme 53 General Function Involved in methyltransferase activity
Enzyme 53 Specific Function Converts DDMQH2 into DMQH2
Enzyme 53 Pathways Not Available
Enzyme 53 Reactions Not Available
Enzyme 53 Pfam Domain Function
Enzyme 53 Signals
  • None
Enzyme 53 Transmembrane Regions
  • None
Enzyme 53 Essentiality Not Available
Enzyme 53 GenBank ID Protein 116063536 Link Image
Enzyme 53 UniProtKB/Swiss-Prot ID Q5HYK3 Link Image
Enzyme 53 UniProtKB/Swiss-Prot Entry Name COQ5_HUMAN Link Image
Enzyme 53 PDB ID Not Available
Enzyme 53 Cellular Location Not Available
Enzyme 53 Gene Sequence >984 bp
ATGGCGGCCCCCGGGAGCTGTGCTCTATGGAGCTATTGCGGCCGTGGGTGGTCGCGGGCG
ATGCGGGGCTGCCAGCTCCTCGGGCTTCGTAGCTCTTGGCCCGGGGACCTACTAAGTGCT
CGGCTCTTGTCCCAAGAGAAGCGGGCAGCGGAAACGCACTTTGGGTTTGAGACTGTGTCG
GAAGAGGAGAAGGGGGGCAAAGTCTATCAGGTGTTTGAAAGTGTGGCTAAGAAGTATGAT
GTGATGAATGATATGATGAGTCTTGGTATCCATCGTGTTTGGAAGGATTTGCTGCTCTGG
AAGATGCACCCGCTTCCTGGGACCCAGCTGCTTGATGTTGCTGGAGGCACAGGTGACATT
GCATTCCGGTTCCTTAATTATGTTCAGTCCCAGCATCAGAGAAAACAGAAGAGGCAGTTA
AGGGCCCAACAAAATTTATCCTGGGAAGAAATTGCCAAAGAGTACCAGAATGAAGAAGAT
TCCTTGGGCGGGTCTCGTGTCGTGGTGTGTGACATCAACAAGGAGATGCTAAAGGTTGGA
AAGCAGAAAGCCTTGGCTCAAGGATACAGAGCTGGACTTGCATGGGTATTAGGAGATGCT
GAAGAACTGCCCTTTGATGATGACAAGTTTGATATTTACACCATTGCCTTTGGGATCCGG
AATGTCACACACATTGATCAGGCACTCCAGGAAGCTCATCGGGTGCTGAAACCAGGAGGA
CGGTTTCTCTGTCTGGAATTTAGCCAAGTGAACAATCCCCTCATATCCAGGCTTTATGAT
CTATATAGCTTCCAGGTCATCCCTGTCCTGGGAGAGGTCATCGCTGGAGACTGGAAGTCC
TATCAGTACCTTGTAGAGAGTATCCGAAGGTTTCCGTCTCAGGAAGAGTTCAAGGACATG
ATAGAAGATGCAGGCTTTCACAAGGTGACTTACGAAAGTCTAACATCAGGCATTGTGGCC
ATTCATTCTGGCTTCAAACTTTAA
Enzyme 53 GenBank Gene ID NM_032314.3 Link Image
Enzyme 53 GeneCard ID COQ5 Link Image
Enzyme 53 GenAtlas ID COQ5 Link Image
Enzyme 53 HGNC ID HGNC:28722 Link Image
Enzyme 53 Chromosome Location 1
Enzyme 53 Locus 12q24.31
Enzyme 53 SNPs SNPJam Report Link Image
Enzyme 53 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. 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. 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 53 Metabolite References Not Available
Enzyme 54 [top]
Enzyme 54 ID 14008
Enzyme 54 Name tRNA wybutosine-synthesizing protein 1 homolog
Enzyme 54 Synonyms
  1. Radical S-adenosyl methionine and flavodoxin domain-containing protein 1
  2. tRNA-yW-synthesizing protein
Enzyme 54 Gene Name TYW1
Enzyme 54 Protein Sequence >tRNA wybutosine-synthesizing protein 1 homolog
MDPSADTWDLFSPLISLWINRFYIYLGFAVSISLWICVQIVIKTQGKNLQEKSVPKAAQD
LMTNGYVSLQEKDIFVSGVKIFYGSQTGTAKGFATVLAEAVTSLDLPVAIINLKEYDPDD
HLIEEVTSKNVCVFLVATYTDGLPTESAEWFCKWLEEASIDFRFGKTYLKGMRYAVFGLG
NSAYASHFNKVGKNVDKWLWMLGAHRVMSRGEGDCDVVKSKHGSIEADFRAWKTKFISQL
QALQKGERKKSCGGHCKKGKCESHQHGSEEREEGSHEQDELHHRDTEEEEPFESSSEEEF
GGEDHQSLNSIVDVEDLGKIMDHVKKEKREKEQQEEKSGLFRNMGRNEDGERRAMITPAL
REALTKQGYQLIGSHSGVKLCRWTKSMLRGRGGCYKHTFYGIESHRCMETTPSLACANKC
VFCWRHHTNPVGTEWRWKMDQPEMILKEAIENHQNMIKQFKGVPGVKAERFEEGMTVKHC
ALSLVGEPIMYPEINRFLKLLHQCKISSFLVTNAQFPAEIRNLEPVTQLYVSVDASTKDS
LKKIDRPLFKDFWQRFLDSLKALAVKQQRTVYRLTLVKAWNVDELQAYAQLVSLGNPDFI
EVKGVTYCGESSASSLTMAHVPWHEEVVQFVHELVDLIPEYEIACEHEHSNCLLIAHRKF
KIGGEWWTWIDYNRFQELIQEYEDSGGSKTFSAKDYMARTPHWALFGASERGFDPKDTRH
QRKNKSKAISGC
Enzyme 54 Number of Residues 732
Enzyme 54 Molecular Weight 83701.7
Enzyme 54 Theoretical pI 6.87
Enzyme 54 GO Classification
Function
  • FMN binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • iron-sulfur cluster binding
  • metal cluster binding
  • metal ion binding
  • nucleotide binding
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 54 General Function Involved in iron ion binding
Enzyme 54 Specific Function Probable component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA
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 50726981 Link Image
Enzyme 54 UniProtKB/Swiss-Prot ID Q9NV66 Link Image
Enzyme 54 UniProtKB/Swiss-Prot Entry Name TYW1_HUMAN Link Image
Enzyme 54 PDB ID Not Available
Enzyme 54 Cellular Location Not Available
Enzyme 54 Gene Sequence >2199 bp
ATGGATCCTTCTGCGGATACATGGGACCTCTTCTCACCTTTAATATCATTATGGATAAAC
AGGTTTTACATTTATTTGGGCTTTGCTGTTAGCATTAGCCTTTGGATTTGTGTCCAGATT
GTCATCAAGACGCAGGGCAAGAACTTACAGGAAAAATCTGTTCCAAAAGCAGCTCAGGAT
TTGATGACAAATGGTTATGTCTCCCTTCAAGAGAAAGACATCTTTGTGTCTGGAGTGAAG
ATTTTTTATGGTTCTCAGACTGGAACAGCGAAGGGATTCGCAACAGTTCTTGCTGAAGCA
GTTACATCCCTGGATCTGCCTGTGGCCATTATTAATCTAAAAGAATATGATCCAGATGAT
CATCTGATAGAAGAGGTGACTAGTAAAAATGTCTGTGTCTTCCTGGTTGCGACATACACT
GACGGCCTACCAACTGAAAGTGCAGAGTGGTTCTGCAAATGGTTAGAGGAAGCATCCATT
GATTTTCGATTTGGCAAAACTTACCTGAAGGGTATGAGATATGCGGTATTTGGCCTGGGA
AATTCTGCCTATGCTAGCCACTTCAACAAGGTTGGCAAAAATGTTGACAAGTGGCTCTGG
ATGCTTGGCGCGCATCGTGTGATGAGTCGAGGGGAGGGCGACTGCGACGTGGTTAAAAGC
AAGCACGGCAGCATTGAGGCCGACTTCAGAGCATGGAAGACCAAGTTCATCTCCCAGCTG
CAGGCACTTCAGAAAGGGGAGAGAAAGAAGTCCTGTGGCGGCCACTGCAAGAAAGGCAAA
TGTGAATCTCACCAACATGGCTCAGAGGAGAGGGAGGAAGGATCTCATGAGCAGGATGAA
TTGCATCATAGAGACACCGAGGAGGAAGAACCCTTTGAGAGCTCCAGTGAAGAAGAGTTT
GGTGGTGAGGACCATCAGAGCCTAAATTCCATTGTTGATGTTGAAGATTTGGGCAAAATT
ATGGATCATGTGAAGAAAGAAAAGAGAGAAAAGGAACAGCAGGAAGAGAAGTCTGGTTTG
TTCAGGAACATGGGGAGGAATGAAGATGGTGAAAGAAGAGCTATGATAACTCCTGCTCTC
CGAGAAGCCCTTACTAAACAAGGTTATCAGTTGATTGGGAGCCACTCGGGGGTGAAGCTT
TGCAGGTGGACAAAGTCCATGCTCCGAGGGAGAGGAGGTTGTTACAAACACACATTCTAT
GGAATTGAGAGCCATCGCTGCATGGAAACCACCCCGAGCTTGGCGTGTGCTAATAAATGT
GTCTTCTGTTGGCGGCACCACACCAACCCCGTGGGCACTGAGTGGCGGTGGAAGATGGAC
CAGCCTGAAATGATCTTGAAGGAAGCCATTGAAAACCATCAGAACATGATTAAGCAGTTT
AAAGGAGTACCGGGCGTCAAAGCAGAACGCTTTGAAGAAGGAATGACGGTAAAGCACTGT
GCATTGTCCCTCGTGGGAGAACCAATAATGTACCCAGAGATCAACAGGTTTTTGAAGCTA
CTCCACCAGTGTAAAATTTCCAGCTTCCTGGTCACAAACGCACAATTTCCTGCGGAAATC
AGGAACCTCGAGCCGGTTACTCAGCTGTATGTCAGTGTGGATGCCAGTACCAAAGACAGC
CTGAAGAAAATCGACCGCCCACTCTTCAAGGATTTCTGGCAGAGATTCCTTGACAGTTTA
AAAGCCTTGGCAGTCAAGCAACAACGAACTGTCTACAGACTGACGCTCGTGAAAGCATGG
AACGTGGACGAGCTCCAGGCCTACGCGCAGCTCGTGTCCCTGGGGAATCCTGACTTCATC
GAAGTGAAGGGCGTTACCTACTGCGGAGAAAGTTCAGCAAGCAGTCTTACCATGGCCCAC
GTGCCCTGGCATGAGGAAGTGGTACAGTTTGTCCACGAGTTGGTGGATCTGATCCCCGAA
TATGAAATTGCATGTGAACACGAACACTCTAATTGCCTCCTGATAGCACACAGAAAGTTT
AAAATTGGTGGTGAATGGTGGACATGGATCGATTATAACCGCTTCCAGGAGCTCATCCAG
GAATATGAAGATAGTGGTGGATCAAAAACGTTCAGCGCAAAGGATTATATGGCCAGAACT
CCTCACTGGGCATTATTTGGTGCCAGTGAAAGAGGCTTTGATCCCAAGGACACAAGACAT
CAGAGAAAGAACAAATCAAAGGCTATTTCTGGATGTTGA
Enzyme 54 GenBank Gene ID NM_018264.2 Link Image
Enzyme 54 GeneCard ID TYW1 Link Image
Enzyme 54 GenAtlas ID TYW1 Link Image
Enzyme 54 HGNC ID HGNC:25598 Link Image
Enzyme 54 Chromosome Location 7
Enzyme 54 Locus 7q11.21
Enzyme 54 SNPs SNPJam Report Link Image
Enzyme 54 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. 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. 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 54 Metabolite References Not Available
Enzyme 55 [top]
Enzyme 55 ID 14009
Enzyme 55 Name tRNA wybutosine-synthesizing protein 1 homolog B
Enzyme 55 Synonyms
  1. Radical S-adenosyl methionine and flavodoxin domain-containing protein 2
Enzyme 55 Gene Name TYW1B
Enzyme 55 Protein Sequence >tRNA wybutosine-synthesizing protein 1 homolog B
MDPSADTWDLSSPLISLWINRFYIYLGFAVSISLWICVQIVIEMQGFATVLAEAVTSLDL
PVAIINLKEYDPDDHLIEEVTSKNVCVFLVATYTDGLPTESAEWFCKWLEEASIDFRFGK
TYLKGMRDAVFGLGNSAYASHFNKVGKNVDKWLWMLGVHRVMSRGEGDCDVVKSKHGSIE
ANFRAWKTKFISQLQALQKGERKKSCGGHCKKGKCESHQHGSEEREEGSQEQDELHHRDT
KEEEPFESSSEEEFGGEDHQSLNSIVDVEDLGKIMDHVKKEKREKEQQEEKSGLFRNMGR
NEDGERRAMITPALREALTKQVDAPRERSLLQTHILWNESHRCMETTPSLACANKCVFCW
WHHNNPVGTEWLWKMDQPEMILKEAIENHQNMIKQFKGVPGVKAERFEEGMTVKHCALSL
VGEPIMYPEINRFLKLLHQCKISSFLVTNAQFPAEIRNLEPVTQLYVSVDASTKDSLKKI
DRPLFKDFWQQFLDSLKALAVKQQRTVYRLMLVKAWNVDELQAYAQLVSLGNPDFIEVKG
VTYCRESSASSLTMAHVPWHEEVVQFVRELVDLIPEYEIACEHEHSNCLLIAHRKFKIGG
EWWTWIDYNRFQELIQEYEDSGGSKTFSAKDYMARTPHWALFGANERSFDPKDTRHQRKN
KSKAISGC
Enzyme 55 Number of Residues 668
Enzyme 55 Molecular Weight 76945.9
Enzyme 55 Theoretical pI 6.22
Enzyme 55 GO Classification
Function
  • FMN binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • iron-sulfur cluster binding
  • metal cluster binding
  • metal ion binding
  • nucleotide binding
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 55 General Function Involved in iron ion binding
Enzyme 55 Specific Function Probable component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA
Enzyme 55 Pathways Not Available
Enzyme 55 Reactions Not Available
Enzyme 55 Pfam Domain Function
Enzyme 55 Signals
  • None
Enzyme 55 Transmembrane Regions
  • None
Enzyme 55 Essentiality Not Available
Enzyme 55 GenBank ID Protein 224282123 Link Image
Enzyme 55 UniProtKB/Swiss-Prot ID Q6NUM6 Link Image
Enzyme 55 UniProtKB/Swiss-Prot Entry Name TYW1B_HUMAN Link Image
Enzyme 55 PDB ID Not Available
Enzyme 55 Cellular Location Not Available
Enzyme 55 Gene Sequence >2007 bp
ATGGATCCTTCTGCGGATACATGGGACCTCTCCTCACCTTTAATATCATTATGGATAAAC
AGGTTTTACATTTATCTGGGCTTTGCTGTTAGCATTAGCCTTTGGATTTGTGTCCAGATT
GTCATCGAGATGCAGGGATTTGCAACAGTTCTTGCTGAAGCAGTTACGTCCCTGGATCTG
CCTGTGGCCATTATTAATCTAAAAGAATATGATCCAGATGATCATCTGATAGAAGAGGTG
ACTAGTAAAAATGTCTGTGTCTTCCTGGTTGCGACATACACTGACGGCCTACCAACCGAA
AGTGCAGAGTGGTTCTGCAAATGGTTAGAGGAAGCATCCATTGATTTTCGATTTGGCAAA
ACTTACCTGAAGGGTATGAGAGATGCGGTATTTGGCCTGGGAAATTCTGCCTATGCTAGC
CACTTCAACAAGGTTGGCAAAAATGTTGACAAGTGGCTCTGGATGCTTGGCGTGCATCGT
GTGATGAGTCGAGGGGAGGGCGACTGCGACGTGGTTAAAAGCAAGCACGGCAGCATTGAG
GCCAACTTCAGAGCATGGAAGACCAAGTTCATCTCCCAGCTGCAGGCACTTCAGAAAGGG
GAGAGAAAGAAGTCCTGTGGCGGCCACTGCAAGAAAGGCAAATGTGAATCTCACCAACAT
GGCTCAGAGGAGAGGGAGGAAGGATCTCAAGAGCAGGACGAATTGCATCACAGAGACACC
AAGGAGGAAGAACCCTTCGAGAGCTCCAGTGAAGAAGAGTTTGGTGGTGAGGACCATCAG
AGCCTAAATTCCATTGTTGATGTTGAAGATTTGGGCAAAATTATGGATCACGTGAAGAAA
GAAAAGAGAGAAAAGGAACAGCAGGAAGAGAAGTCTGGTTTGTTCAGGAACATGGGGAGG
AATGAAGATGGTGAAAGAAGAGCTATGATAACTCCTGCTCTCCGAGAAGCCCTTACTAAA
CAAGTCGATGCTCCGAGGGAGAGGAGCTTGTTACAAACACACATTCTATGGAATGAGAGC
CATCGCTGCATGGAAACCACCCCGAGCTTGGCGTGTGCTAATAAATGTGTCTTCTGTTGG
TGGCACCACAACAACCCTGTGGGCACTGAATGGTTGTGGAAGATGGACCAGCCTGAAATG
ATCTTGAAGGAAGCCATTGAAAACCATCAGAACATGATTAAGCAGTTTAAAGGAGTACCG
GGCGTCAAAGCAGAACGCTTTGAAGAAGGAATGACGGTAAAGCACTGTGCATTGTCCCTC
GTGGGAGAACCAATAATGTACCCAGAGATCAACAGGTTTTTGAAGCTACTCCACCAGTGT
AAAATCTCCAGCTTCCTGGTCACAAATGCACAATTTCCTGCGGAAATCAGGAACCTCGAG
CCAGTTACTCAGCTGTATGTCAGTGTGGATGCCAGTACCAAAGACAGCCTGAAGAAAATC
GACCGCCCACTCTTCAAGGATTTCTGGCAGCAATTCCTTGACAGTTTAAAAGCCTTGGCA
GTCAAGCAACAACGAACTGTCTACAGACTGACGCTCGTGAAAGCATGGAACGTGGACGAG
CTCCAGGCCTACGCGCAGCTCGTGTCCCTGGGGAATCCTGACTTCATCGAAGTGAAGGGC
GTTACCTACTGCAGAGAAAGTTCAGCAAGCAGTCTTACCATGGCCCATGTGCCCTGGCAT
GAGGAAGTGGTACAGTTTGTCCGCGAGCTGGTGGATCTGATCCCCGAATATGAAATTGCA
TGTGAACACGAACACTCTAATTGCCTCCTGATAGCACACAGAAAGTTTAAAATTGGTGGT
GAATGGTGGACATGGATCGATTATAACCGCTTCCAGGAGCTCATCCAGGAATATGAAGAT
AGTGGTGGATCAAAAACGTTCAGCGCAAAGGATTATATGGCCAGAACTCCTCACTGGGCA
TTATTTGGTGCCAATGAAAGAAGCTTTGATCCCAAGGACACAAGACATCAGAGAAAGAAC
AAATCAAAGGCTATTTCTGGATGTTGA
Enzyme 55 GenBank Gene ID NM_001145440.1 Link Image
Enzyme 55 GeneCard ID TYW1B Link Image
Enzyme 55 GenAtlas ID TYW1B Link Image
Enzyme 55 HGNC ID HGNC:33908 Link Image
Enzyme 55 Chromosome Location 7
Enzyme 55 Locus 7q11.23
Enzyme 55 SNPs SNPJam Report Link Image
Enzyme 55 General References
  1. 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]
  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 55 Metabolite References Not Available
Enzyme 56 [top]
Enzyme 56 ID 14196
Enzyme 56 Name Molybdenum cofactor biosynthesis protein 1
Enzyme 56 Synonyms
  1. Cell migration-inducing gene 11 protein
  2. Molybdenum cofactor synthesis-step 1 protein A-B
  3. Molybdenum cofactor biosynthesis protein A
  4. Molybdenum cofactor biosynthesis protein C
Enzyme 56 Gene Name MOCS1
Enzyme 56 Protein Sequence >Molybdenum cofactor biosynthesis protein 1
MAARPLSRMLRRLLRSSARSCSSGAPVTQPCPGESARAASEEVSRRRQFLREHAAPFSAF
LTDSFGRQHSYLRISLTEKCNLRCQYCMPEEGVPLTPKANLLTTEEILTLARLFVKEGID
KIRLTGGEPLIRPDVVDIVAQLQRLEGLRTIGVTTNGINLARLLPQLQKAGLSAINISLD
TLVPAKFEFIVRRKGFHKVMEGIHKAIELGYNPVKVNCVVMRGLNEDELLDFAALTEGLP
LDVRFIEYMPFDGNKWNFKKMVSYKEMLDTVRQQWPELEKVPEEESSTAKAFKIPGFQGQ
ISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEQELLRIIGAAVG
RKKRQHAGMFSISQMKNRPMILIELFLMFPNSPPANPSIFSWDPLHVQGLRPRMSFSSQV
ATLWKGCRVPQTPPLAQQRLGSGSFQRHYTSRADSDANSKCLSPGSWASAAPSGPQLTSE
QLTHVDSEGRAAMVDVGRKPDTERVAVASAVVLLGPVAFKLVQQNQLKKGDALVVAQLAG
VQAAKVTSQLIPLCHHVALSHIQVQLELDSTRHAVKIQASCRARGPTGVEMEALTSAAVA
ALTLYDMCKAVSRDIVLEEIKLISKTGGQRGDFHRA
Enzyme 56 Number of Residues 636
Enzyme 56 Molecular Weight 70104.5
Enzyme 56 Theoretical pI 9.75
Enzyme 56 GO Classification
Function
  • 4 iron, 4 sulfur cluster binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron-sulfur cluster binding
  • metal cluster binding
  • metal ion binding
Process
  • Mo-molybdopterin cofactor biosynthetic process
  • cellular metabolic process
  • coenzyme biosynthetic process
  • coenzyme metabolic process
  • cofactor metabolic process
  • metabolic process
Component
  • macromolecular complex
  • molybdopterin synthase complex
  • protein complex
Enzyme 56 General Function Involved in catalytic activity
Enzyme 56 Specific Function Isoform MOCS1A and isoform MOCS1B probably form a complex that catalyzes the conversion of a guanosine derivative to precursor Z during molybdenum cofactor biosynthesis
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 22027536 Link Image
Enzyme 56 UniProtKB/Swiss-Prot ID Q9NZB8 Link Image
Enzyme 56 UniProtKB/Swiss-Prot Entry Name MOCS1_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 Not Available
Enzyme 56 GeneCard ID MOCS1 Link Image
Enzyme 56 GenAtlas ID MOCS1 Link Image
Enzyme 56 HGNC ID HGNC:7190 Link Image
Enzyme 56 Chromosome Location 6
Enzyme 56 Locus 6p21.3
Enzyme 56 SNPs SNPJam Report Link Image
Enzyme 56 General References
  1. Reiss J, Cohen N, Dorche C, Mandel H, Mendel RR, Stallmeyer B, Zabot MT, Dierks T: Mutations in a polycistronic nuclear gene associated with molybdenum cofactor deficiency. Nat Genet. 1998 Sep;20(1):51-3. [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. Gray TA, Nicholls RD: Diverse splicing mechanisms fuse the evolutionarily conserved bicistronic MOCS1A and MOCS1B open reading frames. RNA. 2000 Jul;6(7):928-36. [PubMed Link Image]
  6. Hanzelmann P, Schwarz G, Mendel RR: Functionality of alternative splice forms of the first enzymes involved in human molybdenum cofactor biosynthesis. J Biol Chem. 2002 May 24;277(21):18303-12. Epub 2002 Mar 12. [PubMed Link Image]
  7. Gross-Hardt S, Reiss J: The bicistronic MOCS1 gene has alternative start codons on two mutually exclusive exons. Mol Genet Metab. 2002 Aug;76(4):340-3. [PubMed Link Image]
  8. Hanzelmann P, Hernandez HL, Menzel C, Garcia-Serres R, Huynh BH, Johnson MK, Mendel RR, Schindelin H: Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis. J Biol Chem. 2004 Aug 13;279(33):34721-32. Epub 2004 Jun 4. [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. Reiss J, Christensen E, Kurlemann G, Zabot MT, Dorche C: Genomic structure and mutational spectrum of the bicistronic MOCS1 gene defective in molybdenum cofactor deficiency type A. Hum Genet. 1998 Dec;103(6):639-44. [PubMed Link Image]
  11. Reiss J, Johnson JL: Mutations in the molybdenum cofactor biosynthetic genes MOCS1, MOCS2, and GEPH. Hum Mutat. 2003 Jun;21(6):569-76. [PubMed Link Image]
  12. Leimkuhler S, Charcosset M, Latour P, Dorche C, Kleppe S, Scaglia F, Szymczak I, Schupp P, Hahnewald R, Reiss J: Ten novel mutations in the molybdenum cofactor genes MOCS1 and MOCS2 and in vitro characterization of a MOCS2 mutation that abolishes the binding ability of molybdopterin synthase. Hum Genet. 2005 Oct;117(6):565-70. Epub 2005 Jul 14. [PubMed Link Image]
Enzyme 56 Metabolite References Not Available
Enzyme 57 [top]
Enzyme 57 ID 14385
Enzyme 57 Name Radical S-adenosyl methionine domain-containing protein 2
Enzyme 57 Synonyms
  1. Cytomegalovirus-induced gene 5 protein
  2. Viperin
  3. Virus inhibitory protein, endoplasmic reticulum-associated, interferon-inducible
Enzyme 57 Gene Name RSAD2
Enzyme 57 Protein Sequence >Radical S-adenosyl methionine domain-containing protein 2
MWVLTPAAFAGKLLSVFRQPLSSLWRSLVPLFCWLRATFWLLATKRRKQQLVLRGPDETK
EEEEDPPLPTTPTSVNYHFTRQCNYKCGFCFHTAKTSFVLPLEEAKRGLLLLKEAGMEKI
NFSGGEPFLQDRGEYLGKLVRFCKVELRLPSVSIVSNGSLIRERWFQNYGEYLDILAISC
DSFDEEVNVLIGRGQGKKNHVENLQKLRRWCRDYRVAFKINSVINRFNVEEDMTEQIKAL
NPVRWKVFQCLLIEGENCGEDALREAERFVIGDEEFERFLERHKEVSCLVPESNQKMKDS
YLILDEYMRFLNCRKGRKDPSKSILDVGVEEAIKFSGFDEKMFLKRGGKYIWSKADLKLD
W
Enzyme 57 Number of Residues 361
Enzyme 57 Molecular Weight 42169.3
Enzyme 57 Theoretical pI 8.33
Enzyme 57 GO Classification
Function
  • binding
  • catalytic activity
  • iron-sulfur cluster binding
  • metal cluster binding
Process
Component
Enzyme 57 General Function Involved in catalytic activity
Enzyme 57 Specific Function Involved in antiviral defense. May impair virus budding by disrupting lipid rafts at the plasma membrane, a feature which is essential for the budding process of many viruses. Acts through binding with and inactivating FPPS, an enzyme involved in synthesis of cholesterol, farnesylated and geranylated proteins, ubiquinones dolichol and heme. Plays a major role in the cell antiviral state induced by type I and type II interferon. Displays antiviral effect against HIV-1 virus, hepatitis C virus, human cytomegalovirus, and aphaviruses, but not vesiculovirus
Enzyme 57 Pathways Not Available
Enzyme 57 Reactions Not Available
Enzyme 57 Pfam Domain Function
Enzyme 57 Signals
  • None
Enzyme 57 Transmembrane Regions
  • None
Enzyme 57 Essentiality Not Available
Enzyme 57 GenBank ID Protein 62822253 Link Image
Enzyme 57 UniProtKB/Swiss-Prot ID Q8WXG1 Link Image
Enzyme 57 UniProtKB/Swiss-Prot Entry Name RSAD2_HUMAN Link Image
Enzyme 57 PDB ID Not Available
Enzyme 57 Cellular Location Not Available
Enzyme 57 Gene Sequence >1086 bp
ATGTGGGTGCTTACACCTGCTGCTTTTGCTGGGAAGCTCTTGAGTGTGTTCAGGCAACCT
CTGAGCTCTCTGTGGAGGAGCCTGGTCCCGCTGTTCTGCTGGCTGAGGGCAACCTTCTGG
CTGCTAGCTACCAAGAGGAGAAAGCAGCAGCTGGTCCTGAGAGGGCCAGATGAGACCAAA
GAGGAGGAAGAGGACCCTCCTCTGCCCACCACCCCAACCAGCGTCAACTATCACTTCACT
CGCCAGTGCAACTACAAATGCGGCTTCTGTTTCCACACAGCCAAAACATCCTTTGTGCTG
CCCCTTGAGGAAGCAAAGAGAGGATTGCTTTTGCTTAAGGAAGCTGGTATGGAGAAGATC
AACTTTTCAGGTGGAGAGCCATTTCTTCAAGACCGGGGAGAATACCTGGGCAAGTTGGTG
AGGTTCTGCAAAGTAGAGTTGCGGCTGCCCAGCGTGAGCATCGTGAGCAATGGAAGCCTG
ATCCGGGAGAGGTGGTTCCAGAATTATGGTGAGTATTTGGACATTCTCGCTATCTCCTGT
GACAGCTTTGACGAGGAAGTCAATGTCCTTATTGGCCGTGGCCAAGGAAAGAAGAACCAT
GTGGAAAACCTTCAAAAGCTGAGGAGGTGGTGTAGGGATTATAGAGTCGCTTTCAAGATA
AATTCTGTCATTAATCGTTTCAACGTGGAAGAGGACATGACGGAACAGATCAAAGCACTA
AACCCTGTCCGCTGGAAAGTGTTCCAGTGCCTCTTAATTGAGGGTGAGAATTGTGGAGAA
GATGCTCTAAGAGAAGCAGAAAGATTTGTTATTGGTGATGAAGAATTTGAAAGATTCTTG
GAGCGCCACAAAGAAGTGTCCTGCTTGGTGCCTGAATCTAACCAGAAGATGAAAGACTCC
TACCTTATTCTGGATGAATATATGCGCTTTCTGAACTGTAGAAAGGGACGGAAGGACCCT
TCCAAGTCCATCCTGGATGTTGGTGTAGAAGAAGCTATAAAATTCAGTGGATTTGATGAA
AAGATGTTTCTGAAGCGAGGAGGAAAATACATATGGAGTAAGGCTGATCTGAAGCTGGAT
TGGTAG
Enzyme 57 GenBank Gene ID AC017076 Link Image
Enzyme 57 GeneCard ID RSAD2 Link Image
Enzyme 57 GenAtlas ID RSAD2 Link Image
Enzyme 57 HGNC ID HGNC:30908 Link Image
Enzyme 57 Chromosome Location 2
Enzyme 57 Locus 2p25.2
Enzyme 57 SNPs SNPJam Report Link Image
Enzyme 57 General References
  1. Zhu H, Cong JP, Shenk T: Use of differential display analysis to assess the effect of human cytomegalovirus infection on the accumulation of cellular RNAs: induction of interferon-responsive RNAs. Proc Natl Acad Sci U S A. 1997 Dec 9;94(25):13985-90. [PubMed Link Image]
  2. Chin KC, Cresswell P: Viperin (cig5), an IFN-inducible antiviral protein directly induced by human cytomegalovirus. Proc Natl Acad Sci U S A. 2001 Dec 18;98(26):15125-30. [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. 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. Olofsson PS, Jatta K, Wagsater D, Gredmark S, Hedin U, Paulsson-Berne G, Soderberg-Naucler C, Hansson GK, Sirsjo A: The antiviral cytomegalovirus inducible gene 5/viperin is expressed in atherosclerosis and regulated by proinflammatory agents. Arterioscler Thromb Vasc Biol. 2005 Jul;25(7):e113-6. Epub 2005 May 12. [PubMed Link Image]
  6. Helbig KJ, Lau DT, Semendric L, Harley HA, Beard MR: Analysis of ISG expression in chronic hepatitis C identifies viperin as a potential antiviral effector. Hepatology. 2005 Sep;42(3):702-10. [PubMed Link Image]
  7. Khaiboullina SF, Rizvanov AA, Holbrook MR, St Jeor S: Yellow fever virus strains Asibi and 17D-204 infect human umbilical cord endothelial cells and induce novel changes in gene expression. Virology. 2005 Nov 25;342(2):167-76. Epub 2005 Sep 15. [PubMed Link Image]
  8. Severa M, Coccia EM, Fitzgerald KA: Toll-like receptor-dependent and -independent viperin gene expression and counter-regulation by PRDI-binding factor-1/BLIMP1. J Biol Chem. 2006 Sep 8;281(36):26188-95. Epub 2006 Jul 18. [PubMed Link Image]
  9. Rivieccio MA, Suh HS, Zhao Y, Zhao ML, Chin KC, Lee SC, Brosnan CF: TLR3 ligation activates an antiviral response in human fetal astrocytes: a role for viperin/cig5. J Immunol. 2006 Oct 1;177(7):4735-41. [PubMed Link Image]
  10. Zhang Y, Burke CW, Ryman KD, Klimstra WB: Identification and characterization of interferon-induced proteins that inhibit alphavirus replication. J Virol. 2007 Oct;81(20):11246-55. Epub 2007 Aug 8. [PubMed Link Image]
  11. Wang X, Hinson ER, Cresswell P: The interferon-inducible protein viperin inhibits influenza virus release by perturbing lipid rafts. Cell Host Microbe. 2007 Aug 16;2(2):96-105. [PubMed Link Image]
  12. Waheed AA, Freed EO: Influenza virus not cRAFTy enough to dodge viperin. Cell Host Microbe. 2007 Aug 16;2(2):71-2. [PubMed Link Image]
Enzyme 57 Metabolite References Not Available
Enzyme 58 [top]
Enzyme 58 ID 14748
Enzyme 58 Name Probable histone-lysine N-methyltransferase ASH1L
Enzyme 58 Synonyms
  1. ASH1-like protein
  2. huASH1
  3. Absent small and homeotic disks protein 1 homolog
  4. Lysine N-methyltransferase 2H
Enzyme 58 Gene Name ASH1L
Enzyme 58 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 58 Number of Residues 2969
Enzyme 58 Molecular Weight 332787.2
Enzyme 58 Theoretical pI 9.95
Enzyme 58 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 58 General Function Involved in DNA binding
Enzyme 58 Specific Function Histone methyltransferase. Probably methylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation
Enzyme 58 Pathways
Enzyme 58 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 58 Pfam Domain Function
Enzyme 58 Signals
  • None
Enzyme 58 Transmembrane Regions
  • None
Enzyme 58 Essentiality Not Available
Enzyme 58 GenBank ID Protein 7739725 Link Image
Enzyme 58 UniProtKB/Swiss-Prot ID Q9NR48 Link Image
Enzyme 58 UniProtKB/Swiss-Prot Entry Name ASH1L_HUMAN Link Image
Enzyme 58 PDB ID Not Available
Enzyme 58 Cellular Location Not Available
Enzyme 58 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 58 GenBank Gene ID AF257305 Link Image
Enzyme 58 GeneCard ID ASH1L Link Image
Enzyme 58 GenAtlas ID ASH1L Link Image
Enzyme 58 HGNC ID HGNC:19088 Link Image
Enzyme 58 Chromosome Location 1
Enzyme 58 Locus 1q22
Enzyme 58 SNPs SNPJam Report Link Image
Enzyme 58 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 58 Metabolite References Not Available
Enzyme 59 [top]
Enzyme 59 ID 14749
Enzyme 59 Name N-acetylserotonin O-methyltransferase-like protein
Enzyme 59 Synonyms
  1. ASMTL
Enzyme 59 Gene Name ASMTL
Enzyme 59 Protein Sequence >N-acetylserotonin O-methyltransferase-like protein
MVLCPVIGKLLHKRVVLASASPRRQEILSNAGLRFEVVPSKFKEKLDKASFATPYGYAME
TAKQKALEVANRLYQKDLRAPDVVIGADTIVTVGGLILEKPVDKQDAYRMLSRLSGREHS
VFTGVAIVHCSSKDHQLDTRVSEFYEETKVKFSELSEELLWEYVHSGEPMDKAGGYGIQA
LGGMLVESVHGDFLNVVGFPLNHFCKQLVKLYYPPRPEDLRRSVKHDSIPAADTFEDLSD
VEGGGSEPTQRDAGSRDEKAEAGEAGQATAEAECHRTRETLPPFPTRLLELIEGFMLSKG
LLTACKLKVFDLLKDEAPQKAADIASKVDASACGMERLLDICAAMGLLEKTEQGYSNTET
ANVYLASDGEYSLHGFIMHNNDLTWNLFTYLEFAIREGTNQHHRALGKKAEDLFQDAYYQ
SPETRLRFMRAMHGMTKLTACQVATAFNLSRFSSACDVGGCTGALARELAREYPRMQVTV
FDLPDIIELAAHFQPPGPQAVQIHFAAGDFFRDPLPSAELYVLCRILHDWPDDKVHKLLS
RVAESCKPGAGLLLVETLLDEEKRVAQRALMQSLNMLVQTEGKERSLGEYQCLLELHGFH
QVQVVHLGGVLDAILATKVAP
Enzyme 59 Number of Residues 621
Enzyme 59 Molecular Weight 68856.1
Enzyme 59 Theoretical pI 5.98
Enzyme 59 GO Classification
Function
  • O-methyltransferase activity
  • 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 O-methyltransferase activity
Enzyme 59 Specific Function Unknown. The presence of the putative catalytic domain of S-adenosyl-L-methionine binding argues for a methyltransferase activity
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 117553627 Link Image
Enzyme 59 UniProtKB/Swiss-Prot ID O95671 Link Image
Enzyme 59 UniProtKB/Swiss-Prot Entry Name ASML_HUMAN Link Image
Enzyme 59 PDB ID Not Available
Enzyme 59 Cellular Location Not Available
Enzyme 59 Gene Sequence >1866 bp
ATGGTGCTGTGCCCGGTGATTGGGAAGCTGCTGCACAAGCGCGTGGTGCTGGCCAGCGCC
TCCCCACGCCGTCAGGAGATCCTCAGCAACGCGGGTCTCAGGTTTGAGGTGGTCCCCTCC
AAGTTTAAAGAGAAGCTGGACAAAGCCTCCTTCGCTACTCCGTATGGGTACGCCATGGAG
ACCGCCAAGCAGAAGGCCCTGGAGGTGGCCAACCGGCTGTACCAGAAAGACCTGCGGGCC
CCCGACGTGGTCATTGGAGCGGACACGATCGTGACAGTCGGGGGGCTGATTCTGGAGAAG
CCGGTGGACAAGCAGGACGCCTACAGGATGCTGTCCCGGTTGAGTGGGAGAGAACACAGC
GTGTTCACAGGTGTCGCGATCGTCCACTGCTCCAGCAAAGACCATCAGCTGGACACCAGG
GTCTCGGAATTCTACGAGGAAACGAAGGTGAAGTTCTCGGAGCTGTCCGAGGAGCTGCTC
TGGGAATACGTCCACAGCGGGGAGCCCATGGACAAAGCTGGCGGCTACGGGATCCAGGCC
CTGGGCGGCATGCTGGTGGAGTCCGTACACGGGGACTTTCTGAACGTGGTGGGATTCCCG
CTGAACCACTTCTGCAAGCAGCTGGTGAAGCTCTACTACCCGCCCCGTCCGGAGGACCTG
CGGCGGAGTGTCAAGCACGACTCCATCCCGGCCGCGGACACCTTCGAAGACCTCAGTGAC
GTGGAGGGGGGCGGCTCGGAGCCCACTCAGAGGGACGCGGGCAGCCGCGATGAGAAGGCC
GAGGCGGGAGAGGCGGGACAGGCCACGGCAGAGGCTGAGTGTCACAGGACTCGGGAGACC
CTGCCTCCGTTCCCGACACGCCTCCTGGAGCTGATTGAGGGCTTTATGCTATCCAAGGGC
CTGCTCACCGCTTGCAAACTGAAGGTGTTCGATTTGTTAAAAGATGAAGCACCCCAGAAG
GCTGCGGATATTGCCAGCAAAGTGGACGCCTCTGCGTGTGGAATGGAGAGGCTTCTGGAC
ATCTGTGCTGCCATGGGGCTCCTGGAGAAGACAGAGCAAGGTTACAGTAACACAGAGACA
GCGAACGTCTACCTGGCATCGGATGGCGAATACTCTCTGCACGGCTTCATCATGCACAAT
AATGACCTCACATGGAACCTCTTTACATACCTGGAGTTTGCCATCCGAGAGGGAACAAAC
CAGCACCACAGGGCGTTGGGGAAGAAGGCGGAAGATCTGTTCCAGGATGCGTACTACCAG
AGCCCGGAGACGCGGCTGAGGTTCATGCGGGCCATGCACGGCATGACGAAGCTGACTGCG
TGCCAGGTGGCCACGGCCTTCAATCTGTCCCGCTTCTCCTCCGCCTGCGACGTGGGAGGC
TGCACGGGTGCACTGGCCCGAGAGCTGGCCCGTGAGTACCCTCGTATGCAGGTGACTGTG
TTTGACCTCCCAGACATTATCGAGCTGGCCGCCCACTTCCAACCCCCCGGACCGCAGGCA
GTGCAGATCCACTTCGCAGCAGGTGACTTTTTCAGGGACCCCCTCCCCAGCGCTGAGCTG
TACGTCCTGTGCCGGATCCTGCATGACTGGCCAGACGACAAAGTCCACAAGTTACTCAGC
AGGGTCGCCGAGAGCTGCAAGCCAGGGGCCGGCCTGCTGCTGGTGGAGACGCTCCTGGAT
GAGGAGAAGAGGGTGGCGCAGCGCGCCCTGATGCAGTCACTGAACATGCTGGTGCAGACT
GAAGGCAAGGAGCGGAGCCTGGGCGAGTATCAGTGCTTGCTGGAGCTGCACGGCTTCCAC
CAGGTGCAGGTGGTGCACTTGGGGGGTGTCCTGGATGCCATCTTGGCCACCAAAGTGGCC
CCCTGA
Enzyme 59 GenBank Gene ID NM_004192.3 Link Image
Enzyme 59 GeneCard ID ASMTL Link Image
Enzyme 59 GenAtlas ID ASMTL Link Image
Enzyme 59 HGNC ID HGNC:751 Link Image
Enzyme 59 Chromosome Location Not Available
Enzyme 59 Locus Not Available
Enzyme 59 SNPs SNPJam Report Link Image
Enzyme 59 General References
  1. Ried K, Rao E, Schiebel K, Rappold GA: Gene duplications as a recurrent theme in the evolution of the human pseudoautosomal region 1: isolation of the gene ASMTL. Hum Mol Genet. 1998 Oct;7(11):1771-8. [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. 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. 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]
  6. 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]
  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. 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]
  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. 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 59 Metabolite References Not Available
Enzyme 60 [top]
Enzyme 60 ID 14750
Enzyme 60 Name Histone-arginine methyltransferase CARM1
Enzyme 60 Synonyms
  1. Coactivator-associated arginine methyltransferase 1
  2. Protein arginine N-methyltransferase 4
Enzyme 60 Gene Name CARM1
Enzyme 60 Protein Sequence >Histone-arginine methyltransferase CARM1
MAAAAAAVGPGAGGAGSAVPGGAGPCATVSVFPGARLLTIGDANGEIQRHAEQQALRLEV
RAGPDSAGIALYSHEDVCVFKCSVSRETECSRVGKQSFIITLGCNSVLIQFATPNDFCSF
YNILKTCRGHTLERSVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNH
TDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDRIVVIPG
KVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSGNMFPTIGDVHLAPFTDE
QLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEYFRQPVVDTFDIRILMAKSVKYTVNFL
EAKEGDLHRIEIPFKFHMLHSGLVHGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRC
LFQSPLFAKAGDTLSGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYTGTT
PSPPPGSHYTSPSENMWNTGSTYNLSSGMAVAGMPTAYDLSSVIASGSSVGHNNLIPLAN
TGIVNHTHSRMGSIMSTGIVQGSSGAQGSGGGSTSAHYAVNSQFTMGGPAISMASPMSIP
TNTMHYGS
Enzyme 60 Number of Residues 608
Enzyme 60 Molecular Weight 65853.2
Enzyme 60 Theoretical pI 6.73
Enzyme 60 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 60 General Function Involved in pathogenesis
Enzyme 60 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 60 Pathways
Enzyme 60 Reactions
  • S-adenosyl-L-methionine + histone-arginine = S-adenosyl-L-homocysteine + histone-Nomega-methyl-arginine [RN:R04718]
Enzyme 60 Pfam Domain Function
Enzyme 60 Signals
  • None
Enzyme 60 Transmembrane Regions
  • None
Enzyme 60 Essentiality Not Available
Enzyme 60 GenBank ID Protein 40288288 Link Image
Enzyme 60 UniProtKB/Swiss-Prot ID Q86X55 Link Image
Enzyme 60 UniProtKB/Swiss-Prot Entry Name CARM1_HUMAN Link Image
Enzyme 60 PDB ID Not Available
Enzyme 60 Cellular Location Not Available
Enzyme 60 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 60 GenBank Gene ID NM_199141.1 Link Image
Enzyme 60 GeneCard ID CARM1 Link Image
Enzyme 60 GenAtlas ID CARM1 Link Image
Enzyme 60 HGNC ID HGNC:23393 Link Image
Enzyme 60 Chromosome Location 1
Enzyme 60 Locus 19p13.2
Enzyme 60 SNPs SNPJam Report Link Image
Enzyme 60 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 60 Metabolite References Not Available
Enzyme 61 [top]
Enzyme 61 ID 14751
Enzyme 61 Name CDK5 regulatory subunit-associated protein 1-like 1
Enzyme 61 Synonyms Not Available
Enzyme 61 Gene Name CDKAL1
Enzyme 61 Protein Sequence >CDK5 regulatory subunit-associated protein 1-like 1
MPSASCDTLLDDIEDIVSQEDSKPQDRHFVRKDVVPKVRRRNTQKYLQEEENSPPSDSTI
PGIQKIWIRTWGCSHNNSDGEYMAGQLAAYGYKITENASDADLWLLNSCTVKNPAEDHFR
NSIKKAQEENKKIVLAGCVPQAQPRQDYLKGLSIIGVQQIDRVVEVVEETIKGHSVRLLG
QKKDNGRRLGGARLDLPKIRKNPLIEIISINTGCLNACTYCKTKHARGNLASYPIDELVD
RAKQSFQEGVCEIWLTSEDTGAYGRDIGTNLPTLLWKLVEVIPEGAMLRLGMTNPPYILE
HLEEMAKILNHPRVYAFLHIPVQSASDSVLMEMKREYCVADFKRVVDFLKEKVPGITIAT
DIICGFPGETDQDFQETVKLVEEYKFPSLFINQFYPRPGTPAAKMEQVPAQVKKQRTKDL
SRVFHSYSPYDHKIGERQQVLVTEESFDSKFYVAHNQFYEQVLVPKNPAFMGKMVEVDIY
ESGKHFMKGQPVSDAKVYTPSISKPLAKGEVSGLTKDFRNGLGNQLSSGSHTSAASQCDS
ASSRMVLPMPRLHQDCALRMSVGLALLGLLFAFFVKVYN
Enzyme 61 Number of Residues 579
Enzyme 61 Molecular Weight 65111.0
Enzyme 61 Theoretical pI 7.51
Enzyme 61 GO Classification
Function
  • 4 iron, 4 sulfur cluster binding
  • binding
  • catalytic activity
  • iron-sulfur cluster binding
  • metal cluster binding
Process
  • RNA metabolic process
  • RNA modification
  • cellular macromolecule metabolic process
  • macromolecule metabolic process
  • metabolic process
Component
Enzyme 61 General Function Involved in catalytic activity
Enzyme 61 Specific Function Not Available
Enzyme 61 Pathways Not Available
Enzyme 61 Reactions Not Available
Enzyme 61 Pfam Domain Function
Enzyme 61 Signals
  • None
Enzyme 61 Transmembrane Regions
  • 556-578
Enzyme 61 Essentiality Not Available
Enzyme 61 GenBank ID Protein 7020375 Link Image
Enzyme 61 UniProtKB/Swiss-Prot ID Q5VV42 Link Image
Enzyme 61 UniProtKB/Swiss-Prot Entry Name CDKAL_HUMAN Link Image
Enzyme 61 PDB ID Not Available
Enzyme 61 Cellular Location Not Available
Enzyme 61 Gene Sequence >1740 bp
ATGCCTTCTGCATCCTGTGATACACTACTGGATGACATCGAAGATATCGTGTCTCAGGAA
GATTCAAAACCACAAGATAGGCATTTTGTAAGAAAGGATGTTGTCCCGAAGGTACGAAGG
CGAAATACCCAAAAATATTTGCAAGAGGAAGAAAACAGTCCACCAAGTGACAGCACTATT
CCAGGCATACAGAAAATTTGGATACGAACATGGGGTTGTTCTCATAATAATTCAGATGGA
GAATATATGGCTGGACAGCTAGCTGCTTATGGCTATAAAATTACAGAAAATGCATCCGAT
GCAGATTTATGGCTCCTGAACAGTTGCACTGTAAAAAACCCAGCTGAAGACCACTTTAGA
AACTCAATTAAAAAAGCTCAAGAGGAGAACAAGAAAATCGTACTGGCTGGATGCGTTCCT
CAAGCCCAGCCTCGCCAGGACTACCTTAAGGGACTGAGTATCATTGGGGTTCAGCAGATA
GATCGTGTGGTAGAAGTTGTGGAGGAGACAATTAAAGGTCACTCTGTGAGACTGCTGGGT
CAGAAAAAGGATAATGGAAGGCGGCTTGGGGGAGCACGATTGGATTTGCCGAAGATTAGG
AAGAATCCACTGATAGAAATCATTTCCATCAGTACCGGGTGTCTCAATGCTTGTACCTAC
TGCAAAACTAAACACGCCAGAGGAAATTTGGCCAGTTATCCAATTGATGAACTAGTAGAT
AGAGCCAAACAATCTTTTCAAGAGGGTGTTTGTGAGATATGGTTGACCAGTGAAGACACG
GGGGCTTATGGCAGAGATATTGGCACCAATCTCCCCACACTCCTGTGGAAACTGGTTGAA
GTGATTCCTGAGGGAGCAATGCTGAGGCTTGGCATGACAAATCCGCCCTATATTTTAGAG
CATCTGGAGGAAATGGCAAAAATCCTTAATCACCCCAGAGTCTACGCTTTTCTGCACATA
CCAGTCCAGTCTGCCTCCGACAGCGTACTCATGGAAATGAAAAGAGAATACTGTGTGGCT
GACTTCAAAAGAGTAGTGGATTTTCTGAAAGAGAAAGTTCCTGGAATAACTATTGCTACA
GATATTATCTGTGGTTTTCCTGGAGAAACAGATCAGGATTTTCAAGAAACAGTGAAACTT
GTTGAAGAGTACAAATTCCCAAGCCTGTTTATTAACCAATTTTACCCAAGACCAGGAACT
CCTGCTGCAAAAATGGAACAAGTTCCAGCACAAGTGAAAAAGCAAAGGACAAAAGATCTT
TCTCGGGTGTTTCATTCTTACAGTCCATATGATCACAAGATTGGTGAAAGACAACAAGTG
TTAGTAACAGAAGAATCTTTTGATTCCAAGTTTTATGTTGCACACAATCAATTCTATGAG
CAGGTTTTAGTGCCAAAGAACCCTGCGTTCATGGGGAAGATGGTTGAAGTGGACATCTAT
GAATCAGGCAAACATTTTATGAAAGGGCAGCCAGTATCTGATGCCAAAGTGTACACGCCC
TCCATCAGCAAACCGCTAGCAAAGGGAGAAGTCTCAGGTTTGACAAAGGACTTCAGAAAT
GGGCTTGGGAACCAGCTGAGTTCAGGATCCCACACCTCTGCTGCATCTCAGTGTGACTCA
GCGAGTTCCAGAATGGTGCTGCCCATGCCAAGGCTACATCAAGACTGTGCGCTGAGGATG
TCCGTGGGCTTGGCTCTGCTGGGTCTTCTTTTTGCTTTTTTTGTCAAGGTCTATAATTAG
Enzyme 61 GenBank Gene ID AK000349 Link Image
Enzyme 61 GeneCard ID CDKAL1 Link Image
Enzyme 61 GenAtlas ID CDKAL1 Link Image
Enzyme 61 HGNC ID HGNC:21050 Link Image
Enzyme 61 Chromosome Location 6
Enzyme 61 Locus 6p22.3
Enzyme 61 SNPs SNPJam Report Link Image
Enzyme 61 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. 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]
  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 61 Metabolite References Not Available
Enzyme 62 [top]
Enzyme 62 ID 14752
Enzyme 62 Name CDK5 regulatory subunit-associated protein 1
Enzyme 62 Synonyms
  1. CDK5 activator-binding protein C42
Enzyme 62 Gene Name CDK5RAP1
Enzyme 62 Protein Sequence >CDK5 regulatory subunit-associated protein 1
MHPLQCVLQVQRSLGWGPLASVSWLSLRMCRAHSSLSSTMCPSPERQEDGARKDFSSRLA
AGPTFQHFLKSASAPQEKLSSEVEDPPPYLMMDELLGRQRKVYLETYGCQMNVNDTEIAW
SILQKSGYLRTSNLQEADVILLVTCSIREKAEQTIWNRLHQLKALKTRRPRSRVPLRIGI
LGCMAERLKEEILNREKMVDILAGPDAYRDLPRLLAVAESGQQAANVLLSLDETYADVMP
VQTSASATSAFVSIMRGCDNMCSYCIVPFTRGRERSRPIASILEEVKKLSEQVFLPPRPP
KVLGLQGLKEVTLLGQNVNSFRDNSEVQFNSAVPTNLSRGFTTNYKTKQGGLRFAHLLDQ
VSRVDPEMRIRFTSPHPKDFPDEVLQLIHERDNICKQIHLPAQSGSSRVLEAMRRGYSRE
AYVELVHHIRESIPGVSLSSDFIAGFCGETEEDHVQTVSLLREVQYNMGFLFAYSMRQKT
RAYHRLKDDVPEEVKLRRLEELITIFREEATKANQTSVGCTQLVLVEGLSKRSATDLCGR
NDGNLKVIFPDAEMEDVNNPGLRVRAQPGDYVLVKITSASSQTLRGHVLCRTTLRDSSAY
C
Enzyme 62 Number of Residues 601
Enzyme 62 Molecular Weight 67687.9
Enzyme 62 Theoretical pI 8.28
Enzyme 62 GO Classification
Function
  • 4 iron, 4 sulfur cluster binding
  • binding
  • catalytic activity
  • iron-sulfur cluster binding
  • metal cluster binding
  • transferase activity
Process
  • RNA metabolic process
  • RNA modification
  • cellular macromolecule metabolic process
  • macromolecule metabolic process
  • metabolic process
  • ncRNA metabolic process
  • tRNA metabolic process
  • tRNA modification
  • tRNA processing
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 62 General Function Involved in catalytic activity
Enzyme 62 Specific Function Specifically inhibits CDK5 activation by CDK5R1
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 56205140 Link Image
Enzyme 62 UniProtKB/Swiss-Prot ID Q96SZ6 Link Image
Enzyme 62 UniProtKB/Swiss-Prot Entry Name CK5P1_HUMAN Link Image
Enzyme 62 PDB ID Not Available
Enzyme 62 Cellular Location Not Available
Enzyme 62 Gene Sequence >3606 bp
ATGCACCCTTTACAGTGTGTCCTCCAAGTGCAGAGGTCTCTGGGGTGGGGACCATTGGCC
TCTGTGTCTTGGCTGTCGCTGAGGATGTGCAGGGCACACAGCAGTCTCTCTAGTACCATG
TGTCCCAGTCCAGAGAGGCAGGAGGATGGAGCTCGGAAGGATTTCAGCTCCAGGCTGGCT
GCTGGACCGACTTTTCAACATTTTTTAAAAAGTGCCTCAGCTCCTCAGGAGAAGCTGTCT
TCAGAAGTGGAAGACCCACCTCCCTATCTCATGATGGATGAACTTCTTGGAAGGCAGAGA
AAAGTCTACCTCGAGACCTATGGCTGCCAGATGAATGTGAATGACACAGAGATAGCCTGG
TCCATCTTACAGAAGAGTGGCTACCTGCGGACCAGTAACCTCCAAGAGGCAGATGTGATT
CTCCTTGTCACATGCTCTATCAGGGAGAAGGCTGAGCAGACCATCTGGAACCGTTTACAT
CAGCTTAAAGCCTTGAAGACAAGGCGGCCCCGCTCCCGGGTTCCTCTGAGGATTGGAATT
CTAGGCTGCATGGCTGAGAGGTTGAAGGAGGAGATTCTCAACAGAGAGAAAATGGTAGAT
ATTTTGGCTGGTCCTGATGCCTACCGGGACCTTCCCCGGCTGCTGGCTGTTGCTGAGTCG
GGCCAGCAAGCTGCCAACGTGCTGCTCTCTCTGGACGAGACCTATGCTGATGTCATGCCA
GTCCAGACAAGCGCCAGTGCCACGTCTGCCTTTGTGTCAATCATGCGAGGCTGTGACAAC
ATGTGTAGCTACTGCATTGTTCCTTTCACCCGGGGCAGGGAGAGGAGTCGGCCTATTGCC
TCCATTCTAGAGGAAGTGAAGAAGCTTTCTGAGCAGGTGTTCCTCCCACCTCGGCCTCCC
AAAGTGTTGGGATTACAGGGGCTGAAAGAAGTGACACTTCTTGGTCAGAATGTTAATAGT
TTTCGGGACAATTCGGAGGTCCAGTTCAACAGTGCAGTGCCTACCAATCTCAGTCGTGGC
TTTACCACCAACTATAAAACCAAGCAAGGAGGACTTCGTTTTGCTCATCTTCTGGATCAG
GTCTCCAGAGTAGATCCTGAAATGAGGATCCGTTTTACCTCTCCCCACCCCAAGGATTTT
CCTGATGAGGTTCTGCAGCTGATTCATGAGAGAGATAACATCTGTAAACAGATCCACCTG
CCAGCCCAGAGTGGAAGCAGCCGTGTGTTGGAGGCCATGCGGAGGGGATATTCAAGAGAA
GCTTATGTGGAGTTAGTTCACCATATTAGAGAATCTATTCCAGGTGTGAGCCTCAGCAGC
GATTTCATTGCTGGCTTTTGTGGTGAGACGGAGGAAGATCACGTCCAGACAGTCTCTTTG
CTCCGGGAAGTTCAGTACAACATGGGCTTCCTCTTTGCCTACAGCATGAGACAGAAGACA
CGGGCATATCATAGGCTGAAGGATGATGTCCCGGAAGAGGTAAAATTAAGGCGTTTGGAG
GAACTCATCACTATCTTCCGAGAAGAAGCAACAAAAGCCAATCAGACCTCTGTGGGCTGT
ACCCAGTTGGTGCTAGTGGAAGGGCTCAGTAAACGCTCTGCCACTGACCTGTGTGGCAGG
AATGATGGAAACCTTAAGGTGATCTTCCCTGATGCAGAGATGGAGGATGTCAATAACCCT
GGGCTCAGGGTCAGAGCCCAGCCTGGGGACTATGTGCTGGTGAAGATCACCTCAGCCAGT
TCTCAGACACTTAGGGGACATGTTCTCTGCAGGACCACTCTGAGGGACTCTTCTGCATAT
TGCTGA
Enzyme 62 GenBank Gene ID AL355392 Link Image
Enzyme 62 GeneCard ID CDK5RAP1 Link Image
Enzyme 62 GenAtlas ID CDK5RAP1 Link Image
Enzyme 62 HGNC ID HGNC:15880 Link Image
Enzyme 62 Chromosome Location 2
Enzyme 62 Locus 20pter-q11.23
Enzyme 62 SNPs SNPJam Report Link Image
Enzyme 62 General References
  1. Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W: Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. Genome Res. 2000 May;10(5):703-13. [PubMed Link Image]
  2. Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed Link Image]
  3. 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. 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]
  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. Ching YP, Qi Z, Wang JH: Cloning of three novel neuronal Cdk5 activator binding proteins. Gene. 2000 Jan 25;242(1-2):285-94. [PubMed Link Image]
  7. Ching YP, Pang AS, Lam WH, Qi RZ, Wang JH: Identification of a neuronal Cdk5 activator-binding protein as Cdk5 inhibitor. J Biol Chem. 2002 May 3;277(18):15237-40. Epub 2002 Mar 6. [PubMed Link Image]
Enzyme 62 Metabolite References Not Available
Enzyme 63 [top]
Enzyme 63 ID 14753
Enzyme 63 Name Elongator complex protein 3
Enzyme 63 Synonyms
  1. hELP3
Enzyme 63 Gene Name ELP3
Enzyme 63 Protein Sequence >Elongator complex protein 3
MRQKRKGDLSPAELMMLTIGDVIKQLIEAHEQGKDIDLNKVKTKTAAKYGLSAQPRLVDI
IAAVPPQYRKVLMPKLKAKPIRTASGIAVVAVMCKPHRCPHISFTGNICVYCPGGPDSDF
EYSTQSYTGYEPTSMRAIRARYDPFLQTRHRIEQLKQLGHSVDKVEFIVMGGTFMALPEE
YRDYFIRNLHDALSGHTSNNIYEAVKYSERSLTKCIGITIETRPDYCMKRHLSDMLTYGC
TRLEIGVQSVYEDVARDTNRGHTVKAVCESFHLAKDSGFKVVAHMMPDLPNVGLERDIEQ
FTEFFENPAFRPDGLKLYPTLVIRGTGLYELWKSGRYKSYSPSDLVELVARILALVPPWT
RVYRVQRDIPMPLVSSGVEHGNLRELALARMKDLGIQCRDVRTREVGIQEIHHKVRPYQV
ELVRRDYVANGGWETFLSYEDPDQDILIGLLRLRKCSEETFRFELGGGVSIVRELHVYGS
VVPVSSRDPTKFQHQGFGMLLMEEAERIAREEHGSGKIAVISGVGTRNYYRKIGYRLQGP
YMVKMLK
Enzyme 63 Number of Residues 547
Enzyme 63 Molecular Weight 62258.4
Enzyme 63 Theoretical pI 9.12
Enzyme 63 GO Classification
Function
  • N-acetyltransferase activity
  • acetyltransferase activity
  • acyltransferase activity
  • binding
  • catalytic activity
  • iron-sulfur cluster binding
  • metal cluster binding
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 63 General Function Involved in N-acetyltransferase activity
Enzyme 63 Specific Function Catalytic histone acetyltransferase subunit of the RNA polymerase II elongator complex, which is a component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation. Elongator may play a role in chromatin remodeling and is involved in acetylation of histones H3 and probably H4. May also have a methyltransferase activity
Enzyme 63 Pathways
Enzyme 63 Reactions
  • acetyl-CoA + histone = CoA + acetylhistone
Enzyme 63 Pfam Domain Function
Enzyme 63 Signals
  • None
Enzyme 63 Transmembrane Regions
  • None
Enzyme 63 Essentiality Not Available
Enzyme 63 GenBank ID Protein 23510283 Link Image
Enzyme 63 UniProtKB/Swiss-Prot ID Q9H9T3 Link Image
Enzyme 63 UniProtKB/Swiss-Prot Entry Name ELP3_HUMAN Link Image
Enzyme 63 PDB ID Not Available
Enzyme 63 Cellular Location Not Available
Enzyme 63 Gene Sequence >1644 bp
ATGAGGCAGAAGCGGAAAGGAGATCTCAGCCCTGCTGAGCTGATGATGCTGACTATAGGA
GATGTTATTAAACAACTGATTGAAGCCCACGAGCAGGGGAAAGACATCGATCTAAATAAG
GTGAAAACCAAGACAGCTGCCAAATATGGCCTTTCTGCCCAGCCCCGCCTGGTGGATATC
ATTGCTGCCGTCCCTCCTCAGTATCGCAAGGTCTTGATGCCCAAGTTAAAGGCGAAACCC
ATCAGAACTGCTAGTGGGATTGCTGTCGTGGCTGTGATGTGCAAACCCCACAGATGTCCA
CACATCAGTTTTACAGGAAATATATGTGTATACTGCCCTGGTGGACCTGATTCTGATTTT
GAGTATTCCACCCAGTCTTACACTGGCTATGAGCCAACCTCCATGAGAGCTATCCGTGCC
AGATATGACCCTTTCCTACAGACAAGACACCGAATAGAACAGTTAAAACAACTTGGTCAT
AGTGTGGATAAAGTGGAGTTTATTGTGATGGGTGGAACGTTTATGGCCCTTCCAGAAGAA
TACAGAGATTATTTTATTCGAAATTTACATGATGCCTTATCAGGACATACTTCCAACAAT
ATTTACGAGGCAGTCAAGTATTCTGAGAGAAGCCTCACAAAGTGTATTGGAATTACTATT
GAAACCAGACCAGATTACTGCATGAAGCGACATTTAAGTGACATGTTGACCTATGGCTGC
ACAAGGCTGGAGATTGGGGTGCAGAGTGTTTATGAAGATGTGGCTAGAGACACCAACAGG
GGCCACACTGTGAAGGCAGTGTGTGAGTCATTTCACCTGGCCAAAGATTCCGGTTTTAAA
GTGGTGGCCCATATGATGCCTGACCTGCCAAACGTGGGACTAGAAAGAGACATTGAACAG
TTCACAGAGTTTTTTGAGAACCCTGCTTTTCGTCCCGATGGGCTGAAACTCTATCCTACC
CTGGTGATTCGTGGGACCGGGCTTTATGAGCTTTGGAAATCAGGAAGATATAAGAGTTAC
TCTCCTAGTGACCTGGTTGAATTGGTGGCTCGGATCCTAGCCCTCGTGCCTCCATGGACT
CGAGTGTACCGAGTACAGAGGGATATTCCAATGCCTTTAGTTAGCTCAGGAGTAGAGCAT
GGTAACCTGAGAGAGCTGGCACTTGCAAGAATGAAAGACCTCGGAATACAGTGTCGAGAT
GTGAGAACCAGAGAAGTTGGAATCCAAGAAATTCATCACAAAGTACGGCCATACCAGGTT
GAATTGGTAAGGAGAGATTATGTTGCAAATGGTGGCTGGGAAACATTCTTGTCATACGAA
GACCCAGATCAAGACATTTTGATTGGCCTCCTACGATTACGCAAGTGTTCAGAAGAAACT
TTCCGTTTCGAATTGGGTGGAGGTGTCTCCATAGTACGAGAGCTGCATGTGTATGGGAGT
GTGGTCCCTGTGAGCAGCCGGGATCCTACTAAATTTCAGCATCAGGGATTTGGCATGCTG
CTGATGGAGGAAGCAGAAAGAATAGCTAGAGAAGAACATGGGTCTGGGAAAATCGCTGTG
ATATCAGGGGTCGGCACCAGGAATTATTATAGAAAGATCGGCTACAGATTACAAGGCCCG
TACATGGTGAAGATGCTGAAATAA
Enzyme 63 GenBank Gene ID NM_018091.5 Link Image
Enzyme 63 GeneCard ID ELP3 Link Image
Enzyme 63 GenAtlas ID ELP3 Link Image
Enzyme 63 HGNC ID HGNC:20696 Link Image
Enzyme 63 Chromosome Location 8
Enzyme 63 Locus 8p21.1
Enzyme 63 SNPs SNPJam Report Link Image
Enzyme 63 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. 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. 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. Hawkes NA, Otero G, Winkler GS, Marshall N, Dahmus ME, Krappmann D, Scheidereit C, Thomas CL, Schiavo G, Erdjument-Bromage H, Tempst P, Svejstrup JQ: Purification and characterization of the human elongator complex. J Biol Chem. 2002 Jan 25;277(4):3047-52. Epub 2001 Nov 19. [PubMed Link Image]
  5. Kim JH, Lane WS, Reinberg D: Human Elongator facilitates RNA polymerase II transcription through chromatin. Proc Natl Acad Sci U S A. 2002 Feb 5;99(3):1241-6. Epub 2002 Jan 29. [PubMed Link Image]
  6. Li F, Lu J, Han Q, Zhang G, Huang B: The Elp3 subunit of human Elongator complex is functionally similar to its counterpart in yeast. Mol Genet Genomics. 2005 May;273(3):264-72. Epub 2005 Apr 16. [PubMed Link Image]
  7. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  8. Close P, Hawkes N, Cornez I, Creppe C, Lambert CA, Rogister B, Siebenlist U, Merville MP, Slaugenhaupt SA, Bours V, Svejstrup JQ, Chariot A: Transcription impairment and cell migration defects in elongator-depleted cells: implication for familial dysautonomia. Mol Cell. 2006 May 19;22(4):521-31. [PubMed Link Image]
  9. 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]
Enzyme 63 Metabolite References Not Available
Enzyme 64 [top]
Enzyme 64 ID 14754
Enzyme 64 Name Histone-lysine N-methyltransferase EZH2
Enzyme 64 Synonyms
  1. ENX-1
  2. Enhancer of zeste homolog 2
  3. Lysine N-methyltransferase 6
Enzyme 64 Gene Name EZH2
Enzyme 64 Protein Sequence >Histone-lysine N-methyltransferase EZH2
MGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKSMFSSNRQKILERTEILNQEW
KQRRIQPVHILTSVSSLRGTRECSVTSDLDFPTQVIPLKTLNAVASVPIMYSWSPLQQNF
MVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQ
YNDDDDDDDGDDPEEREEKQKDLEDHRDDKESRPPRKFPSDKIFEAISSMFPDKGTAEEL
KEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFH
ATPNTYKRKNTETALDNKPCGPQCYQHLEGAKEFAAALTAERIKTPPKRPGGRRRGRLPN
NSSRPSTPTINVLESKDTDSDREAGTETGGENNDKEEEEKKDETSSSSEANSRCQTPIKM
KPNIEPPENVEWSGAEASMFRVLIGTYYDNFCAIARLIGTKTCRQVYEFRVKESSIIAPA
PAEDVDTPPRKKKRKHRLWAAHCRKIQLKKDGSSNHVYNYQPCDHPRQPCDSSCPCVIAQ
NFCEKFCQCSSECQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCLTCGAADHWDSKNVS
CKNCSIQRGSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDK
YMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGE
ELFFDYRYSQADALKYVGIEREMEIP
Enzyme 64 Number of Residues 746
Enzyme 64 Molecular Weight 85362.4
Enzyme 64 Theoretical pI 7.01
Enzyme 64 GO Classification
Function
  • DNA binding
  • binding
  • nucleic acid binding
Process
Component
Enzyme 64 General Function Involved in DNA binding
Enzyme 64 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 64 Pathways Not Available
Enzyme 64 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 64 Pfam Domain Function
Enzyme 64 Signals
  • None
Enzyme 64 Transmembrane Regions
  • None
Enzyme 64 Essentiality Not Available
Enzyme 64 GenBank ID Protein 1575349 Link Image
Enzyme 64 UniProtKB/Swiss-Prot ID Q15910 Link Image
Enzyme 64 UniProtKB/Swiss-Prot Entry Name EZH2_HUMAN Link Image
Enzyme 64 PDB ID Not Available
Enzyme 64 Cellular Location Not Available
Enzyme 64 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 64 GenBank Gene ID U61145 Link Image
Enzyme 64 GeneCard ID EZH2 Link Image
Enzyme 64 GenAtlas ID EZH2 Link Image
Enzyme 64 HGNC ID HGNC:3527 Link Image
Enzyme 64 Chromosome Location 7
Enzyme 64 Locus 7q35-q36
Enzyme 64 SNPs SNPJam Report Link Image
Enzyme 64 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 64 Metabolite References Not Available
Enzyme 65 [top]
Enzyme 65 ID 14755
Enzyme 65 Name rRNA/tRNA 2'-O-methyltransferase fibrillarin-like protein 1
Enzyme 65 Synonyms Not Available
Enzyme 65 Gene Name FBLL1
Enzyme 65 Protein Sequence >rRNA/tRNA 2'-O-methyltransferase fibrillarin-like protein 1
MKSAASSRGGGGGGRGGGGWGSWGGGRGGGGGAGKGGGGDGGGQGGKGGFGARARGFGGG
GRGRGRGGGDGKDRGGGGQRRGGVAKSKSRRRKGAMVVSVEPHRHEGVFIYRGAEDALVT
LNMVPGQSVYGERRVTVTEGGVKQEYRTWNPFRSKLAAAILGGVDQIHIKPKSKVLYLGA
ASGTTVSHVSDIIGPDGLVYAVEFSHRAGRDLVNVAKKRTNIIPVLEDARHPLKYRMLIG
MVDVIFADVAQPDQSRIVALNAHTFLRNGGHFLISIKANCIDSTASAEAVFASEVRKLQQ
ENLKPQEQLTLEPYERDHAVVVGVYRPLPKSSS
Enzyme 65 Number of Residues 333
Enzyme 65 Molecular Weight 34675.1
Enzyme 65 Theoretical pI 10.95
Enzyme 65 GO Classification
Function
  • RNA binding
  • binding
  • catalytic activity
  • methyltransferase activity
  • nucleic acid binding
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • RNA metabolic process
  • cellular macromolecule metabolic process
  • macromolecule metabolic process
  • metabolic process
  • ncRNA metabolic process
  • rRNA metabolic process
  • rRNA processing
  • tRNA metabolic process
  • tRNA processing
Component
Enzyme 65 General Function Involved in RNA binding
Enzyme 65 Specific Function Involved in pre-rRNA processing. Utilizes the methyl donor S-adenosyl-L-methionine to catalyze the site-specific 2'- hydroxyl methylation of ribose moieties in pre-ribosomal RNA
Enzyme 65 Pathways Not Available
Enzyme 65 Reactions Not Available
Enzyme 65 Pfam Domain Function
Enzyme 65 Signals
  • None
Enzyme 65 Transmembrane Regions
  • None
Enzyme 65 Essentiality Not Available
Enzyme 65 GenBank ID Protein Not Available
Enzyme 65 UniProtKB/Swiss-Prot ID A6NHQ2 Link Image
Enzyme 65 UniProtKB/Swiss-Prot Entry Name FBLL1_HUMAN Link Image
Enzyme 65 PDB ID Not Available
Enzyme 65 Cellular Location Not Available
Enzyme 65 Gene Sequence Not Available
Enzyme 65 GenBank Gene ID Not Available
Enzyme 65 GeneCard ID FBLL1 Link Image
Enzyme 65 GenAtlas ID FBLL1 Link Image
Enzyme 65 HGNC ID HGNC:35458 Link Image
Enzyme 65 Chromosome Location 5
Enzyme 65 Locus 5q34
Enzyme 65 SNPs SNPJam Report Link Image
Enzyme 65 General References
  1. 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]
Enzyme 65 Metabolite References Not Available
Enzyme 66 [top]
Enzyme 66 ID 14756
Enzyme 66 Name Leucine carboxyl methyltransferase 2
Enzyme 66 Synonyms
  1. p21WAF1/CIP1 promoter-interacting protein
  2. tRNA wybutosine-synthesizing protein 4 homolog
  3. tRNA yW-synthesizing protein 4 homolog
Enzyme 66 Gene Name LCMT2
Enzyme 66 Protein Sequence >Leucine carboxyl methyltransferase 2
MGPRSRERRAGAVQNTNDSSALSKRSLAARGYVQDPFAALLVPGAARRAPLIHRGYYVRA
RAVRHCVRAFLEQIGAPQAALRAQILSLGAGFDSLYFRLKTAGRLARAAVWEVDFPDVAR
RKAERIGETPELCALTGPFERGEPASALCFESADYCILGLDLRQLQRVEEALGAAGLDAA
SPTLLLAEAVLTYLEPESAAALIAWAAQRFPNALFVVYEQMRPQDAFGQFMLQHFRQLNS
PLHGLERFPDVEAQRRRFLQAGWTACGAVDMNEFYHCFLPAEERRRVENIEPFDEFEEWH
LKCAHYFILAASRGDTLSHTLVFPSSEAFPRVNPASPSGVFPASVVSSEGQVPNLKRYGH
ASVFLSPDVILSAGGFGEQEGRHCRVSQFHLLSRDCDSEWKGSQIGSCGTGVQWDGRLYH
TMTRLSESRVLVLGGRLSPVSPALGVLQLHFFKSEDNNTEDLKVTITKAGRKDDSTLCCW
RHSTTEVSCQNQEYLFVYGGRSVVEPVLSDWHFLHVGTMAWVRIPVEGEVPEARHSHSAC
TWQGGALIAGGLGASEEPLNSVLFLRPISCGFLWESVDIQPPITPRYSHTAHVLNGKLLL
VGGIWIHSSSFPGVTVINLTTGLSSEYQIDTTYVPWPLMLHNHTSILLPEEQQLLLLGGG
GNCFSFGTYFNPHTVTLDLSSLSAGQ
Enzyme 66 Number of Residues 686
Enzyme 66 Molecular Weight 75601.1
Enzyme 66 Theoretical pI 6.71
Enzyme 66 GO Classification
Function
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
Component
Enzyme 66 General Function Involved in methyltransferase activity
Enzyme 66 Specific Function Probable S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. May methylate the carboxyl group of leucine residues to form alpha- leucine ester residues
Enzyme 66 Pathways Not Available
Enzyme 66 Reactions Not Available
Enzyme 66 Pfam Domain Function
Enzyme 66 Signals
  • None
Enzyme 66 Transmembrane Regions
  • None
Enzyme 66 Essentiality Not Available
Enzyme 66 GenBank ID Protein 25188199 Link Image
Enzyme 66 UniProtKB/Swiss-Prot ID O60294 Link Image
Enzyme 66 UniProtKB/Swiss-Prot Entry Name LCMT2_HUMAN Link Image
Enzyme 66 PDB ID Not Available
Enzyme 66 Cellular Location Not Available
Enzyme 66 Gene Sequence >2061 bp
ATGGGCCCCCGGAGCCGTGAGCGTCGGGCAGGCGCGGTACAGAACACCAACGACAGCAGC
GCCCTCAGCAAGCGTTCCCTGGCCGCGCGCGGGTACGTGCAGGACCCCTTTGCCGCGTTG
CTGGTTCCGGGCGCGGCGCGCCGCGCACCGCTCATTCACCGAGGCTACTACGTCCGCGCA
CGCGCCGTGAGGCACTGCGTGCGCGCTTTTTTGGAGCAGATTGGCGCGCCCCAGGCCGCG
CTTCGCGCGCAGATCTTGTCTCTCGGCGCTGGCTTCGACTCGCTCTATTTTCGCTTAAAA
ACCGCGGGCCGCCTGGCCCGGGCTGCAGTCTGGGAGGTGGATTTTCCGGACGTGGCGCGG
CGCAAAGCAGAAAGGATTGGAGAGACGCCAGAGCTGTGCGCGTTAACCGGGCCTTTCGAG
AGGGGGGAGCCCGCGTCCGCGCTGTGCTTTGAGAGCGCAGACTACTGCATCCTGGGTCTG
GACTTGCGGCAGCTCCAGCGAGTGGAGGAGGCCCTGGGCGCCGCGGGGCTCGACGCAGCC
TCACCCACTCTGCTCCTGGCCGAGGCGGTGCTGACCTACCTCGAGCCGGAGAGTGCCGCG
GCCCTCATCGCCTGGGCAGCCCAGCGTTTTCCTAATGCCCTTTTCGTGGTCTATGAGCAG
ATGAGGCCTCAAGACGCCTTTGGCCAGTTCATGCTGCAACATTTTCGGCAGCTAAACTCC
CCCCTGCATGGCCTGGAGCGTTTTCCTGACGTGGAGGCGCAGCGGCGCCGCTTCCTTCAA
GCTGGCTGGACCGCCTGCGGTGCCGTGGACATGAATGAATTCTATCACTGCTTTCTTCCC
GCAGAAGAACGCCGGCGGGTGGAAAATATTGAACCCTTTGACGAATTTGAGGAGTGGCAT
CTGAAGTGCGCCCATTATTTCATTCTGGCAGCTTCTAGGGGAGACACCCTCTCCCACACC
CTAGTGTTTCCATCCTCAGAGGCATTTCCTCGCGTAAATCCTGCTTCGCCTTCAGGGGTA
TTCCCTGCCAGCGTAGTCAGTAGCGAGGGCCAGGTCCCAAACCTGAAGAGATATGGCCAC
GCCTCTGTCTTCTTGAGCCCAGACGTTATTCTCAGTGCAGGAGGATTTGGAGAGCAGGAG
GGGCGGCACTGCCGAGTGAGCCAGTTTCACTTGCTCTCAAGAGATTGTGACTCTGAATGG
AAAGGCAGCCAAATAGGCAGTTGTGGGACTGGAGTTCAGTGGGATGGACGCCTTTATCAC
ACCATGACAAGACTCTCAGAGAGTCGGGTTCTGGTTCTGGGAGGGAGACTGTCCCCAGTA
AGTCCAGCCTTGGGGGTTCTCCAGCTTCATTTTTTTAAGAGTGAGGATAATAACACTGAG
GACCTGAAAGTGACAATAACAAAGGCTGGCCGAAAGGATGATTCCACTTTGTGTTGTTGG
CGGCATTCAACAACAGAAGTGTCCTGTCAGAATCAGGAATATTTGTTTGTGTATGGGGGT
CGAAGCGTGGTGGAACCTGTACTAAGTGACTGGCATTTCCTCCATGTAGGGACAATGGCT
TGGGTCAGGATCCCAGTGGAGGGAGAAGTACCTGAAGCCCGGCATTCTCACAGTGCCTGC
ACTTGGCAAGGGGGAGCCCTTATTGCTGGAGGTCTCGGGGCTTCTGAGGAGCCATTGAAC
TCTGTGCTCTTTCTGAGACCAATCTCTTGTGGATTCCTCTGGGAGTCAGTAGACATCCAG
CCTCCCATTACCCCAAGGTACTCCCACACAGCTCATGTGCTCAATGGAAAGCTGTTACTG
GTTGGAGGGATCTGGATTCATTCCTCCTCATTTCCTGGAGTGACTGTGATCAATTTGACT
ACAGGATTGAGCTCTGAGTATCAGATTGACACAACATATGTGCCATGGCCATTAATGTTA
CACAACCATACTAGTATCCTTCTTCCTGAAGAGCAACAGCTCCTGCTCCTTGGAGGTGGT
GGGAACTGCTTTTCCTTTGGTACCTACTTCAACCCCCATACAGTCACATTAGACCTTTCT
TCCTTAAGTGCTGGGCAGTAA
Enzyme 66 GenBank Gene ID NM_014793.3 Link Image
Enzyme 66 GeneCard ID LCMT2 Link Image
Enzyme 66 GenAtlas ID LCMT2 Link Image
Enzyme 66 HGNC ID HGNC:17558 Link Image
Enzyme 66 Chromosome Location 1
Enzyme 66 Locus 15q15.3
Enzyme 66 SNPs SNPJam Report Link Image
Enzyme 66 General References
  1. Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [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. De Baere I, Derua R, Janssens V, Van Hoof C, Waelkens E, Merlevede W, Goris J: Purification of porcine brain protein phosphatase 2A leucine carboxyl methyltransferase and cloning of the human homologue. Biochemistry. 1999 Dec 14;38(50):16539-47. [PubMed Link Image]
  4. Ng CC, Arakawa H, Fukuda S, Kondoh H, Nakamura Y: p53RFP, a p53-inducible RING-finger protein, regulates the stability of p21WAF1. Oncogene. 2003 Jul 10;22(28):4449-58. [PubMed Link Image]
Enzyme 66 Metabolite References Not Available
Enzyme 67 [top]
Enzyme 67 ID 14757
Enzyme 67 Name mRNA cap guanine-N7 methyltransferase
Enzyme 67 Synonyms
  1. RG7MT1
  2. mRNA (guanine-N(7)-)-methyltransferase
  3. mRNA cap methyltransferase
  4. hCMT1
  5. hMet
  6. hcm1p
Enzyme 67 Gene Name RNMT
Enzyme 67 Protein Sequence >mRNA cap guanine-N7 methyltransferase
MANSAKAEEYEKMSLEQAKASVNSETESSFNINENTTASGTGLSEKTSVCRQVDIARKRK
EFEDDLVKESSSCGKDTPSKKRKLDPEIVPEEKDCGDAEGNSKKRKRETEDVPKDKSSTG
DGTQNKRKIALEDVPEKQKNLEEGHSSTVAAHYNELQEVGLEKRSQSRIFYLRNFNNWMK
SVLIGEFLEKVRQKKKRDITVLDLGCGKGGDLLKWKKGRINKLVCTDIADVSVKQCQQRY
EDMKNRRDSEYIFSAEFITADSSKELLIDKFRDPQMCFDICSCQFVCHYSFESYEQADMM
LRNACERLSPGGYFIGTTPNSFELIRRLEASETESFGNEIYTVKFQKKGDYPLFGCKYDF
NLEGVVDVPEFLVYFPLLNEMAKKYNMKLVYKKTFLEFYEEKIKNNENKMLLKRMQALEP
YPANESSKLVSEKVDDYEHAAKYMKNSQVRLPLGTLSKSEWEATSIYLVFAFEKQQ
Enzyme 67 Number of Residues 476
Enzyme 67 Molecular Weight 54843.7
Enzyme 67 Theoretical pI 6.54
Enzyme 67 GO Classification
Function
Process
  • RNA metabolic process
  • RNA processing
  • cellular macromolecule metabolic process
  • mRNA capping
  • mRNA processing
  • macromolecule metabolic process
  • metabolic process
Component
Enzyme 67 General Function Involved in mRNA capping
Enzyme 67 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 67 Pathways Not Available
Enzyme 67 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 67 Pfam Domain Function
Enzyme 67 Signals
  • None
Enzyme 67 Transmembrane Regions
  • None
Enzyme 67 Essentiality Not Available
Enzyme 67 GenBank ID Protein 2662077 Link Image
Enzyme 67 UniProtKB/Swiss-Prot ID O43148 Link Image
Enzyme 67 UniProtKB/Swiss-Prot Entry Name MCES_HUMAN Link Image
Enzyme 67 PDB ID Not Available
Enzyme 67 Cellular Location Not Available
Enzyme 67 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 67 GenBank Gene ID AB007858 Link Image
Enzyme 67 GeneCard ID RNMT Link Image
Enzyme 67 GenAtlas ID RNMT Link Image
Enzyme 67 HGNC ID HGNC:10075 Link Image
Enzyme 67 Chromosome Location 1
Enzyme 67 Locus 18p11.21
Enzyme 67 SNPs SNPJam Report Link Image
Enzyme 67 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 67 Metabolite References Not Available
Enzyme 68 [top]
Enzyme 68 ID 14758
Enzyme 68 Name Probable S-adenosyl-L-methionine-dependent methyltransferase METT5D1
Enzyme 68 Synonyms
  1. Methyltransferase 5 domain-containing protein 1
Enzyme 68 Gene Name METT5D1
Enzyme 68 Protein Sequence >Probable S-adenosyl-L-methionine-dependent methyltransferase METT5D1
MLRYPYFCRMYKECLSCWLESGIPNLGVWPNRIHTTAEKYREYEAREQTDQTQAQELHRS
QDRDFETMAKLHIPVMVDEVVHCLSPQKGQIFLDMTFGSGGHTKAILQKESDIVLYALDR
DPTAYALAEHLSELYPKQIRAMLGQFSQAEALLMKAGVQPGTFDGVLMDLGCSSMQLDTP
ERGFSLRKDGPLDMRMDGGRYPDMPTAADVVNALDQQALASILRTYGEEKHAKKIASAIV
QARSIYPITRTQQLASIVAGAFPPSAIYTRKDLLQRSTHIATKTFQALRIFVNNELNELY
TGLKTAQKFLRPGGRLVALSFHSLEDRIVKRFLLGISMTERFNLSVRQQVMKTSQLGSDH
ENTEEVSMRRAPLMWELIHKKVLSPQDQDVQDNPRGRSAKLRAAIKL
Enzyme 68 Number of Residues 407
Enzyme 68 Molecular Weight 46120.6
Enzyme 68 Theoretical pI 8.85
Enzyme 68 GO Classification
Function
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
Component
Enzyme 68 General Function Involved in methyltransferase activity
Enzyme 68 Specific Function Probable S-adenosyl-L-methionine-dependent methyltransferase
Enzyme 68 Pathways Not Available
Enzyme 68 Reactions Not Available
Enzyme 68 Pfam Domain Function
Enzyme 68 Signals
  • None
Enzyme 68 Transmembrane Regions
  • None
Enzyme 68 Essentiality Not Available
Enzyme 68 GenBank ID Protein 165377209 Link Image
Enzyme 68 UniProtKB/Swiss-Prot ID A6NJ78 Link Image
Enzyme 68 UniProtKB/Swiss-Prot Entry Name ME5D1_HUMAN Link Image
Enzyme 68 PDB ID Not Available
Enzyme 68 Cellular Location Not Available
Enzyme 68 Gene Sequence >1224 bp
ATGCTTCGGTATCCATATTTTTGTAGAATGTATAAAGAATGCCTTTCATGTTGGTTGGAA
TCTGGCATACCTAATTTAGGTGTCTGGCCAAACAGAATACATACTACAGCAGAAAAATAT
AGAGAATATGAAGCCCGGGAGCAAACAGATCAAACTCAAGCCCAGGAGTTACACAGATCT
CAAGATAGAGATTTTGAAACTATGGCTAAATTACATATTCCAGTAATGGTGGATGAAGTT
GTTCATTGTTTGTCACCACAAAAAGGACAGATTTTTCTAGATATGACATTTGGTTCGGGA
GGGCACACAAAAGCCATTCTGCAGAAGGAGTCAGATATTGTTCTCTATGCCTTGGACAGA
GACCCAACAGCTTATGCATTAGCTGAACATCTTTCAGAGTTGTATCCTAAACAAATCCGA
GCTATGCTGGGCCAGTTCAGCCAGGCAGAAGCCTTATTAATGAAAGCTGGAGTGCAGCCA
GGAACTTTTGATGGAGTTCTTATGGATCTTGGGTGTTCCTCCATGCAACTTGATACTCCT
GAAAGAGGTTTTTCCCTTCGGAAAGATGGCCCTTTGGACATGAGAATGGATGGTGGCAGG
TACCCTGACATGCCCACTGCTGCTGATGTTGTGAATGCTTTAGATCAACAGGCACTTGCA
TCTATCCTAAGAACATACGGGGAGGAGAAGCATGCCAAGAAAATCGCTTCAGCAATTGTT
CAGGCACGCAGCATCTACCCCATCACCAGAACCCAGCAGCTTGCCAGCATCGTTGCAGGA
GCATTTCCTCCCTCTGCTATTTATACACGGAAAGACTTACTACAGCGATCTACCCATATT
GCCACCAAGACTTTCCAGGCTCTTCGCATATTTGTGAACAATGAGCTCAATGAACTCTAC
ACGGGACTGAAGACAGCTCAGAAGTTTCTGAGACCTGGTGGTCGTCTTGTTGCCCTCTCC
TTCCATTCACTAGAGGATCGCATCGTCAAAAGATTTTTGCTTGGAATAAGCATGACAGAA
AGATTTAACCTAAGTGTTAGACAACAAGTGATGAAAACATCTCAATTGGGTTCAGATCAC
GAAAACACGGAAGAAGTCTCTATGAGAAGAGCTCCTTTAATGTGGGAATTGATACACAAG
AAGGTACTTAGTCCACAAGATCAGGATGTACAAGATAACCCCAGAGGGCGCTCAGCCAAG
CTTAGAGCAGCTATCAAATTATAA
Enzyme 68 GenBank Gene ID NM_001113528.1 Link Image
Enzyme 68 GeneCard ID METT5D1 Link Image
Enzyme 68 GenAtlas ID METT5D1 Link Image
Enzyme 68 HGNC ID HGNC:26606 Link Image
Enzyme 68 Chromosome Location 1
Enzyme 68 Locus 11p14.1
Enzyme 68 SNPs SNPJam Report Link Image
Enzyme 68 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. 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]
  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]
Enzyme 68 Metabolite References Not Available
Enzyme 69 [top]
Enzyme 69 ID 14760
Enzyme 69 Name 7SK snRNA methylphosphate capping enzyme
Enzyme 69 Synonyms
  1. MePCE
  2. Bicoid-interacting protein 3 homolog
  3. Bin3 homolog
Enzyme 69 Gene Name MEPCE
Enzyme 69 Protein Sequence >7SK snRNA methylphosphate capping enzyme
MIEMAAEKEPFLVPAPPPPLKDESGGGGGPTVPPHQEAASGELRGGTERGPGRCAPSAGS
PAAAVGRESPGAAATSSSGPQAQQHRGGGPQAQSHGEARLSDPPGRAAPPDVGEERRGGG
GTELGPPAPPRPRNGYQPHRPPGGGGGKRRNSCNVGGGGGGFKHPAFKRRRRVNSDCDSV
LPSNFLLGGNIFDPLNLNSLLDEEVSRTLNAETPKSSPLPAKGRDPVEILIPKDITDPLS
LNTCTDEGHVVLASPLKTGRKRHRHRGQHHQQQQAAGGSESHPVPPTAPLTPLLHGEGAS
QQPRHRGQNRDAPQPYELNTAINCRDEVVSPLPSALQGPSGSLSAPPAASVISAPPSSSS
RHRKRRRTSSKSEAGARGGGQGSKEKGRGSWGGRHHHHHPLPAAGFKKQQRKFQYGNYCK
YYGYRNPSCEDGRLRVLKPEWFRGRDVLDLGCNVGHLTLSIACKWGPSRMVGLDIDSRLI
HSARQNIRHYLSEELRLPPQTLEGDPGAEGEEGTTTVRKRSCFPASLTASRGPIAAPQVP
LDGADTSVFPNNVVFVTGNYVLDRDDLVEAQTPEYDVVLCLSLTKWVHLNWGDEGLKRMF
RRIYRHLRPGGILVLEPQPWSSYGKRKTLTETIYKNYYRIQLKPEQFSSYLTSPDVGFSS
YELVATPHNTSKGFQRPVYLFHKARSPSH
Enzyme 69 Number of Residues 689
Enzyme 69 Molecular Weight 74354.7
Enzyme 69 Theoretical pI 10.01
Enzyme 69 GO Classification
Function
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
Component
Enzyme 69 General Function Involved in methyltransferase activity
Enzyme 69 Specific Function S-adenosyl-L-methionine-dependent methyltransferase that adds a methylphosphate cap at the 5'-end of 7SK snRNA, leading to stabilize it
Enzyme 69 Pathways Not Available
Enzyme 69 Reactions Not Available
Enzyme 69 Pfam Domain Function
Enzyme 69 Signals
  • None
Enzyme 69 Transmembrane Regions
  • None
Enzyme 69 Essentiality Not Available
Enzyme 69 GenBank ID Protein 47271406 Link Image
Enzyme 69 UniProtKB/Swiss-Prot ID Q7L2J0 Link Image
Enzyme 69 UniProtKB/Swiss-Prot Entry Name MEPCE_HUMAN Link Image
Enzyme 69 PDB ID Not Available
Enzyme 69 Cellular Location Not Available
Enzyme 69 Gene Sequence >2070 bp
ATGATCGAGATGGCGGCGGAGAAGGAGCCGTTTCTGGTGCCGGCCCCGCCGCCGCCGCTC
AAAGATGAGTCGGGCGGAGGGGGCGGCCCCACGGTGCCACCGCACCAAGAGGCCGCCTCT
GGGGAGCTCCGCGGCGGGACGGAGCGTGGTCCGGGTCGTTGCGCGCCATCTGCGGGGTCC
CCAGCCGCTGCGGTCGGTCGGGAAAGCCCCGGGGCCGCGGCCACCTCCTCCAGTGGTCCC
CAGGCGCAGCAGCACCGAGGGGGCGGCCCCCAGGCGCAGTCGCATGGGGAGGCCCGCCTG
TCGGATCCCCCGGGGCGAGCCGCTCCCCCGGACGTGGGGGAGGAGCGCCGGGGAGGGGGC
GGGACAGAGCTGGGTCCCCCTGCTCCTCCTCGACCCCGCAATGGCTATCAGCCCCACCGG
CCACCTGGGGGGGGCGGGGGCAAGAGGAGAAATAGCTGTAATGTAGGGGGAGGCGGGGGA
GGCTTCAAACATCCGGCCTTCAAGAGGCGCAGGCGGGTGAATTCGGACTGTGACTCTGTG
TTACCCTCCAACTTCCTCCTGGGGGGCAATATCTTTGATCCCCTGAACCTGAATAGCCTC
CTGGATGAGGAAGTGAGCCGCACTCTCAACGCGGAGACCCCTAAGTCATCCCCCCTTCCG
GCCAAAGGGCGAGATCCGGTGGAGATCCTCATCCCCAAAGATATTACTGACCCGCTCAGT
CTCAATACTTGCACTGATGAGGGCCATGTAGTTCTTGCTTCGCCACTCAAGACTGGTCGG
AAGCGGCATAGACACCGGGGACAGCACCACCAGCAGCAGCAGGCAGCCGGAGGGAGTGAG
AGTCACCCCGTGCCGCCCACAGCCCCTCTCACCCCCTTACTCCACGGGGAGGGCGCCTCA
CAGCAGCCGCGGCACAGGGGCCAGAACCGGGATGCCCCCCAACCCTATGAACTCAACACA
GCCATCAACTGCAGGGATGAAGTGGTGTCTCCCCTTCCATCTGCTCTGCAGGGTCCCTCA
GGCTCCCTATCAGCCCCTCCAGCTGCCTCAGTTATCTCTGCACCCCCATCTTCCTCCTCC
CGACATCGCAAACGTCGCAGGACTTCCAGCAAGTCGGAGGCAGGGGCTAGGGGTGGAGGC
CAGGGTTCCAAGGAAAAGGGCCGAGGGAGTTGGGGAGGCCGCCACCACCACCACCACCCA
CTGCCTGCAGCAGGCTTCAAAAAGCAACAGCGCAAGTTCCAGTATGGGAATTATTGCAAA
TACTATGGGTACCGCAATCCTTCCTGTGAGGATGGGCGCCTTCGGGTGTTGAAGCCTGAG
TGGTTTCGGGGCCGGGACGTCCTAGATCTGGGCTGCAATGTGGGCCATCTGACCCTGAGC
ATTGCCTGCAAGTGGGGCCCGTCCCGCATGGTGGGCCTGGATATCGATTCCCGGCTCATC
CATTCTGCCCGCCAAAACATCCGACACTACCTTTCCGAGGAGCTGCGTCTCCCACCCCAG
ACTTTGGAAGGGGACCCGGGGGCAGAGGGTGAGGAAGGGACCACCACCGTTCGAAAGAGG
AGCTGCTTCCCAGCCTCGCTGACTGCCAGCCGGGGTCCCATCGCTGCCCCCCAAGTGCCC
TTGGATGGAGCGGACACATCAGTCTTCCCCAACAATGTTGTCTTCGTCACGGGTAATTAT
GTGCTGGATCGAGATGACCTGGTGGAGGCCCAAACACCTGAGTATGATGTGGTGCTCTGC
CTCAGCCTCACCAAGTGGGTGCATCTGAACTGGGGAGACGAGGGCCTGAAGCGCATGTTT
CGCCGGATCTACCGGCACCTACGCCCTGGGGGCATCCTGGTCCTAGAGCCCCAACCCTGG
TCGTCGTATGGCAAGAGAAAGACTCTTACAGAAACGATCTACAAGAACTACTACCGAATC
CAATTGAAGCCAGAGCAGTTCAGTTCCTACCTGACATCCCCAGACGTGGGCTTCTCCAGC
TATGAGCTTGTGGCCACACCCCACAACACCTCTAAAGGCTTCCAGCGTCCTGTGTACCTG
TTCCACAAGGCCCGATCCCCCAGCCACTAA
Enzyme 69 GenBank Gene ID NM_019606.5 Link Image
Enzyme 69 GeneCard ID MEPCE Link Image
Enzyme 69 GenAtlas ID MEPCE Link Image
Enzyme 69 HGNC ID HGNC:20247 Link Image
Enzyme 69 Chromosome Location 7
Enzyme 69 Locus 7q22.1
Enzyme 69 SNPs SNPJam Report Link Image
Enzyme 69 General References
  1. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [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. Rogers SA, Bowen DJ, Ling M, Thomson P, Wang Z, Lim SH: Identification and characterization of a novel gene encoding a SEREX antigen in chronic myeloid leukaemia. Br J Haematol. 2002 Oct;119(1):112-4. [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. 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]
  6. 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]
  7. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  8. Jeronimo C, Forget D, Bouchard A, Li Q, Chua G, Poitras C, Therien C, Bergeron D, Bourassa S, Greenblatt J, Chabot B, Poirier GG, Hughes TR, Blanchette M, Price DH, Coulombe B: Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme. Mol Cell. 2007 Jul 20;27(2):262-74. [PubMed Link Image]
  9. 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]
  10. 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]
  11. 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]
  12. 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]
  13. 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]
  14. 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]
  15. 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 69 Metabolite References Not Available
Enzyme 70 [top]
Enzyme 70 ID 14761
Enzyme 70 Name Histone-lysine N-methyltransferase MLL2
Enzyme 70 Synonyms
  1. ALL1-related protein
  2. Lysine N-methyltransferase 2B
  3. KMT2B
  4. Myeloid/lymphoid or mixed-lineage leukemia protein 2
Enzyme 70 Gene Name MLL2
Enzyme 70 Protein Sequence >Histone-lysine N-methyltransferase MLL2
MDSQNLAGEDKDSQPAADGPAASEDPSATESDLPNPHVGEVSVLSSGSPRLQETPQDCSG
GPVRRCALCNCGEPALHGQRELRRFELPFDWPRCPVVSPGGSPGPNEAVLPSEDLSQIGF
PEGLTPAHLGEPGGSCWAHHWCAAWSAGVWGQEGPQLCGVDKAIFSGISQRCSHCTRLGA
SIPCRSPGCPRLYHFPCATASGSFLSMKTLQLLCPEHSEGAAYLEEARCAVCEGPGELCD
LFFCTSCGHHYHGACLDTALTARKRAGWQCPECKVCQACRKPGNDSKMLVCETCDKGYHT
FCLKPPMEELPAHSWKCKACRVCRACGAGSAELNPNSEWFENYSLCHRCHKAQGGQTIRS
VAEQHTPVCSRFSPPEPGDTPTDEPDALYVACQGQPKGGHVTSMQPKEPGPLQCEAKPLG
KAGVQLEPQLEAPLNEEMPLLPPPEESPLSPPPEESPTSPPPEASRLSPPPEELPASPLP
EALHLSRPLEESPLSPPPEESPLSPPPESSPFSPLEESPLSPPEESPPSPALETPLSPPP
EASPLSPPFEESPLSPPPEELPTSPPPEASRLSPPPEESPMSPPPEESPMSPPPEASRLF
PPFEESPLSPPPEESPLSPPPEASRLSPPPEDSPMSPPPEESPMSPPPEVSRLSPLPVVS
RLSPPPEESPLSPPALSPLGELEYPFGAKGDSDPESPLAAPILETPISPPPEANCTDPEP
VPPMILPPSPGSPVGPASPILMEPLPPQCSPLLQHSLVPQNSPPSQCSPPALPLSVPSPL
SPIGKVVGVSDEAELHEMETEKVSEPECPALEPSATSPLPSPMGDLSCPAPSPAPALDDF
SGLGEDTAPLDGIDAPGSQPEPGQTPGSLASELKGSPVLLDPEELAPVTPMEVYPECKQT
AGRGSPCEEQEEPRAPVAPTPPTLIKSDIVNEISNLSQGDASASFPGSEPLLGSPDPEGG
GSLSMELGVSTDVSPARDEGSLRLCTDSLPETDDSLLCDAGTAISGGKAEGEKGRRRSSP
ARSRIKQGRSSSFPGRRRPRGGAHGGRGRGRARLKSTASSIETLVVADIDSSPSKEEEEE
DDDTMQNTVVLFSNTDKFVLMQDMCVVCGSFGRGAEGHLLACSQCSQCYHPYCVNSKITK
VMLLKGWRCVECIVCEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWCV
SCMQCGAASPGFHCEWQNSYTHCGPCASLVTCPICHAPYVEEDLLIQCRHCERWMHAGCE
SLFTEDDVDHAPDEGFDCVSCQPYVVKPVAPVAPPELVPMKVKEPEPQYFRFEGVWLTET
GMALLRNLTMSPLHKRRQRRGRLGLPGEAGLEGSEPSDALGPDDKKDGDLDTDELLKGEG
GVEHMECEIKLEGPVSPDVEPGKEETEESKKRKRKPYRPGIGGFMVRQRKSHTRTKKGPA
AQAEVLSGDGQPDEVIPADLPAEGAVEQSLAEGDEKKKQQRRGRKRSKLEGMFPAYLQEA
FFGKELLDLSRKALFAVGVGRPSFGLGTPKAKGDGGSERKELPTSQKGDDGPDIADEESR
GLEGKADTPGPEDGGVKASPVPSDPEKPGTPGEGMLSSDLDRISTEELPKMESKDLQQLF
KDVLGSEREQHLGCGTPGLEGSRTPLQRPFLQGGLPLGNLPSSSPMDSYPGLCQSPFLDS
RERGGFFSPEPGEPDSPWTGSGGTTPSTPTTPTTEGEGDGLSYNQRSLQRWEKDEELGQL
STISPVLYANINFPNLKQDYPDWSSRCKQIMKLWRKVPAADKAPYLQKAKDNRAAHRINK
VQKQAESQINKQTKVGDIARKTDRPALHLRIPPQPGALGSPPPAAAPTIFIGSPTTPAGL
STSADGFLKPPAGSVPGPDSPGELFLKLPPQVPAQAPSQDPFGLAPAYPLEPRFPTAPPT
YPPYPSPTGAPAQPPMLGASSRPGAGQPGEFHTTPPGTPRHQPSTPDPFLKPRCPSLDNL
AVPESPGVGGGKASEPLLSPPPFGESRKALEVKKEELGASSPSYGPPNLGFVDSPSSGTH
LGGLELKTPDVFKAPLTPRASQVEPQSPGLGLRPQEPPPAQALAPSPPSHPDIFRPGSYT
DPYAQPPLTPRPQPPPPESCCALPPRSLPSDPFSRVPVSPQSQSSSQSPLTPRPLSAEAF
CPSPVTPRFQSPDPYSRPPSRPQSRDPFAPLHKPPRPQPPEVAFKAGSLAHTSLGAGGFP
AALPAGPAGELHAKVPSGQPPNFVRSPGTGAFVGTPSPMRFTFPQAVGEPSLKPPVPQPG
LPPPHGINSHFGPGPTLGKPQSTNYTVATGNFHPSGSPLGPSSGSTGESYGLSPLRPPSV
LPPPAPDGSLPYLSHGASQRSGITSPVEKREDPGTGMGSSLATAELPGTQDPGMSGLSQT
ELEKQRQRQRLRELLIRQQIQRNTLRQEKETAAAAAGAVGPPGSWGAEPSSPAFEQLSRG
QTPFAGTQDKSSLVGLPPSKLSGPILGPGSFPSDDRLSRPPPPATPSSMDVNSRQLVGGS
QAFYQRAPYPGSLPLQQQQQQLWQQQQATAATSMRFAMSARFPSTPGPELGRQALGSPLA
GISTRLPGPGEPVPGPAGPAQFIELRHNVQKGLGPGGTPFPGQGPPQRPRFYPVSEDPHR
LAPEGLRGLAVSGLPPQKPSAPPAPELNNSLHPTPHTKGPTLPTGLELVNRPPSSTELGR
PNPLALEAGKLPCEDPELDDDFDAHKALEDDEELAHLGLGVDVAKGDDELGTLENLETND
PHLDDLLNGDEFDLLAYTDPELDTGDKKDIFNEHLRLVESANEEAEREALLRGVEPGPLG
PEERPPPAADASEPRLASVLPEVKPKVEEGGRHPSPCQFTIATPKVEPAPAANSLGLGLK
PGQSMMGSRDTRMGTGPFSSSGHTAEKASFGATGGPPAHLLTPSPLSGPGGSSLLEKFEL
ESGALTLPGGPAASGDELDKMESSLVASELPLLIEDLLEHEKKELQKKQQLSAQLQPAQQ
QQQQQQQHSLLPAPGPAQAMSLPHEGSSPSLAGSQQQLSLGLAVARQPGLPQPLMPTQPP
AHALQQRLAPSMAMVSNQGHMLSGQHGGQAGLVPQQSSQPVLSQKPMGTMPPSMCMKPQQ
LAMQQQLANSFFPDTDLDKFAAEDIIGPIAKAKMVALKGIKKVMAQGSIGVAPGMNRQQV
SLLAQRLSGGPSSDLQNHVAAGSGQERSAGDPSQPRPNPPTFAQGVINEADQRQYEEWLF
HTQQLLQMQLKVLEEQIGVHRKSRKALCAKQRTAKKAGREFPEADAEKLKLVTEQQSKIQ
KQLDQVRKQQKEHTNLMAEYRNKQQQQQQQQQQQQQQHSAVLALSPSQSPRLLTKLPGQL
LPGHGLQPPQGPPGGQAGGLRLTPGGMALPGQPGGPFLNTALAQQQQQQHSGGAGSLAGP
SGGFFPGNLALRSLGPDSRLLQERQLQLQQQRMQLAQKLQQQQQQQQQQQHLLGQVAIQQ
QQQQGPGVQTNQALGPKPQGLMPPSSHQGLLVQQLSPQPPQGPQGMLGPAQVAVLQQQHP
GALGPQGPHRQVLMTQSRVLSSPQLAQQGQGLMGHRLVTAQQQQQQQQHQQQGSMAGLSH
LQQSLMSHSGQPKLSAQPMGSLQQLQQQQQLQQQQQLQQQQQQQLQQQQQLQQQQLQQQQ
QQQQLQQQQQQQLQQQQQQLQQQQQQQQQQFQQQQQQQQMGLLNQSRTLLSPQQQQQQQV
ALGPGMPAKPLQHFSSPGALGPTLLLTGKEQNTVDPAVSSEATEGPSTHQGGPLAIGTTP
ESMATEPGEVKPSLSGDSQLLLVQPQPQPQPSSLQLQPPLRLPGQQQQQVSLLHTAGGGS
HGQLGSGSSSEASSVPHLLAQPSVSLGDQPGSMTQNLLGPQQPMLERPMQNNTGPQPPKP
GPVLQSGQGLPGVGIMPTVGQLRAQLQGVLAKNPQLRHLSPQQQQQLQALLMQRQLQQSQ
AVRQTPPYQEPGTQTSPLQGLLGCQPQLGGFPGPQTGPLQELGAGPRPQGPPRLPAPPGA
LSTGPVLGPVHPTPPPSSPQEPKRPSQLPSPSSQLPTEAQLPPTHPGTPKPQGPTLEPPP
GRVSPAAAQLADTLFSKGLGPWDPPDNLAETQKPEQSSLVPGHLDQVNGQVVPEASQLSI
KQEPREEPCALGAQSVKREANGEPIGAPGTSNHLLLAGPRSEAGHLLLQKLLRAKNVQLS
TGQGSEGLRAEINGHIDSKLAGLEQKLQGTPSNKEDAAARKPLTPKPKRVQKASDRLVSS
RKKLRKEDGVRASEALLKQLKQELSLLPLTEPAITANFSLFAPFGSGCPVNGQSQLRGAF
GSGALPTGPDYYSQLLTKNNLSNPPTPPSSLPPTPPPSVQQKMVNGVTPSEELGEHPKDA
ASARDSERALRDTSEVKSLDLLAALPTPPHNQTEDVRMESDEDSDSPDSIVPASSPESIL
GEEAPRFPHLGSGRWEQEDRALSPVIPLIPRDSIPVFPDTKPYGALGLEVPGKLPVTTWE
KGKGSEVSVMLTVSAAADKNLNGVMVAVAELLSMKIPNSYEVLFPESPARGGTEPKKGEA
EGPGGKEKGLEGKSPDTGPDWLKQFDAVLAGYTLKRQLDILSLLKQESPAPEPPTQHRYT
YNVSNLDVRQLSAPPPEEPSPPPSPLAPSPASPPTEPLVELPTEPLAEPPVPSPLPLASS
PESARPKPRARPPEEGEDTRPPRLKKWKGVRWKRLRLLLTIQKGSGRQEDEREVAEFMEQ
LGTALRPDKVPRDMRRCCFCHEEGDGATDGPARLLNLDLDLWVHLNCALWSTEVYETQGG
ALMNVEVALHRGLLTKCSLCQRTGATSSCNRMRCPNVYHFGCAIRAKCMFFKDKTMLCPM
HKIKGPCEQELSSFAVFRRVYIERDEVKQIASIIQRGERLHMFRVGGLVFHAIGQLLPHQ
MADFHSATALYPVGYEATRIYWSLRTNNRRCCYRCSIGENNGRPEFVIKVIEQGLEDLVF
TDASPQAVWNRIIEPVAAMRKEADMLRLFPEYLKGEELFGLTVHAVLRIAESLPGVESCQ
NYLFRYGRHPLMELPLMINPTGCARSEPKILTHYKRPHTLNSTSMSKAYQSTFTGETNTP
YSKQFVHSKSSQYRRLRTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEV
ANRREKIYEEQNRGIYMFRINNEHVIDATLTGGPARYINHSCAPNCVAEVVTFDKEDKII
IISSRRIPKGEELTYDYQFDFEDDQHEIPCHCGAWNCRKWMN
Enzyme 70 Number of Residues 5262
Enzyme 70 Molecular Weight 564180.6
Enzyme 70 Theoretical pI 5.79
Enzyme 70 GO Classification
Function
  • DNA binding
  • binding
  • cation binding
  • ion binding
  • metal ion binding
  • nucleic acid binding
  • protein binding
  • transition metal ion binding
  • zinc ion binding
Process
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 70 General Function Involved in DNA binding
Enzyme 70 Specific Function Histone methyltransferase. Methylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in beta-globin locus transcription regulation by being recruited by NFE2. Acts as a coactivator for estrogen receptor by being recruited by ESR1, thereby activating transcription
Enzyme 70 Pathways Not Available
Enzyme 70 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 70 Pfam Domain Function
Enzyme 70 Signals
  • None
Enzyme 70 Transmembrane Regions
  • None
Enzyme 70 Essentiality Not Available
Enzyme 70 GenBank ID Protein 2358285 Link Image
Enzyme 70 UniProtKB/Swiss-Prot ID O14686 Link Image
Enzyme 70 UniProtKB/Swiss-Prot Entry Name MLL2_HUMAN Link Image
Enzyme 70 PDB ID Not Available
Enzyme 70 Cellular Location Not Available
Enzyme 70 Gene Sequence >15789 bp
ATGGACAGCCAGAACCTGGCTGGTGAGGATAAAGATTCACAACCGGCAGCTGATGGACCT
GCAGCCTCTGAGGACCCAAGTGCCACTGAGTCAGACCTGCCCAACCCACATGTGGGAGAG
GTCTCTGTCCTTAGTTCTGGGAGTCCCAGGCTTCAGGAGACTCCTCAGGACTGCAGTGGG
GGTCCGGTGCGGCGTTGTGCTCTCTGTAACTGCGGGGAGCCCGCTCTACACGGGCAGCGG
GAGCTACGGCGCTTTGAGTTGCCATTTGATTGGCCCCGGTGTCCAGTGGTGTCCCCTGGG
GGGAGCCCAGGGCCCAATGAGGCAGTGCTGCCCAGTGAGGACCTATCACAGATTGGTTTC
CCTGAGGGCCTTACACCTGCCCACCTAGGAGAACCTGGAGGGTCCTGCTGGGCTCACCAT
TGGTGTGCTGCATGGTCGGCAGGCGTATGGGGGCAGGAGGGCCCACAACTATGTGGTGTG
GACAAGGCCATCTTCTCAGGGATCTCACAGCGCTGCTCCCACTGCACCAGGCTCGGTGCC
TCCATCCCTTGCCGCTCACCTGGATGTCCACGGCTTTACCACTTCCCCTGCGCGACTGCC
AGCGGTTCCTTCCTATCCATGAAAACACTGCAGCTGCTATGCCCAGAGCACAGTGAGGGG
GCTGCATATCTGGAGGAGGCTCGCTGTGCAGTGTGTGAGGGGCCAGGGGAGCTGTGTGAC
CTGTTCTTCTGTACCAGCTGTGGGCATCACTATCACGGGGCCTGCCTGGACACTGCTCTG
ACTGCCCGCAAACGTGCTGGCTGGCAGTGCCCTGAATGCAAAGTGTGCCAAGCCTGCAGG
AAACCTGGGAATGACTCTAAGATGTTGGTTTGCGAGACGTGTGACAAAGGATACCATACT
TTCTGCCTAAAACCACCCATGGAGGAACTGCCTGCTCACTCTTGGAAGTGCAAGGCGTGC
CGGGTGTGCCGGGCCTGTGGGGCGGGCTCAGCAGAACTGAATCCCAACTCGGAGTGGTTT
GAGAACTACTCTCTCTGTCACCGCTGTCACAAAGCCCAGGGAGGTCAGACTATCCGCTCC
GTTGCTGAGCAGCATACCCCGGTGTGTAGCAGATTTTCACCCCCAGAGCCTGGCGATACC
CCCACTGACGAGCCCGATGCTCTGTACGTTGCATGCCAAGGGCAGCCAAAGGGTGGGCAC
GTGACCTCTATGCAACCCAAGGAACCAGGGCCCCTGCAATGTGAAGCCAAACCACTAGGG
AAAGCAGGGGTCCAACTTGAGCCCCAGTTGGAGGCCCCCCTAAACGAGGAGATGCCACTG
CTGCCCCCACCTGAGGAGTCACCCCTGTCCCCACCACCTGAGGAATCACCCACGTCCCCA
CCACCTGAGGCATCACGCCTGTCGCCACCACCTGAGGAATTGCCCGCATCCCCACTTCCT
GAGGCATTGCACCTGTCCCGGCCGCTGGAGGAATCGCCCCTCTCTCCGCCGCCTGAGGAG
TCTCCTCTGTCTCCCCCACCTGAATCATCACCTTTTTCTCCACTGGAGGAGTCGCCCTTG
TCTCCACCGGAAGAGTCACCCCCATCTCCTGCACTTGAGACGCCTCTATCCCCACCACCT
GAAGCATCGCCCCTGTCCCCACCATTTGAAGAATCTCCTTTGTCCCCGCCACCTGAGGAA
TTGCCCACTTCCCCGCCACCTGAAGCATCTCGCCTGTCTCCACCACCTGAGGAGTCACCC
ATGTCCCCTCCACCTGAAGAGTCACCCATGTCTCCACCACCGGAGGCATCTCGTCTGTTC
CCACCATTTGAAGAGTCTCCTCTGTCCCCTCCACCTGAGGAGTCTCCCCTTTCCCCACCA
CCTGAGGCATCACGCCTGTCCCCACCACCTGAGGACTCGCCTATGTCCCCACCACCTGAA
GAATCACCTATGTCCCCCCCACCTGAGGTATCGCGCCTATCCCCCCTGCCTGTGGTGTCA
CGCCTGTCTCCACCGCCTGAGGAATCTCCCTTGTCCCCACCGGCCCTGTCTCCTTTGGGG
GAGTTAGAGTACCCCTTTGGTGCCAAAGGGGACAGTGACCCTGAGTCACCGTTGGCTGCC
CCCATCCTGGAGACACCCATCAGCCCTCCACCAGAAGCTAACTGCACTGACCCTGAGCCT
GTCCCCCCTATGATCCTTCCCCCATCTCCAGGCTCCCCAGTGGGGCCGGCTTCTCCCATC
CTGATGGAGCCCCTTCCTCCTCAGTGTTCGCCACTCCTTCAGCATTCCCTGGTTCCCCAA
AACTCCCCTCCTTCCCAGTGCTCTCCTCCTGCCCTACCACTGTCCGTTCCCTCCCCGTTG
AGTCCCATAGGGAAGGTAGTGGGGGTCTCAGATGAGGCTGAGCTGCACGAGATGGAGACT
GAGAAAGTTTCAGAACCTGAATGCCCAGCCTTGGAACCCAGTGCCACCAGTCCTCTCCCT
TCCCCAATGGGGGACCTTTCCTGCCCCGCCCCCAGCCCTGCCCCAGCCCTGGATGACTTC
TCTGGCCTAGGGGAAGACACAGCCCCTCTGGATGGGATTGATGCTCCGGGTTCACAGCCA
GAGCCTGGACAGACCCCTGGCAGTTTGGCTAGTGAACTTAAAGGCTCCCCTGTGCTCCTG
GACCCCGAGGAGCTGGCCCCTGTGACCCCTATGGAGGTCTACCCCGAATGCAAGCAGACA
GCAGGGCGGGGCTCACCATGTGAAGAACAGGAAGAGCCACGTGCACCGGTGGCCCCCACA
CCACCCACTCTCATCAAATCCGACATCGTTAACGAGATCTCTAATCTGAGCCAGGGTGAT
GCCAGTGCCAGTTTTCCTGGCTCAGAGCCCCTCCTGGGCTCTCCAGACCCGGAGGGGGGT
GGCTCCCTGTCCATGGAGTTGGGGGTCTCTACGGATGTTAGTCCAGCCCGAGATGAGGGC
TCCCTACGGCTCTGTACTGACTCACTGCCAGAGACTGATGACTCACTATTGTGCGATGCT
GGGACAGCTATCAGCGGAGGCAAAGCTGAGGGGGAGAAGGGGCGGCGGCGCAGCTCCCCA
GCCCGTTCCCGCATCAAACAGGGTCGCAGCAGCAGTTTCCCAGGAAGACGCCGGCCTCGT
GGAGGAGCCCATGGAGGGCGTGGTAGAGGACGGGCCCGGCTAAAGTCAACTGCTTCTTCC
ATTGAGACTCTGGTAGTTGCTGACATTGATAGCTCTCCCAGTAAGGAGGAGGAGGAAGAA
GATGATGACACCATGCAGAATACCGTGGTTCTCTTCTCCAACACAGACAAATTTGTCCTA
ATGCAGGACATGTGTGTGGTATGTGGCAGCTTTGGCCGGGGGGCAGAGGGCCACCTCCTT
GCCTGTTCGCAGTGCTCTCAGTGCTATCACCCTTACTGTGTCAACAGCAAGATCACCAAG
GTGATGCTGCTCAAGGGCTGGCGTTGTGTGGAGTGTATTGTGTGTGAGGTGTGTGGCCAG
GCCTCCGACCCCTCACGCCTGCTGCTCTGTGATGACTGTGATATTAGCTACCACACATAC
TGCCTGGACCCCCCACTGCTCACCGTCCCCAAGGGCGGCTGGAAGTGCAAGTGGTGTGTG
TCCTGTATGCAGTGTGGGGCTGCTTCCCCTGGCTTCCACTGTGAATGGCAGAATAGTTAC
ACACACTGTGGGCCCTGTGCCAGCCTGGTGACCTGCCCTATCTGTCATGCTCCTTACGTA
GAAGAGGACCTACTAATCCAGTGCCGCCACTGTGAACGGTGGATGCATGCAGGCTGTGAG
AGCCTCTTCACAGAGGACGATGTGGACCACGCACCCGATGAAGGCTTTGACTGTGTCTCC
TGCCAGCCCTACGTGGTAAAGCCTGTGGCGCCTGTTGCACCTCCAGAGCTGGTGCCCATG
AAGGTGAAAGAGCCAGAGCCCCAGTACTTTCGCTTCGAAGGCGTGTGGCTGACAGAAACT
GGCATGGCCTTGCTGCGTAACCTGACCATGTCACCACTGCACAAGCGGCGCCAACGGCGA
GGACGGCTTGGCCTCCCAGGCGAGGCAGGATTGGAGGGTTCTGAGCCCTCAGATGCCCTT
GGCCCTGATGACAAGAAGGATGGGGACCTGGACACCGATGAGCTGCTCAAGGGTGAAGGT
GGTGTGGAGCACATGGAGTGCGAAATTAAACTGGAGGGCCCCGTCAGCCCTGATGTGGAG
CCTGGCAAAGAGGAGACCGAGGAAAGCAAAAAACGCAAGCGTAAACCATATCGGCCTGGC
ATTGGTGGTTTCATGGTGCGACAGCGGAAATCCCACACACGCACGAAAAAGGGGCCTGCT
GCACAGGCGGAGGTGTTGAGTGGGGATGGGCAGCCCGACGAGGTGATACCTGCTGACCTG
CCTGCAGAGGGCGCCGTGGAGCAGAGCTTAGCTGAAGGGGATGAGAAGAAGAAGCAACAG
CGGCGAGGGCGCAAGAGGAGCAAACTGGAGGGCATGTTCCCTGCTTACTTGCAGGAAGCC
TTCTTTGGGAAGGAGCTGCTGGACCTGAGCCGTAAGGCCCTTTTTGCAGTTGGGGTGGGC
CGGCCAAGCTTTGGACTAGGGACCCCAAAAGCCAAGGGAGATGGAGGCTCAGAAAGGAAG
GAACTCCCCACATCGCAGAAAGGAGATGATGGTCCAGATATTGCAGATGAAGAATCCCGT
GGCCTCGAGGGCAAAGCCGATACACCAGGACCTGAGGATGGGGGCGTGAAGGCATCCCCA
GTGCCCAGTGACCCTGAGAAGCCAGGCACCCCAGGTGAAGGGATGCTTAGCTCTGACTTA
GACAGGATTTCCACAGAAGAACTGCCCAAGATGGAATCCAAGGACCTGCAGCAGCTCTTC
AAGGATGTTCTGGGCTCTGAACGAGAACAGCATCTGGGTTGTGGAACCCCTGGCCTAGAA
GGCAGCCGTACGCCACTGCAGAGGCCCTTTCTTCAAGGTGGACTCCCTTTGGGCAATCTG
CCCTCCAGCAGCCCAATGGACTCCTACCCAGGCCTCTGCCAGTCCCCGTTCCTGGATTCT
AGGGAGCGCGGGGGCTTCTTTAGCCCGGAACCCGGTGAGCCCGACAGCCCCTGGACGGGC
TCAGGTGGCACCACGCCCTCCACCCCCACAACCCCCACCACGGAGGGTGAGGGCGACGGA
CTCTCCTATAACCAGCGGAGTCTTCAGCGCTGGGAGAAGGATGAGGAGTTGGGCCAGCTG
TCCACCATCTCGCCTGTGCTCTATGCCAACATTAATTTTCCTAATCTCAAGCAAGACTAC
CCAGACTGGTCAAGCCGTTGCAAACAAATCATGAAGCTCTGGAGAAAGGTTCCAGCAGCT
GACAAAGCCCCCTACCTGCAAAAGGCCAAAGATAACCGGGCAGCTCACCGCATCAACAAG
GTGCAGAAGCAGGCTGAGAGCCAGATCAACAAGCAGACCAAGGTGGGCGACATAGCCCGT
AAGACTGACCGACCGGCCCTACATCTCCGCATTCCCCCGCAGCCAGGGGCACTGGGCAGC
CCGCCCCCCGCTGCTGCCCCCACCATTTTCATTGGCAGCCCCACTACCCCCGCCGGCTTG
TCTACCTCTGCGGACGGGTTCCTGAAGCCGCCGGCGGGCTCGGTGCCTGGCCCTGACTCG
CCTGGTGAGCTCTTCCTCAAGCTCCCACCCCAGGTGCCCGCCCAAGCGCCTTCGCAGGAC
CCCTTTGGACTGGCCCCTGCCTATCCCCTGGAGCCCCGCTTCCCCACGGCACCGCCCACC
TATCCCCCCTATCCTAGTCCTACGGGGGCCCCTGCGCAGCCCCCGATGCTGGGCGCCTCA
TCTCGTCCTGGGGCTGGCCAGCCAGGGGAATTCCACACTACCCCACCTGGCACCCCCAGA
CACCAGCCCTCCACACCTGACCCGTTCCTCAAACCCCGCTGCCCCTCGCTGGATAACTTG
GCTGTGCCTGAGAGCCCTGGGGTAGGGGGAGGCAAAGCTTCCGAGCCCCTGCTCTCGCCC
CCACCTTTTGGGGAGTCCCGGAAGGCCCTAGAGGTGAAGAAGGAAGAGCTTGGGGCATCC
TCTCCTAGCTATGGGCCCCCAAACCTGGGCTTTGTTGACTCACCCTCCTCAGGCACCCAC
CTGGGTGGCCTGGAGTTAAAGACACCTGATGTCTTCAAAGCCCCCCTGACCCCTCGGGCA
TCTCAGGTAGAGCCCCAGAGCCCGGGCTTGGGCCTAAGGCCCCAGGAGCCACCCCCTGCC
CAGGCTTTGGCACCTTCTCCTCCAAGTCACCCAGACATCTTTCGCCCTGGCTCCTACACT
GACCCATATGCTCAGCCCCCATTGACTCCTCGGCCCCAACCTCCGCCCCCTGAGAGCTGC
TGTGCTCTGCCCCCTCGCTCACTGCCCTCCGACCCTTTCTCCCGAGTGCCTGTCAGTCCT
CAGTCCCAGTCCAGCTCCCAGTCTCCACTGACACCCCGGCCTCTGTCTGCTGAAGCTTTT
TGCCCATCACCCGTTACCCCTCGCTTCCAGTCCCCTGACCCTTATTCTCGCCCACCCTCA
CGCCCTCAGTCCCGTGACCCATTTGCCCCATTGCATAAGCCACCCCGACCCCAGCCCCCT
GAAGTTGCCTTTAAGGCTGGGTCTCTAGCCCACACTTCGCTGGGGGCTGGGGGGTTCCCA
GCAGCCCTGCCCGCGGGGCCAGCAGGTGAGCTCCATGCCAAGGTCCCAAGTGGGCAGCCC
CCCAATTTTGTCCGGTCCCCTGGGACGGGTGCATTTGTGGGCACCCCCTCTCCCATGCGT
TTCACTTTCCCTCAGGCAGTAGGGGAGCCTTCCCTAAAGCCCCCTGTCCCTCAGCCTGGT
CTCCCGCCACCCCATGGGATCAACAGCCATTTTGGGCCCGGCCCCACCTTGGGCAAGCCT
CAAAGCACAAACTACACAGTAGCCACAGGGAACTTCCACCCATCGGGCAGCCCCCTGGGG
CCCAGCAGCGGGTCCACAGGGGAGAGCTATGGGCTGTCCCCACTACGCCCTCCGTCGGTT
CTGCCACCACCTGCACCCGACGGATCCCTCCCCTACCTGTCCCATGGAGCCTCACAGCGA
TCAGGCATCACCTCTCCTGTCGAAAAGCGAGAAGACCCAGGGACTGGAATGGGTAGCTCT
TTGGCGACAGCTGAACTCCCAGGTACCCAGGACCCAGGCATGTCCGGCCTTAGCCAAACA
GAGCTGGAGAAGCAACGGCAGCGCCAGCGGCTACGAGAGCTGCTGATTCGGCAGCAGATC
CAGCGCAACACCCTGCGGCAGGAGAAGGAAACAGCTGCAGCAGCTGCGGGAGCAGTGGGG
CCTCCAGGCAGCTGGGGTGCTGAGCCCAGCAGCCCTGCCTTTGAGCAGCTGAGTCGAGGC
CAGACCCCCTTTGCTGGGACACAGGACAAGAGCAGCCTTGTGGGGTTGCCCCCAAGCAAG
CTGAGTGGCCCCATCCTGGGGCCAGGGTCCTTCCCTAGCGATGACCGACTCTCCCGGCCA
CCTCCACCAGCCACGCCTTCCTCTATGGATGTGAACAGCCGGCAACTGGTAGGAGGCTCC
CAAGCTTTCTATCAGCGAGCACCCTATCCTGGGTCCCTGCCCTTACAGCAGCAACAGCAA
CAACTGTGGCAGCAACAACAGGCAACAGCAGCAACCTCCATGCGATTTGCCATGTCAGCT
CGCTTTCCATCAACTCCTGGACCTGAACTTGGCCGCCAAGCCCTAGGTTCCCCGTTGGCG
GGAATTTCCACCCGTCTGCCAGGCCCTGGTGAGCCAGTGCCTGGTCCAGCTGGTCCTGCC
CAGTTCATTGAGCTGCGGCACAATGTACAGAAAGGACTGGGACCTGGGGGCACTCCGTTT
CCTGGTCAGGGCCCACCTCAGAGACCCCGTTTTTACCCTGTAAGTGAGGACCCCCACCGA
CTGGCTCCTGAAGGGCTTCGGGGCCTGGCGGTATCAGGTCTTCCCCCACAGAAACCCTCA
GCCCCACCGGCCCCTGAATTGAACAACAGTCTTCATCCAACACCCCACACCAAGGGTCCT
ACCCTGCCAACTGGTTTGGAGCTGGTCAACCGGCCCCCGTCGAGCACTGAGCTTGGCCGC
CCCAATCCTCTGGCCCTGGAAGCTGGGAAGTTGCCCTGTGAGGATCCCGAGCTGGATGAC
GATTTTGATGCCCACAAGGCCCTAGAGGATGATGAAGAGCTTGCTCACCTGGGTCTGGGT
GTGGATGTGGCCAAGGGTGATGATGAACTTGGCACCTTAGAAAACCTGGAGACCAATGAC
CCCCACTTGGATGACCTGCTCAATGGAGACGAGTTTGACCTGCTGGCATATACTGATCCT
GAGCTGGACACTGGGGACAAGAAGGATATCTTCAATGAGCACCTGAGGCTGGTAGAATCG
GCTAATGAGGAGGCTGAACGGGAGGCCCTGCTGCGGGGGGTGGAGCCAGGACCCTTGGGC
CCTGAGGAGCGCCCTCCCCCTGCTGCTGATGCCTCTGAACCCCGCCTGGCATCTGTGCTC
CCTGAGGTGAAGCCCAAGGTGGAGGAGGGTGGACGCCACCCTTCTCCTTGCCAATTCACC
ATTGCTACCCCCAAGGTAGAGCCCGCACCTGCTGCCAATTCCCTTGGCCTGGGGCTAAAG
CCAGGACAGAGCATGATGGGCAGCCGGGATACCCGGATGGGCACAGGGCCATTTTCTAGC
AGTGGGCACACAGCTGAGAAGGCCTCCTTTGGGGCCACGGGAGGGCCACCAGCTCACCTG
CTGACCCCCAGCCCACTGAGTGGCCCAGGAGGATCCTCCCTGCTGGAAAAGTTTGAGCTC
GAGAGTGGGGCTTTGACCTTGCCTGGTGGACCTGCAGCATCTGGGGATGAGCTAGACAAG
ATGGAGAGCTCACTGGTAGCCAGCGAGTTACCCCTGCTCATTGAGGACCTGTTGGAGCAT
GAGAAGAAGGAGCTGCAGAAGAAGCAGCAGCTTTCAGCACAGTTGCAGCCTGCCCAGCAG
CAGCAGCAACAGCAGCAGCAGCATTCCCTACTGCCTGCACCAGGCCCTGCCCAGGCCATG
TCTTTGCCACATGAGGGCTCTTCTCCCAGTTTGGCTGGGTCCCAACAGCAGCTTTCCCTG
GGTCTTGCAGTTGCCCGACAGCCAGGTTTGCCCCAGCCACTGATGCCCACCCAGCCACCA
GCTCATGCCCTCCAGCAACGCCTGGCTCCATCCATGGCTATGGTGTCCAATCAAGGGCAT
ATGCTAAGTGGGCAGCATGGAGGGCAGGCAGGCTTGGTACCCCAGCAGAGCTCACAGCCA
GTGCTATCACAGAAGCCCATGGGCACCATGCCACCTTCCATGTGCATGAAGCCGCAGCAA
TTGGCAATGCAGCAGCAGCTGGCAAACAGCTTCTTCCCAGATACAGACCTGGACAAATTT
GCTGCAGAAGATATCATTGGTCCCATTGCAAAGGCCAAGATGGTGGCTTTGAAAGGCATC
AAGAAAGTGATGGCTCAGGGCAGCATTGGGGTGGCACCTGGTATGAACAGACAGCAAGTG
TCTCTGCTAGCCCAGAGGCTCTCGGGGGGACCTAGCAGTGATCTGCAGAACCATGTGGCA
GCTGGGAGTGGCCAGGAGCGGAGTGCTGGTGATCCCTCCCAGCCTCGTCCCAACCCGCCC
ACTTTTGCTCAGGGAGTGATCAATGAAGCTGACCAGCGGCAGTATGAGGAGTGGCTGTTC
CATACCCAGCAGCTCCTACAGATGCAGCTGAAGGTGCTAGAGGAGCAGATTGGTGTACAC
CGCAAGTCCCGGAAGGCTCTGTGTGCCAAGCAGCGCACTGCCAAAAAAGCTGGCCGTGAG
TTCCCAGAAGCTGATGCTGAGAAGCTCAAGCTGGTTACAGAGCAGCAGAGCAAGATCCAG
AAACAACTGGATCAGGTCCGGAAACAGCAGAAGGAGCACACTAATCTCATGGCAGAATAT
CGGAACAAGCAGCAGCAACAACAGCAGCAGCAGCAGCAACAACAGCAACAGCACTCAGCT
GTGCTGGCTCTCAGCCCTTCCCAGAGTCCCCGGCTGCTCACCAAGCTCCCTGGTCAGCTG
CTCCCTGGCCATGGGCTGCAGCCACCACAGGGGCCTCCGGGTGGGCAAGCCGGAGGTCTT
CGCCTGACCCCTGGGGGTATGGCACTACCTGGACAGCCTGGTGGCCCCTTCCTTAATACA
GCTCTGGCCCAACAGCAGCAACAGCAACATTCTGGTGGGGCTGGATCCCTGGCTGGCCCT
TCAGGGGGCTTCTTCCCTGGCAACCTTGCTCTTCGAAGCCTCGGACCTGATTCAAGGCTT
TTACAGGAAAGGCAGCTGCAGCTGCAGCAGCAACGTATGCAGCTGGCCCAGAAACTGCAG
CAGCAGCAGCAGCAGCAACAGCAGCAGCAGCACCTTCTAGGACAGGTGGCAATCCAGCAG
CAACAGCAGCAGGGTCCTGGAGTACAGACAAACCAAGCTCTGGGTCCCAAGCCCCAGGGC
CTTATGCCTCCCAGCAGCCACCAAGGCCTCCTGGTCCAGCAGCTGTCCCCTCAACCACCC
CAGGGGCCCCAGGGCATGCTGGGCCCTGCCCAGGTGGCTGTGTTGCAGCAGCAGCACCCT
GGAGCTTTGGGCCCCCAGGGCCCTCACAGACAGGTGCTTATGACCCAGTCCCGGGTGCTC
AGTTCCCCCCAGCTGGCACAGCAGGGTCAGGGCCTTATGGGACACAGGCTGGTCACAGCC
CAGCAGCAGCAGCAGCAACAACAGCACCAACAGCAAGGGTCCATGGCAGGGCTGTCCCAT
CTTCAGCAAAGTCTGATGTCACACAGTGGGCAGCCCAAACTGAGCGCTCAGCCCATGGGC
TCTTTACAGCAGCTTCAGCAGCAGCAGCAGCTGCAACAGCAACAGCAACTTCAGCAGCAG
CAGCAGCAGCAGCTACAACAGCAACAGCAACTTCAGCAGCAACAGCTTCAACAGCAGCAA
CAGCAGCAGCAGCTTCAACAACAGCAGCAGCAACAGCTTCAACAGCAGCAACAGCAGCTA
CAACAGCAACAGCAACAACAACAGCAGCAGTTTCAACAGCAGCAGCAACAGCAGCAGATG
GGCCTTTTAAACCAGAGTCGAACTTTACTGTCCCCTCAGCAACAACAGCAGCAGCAAGTG
GCACTTGGCCCTGGCATGCCAGCAAAGCCTCTTCAACACTTTTCTAGCCCTGGAGCCCTG
GGTCCAACCCTCCTCCTGACGGGCAAGGAACAAAACACCGTAGACCCAGCCGTTTCTTCA
GAGGCCACTGAGGGGCCCTCTACACATCAGGGAGGGCCGTTAGCAATAGGAACTACCCCT
GAGTCAATGGCCACTGAACCAGGAGAGGTAAAGCCCTCACTCTCTGGGGACTCACAACTC
CTGCTTGTCCAACCCCAGCCCCAGCCTCAGCCCAGCTCTCTGCAGCTGCAGCCACCTCTG
AGGCTTCCAGGACAACAGCAGCAGCAAGTTAGCCTGCTCCACACAGCAGGTGGAGGAAGC
CATGGGCAGCTAGGCAGTGGATCATCTTCTGAGGCCTCATCTGTGCCCCACCTGCTGGCT
CAGCCCTCTGTTTCCTTAGGGGATCAGCCTGGGTCCATGACCCAGAACCTTCTGGGCCCC
CAACAGCCCATGCTAGAGCGGCCCATGCAAAATAATACAGGGCCACAACCTCCCAAACCA
GGACCTGTCCTCCAGTCTGGGCAGGGTCTGCCTGGGGTTGGAATCATGCCTACGGTGGGT
CAGCTTCGAGCACAGCTCCAAGGAGTCCTGGCCAAAAACCCACAGCTGCGGCACTTAAGT
CCTCAGCAGCAGCAGCAGCTACAGGCACTCCTCATGCAGCGGCAGCTGCAGCAGAGTCAG
GCAGTACGCCAGACCCCACCCTACCAGGAGCCTGGGACCCAGACCTCTCCCCTCCAGGGC
CTCCTGGGCTGCCAACCTCAACTTGGGGGCTTCCCTGGACCACAGACAGGCCCCCTCCAG
GAGCTAGGGGCAGGGCCTCGACCTCAGGGCCCACCCCGGCTCCCTGCCCCACCAGGAGCC
TTATCTACAGGACCAGTCCTTGGCCCTGTCCATCCCACACCTCCACCATCCAGCCCTCAA
GAGCCAAAGAGACCTTCACAATTACCTTCCCCCAGCTCCCAGCTTCCCACTGAGGCCCAG
CTCCCTCCCACCCATCCAGGGACCCCCAAACCTCAGGGGCCAACCTTGGAGCCGCCTCCT
GGGAGGGTCTCACCTGCTGCTGCCCAGCTTGCAGATACCTTGTTTAGCAAGGGTCTGGGA
CCTTGGGATCCCCCAGACAACCTAGCAGAAACCCAGAAGCCAGAGCAGAGCAGCCTGGTA
CCTGGGCATCTGGACCAGGTGAATGGACAGGTGGTGCCTGAGGCATCCCAACTCAGCATC
AAGCAGGAACCTCGGGAAGAGCCATGTGCCCTGGGAGCCCAGTCAGTGAAGAGGGAGGCC
AATGGGGAGCCAATAGGGGCACCAGGAACCAGCAACCACCTCCTGCTGGCAGGCCCTCGC
TCAGAAGCTGGGCATCTGCTCTTGCAGAAGCTACTCCGGGCAAAGAATGTGCAACTCAGC
ACTGGGCAGGGGTCCGAGGGGCTGCGAGCTGAGATCAACGGGCACATTGACAGCAAGCTG
GCTGGGCTGGAGCAGAAACTACAGGGTACCCCCAGCAACAAGGAGGATGCAGCAGCAAGG
AAGCCTTTGACACCGAAGCCCAAGCGGGTACAGAAGGCAAGCGACAGGTTGGTGAGCTCC
CGAAAGAAGCTGCGGAAGGAGGACGGCGTCAGGGCCAGCGAGGCCTTGCTGAAACAGCTG
AAACAGGAGCTGTCCCTGCTGCCCCTAACGGAGCCTGCTATCACCGCCAATTTTAGCCTC
TTTGCCCCCTTTGGCAGTGGCTGCCCAGTCAATGGGCAGAGCCAGCTGAGGGGGGCCTTT
GGAAGTGGGGCGCTGCCCACTGGCCCTGACTACTATTCCCAGCTGCTTACCAAGAATAAC
CTGAGTAACCCGCCGACACCACCCTCGTCGCTGCCCCCCACCCCACCCCCATCGGTGCAG
CAGAAGATGGTGAATGGCGTCACCCCATCTGAAGAGCTGGGGGAGCACCCCAAGGATGCT
GCCTCTGCCCGGGATAGTGAAAGGGCACTGAGGGATACTTCAGAGGTGAAGAGTCTAGAC
CTGCTGGCTGCCTTGCCTACACCCCCTCACAATCAGACTGAGGATGTCAGGATGGAGAGT
GATGAGGATAGCGATTCTCCTGACAGCATTGTGCCAGCTTCATCCCCTGAGAGCATCTTG
GGGGAGGAGGCCCCTCGTTTCCCTCATCTGGGCTCAGGCCGGTGGGAGCAAGAGGACCGG
GCCCTCTCCCCTGTCATCCCCCTCATTCCTCGGGACAGCATCCCAGTCTTCCCAGATACC
AAACCTTATGGGGCCCTTGGCCTGGAGGTCCCTGGAAAGCTGCCTGTCACAACTTGGGAA
AAGGGCAAAGGAAGTGAGGTGTCAGTCATGCTCACAGTCTCTGCTGCTGCAGACAAGAAC
CTGAATGGCGTGATGGTGGCAGTGGCGGAGCTGCTGAGCATGAAGATCCCCAACTCCTAT
GAGGTGCTGTTCCCAGAGAGCCCCGCCCGGGGAGGCACTGAGCCAAAGAAGGGGGAAGCT
GAGGGTCCTGGTGGGAAGGAAAAGGGTCTGGAAGGCAAGAGCCCAGACACTGGCCCTGAT
TGGCTGAAGCAGTTTGATGCAGTGTTGGCTGGCTATACCCTGAAGAGGCAACTAGACATC
TTGAGCCTCCTGAAACAGGAGAGCCCCGCCCCAGAGCCACCCACTCAGCACAGGTATACC
TACAATGTCTCCAATCTGGATGTGCGACAGCTCTCGGCCCCACCTCCTGAAGAACCCTCC
CCGCCCCCTTCCCCCTTGGCACCTTCTCCTGCCAGTCCCCCTACTGAGCCCTTGGTTGAA
CTTCCCACCGAACCCTTGGCTGAGCCACCCGTCCCCTCACCTCTGCCACTGGCCTCATCC
CCTGAATCAGCCCGACCCAAGCCCCGTGCCCGGCCCCCTGAAGAAGGTGAAGATACCCGT
CCTCCTCGCCTCAAGAAATGGAAAGGAGTGCGCTGGAAGCGGCTTCGGCTGCTGCTGACC
ATCCAGAAGGGCAGTGGACGGCAGGAGGATGAGCGGGAAGTGGCAGAGTTTATGGAGCAG
CTTGGCACAGCCTTGCGACCTGACAAGGTACCGCGAGACATGCGTCGCTGCTGTTTCTGT
CATGAGGAGGGTGACGGGGCCACTGATGGGCCTGCCCGTCTGCTGAACCTGGACCTGGAC
CTGTGGGTGCACCTCAACTGTGCCCTTTGGTCCACGGAGGTGTATGAGACCCAGGGCGGA
GCACTGATGAATGTGGAGGTTGCCCTGCACCGAGGACTGCTAACCAAGTGCTCCCTGTGC
CAGCGAACTGGTGCCACCAGCAGCTGCAATCGCATGCGTTGCCCCAATGTCTACCATTTT
GGTTGTGCCATCCGCGCCAAGTGCATGTTCTTCAAGGACAAGACCATGCTGTGTCCAATG
CATAAGATCAAGGGGCCCTGTGAGCAAGAGCTGAGCTCTTTTGCTGTCTTCCGGCGGGTC
TACATTGAGCGGGACGAGGTGAAGCAAATCGCTAGCATCATTCAGCGGGGAGAACGGCTG
CACATGTTCCGTGTGGGGGGGCTTGTGTTCCACGCCATCGGACAGCTGCTGCCTCACCAG
ATGGCTGACTTTCATAGTGCCACTGCCCTCTATCCCGTGGGCTACGAGGCCACGCGCATC
TATTGGAGCCTCCGCACCAACAATCGTCGCTGCTGCTATCGCTGTTCTATTGGTGAGAAC
AACGGGCGGCCGGAGTTTGTAATCAAAGTCATCGAGCAGGGCCTGGAGGACCTGGTCTTC
ACTGACGCCTCTCCCCAGGCCGTGTGGAATCGCATCATTGAGCCTGTGGCTGCCATGAGA
AAAGAGGCTGACATGCTGCGACTCTTCCCTGAGTATCTGAAGGGCGAGGAGCTCTTTGGG
CTGACGGTGCATGCCGTGCTTCGCATAGCTGAATCACTGCCCGGGGTGGAGAGCTGTCAA
AACTATTTATTCCGCTATGGGCGCCACCCCCTTATGGAGCTGCCACTCATGATCAACCCC
ACTGGCTGTGCCCGATCAGAGCCTAAAATCCTCACACACTACAAACGGCCCCATACCCTG
AACAGCACCAGCATGTCTAAGGCATATCAGAGCACCTTCACAGGCGAGACCAACACCCCC
TACAGCAAGCAGTTTGTGCACTCCAAGTCATCTCAGTACCGGCGGCTGCGCACCGAATGG
AAGAACAACGTGTACCTGGCTCGCTCCCGTATCCAGGGCCTGGGGCTCTATGCAGCCAAG
GACCTAGAAAAGCACACAATGGTTATCGAGTACATTGGCACCATCATTCGGAACGAGGTG
GCCAACCGGCGGGAGAAAATCTACGAAGAGCAGAATCGAGGCATCTACATGTTCCGAATA
AACAATGAACATGTGATTGATGCTACGTTGACCGGCGGCCCTGCCAGGTACATTAACCAT
TCCTGTGCCCCTAACTGTGTGGCCGAAGTCGTGACATTTGACAAAGAGGACAAAATCATC
ATCATCTCCAGCCGGCGAATCCCCAAAGGAGAGGAGCTAACCTATGACTATCAGTTTGAT
TTTGAGGACGATCAGCACGAGATCCCCTGCCACTGTGGAGCCTGGAATTGTCGGAAATGG
ATGAACTAA
Enzyme 70 GenBank Gene ID AF010403 Link Image
Enzyme 70 GeneCard ID MLL2 Link Image
Enzyme 70 GenAtlas ID MLL2 Link Image
Enzyme 70 HGNC ID HGNC:7133 Link Image
Enzyme 70 Chromosome Location 1
Enzyme 70 Locus 12q12-q14
Enzyme 70 SNPs SNPJam Report Link Image
Enzyme 70 General References
  1. Prasad R, Zhadanov AB, Sedkov Y, Bullrich F, Druck T, Rallapalli R, Yano T, Alder H, Croce CM, Huebner K, Mazo A, Canaani E: Structure and expression pattern of human ALR, a novel gene with strong homology to ALL-1 involved in acute leukemia and to Drosophila trithorax. Oncogene. 1997 Jul 31;15(5):549-60. [PubMed Link Image]
  2. Goo YH, Sohn YC, Kim DH, Kim SW, Kang MJ, Jung DJ, Kwak E, Barlev NA, Berger SL, Chow VT, Roeder RG, Azorsa DO, Meltzer PS, Suh PG, Song EJ, Lee KJ, Lee YC, Lee JW: Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins. Mol Cell Biol. 2003 Jan;23(1):140-9. [PubMed Link Image]
  3. 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]
  4. 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]
  5. Mo R, Rao SM, Zhu YJ: Identification of the MLL2 complex as a coactivator for estrogen receptor alpha. J Biol Chem. 2006 Jun 9;281(23):15714-20. Epub 2006 Apr 7. [PubMed Link Image]
  6. Cho YW, Hong T, Hong S, Guo H, Yu H, Kim D, Guszczynski T, Dressler GR, Copeland TD, Kalkum M, Ge K: PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex. J Biol Chem. 2007 Jul 13;282(28):20395-406. Epub 2007 May 11. [PubMed Link Image]
  7. Demers C, Chaturvedi CP, Ranish JA, Juban G, Lai P, Morle F, Aebersold R, Dilworth FJ, Groudine M, Brand M: Activator-mediated recruitment of the MLL2 methyltransferase complex to the beta-globin locus. Mol Cell. 2007 Aug 17;27(4):573-84. [PubMed Link Image]
  8. Lan F, Bayliss PE, Rinn JL, Whetstine JR, Wang JK, Chen S, Iwase S, Alpatov R, Issaeva I, Canaani E, Roberts TM, Chang HY, Shi Y: A histone H3 lysine 27 demethylase regulates animal posterior development. Nature. 2007 Oct 11;449(7163):689-94. Epub 2007 Sep 12. [PubMed Link Image]
  9. Lee MG, Villa R, Trojer P, Norman J, Yan KP, Reinberg D, Di Croce L, Shiekhattar R: Demethylation of H3K27 regulates polycomb recruitment and H2A ubiquitination. Science. 2007 Oct 19;318(5849):447-50. Epub 2007 Aug 30. [PubMed Link Image]
  10. 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]
  11. 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]
  12. 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]
  13. 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]
  14. 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]
  15. 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 70 Metabolite References Not Available
Enzyme 71 [top]
Enzyme 71 ID 14762
Enzyme 71 Name Histone-lysine N-methyltransferase MLL4
Enzyme 71 Synonyms
  1. Lysine N-methyltransferase 2D
  2. KMT2D
  3. Myeloid/lymphoid or mixed-lineage leukemia protein 4
  4. Trithorax homolog 2
  5. WW domain-binding protein 7
  6. WBP-7
Enzyme 71 Gene Name WBP7
Enzyme 71 Protein Sequence >Histone-lysine N-methyltransferase MLL4
MAAAAGGGSCPGPGSARGRFPGRPRGAGGGGGRGGRGNGAERVRVALRRGGGATGPGGAE
PGEDTALLRLLGLRRGLRRLRRLWAGPRVQRGRGRGRGRGWGPSRGCVPEEESSDGESDE
EEFQGFHSDEDVAPSSLRSALRSQRGRAPRGRGRKHKTTPLPPPRLADVAPTPPKTPARK
RGEEGTERMVQALTELLRRAQAPQAPRSRACEPSTPRRSRGRPPGRPAGPCRRKQQAVVV
AEAAVTIPKPEPPPPVVPVKHQTGSWKCKEGPGPGPGTPRRGGQSSRGGRGGRGRGRGGG
LPFVIKFVSRAKKVKMGQLSLGLESGQGQGQHEESWQDVPQRRVGSGQGGSPCWKKQEQK
LDDEEEEKKEEEEKDKEGEEKEERAVAEEMMPAAEKEEAKLPPPPLTPPAPSPPPPLPPP
STSPPPPLCPPPPPPVSPPPLPSPPPPPAQEEQEESPPPVVPATCSRKRGRPPLTPSQRA
EREAARAGPEGTSPPTPTPSTATGGPPEDSPTVAPKSTTFLKNIRQFIMPVVSARSSRVI
KTPRRFMDEDPPKPPKVEVSPVLRPPITTSPPVPQEPAPVPSPPRAPTPPSTPVPLPEKR
RSILREPTFRWTSLTRELPPPPPAPPPPPAPSPPPAPATSSRRPLLLRAPQFTPSEAHLK
IYESVLTPPPLGAPEAPEPEPPPADDSPAEPEPRAVGRTNHLSLPRFAPVVTTPVKAEVS
PHGAPALSNGPQTQAQLLQPLQALQTQLLPQALPPPQPQLQPPPSPQQMPPLEKARIAGV
GSLPLSGVEEKMFSLLKRAKVQLFKIDQQQQQKVAASMPLSPGGQMEEVAGAVKQISDRG
PVRSEDESVEAKRERPSGPESPVQGPRIKHVCRHAAVALGQARAMVPEDVPRLSALPLRD
RQDLATEDTSSASETESVPSRSRRGKVEAAGPGGESEPTGSGGTLAHTPRRSLPSHHGKK
MRMARCGHCRGCLRVQDCGSCVNCLDKPKFGGPNTKKQCCVYRKCDKIEARKMERLAKKG
RTIVKTLLPWDSDESPEASPGPPGPRRGAGAGGPREEVVAHPGPEEQDSLLQRKSARRCV
KQRPSYDIFEDSDDSEPGGPPAPRRRTPRENELPLPEPEEQSRPRKPTLQPVLQLKARRR
LDKDALAPGPFASFPNGWTGKQKSPDGVHRVRVDFKEDCDLENVWLMGGLSVLTSVPGGP
PMVCLLCASKGLHELVFCQVCCDPFHPFCLEEAERPLPQHHDTWCCRRCKFCHVCGRKGR
GSKHLLECERCRHAYHPACLGPSYPTRATRKRRHWICSACVRCKSCGATPGKNWDVEWSG
DYSLCPRCTQLYEKGNYCPICTRCYEDNDYESKMMQCAQCDHWVHAKCEGLSDEDYEILS
GLPDSVLYTCGPCAGAAQPRWREALSGALQGGLRQVLQGLLSSKVVGPLLLCTQCGPDGK
QLHPGPCGLQAVSQRFEDGHYKSVHSFMEDMVGILMRHSEEGETPDRRAGGQMKGLLLKL
LESAFGWFDAHDPKYWRRSTRLPNGVLPNAVLPPSLDHVYAQWRQQEPETPESGQPPGDP
SAAFQGKDPAAFSHLEDPRQCALCLKYGDADSKEAGRLLYIGQNEWTHVNCAIWSAEVFE
ENDGSLKNVHAAVARGRQMRCELCLKPGATVGCCLSSCLSNFHFMCARASYCIFQDDKKV
FCQKHTDLLDGKEIVNPDGFDVLRRVYVDFEGINFKRKFLTGLEPDAINVLIGSIRIDSL
GTLSDLSDCEGRLFPIGYQCSRLYWSTVDARRRCWYRCRILEYRPWGPREEPAHLEAAEE
NQTIVHSPAPSSEPPGGEDPPLDTDVLVPGAPERHSPIQNLDPPLRPDSGSAPPPAPRSF
SGARIKVPNYSPSRRPLGGVSFGPLPSPGSPSSLTHHIPTVGDPDFPAPPRRSRRPSPLA
PRPPPSRWASPPLKTSPQLRVPPPTSVVTALTPTSGELAPPGPAPSPPPPEDLGPDFEDM
EVVSGLSAADLDFAASLLGTEPFQEEIVAAGAMGSSHGGPGDSSEEESSPTSRYIHFPVT
VVSAPGLAPSATPGAPRIEQLDGVDDGTDSEAEAVQQPRGQGTPPSGPGVVRAGVLGAAG
DRARPPEDLPSEIVDFVLKNLGGPGDGGAGPREESLPPAPPLANGSQPSQGLTASPADPT
RTFAWLPGAPGVRVLSLGPAPEPPKPATSKIILVNKLGQVFVKMAGEGEPVPPPVKQPPL
PPTISPTAPTSWTLPPGPLLGVLPVVGVVRPAPPPPPPPLTLVLSSGPASPPRQAIRVKR
VSTFSGRSPPAPPPYKAPRLDEDGEASEDTPQVPGLGSGGFSRVRMKTPTVRGVLDLDRP
GEPAGEESPGPLQERSPLLPLPEDGPPQVPDGPPDLLLESQWHHYSGEASSSEEEPPSPD
DKENQAPKRTGPHLRFEISSEDGFSVEAESLEGAWRTLIEKVQEARGHARLRHLSFSGMS
GARLLGIHHDAVIFLAEQLPGAQRCQHYKFRYHQQGEGQEEPPLNPHGAARAEVYLRKCT
FDMFNFLASQHRVLPEGATCDEEEDEVQLRSTRRATSLELPMAMRFRHLKKTSKEAVGVY
RSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKGIGCYMFRMDDFDVVD
ATMHGNAARFINHSCEPNCFSRVIHVEGQKHIVIFALRRILRGEELTYDYKFPIEDASNK
LPCNCGAKRCRRFLN
Enzyme 71 Number of Residues 2715
Enzyme 71 Molecular Weight 293512.1
Enzyme 71 Theoretical pI 8.26
Enzyme 71 GO Classification
Function
  • DNA binding
  • binding
  • catalytic activity
  • cation binding
  • histone methyltransferase activity (H3-K4 specific)
  • 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
  • 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
  • histone methyltransferase complex
  • intracellular membrane-bounded organelle
  • macromolecular complex
  • membrane-bounded organelle
  • methyltransferase complex
  • nucleus
  • organelle
  • protein complex
Enzyme 71 General Function Involved in DNA binding
Enzyme 71 Specific Function Histone methyltransferase. Methylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation
Enzyme 71 Pathways Not Available
Enzyme 71 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 71 Pfam Domain Function
Enzyme 71 Signals
  • None
Enzyme 71 Transmembrane Regions
  • None
Enzyme 71 Essentiality Not Available
Enzyme 71 GenBank ID Protein 7662046 Link Image
Enzyme 71 UniProtKB/Swiss-Prot ID Q9UMN6 Link Image
Enzyme 71 UniProtKB/Swiss-Prot Entry Name MLL4_HUMAN Link Image
Enzyme 71 PDB ID Not Available
Enzyme 71 Cellular Location Not Available
Enzyme 71 Gene Sequence >8148 bp
ATGGCGGCGGCGGCGGGCGGCGGCAGTTGCCCCGGGCCTGGCTCCGCGCGGGGCCGCTTC
CCGGGCCGGCCGCGGGGCGCCGGCGGGGGCGGGGGCCGCGGCGGACGGGGCAACGGGGCC
GAAAGAGTGCGGGTAGCTCTGCGGCGCGGCGGTGGCGCGACGGGGCCGGGCGGAGCCGAG
CCCGGGGAGGACACGGCCCTGCTCCGTTTGCTGGGGCTCCGCCGGGGCCTGCGCCGGCTC
CGCCGCCTGTGGGCCGGCCCGCGGGTCCAGCGGGGCCGGGGACGGGGTCGGGGCCGGGGC
TGGGGCCCGAGTCGAGGCTGCGTGCCGGAGGAGGAGAGCAGTGACGGGGAATCCGACGAG
GAGGAGTTTCAGGGTTTTCATTCAGATGAAGATGTGGCCCCCAGTTCCCTGCGCTCTGCG
CTCCGATCCCAGCGAGGTCGAGCGCCCCGAGGTCGGGGTCGCAAGCATAAGACGACCCCC
CTTCCTCCTCCTCGCCTAGCAGATGTGGCTCCTACCCCCCCAAAGACCCCTGCCCGGAAA
CGGGGTGAGGAAGGCACAGAACGGATGGTGCAGGCACTGACTGAACTTCTCCGGCGGGCC
CAGGCACCCCAAGCACCCCGGAGCCGGGCATGTGAGCCCTCCACCCCCCGGCGGTCTCGG
GGACGGCCCCCAGGACGGCCAGCAGGCCCCTGCAGGAGGAAGCAGCAAGCAGTAGTGGTG
GCAGAAGCAGCTGTGACAATCCCCAAACCTGAGCCCCCACCTCCTGTGGTTCCAGTGAAA
CATCAGACTGGCAGCTGGAAATGCAAGGAGGGGCCCGGTCCAGGACCTGGGACCCCCAGG
CGTGGAGGACAGTCAAGCCGTGGAGGCCGTGGAGGCAGGGGCCGCGGCCGAGGTGGTGGG
CTCCCCTTTGTGATCAAGTTTGTTTCAAGGGCCAAAAAAGTAAAGATGGGACAATTGTCC
TTGGGACTCGAATCAGGTCAAGGTCAAGGTCAACATGAGGAAAGTTGGCAGGATGTCCCC
CAAAGAAGAGTTGGATCTGGACAGGGAGGGAGCCCTTGCTGGAAAAAGCAGGAACAGAAG
CTGGATGACGAGGAAGAAGAGAAGAAAGAAGAAGAAGAAAAAGACAAGGAGGGAGAAGAG
AAGGAAGAAAGAGCTGTAGCTGAGGAGATGATGCCAGCTGCGGAAAAGGAAGAGGCAAAG
CTGCCACCACCGCCTCTGACTCCTCCAGCCCCTTCACCTCCTCCACCCCTCCCACCCCCT
TCGACATCTCCTCCACCCCCACTCTGCCCTCCACCACCACCCCCAGTGTCCCCACCACCT
CTACCATCCCCTCCACCGCCTCCTGCCCAAGAGGAGCAGGAGGAATCCCCTCCTCCTGTG
GTCCCAGCTACGTGCTCCAGGAAGAGGGGCCGGCCTCCCCTGACTCCCAGCCAGCGGGCG
GAGCGGGAAGCTGCTCGGGCAGGGCCAGAGGGCACCTCTCCTCCCACTCCAACCCCCAGC
ACCGCCACGGGAGGCCCTCCGGAAGACAGTCCCACCGTGGCCCCCAAAAGCACCACCTTC
CTGAAGAATATCCGGCAGTTTATTATGCCTGTGGTGAGTGCCCGCTCCTCCCGTGTCATC
AAGACACCCCGGCGATTTATGGATGAAGACCCCCCCAAACCCCCAAAGGTGGAGGTCTCA
CCTGTCCTGCGACCTCCCATTACCACCTCCCCACCTGTTCCCCAGGAGCCAGCACCAGTC
CCCTCTCCACCACGTGCCCCAACTCCTCCATCTACCCCAGTTCCACTCCCTGAGAAGAGA
CGGTCCATCCTAAGGGAACCCACATTTCGCTGGACCTCACTGACCCGGGAGCTGCCCCCT
CCTCCCCCAGCCCCTCCACCTCCCCCGGCCCCCTCCCCACCCCCTGCTCCTGCCACCTCC
TCCCGGAGGCCCCTACTCCTTCGGGCCCCTCAGTTTACCCCAAGCGAAGCCCACCTGAAG
ATCTACGAATCGGTGCTTACTCCTCCTCCTCTTGGGGCTCCTGAAGCCCCTGAGCCAGAG
CCTCCTCCTGCCGATGACTCTCCAGCTGAGCCTGAGCCTCGGGCAGTGGGCCGCACCAAC
CACCTCAGCCTGCCTCGATTCGCCCCTGTGGTCACCACTCCTGTTAAGGCCGAGGTGTCC
CCTCACGGGGCTCCAGCTCTGAGCAACGGGCCACAGACACAGGCTCAGCTACTGCAGCCC
CTGCAGGCCTTGCAAACCCAGCTCCTGCCCCAGGCACTACCGCCACCACAGCCACAGCTG
CAGCCACCGCCGTCACCACAGCAGATGCCTCCCCTGGAAAAAGCCCGGATTGCGGGCGTG
GGTTCCTTGCCGCTGTCTGGGGTAGAGGAGAAGATGTTCAGCCTCCTCAAGAGAGCCAAA
GTGCAGCTATTCAAGATCGATCAGCAGCAGCAGCAGAAGGTGGCAGCTTCCATGCCGCTG
AGCCCTGGAGGGCAGATGGAGGAGGTGGCCGGGGCTGTCAAGCAGATCTCCGACAGAGGC
CCTGTCCGGTCTGAAGATGAGTCGGTGGAAGCTAAGAGAGAGCGGCCCTCAGGTCCCGAG
TCCCCTGTGCAAGGTCCCCGCATCAAACATGTCTGCCGTCATGCTGCTGTGGCCCTGGGT
CAGGCCCGGGCCATGGTGCCTGAAGATGTCCCTCGCCTCAGTGCCCTCCCTCTCCGGGAT
CGGCAGGACCTCGCCACAGAGGATACATCATCGGCGTCCGAGACTGAGAGTGTCCCGTCA
CGGTCCCGGCGGGGAAAGGTGGAGGCAGCAGGCCCTGGGGGAGAATCAGAGCCCACAGGT
TCTGGAGGGACCCTGGCCCACACACCCCGGCGCTCACTGCCCTCCCATCACGGCAAGAAG
ATGCGCATGGCTCGATGTGGACACTGTCGGGGCTGCCTACGTGTGCAGGACTGTGGGTCC
TGTGTCAACTGCCTAGACAAGCCCAAGTTTGGGGGCCCTAACACCAAGAAGCAGTGCTGT
GTATACCGGAAGTGTGACAAAATAGAGGCTCGGAAGATGGAACGACTGGCTAAAAAAGGC
CGGACGATAGTGAAGACGCTGTTGCCCTGGGATTCCGATGAATCTCCTGAGGCCTCCCCT
GGTCCTCCAGGCCCACGCCGGGGGGCGGGAGCTGGGGGGCCCCGGGAGGAGGTGGTGGCC
CACCCAGGGCCCGAGGAGCAGGACTCCCTCCTGCAGCGCAAGTCAGCTCGGCGCTGCGTC
AAACAGCGACCCTCCTATGATATCTTCGAGGATTCGGATGACTCGGAGCCCGGGGGCCCC
CCTGCTCCTCGGCGTCGGACCCCCCGAGAAAATGAGCTGCCACTGCCAGAACCTGAGGAG
CAGAGCCGGCCCCGCAAACCTACCCTGCAGCCTGTGTTGCAGCTCAAGGCCCGAAGGCGC
CTGGACAAGGATGCTTTGGCCCCTGGCCCCTTTGCTTCTTTTCCCAATGGCTGGACTGGA
AAGCAGAAGTCTCCCGATGGTGTGCACCGCGTCCGTGTGGATTTTAAGGAGGATTGTGAT
TTAGAGAACGTGTGGCTGATGGGGGGCCTGAGTGTGCTCACCTCTGTGCCAGGGGGCCCC
CCGATGGTGTGCTTGCTGTGTGCCAGCAAAGGACTCCACGAGCTGGTGTTCTGTCAAGTC
TGCTGTGACCCATTCCACCCATTCTGCCTGGAGGAGGCCGAGCGGCCCCTGCCCCAGCAT
CACGACACCTGGTGCTGCCGTCGCTGCAAATTCTGCCACGTCTGTGGACGCAAAGGTCGT
GGATCCAAGCACCTCCTGGAGTGCGAGCGCTGCCGCCATGCATACCACCCGGCCTGTCTG
GGGCCCAGCTATCCAACCCGGGCCACGCGCAAACGGCGCCACTGGATCTGTTCAGCCTGT
GTGCGCTGTAAGAGCTGTGGGGCAACTCCAGGCAAGAACTGGGACGTCGAGTGGTCTGGA
GATTACAGCCTCTGCCCCAGGTGCACCCAGCTATATGAGAAAGGAAACTACTGCCCGATC
TGTACACGCTGCTATGAAGACAACGACTATGAGAGCAAGATGATGCAGTGCGCACAGTGC
GATCACTGGGTGCATGCCAAGTGCGAGGGGCTCTCAGATGAAGACTACGAGATCCTTTCA
GGACTGCCAGACTCGGTGCTGTACACCTGCGGACCGTGTGCTGGGGCAGCGCAGCCCCGC
TGGCGAGAGGCCCTGAGCGGGGCCCTCCAGGGGGGCCTGCGCCAGGTGCTCCAGGGCCTG
CTGAGCTCCAAGGTGGTGGGCCCACTGCTGCTCTGCACCCAGTGTGGGCCAGATGGGAAG
CAACTGCACCCAGGACCCTGCGGCCTGCAAGCTGTGAGTCAGCGCTTCGAGGATGGCCAC
TACAAGTCTGTGCACAGCTTCATGGAGGACATGGTGGGCATCCTCATGCGGCACTCGGAG
GAGGGAGAGACCCCGGACCGCCGGGCTGGAGGCCAGATGAAGGGGCTCCTGCTGAAGCTG
CTAGAATCTGCGTTCGGCTGGTTCGACGCCCACGACCCCAAGTACTGGCGACGGAGTACC
CGGCTGCCAAACGGAGTCCTTCCCAATGCGGTGTTGCCCCCATCCCTGGATCATGTCTAT
GCGCAGTGGAGACAGCAGGAACCAGAGACCCCAGAATCAGGGCAGCCTCCAGGGGATCCC
TCAGCAGCATTCCAGGGCAAGGATCCGGCTGCCTTCTCACACCTGGAGGACCCCCGTCAG
TGTGCACTCTGCCTCAAATACGGGGATGCAGACTCCAAGGAGGCGGGGCGGCTCTTGTAC
ATCGGGCAGAACGAGTGGACACACGTCAACTGTGCCATCTGGTCGGCGGAAGTCTTCGAG
GAGAACGACGGCTCCCTCAAGAATGTGCATGCTGCTGTGGCCCGAGGGAGGCAGATGCGC
TGCGAGCTCTGCCTGAAGCCTGGCGCCACGGTGGGCTGCTGCCTGTCCTCCTGCCTCAGC
AACTTCCACTTCATGTGTGCCCGGGCCAGCTACTGCATCTTCCAGGATGACAAGAAAGTC
TTCTGCCAGAAACACACTGATCTCCTGGATGGCAAGGAAATTGTGAACCCCGATGGTTTT
GATGTTCTCCGCCGAGTCTATGTGGACTTCGAGGGCATCAACTTCAAGCGGAAGTTCTTG
ACGGGGCTTGAACCCGATGCCATCAACGTGCTCATTGGTTCCATCCGCATTGACTCCCTG
GGTACTCTGTCTGATCTCTCGGACTGCGAGGGACGGCTCTTCCCCATTGGCTACCAGTGC
TCCCGTCTGTACTGGAGCACAGTGGATGCTCGGAGGCGCTGCTGGTATCGGTGCCGAATT
CTGGAGTATCGGCCATGGGGGCCGAGGGAAGAGCCAGCTCACCTGGAGGCTGCAGAGGAG
AACCAGACCATTGTGCACAGCCCCGCCCCTTCCTCAGAGCCCCCAGGTGGTGAGGACCCC
CCACTGGACACAGATGTTCTTGTCCCTGGAGCTCCTGAGCGCCACTCGCCCATTCAGAAC
CTGGACCCTCCACTGCGGCCAGATTCAGGCAGCGCCCCTCCTCCAGCCCCCCGTTCTTTT
TCGGGGGCTCGAATCAAAGTGCCCAACTACTCGCCATCCCGGAGGCCCTTGGGGGGTGTC
TCCTTTGGCCCCCTGCCCTCCCCTGGAAGTCCATCTTCACTGACCCACCACATCCCCACA
GTGGGAGACCCGGACTTCCCAGCTCCCCCCAGACGTTCCCGTCGTCCCAGCCCTTTGGCT
CCCAGGCCGCCTCCATCACGGTGGGCCTCCCCTCCTCTAAAAACCTCCCCTCAGCTCAGG
GTGCCCCCTCCTACCTCAGTCGTCACAGCCCTCACACCTACCTCAGGGGAGCTGGCTCCC
CCTGGCCCGGCCCCATCTCCACCACCCCCTGAAGACCTGGGCCCAGACTTCGAGGACATG
GAGGTGGTGTCAGGACTGAGTGCTGCTGACCTGGACTTCGCGGCCAGCCTGCTGGGGACT
GAGCCCTTCCAGGAAGAGATTGTAGCCGCTGGGGCCATGGGGAGCAGCCACGGGGGCCCG
GGGGACAGCTCCGAGGAGGAGTCCAGCCCCACCTCCCGCTACATCCACTTCCCTGTGACT
GTGGTGTCCGCCCCTGGTCTGGCCCCCAGCGCTACCCCTGGAGCCCCCCGCATTGAACAG
CTGGACGGCGTGGACGACGGCACTGACAGTGAGGCTGAGGCGGTGCAGCAGCCTCGGGGC
CAGGGCACGCCTCCTTCGGGGCCAGGAGTAGTCCGGGCAGGGGTCCTTGGGGCTGCAGGG
GACAGGGCCCGGCCTCCTGAGGACCTGCCATCGGAAATTGTGGATTTTGTGTTGAAGAAC
CTAGGGGGTCCTGGGGATGGAGGTGCTGGCCCTAGAGAGGAGTCACTCCCCCCGGCGCCT
CCCCTGGCTAATGGCAGCCAGCCCTCCCAAGGCCTGACCGCCAGCCCAGCTGACCCCACC
CGCACATTTGCCTGGCTCCCAGGGGCCCCAGGGGTCCGGGTGTTAAGCCTTGGCCCTGCC
CCTGAGCCCCCCAAACCCGCCACATCCAAAATCATACTTGTCAACAAGCTGGGGCAAGTA
TTTGTGAAGATGGCTGGGGAGGGTGAACCTGTCCCACCCCCAGTGAAGCAGCCACCTTTG
CCCCCCACCATTTCCCCCACGGCTCCCACCTCCTGGACTCTGCCCCCAGGCCCCCTCCTC
GGCGTGCTGCCCGTGGTCGGAGTGGTCCGCCCTGCCCCGCCCCCGCCACCCCCTCCCCTG
ACGCTGGTGCTGAGCAGTGGGCCAGCCAGCCCGCCCCGCCAGGCCATCCGCGTCAAGAGG
GTGTCCACTTTCTCCGGCCGGTCCCCGCCAGCACCTCCCCCATACAAAGCCCCCCGGCTG
GATGAAGATGGAGAGGCCTCAGAGGATACCCCTCAGGTTCCAGGGCTTGGCAGTGGCGGG
TTTAGCCGTGTGAGGATGAAAACCCCCACAGTGCGTGGGGTCCTTGACCTGGATCGGCCT
GGGGAGCCCGCTGGGGAAGAAAGTCCTGGGCCCCTCCAGGAACGGTCCCCTTTGCTGCCA
CTTCCGGAAGATGGTCCTCCCCAGGTCCCCGATGGTCCCCCAGACCTGCTGCTTGAGTCC
CAGTGGCACCACTATTCAGGTGAGGCTTCGAGCTCTGAGGAAGAGCCTCCATCCCCAGAT
GATAAAGAGAACCAGGCCCCAAAACGGACTGGCCCACATCTGCGCTTCGAGATCAGCAGT
GAGGATGGGTTCAGCGTTGAGGCAGAGAGCTTGGAGGGGGCGTGGAGAACTCTGATCGAG
AAAGTGCAAGAGGCCCGAGGGCATGCCCGACTCAGACATCTCTCCTTTAGTGGAATGAGT
GGGGCGAGACTCCTGGGCATCCACCATGATGCTGTCATCTTCCTGGCCGAGCAGCTCCCC
GGAGCCCAGCGTTGCCAGCACTATAAGTTCCGTTACCACCAGCAGGGAGAGGGCCAGGAG
GAGCCGCCCCTGAATCCCCATGGGGCTGCTCGGGCAGAGGTCTATCTCCGGAAGTGCACC
TTTGACATGTTCAACTTCCTGGCCTCCCAGCACCGGGTGCTCCCTGAGGGGGCCACCTGT
GATGAGGAAGAGGATGAGGTGCAGCTCAGGTCAACCAGACGTGCCACCAGCCTGGAGCTG
CCCATGGCCATGCGTTTTCGTCACCTTAAGAAGACGTCCAAAGAAGCTGTGGGTGTCTAC
AGATCAGCCATCCACGGGCGAGGCCTGTTCTGTAAGCGCAACATCGACGCGGGGGAGATG
GTCATCGAGTACTCTGGCATTGTCATCCGCTCGGTGTTGACTGACAAGCGGGAGAAGTTC
TACGATGGGAAGGGCATCGGGTGCTATATGTTCCGCATGGATGACTTTGATGTAGTGGAC
GCCACGATGCATGGCAATGCCGCCCGCTTCATCAACCACTCCTGTGAGCCCAACTGCTTC
TCTCGGGTCATCCACGTGGAGGGCCAGAAACACATTGTTATCTTCGCCCTGCGCCGCATC
CTGCGTGGTGAGGAGCTCACCTACGACTACAAGTTCCCCATCGAGGATGCCAGCAACAAG
CTGCCCTGCAACTGTGGCGCCAAGCGCTGCCGTCGGTTCCTTAACTGA
Enzyme 71 GenBank Gene ID NM_014727.1 Link Image
Enzyme 71 GeneCard ID WBP7 Link Image
Enzyme 71 GenAtlas ID Not Available
Enzyme 71 HGNC ID Not Available
Enzyme 71 Chromosome Location Not Available
Enzyme 71 Locus Not Available
Enzyme 71 SNPs SNPJam Report Link Image
Enzyme 71 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. Huntsman DG, Chin SF, Muleris M, Batley SJ, Collins VP, Wiedemann LM, Aparicio S, Caldas C: MLL2, the second human homolog of the Drosophila trithorax gene, maps to 19q13.1 and is amplified in solid tumor cell lines. Oncogene. 1999 Dec 23;18(56):7975-84. [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. 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. FitzGerald KT, Diaz MO: MLL2: A new mammalian member of the trx/MLL family of genes. Genomics. 1999 Jul 15;59(2):187-92. [PubMed Link Image]
  6. 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]
  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. De Santa F, Totaro MG, Prosperini E, Notarbartolo S, Testa G, Natoli G: The histone H3 lysine-27 demethylase Jmjd3 links inflammation to inhibition of polycomb-mediated gene silencing. Cell. 2007 Sep 21;130(6):1083-94. Epub 2007 Sep 6. [PubMed Link Image]
  9. Cho YW, Hong T, Hong S, Guo H, Yu H, Kim D, Guszczynski T, Dressler GR, Copeland TD, Kalkum M, Ge K: PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex. J Biol Chem. 2007 Jul 13;282(28):20395-406. Epub 2007 May 11. [PubMed Link Image]
  10. 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]
  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]
Enzyme 71 Metabolite References Not Available
Enzyme 72 [top]
Enzyme 72 ID 14763
Enzyme 72 Name Histone-lysine N-methyltransferase MLL5
Enzyme 72 Synonyms
  1. Lysine N-methyltransferase 2E
  2. KMT2E
  3. Myeloid/lymphoid or mixed-lineage leukemia protein 5
Enzyme 72 Gene Name MLL5
Enzyme 72 Protein Sequence >Histone-lysine N-methyltransferase MLL5
MSIVIPLGVDTAETSYLEMAAGSEPESVEASPVVVEKSNSYPHQLYTSSSHHSHSYIGLP
YADHNYGARPPPTPPASPPPSVLISKNEVGIFTTPNFDETSSATTISTSEDGSYGTDVTR
CICGFTHDDGYMICCDKCSVWQHIDCMGIDRQHIPDTYLCERCQPRNLDKERAVLLQRRK
RENMSDGDTSATESGDEVPVELYTAFQHTPTSITLTASRVSKVNDKRRKKSGEKEQHISK
CKKAFREGSRKSSRVKGSAPEIDPSSDGSNFGWETKIKAWMDRYEEANNNQYSEGVQREA
QRIALRLGNGNDKKEMNKSDLNTNNLLFKPPVESHIQKNKKILKSAKDLPPDALIIEYRG
KFMLREQFEANGYFFKRPYPFVLFYSKFHGLEMCVDARTFGNEARFIRRSCTPNAEVRHE
IQDGTIHLYIYSIHSIPKGTEITIAFDFDYGNCKYKVDCACLKENPECPVLKRSSESMEN
INSGYETRRKKGKKDKDISKEKDTQNQNITLDCEGTTNKMKSPETKQRKLSPLRLSVSNN
QEPDFIDDIEEKTPISNEVEMESEEQIAERKRKMTREERKMEAILQAFARLEKREKRREQ
ALERISTAKTEVKTECKDTQIVSDAEVIQEQAKEENASKPTPAKVNRTKQRKSFSRSRTH
IGQQRRRHRTVSMCSDIQPSSPDIEVTSQQNDIENTVLTIEPETETALAEIITETEVPAL
NKCPTKYPKTKKHLVNEWLSEKNEKTGKPSDGLSERPLRITTDPEVLATQLNSLPGLTYS
PHVYSTPKHYIRFTSPFLSEKRRRKEPTENISGSCKKRWLKQALEEENSAILHRFNSPCQ
ERSRSPAVNGENKSPLLLNDSCSLPDLTTPLKKRRFYQLLDSVYSETSTPTPSPYATPTH
TDITPMDPSFATPPRIKSDDETCRNGYKPIYSPVTPVTPGTPGNTMHFENISSPESSPEI
KRRTYSQEGYDRSSTMLTLGPFRNSNLTELGLQEIKTIGYTSPRSRTEVNRQCPGEKEPV
SDLQLGLDAVEPTALHKTLETPAHDRAEPNSQLDSTHSGRGTMYSSWVKSPDRTGVNFSV
NSNLRDLTPSHQLEVGGGFRISESKCLMQDDTRGMFMETTVFCTSEDGLVSGFGRTVNDN
LIDGNCTPQNPPQKKKVSLLEYRKRQREARKSGSKTENFPLISVSPHASGSLSNNGDGCA
SSNDNGEQVDHTASLPLPTPATVYNATSEETSNNCPVKDATASEKNEPEVQWTASTSVEQ
VRERSYQRALLLSDHRKDKDSGGESPCVSCSPSHVQSSPSSHSNHIPQLQAKGPVPSFSE
LMEDPDPENPEPTTTNECPSPDTSQNTCKSPPKMSKPGSPGSVIPAQAHGKIFTKPDPQW
DSTVSASEAENGVHLKTELQQKQLSNNNQALSKNHPPQTHVRNSSEQLSQKLPSVPTKLH
CPPSPHLENPPKSSTPHTPVQHGYLSPKPPSQQLGSPYRPHHSQSPQVGTPQREPQRNFY
PAAQNLPANTQQATSGTLFTQTPSGQSSATYSQFNQQSLNSTAPPPPPPPPPSSSYYQNQ
QPSANFQNYNQLKGSLSQQTVFTSGPNQALPGTTSQQTVPGHHVTPGHFLPSQNPTIHHQ
TAAAVVPPPPPPPPAPGPHLVQQPNSHQQHSVAHVVGPVHAVTPGSHIHSQTAGHHLPPP
PPPPGPAPHHHPPPHPSTGLQGLQAQHQHVVNSAPPPPPPPPPSSVLASGHHTTSAQALH
HPPHQGPPLFPSSAHPTVPPYPSQATHHTTLGPGPQHQPSGTGPHCPLPVTGPHLQPQGP
NSIPTPTASGFCPHPGSVALPHGVQGPQQASPVPGQIPIHRAQVPPTFQNNYHGSGWH
Enzyme 72 Number of Residues 1858
Enzyme 72 Molecular Weight 204963.6
Enzyme 72 Theoretical pI 7.63
Enzyme 72 GO Classification
Function
  • binding
  • cation binding
  • ion binding
  • metal ion binding
  • protein binding
  • transition metal ion binding
  • zinc ion binding
Process
Component
Enzyme 72 General Function Involved in zinc ion binding
Enzyme 72 Specific Function Histone methyltransferase that specifically mono- and dimethylates 'Lys-4' of histone H3 (H3K4me1 and H3K4me2). H3 'Lys- 4' methylation represents a specific tag for epigenetic transcriptional activation. Key regulator of hematopoiesis involved in terminal myeloid differentiation and in the regulation of hematopoietic stem cell (HSCs) self-renewal by a mechanism that involves DNA methylation. Plays an essential role in retinoic- acid-induced granulopoiesis by acting as a coactivator of RAR- alpha (RARA) in target gene promoters. Also acts as an important cell cycle regulator, participating in cell cycle regulatory network machinery at multiple cell cycle stages. Required to suppress inappropriate expression of S-phase-promoting genes and maintain expression of determination genes in quiescent cells. Overexpression inhibits cell cycle progression, while knockdown induces cell cycle arrest at both the G1 and G2/M phases
Enzyme 72 Pathways Not Available
Enzyme 72 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 72 Pfam Domain Function
Enzyme 72 Signals
  • None
Enzyme 72 Transmembrane Regions
  • None
Enzyme 72 Essentiality Not Available
Enzyme 72 GenBank ID Protein 91199543 Link Image
Enzyme 72 UniProtKB/Swiss-Prot ID Q8IZD2 Link Image
Enzyme 72 UniProtKB/Swiss-Prot Entry Name MLL5_HUMAN Link Image
Enzyme 72 PDB ID Not Available
Enzyme 72 Cellular Location Not Available
Enzyme 72 Gene Sequence >5577 bp
ATGAGCATAGTGATCCCATTGGGGGTTGATACAGCAGAGACGTCATACTTGGAAATGGCT
GCAGGTTCAGAACCAGAATCCGTAGAAGCTAGCCCTGTGGTAGTTGAGAAATCCAACAGT
TATCCCCACCAGTTATATACCAGCAGCTCACATCATTCACACAGTTACATTGGTTTGCCC
TATGCGGACCATAATTATGGTGCTCGTCCTCCTCCGACACCTCCGGCTTCCCCTCCTCCA
TCAGTCCTTATTAGCAAAAATGAAGTAGGCATATTTACCACTCCTAATTTTGATGAAACT
TCCAGTGCTACTACAATCAGCACATCTGAGGATGGAAGTTATGGTACTGATGTAACCAGG
TGCATATGTGGTTTTACACATGATGATGGATACATGATCTGTTGTGACAAATGCAGCGTT
TGGCAACATATTGACTGCATGGGGATTGATAGGCAGCATATTCCTGATACATATCTATGT
GAACGTTGTCAGCCTAGGAATTTGGATAAAGAGAGGGCAGTGCTACTACAACGCCGGAAA
AGGGAAAATATGTCAGATGGTGATACCAGTGCAACTGAGAGTGGTGATGAGGTTCCTGTG
GAATTATATACTGCATTTCAGCATACTCCAACATCAATTACTTTAACTGCTTCAAGAGTT
TCCAAAGTTAATGATAAAAGAAGGAAAAAAAGCGGGGAGAAAGAACAACACATTTCAAAA
TGTAAAAAGGCATTTCGTGAAGGATCTAGGAAGTCATCAAGAGTTAAGGGTTCAGCTCCA
GAGATTGATCCTTCATCTGATGGTTCAAATTTTGGATGGGAGACAAAGATCAAAGCATGG
ATGGATCGATATGAAGAAGCAAATAACAACCAGTACAGTGAGGGTGTTCAGAGGGAGGCA
CAAAGAATAGCTCTGAGATTAGGCAATGGAAATGACAAAAAAGAGATGAATAAATCCGAT
TTGAATACCAACAATTTGCTCTTCAAACCTCCTGTAGAGAGCCATATACAAAAGAATAAG
AAAATTCTTAAATCTGCAAAAGATTTGCCTCCTGATGCACTTATCATTGAATACAGAGGG
AAGTTTATGCTGAGAGAACAGTTTGAAGCAAATGGGTATTTCTTTAAAAGACCATACCCT
TTTGTGTTATTCTACTCTAAATTTCATGGGCTAGAAATGTGTGTTGATGCAAGGACTTTT
GGGAATGAGGCTCGATTCATCAGGCGGTCTTGTACACCCAATGCAGAGGTGAGGCATGAA
ATTCAAGATGGAACCATACATCTTTATATTTATTCTATACACAGTATTCCAAAGGGAACT
GAAATTACTATTGCCTTTGATTTTGACTATGGAAATTGTAAGTACAAGGTGGACTGTGCA
TGCCTCAAAGAAAACCCAGAGTGCCCTGTTCTAAAACGTAGTTCTGAATCCATGGAAAAT
ATCAATAGTGGTTATGAGACCAGACGGAAAAAAGGAAAAAAAGACAAAGATATTTCAAAA
GAAAAAGATACACAAAATCAGAATATTACTTTGGATTGTGAAGGAACGACCAACAAAATG
AAGAGCCCAGAAACTAAACAAAGAAAGCTTTCTCCACTGAGACTATCAGTATCAAATAAT
CAGGAACCAGATTTTATTGATGATATAGAAGAAAAAACTCCTATTAGTAATGAAGTAGAA
ATGGAATCAGAGGAGCAGATTGCAGAAAGGAAAAGGAAGATGACAAGAGAAGAAAGAAAA
ATGGAAGCAATTTTGCAAGCTTTTGCCAGACTTGAAAAGAGAGAGAAAAGAAGAGAACAA
GCTTTGGAAAGGATCAGCACAGCCAAAACTGAAGTTAAAACTGAATGTAAAGATACACAG
ATTGTCAGTGATGCTGAAGTTATTCAGGAACAAGCAAAAGAAGAAAATGCTAGCAAGCCA
ACCCCTGCCAAAGTAAATAGAACTAAACAGAGAAAAAGTTTTTCTCGGAGTAGGACTCAC
ATTGGACAGCAGCGTCGGAGACACAGAACTGTCAGCATGTGTTCAGATATCCAGCCATCT
TCTCCTGATATAGAAGTTACTTCACAACAAAATGATATTGAAAATACTGTACTTACAATA
GAACCAGAAACTGAAACTGCACTAGCAGAAATAATTACTGAAACTGAAGTTCCAGCACTT
AATAAATGTCCTACCAAGTACCCCAAAACAAAGAAGCACTTGGTTAATGAATGGTTAAGT
GAGAAGAATGAGAAGACAGGAAAACCTTCAGATGGCCTTTCAGAAAGGCCTCTACGCATA
ACTACAGATCCTGAAGTGTTAGCTACACAACTCAATTCTTTACCAGGTCTCACTTACAGC
CCCCATGTATACTCCACTCCTAAGCATTATATTAGATTTACTTCACCATTCCTTTCAGAA
AAAAGGAGAAGAAAAGAACCTACTGAAAACATTTCTGGTTCATGCAAGAAGCGATGGTTG
AAACAAGCTCTGGAAGAAGAAAATTCAGCAATTTTACATAGATTTAATTCACCCTGTCAA
GAAAGATCCAGAAGTCCTGCAGTCAATGGTGAAAATAAAAGTCCACTACTATTAAATGAC
AGCTGTTCCCTTCCAGATTTAACTACACCACTAAAAAAACGAAGATTTTATCAGTTGCTA
GATTCGGTTTACTCAGAAACCTCCACACCTACTCCTTCCCCGTATGCTACACCAACTCAC
ACCGATATTACTCCTATGGACCCATCTTTTGCCACGCCTCCACGGATAAAATCAGATGAT
GAAACTTGTAGAAATGGTTATAAACCCATATATTCACCAGTTACCCCAGTAACTCCTGGT
ACACCAGGAAATACCATGCACTTTGAGAATATTTCTTCCCCAGAAAGTTCTCCAGAAATA
AAGAGACGCACTTATAGTCAAGAGGGATATGACAGATCTTCAACCATGTTAACATTGGGG
CCTTTTAGAAATTCTAATTTAACTGAACTGGGTCTGCAAGAAATAAAGACTATTGGTTAT
ACGAGCCCTAGGAGTAGGACTGAAGTCAACAGGCAGTGTCCTGGAGAAAAGGAACCTGTG
TCAGACCTTCAGCTAGGACTCGATGCAGTTGAGCCAACTGCCCTACATAAAACCCTGGAA
ACGCCTGCACATGACAGGGCTGAGCCCAACAGCCAACTGGACTCGACTCACTCTGGACGG
GGCACAATGTATTCTTCCTGGGTAAAGAGCCCTGACAGAACAGGAGTTAACTTCTCAGTG
AACTCCAACTTGAGGGACCTGACACCCTCGCATCAGTTGGAGGTTGGAGGAGGCTTCCGA
ATAAGTGAGTCAAAGTGCCTGATGCAGGATGATACTAGAGGCATGTTTATGGAAACAACT
GTGTTTTGTACTTCCGAAGATGGGCTTGTATCTGGTTTCGGACGGACTGTTAATGACAAT
TTGATCGACGGGAATTGCACACCCCAGAATCCACCACAAAAGAAAAAGGTTTCTCTATTA
GAATACCGTAAGAGACAACGTGAAGCTAGGAAAAGTGGCTCTAAGACAGAGAACTTTCCA
CTCATTAGTGTATCACCCCATGCAAGTGGAAGCTTGAGCAACAATGGTGATGGCTGTGCC
AGCAGTAATGACAATGGGGAGCAGGTGGACCACACTGCTAGCCTACCTTTACCAACACCA
GCTACAGTTTATAATGCCACTTCTGAAGAAACTAGCAATAACTGCCCTGTTAAGGATGCT
ACTGCTAGTGAGAAGAATGAACCAGAAGTTCAATGGACTGCCTCAACTTCAGTGGAACAA
GTCAGAGAAAGGAGTTATCAGAGAGCTTTACTTCTCAGTGATCACCGAAAAGATAAAGAT
AGTGGGGGAGAATCACCATGTGTCTCATGTTCACCGAGTCATGTTCAGTCTTCACCTTCA
TCTCATTCAAATCACATACCCCAGTTGCAAGCTAAGGGCCCAGTCCCTTCTTTCAGTGAA
CTTATGGAAGACCCTGATCCTGAAAATCCAGAACCCACAACTACGAATGAATGTCCATCC
CCAGATACTTCTCAAAATACTTGTAAAAGTCCTCCAAAAATGAGCAAGCCTGGTTCACCT
GGATCTGTAATTCCTGCTCAAGCACACGGGAAAATATTCACAAAACCAGATCCCCAATGG
GACTCCACAGTTAGTGCATCCGAAGCTGAAAATGGTGTTCACCTAAAAACAGAGCTCCAA
CAAAAACAGCTATCAAATAACAACCAAGCACTTTCAAAGAATCATCCTCCTCAGACACAC
GTTCGTAATTCATCTGAGCAACTTTCACAAAAGCTGCCTTCTGTGCCAACAAAGTTGCAC
TGTCCTCCATCACCTCACCTAGAAAATCCTCCAAAGTCATCCACGCCTCACACACCTGTA
CAGCATGGTTATCTTTCACCAAAGCCTCCTTCACAGCAGTTAGGATCTCCCTACAGGCCT
CATCATTCACAGTCACCTCAAGTTGGAACACCTCAGCGAGAGCCTCAAAGAAACTTTTAT
CCAGCAGCACAGAACCTTCCAGCCAATACTCAGCAGGCAACTTCTGGAACATTATTTACA
CAGACACCCTCAGGACAATCTTCAGCAACATACAGTCAGTTTAACCAACAAAGTCTGAAC
AGCACGGCACCACCCCCTCCACCTCCTCCACCTCCTTCTTCGTCTTACTATCAAAACCAG
CAGCCCTCTGCAAACTTTCAGAATTATAATCAGCTCAAAGGTAGTCTTTCTCAACAAACT
GTGTTTACATCAGGACCAAATCAAGCACTTCCTGGCACCACAAGCCAGCAAACAGTTCCA
GGACACCACGTGACTCCAGGGCATTTTTTGCCCTCTCAGAACCCTACCATTCACCATCAA
ACTGCTGCTGCCGTAGTCCCCCCTCCTCCTCCACCACCACCTGCTCCAGGACCGCACCTT
GTACAACAGCCGAATTCCCATCAGCAACACTCTGTAGCACATGTAGTAGGGCCTGTTCAT
GCGGTCACCCCTGGGTCGCATATTCATTCTCAAACTGCTGGACACCACTTACCCCCACCC
CCACCCCCTCCTGGTCCTGCCCCTCATCACCATCCACCACCCCATCCATCCACAGGACTC
CAAGGTCTACAAGCACAACACCAGCATGTTGTAAATTCAGCACCCCCACCACCCCCTCCG
CCGCCACCTTCCAGTGTTTTGGCTTCTGGGCATCATACCACATCAGCTCAAGCCTTACAC
CACCCACCTCATCAAGGACCTCCACTTTTTCCTTCGAGTGCTCATCCAACTGTACCACCG
TATCCCTCACAAGCTACACATCATACCACTTTGGGACCGGGACCCCAGCACCAGCCTTCT
GGAACAGGGCCACATTGTCCATTACCTGTCACAGGTCCTCATCTCCAGCCCCAAGGACCA
AACAGTATTCCAACACCTACTGCTTCAGGGTTCTGTCCTCATCCTGGCTCTGTGGCCCTG
CCACATGGGGTTCAAGGACCTCAGCAGGCATCTCCAGTGCCTGGACAGATTCCAATTCAC
AGAGCACAGGTGCCACCAACATTTCAAAACAATTACCATGGGTCAGGGTGGCATTAA
Enzyme 72 GenBank Gene ID NM_018682.3 Link Image
Enzyme 72 GeneCard ID MLL5 Link Image
Enzyme 72 GenAtlas ID MLL5 Link Image
Enzyme 72 HGNC ID HGNC:18541 Link Image
Enzyme 72 Chromosome Location 7
Enzyme 72 Locus 7q22.1
Enzyme 72 SNPs SNPJam Report Link Image
Enzyme 72 General References
  1. Emerling BM, Bonifas J, Kratz CP, Donovan S, Taylor BR, Green ED, Le Beau MM, Shannon KM: MLL5, a homolog of Drosophila trithorax located within a segment of chromosome band 7q22 implicated in myeloid leukemia. Oncogene. 2002 Jul 18;21(31):4849-54. [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. 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. Deng LW, Chiu I, Strominger JL: MLL 5 protein forms intranuclear foci, and overexpression inhibits cell cycle progression. Proc Natl Acad Sci U S A. 2004 Jan 20;101(3):757-62. Epub 2004 Jan 12. [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. Cheng F, Liu J, Zhou SH, Wang XN, Chew JF, Deng LW: RNA interference against mixed lineage leukemia 5 resulted in cell cycle arrest. Int J Biochem Cell Biol. 2008;40(11):2472-81. Epub 2008 May 15. [PubMed Link Image]
  8. Fujiki R, Chikanishi T, Hashiba W, Ito H, Takada I, Roeder RG, Kitagawa H, Kato S: GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis. Nature. 2009 May 21;459(7245):455-9. Epub 2009 Apr 19. [PubMed Link Image]
Enzyme 72 Metabolite References Not Available
Enzyme 73 [top]
Enzyme 73 ID 14764
Enzyme 73 Name Probable histone-lysine N-methyltransferase NSD2
Enzyme 73 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 73 Gene Name WHSC1
Enzyme 73 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 73 Number of Residues 1365
Enzyme 73 Molecular Weight 152257.0
Enzyme 73 Theoretical pI 8.81
Enzyme 73 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 73 General Function Involved in histone-lysine N-methyltransferase activity
Enzyme 73 Specific Function Probable histone methyltransferase. May act as a transcription regulator that binds DNA and suppresses IL5 transcription
Enzyme 73 Pathways
Enzyme 73 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 73 Pfam Domain Function
Enzyme 73 Signals
  • None
Enzyme 73 Transmembrane Regions
  • None
Enzyme 73 Essentiality Not Available
Enzyme 73 GenBank ID Protein 109633019 Link Image
Enzyme 73 UniProtKB/Swiss-Prot ID O96028 Link Image
Enzyme 73 UniProtKB/Swiss-Prot Entry Name NSD2_HUMAN Link Image
Enzyme 73 PDB ID Not Available
Enzyme 73 Cellular Location Not Available
Enzyme 73 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 73 GenBank Gene ID NM_001042424.2 Link Image
Enzyme 73 GeneCard ID WHSC1 Link Image
Enzyme 73 GenAtlas ID WHSC1 Link Image
Enzyme 73 HGNC ID HGNC:12766 Link Image
Enzyme 73 Chromosome Location 4
Enzyme 73 Locus 4p16.3
Enzyme 73 SNPs SNPJam Report Link Image
Enzyme 73 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 73 Metabolite References Not Available
Enzyme 74 [top]
Enzyme 74 ID 14765
Enzyme 74 Name Histone-lysine N-methyltransferase NSD3
Enzyme 74 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 74 Gene Name WHSC1L1
Enzyme 74 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 74 Number of Residues 1437
Enzyme 74 Molecular Weight 161611.8
Enzyme 74 Theoretical pI 8.26
Enzyme 74 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 74 General Function Involved in histone-lysine N-methyltransferase activity
Enzyme 74 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 74 Pathways
Enzyme 74 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 74 Pfam Domain Function
Enzyme 74 Signals
  • None
Enzyme 74 Transmembrane Regions
  • None
Enzyme 74 Essentiality Not Available
Enzyme 74 GenBank ID Protein 13699811 Link Image
Enzyme 74 UniProtKB/Swiss-Prot ID Q9BZ95 Link Image
Enzyme 74 UniProtKB/Swiss-Prot Entry Name NSD3_HUMAN Link Image
Enzyme 74 PDB ID Not Available
Enzyme 74 Cellular Location Not Available
Enzyme 74 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 74 GenBank Gene ID NM_023034.1 Link Image
Enzyme 74 GeneCard ID WHSC1L1 Link Image
Enzyme 74 GenAtlas ID WHSC1L1 Link Image
Enzyme 74 HGNC ID HGNC:12767 Link Image
Enzyme 74 Chromosome Location 8
Enzyme 74 Locus 8p11.2
Enzyme 74 SNPs SNPJam Report Link Image
Enzyme 74 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 74 Metabolite References Not Available
Enzyme 75 [top]
Enzyme 75 ID 14766
Enzyme 75 Name Putative methyltransferase NSUN5C
Enzyme 75 Synonyms
  1. NOL1/NOP2/Sun domain family member 5C
  2. Williams-Beuren syndrome chromosomal region 20C protein
Enzyme 75 Gene Name NSUN5P2
Enzyme 75 Protein Sequence >Putative methyltransferase NSUN5C
MPELLVFPAQTDLHEHPLYRAGHLILQDRASCLPAMLLDPRQAPMSWMPVPPQAIKTSHL
AALLKNQGKIFAFDLDARRLASMATLLAWAGVSCCELAEEDFLAVSPLDPRYREVHYVLL
DPSCSGSGMPSRQLEEPGAGTPSPVRLHALAGFQQRALCHALTFPSLQRLVYSMCSLCQE
ENEDMVQDALQQNPGAFRLAPALPARPHRGLSTFPGAEHCLRASPKTTLSGGFFVAVIER
VEMPTSASQAKASAPERTPSPAPKRKKRAKSCSRCLHTALHIAEAPGSLLPGGKGRCLSS
PWKTLGPHRRQQFAF
Enzyme 75 Number of Residues 315
Enzyme 75 Molecular Weight 34346.3
Enzyme 75 Theoretical pI 8.77
Enzyme 75 GO Classification Not Available
Enzyme 75 General Function Translation, ribosomal structure and biogenesis
Enzyme 75 Specific Function May have S-adenosyl-L-methionine-dependent methyl- transferase activity (Potential)
Enzyme 75 Pathways Not Available
Enzyme 75 Reactions Not Available
Enzyme 75 Pfam Domain Function
Enzyme 75 Signals
  • None
Enzyme 75 Transmembrane Regions
  • None
Enzyme 75 Essentiality Not Available
Enzyme 75 GenBank ID Protein 16226075 Link Image
Enzyme 75 UniProtKB/Swiss-Prot ID Q63ZY6 Link Image
Enzyme 75 UniProtKB/Swiss-Prot Entry Name NSN5C_HUMAN Link Image
Enzyme 75 PDB ID Not Available
Enzyme 75 Cellular Location Not Available
Enzyme 75 Gene Sequence >948 bp
ATGCCGGAGCTGCTGGTGTTTCCCGCCCAGACAGATCTGCATGAACACCCACTGTACCGG
GCCGGACACCTCATTCTGCAGGACAGGGCCAGCTGTCTCCCAGCCATGCTGCTGGACCCC
CGCCGGGCTCCCATGTCATGGATGCCTGTGCCACCCCAGGCAATAAAGACCAGTCACTTG
GCTGCTCTTCTGAAGAACCAAGGGAAGATCTTTGCCTTTGACCTGGATGCCAGGCGGCTG
GCATCCATGGCCACGCTGCTGGCCTGGGCTGGCGTCTCCTGCTGTGAGCTGGCTGAGGAG
GACTTCCTGGCGGTCTCCCCCTTAGATCCGCGCTATCGTGAGGTCCACTATGTCCTGCTG
GATCCTTCCTGCAGTGGCTCGGGTATGCCGAGCAGACAGCTGGAGGAGCCCGGGGCAGGG
ACACCTAGCCCGGTGCGTCTGCATGCCCTGGCAGGGTTCCAGCAGCGAGCCCTGTGCCAC
GCGCTCACTTTCCCTTCCCTGCAGCGGCTCGTCTACTCCATGTGCTCCCTCTGCCAGGAG
GAGAATGAAGACATGGTACAAGATGCGCTGCAGCAGAACCCGGACGCCTTCAGGCTAGCT
CCCGCCCTGCCTGCCCGGCCCCACCGAGGCCTGAGCACGTTCCCGGGTGCCGAGCACTGC
CTCCGGGCTTCCCCCAAGACCACGCTTAGCGGTGGCTTCTTCGTTGCTGTAATTGAACGG
GTCGAGATGCCGACCTCAGCCTCACAGGCCAAAGCATCAGCACCAGAACGCACACCCAGC
CCAGCCCCAAAGAGAAAGAAGAGAGCAAAAAGCTGCAGCCGGTGCCTGCACACCGCCTTG
CGCATAGCAGAGGCTCCGGGCTCACTCCTTCCTGGTGGGAAAGGAAGATGCCTGTCCTCT
CCGTGGAGGACCCTGGGCCCTCACCGCAGGCAGCAGTTTGCGTTTTGA
Enzyme 75 GenBank Gene ID AF420250 Link Image
Enzyme 75 GeneCard ID NSUN5P2 Link Image
Enzyme 75 GenAtlas ID NSUN5P2 Link Image
Enzyme 75 HGNC ID HGNC:16609 Link Image
Enzyme 75 Chromosome Location 7
Enzyme 75 Locus 7q11.23
Enzyme 75 SNPs SNPJam Report Link Image
Enzyme 75 General References
  1. Doll A, Grzeschik KH: Characterization of two novel genes, WBSCR20 and WBSCR22, deleted in Williams-Beuren syndrome. Cytogenet Cell Genet. 2001;95(1-2):20-7. [PubMed Link Image]
  2. Merla G, Ucla C, Guipponi M, Reymond A: Identification of additional transcripts in the Williams-Beuren syndrome critical region. Hum Genet. 2002 May;110(5):429-38. Epub 2002 Mar 28. [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. 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. 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. 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. 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]
  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. 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 75 Metabolite References Not Available
Enzyme 76 [top]
Enzyme 76 ID 14767
Enzyme 76 Name Putative methyltransferase NSUN3
Enzyme 76 Synonyms
  1. NOL1/NOP2/Sun domain family member 3
Enzyme 76 Gene Name NSUN3
Enzyme 76 Protein Sequence >Putative methyltransferase NSUN3
MLTQLKAKSEGKLAKQICKVVLDHFEKQYSKELGDAWNTVREILTSPSCWQYAVLLNRFN
YPFELEKDLHLKGYHTLSQGSLPNYPKSVKCYLSRTPGRIPSERHQIGNLKKYYLLNAAS
LLPVLALELRDGEKVLDLCAAPGGKSIALLQCACPGYLHCNEYDSLRLRWLRQTLESFIP
QPLINVIKVSELDGRKMGDAQPEMFDKVLVDAPCSNDRSWLFSSDSQKASCRISQRRNLP
LLQIELLRSAIKALRPGGILVYSTCTLSKAENQDVISEILNSHGNIMPMDIKGIARTCSH
DFTFAPTGQECGLLVIPDKGKAWGPMYVAKLKKSWSTGKW
Enzyme 76 Number of Residues 340
Enzyme 76 Molecular Weight 38244.0
Enzyme 76 Theoretical pI 9.10
Enzyme 76 GO Classification Not Available
Enzyme 76 General Function Translation, ribosomal structure and biogenesis
Enzyme 76 Specific Function May have S-adenosyl-L-methionine-dependent methyl- transferase activity (Potential)
Enzyme 76 Pathways Not Available
Enzyme 76 Reactions Not Available
Enzyme 76 Pfam Domain Function
Enzyme 76 Signals
  • None
Enzyme 76 Transmembrane Regions
  • None
Enzyme 76 Essentiality Not Available
Enzyme 76 GenBank ID Protein 11545785 Link Image
Enzyme 76 UniProtKB/Swiss-Prot ID Q9H649 Link Image
Enzyme 76 UniProtKB/Swiss-Prot Entry Name NSUN3_HUMAN Link Image
Enzyme 76 PDB ID Not Available
Enzyme 76 Cellular Location Not Available
Enzyme 76 Gene Sequence >1023 bp
ATGCTGACCCAGCTGAAAGCAAAATCAGAGGGGAAGCTTGCAAAACAGATTTGCAAAGTT
GTGTTGGATCATTTTGAAAAACAGTATTCCAAAGAACTCGGAGATGCCTGGAATACAGTA
AGGGAGATACTAACATCTCCATCATGCTGGCAATATGCTGTCCTGCTTAACCGATTCAAT
TATCCTTTTGAACTGGAAAAGGATTTACATTTGAAGGGCTATCACACACTCTCTCAGGGA
TCTTTACCCAACTATCCTAAATCAGTGAAGTGTTACCTTAGCAGAACTCCGGGCCGAATC
CCTTCAGAAAGACACCAAATTGGAAACCTGAAAAAATATTATCTCCTAAATGCTGCTTCT
CTTCTCCCAGTGTTGGCTCTGGAATTAAGGGATGGGGAGAAGGTTCTGGATCTCTGTGCT
GCTCCTGGAGGGAAATCAATAGCTCTGCTGCAGTGTGCTTGTCCAGGTTATCTTCATTGT
AATGAATATGATAGTCTGAGATTGAGGTGGCTAAGGCAGACGTTGGAATCTTTCATCCCA
CAGCCTTTGATAAATGTAATTAAAGTGTCTGAATTGGATGGCAGAAAAATGGGAGATGCC
CAGCCTGAAATGTTTGACAAGGTGTTAGTGGATGCTCCGTGTTCAAATGATCGAAGCTGG
TTGTTTTCTTCTGACTCTCAGAAGGCATCCTGTAGGATAAGTCAAAGGAGGAATTTGCCT
CTTCTACAGATAGAGCTGTTAAGGTCTGCAATTAAGGCCTTACGTCCTGGAGGGATACTT
GTATACTCTACATGCACGCTTTCCAAGGCAGAAAATCAAGATGTGATCAGTGAAATTTTA
AACTCCCACGGTAACATCATGCCTATGGACATTAAAGGAATAGCAAGGACTTGCTCCCAC
GACTTCACATTTGCTCCCACTGGCCAGGAATGTGGGCTCTTAGTGATTCCAGATAAGGGC
AAAGCCTGGGGCCCAATGTATGTAGCCAAATTGAAGAAATCATGGAGCACAGGAAAATGG
TGA
Enzyme 76 GenBank Gene ID NM_022072.3 Link Image
Enzyme 76 GeneCard ID NSUN3 Link Image
Enzyme 76 GenAtlas ID NSUN3 Link Image
Enzyme 76 HGNC ID HGNC:26208 Link Image
Enzyme 76 Chromosome Location 3
Enzyme 76 Locus 3q11.1
Enzyme 76 SNPs SNPJam Report Link Image
Enzyme 76 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. 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 76 Metabolite References Not Available
Enzyme 77 [top]
Enzyme 77 ID 14768
Enzyme 77 Name Putative methyltransferase NSUN4
Enzyme 77 Synonyms
  1. NOL1/NOP2/Sun domain family member 4
Enzyme 77 Gene Name NSUN4
Enzyme 77 Protein Sequence >Putative methyltransferase NSUN4
MAALTLRGVRELLKRVDLATVPRRHRYKKKWAATEPKFPAVRLALQNFDMTYSVQFGDLW
PSIRVSLLSEQKYGALVNNFAAWDHVSAKLEQLSAKDFVNEAISHWELQSEGGQSAAPSP
ASWACSPNLRCFTFDRGDISRFPPARPGSLGVMEYYLMDAASLLPVLALGLQPGDIVLDL
CAAPGGKTLALLQTGCCRNLAANDLSPSRIARLQKILHSYVPEEIRDGNQVRVTSWDGRK
WGELEGDTYDRVLVDVPCTTDRHSLHEEENNIFKRSRKKERQILPVLQVQLLAAGLLATK
PGGHVVYSTCSLSHLQNEYVVQGAIELLANQYSIQVQVEDLTHFRRVFMDTFCFFSSCQV
GELVIPNLMANFGPMYFCKMRRLT
Enzyme 77 Number of Residues 384
Enzyme 77 Molecular Weight 43088.2
Enzyme 77 Theoretical pI 8.26
Enzyme 77 GO Classification Not Available
Enzyme 77 General Function Translation, ribosomal structure and biogenesis
Enzyme 77 Specific Function May have S-adenosyl-L-methionine-dependent methyl- transferase activity (Potential)
Enzyme 77 Pathways Not Available
Enzyme 77 Reactions Not Available
Enzyme 77 Pfam Domain Function
Enzyme 77 Signals
  • None
Enzyme 77 Transmembrane Regions
  • None
Enzyme 77 Essentiality Not Available
Enzyme 77 GenBank ID Protein 40316918 Link Image
Enzyme 77 UniProtKB/Swiss-Prot ID Q96CB9 Link Image
Enzyme 77 UniProtKB/Swiss-Prot Entry Name NSUN4_HUMAN Link Image
Enzyme 77 PDB ID Not Available
Enzyme 77 Cellular Location Not Available
Enzyme 77 Gene Sequence >1155 bp
ATGGCTGCGCTGACACTGAGGGGTGTCCGGGAGCTGCTGAAGCGTGTGGACCTCGCGACG
GTCCCGCGGAGACATCGATATAAGAAGAAATGGGCTGCCACAGAGCCCAAATTCCCTGCT
GTTCGACTGGCTTTGCAGAATTTTGACATGACTTACAGTGTGCAGTTTGGAGATCTTTGG
CCATCAATCCGTGTCAGTCTCCTCTCAGAGCAGAAGTATGGTGCACTGGTCAATAACTTT
GCTGCCTGGGATCATGTAAGTGCTAAGCTGGAGCAGCTGAGTGCCAAGGATTTTGTGAAT
GAAGCCATCTCCCACTGGGAACTGCAGTCTGAGGGTGGCCAATCTGCAGCCCCATCCCCT
GCCTCCTGGGCCTGCAGTCCGAACCTTCGATGCTTCACTTTTGACAGAGGGGATATCAGT
CGCTTCCCTCCTGCCAGACCTGGCAGCCTGGGTGTCATGGAGTACTACCTGATGGATGCT
GCCTCCTTGCTGCCTGTTCTGGCCCTCGGCCTGCAGCCTGGGGACATCGTGCTTGACCTA
TGTGCAGCTCCTGGGGGAAAGACACTAGCGTTGCTTCAGACTGGCTGTTGCCGCAATCTT
GCTGCCAATGATCTCTCCCCGTCCCGAATAGCCAGACTACAGAAGATCCTTCACAGCTAT
GTGCCTGAAGAGATCAGGGATGGAAATCAAGTTCGAGTTACCTCATGGGATGGCAGGAAA
TGGGGAGAACTGGAGGGGGACACCTATGACCGGGTGCTGGTGGATGTGCCCTGTACCACA
GACCGCCACTCCCTTCATGAGGAGGAGAACAACATCTTTAAGCGGTCAAGGAAGAAGGAG
CGACAGATATTGCCTGTGCTGCAAGTGCAGCTTCTTGCGGCTGGACTCCTTGCCACCAAA
CCAGGAGGCCATGTTGTCTATTCTACCTGCTCACTCTCACACTTACAGAACGAGTATGTG
GTGCAAGGTGCCATTGAGCTCCTGGCCAATCAATACAGCATCCAGGTACAGGTGGAAGAT
CTGACTCACTTCCGAAGGGTTTTCATGGACACATTTTGTTTCTTCTCATCCTGTCAGGTT
GGGGAGCTGGTAATACCAAACCTCATGGCCAATTTTGGCCCCATGTACTTCTGCAAAATG
CGTAGGCTGACATAG
Enzyme 77 GenBank Gene ID NM_199044.2 Link Image
Enzyme 77 GeneCard ID NSUN4 Link Image
Enzyme 77 GenAtlas ID NSUN4 Link Image
Enzyme 77 HGNC ID HGNC:31802 Link Image
Enzyme 77 Chromosome Location 1
Enzyme 77 Locus 1p34
Enzyme 77 SNPs SNPJam Report Link Image
Enzyme 77 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. 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]
Enzyme 77 Metabolite References Not Available
Enzyme 78 [top]
Enzyme 78 ID 14769
Enzyme 78 Name Putative methyltransferase NSUN5
Enzyme 78 Synonyms
  1. NOL1-related protein
  2. NOL1R
  3. NOL1/NOP2/Sun domain family member 5
  4. Williams-Beuren syndrome chromosomal region 20A protein
Enzyme 78 Gene Name NSUN5
Enzyme 78 Protein Sequence >Putative methyltransferase NSUN5
MGLYAAAAGVLAGVESRQGSIKGLVYSSNFQNVKQLYALVCETQRYSAVLDAVIASAGLL
RAEKKLRPHLAKVLVYELLLGKGFRGGGGRWKALLGRHQARLKAELARLKVHRGVSRNED
LLEVGSRPGPASQLPRFVRVNTLKTCSDDVVDYFKRQGFSYQGRASSLDDLRALKGKHFL
LDPLMPELLVFPAQTDLHEHPLYRAGHLILQDRASCLPAMLLDPPPGSHVIDACAAPGNK
TSHLAALLKNQGKIFAFDLDAKRLASMATLLARAGVSCCELAEEDFLAVSPSDPRYHEVH
YILLDPSCSGSGMPSRQLEEPGAGTPSPVRLHALAGFQQRALCHALTFPSLQRLVYSTCS
LCQEENEDVVRDALQQNPGAFRLAPALPAWPHRGLSTFPGAEHCLRASPETTLSSGFFVA
VIERVEVPR
Enzyme 78 Number of Residues 429
Enzyme 78 Molecular Weight 46691.2
Enzyme 78 Theoretical pI 8.73
Enzyme 78 GO Classification Not Available
Enzyme 78 General Function Translation, ribosomal structure and biogenesis
Enzyme 78 Specific Function May have S-adenosyl-L-methionine-dependent methyl- transferase activity (Potential)
Enzyme 78 Pathways Not Available
Enzyme 78 Reactions Not Available
Enzyme 78 Pfam Domain Function
Enzyme 78 Signals
  • None
Enzyme 78 Transmembrane Regions
  • None
Enzyme 78 Essentiality Not Available
Enzyme 78 GenBank ID Protein 37674385 Link Image
Enzyme 78 UniProtKB/Swiss-Prot ID Q96P11 Link Image
Enzyme 78 UniProtKB/Swiss-Prot Entry Name NSUN5_HUMAN Link Image
Enzyme 78 PDB ID Not Available
Enzyme 78 Cellular Location Not Available
Enzyme 78 Gene Sequence >1290 bp
ATGGGGCTGTATGCTGCAGCTGCAGGCGTGTTGGCCGGCGTGGAGAGCCGCCAGGGCTCT
ATCAAGGGGTTGGTGTACTCCAGCAACTTCCAGAACGTGAAGCAGCTGTACGCGCTGGTG
TGCGAAACGCAGCGCTACTCCGCCGTGCTGGATGCTGTGATCGCCAGCGCCGGCCTCCTC
CGTGCGGAGAAGAAGCTGCGGCCGCACCTGGCCAAGGTGCTAGTGTATGAGTTGTTGTTG
GGAAAGGGCTTTCGAGGGGGTGGGGGCCGATGGAAGGCTCTGTTGGGCCGGCACCAGGCG
AGGCTCAAGGCTGAGTTGGCTCGGCTCAAGGTTCATCGGGGTGTGAGCCGGAATGAGGAC
CTGTTGGAAGTGGGATCCAGGCCTGGTCCAGCCTCCCAGCTGCCTCGATTTGTGCGTGTG
AACACTCTCAAGACCTGCTCCGATGATGTAGTTGATTATTTCAAGAGACAAGGTTTCTCC
TATCAGGGTCGGGCTTCCAGCCTCGATGACTTACGAGCCCTCAAGGGGAAGCATTTTCTC
CTGGACCCCTTGATGCCGGAGCTGCTGGTGTTTCCCGCCCAGACAGATCTGCATGAACAC
CCACTGTACCGGGCCGGACACCTCATTCTGCAGGACAGGGCCAGCTGTCTCCCAGCCATG
CTGCTGGACCCCCCGCCAGGCTCCCATGTCATCGATGCCTGTGCCGCCCCAGGCAATAAG
ACCAGTCACTTGGCTGCTCTTCTGAAGAACCAAGGGAAGATCTTTGCCTTTGACCTGGAT
GCCAAGCGGCTGGCATCCATGGCCACGCTGCTGGCCCGGGCTGGCGTCTCTTGCTGTGAA
CTGGCTGAGGAGGACTTCCTGGCGGTCTCCCCCTCGGATCCACGCTACCATGAGGTCCAC
TACATCCTGCTGGATCCTTCCTGCAGTGGCTCGGGTATGCCGAGCAGACAGCTGGAGGAG
CCCGGGGCAGGCACACCTAGCCCGGTGCGTCTGCATGCCCTGGCAGGGTTCCAGCAGCGA
GCCCTGTGCCACGCGCTCACTTTCCCTTCCCTGCAGCGGCTCGTCTACTCCACGTGCTCC
CTCTGCCAGGAGGAGAATGAAGACGTGGTGCGAGATGCGCTGCAGCAGAACCCGGGCGCC
TTCAGGCTAGCTCCCGCCCTGCCTGCCTGGCCCCACCGAGGCCTGAGCACGTTCCCGGGT
GCCGAGCACTGCCTCCGGGCCTCCCCTGAGACCACACTCAGCAGTGGCTTCTTCGTTGCT
GTAATTGAACGGGTCGAGGTGCCAAGGTGA
Enzyme 78 GenBank Gene ID AC073841 Link Image
Enzyme 78 GeneCard ID NSUN5 Link Image
Enzyme 78 GenAtlas ID NSUN5 Link Image
Enzyme 78 HGNC ID HGNC:16385 Link Image
Enzyme 78 Chromosome Location 7
Enzyme 78 Locus 7q11.23
Enzyme 78 SNPs SNPJam Report Link Image
Enzyme 78 General References
  1. Doll A, Grzeschik KH: Characterization of two novel genes, WBSCR20 and WBSCR22, deleted in Williams-Beuren syndrome. Cytogenet Cell Genet. 2001;95(1-2):20-7. [PubMed Link Image]
  2. Merla G, Ucla C, Guipponi M, Reymond A: Identification of additional transcripts in the Williams-Beuren syndrome critical region. Hum Genet. 2002 May;110(5):429-38. Epub 2002 Mar 28. [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. 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]
  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. 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 78 Metabolite References Not Available
Enzyme 79 [top]
Enzyme 79 ID 14770
Enzyme 79 Name Putative methyltransferase NSUN6
Enzyme 79 Synonyms
  1. NOL1/NOP2/Sun and PUA domain-containing protein 1
  2. NOL1/NOP2/Sun domain family member 6
Enzyme 79 Gene Name NSUN6
Enzyme 79 Protein Sequence >Putative methyltransferase NSUN6
MSIFPKISLRPEVENYLKEGFMNKEIVTALGKQEAERKFETLLKHLSHPPSFTTVRVNTH
LASVQHVKNLLLDELQKQFNGLSVPILQHPDLQDVLLIPVIGPRKNIKKQQCEAIVGAQC
GNAVLRGAHVYAPGIVSASQFMKAGDVISVYSDIKGKCKKGAKEFDGTKVFLGNGISELS
RKEIFSGLPELKGMGIRMTEPVYLSPSFDSVLPRYLFLQNLPSALVSHVLNPQPGEKILD
LCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDGTKAVKL
DMVEDTEGEPPFLPESFDRILLDAPCSGMGQRPNMACTWSVKEVASYQPLQRKLFTAAVQ
LLKPEGVLVYSTCTITLAENEEQVAWALTKFPCLQLQPQEPQIGGEGMRGAGLSCEQLKQ
LQRFDPSAVPLPDTDMDSLREARREDMLRLANKDSIGFFIAKFVKCKST
Enzyme 79 Number of Residues 469
Enzyme 79 Molecular Weight 51769.8
Enzyme 79 Theoretical pI 8.05
Enzyme 79 GO Classification
Function
  • RNA binding
  • binding
  • catalytic activity
  • methyltransferase activity
  • nucleic acid binding
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
Component
Enzyme 79 General Function Involved in RNA binding
Enzyme 79 Specific Function May have S-adenosyl-L-methionine-dependent methyl- transferase activity (Potential)
Enzyme 79 Pathways Not Available
Enzyme 79 Reactions Not Available
Enzyme 79 Pfam Domain Function
Enzyme 79 Signals
  • None
Enzyme 79 Transmembrane Regions
  • None
Enzyme 79 Essentiality Not Available
Enzyme 79 GenBank ID Protein 18676896 Link Image
Enzyme 79 UniProtKB/Swiss-Prot ID Q8TEA1 Link Image
Enzyme 79 UniProtKB/Swiss-Prot Entry Name NSUN6_HUMAN Link Image
Enzyme 79 PDB ID Not Available
Enzyme 79 Cellular Location Not Available
Enzyme 79 Gene Sequence >1410 bp
ATGTCTATTTTCCCTAAGATATCTTTGAGACCTGAGGTTGAAAACTATCTTAAGGAAGGC
TTTATGAATAAGGAGATTGTGACTGCTTTAGGTAAACAAGAAGCAGAAAGGAAGTTTGAA
ACTTTGTTAAAGCACCTGTCACATCCTCCATCATTTACAACTGTCAGAGTGAATACACAT
TTAGCCTCAGTACAACATGTGAAAAATCTGTTACTTGATGAACTTCAGAAGCAGTTTAAT
GGATTAAGTGTTCCTATTCTTCAACATCCAGACCTTCAAGATGTGTTACTTATTCCTGTT
ATTGGACCCAGAAAGAATATTAAAAAACAACAGTGTGAAGCCATTGTTGGAGCCCAGTGT
GGCAATGCAGTTTTAAGAGGAGCCCATGTCTATGCCCCAGGAATTGTGTCAGCATCACAA
TTTATGAAAGCTGGAGATGTTATTTCTGTATACTCTGATATTAAAGGAAAATGTAAGAAA
GGAGCCAAAGAATTTGATGGAACAAAAGTATTTCTTGGAAATGGGATTTCTGAACTAAGC
CGCAAAGAAATCTTCAGTGGATTACCTGAACTGAAAGGCATGGGCATAAGAATGACAGAA
CCAGTATATCTCAGCCCTTCATTTGACAGTGTACTGCCCCGTTACTTATTTTTACAAAAT
TTGCCATCTGCCTTAGTAAGTCATGTACTAAATCCTCAACCTGGAGAGAAGATTCTAGAC
TTGTGTGCAGCACCTGGAGGGAAAACAACACACATTGCAGCACTAATGCATGATCAGGGA
GAAGTTATAGCACTGGATAAAATCTTCAACAAAGTAGAAAAAATCAAACAGAATGCCTTA
TTGTTAGGGCTGAATTCCATCAGGGCATTTTGTTTTGATGGAACAAAGGCGGTTAAACTT
GATATGGTGGAGGACACAGAAGGAGAACCTCCATTTCTACCAGAATCCTTTGACCGAATT
CTTCTGGATGCACCCTGTAGTGGAATGGGACAGAGACCAAACATGGCCTGTACTTGGTCT
GTGAAGGAAGTGGCATCATATCAGCCATTACAGCGAAAACTCTTCACTGCAGCGGTTCAG
CTGCTGAAGCCAGAGGGTGTGCTGGTTTATAGCACGTGCACTATAACACTGGCCGAAAAT
GAAGAACAGGTTGCCTGGGCCCTGACAAAATTTCCTTGCCTTCAGCTTCAGCCCCAGGAA
CCGCAGATTGGAGGAGAAGGAATGAGGGGAGCTGGGCTCTCATGTGAACAGTTGAAACAG
CTGCAGCGATTTGATCCATCGGCTGTGCCATTACCGGACACTGACATGGACTCTCTTAGA
GAGGCCAGAAGAGAAGACATGTTGCGTCTGGCTAATAAGGACTCTATAGGTTTTTTTATT
GCAAAATTTGTAAAATGCAAAAGCACATAG
Enzyme 79 GenBank Gene ID AK074323 Link Image
Enzyme 79 GeneCard ID NSUN6 Link Image
Enzyme 79 GenAtlas ID NSUN6 Link Image
Enzyme 79 HGNC ID HGNC:23529 Link Image
Enzyme 79 Chromosome Location 1
Enzyme 79 Locus 10p12.31
Enzyme 79 SNPs SNPJam Report Link Image
Enzyme 79 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. 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]
  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 79 Metabolite References Not Available
Enzyme 80 [top]
Enzyme 80 ID 14771
Enzyme 80 Name Putative methyltransferase NSUN7
Enzyme 80 Synonyms
  1. NOL1/NOP2/Sun domain family member 7
Enzyme 80 Gene Name NSUN7
Enzyme 80 Protein Sequence >Putative methyltransferase NSUN7
MLNSTGELEFSNEEDPEIISQLTSLPLSGGKSSAGVPEKTGYPDSVYVMAANIFQGIRIE
KSAQKVLIKYGNEPLRSLSESEDQSFQRLSYELAFSALKYQDILETILIDSCIFPSTTIP
DHLSSLIIVMLYDFQDRKFQTRVLSDNEEPISEVQEVENLLNSFKIKLAAALARCRIKHD
ALSIYHILPETVRKQELRASTLPLYAWINTCKISPEEVYNNLKRRGYNKVKSVLHIDDKV
FAVDQHCYDVLIFPSHLKNDLINIDLFKDYKLIFQDKSRSLAVHSVKALLNMDDDVLMVN
TGSWYTVAHMSILTNNNTSKVFVCGVQSQAKDPDLKTLFTKIGCKNIEILHEKFINIESK
DHRLQKVKVILLLPRCSGLGVSNPVEFILNEHEDTEFLKDHSQGGISVDKLHVLAQQQYE
QLTHAMKFTKAQAVVYCTCSVFPEENEAVVKKALEFQDLGNKGQPYRLSPPVLPLCSLKE
IQLSTDKFFRMEPSEITNGCFLSILTRERDPSETVSVNDVLARAAAKGLLDGIELGKSSK
REKKKKKSKTSLTKGATTDNGIQMKIAEFLNRETKASANLSETVTKPPLPQKNTAQVGAS
SQTRKPNKLAPHPAVPAFVKNTCPSRPRERQTHFLRPRPEDRMVALKPIKIVLPPVFMPF
SSPQGIRSRMPTQHLYCRWVAPKALVPTCLPTHSLSRKEEKPKDDTPSSLLRPPRRWL
Enzyme 80 Number of Residues 718
Enzyme 80 Molecular Weight 81022.7
Enzyme 80 Theoretical pI 9.04
Enzyme 80 GO Classification Not Available
Enzyme 80 General Function Translation, ribosomal structure and biogenesis
Enzyme 80 Specific Function May have S-adenosyl-L-methionine-dependent methyl- transferase activity (Potential)
Enzyme 80 Pathways Not Available
Enzyme 80 Reactions Not Available
Enzyme 80 Pfam Domain Function
Enzyme 80 Signals
  • None
Enzyme 80 Transmembrane Regions
  • None
Enzyme 80 Essentiality Not Available
Enzyme 80 GenBank ID Protein 187828635 Link Image
Enzyme 80 UniProtKB/Swiss-Prot ID Q8NE18 Link Image
Enzyme 80 UniProtKB/Swiss-Prot Entry Name NSUN7_HUMAN Link Image
Enzyme 80 PDB ID Not Available
Enzyme 80 Cellular Location Not Available
Enzyme 80 Gene Sequence >2157 bp
ATGCTGAATTCCACGGGCGAACTGGAGTTTTCGAACGAAGAAGATCCCGAGATCATCTCC
CAACTCACTTCCCTGCCTCTGTCCGGTGGGAAAAGCTCAGCTGGTGTGCCCGAAAAAACG
GGCTATCCGGACTCCGTTTATGTCATGGCAGCCAACATTTTTCAGGGTATTCGAATCGAA
AAGTCGGCACAGAAAGTCTTAATCAAGTATGGGAATGAACCCCTGCGGTCCTTGTCCGAG
TCTGAGGATCAGTCCTTTCAGCGTTTGTCTTATGAGCTGGCTTTCAGTGCCCTGAAATAT
CAAGATATTTTGGAAACTATATTGATAGACAGCTGTATCTTCCCAAGTACCACAATACCA
GATCATTTGAGCAGTCTTATTATTGTGATGCTATATGATTTCCAAGATAGAAAATTTCAA
ACTCGTGTCCTTTCTGATAATGAAGAGCCCATATCAGAAGTTCAAGAAGTAGAGAACCTT
CTTAACAGTTTTAAGATAAAATTGGCTGCAGCATTGGCAAGATGTCGAATCAAGCATGAT
GCCCTTTCAATTTACCACATCCTTCCAGAAACAGTTAGGAAACAGGAACTAAGGGCCTCC
ACTTTACCACTTTATGCTTGGATAAATACTTGTAAAATCAGCCCTGAAGAAGTTTATAAT
AATTTGAAGAGAAGAGGCTATAATAAAGTCAAATCTGTATTGCATATTGATGATAAAGTC
TTTGCTGTGGATCAACATTGCTATGATGTCTTAATTTTTCCATCTCATCTTAAAAATGAT
CTTATAAATATAGATCTTTTCAAAGATTACAAACTTATATTTCAGGACAAATCTCGAAGT
CTTGCTGTCCATTCTGTAAAGGCTTTATTAAATATGGATGATGATGTCTTAATGGTCAAT
ACAGGCTCATGGTACACAGTTTCCCACATGTCAATTTTAACAAATAATAATACCTCAAAA
GTATTTGTGTGTGGAGTACAATCACAAGCTAAGGATCCTGACTTGAAGACCCTTTTCACA
AAAATAGGATGTAAAAATATTGAAATACTTCATGAGAAATTTATTAACATTGAATCAAAG
GATCACAGGTTACAGAAAGTTAAAGTGATTTTGCTGCTACCTCGTTGTTCAGGACTGGGT
GTTAGTAATCCAGTAGAATTTATTTTAAATGAACATGAAGATACAGAATTCCTTAAAGAT
CACTCTCAAGGAGGCATCTCAGTGGACAAACTTCACGTTCTTGCTCAACAGCAGTATGAA
CAGCTAACACATGCAATGAAATTTACTAAAGCTCAAGCAGTTGTTTACTGCACATGTTCA
GTTTTTCCAGAAGAAAATGAAGCTGTTGTTAAGAAAGCACTGGAATTTCAAGACCTTGGG
AATAAAGGACAACCTTACAGGCTTAGTCCTCCTGTTCTTCCACTGTGCTCCTTAAAGGAA
ATTCAATTGTCTACTGATAAATTTTTCAGAATGGAACCATCTGAAATTACCAATGGTTGT
TTTCTTTCTATTTTAACAAGGGAGCGGGACCCTTCTGAGACAGTGTCTGTGAATGATGTT
TTGGCCCGAGCTGCAGCCAAGGGTCTGCTGGATGGGATTGAGTTGGGTAAATCATCAAAA
CGGGAGAAGAAGAAGAAAAAATCAAAAACATCATTGACAAAAGGTGCCACTACTGATAAT
GGCATCCAAATGAAAATTGCTGAGTTCCTGAATCGAGAAACTAAAGCCAGTGCTAATCTA
TCAGAGACTGTAACAAAACCACCTCTTCCCCAGAAAAATACTGCTCAAGTGGGGGCTTCC
TCACAGACCAGAAAACCCAACAAGCTGGCCCCCCATCCTGCAGTGCCTGCATTTGTGAAG
AACACTTGTCCCTCCAGACCGCGTGAACGGCAGACACACTTCTTAAGACCTCGGCCAGAA
GACAGAATGGTTGCTCTGAAACCCATCGAGATTGTTCTGCCTCCAGTCTTTATGCCATTT
TCAAGTCCCCAAGGGATCAGATCTCGGATGCCAACTCAACATTTGTACTGTCGTTGGGTT
GCACCCAAGGCACTTGTGCCCACCTGCCTTCCCACACACTCACTATCCAGAAAAGAGGAA
AAGCCTAAAGATGACACACCTTCCTCCCTACTCAGGCCTCCTCGGCGATGGCTTTGA
Enzyme 80 GenBank Gene ID NM_024677 Link Image
Enzyme 80 GeneCard ID NSUN7 Link Image
Enzyme 80 GenAtlas ID NSUN7 Link Image
Enzyme 80 HGNC ID HGNC:25857 Link Image
Enzyme 80 Chromosome Location 4
Enzyme 80 Locus 4p14
Enzyme 80 SNPs SNPJam Report Link Image
Enzyme 80 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. 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]
  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]
Enzyme 80 Metabolite References Not Available
Enzyme 81 [top]
Enzyme 81 ID 14772
Enzyme 81 Name Putative ribosomal RNA methyltransferase 1
Enzyme 81 Synonyms
  1. Protein ftsJ homolog 1
  2. rRNA (uridine-2'-O-)-methyltransferase
Enzyme 81 Gene Name FTSJ1
Enzyme 81 Protein Sequence >Putative ribosomal RNA methyltransferase 1
MGRTSKDKRDVYYRLAKENGWRARSAFKLLQLDKEFQLFQGVTRAVDLCAAPGSWSQVLS
QKIGGQGSGHVVAVDLQAMAPLPGVVQIQGDITQLSTAKEIIQHFKGCPADLVVCDGAPD
VTGLHDVDEYMQAQLLLAALNIATHVLKPGGCFVAKIFRGRDVTLLYSQLQVFFSSVLCA
KPRSSRNSSIEAFAVCQGYDPPEGFIPDLSKPLLDHSYDPDFNQLDGPTRIIVPFVTCGD
LSSYDSDRSYPLDLEGGSEYKYTPPTQPPISPPYQEACTLKRKGQLAKEIRPQDCPISRV
DTFPQPLAAPQCHTLLAPEMEDNEMSCSP
Enzyme 81 Number of Residues 329
Enzyme 81 Molecular Weight 36078.8
Enzyme 81 Theoretical pI 5.39
Enzyme 81 GO Classification
Function
  • binding
  • catalytic activity
  • methyltransferase activity
  • nucleic acid binding
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • RNA metabolic process
  • cellular macromolecule metabolic process
  • cellular metabolic process
  • macromolecule metabolic process
  • metabolic process
  • methylation
  • ncRNA metabolic process
  • one-carbon metabolic process
  • rRNA metabolic process
  • rRNA methylation
  • rRNA modification
  • rRNA processing
Component
Enzyme 81 General Function Involved in methyltransferase activity
Enzyme 81 Specific Function S-adenosyl-L-methionine + rRNA = S-adenosyl-L- homocysteine + rRNA containing 2'-O-methyluridine
Enzyme 81 Pathways Not Available
Enzyme 81 Reactions Not Available
Enzyme 81 Pfam Domain Function
Enzyme 81 Signals
  • None
Enzyme 81 Transmembrane Regions
  • None
Enzyme 81 Essentiality Not Available
Enzyme 81 GenBank ID Protein 7110661 Link Image
Enzyme 81 UniProtKB/Swiss-Prot ID Q9UET6 Link Image
Enzyme 81 UniProtKB/Swiss-Prot Entry Name RRMJ1_HUMAN Link Image
Enzyme 81 PDB ID Not Available
Enzyme 81 Cellular Location Not Available
Enzyme 81 Gene Sequence >990 bp
ATGGGACGGACGTCAAAGGACAAGCGGGATGTCTACTACCGCCTGGCCAAGGAGAATGGC
TGGCGTGCTCGCAGCGCCTTCAAACTGCTACAACTGGATAAGGAATTCCAACTCTTCCAA
GGCGTGACACGGGCAGTTGACCTGTGTGCAGCCCCAGGCAGCTGGAGCCAGGTGCTGAGC
CAGAAGATCGGGGGCCAAGGGTCCGGCCACGTGGTGGCTGTGGACCTGCAGGCTATGGCT
CCACTACCAGGTGTGGTACAGATCCAGGGGGACATCACCCAGCTGTCCACTGCCAAGGAG
ATCATCCAGCACTTTAAGGGCTGCCCTGCGGACCTAGTGGTGTGTGACGGGGCTCCTGAT
GTAACCGGTCTCCATGATGTTGATGAGTATATGCAGGCCCAGCTCCTCCTAGCTGCTCTG
AACATTGCTACACATGTCCTGAAGCCAGGGGGCTGCTTTGTGGCCAAGATATTCCGAGGC
CGGGATGTGACGCTCCTCTACAGCCAGCTGCAGGTCTTCTTCTCCAGCGTGCTGTGTGCC
AAGCCCAGGAGCAGCCGGAACTCTAGCATCGAGGCCTTCGCTGTCTGTCAGGGCTATGAC
CCTCCCGAGGGCTTCATCCCGGACCTGAGCAAACCCCTGCTGGACCATTCTTACGACCCA
GATTTCAACCAGCTGGATGGTCCCACCCGCATCATTGTGCCTTTTGTGACCTGTGGGGAC
CTGAGCTCCTATGATTCGGACCGCAGTTACCCACTGGACCTAGAGGGCGGCTCAGAGTAC
AAGTACACTCCACCCACACAGCCCCCCATCTCGCCACCATACCAGGAGGCCTGCACGTTG
AAGAGGAAGGGGCAGCTGGCCAAGGAGATCCGCCCCCAGGACTGCCCCATCAGCAGAGTG
GACACGTTTCCCCAGCCCCTGGCCGCCCCTCAGTGCCACACCCTGCTGGCCCCTGAGATG
GAAGACAATGAAATGAGTTGTTCACCTTAA
Enzyme 81 GenBank Gene ID NM_012280.2 Link Image
Enzyme 81 GeneCard ID FTSJ1 Link Image
Enzyme 81 GenAtlas ID FTSJ1 Link Image
Enzyme 81 HGNC ID HGNC:13254 Link Image
Enzyme 81 Chromosome Location Not Available
Enzyme 81 Locus Not Available
Enzyme 81 SNPs SNPJam Report Link Image
Enzyme 81 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. 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]
  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. Freude K, Hoffmann K, Jensen LR, Delatycki MB, des Portes V, Moser B, Hamel B, van Bokhoven H, Moraine C, Fryns JP, Chelly J, Gecz J, Lenzner S, Kalscheuer VM, Ropers HH: Mutations in the FTSJ1 gene coding for a novel S-adenosylmethionine-binding protein cause nonsyndromic X-linked mental retardation. Am J Hum Genet. 2004 Aug;75(2):305-9. Epub 2004 May 25. [PubMed Link Image]
  5. 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 81 Metabolite References Not Available
Enzyme 82 [top]
Enzyme 82 ID 14773
Enzyme 82 Name Putative ribosomal RNA methyltransferase 2
Enzyme 82 Synonyms
  1. Protein ftsJ homolog 2
  2. rRNA (uridine-2'-O-)-methyltransferase
Enzyme 82 Gene Name FTSJ2
Enzyme 82 Protein Sequence >Putative ribosomal RNA methyltransferase 2
MAGYLKLVCVSFQRQGFHTVGSRCKNRTGAEHLWLTRHLRDPFVKAAKVESYRCRSAFKL
LEVNERHQILRPGLRVLDCGAAPGAWSQVAVQKVNAAGTDPSSPVGFVLGVDLLHIFPLE
GATFLCPADVTDPRTSQRILEVLPGRRADVILSDMAPNATGFRDLDHDRLISLCLTLLSV
TPDILQPGGTFLCKTWAGSQSRRLQRRLTEEFQNVRIIKPEASRKESSEVYFLATQYHGR
KGTVKQ
Enzyme 82 Number of Residues 246
Enzyme 82 Molecular Weight 27423.4
Enzyme 82 Theoretical pI 9.98
Enzyme 82 GO Classification
Function
  • binding
  • catalytic activity
  • methyltransferase activity
  • nucleic acid binding
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • RNA metabolic process
  • cellular macromolecule metabolic process
  • cellular metabolic process
  • macromolecule metabolic process
  • metabolic process
  • methylation
  • ncRNA metabolic process
  • one-carbon metabolic process
  • rRNA metabolic process
  • rRNA methylation
  • rRNA modification
  • rRNA processing
Component
Enzyme 82 General Function Involved in methyltransferase activity
Enzyme 82 Specific Function Probable methyltransferase
Enzyme 82 Pathways Not Available
Enzyme 82 Reactions Not Available
Enzyme 82 Pfam Domain Function
Enzyme 82 Signals
  • None
Enzyme 82 Transmembrane Regions
  • None
Enzyme 82 Essentiality Not Available
Enzyme 82 GenBank ID Protein 6652820 Link Image
Enzyme 82 UniProtKB/Swiss-Prot ID Q9UI43 Link Image
Enzyme 82 UniProtKB/Swiss-Prot Entry Name RRMJ2_HUMAN Link Image
Enzyme 82 PDB ID Not Available
Enzyme 82 Cellular Location Not Available
Enzyme 82 Gene Sequence >741 bp
ATGGCGGGGTACTTGAAGCTGGTGTGTGTTTCCTTTCAGCGTCAAGGGTTCCACACTGTT
GGGAGTCGCTGCAAGAATCGGACAGGCGCTGAGCACCTGTGGCTGACCCGACATCTCAGG
GACCCATTTGTGAAGGCTGCGAAGGTGGAGAGTTACCGGTGTCGAAGCGCCTTCAAGCTC
CTGGAGGTGAACGAGAGGCACCAGATTCTGCGGCCCGGCCTTCGGGTGTTAGACTGTGGG
GCAGCTCCTGGGGCCTGGAGTCAGGTGGCGGTGCAGAAGGTCAACGCCGCAGGCACAGAT
CCCAGCTCTCCTGTTGGCTTCGTGCTTGGGGTAGATCTTCTTCACATATTCCCCCTGGAA
GGAGCAACTTTTCTGTGCCCTGCTGACGTGACTGACCCGAGAACCTCACAGAGAATCCTC
GAGGTGCTTCCTGGCAGGAGAGCAGATGTGATTCTGAGCGACATGGCGCCCAATGCCACA
GGGTTCCGGGACCTCGATCATGACAGGCTCATCAGCCTGTGCCTGACCCTTCTCAGCGTG
ACCCCAGACATCCTGCAACCTGGGGGGACATTCCTTTGTAAAACCTGGGCTGGAAGTCAA
AGCCGTCGGTTACAGAGGAGACTGACAGAGGAATTCCAGAATGTAAGGATCATCAAACCT
GAAGCCAGCAGGAAAGAGTCATCAGAAGTGTACTTCTTGGCCACACAGTACCACGGAAGG
AAGGGCACTGTGAAGCAGTGA
Enzyme 82 GenBank Gene ID AF093415 Link Image
Enzyme 82 GeneCard ID FTSJ2 Link Image
Enzyme 82 GenAtlas ID FTSJ2 Link Image
Enzyme 82 HGNC ID HGNC:16352 Link Image
Enzyme 82 Chromosome Location 7
Enzyme 82 Locus 7p22
Enzyme 82 SNPs SNPJam Report Link Image
Enzyme 82 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. Ching YP, Zhou HJ, Yuan JG, Qiang BQ, Kung Hf HF, Jin DY: Identification and characterization of FTSJ2, a novel human nucleolar protein homologous to bacterial ribosomal RNA methyltransferase. Genomics. 2002 Jan;79(1):2-6. [PubMed Link Image]
Enzyme 82 Metabolite References Not Available
Enzyme 83 [top]
Enzyme 83 ID 14774
Enzyme 83 Name Putative rRNA methyltransferase 3
Enzyme 83 Synonyms
  1. Protein ftsJ homolog 3
  2. rRNA (uridine-2'-O-)-methyltransferase 3
Enzyme 83 Gene Name FTSJ3
Enzyme 83 Protein Sequence >Putative rRNA methyltransferase 3
MGKKGKVGKSRRDKFYHLAKETGYRSRSAFKLIQLNRRFQFLQKARALLDLCAAPGGWLQ
VAAKFMPVSSLIVGVDLVPIKPLPNVVTLQQDITTERCRQALRKELKTWKVDVVLNDGAP
NVGASWVHDAYSQAHLTLMALRLACDFLARGGSFITKVFRSRDYQPLLWIFQQLFRRVQA
TKPQASRHESAEIFVVCQGFLAPDKVDSKFFDPKFAFKEVEVQAKTVTELVTKKKPKAEG
YAEGDLTLYHRTSVTDFLRAANPVDFLSKASEIMVDDEELAQHPATTEDIRVCCQDIRVL
GRKELRSLLNWRTKLRRYVAKKLKEQAKALDISLSSGEEDEGDEEDSTAGTTKQPSKEEE
EEEEEEQLNQTLAEMKAQEVAELKRKKKKLLREQRKQRERVELKMDLPGVSIADEGETGM
FSLSTIRGHQLLEEVTQGDMSAADTFLSDLPRDDIYVSDVEDDGDDTSLDSDLDPEELAG
VRGHQGLRDQKRMRLTEVQDDKEEEEEENPLLVPLEEKAVLQEEQANLWFSKGSFAGIED
DADEALEISQAQLLFENRRKGRQQQQKQQLPQTPPSCLKTEIMSPLYQDEAPKGTEASSG
TEAATGLEGEEKDGISDSDSSTSSEEEESWEPLRGKKRSRGPKSDDDGFEIVPIEDPAKH
RILDPEGLALGAVIASSKKAKRDLIDNSFNRYTFNEDEGELPEWFVQEEKQHRIRQLPVG
KKEVEHYRKRWREINARPIKKVAEAKARKKRRMLKRLEQTRKKAEAVVNTVDISEREKVA
QLRSLYKKAGLGKEKRHVTYVVAKKGVGRKVRRPAGVRGHFKVVDSRMKKDQRAQQRKEQ
KKKHKRK
Enzyme 83 Number of Residues 847
Enzyme 83 Molecular Weight 96557.7
Enzyme 83 Theoretical pI 8.71
Enzyme 83 GO Classification
Function
  • binding
  • catalytic activity
  • methyltransferase activity
  • nucleic acid binding
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • RNA metabolic process
  • cellular macromolecule metabolic process
  • cellular metabolic process
  • macromolecule metabolic process
  • metabolic process
  • methylation
  • ncRNA metabolic process
  • one-carbon metabolic process
  • rRNA metabolic process
  • rRNA methylation
  • rRNA modification
  • rRNA processing
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 83 General Function Involved in methyltransferase activity
Enzyme 83 Specific Function Probable methyltransferase
Enzyme 83 Pathways Not Available
Enzyme 83 Reactions Not Available
Enzyme 83 Pfam Domain Function
Enzyme 83 Signals
  • None
Enzyme 83 Transmembrane Regions
  • None
Enzyme 83 Essentiality Not Available
Enzyme 83 GenBank ID Protein 194097365 Link Image
Enzyme 83 UniProtKB/Swiss-Prot ID Q8IY81 Link Image
Enzyme 83 UniProtKB/Swiss-Prot Entry Name RRMJ3_HUMAN Link Image
Enzyme 83 PDB ID Not Available
Enzyme 83 Cellular Location Not Available
Enzyme 83 Gene Sequence >2544 bp
ATGGGCAAGAAGGGCAAAGTTGGCAAGAGCCGACGAGACAAGTTTTATCACTTGGCGAAG
GAGACGGGTTACCGTTCCCGATCTGCTTTCAAGCTGATCCAGCTCAATCGCCGCTTTCAG
TTCCTGCAGAAAGCCCGAGCCTTGCTGGACCTGTGTGCTGCGCCAGGGGGATGGCTGCAG
GTAGCTGCCAAGTTTATGCCTGTATCCAGCCTTATTGTGGGAGTGGACCTGGTTCCAATC
AAGCCTCTCCCCAATGTGGTGACTCTCCAGCAGGACATCACAACAGAACGTTGTAGGCAG
GCCCTGAGGAAGGAGCTGAAGACCTGGAAGGTTGATGTTGTGCTCAATGATGGGGCCCCC
AACGTTGGGGCTAGCTGGGTCCATGATGCTTACTCACAAGCCCATTTGACACTGATGGCT
CTACGTTTGGCTTGTGACTTTTTGGCCCGTGGTGGCAGCTTCATCACAAAGGTTTTCCGT
TCTCGTGACTATCAGCCTCTGCTATGGATCTTTCAGCAGCTGTTCCGCCGTGTCCAGGCC
ACCAAGCCCCAAGCCTCTCGCCATGAATCTGCAGAGATCTTTGTAGTCTGCCAAGGATTC
CTGGCCCCTGACAAGGTTGACAGTAAATTCTTTGACCCCAAATTTGCCTTTAAGGAGGTT
GAAGTTCAGGCTAAGACCGTTACTGAATTGGTTACTAAGAAGAAGCCAAAGGCTGAAGGC
TATGCTGAGGGTGACCTCACTCTCTATCACCGTACCTCAGTCACTGACTTCCTCCGAGCT
GCCAACCCTGTTGACTTCCTCTCCAAGGCCAGCGAAATCATGGTAGATGATGAAGAGTTG
GCACAGCATCCAGCTACCACTGAGGACATACGGGTGTGCTGTCAGGACATCAGAGTGTTG
GGGCGCAAGGAGCTCAGGTCGCTACTAAACTGGAGAACAAAACTTCGGCGATATGTGGCC
AAGAAGCTGAAAGAACAAGCAAAGGCACTGGACATCAGCCTCAGCTCTGGAGAGGAAGAT
GAAGGTGATGAGGAGGACTCAACAGCTGGAACCACAAAGCAGCCCTCTAAGGAGGAGGAG
GAAGAGGAGGAGGAGGAACAACTGAACCAGACCTTGGCAGAAATGAAGGCCCAGGAGGTG
GCGGAATTGAAGAGGAAGAAAAAGAAGCTGTTGCGTGAGCAGAGAAAGCAGCGGGAGCGT
GTGGAGCTGAAGATGGATCTGCCTGGGGTTTCCATTGCAGACGAGGGGGAGACTGGCATG
TTCTCCTTGAGCACCATCCGGGGTCACCAGTTATTAGAGGAAGTAACACAAGGGGATATG
AGTGCAGCAGACACATTTCTGTCCGATCTGCCAAGGGATGATATCTATGTGTCAGATGTT
GAGGACGACGGTGATGACACATCTCTGGATAGTGACCTGGATCCAGAGGAGCTGGCAGGA
GTCAGGGGACATCAGGGTCTAAGGGACCAAAAGCGTATGCGACTTACTGAAGTGCAAGAT
GATAAAGAGGAGGAGGAGGAGGAGAATCCACTGCTGGTACCACTGGAGGAAAAGGCAGTA
CTGCAGGAAGAACAAGCCAACCTGTGGTTCTCAAAGGGCAGCTTTGCTGGGATCGAGGAC
GATGCCGATGAGGCCCTGGAGATCAGTCAGGCCCAGCTGTTATTTGAGAACCGGCGGAAG
GGACGGCAGCAGCAGCAGAAGCAGCAGCTGCCACAGACACCCCCTTCCTGTTTGAAGACT
GAGATAATGTCTCCCCTGTACCAAGATGAAGCCCCTAAGGGAACAGAGGCTTCTTCGGGG
ACAGAAGCTGCCACTGGCCTTGAAGGGGAAGAAAAGGATGGCATCTCAGACAGTGATAGC
AGTACTAGCAGTGAGGAAGAAGAGAGCTGGGAACCCCTCCGTGGTAAGAAGCGAAGCCGT
GGGCCTAAGTCAGATGATGACGGGTTTGAGATAGTGCCTATTGAGGACCCAGCGAAACAT
CGGATACTGGACCCCGAAGGCCTTGCTCTAGGTGCTGTTATTGCCTCTTCCAAAAAGGCC
AAGAGAGACCTCATAGATAACTCCTTCAACCGGTACACATTTAATGAGGATGAGGGGGAG
CTTCCGGAGTGGTTTGTGCAAGAGGAAAAGCAGCACCGGATACGACAGTTGCCTGTTGGT
AAGAAGGAGGTGGAGCATTACCGGAAACGCTGGCGGGAAATCAATGCACGTCCCATCAAG
AAGGTGGCTGAGGCTAAGGCTAGAAAGAAAAGGAGGATGCTGAAGAGGCTGGAGCAGACC
AGGAAGAAGGCAGAAGCCGTGGTGAACACAGTGGACATCTCAGAACGAGAGAAAGTGGCA
CAGCTGCGAAGTCTCTACAAGAAGGCTGGGCTTGGCAAGGAGAAACGCCATGTCACCTAC
GTTGTAGCCAAAAAAGGTGTGGGCCGCAAAGTGCGCCGGCCAGCTGGAGTCAGAGGTCAT
TTCAAGGTGGTGGACTCAAGGATGAAGAAGGACCAAAGAGCACAGCAACGTAAGGAACAA
AAGAAAAAACACAAACGGAAGTAA
Enzyme 83 GenBank Gene ID NM_017647.3 Link Image
Enzyme 83 GeneCard ID FTSJ3 Link Image
Enzyme 83 GenAtlas ID FTSJ3 Link Image
Enzyme 83 HGNC ID HGNC:17136 Link Image
Enzyme 83 Chromosome Location 1
Enzyme 83 Locus 17q23.3
Enzyme 83 SNPs SNPJam Report Link Image
Enzyme 83 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. 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]
  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. Scherl A, Coute Y, Deon C, Calle A, Kindbeiter K, Sanchez JC, Greco A, Hochstrasser D, Diaz JJ: Functional proteomic analysis of human nucleolus. Mol Biol Cell. 2002 Nov;13(11):4100-9. [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. 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]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
  12. 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]
  13. 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]
  14. 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]
  15. 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 83 Metabolite References Not Available
Enzyme 84 [top]
Enzyme 84 ID 14775
Enzyme 84 Name Radical S-adenosyl methionine domain-containing protein 1, mitochondrial
Enzyme 84 Synonyms
  1. Oxygen-independent coproporphyrinogen-III oxidase-like protein RSAD1
Enzyme 84 Gene Name RSAD1
Enzyme 84 Protein Sequence >Radical S-adenosyl methionine domain-containing protein 1, mitochondrial
MALPGARARGWAAAARAAQRRRRVENAGGSPSPEPAGRRAALYVHWPYCEKRCSYCNFNK
YIPRRLEEAAMQKCLVTEAQTLLRLSGVQRVESVFFGGGTPSLASPHTVAAVLEAVAQAA
HLPADLEVTLEANPTSAPGSRLAEFGAAGVNRLSIGLQSLDDTELRLLGRTHSACDALRT
LAEARRLFPGRVSVDLMLGLPAQQVGPWLGQLQELLHHCDDHLSLYQLSLERGTALFAQV
QRGALPAPDPELAAEMYQRGRAVLREAGFHQYEVSNFARNGALSTHNWTYWQCGQYLGVG
PGAHGRFMPQGAGGHTREARIQTLEPDNWMKEVMLFGHGTRKRVPLGRLELLEEVLALGL
RTDVGITHQHWQQFEPQLTLWDVFGANKEVQELLERGLLQLDHRGLRCSWEGLAVLDSLL
LTLLPQLQEAWQQRTPSPVPGG
Enzyme 84 Number of Residues 442
Enzyme 84 Molecular Weight 48713.1
Enzyme 84 Theoretical pI 7.84
Enzyme 84 GO Classification
Function
  • binding
  • catalytic activity
  • coproporphyrinogen oxidase activity
  • iron-sulfur cluster binding
  • metal cluster binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
Process
  • metabolic process
  • nitrogen compound metabolic process
  • oxidation reduction
  • porphyrin biosynthetic process
  • porphyrin metabolic process
  • tetrapyrrole metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 84 General Function Involved in coproporphyrinogen oxidase activity
Enzyme 84 Specific Function May be involved in porphyrin cofactor biosynthesis
Enzyme 84 Pathways Not Available
Enzyme 84 Reactions Not Available
Enzyme 84 Pfam Domain Function
Enzyme 84 Signals
  • None
Enzyme 84 Transmembrane Regions
  • None
Enzyme 84 Essentiality Not Available
Enzyme 84 GenBank ID Protein Not Available
Enzyme 84 UniProtKB/Swiss-Prot ID Q9HA92 Link Image
Enzyme 84 UniProtKB/Swiss-Prot Entry Name RSAD1_HUMAN Link Image
Enzyme 84 PDB ID Not Available
Enzyme 84 Cellular Location Not Available
Enzyme 84 Gene Sequence >1329 bp
ATGGCGCTCCCCGGAGCCCGGGCTCGCGGCTGGGCGGCAGCAGCCAGAGCGGCCCAGAGG
CGCCGCCGCGTGGAGAACGCAGGAGGGTCCCCGAGTCCTGAGCCTGCGGGCCGGCGCGCG
GCGCTTTACGTACACTGGCCTTACTGCGAGAAGCGCTGCAGTTACTGCAACTTCAACAAG
TACATCCCTCGCCGCCTGGAGGAGGCTGCCATGCAGAAGTGTCTGGTGACCGAAGCTCAG
ACGCTGCTGCGGCTCAGCGGGGTGCAACGGGTGGAGTCTGTGTTCTTTGGTGGGGGGACC
CCCAGTCTAGCCAGTCCCCACACGGTGGCTGCTGTCCTGGAGGCTGTGGCACAGGCAGCC
CACCTGCCTGCAGACTTGGAAGTCACATTGGAGGCTAATCCTACTTCAGCTCCGGGCTCC
AGACTGGCAGAGTTCGGGGCAGCAGGGGTTAACAGGTTGTCTATAGGCCTCCAGTCCCTA
GATGACACTGAGCTCCGGCTGTTGGGACGGACGCACTCGGCCTGCGATGCTCTGCGGACG
CTGGCAGAGGCCCGGCGCCTCTTTCCCGGGCGCGTGTCTGTAGACTTGATGCTGGGGCTG
CCGGCACAGCAGGTGGGGCCGTGGCTTGGGCAGCTGCAGGAACTGCTGCACCACTGTGAT
GACCACCTCTCCCTCTACCAGCTGTCCCTGGAGCGGGGCACCGCACTCTTCGCCCAGGTG
CAGCGGGGTGCCCTTCCAGCCCCTGACCCGGAGCTCGCAGCTGAGATGTACCAGAGGGGC
CGGGCTGTCCTTCGGGAGGCTGGCTTCCACCAGTATGAGGTCTCCAACTTTGCCCGGAAT
GGGGCGCTCAGTACCCACAATTGGACTTACTGGCAGTGTGGTCAGTACCTTGGCGTTGGG
CCTGGGGCCCATGGACGATTTATGCCCCAGGGGGCTGGAGGCCACACCCGGGAGGCTCGG
ATCCAGACACTGGAGCCTGACAACTGGATGAAGGAGGTGATGCTGTTTGGCCATGGCACC
CGGAAGCGTGTCCCCCTGGGCAGGCTGGAGCTGCTGGAGGAAGTTTTGGCCCTGGGGCTA
CGCACCGATGTGGGGATCACTCACCAGCACTGGCAGCAGTTTGAGCCCCAGCTGACCCTG
TGGGATGTGTTTGGAGCGAACAAGGAGGTGCAGGAGCTGCTGGAGCGGGGCCTACTGCAG
CTGGATCACAGGGGTCTTCGGTGTTCCTGGGAGGGTCTGGCTGTGCTGGACTCTCTCTTG
CTGACCCTCCTGCCTCAGCTCCAAGAAGCCTGGCAGCAGAGAACCCCCTCCCCTGTGCCA
GGAGGATGA
Enzyme 84 GenBank Gene ID AK002026 Link Image
Enzyme 84 GeneCard ID RSAD1 Link Image
Enzyme 84 GenAtlas ID RSAD1 Link Image
Enzyme 84 HGNC ID HGNC:25634 Link Image
Enzyme 84 Chromosome Location 1
Enzyme 84 Locus 17q21.33
Enzyme 84 SNPs SNPJam Report Link Image
Enzyme 84 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. 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 84 Metabolite References Not Available
Enzyme 85 [top]
Enzyme 85 ID 14776
Enzyme 85 Name Histone-lysine N-methyltransferase SETD1B
Enzyme 85 Synonyms
  1. Lysine N-methyltransferase 2G
  2. SET domain-containing protein 1B
  3. hSET1B
Enzyme 85 Gene Name SETD1B
Enzyme 85 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 85 Number of Residues 1923
Enzyme 85 Molecular Weight 208729.7
Enzyme 85 Theoretical pI 4.59
Enzyme 85 GO Classification
Function
  • binding
  • nucleic acid binding
  • nucleotide binding
Process
Component
Enzyme 85 General Function Involved in nucleotide binding
Enzyme 85 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 85 Pathways Not Available
Enzyme 85 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 85 Pfam Domain Function
Enzyme 85 Signals
  • None
Enzyme 85 Transmembrane Regions
  • None
Enzyme 85 Essentiality Not Available
Enzyme 85 GenBank ID Protein 210032580 Link Image
Enzyme 85 UniProtKB/Swiss-Prot ID Q9UPS6 Link Image
Enzyme 85 UniProtKB/Swiss-Prot Entry Name SET1B_HUMAN Link Image
Enzyme 85 PDB ID Not Available
Enzyme 85 Cellular Location Not Available
Enzyme 85 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 85 GenBank Gene ID NM_015048.1 Link Image
Enzyme 85 GeneCard ID SETD1B Link Image
Enzyme 85 GenAtlas ID SETD1B Link Image
Enzyme 85 HGNC ID HGNC:29187 Link Image
Enzyme 85 Chromosome Location 1
Enzyme 85 Locus 12q24.31
Enzyme 85 SNPs SNPJam Report Link Image
Enzyme 85 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 85 Metabolite References Not Available
Enzyme 86 [top]
Enzyme 86 ID 14777
Enzyme 86 Name Histone-lysine N-methyltransferase SETD2
Enzyme 86 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 86 Gene Name SETD2
Enzyme 86 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 86 Number of Residues 2564
Enzyme 86 Molecular Weight 287594.2
Enzyme 86 Theoretical pI 6.02
Enzyme 86 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 86 General Function Involved in histone-lysine N-methyltransferase activity
Enzyme 86 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 86 Pathways
Enzyme 86 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 86 Pfam Domain Function
Enzyme 86 Signals
  • None
Enzyme 86 Transmembrane Regions
  • None
Enzyme 86 Essentiality Not Available
Enzyme 86 GenBank ID Protein 197313748 Link Image
Enzyme 86 UniProtKB/Swiss-Prot ID Q9BYW2 Link Image
Enzyme 86 UniProtKB/Swiss-Prot Entry Name SETD2_HUMAN Link Image
Enzyme 86 PDB ID Not Available
Enzyme 86 Cellular Location Not Available
Enzyme 86 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 86 GenBank Gene ID NM_014159.6 Link Image
Enzyme 86 GeneCard ID SETD2 Link Image
Enzyme 86 GenAtlas ID SETD2 Link Image
Enzyme 86 HGNC ID HGNC:18420 Link Image
Enzyme 86 Chromosome Location 3
Enzyme 86 Locus 3p21.31
Enzyme 86 SNPs SNPJam Report Link Image
Enzyme 86 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 86 Metabolite References Not Available
Enzyme 87 [top]
Enzyme 87 ID 14778
Enzyme 87 Name Histone-lysine N-methyltransferase SETMAR
Enzyme 87 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 87 Gene Name SETMAR
Enzyme 87 Protein Sequence >Histone-lysine N-methyltransferase SETMAR
MAEFKEKPEAPTEQLDVACGQENLPVGAWPPGAAPAPFQYTPDHVVGPGADIDPTQITFP
GCICVKTPCLPGTCSCLRHGENYDDNSCLRDIGSGGKYAEPVFECNVLCRCSDHCRNRVV
QKGLQFHFQVFKTHKKGWGLRTLEFIPKGRFVCEYAGEVLGFSEVQRRIHLQTKSDSNYI
IAIREHVYNGQVMETFVDPTYIGNIGRFLNHSCEPNLLMIPVRIDSMVPKLALFAAKDIV
PEEELSYDYSGRYLNLTVSEDKERLDHGKLRKPCYCGAKSCTAFLPFDSSLYCPVEKSNI
SCGNEKEPSMCGSAPSVFPSCKRLTLETMKMMLDKKQIRAIFLFEFKMGRKAAETTRNIN
NAFGPGTANERTVQWWFKKFCKGDESLEDEERSGRPSEVDNDQLRAIIEADPLTTTREVA
EELNVNHSTVVRHLKQIGKVKKLDKWVPHELTENQKNRRFEVSSSLILRNHNEPFLDRIV
TCDEKWILYDNRRRSAQWLDQEEAPKHFPKPILHPKKVMVTIWWSAAGLIHYSFLNPGET
ITSEKYAQEIDEMNQKLQRLQLALVNRKGPILLHDNARPHVAQPTLQKLNELGYEVLPHP
PYSPDLLPTNYHVFKHLNNFLQGKRFHNQQDAENAFQEFVESQSTDFYATGINQLISRWQ
KCVDCNGSYFD
Enzyme 87 Number of Residues 671
Enzyme 87 Molecular Weight 76668.7
Enzyme 87 Theoretical pI 7.05
Enzyme 87 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 87 General Function Involved in zinc ion binding
Enzyme 87 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 87 Pathways
Enzyme 87 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 87 Pfam Domain Function
Enzyme 87 Signals
  • None
Enzyme 87 Transmembrane Regions
  • None
Enzyme 87 Essentiality Not Available
Enzyme 87 GenBank ID Protein 62897027 Link Image
Enzyme 87 UniProtKB/Swiss-Prot ID Q53H47 Link Image
Enzyme 87 UniProtKB/Swiss-Prot Entry Name SETMR_HUMAN Link Image
Enzyme 87 PDB ID Not Available
Enzyme 87 Cellular Location Not Available
Enzyme 87 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 87 GenBank Gene ID AK222734 Link Image
Enzyme 87 GeneCard ID SETMAR Link Image
Enzyme 87 GenAtlas ID SETMAR Link Image
Enzyme 87 HGNC ID HGNC:10762 Link Image
Enzyme 87 Chromosome Location 3
Enzyme 87 Locus 3p26.1
Enzyme 87 SNPs SNPJam Report Link Image
Enzyme 87 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 87 Metabolite References Not Available
Enzyme 88 [top]
Enzyme 88 ID 14779
Enzyme 88 Name SET and MYND domain-containing protein 3
Enzyme 88 Synonyms
  1. Zinc finger MYND domain-containing protein 1
Enzyme 88 Gene Name SMYD3
Enzyme 88 Protein Sequence >SET and MYND domain-containing protein 3
MEPLKVEKFATAKRGNGLRAVTPLRPGELLFRSDPLAYTVCKGSRGVVCDRCLLGKEKLM
RCSQCRVAKYCSAKCQKKAWPDHKRECKCLKSCKPRYPPDSVRLLGRVVFKLMDGAPSES
EKLYSFYDLESNINKLTEDKKEGLRQLVMTFQHFMREEIQDASQLPPAFDLFEAFAKVIC
NSFTICNAEMQEVGVGLYPSISLLNHSCDPNCSIVFNGPHLLLRAVRDIEVGEELTICYL
DMLMTSEERRKQLRDQYCFECDCFRCQTQDKDADMLTGDEQVWKEVQESLKKIEELKAHW
KWEQVLAMCQAIISSNSERLPDINIYQLKVLDCAMDACINLGLLEEALFYGTRTMEPYRI
FFPGSHPVRGVQVMKVGKLQLHQGMFPQAMKNLRLAFDIMRVTHGREHSLIEDLILLLEE
CDANIRAS
Enzyme 88 Number of Residues 428
Enzyme 88 Molecular Weight 49096.7
Enzyme 88 Theoretical pI 7.27
Enzyme 88 GO Classification
Function
  • binding
  • cation binding
  • ion binding
  • metal ion binding
  • transition metal ion binding
  • zinc ion binding
Process
Component
Enzyme 88 General Function Involved in zinc ion binding
Enzyme 88 Specific Function Histone methyltransferase. Specifically methylates 'Lys- 4' of histone H3, inducing di- and tri-methylation, but not monomethylation. Plays an important role in transcriptional activation as a member of an RNA polymerase complex. Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences
Enzyme 88 Pathways
Enzyme 88 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 88 Pfam Domain Function
Enzyme 88 Signals
  • None
Enzyme 88 Transmembrane Regions
  • None
Enzyme 88 Essentiality Not Available
Enzyme 88 GenBank ID Protein 19570495 Link Image
Enzyme 88 UniProtKB/Swiss-Prot ID Q9H7B4 Link Image
Enzyme 88 UniProtKB/Swiss-Prot Entry Name SMYD3_HUMAN Link Image
Enzyme 88 PDB ID Not Available
Enzyme 88 Cellular Location Not Available
Enzyme 88 Gene Sequence >1287 bp
ATGGAGCCGCTGAAGGTGGAAAAGTTCGCAACCGCCAACAGGGGAAACGGGCTGCGCGCC
GTGACCCCGCTGCGCCCCGGAGAGCTACTCTTCCGCTCGGATCCCTTGGCGTACACGGTG
TGCAAGGGGAGTCGTGGCGTCGTCTGCGACCGCTGCCTTCTCGGGAAGGAAAAGCTGATG
CGATGCTCTCAGTGCCGCGTCGCCAAATACTGTAGTGCTAAGTGTCAGAAAAAAGCTTGG
CCAGACCACAAGCGGGAATGCAAATGCCTTAAAAGCTGCAAACCCAGATATCCTCCAGAC
TCCGTTCGACTTCTTGGCAGAGTTGTCTTCAAACTTATGGATGGAGCACCTTCAGAATCA
GAGAAGCTTTACTCATTTTATGATCTGGAGTCAAATATTAACAAACTGACTGAAGATAAG
AAAGAGGGCCTCAGGCAACTCGTAATGACATTTCAACATTTCATGAGAGAAGAAATACAG
GATGCCTCTCAGCTGCCACCTGCCTTTGACCTTTTTGAAGCCTTTGCAAAAGTGATCTGC
AACTCTTTCACCATCTGTAATGCGGAGATGCAGGAAGTTGGTGTTGGCCTATATCCCAGT
ATCTCTTTGCTCAATCACAGCTGTGACCCCAACTGTTCGATTGTGTTCAATGGGCCCCAC
CTCTTACTGCGAGCAGTCCGAGACATCGAGGTGGGAGAGGAGCTCACCATCTGCTACCTG
GATATGCTGATGACCAGTGAGGAGCGCCGGAAGCAGCTGAGGGACCAGTACTGCTTTGAA
TGTGACTGTTTCCGTTGCCAAACCCAGGACAAGGATGCTGATATGCTAACTGGTGATGAG
CAAGTATGGAAGGAAGTTCAAGAATCCCTGAAAAAAATTGAAGAACTGAAGGCACACTGG
AAGTGGGAGCAGGTTCTGGCCATGTGCCAGGCAATCATAAGCAGCAATTCTGAACGGCTT
CCCGATATCAACATCTACCAGCTGAAGGTGCTCGACTGCGCCATGGATGCCTGCATCAAC
CTCGGCCTGTTGGAGGAAGCCTTGTTCTATGGTACTCGGACCATGGAGCCATACAGGATT
TTTTTCCCAGGAAGCCATCCCGTCAGAGGGGTTCAAGTGATGAAAGTTGGCAAACTGCAG
CTACATCAAGGCATGTTTCCCCAAGCAATGAAGAATCTGAGACTGGCTTTTGATATTATG
AGAGTGACACATGGCAGAGAACACAGCCTGATTGAAGATTTGATTCTACTTTTAGAAGAA
TGCGACGCCAACATCAGAGCATCCTAA
Enzyme 88 GenBank Gene ID AB057595 Link Image
Enzyme 88 GeneCard ID SMYD3 Link Image
Enzyme 88 GenAtlas ID SMYD3 Link Image
Enzyme 88 HGNC ID HGNC:15513 Link Image
Enzyme 88 Chromosome Location 1
Enzyme 88 Locus 1q44
Enzyme 88 SNPs SNPJam Report Link Image
Enzyme 88 General References
  1. Hamamoto R, Furukawa Y, Morita M, Iimura Y, Silva FP, Li M, Yagyu R, Nakamura Y: SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells. Nat Cell Biol. 2004 Aug;6(8):731-40. Epub 2004 Jul 4. [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. 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]
Enzyme 88 Metabolite References Not Available
Enzyme 89 [top]
Enzyme 89 ID 14780
Enzyme 89 Name Histone-lysine N-methyltransferase SUV420H1
Enzyme 89 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 89 Gene Name SUV420H1
Enzyme 89 Protein Sequence >Histone-lysine N-methyltransferase SUV420H1
MKWLGESKIMVVNGRRNGGKLSNDHQQNQSKLQHTGKDTLKAGKNAVERRSNRCNGNSGF
EGQSRYVPSSGMSAKELCENDDLATSLVLDPYLGFQTHKMNTSAFPSRSSRHFSKSDSFS
HNNPVRFRPIKGRQEELKEVIERFKKDEHLEKAFKCLTSGEWARHYFLNKNKMQEKLFKE
HVFIYLRMFATDSGFEILPCNRYSSEQNGAKIVATKEWKRNDKIELLVGCIAELSEIEEN
MLLRHGENDFSVMYSTRKNCAQLWLGPAAFINHDCRPNCKFVSTGRDTACVKALRDIEPG
EEISCYYGDGFFGENNEFCECYTCERRGTGAFKSRVGLPAPAPVINSKYGLRETDKRLNR
LKKLGDSSKNSDSQSVSSNTDADTTQEKNNATSNRKSSVGVKKNSKSRTLTRQSMSRIPA
SSNSTSSKLTHINNSRVPKKLKKPAKPLLSKIKLRNHCKRLEQKNASRKLEMGNLVLKEP
KVVLYKNLPIKKDKEPEGPAQAAVASGCLTRHAAREHRQNPVRGAHSQGESSPCTYITRR
SVRTRTNLKEASDIKLEPNTLNGYKSSVTEPCPDSGEQLQPAPVLQEEELAHETAQKGEA
KCHKSDTGMSKKKSRQGKLVKQFAKIEESTPVHDSPGKDDAVPDLMGPHSDQGEHSGTVG
VPVSYTDCAPSPVGCSVVTSDSFKTKDSFRTAKSKKKRRITRYDAQLILENNSGIPKLTL
RRRHDSSSKTNDQENDGMNSSKISIKLSKDHDNDNNLYVAKLNNGFNSGSGSSSTKLKIQ
LKRDEENRGSYTEGLHENGVCCSDPLSLLESRMEVDDYSQYEEESTDDSSSSEGDEEEDD
YDDDFEDDFIPLPPAKRLRLIVGKDSIDIDISSRRREDQSLRLNA
Enzyme 89 Number of Residues 885
Enzyme 89 Molecular Weight 99186.1
Enzyme 89 Theoretical pI 9.05
Enzyme 89 GO Classification Not Available
Enzyme 89 General Function Involved in protein binding
Enzyme 89 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 89 Pathways
Enzyme 89 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 89 Pfam Domain Function
Enzyme 89 Signals
  • None
Enzyme 89 Transmembrane Regions
  • None
Enzyme 89 Essentiality Not Available
Enzyme 89 GenBank ID Protein 50659082 Link Image
Enzyme 89 UniProtKB/Swiss-Prot ID Q4FZB7 Link Image
Enzyme 89 UniProtKB/Swiss-Prot Entry Name SV421_HUMAN Link Image
Enzyme 89 PDB ID Not Available
Enzyme 89 Cellular Location Not Available
Enzyme 89 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 89 GenBank Gene ID NM_017635.3 Link Image
Enzyme 89 GeneCard ID SUV420H1 Link Image
Enzyme 89 GenAtlas ID SUV420H1 Link Image
Enzyme 89 HGNC ID HGNC:24283 Link Image
Enzyme 89 Chromosome Location 1
Enzyme 89 Locus 11q13.2
Enzyme 89 SNPs SNPJam Report Link Image
Enzyme 89 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 89 Metabolite References Not Available
Enzyme 90 [top]
Enzyme 90 ID 14781
Enzyme 90 Name Histone-lysine N-methyltransferase SUV420H2
Enzyme 90 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 90 Gene Name SUV420H2
Enzyme 90 Protein Sequence >Histone-lysine N-methyltransferase SUV420H2
MGPDRVTARELCENDDLATSLVLDPYLGFRTHKMNVSPVPPLRRQQHLRSALETFLRQRD
LEAAYRALTLGGWTARYFQSRGPRQEAALKTHVYRYLRAFLPESGFTILPCTRYSMETNG
AKIVSTRAWKKNEKLELLVGCIAELREADEGLLRAGENDFSIMYSTRKRSAQLWLGPAAF
INHDCKPNCKFVPADGNAACVKVLRDIEPGDEVTCFYGEGFFGEKNEHCECHTCERKGEG
AFRTRPREPALPPRPLDKYQLRETKRRLQQGLDSGSRQGLLGPRACVHPSPLRRDPFCAA
CQPLRLPACSARPDTSPLWLQWLPQPQPRVRPRKRRRPRPRRAPVLSTHHAARVSLHRWG
GCGPHCRLRGEALVALGQPPHARWAPQQDWHWARRYGLPYVVRVDLRRLAPAPPATPAPA
GTPGPILIPKQALAFAPFSPPKRLRLVVSHGSIDLDVGGEEL
Enzyme 90 Number of Residues 462
Enzyme 90 Molecular Weight 52112.4
Enzyme 90 Theoretical pI 10.31
Enzyme 90 GO Classification Not Available
Enzyme 90 General Function Involved in protein binding
Enzyme 90 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 90 Pathways
Enzyme 90 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 90 Pfam Domain Function
Enzyme 90 Signals
  • None
Enzyme 90 Transmembrane Regions
  • None
Enzyme 90 Essentiality Not Available
Enzyme 90 GenBank ID Protein 31543169 Link Image
Enzyme 90 UniProtKB/Swiss-Prot ID Q86Y97 Link Image
Enzyme 90 UniProtKB/Swiss-Prot Entry Name SV422_HUMAN Link Image
Enzyme 90 PDB ID Not Available
Enzyme 90 Cellular Location Not Available
Enzyme 90 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 90 GenBank Gene ID NM_032701.3 Link Image
Enzyme 90 GeneCard ID SUV420H2 Link Image
Enzyme 90 GenAtlas ID SUV420H2 Link Image
Enzyme 90 HGNC ID HGNC:28405 Link Image
Enzyme 90 Chromosome Location 1
Enzyme 90 Locus 19q13.42
Enzyme 90 SNPs SNPJam Report Link Image
Enzyme 90 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 90 Metabolite References Not Available
Enzyme 91 [top]
Enzyme 91 ID 14782
Enzyme 91 Name Probable methyltransferase TARBP1
Enzyme 91 Synonyms
  1. TAR RNA-binding protein 1
  2. TAR RNA-binding protein of 185 kDa
  3. TRP-185
Enzyme 91 Gene Name TARBP1
Enzyme 91 Protein Sequence >Probable methyltransferase TARBP1
MEWVLAEALLSQSRDPRALLGALCQGEASAERVETLRFLLQRLEDEEARGSGGAGALPEA
AREVAAGYLVPLLRSLRGRPAGGPDPSLQPRHRRRVLRAAGAALRSCVRLAGRPQLAAAL
AEEALRDLLAGWRAPGAEAAVEVLAAVGPCLRPREDGPLLERVAGTAVALALGGGGDGDE
AGPAEDAAALVAGRLLPVLVQCGGAALRAVWGGLAAPGASLGSGRVEEKLLVLSALAEKL
LPEPGGDRARGAREAGPDARRCWRFWRTVQAGLGQADALTRKRARYLLQRAVEVSAELGA
DCTCGPQEGNGPSLFWWSERKKDELLKFWENYILIMETLEGNQIHVIKPVLPKLNNLFEY
AVSEENGCWLFHPSWHMCIYKRMFESENKILSKEGVIHFLELYETKILPFSPEFSEFIIG
PLMDALSESSLYSRSPGQPIGSCSPLGLKLQKFLVTYISLLPEEIKSSFLLKFIRKMTSR
HWCAVPILFLSKALANVPRHKALGIDGLLALRDVIHCTMITHQILLRGAAQCYLLQTAMN
LLDVEKVSLSDVSTFLMSLRQEESLGRGTSLWTELCDWLRVNESYFKPSPTCSSIGLHKT
SLNAYVKSIVQEYVKSSAWETGENCFMPDWFEAKLVSLMVLLAVDVEGMKTQYSGKQRTE
NVLRIFLDPLLDVLMKFSTNAYMPLLKTDRCLQLLLKLLNTCRLKGSSAQDDEVSTVLQN
FFMSTTESISEFILRRLTMNELNSVSDLDRCHLYLMVLTELINLHLKVGWKRGNPIWRVI
SLLKNASIQHLQEMDSGQEPTVGSQIQRVVSMAALAMVCEAIDQKPELQLDSLHAGPLES
FLSSLQLNQTLQKPHAEEQSSYAHPLECSSVLEESSSSQGWGKIVAQYIHDQWVCLSFLL
KKYHTLIPTTGSEILEPFLPAVQMPIRTLQSALEALTVLSSDQVLPVFHCLKVLVPKLLT
SSESLCIESFDMAWKIISSLSNTQLIFWANLKAFVQFVFDNKVLTIAAKIKGQAYFKIKE
IMYKIIEMSAIKTGVFNTLISYCCQSWIVSASNVSQGSLSSAKNYSELILEACIFGTVFR
RDQRLVQDVQTFIENLGHDCAANIVMENTKREDHYVRICAVKFLCLLDGSNMSHKLFIED
LAIKLLDKDELVSKSKKRYYVNSLQHRVKNRVWQTLLVLFPRLDQNFLNGIIDRIFQAGF
TNNQASIKYFIEWIIILILHKFPQFLPKFWDCFSYGEENLKTSICTFLAVLSHLDIITQN
IPEKKLILKQALIVVLQWCFNHNFSVRLYALVALKKLWTVCKVLSVEEFDALTPVIESSL
HQVESMHGAGNAKKNWQRIQEHFFFATFHPLKDYCLETIFYILPRLSGLIEDEWITIDKF
TRFTDVPLAAGFQWYLSQTQLSKLKPGDWSQQDIGTNLVEADNQAEWTDVQKKIIPWNSR
VSDLDLELLFQDRAARLGKSISRLIVVASLIDKPTNLGGLCRTCEVFGASVLVVGSLQCI
SDKQFQHLSVSAEQWLPLVEVKPPQLIDYLQQKKTEGYTIIGVEQTAKSLDLTQYCFPEK
SLLLLGNEREGIPANLIQQLDVCVEIPQQGIIRSLNVHVSGALLIWEYTRQQLLSHGDTK
P
Enzyme 91 Number of Residues 1621
Enzyme 91 Molecular Weight 181672.8
Enzyme 91 Theoretical pI 7.05
Enzyme 91 GO Classification
Function
  • RNA binding
  • RNA methyltransferase activity
  • binding
  • catalytic activity
  • methyltransferase activity
  • nucleic acid binding
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • RNA metabolic process
  • RNA processing
  • cellular macromolecule metabolic process
  • macromolecule metabolic process
  • metabolic process
Component
Enzyme 91 General Function Involved in binding
Enzyme 91 Specific Function Probable S-adenosyl-L-methionine-dependent methyltransferase which methylates RNA molecules such as tRNAs. In case of infection by HIV-1, it binds to the loop region of TAR RNA, a region also bound by RNA polymerase II. Binding of TARBP1 and RNA polymerase II to HIV-1 TAR RNA is mutually exclusive, suggesting that TARBP1 may function alone or in conjunction with HIV-1 Tat to disengage RNA polymerase II from HIV-1 TAR RNA. May act by methylating HIV-1 TAR RNA
Enzyme 91 Pathways Not Available
Enzyme 91 Reactions Not Available
Enzyme 91 Pfam Domain Function
Enzyme 91 Signals
  • None
Enzyme 91 Transmembrane Regions
  • None
Enzyme 91 Essentiality Not Available
Enzyme 91 GenBank ID Protein 56204383 Link Image
Enzyme 91 UniProtKB/Swiss-Prot ID Q13395 Link Image
Enzyme 91 UniProtKB/Swiss-Prot Entry Name TARB1_HUMAN Link Image
Enzyme 91 PDB ID Not Available
Enzyme 91 Cellular Location Not Available
Enzyme 91 Gene Sequence >4866 bp
ATGGAGTGGGTGCTCGCGGAAGCGCTGCTCTCGCAGAGCCGGGACCCCCGGGCCCTGCTT
GGGGCGCTGTGCCAAGGGGAGGCATCCGCGGAGCGCGTGGAGACGCTGCGCTTCCTTCTG
CAGCGGCTCGAGGACGAGGAGGCGCGCGGCAGCGGGGGCGCAGGCGCGCTCCCGGAGGCG
GCGCGCGAGGTGGCTGCAGGGTACCTCGTGCCACTGCTGCGGAGCCTGCGCGGACGCCCC
GCGGGCGGCCCGGACCCCAGTCTGCAGCCTCGCCACCGCCGGCGCGTGCTGAGGGCGGCG
GGCGCGGCCCTGCGCTCGTGCGTCCGCCTGGCCGGGCGTCCGCAGCTGGCGGCCGCGCTG
GCTGAGGAGGCGCTGCGCGATCTGCTCGCCGGGTGGCGCGCGCCTGGCGCCGAGGCTGCC
GTGGAAGTGCTAGCAGCCGTCGGGCCATGTTTGCGGCCCCGCGAGGACGGGCCGCTACTG
GAGCGCGTGGCGGGGACCGCCGTCGCCCTGGCGCTGGGCGGGGGCGGGGACGGGGATGAG
GCCGGGCCTGCCGAGGACGCGGCGGCGCTGGTGGCCGGGCGACTGCTGCCAGTGCTGGTC
CAATGTGGCGGGGCGGCGCTGCGGGCCGTGTGGGGCGGGCTGGCCGCGCCTGGGGCGTCC
CTGGGGTCCGGCCGCGTAGAGGAGAAGCTGCTGGTCCTGAGCGCCCTGGCCGAGAAGCTG
TTGCCCGAGCCCGGCGGCGACCGCGCCCGCGGCGCGCGCGAGGCGGGCCCGGACGCCCGG
CGCTGCTGGCGCTTCTGGAGGACGGTGCAGGCGGGGCTGGGCCAGGCGGACGCCCTGACG
CGCAAGCGAGCGCGCTACCTGCTGCAGAGGGCGGTGGAGGTGTCGGCGGAGCTGGGGGCC
GACTGCACCTGCGGGCCCCAGGAAGGAAACGGCCCAAGTCTGTTTTGGTGGTCTGAGAGG
AAAAAAGATGAGCTTCTAAAGTTTTGGGAAAATTATATTTTAATTATGGAGACTTTAGAA
GGAAATCAGATACATGTTATAAAGCCAGTTTTACCAAAGCTAAACAATCTGTTTGAATAT
GCGGTGTCAGAGGAAAATGGATGTTGGCTCTTTCACCCATCCTGGCATATGTGTATTTAT
AAAAGAATGTTTGAAAGTGAAAACAAAATCCTGTCCAAAGAAGGTGTTATCCATTTTTTG
GAGCTGTATGAAACAAAGATTCTTCCATTTTCACCAGAATTTTCTGAGTTTATTATTGGA
CCATTAATGGATGCGCTTTCAGAGAGCTCTCTGTATAGCAGGTCCCCAGGCCAGCCAATA
GGAAGCTGTTCTCCATTGGGACTGAAATTACAGAAGTTTTTAGTCACTTATATTTCTCTT
CTTCCAGAAGAAATAAAGAGTAGCTTCCTATTGAAGTTTATTCGGAAGATGACAAGTAGG
CATTGGTGTGCTGTTCCCATTTTGTTTCTATCTAAGGCTTTGGCAAATGTCCCAAGACAT
AAGGCCCTGGGTATAGATGGGCTTCTTGCTCTCAGGGATGTTATTCATTGCACTATGATC
ACACATCAGATTCTCCTGAGAGGGGCAGCCCAATGCTACCTTCTTCAAACAGCTATGAAT
TTGCTAGATGTGGAGAAAGTGTCACTTTCTGATGTCTCAACTTTTCTCATGTCTCTGAGA
CAAGAGGAATCCTTAGGACGAGGAACTTCATTGTGGACAGAGCTGTGTGACTGGCTACGT
GTTAATGAAAGCTATTTTAAGCCATCCCCTACGTGTAGCTCCATTGGACTTCACAAGACA
TCTTTAAATGCTTATGTAAAGAGCATTGTTCAAGAGTATGTTAAGTCATCTGCTTGGGAA
ACAGGAGAAAACTGCTTTATGCCTGATTGGTTTGAAGCCAAGCTTGTTTCTCTGATGGTC
TTGCTGGCTGTGGATGTGGAAGGAATGAAGACTCAGTATAGCGGAAAGCAGAGAACAGAG
AATGTATTGCGGATATTCTTAGACCCTCTTCTGGATGTGCTTATGAAGTTTAGTACCAAT
GCCTACATGCCCTTGCTGAAGACTGACAGATGCCTCCAGCTGCTGTTGAAGCTGTTGAAC
ACATGCAGGTTGAAAGGTTCCAGTGCCCAAGATGATGAGGTGTCTACTGTTCTTCAGAAC
TTTTTCATGTCTACTACAGAGAGCATTTCTGAATTTATTCTCAGAAGACTTACTATGAAT
GAGCTAAATAGTGTTTCAGATCTGGATCGTTGCCATTTATACCTGATGGTGTTAACTGAG
CTTATAAATCTGCATTTGAAGGTTGGGTGGAAAAGGGGTAACCCTATCTGGAGAGTTATT
TCTCTTTTGAAAAATGCATCCATTCAGCATCTTCAAGAGATGGACAGTGGACAGGAGCCA
ACAGTTGGAAGTCAGATTCAGAGAGTAGTGAGCATGGCTGCCTTGGCCATGGTGTGTGAG
GCCATAGACCAGAAGCCTGAGCTGCAGCTGGACTCTCTCCATGCTGGGCCCCTGGAAAGC
TTCCTTTCCTCTCTTCAGCTCAATCAGACGCTGCAGAAGCCCCACGCAGAGGAGCAGAGC
AGTTATGCTCACCCCTTGGAGTGCAGCAGTGTTTTGGAAGAATCGTCATCTTCCCAAGGA
TGGGGAAAAATAGTTGCACAATATATTCATGATCAATGGGTGTGCCTCTCTTTCCTGTTG
AAAAAATATCACACCCTTATACCAACCACAGGGAGTGAAATTCTGGAACCGTTTCTACCT
GCCGTTCAGATGCCAATAAGGACTTTGCAGTCTGCACTAGAAGCCCTCACAGTTCTTTCT
TCTGATCAAGTTTTACCAGTGTTCCATTGCTTGAAAGTGTTGGTTCCCAAGCTTCTGACT
TCCTCTGAATCACTCTGCATAGAGTCTTTTGACATGGCGTGGAAAATTATATCTTCTTTA
AGCAACACTCAGCTGATATTCTGGGCTAATTTAAAAGCTTTTGTTCAGTTTGTTTTTGAT
AACAAAGTTCTTACCATTGCTGCCAAAATCAAGGGCCAGGCATATTTCAAAATAAAAGAG
ATTATGTACAAGATAATTGAAATGTCTGCTATAAAGACTGGAGTCTTCAATACACTGATA
AGTTACTGCTGTCAGTCTTGGATAGTGTCTGCTTCAAATGTGTCCCAAGGATCTTTATCA
AGTGCTAAAAATTATAGCGAACTTATCCTTGAGGCTTGTATATTTGGAACTGTGTTTAGG
CGTGATCAAAGACTTGTTCAGGATGTACAGACCTTCATAGAAAACCTTGGACATGACTGT
GCGGCAAATATTGTTATGGAAAATACTAAGAGAGAAGACCATTATGTGAGAATTTGTGCT
GTCAAATTCCTGTGTTTATTAGATGGCTCCAATATGTCCCACAAGTTGTTTATTGAGGAT
CTTGCAATCAAGCTATTAGATAAAGATGAATTAGTGTCCAAGTCCAAAAAACGCTACTAT
GTGAATTCTCTACAGCACAGAGTGAAAAACCGAGTGTGGCAGACTCTGCTGGTACTTTTC
CCTAGACTTGACCAGAATTTCTTGAATGGAATTATTGACAGGATTTTCCAGGCTGGTTTC
ACCAACAATCAAGCATCCATAAAATATTTTATAGAATGGATTATTATATTGATTCTTCAT
AAATTCCCTCAATTTCTTCCAAAGTTCTGGGATTGTTTTTCTTATGGTGAAGAAAATCTT
AAAACAAGCATTTGTACGTTTTTAGCAGTTTTATCACATTTAGACATTATTACTCAAAAT
ATTCCAGAAAAGAAACTAATTCTGAAGCAAGCCCTTATAGTTGTGCTGCAGTGGTGTTTC
AATCACAATTTTAGTGTTCGACTGTATGCTTTAGTTGCTCTTAAGAAACTCTGGACTGTG
TGTAAAGTGTTAAGTGTTGAAGAATTTGATGCCCTGACTCCTGTGATTGAATCCAGCCTC
CATCAAGTGGAAAGCATGCACGGAGCAGGGAATGCCAAGAAGAATTGGCAACGCATTCAG
GAGCATTTCTTTTTTGCAACATTTCACCCACTCAAGGATTATTGTCTAGAGACCATATTT
TACATCCTTCCACGCCTTTCAGGCCTTATTGAAGATGAATGGATCACCATTGATAAATTT
ACCAGATTCACTGATGTTCCTTTAGCTGCGGGATTTCAGTGGTACCTTTCTCAAACTCAA
CTTAGTAAACTAAAACCAGGTGACTGGTCTCAGCAAGACATAGGTACTAATTTGGTCGAA
GCAGATAACCAAGCGGAGTGGACCGACGTTCAGAAGAAGATTATCCCGTGGAACAGTCGT
GTTTCCGACTTAGACCTGGAGCTCCTGTTTCAGGATCGTGCTGCCAGACTTGGAAAGTCA
ATTAGTAGACTCATCGTTGTGGCCTCGCTCATCGACAAACCGACCAATTTAGGAGGACTG
TGCAGGACCTGTGAGGTATTTGGGGCTTCAGTGCTCGTTGTTGGCAGCCTTCAGTGTATC
AGCGACAAACAGTTTCAGCACCTCAGTGTCTCTGCAGAACAGTGGCTTCCTCTAGTGGAG
GTAAAACCACCTCAGCTAATTGATTATCTGCAGCAGAAGAAAACAGAAGGTTATACCATC
ATTGGAGTGGAACAAACTGCCAAAAGTTTAGACCTAACCCAATATTGCTTTCCTGAGAAA
TCTCTGCTCTTGTTGGGAAATGAACGTGAGGGAATTCCAGCAAATCTGATCCAACAGTTG
GACGTTTGTGTGGAAATTCCTCAACAGGGCATTATCCGCTCCCTGAATGTCCATGTGAGT
GGAGCCCTGCTGATCTGGGAGTACACCAGGCAGCAGCTGCTCTCGCACGGAGATACCAAG
CCATGA
Enzyme 91 GenBank Gene ID AL136124 Link Image
Enzyme 91 GeneCard ID TARBP1 Link Image
Enzyme 91 GenAtlas ID TARBP1 Link Image
Enzyme 91 HGNC ID HGNC:11568 Link Image
Enzyme 91 Chromosome Location 1
Enzyme 91 Locus 1q42.3
Enzyme 91 SNPs SNPJam Report Link Image
Enzyme 91 General References
  1. Wu-Baer F, Lane WS, Gaynor RB: The cellular factor TRP-185 regulates RNA polymerase II binding to HIV-1 TAR RNA. EMBO J. 1995 Dec 1;14(23):5995-6009. [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. Wu-Baer F, Sigman D, Gaynor RB: Specific binding of RNA polymerase II to the human immunodeficiency virus trans-activating region RNA is regulated by cellular cofactors and Tat. Proc Natl Acad Sci U S A. 1995 Aug 1;92(16):7153-7. [PubMed Link Image]
  4. Wu-Baer F, Lane WS, Gaynor RB: Identification of a group of cellular cofactors that stimulate the binding of RNA polymerase II and TRP-185 to human immunodeficiency virus 1 TAR RNA. J Biol Chem. 1996 Feb 23;271(8):4201-8. [PubMed Link Image]
  5. 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]
  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 91 Metabolite References Not Available
Enzyme 92 [top]
Enzyme 92 ID 14783
Enzyme 92 Name Dimethyladenosine transferase 1, mitochondrial
Enzyme 92 Synonyms
  1. Mitochondrial 12S rRNA dimethylase 1
  2. Mitochondrial transcription factor B1
  3. h-mtTFB
  4. h-mtTFB1
  5. hTFB1M
  6. mtTFB1
  7. S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 1
Enzyme 92 Gene Name TFB1M
Enzyme 92 Protein Sequence >Dimethyladenosine transferase 1, mitochondrial
MAASGKLSTCRLPPLPTIREIIKLLRLQAAKQLSQNFLLDLRLTDKIVRKAGNLTNAYVY
EVGPGPGGITRSILNADVAELLVVEKDTRFIPGLQMLSDAAPGKLRIVHGDVLTFKVEKA
FSESLKRPWEDDPPNVHIIGNLPFSVSTPLIIKWLENISCRDGPFVYGRTQMTLTFQKEV
AERLAANTGSKQRSRLSVMAQYLCNVRHIFTIPGQAFVPKPEVDVGVVHFTPLIQPKIEQ
PFKLVEKVVQNVFQFRRKYCHRGLRMLFPEAQRLESTGRLLELADIDPTLRPRQLSISHF
KSLCDVYRKMCDEDPQLFAYNFREELKRRKSKNEEKEEDDAENYRL
Enzyme 92 Number of Residues 346
Enzyme 92 Molecular Weight 39542.6
Enzyme 92 Theoretical pI 9.74
Enzyme 92 GO Classification
Function
  • N-methyltransferase activity
  • RNA methyltransferase activity
  • catalytic activity
  • methyltransferase activity
  • rRNA (adenine) methyltransferase activity
  • rRNA (adenine-N6,N6-)-dimethyltransferase activity
  • rRNA (adenine-N6,N6-)-dimethyltransferase activity
  • rRNA (adenine-N6,N6-)-dimethyltransferase activity
  • rRNA 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
  • rRNA metabolic process
  • rRNA modification
  • rRNA processing
Component
Enzyme 92 General Function Involved in rRNA (adenine-N6,N6-)-dimethyltransferase activity
Enzyme 92 Specific Function S-adenosyl-L-methionine-dependent methyltransferase which specifically dimethylates mitochondrial 12S rRNA at the conserved stem loop. Also required for basal transcription of mitochondrial DNA, probably via its interaction with POLRMT and TFAM. Stimulates transcription independently of the methyltransferase activity
Enzyme 92 Pathways Not Available
Enzyme 92 Reactions Not Available
Enzyme 92 Pfam Domain Function
Enzyme 92 Signals
  • None
Enzyme 92 Transmembrane Regions
  • None
Enzyme 92 Essentiality Not Available
Enzyme 92 GenBank ID Protein 4929619 Link Image
Enzyme 92 UniProtKB/Swiss-Prot ID Q8WVM0 Link Image
Enzyme 92 UniProtKB/Swiss-Prot Entry Name TFB1M_HUMAN Link Image
Enzyme 92 PDB ID Not Available
Enzyme 92 Cellular Location Not Available
Enzyme 92 Gene Sequence >1041 bp
ATGGCTGCCTCCGGAAAACTCAGCACTTGCCGTCTCCCTCCGTTGCCCACGATTCGAGAA
ATCATTAAGTTGTTAAGACTGCAAGCAGCGAACGAGCTATCACAGAATTTCCTCCTGGAC
TTGAGGCTGACAGATAAGATTGTAAGGAAAGCTGGCAATCTGACAAATGCTTATGTTTAC
GAAGTGGGCCCTGGGCCAGGGGGAATCACAAGATCTATTCTTAATGCCGACGTCGCTGAA
CTTCTGGTGGTTGAAAAGGACACTCGATTTATTCCTGGATTACAGATGCTTTCTGATGCA
GCACCTGGGAAACTGAGAATTGTTCATGGAGATGTCTTGACATTTAAGGTAGAAAAGGCT
TTTTCAGAAAGTCTTAAAAGACCCTGGGAAGATGATCCTCCAAATGTACATATTATTGGA
AATCTGCCTTTTAGTGTTTCAACTCCACTGATTATCAAGTGGCTTGAAAATATTTCCTGT
AGAGATGGACCTTTTGTTTATGGCAGAACTCAGATGACTTTGACTTTTCAAAAGGAAGTG
GCAGAGAGACTTGCAGCCAATACAGGAAGCAAACAGCGTAGTCGCCTCTCTGTTATGGCT
CAGTACCTCTGCAATGTTCGACACATCTTTACAATTCCAGGACAAGCTTTTGTCCCCAAA
CCAGAGGTGGACGTGGGCGTGGTGCACTTCACTCCCTTGATACAGCCCAAGATAGAGCAG
CCATTCAAGCTGGTGGAAAAAGTGGTTCAGAATGTATTTCAGTTCCGAAGGAAATACTGC
CATCGAGGGCTCAGAATGTTATTCCCTGAAGCGCAGCGCTTGGAAAGCACGGGCAGGCTG
TTAGAGTTGGCAGACATAGACCCTACTCTTCGGCCCCGCCAGCTCTCCATCTCACACTTT
AAGAGCCTCTGTGATGTATACAGAAAAATGTGTGATGAAGACCCACAACTCTTTGCATAT
AATTTCAGAGAAGAACTCAAGCGAAGAAAAAGCAAAAATGAAGAAAAAGAAGAGGATGAC
GCAGAGAATTACAGACTCTAG
Enzyme 92 GenBank Gene ID AF151833 Link Image
Enzyme 92 GeneCard ID TFB1M Link Image
Enzyme 92 GenAtlas ID TFB1M Link Image
Enzyme 92 HGNC ID HGNC:17037 Link Image
Enzyme 92 Chromosome Location 6
Enzyme 92 Locus 6q25.1-q25.3
Enzyme 92 SNPs SNPJam Report Link Image
Enzyme 92 General References
  1. Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W: Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. Genome Res. 2000 May;10(5):703-13. [PubMed Link Image]
  2. 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]
  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. McCulloch V, Seidel-Rogol BL, Shadel GS: A human mitochondrial transcription factor is related to RNA adenine methyltransferases and binds S-adenosylmethionine. Mol Cell Biol. 2002 Feb;22(4):1116-25. [PubMed Link Image]
  5. Falkenberg M, Gaspari M, Rantanen A, Trifunovic A, Larsson NG, Gustafsson CM: Mitochondrial transcription factors B1 and B2 activate transcription of human mtDNA. Nat Genet. 2002 Jul;31(3):289-94. Epub 2002 Jun 17. [PubMed Link Image]
  6. McCulloch V, Shadel GS: Human mitochondrial transcription factor B1 interacts with the C-terminal activation region of h-mtTFA and stimulates transcription independently of its RNA methyltransferase activity. Mol Cell Biol. 2003 Aug;23(16):5816-24. [PubMed Link Image]
  7. Seidel-Rogol BL, McCulloch V, Shadel GS: Human mitochondrial transcription factor B1 methylates ribosomal RNA at a conserved stem-loop. Nat Genet. 2003 Jan;33(1):23-4. Epub 2002 Dec 23. [PubMed Link Image]
  8. Bykhovskaya Y, Mengesha E, Wang D, Yang H, Estivill X, Shohat M, Fischel-Ghodsian N: Human mitochondrial transcription factor B1 as a modifier gene for hearing loss associated with the mitochondrial A1555G mutation. Mol Genet Metab. 2004 May;82(1):27-32. [PubMed Link Image]
  9. Gleyzer N, Vercauteren K, Scarpulla RC: Control of mitochondrial transcription specificity factors (TFB1M and TFB2M) by nuclear respiratory factors (NRF-1 and NRF-2) and PGC-1 family coactivators. Mol Cell Biol. 2005 Feb;25(4):1354-66. [PubMed Link Image]
Enzyme 92 Metabolite References Not Available
Enzyme 93 [top]
Enzyme 93 ID 14784
Enzyme 93 Name Dimethyladenosine transferase 2, mitochondrial
Enzyme 93 Synonyms
  1. Hepatitis C virus NS5A-transactivated protein 5
  2. HCV NS5A-transactivated protein 5
  3. Mitochondrial 12S rRNA dimethylase 2
  4. Mitochondrial transcription factor B2
  5. h-mtTFB
  6. h-mtTFB2
  7. hTFB2M
  8. mtTFB2
  9. S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 2
Enzyme 93 Gene Name TFB2M
Enzyme 93 Protein Sequence >Dimethyladenosine transferase 2, mitochondrial
MWIPVVGLPRRLRLSALAGAGRFCILGSEAATRKHLPARNHCGLSDSSPQLWPEPDFRNP
PRKASKASLDFKRYVTDRRLAETLAQIYLGKPSRPPHLLLECNPGPGILTQALLEAGAKV
VALESDKTFIPHLESLGKNLDGKLRVIHCDFFKLDPRSGGVIKPPAMSSRGLFKNLGIEA
VPWTADIPLKVVGMFPSRGEKRALWKLAYDLYSCTSIYKFGRIEVNMFIGEKEFQKLMAD
PGNPDLYHVLSVIWQLACEIKVLHMEPWSSFDIYTRKGPLENPKRRELLDQLQQKLYLIQ
MIPRQNLFTKNLTPMNYNIFFHLLKHCFGRRSATVIDHLRSLTPLDARDILMQIGKQEDE
KVVNMHPQDFKTLFETIERSKDCAYKWLYDETLEDR
Enzyme 93 Number of Residues 396
Enzyme 93 Molecular Weight 45348.4
Enzyme 93 Theoretical pI 9.63
Enzyme 93 GO Classification
Function
  • N-methyltransferase activity
  • RNA methyltransferase activity
  • binding
  • catalytic activity
  • methyltransferase activity
  • protein binding
  • rRNA (adenine-N6,N6-)-dimethyltransferase activity
  • rRNA (adenine-N6,N6-)-dimethyltransferase activity
  • rRNA methyltransferase activity
  • transcription cofactor activity
  • transcription factor binding
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • RNA metabolic process
  • biological regulation
  • cellular macromolecule metabolic process
  • macromolecule metabolic process
  • metabolic process
  • ncRNA metabolic process
  • rRNA metabolic process
  • rRNA methylation
  • rRNA modification
  • rRNA processing
  • 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
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • mitochondrion
  • organelle
Enzyme 93 General Function Involved in rRNA (adenine-N6,N6-)-dimethyltransferase activity
Enzyme 93 Specific Function S-adenosyl-L-methionine-dependent methyltransferase which specifically dimethylates mitochondrial 12S rRNA at the conserved stem loop. Also required for basal transcription of mitochondrial DNA, probably via its interaction with POLRMT and TFAM. Stimulates transcription independently of the methyltransferase activity. Compared to TFB1M, it activates transcription of mitochondrial DNA more efficiently, while it has less methyltransferase activity
Enzyme 93 Pathways Not Available
Enzyme 93 Reactions Not Available
Enzyme 93 Pfam Domain Function
Enzyme 93 Signals
  • None
Enzyme 93 Transmembrane Regions
  • None
Enzyme 93 Essentiality Not Available
Enzyme 93 GenBank ID Protein 33328300 Link Image
Enzyme 93 UniProtKB/Swiss-Prot ID Q9H5Q4 Link Image
Enzyme 93 UniProtKB/Swiss-Prot Entry Name TFB2M_HUMAN Link Image
Enzyme 93 PDB ID Not Available
Enzyme 93 Cellular Location Not Available
Enzyme 93 Gene Sequence >1191 bp
ATGTGGATCCCAGTGGTCGGGCTTCCTCGGCGGCTGAGGCTCTCCGCCTTGGCGGGCGCT
GGTCGCTTTTGCATTTTAGGGTCTGAAGCGGCGACGCGAAAGCATTTGCCGGCGAGGAAC
CACTGTGGGCTCTCTGACTCCTCTCCGCAGCTGTGGCCCGAACCGGATTTCAGGAATCCG
CCAAGGAAGGCGTCTAAGGCCAGCTTAGACTTTAAGCGTTACGTAACCGATCGGAGATTG
GCTGAGACCCTGGCGCAAATCTATTTGGGAAAACCAAGTAGACCTCCACACCTACTGCTG
GAGTGCAATCCAGGTCCTGGAATCCTGACTCAGGCATTACTTGAAGCTGGTGCCAAAGTG
GTTGCGCTCGAAAGTGACAAAACTTTTATTCCACATTTGGAGTCCTTAGGAAAAAATCTG
GATGGAAAACTACGAGTGATTCACTGTGACTTCTTTAAACTAGATCCTAGAAGTGGTGGA
GTAATAAAACCACCTGCTATGTCTTCTCGAGGGCTCTTTAAGAATTTGGGAATAGAAGCA
GTTCCTTGGACAGCAGACATCCCTTTAAAAGTAGTTGGAATGTTCCCAAGTAGAGGTGAG
AAAAGGGCACTTTGGAAACTCGCATATGACTTGTATTCCTGTACTTCTATATATAAATTT
GGACGAATAGAAGTAAATATGTTTATTGGTGAAAAAGAATTCCAGAAACTAATGGCAGAT
CCTGGAAATCCAGACTTGTATCATGTATTAAGTGTTATCTGGCAATTAGCTTGTGAGATT
AAGGTTCTGCACATGGAGCCTTGGTCATCATTTGATATATACACCCGGAAAGGGCCGCTG
GAAAACCCAAAGCGTAGGGAATTATTAGACCAATTACAACAAAAGCTGTATCTTATTCAA
ATGATTCCTCGTCAAAATTTATTTACCAAGAACTTAACACCTATGAACTATAATATATTT
TTTCACTTGTTAAAGCACTGTTTTGGGAGGCGCAGCGCCACTGTAATAGACCACTTACGT
TCATTGACTCCACTTGATGCGAGAGATATATTGATGCAAATAGGAAAACAGGAGGATGAG
AAAGTAGTTAACATGCACCCTCAAGACTTCAAAACACTTTTTGAAACTATAGAGCGTTCC
AAAGATTGTGCTTATAAATGGCTGTATGATGAAACCCTGGAAGATAGGTAG
Enzyme 93 GenBank Gene ID AF529366 Link Image
Enzyme 93 GeneCard ID TFB2M Link Image
Enzyme 93 GenAtlas ID TFB2M Link Image
Enzyme 93 HGNC ID HGNC:18559 Link Image
Enzyme 93 Chromosome Location 1
Enzyme 93 Locus 1q44
Enzyme 93 SNPs SNPJam Report Link Image
Enzyme 93 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. 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. Falkenberg M, Gaspari M, Rantanen A, Trifunovic A, Larsson NG, Gustafsson CM: Mitochondrial transcription factors B1 and B2 activate transcription of human mtDNA. Nat Genet. 2002 Jul;31(3):289-94. Epub 2002 Jun 17. [PubMed Link Image]
  5. McCulloch V, Shadel GS: Human mitochondrial transcription factor B1 interacts with the C-terminal activation region of h-mtTFA and stimulates transcription independently of its RNA methyltransferase activity. Mol Cell Biol. 2003 Aug;23(16):5816-24. [PubMed Link Image]
  6. Gaspari M, Falkenberg M, Larsson NG, Gustafsson CM: The mitochondrial RNA polymerase contributes critically to promoter specificity in mammalian cells. EMBO J. 2004 Nov 24;23(23):4606-14. Epub 2004 Nov 4. [PubMed Link Image]
  7. Gleyzer N, Vercauteren K, Scarpulla RC: Control of mitochondrial transcription specificity factors (TFB1M and TFB2M) by nuclear respiratory factors (NRF-1 and NRF-2) and PGC-1 family coactivators. Mol Cell Biol. 2005 Feb;25(4):1354-66. [PubMed Link Image]
  8. Cotney J, Shadel GS: Evidence for an early gene duplication event in the evolution of the mitochondrial transcription factor B family and maintenance of rRNA methyltransferase activity in human mtTFB1 and mtTFB2. J Mol Evol. 2006 Nov;63(5):707-17. Epub 2006 Oct 6. [PubMed Link Image]
Enzyme 93 Metabolite References Not Available
Enzyme 94 [top]
Enzyme 94 ID 14785
Enzyme 94 Name tRNA guanosine-2'-O-methyltransferase TRM11 homolog
Enzyme 94 Synonyms Not Available
Enzyme 94 Gene Name TRMT11
Enzyme 94 Protein Sequence >tRNA guanosine-2'-O-methyltransferase TRM11 homolog
MALSCTLNRYLLLMAQEHLEFRLPEIKSLLLLFGGQFASSQETYGKSPFWILSIPSEDIA
RNLMKRTVCAKSIFELWGHGQSPEELYSSLKNYPVEKMVPFLHSDSTYKIKIHTFNKTLT
QEEKIKRIDALEFLPFEGKVNLKKPQHVFSVLEDYGLDPNCIPENPHNIYFGRWIADGQR
ELIESYSVKKRHFIGNTSMDAGLSFIMANHGKVKENDIVFDPFVGTGGLLIACAHFGAYV
YGTDIDYNTVHGLGKATRKNQKWRGPDENIRANLRQYGLEKYYLDVLVSDASKPSWRKGT
YFDAIITDPPYGIRESTRRTGSQKEIPKGIEKWEKCPESHVPVSLSYHLSDMFLDLLNFA
AETLVLGGRLVYWLPVYTPEYTEEMVPWHPCLELVSNCEQKLSSHTSRRLITMEKVKKFE
NRDQYSHLLSDHFLPYQGHNSFREKYFSGVTKRIAKEEKSTQE
Enzyme 94 Number of Residues 463
Enzyme 94 Molecular Weight 53420.6
Enzyme 94 Theoretical pI 7.88
Enzyme 94 GO Classification
Function
  • binding
  • catalytic activity
  • methyltransferase activity
  • nucleic acid binding
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • cellular metabolic process
  • metabolic process
  • methylation
  • one-carbon metabolic process
Component
Enzyme 94 General Function Involved in nucleic acid binding
Enzyme 94 Specific Function Catalytic subunit of an S-adenosyl-L-methionine- dependent tRNA methyltransferase complex that mediates the methylation of the guanosine nucleotide at position 10 (m2G10) in tRNAs
Enzyme 94 Pathways Not Available
Enzyme 94 Reactions Not Available
Enzyme 94 Pfam Domain Function
Enzyme 94 Signals
  • None
Enzyme 94 Transmembrane Regions
  • None
Enzyme 94 Essentiality Not Available
Enzyme 94 GenBank ID Protein 94420683 Link Image
Enzyme 94 UniProtKB/Swiss-Prot ID Q7Z4G4 Link Image
Enzyme 94 UniProtKB/Swiss-Prot Entry Name TRM11_HUMAN Link Image
Enzyme 94 PDB ID Not Available
Enzyme 94 Cellular Location Not Available
Enzyme 94 Gene Sequence >1392 bp
ATGGCGCTGTCGTGTACCCTTAACAGGTATCTGCTCCTCATGGCGCAGGAGCATCTGGAG
TTCCGCCTGCCGGAAATAAAGTCTTTGCTTTTGCTTTTTGGAGGTCAGTTTGCCAGCAGT
CAAGAAACTTATGGAAAGTCACCATTTTGGATTCTTAGCATTCCCTCTGAAGATATTGCA
AGAAATTTGATGAAACGGACAGTGTGTGCCAAGTCTATATTTGAACTATGGGGTCATGGA
CAATCTCCTGAGGAGCTGTACAGTTCTCTTAAAAACTACCCTGTGGAGAAGATGGTTCCA
TTTCTACATTCGGACTCTACATATAAAATAAAGATTCACACTTTTAATAAGACATTGACA
CAAGAAGAGAAAATCAAGCGAATAGATGCACTTGAATTTCTGCCATTTGAAGGAAAAGTG
AATTTAAAGAAACCGCAACATGTATTTTCTGTTTTGGAGGATTATGGTTTAGACCCAAAC
TGCATCCCTGAGAATCCACATAATATTTATTTTGGTAGATGGATTGCAGATGGACAGAGA
GAGCTTATTGAGTCATACAGTGTCAAAAAGAGACACTTTATTGGAAATACAAGTATGGAT
GCTGGTTTGTCATTCATTATGGCTAACCATGGAAAAGTGAAAGAAAATGATATTGTCTTT
GATCCATTTGTTGGAACAGGTGGCCTGCTGATAGCATGTGCTCATTTTGGTGCATATGTG
TATGGGACAGACATAGACTACAACACAGTTCATGGCTTGGGAAAGGCTACTAGGAAAAAC
CAGAAGTGGAGAGGACCAGATGAAAACATTAGGGCCAATCTTCGTCAATATGGTTTAGAG
AAGTATTACCTTGATGTCCTGGTTTCAGATGCATCTAAACCTTCCTGGAGGAAGGGCACA
TATTTTGATGCAATCATTACTGATCCTCCATATGGTATCAGAGAATCTACAAGAAGAACA
GGTTCACAGAAGGAGATACCAAAGGGGATAGAAAAATGGGAAAAATGTCCAGAAAGCCAT
GTTCCTGTTTCCTTGAGTTATCATCTGAGTGATATGTTTCTTGACCTGTTAAACTTCGCA
GCTGAGACCCTCGTTTTAGGTGGAAGACTAGTCTATTGGTTACCGGTGTATACGCCAGAA
TACACTGAAGAGATGGTGCCTTGGCACCCTTGCCTGGAACTCGTTAGCAACTGCGAGCAG
AAGCTTTCCAGTCACACATCAAGGCGCTTGATCACAATGGAAAAGGTGAAGAAATTTGAG
AATCGGGACCAGTATTCACATCTGCTAAGTGATCATTTTCTGCCATACCAAGGTCATAAT
TCCTTCCGTGAGAAATATTTTAGTGGGGTAACAAAAAGAATTGCCAAGGAAGAAAAATCC
ACCCAGGAATGA
Enzyme 94 GenBank Gene ID NM_001031712.2 Link Image
Enzyme 94 GeneCard ID TRMT11 Link Image
Enzyme 94 GenAtlas ID TRMT11 Link Image
Enzyme 94 HGNC ID HGNC:21080 Link Image
Enzyme 94 Chromosome Location 6
Enzyme 94 Locus 6q11.1-q22.33
Enzyme 94 SNPs SNPJam Report Link Image
Enzyme 94 General References
  1. 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]
  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. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
Enzyme 94 Metabolite References Not Available
Enzyme 95 [top]
Enzyme 95 ID 14786
Enzyme 95 Name tRNA guanosine-2'-O-methyltransferase TRM13 homolog
Enzyme 95 Synonyms
  1. Coiled-coil domain-containing protein 76
  2. tRNA [Gm4] methyltransferase
Enzyme 95 Gene Name CCDC76
Enzyme 95 Protein Sequence >tRNA guanosine-2'-O-methyltransferase TRM13 homolog
MATSATSPHAPGFPAEGRCGYYVEKKKRFCRMVVAAGKRFCGEHAGAAEEEDARKRILCP
LDPKHTVYEDQLAKHLKKCNSREKPKPDFYIQDINAGLRDETEIPEQLVPISSLSEEQLE
KLIKKLRKASEGLNSTLKDHIMSHPALHDALNDPKNGDSATKHLKQQASILGNIENLKLL
GPRRCFVEFGAGKGKLSHWVDIALKDAEKVHFILVEKVTTRFKVDGKHRKKNSVFERLQI
DIQHLCLNKIPVLREEKLPVVGIGKHLCGMATDLALRCLVETYAASFEERNEEPLAKRIK
NDKTEKEIYTLAKEGNEKNVPEKWNPVAGIVIALCCHHRCDWRHYVGKEYFRALGLGAVE
FHYFQRMSSWATCGMRKTSLETSNSTTKRQDNQNDDSEEHDDGGYRITDDGADCLPGLLS
VEEKKKIGHLCKLLIDQGRIQYLQQKGFSPALQYYTDPLVSLENVLLTALPNHSSSPETT
A
Enzyme 95 Number of Residues 481
Enzyme 95 Molecular Weight 54246.6
Enzyme 95 Theoretical pI 8.18
Enzyme 95 GO Classification
Function
  • catalytic activity
  • 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 processing
Component
Enzyme 95 General Function Involved in methyltransferase activity
Enzyme 95 Specific Function Specifically methylates guanosine-4 in various tRNAs with a Gly(CCG), His or Pro signature
Enzyme 95 Pathways Not Available
Enzyme 95 Reactions Not Available
Enzyme 95 Pfam Domain Function
Enzyme 95 Signals
  • None
Enzyme 95 Transmembrane Regions
  • None
Enzyme 95 Essentiality Not Available
Enzyme 95 GenBank ID Protein 226493203 Link Image
Enzyme 95 UniProtKB/Swiss-Prot ID Q9NUP7 Link Image
Enzyme 95 UniProtKB/Swiss-Prot Entry Name TRM13_HUMAN Link Image
Enzyme 95 PDB ID Not Available
Enzyme 95 Cellular Location Not Available
Enzyme 95 Gene Sequence >1446 bp
ATGGCGACCTCCGCGACGTCGCCGCACGCGCCTGGTTTTCCAGCTGAGGGTAGATGCGGT
TACTATGTGGAAAAGAAGAAACGGTTCTGCAGGATGGTGGTGGCCGCAGGGAAAAGATTT
TGTGGTGAACACGCTGGAGCCGCGGAGGAAGAAGATGCTCGGAAAAGAATCCTGTGTCCT
TTAGATCCAAAACACACAGTATATGAAGATCAACTAGCAAAGCATTTGAAAAAATGTAAC
TCAAGAGAGAAACCAAAACCTGATTTCTATATTCAAGATATTAATGCAGGCTTAAGAGAT
GAAACAGAAATACCTGAACAATTAGTTCCAATTTCTTCTCTATCTGAAGAGCAGTTGGAA
AAGTTAATTAAGAAATTGAGAAAAGCAAGTGAAGGCTTGAATTCTACACTTAAAGATCAT
ATTATGTCCCATCCAGCATTACACGATGCACTTAATGACCCTAAAAATGGCGATTCTGCA
ACCAAGCACCTGAAACAGCAGGCTTCTATTTTAGGTAACATTGAAAATTTAAAGTTACTT
GGTCCAAGAAGATGCTTTGTTGAGTTTGGAGCGGGAAAGGGAAAATTATCTCATTGGGTT
GATATTGCCTTAAAAGATGCTGAAAAAGTTCACTTCATCCTAGTGGAAAAGGTGACCACA
AGATTCAAGGTGGATGGAAAACACAGAAAGAAAAATTCAGTGTTTGAAAGACTTCAAATT
GATATTCAACACTTGTGTTTGAACAAGATTCCTGTGCTAAGAGAAGAAAAACTACCTGTG
GTAGGAATTGGAAAGCATCTGTGTGGTATGGCAACAGATCTTGCATTACGATGTTTGGTT
GAAACCTATGCTGCCAGTTTTGAGGAAAGGAATGAAGAACCTTTAGCCAAACGCATAAAG
AATGATAAAACAGAAAAAGAAATTTACACTTTGGCCAAGGAAGGAAATGAAAAAAATGTC
CCAGAGAAGTGGAACCCTGTGGCTGGCATTGTTATTGCACTCTGTTGTCACCACAGGTGT
GATTGGAGACATTATGTGGGCAAAGAATATTTCAGGGCTCTAGGCCTTGGAGCAGTGGAA
TTCCATTATTTCCAGCGAATGAGTAGTTGGGCAACTTGTGGGATGCGGAAAACATCTTTG
GAAACCTCAAATAGTACCACAAAGAGGCAAGATAATCAGAATGATGATAGTGAAGAGCAT
GATGATGGAGGATACAGAATCACAGATGATGGCGCTGATTGTTTGCCTGGGCTTCTTAGT
GTTGAAGAAAAGAAGAAAATAGGGCATCTTTGTAAATTGCTGATTGACCAAGGTCGAATC
CAGTATTTGCAGCAGAAGGGATTCAGTCCTGCTTTGCAGTACTATACAGACCCTCTGGTG
TCTTTGGAAAATGTTTTGTTAACTGCTTTACCAAATCATTCTTCATCACCAGAAACAACT
GCTTAA
Enzyme 95 GenBank Gene ID NM_019083.2 Link Image
Enzyme 95 GeneCard ID CCDC76 Link Image
Enzyme 95 GenAtlas ID CCDC76 Link Image
Enzyme 95 HGNC ID HGNC:25502 Link Image
Enzyme 95 Chromosome Location 1
Enzyme 95 Locus 1p21.2
Enzyme 95 SNPs SNPJam Report Link Image
Enzyme 95 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. 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. Andreeva A, Tidow H: A novel CHHC Zn-finger domain found in spliceosomal proteins and tRNA modifying enzymes. Bioinformatics. 2008 Oct 15;24(20):2277-80. Epub 2008 Aug 14. [PubMed Link Image]
  5. 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 95 Metabolite References Not Available
Enzyme 96 [top]
Enzyme 96 ID 14787
Enzyme 96 Name N(2),N(2)-dimethylguanosine tRNA methyltransferase
Enzyme 96 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 96 Gene Name TRMT1
Enzyme 96 Protein Sequence >N(2),N(2)-dimethylguanosine tRNA methyltransferase
MQGSSLWLSLTFRSARVLSRARFFEWQSPGLPNTAAMENGTGPYGEERPREVQETTVTEG
AAKIAFPSANEVFYNPVQEFNRDLTCAVITEFARIQLGAKGIQIKVPGEKDTQKVVVDLS
EQEEEKVELKESENLASGDQPRTAAVGEICEEGLHVLEGLAASGLRSIRFALEVPGLRSV
VANDASTRAVDLIRRNVQLNDVAHLVQPSQADARMLMYQHQRVSERFDVIDLDPYGSPAT
FLDAAVQAVSEGGLLCVTCTDMAVLAGNSGETCYSKYGAMALKSRACHEMALRIVLHSLD
LRANCYQRFVVPLLSISADFYVRVFVRVFTGQAKVKASASKQALVFQCVGCGAFHLQRLG
KASGVPSGRAKFSAACGPPVTPECEHCGQRHQLGGPMWAEPIHDLDFVGRVLEAVSANPG
RFHTSERIRGVLSVITEELPDVPLYYTLDQLSSTIHCNTPSLLQLRSALLHADFRVSLSH
ACKNAVKTDAPASALWDIMRCWEKECPVKRERLSETSPAFRILSVEPRLQANFTIREDAN
PSSRQRGLKRFQANPEANWGPRPRARPGGKAADEAMEERRRLLQNKRKEPPEDVAQRAAR
LKTFPCKRFKEGTCQRGDQCCYSHSPPTPRVSADAAPDCPETSNQTPPGPGAAAGPGID
Enzyme 96 Number of Residues 659
Enzyme 96 Molecular Weight 72233.4
Enzyme 96 Theoretical pI 7.67
Enzyme 96 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 96 General Function Involved in RNA binding
Enzyme 96 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 96 Pathways Not Available
Enzyme 96 Reactions
  • S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N2-methylguanine [RN:R00598]
Enzyme 96 Pfam Domain Function
Enzyme 96 Signals
  • None
Enzyme 96 Transmembrane Regions
  • None
Enzyme 96 Essentiality Not Available
Enzyme 96 GenBank ID Protein 209862871 Link Image
Enzyme 96 UniProtKB/Swiss-Prot ID Q9NXH9 Link Image
Enzyme 96 UniProtKB/Swiss-Prot Entry Name TRM1_HUMAN Link Image
Enzyme 96 PDB ID Not Available
Enzyme 96 Cellular Location Not Available
Enzyme 96 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 96 GenBank Gene ID NM_001136035.2 Link Image
Enzyme 96 GeneCard ID TRMT1 Link Image
Enzyme 96 GenAtlas ID TRMT1 Link Image
Enzyme 96 HGNC ID HGNC:25980 Link Image
Enzyme 96 Chromosome Location 1
Enzyme 96 Locus 19p13.2
Enzyme 96 SNPs SNPJam Report Link Image
Enzyme 96 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 96 Metabolite References Not Available
Enzyme 97 [top]
Enzyme 97 ID 14788
Enzyme 97 Name tRNA (adenine-N(1)-)-methyltransferase catalytic subunit TRMT61A
Enzyme 97 Synonyms
  1. tRNA(m1A58)-methyltransferase subunit TRMT61A
  2. tRNA(m1A58)MTase subunit TRMT61A
Enzyme 97 Gene Name TRMT61A
Enzyme 97 Protein Sequence >tRNA (adenine-N(1)-)-methyltransferase catalytic subunit TRMT61A
MSFVAYEELIKEGDTAILSLGHGAMVAVRVQRGAQTQTRHGVLRHSVDLIGRPFGSKVTC
GRGGWVYVLHPTPELWTLNLPHRTQILYSTDIALITMMLELRPGSVVCESGTGSGSVSHA
IIRTIAPTGHLHTVEFHQQRAEKAREEFQEHRVGRWVTVRTQDVCRSGFGVSHVADAVFL
DIPSPWEAVGHAWDALKVEGGRFCSFSPCIEQVQRTCQALAARGFSELSTLEVLPQVYNV
RTVSLPPPDLGTGTDGPAGSDTSPFRSGTPMKEAVGHTGYLTFATKTPG
Enzyme 97 Number of Residues 289
Enzyme 97 Molecular Weight 31381.5
Enzyme 97 Theoretical pI 7.39
Enzyme 97 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 97 General Function Involved in tRNA (adenine-N1-)-methyltransferase activity
Enzyme 97 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 97 Pathways Not Available
Enzyme 97 Reactions
  • S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N1-methyladenine [RN:R00596]
Enzyme 97 Pfam Domain Function
Enzyme 97 Signals
  • None
Enzyme 97 Transmembrane Regions
  • None
Enzyme 97 Essentiality Not Available
Enzyme 97 GenBank ID Protein 123173772 Link Image
Enzyme 97 UniProtKB/Swiss-Prot ID Q96FX7 Link Image
Enzyme 97 UniProtKB/Swiss-Prot Entry Name TRM61_HUMAN Link Image
Enzyme 97 PDB ID Not Available
Enzyme 97 Cellular Location Not Available
Enzyme 97 Gene Sequence >870 bp
ATGAGCTTCGTGGCATACGAGGAGCTGATCAAGGAGGGTGACACGGCCATCCTGTCACTG
GGCCATGGTGCAATGGTGGCAGTGCGTGTGCAGCGTGGGGCACAGACCCAGACCCGGCAT
GGTGTCCTGCGGCACTCAGTTGACCTTATCGGCCGCCCCTTCGGCTCCAAGGTGACGTGC
GGCCGAGGTGGCTGGGTGTATGTGCTGCACCCCACGCCCGAGCTCTGGACGCTGAACCTG
CCGCACCGCACGCAGATCCTCTACTCCACAGACATCGCCCTCATCACCATGATGTTGGAG
CTTCGGCCCGGCTCTGTGGTCTGTGAGTCTGGCACCGGCAGTGGCTCTGTGTCCCACGCC
ATCATCCGCACCATTGCACCCACGGGTCACCTGCACACGGTGGAGTTCCACCAGCAGCGG
GCAGAGAAGGCCCGGGAGGAGTTCCAGGAGCACCGTGTGGGCCGCTGGGTGACTGTGCGC
ACCCAGGACGTGTGCCGCAGTGGCTTTGGCGTGAGCCACGTGGCCGACGCCGTCTTCCTG
GACATCCCATCACCCTGGGAGGCCGTGGGCCACGCCTGGGACGCCCTCAAGGTCGAAGGC
GGGCGCTTCTGCTCCTTCTCACCGTGCATCGAGCAGGTGCAACGCACATGCCAGGCGCTG
GCAGCGCGCGGCTTCTCAGAGCTGAGCACCCTGGAGGTGCTGCCACAGGTCTACAACGTG
CGCACTGTCAGCCTGCCACCGCCCGACCTGGGCACAGGCACAGATGGCCCTGCCGGCTCC
GACACCAGCCCCTTCCGCAGCGGCACGCCCATGAAGGAGGCCGTGGGCCACACCGGCTAC
CTGACCTTCGCCACCAAGACCCCAGGCTAG
Enzyme 97 GenBank Gene ID NM_152307.2 Link Image
Enzyme 97 GeneCard ID TRMT61A Link Image
Enzyme 97 GenAtlas ID TRMT61A Link Image
Enzyme 97 HGNC ID HGNC:23790 Link Image
Enzyme 97 Chromosome Location 1
Enzyme 97 Locus 14q32
Enzyme 97 SNPs SNPJam Report Link Image
Enzyme 97 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 97 Metabolite References Not Available
Enzyme 98 [top]
Enzyme 98 ID 14789
Enzyme 98 Name tRNA (guanine-N(7)-)-methyltransferase
Enzyme 98 Synonyms
  1. Methyltransferase-like protein 1
  2. tRNA(m7G46)-methyltransferase
Enzyme 98 Gene Name METTL1
Enzyme 98 Protein Sequence >tRNA (guanine-N(7)-)-methyltransferase
MAAETRNVAGAEAPPPQKRYYRQRAHSNPMADHTLRYPVKPEEMDWSELYPEFFAPLTQN
QSHDDPKDKKEKRAQAQVEFADIGCGYGGLLVELSPLFPDTLILGLEIRVKVSDYVQDRI
RALRAAPAGGFQNIACLRSNAMKHLPNFFYKGQLTKMFFLFPDPHFKRTKHKWRIISPTL
LAEYAYVLRVGGLVYTITDVLELHDWMCTHFEEHPLFERVPLEDLSEDPVVGHLGTSTEE
GKKVLRNGGKNFPAIFRRIQDPVLQAVTSQTSLPGH
Enzyme 98 Number of Residues 276
Enzyme 98 Molecular Weight 31470.8
Enzyme 98 Theoretical pI 7.73
Enzyme 98 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 98 General Function Involved in tRNA (guanine-N7-)-methyltransferase activity
Enzyme 98 Specific Function Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA
Enzyme 98 Pathways Not Available
Enzyme 98 Reactions
  • S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N7-methylguanine [RN:R00600]
Enzyme 98 Pfam Domain Function
Enzyme 98 Signals
  • None
Enzyme 98 Transmembrane Regions
  • None
Enzyme 98 Essentiality Not Available
Enzyme 98 GenBank ID Protein 189054580 Link Image
Enzyme 98 UniProtKB/Swiss-Prot ID Q9UBP6 Link Image
Enzyme 98 UniProtKB/Swiss-Prot Entry Name TRMB_HUMAN Link Image
Enzyme 98 PDB ID Not Available
Enzyme 98 Cellular Location Not Available
Enzyme 98 Gene Sequence >831 bp
ATGGCAGCCGAGACTCGGAACGTGGCCGGAGCAGAGGCCCCACCGCCCCAGAAGCGCTAC
TACCGGCAACGTGCTCACTCCAACCCCATGGCGGACCACACGCTGCGCTACCCTGTGAAG
CCAGAGGAGATGGACTGGTCTGAGCTATACCCAGAGTTCTTCGCTCCACTCACTCAAAAT
CAGAGCCACGATGACCCAAAGGATAAGAAAGAAAAGAGAGCTCAGGCCCAAGTGGAGTTT
GCAGACATAGGCTGTGGCTATGGTGGCCTGTTAGTGGAACTGTCACCGCTGTTCCCAGAC
ACACTTATTCTGGGTCTGGAGATCCGGGTGAAGGTCTCAGACTATGTACAAGACCGGATT
CGGGCCCTACGCGCAGCTCCTGCAGGTGGCTTCCAGAACATCGCCTGTCTCCGTAGCAAT
GCCATGAAGCACCTTCCTAACTTCTTCTACAAGGGCCAGCTGACAAAGATGTTCTTCCTC
TTCCCCGACCCACATTTCAAGCGGACAAAGCACAAGTGGCGAATCATCAGTCCCACCCTG
CTAGCAGAATATGCCTACGTGCTAAGAGTTGGGGGGCTGGTGTATACCATAACCGATGTG
CTGGAGCTACACGACTGGATGTGCACTCATTTCGAAGAGCACCCACTGTTTGAGCGTGTG
CCTCTGGAGGACCTGAGTGAAGACCCCGTTGTGGGACATCTAGGCACCTCAACTGAGGAG
GGGAAGAAAGTTCTACGTAATGGAGGGAAGAATTTCCCAGCCATCTTCCGAAGAATACAA
GATCCCGTCCTCCAGGCAGTGACCTCCCAAACCAGCCTGCCTGGTCACTGA
Enzyme 98 GenBank Gene ID AK314851 Link Image
Enzyme 98 GeneCard ID METTL1 Link Image
Enzyme 98 GenAtlas ID METTL1 Link Image
Enzyme 98 HGNC ID HGNC:7030 Link Image
Enzyme 98 Chromosome Location 1
Enzyme 98 Locus 12q13
Enzyme 98 SNPs SNPJam Report Link Image
Enzyme 98 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 98 Metabolite References Not Available
Enzyme 99 [top]
Enzyme 99 ID 14790
Enzyme 99 Name Potential tRNA (adenine-N(1)-)-methyltransferase catalytic subunit TRMT61B
Enzyme 99 Synonyms Not Available
Enzyme 99 Gene Name TRMT61B
Enzyme 99 Protein Sequence >Potential tRNA (adenine-N(1)-)-methyltransferase catalytic subunit TRMT61B
MLMAWCRGPVLLCLRQGLGTNSFLHGLGQEPFEGARSLCCRSSPRDLRDGEREHEAAQRK
APGAESCPSLPLSISDIGTGCLSSLENLRLPTLREESSPRELEDSSGDQGRCGPTHQGSE
DPSMLSQAQSATEVEERHVSPSCSTSRERPFQAGELILAETGEGETKFKKLFRLNNFGLL
NSNWGAVPFGKIVGKFPGQILRSSFGKQYMLRRPALEDYVVLMKRGTAITFPKDINMILS
MMDINPGDTVLEAGSGSGGMSLFLSKAVGSQGRVISFEVRKDHHDLAKKNYKHWRDSWKL
SHVEEWPDNVDFIHKDISGATEDIKSLTFDAVALDMLNPHVTLPVFYPHLKHGGVCAVYV
VNITQVIELLDGIRTCELALSCEKISEVIVRDWLVCLAKQKNGILAQKVESKINTDVQLD
SQEKIGVKGELFQEDDHEESHSDFPYGSFPYVARPVHWQPGHTAFLVKLRKVKPQLN
Enzyme 99 Number of Residues 477
Enzyme 99 Molecular Weight 52964.9
Enzyme 99 Theoretical pI 6.61
Enzyme 99 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 99 General Function Involved in tRNA (adenine-N1-)-methyltransferase activity
Enzyme 99 Specific Function S-adenosyl-L-methionine + tRNA = S-adenosyl-L- homocysteine + tRNA containing N(1)-methyladenine
Enzyme 99 Pathways Not Available
Enzyme 99 Reactions
  • S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N1-methyladenine [RN:R00596]
Enzyme 99 Pfam Domain Function
Enzyme 99 Signals
  • None
Enzyme 99 Transmembrane Regions
  • None
Enzyme 99 Essentiality Not Available
Enzyme 99 GenBank ID Protein 62988627 Link Image
Enzyme 99 UniProtKB/Swiss-Prot ID Q9BVS5 Link Image
Enzyme 99 UniProtKB/Swiss-Prot Entry Name TR61B_HUMAN Link Image
Enzyme 99 PDB ID Not Available
Enzyme 99 Cellular Location Not Available
Enzyme 99 Gene Sequence >1434 bp
ATGCTAATGGCATGGTGCCGCGGTCCTGTCTTGCTGTGCCTGCGGCAGGGGCTCGGAACC
AATTCATTCCTGCACGGCCTGGGGCAGGAGCCCTTCGAGGGAGCTCGGTCACTGTGTTGC
AGGTCCTCGCCTAGAGACCTGCGAGATGGAGAAAGAGAGCACGAGGCGGCACAAAGGAAA
GCCCCAGGAGCAGAGTCTTGCCCATCTCTCCCTCTGAGCATCTCGGACATTGGGACTGGA
TGTCTTTCGTCACTGGAAAACCTCAGACTGCCGACGCTGCGGGAAGAGTCATCCCCTCGA
GAGCTCGAGGACTCGAGCGGAGACCAGGGCCGGTGCGGTCCCACACACCAGGGATCCGAG
GATCCTTCGATGCTCTCGCAGGCCCAGTCCGCTACCGAGGTCGAAGAGCGTCACGTCTCC
CCTTCTTGTTCAACTTCCAGAGAGAGACCCTTTCAGGCTGGGGAACTGATTTTAGCTGAG
ACTGGGGAGGGAGAAACAAAATTTAAGAAATTATTTAGGTTGAACAACTTCGGACTCTTA
AATAGTAACTGGGGGGCAGTCCCGTTCGGCAAGATCGTGGGGAAGTTCCCCGGCCAGATA
CTGAGGAGTTCCTTCGGTAAGCAGTACATGCTGAGGAGGCCAGCCTTGGAAGACTATGTA
GTATTGATGAAAAGAGGGACTGCCATAACATTCCCAAAGGATATTAATATGATTCTCTCA
ATGATGGATATCAACCCAGGTGATACTGTTTTGGAAGCTGGCTCAGGCTCTGGTGGAATG
AGCTTATTTTTATCCAAAGCAGTTGGATCACAAGGACGAGTCATAAGTTTTGAGGTACGA
AAAGACCACCATGATCTGGCTAAGAAGAATTACAAACACTGGCGTGATTCATGGAAATTA
AGTCATGTAGAAGAGTGGCCAGACAATGTGGATTTTATTCATAAGGACATTTCAGGAGCA
ACCGAAGACATAAAATCTTTAACATTTGACGCAGTAGCTTTGGATATGTTAAATCCTCAT
GTTACTTTGCCTGTTTTTTACCCACATCTTAAGCATGGTGGTGTATGTGCTGTATATGTA
GTAAACATCACACAGGTTATTGAACTTTTAGATGGAATTCGCACCTGTGAACTTGCTCTT
TCATGTGAAAAGATAAGCGAGGTCATTGTCAGAGATTGGTTGGTTTGCCTTGCAAAACAG
AAAAATGGAATTTTAGCTCAAAAAGTAGAATCTAAAATCAACACAGATGTACAACTAGAT
TCTCAAGAGAAAATTGGAGTTAAAGGTGAGCTGTTTCAAGAGGATGACCATGAAGAATCG
CATTCTGATTTTCCATATGGATCATTTCCCTATGTTGCTAGACCAGTACACTGGCAACCT
GGTCATACAGCTTTTCTTGTCAAGTTGAGGAAGGTCAAACCACAACTTAACTGA
Enzyme 99 GenBank Gene ID AC097720 Link Image
Enzyme 99 GeneCard ID TRMT61B Link Image
Enzyme 99 GenAtlas ID TRMT61B Link Image
Enzyme 99 HGNC ID HGNC:26070 Link Image
Enzyme 99 Chromosome Location 2
Enzyme 99 Locus 2p23.2
Enzyme 99 SNPs SNPJam Report Link Image
Enzyme 99 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. 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. 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 99 Metabolite References Not Available
Enzyme 100 [top]
Enzyme 100 ID 14791
Enzyme 100 Name tRNA (guanine-N(1)-)-methyltransferase
Enzyme 100 Synonyms
  1. M1G-methyltransferase
  2. tRNA [GM37] methyltransferase
  3. tRNA methyltransferase 5
  4. TRM5
Enzyme 100 Gene Name TRMT5
Enzyme 100 Protein Sequence >tRNA (guanine-N(1)-)-methyltransferase
MVLWILWRPFGFSGRFLKLESHSITESKSLIPVAWTSLTQMLLEAPGIFLLGQRKRFSTM
PETETHERETELFSPPSDVRGMTKLDRTAFKKTVNIPVLKVRKEIVSKLMRSLKRAALQR
PGIRRVIEDPEDKESRLIMLDPYKIFTHDSFEKAELSVLEQLNVSPQISKYNLELTYEHF
KSEEILRAVLPEGQDVTSGFSRIGHIAHLNLRDHQLSFKHLIGQVMIDKNPGITSAVNKI
NNIDNMYRNFQMEVLSGEQNMMTKVRENNYTYEFDFSKVYWNPRLSTEHSRITELLKPGD
VLFDVFAGVGPFAIPVAKKNCTVFANDLNPESHKWLLYNCKLNKVDQKVKVFNLDGKDFL
QGPVKEELMQLLGLSKERKPSVHVVMNLPAKAIEFLSAFKWLLDGQPCSSEFLPIVHCYS
FSKDANPAEDVRQRAGAVLGISLEACSSVHLVRNVAPNKEMLCITFQIPASVLYKNQTRN
PENHEDPPLKRQRTAEAFSDEKTQIVSNT
Enzyme 100 Number of Residues 509
Enzyme 100 Molecular Weight 58245.7
Enzyme 100 Theoretical pI 8.90
Enzyme 100 GO Classification Not Available
Enzyme 100 General Function Involved in tRNA (guanine-N1-)-methyltransferase activity
Enzyme 100 Specific Function Specifically methylates guanosine-37 in various tRNAs. Not dependent on the nature of the nucleoside 5' of the target nucleoside
Enzyme 100 Pathways Not Available
Enzyme 100 Reactions
  • S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N1-methylguanine [RN:R00597]
Enzyme 100 Pfam Domain Function
Enzyme 100 Signals
  • None
Enzyme 100 Transmembrane Regions
  • None
Enzyme 100 Essentiality Not Available
Enzyme 100 GenBank ID Protein 145275187 Link Image
Enzyme 100 UniProtKB/Swiss-Prot ID Q32P41 Link Image
Enzyme 100 UniProtKB/Swiss-Prot Entry Name TRMT5_HUMAN Link Image
Enzyme 100 PDB ID Not Available
Enzyme 100 Cellular Location Not Available
Enzyme 100 Gene Sequence >1530 bp
ATGGTGCTTTGGATCTTATGGAGGCCATTTGGATTCTCAGGAAGATTTCTGAAACTGGAA
AGCCATAGCATAACTGAATCAAAATCGTTGATTCCAGTAGCTTGGACATCCCTGACACAG
ATGCTTTTGGAAGCACCTGGTATTTTCTTATTGGGTCAAAGAAAAAGATTCTCAACCATG
CCAGAAACAGAAACACATGAGAGAGAGACTGAATTGTTTTCACCACCTTCTGATGTCCGA
GGCATGACAAAACTTGATAGAACAGCTTTTAAAAAGACAGTCAACATTCCAGTGCTTAAA
GTGAGGAAAGAAATAGTCAGTAAATTGATGCGATCCCTAAAAAGGGCAGCATTGCAGCGC
CCAGGCATAAGACGTGTGATTGAAGATCCGGAAGATAAAGAAAGTAGACTAATCATGTTG
GATCCCTATAAAATATTTACTCATGATTCCTTTGAGAAAGCAGAACTCAGTGTTTTAGAG
CAGCTTAATGTCAGTCCACAGATCTCTAAATACAATTTGGAACTAACATATGAACACTTT
AAGTCAGAAGAAATCTTGAGAGCTGTGCTTCCTGAAGGTCAAGATGTAACTTCAGGGTTT
AGCAGGATTGGACATATTGCACACCTAAACCTTCGAGATCATCAGCTGTCTTTCAAACAT
TTAATTGGCCAGGTTATGATTGACAAAAATCCAGGAATCACCTCAGCAGTAAATAAAATA
AATAATATTGACAATATGTACCGAAATTTCCAAATGGAAGTGCTATCTGGAGAGCAGAAC
ATGATGACAAAGGTTCGAGAAAACAACTACACCTATGAATTTGATTTTTCAAAAGTCTAT
TGGAATCCTCGTCTGTCTACAGAACACAGCCGTATCACAGAACTTCTCAAACCTGGGGAT
GTCCTATTTGATGTTTTTGCTGGGGTTGGGCCCTTTGCCATTCCAGTAGCAAAGAAAAAC
TGCACTGTATTTGCCAATGATCTCAATCCTGAATCTCATAAATGGCTGTTGTACAACTGT
AAATTAAATAAAGTGGACCAAAAGGTGAAAGTCTTCAACTTGGATGGGAAAGACTTCCTC
CAAGGACCAGTCAAAGAAGAGTTAATGCAGCTGCTGGGTCTGTCAAAAGAAAGAAAACCC
TCTGTGCACGTTGTCATGAACTTGCCAGCAAAAGCTATAGAGTTTCTTAGTGCTTTCAAG
TGGCTTTTAGATGGGCAGCCATGCAGCAGTGAGTTCCTTCCCATAGTGCATTGTTATAGC
TTTTCCAAAGATGCTAACCCTGCTGAGGATGTTCGGCAAAGGGCTGGAGCTGTGTTAGGC
ATTTCTCTGGAGGCATGCAGTTCAGTTCACCTGGTAAGAAATGTGGCCCCAAACAAGGAA
ATGCTGTGCATCACGTTTCAGATTCCTGCCTCTGTCCTCTACAAGAACCAGACCAGAAAT
CCAGAGAATCATGAAGATCCACCTCTTAAAAGGCAGAGGACGGCTGAAGCCTTTTCAGAC
GAAAAAACACAAATTGTTTCAAACACTTAA
Enzyme 100 GenBank Gene ID NM_020810.2 Link Image
Enzyme 100 GeneCard ID TRMT5 Link Image
Enzyme 100 GenAtlas ID TRMT5 Link Image
Enzyme 100 HGNC ID HGNC:23141 Link Image
Enzyme 100 Chromosome Location 1
Enzyme 100 Locus 14q23.1
Enzyme 100 SNPs SNPJam Report Link Image
Enzyme 100 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. 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. 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. Brule H, Elliott M, Redlak M, Zehner ZE, Holmes WM: Isolation and characterization of the human tRNA-(N1G37) methyltransferase (TRM5) and comparison to the Escherichia coli TrmD protein. Biochemistry. 2004 Jul 20;43(28):9243-55. [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 100 Metabolite References Not Available
Enzyme 101 [top]
Enzyme 101 ID 14792
Enzyme 101 Name tRNA wybutosine-synthesizing protein 2 homolog
Enzyme 101 Synonyms
  1. tRNA methyltransferase 12
  2. tRNA-yW-synthesizing protein 2
Enzyme 101 Gene Name TRMT12
Enzyme 101 Protein Sequence >tRNA wybutosine-synthesizing protein 2 homolog
MRENVVVSNMERESGKPVAVVAVVTEPWFTQRYREYLQRQKLFDTQHRVEKMPDGSVALP
VLGETLPEQHLQELRNRVAPGSPCMLTQLPDPVPSKRAQGCSPAQKLCLEVSRWVEGRGV
KWSAELEADLPRSWQRHGNLLLLSEDCFQAKQWKNLGPELWETVALALGVQRLAKRGRVS
PDGTRTPAVTLLLGDHGWVEHVDNGIRYKFDVTQCMFSFGNITEKLRVASLSCAGEVLVD
LYAGIGYFTLPFLVHAGAAFVHACEWNPHAVVALRNNLEINGVADRCQIHFGDNRKLKLS
NIADRVILGLIPSSEEGWPIACQVLRQDAGGILHIHQNVESFPGKNLQALGVSKVEKEHW
LYPQQITTNQWKNGATRDSRGKMLSPATKPEWQRWAESAETRIATLLQQVHGKPWKTQIL
HIQPVKSYAPHVDHIVLDLECCPCPSVG
Enzyme 101 Number of Residues 448
Enzyme 101 Molecular Weight 50235.3
Enzyme 101 Theoretical pI 8.05
Enzyme 101 GO Classification Not Available
Enzyme 101 General Function Involved in methyltransferase activity
Enzyme 101 Specific Function Probable S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA
Enzyme 101 Pathways Not Available
Enzyme 101 Reactions Not Available
Enzyme 101 Pfam Domain Function
Enzyme 101 Signals
  • None
Enzyme 101 Transmembrane Regions
  • None
Enzyme 101 Essentiality Not Available
Enzyme 101 GenBank ID Protein 7021077 Link Image
Enzyme 101 UniProtKB/Swiss-Prot ID Q53H54 Link Image
Enzyme 101 UniProtKB/Swiss-Prot Entry Name TYW2_HUMAN Link Image
Enzyme 101 PDB ID Not Available
Enzyme 101 Cellular Location Not Available
Enzyme 101 Gene Sequence >1347 bp
ATGAGAGAGAATGTGGTTGTTAGCAACATGGAGAGAGAAAGTGGGAAGCCCGTGGCTGTT
GTCGCAGTTGTGACTGAGCCTTGGTTTACCCAGCGATACAGAGAATATCTCCAGAGGCAG
AAACTCTTTGATACACAGCACCGTGTGGAAAAGATGCCGGATGGCTCGGTGGCGCTACCG
GTGCTGGGAGAGACGCTTCCAGAGCAGCACCTGCAGGAGCTGAGGAATCGTGTTGCCCCA
GGCAGTCCCTGTATGCTCACGCAGCTCCCGGATCCTGTTCCTTCGAAGAGGGCCCAGGGT
TGTTCACCTGCCCAAAAATTGTGTCTTGAGGTGAGTCGCTGGGTGGAGGGTCGGGGAGTC
AAGTGGTCAGCCGAGTTGGAGGCTGATTTGCCCCGATCATGGCAACGGCATGGTAATCTC
TTGTTGCTGAGTGAAGACTGTTTCCAAGCCAAGCAGTGGAAAAATCTGGGACCGGAACTC
TGGGAGACCGTTGCCTTGGCACTTGGCGTCCAGCGTTTGGCAAAACGAGGGCGGGTATCA
CCGGATGGTACTCGAACTCCAGCAGTGACACTGCTGCTGGGTGACCATGGCTGGGTAGAG
CATGTGGATAATGGTATCCGTTATAAGTTTGACGTGACCCAGTGTATGTTCTCCTTTGGA
AACATCACTGAGAAGCTTCGAGTGGCATCGTTGTCCTGTGCTGGAGAAGTGCTGGTGGAT
CTCTATGCAGGGATTGGTTATTTTACATTGCCTTTCCTAGTTCATGCTGGTGCTGCCTTC
GTCCATGCTTGTGAGTGGAATCCCCATGCTGTAGTTGCTCTGAGAAATAACCTTGAGATC
AATGGAGTAGCAGATCGGTGCCAAATACACTTTGGAGATAACAGAAAACTGAAGCTCTCA
AATATTGCAGATAGGGTGATCCTGGGGCTGATTCCCAGCTCTGAAGAAGGCTGGCCCATT
GCCTGCCAAGTGTTAAGGCAGGATGCTGGAGGCATTTTGCATATCCACCAAAATGTGGAA
TCTTCCCCAGGGAAGAATCTTCAGGCTCTTGGAGTCAGCAAAGTAGAGAAAGAGCATTGG
CTGTATCCTCAGCAAATTACCACCAACCAATGGAAAAATGGAGCTACCAGGGATTCTAGG
GGAAAAATGCTGTCACCAGCCACCAAGCCAGAGTGGCAAAGGTGGGCAGAATCTGCAGAA
ACTCGAATCGCCACTCTTCTTCAGCAGGTGCATGGGAAACCATGGAAGACACAAATTCTG
CACATCCAACCAGTGAAATCCTATGCTCCCCATGTGGATCACATAGTCCTGGATCTGGAA
TGCTGCCCCTGTCCTTCAGTTGGCTAG
Enzyme 101 GenBank Gene ID AK000779 Link Image
Enzyme 101 GeneCard ID TRMT12 Link Image
Enzyme 101 GenAtlas ID TRMT12 Link Image
Enzyme 101 HGNC ID HGNC:26091 Link Image
Enzyme 101 Chromosome Location 8
Enzyme 101 Locus 8q24.13
Enzyme 101 SNPs SNPJam Report Link Image
Enzyme 101 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. 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 101 Metabolite References Not Available
Enzyme 102 [top]
Enzyme 102 ID 14793
Enzyme 102 Name tRNA wybutosine-synthesizing protein 3 homolog
Enzyme 102 Synonyms
  1. tRNA-yW-synthesizing protein 3
Enzyme 102 Gene Name TYW3
Enzyme 102 Protein Sequence >tRNA wybutosine-synthesizing protein 3 homolog
MDRSAEFRKWKAQCLSKADLSRKGSVDEDVVELVQFLNMRDQFFTTSSCAGRILLLDRGI
NGFEVQKQNCCWLLVTHKLCVKDDVIVALKKANGDATLKFEPFVLHVQCRQLQDAQILHS
MAIDSGFRNSGITVGKRGKTMLAVRSTHGLEVPLSHKGKLMVTEEYIDFLLNVANQKMEE
NKKRIERFYNCLQHALERETMTNLHPKIKEKNNSSYIHKKKRNPEKTRAQCITKESDEEL
ENDDDDDLGINVTIFPEDY
Enzyme 102 Number of Residues 259
Enzyme 102 Molecular Weight 29793.9
Enzyme 102 Theoretical pI 7.77
Enzyme 102 GO Classification Not Available
Enzyme 102 General Function Involved in methyltransferase activity
Enzyme 102 Specific Function Probable S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA
Enzyme 102 Pathways Not Available
Enzyme 102 Reactions Not Available
Enzyme 102 Pfam Domain Function
Enzyme 102 Signals
  • None
Enzyme 102 Transmembrane Regions
  • None
Enzyme 102 Essentiality Not Available
Enzyme 102 GenBank ID Protein 42734381 Link Image
Enzyme 102 UniProtKB/Swiss-Prot ID Q6IPR3 Link Image
Enzyme 102 UniProtKB/Swiss-Prot Entry Name TYW3_HUMAN Link Image
Enzyme 102 PDB ID Not Available
Enzyme 102 Cellular Location Not Available
Enzyme 102 Gene Sequence >780 bp
ATGGATCGCAGCGCGGAGTTCAGGAAATGGAAGGCGCAATGTTTGAGCAAAGCGGACCTC
AGCCGGAAGGGCAGTGTTGACGAGGATGTGGTAGAGCTTGTGCAGTTTCTGAACATGCGA
GATCAGTTTTTCACCACCAGCTCCTGCGCTGGCCGCATCCTACTCCTTGACCGGGGTATA
AATGGTTTTGAGGTTCAGAAACAAAACTGTTGCTGGCTACTGGTTACACACAAACTTTGT
GTAAAAGATGATGTGATTGTAGCTCTGAAGAAAGCAAATGGTGATGCCACTTTGAAATTT
GAACCATTTGTTCTTCATGTGCAGTGTCGACAATTGCAGGATGCACAGATTCTGCATTCC
ATGGCAATAGATTCTGGTTTCAGGAACTCTGGCATAACGGTGGGAAAGAGAGGAAAAACT
ATGTTGGCTGTCCGGAGTACACATGGCTTAGAAGTTCCATTAAGCCATAAGGGAAAACTG
ATGGTGACAGAGGAATATATTGACTTCCTGTTAAATGTGGCAAATCAAAAAATGGAGGAA
AACAAGAAAAGAATTGAGAGGTTTTACAACTGCCTACAGCATGCTTTGGAAAGGGAAACG
ATGACTAACTTACATCCCAAGATCAAAGAGAAAAATAACTCATCATATATTCATAAGAAA
AAAAGAAACCCAGAAAAAACACGTGCCCAGTGTATTACTAAAGAAAGTGATGAAGAACTT
GAAAATGATGATGATGATGATCTAGGAATCAATGTTACCATCTTCCCTGAAGATTACTAA
Enzyme 102 GenBank Gene ID NM_138467.2 Link Image
Enzyme 102 GeneCard ID TYW3 Link Image
Enzyme 102 GenAtlas ID TYW3 Link Image
Enzyme 102 HGNC ID HGNC:24757 Link Image
Enzyme 102 Chromosome Location 1
Enzyme 102 Locus 1p31.1
Enzyme 102 SNPs SNPJam Report Link Image
Enzyme 102 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. 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. 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]
Enzyme 102 Metabolite References Not Available
Enzyme 103 [top]
Enzyme 103 ID 14870
Enzyme 103 Name Probable S-adenosyl-L-methionine-dependent methyltransferase METT5D2
Enzyme 103 Synonyms
  1. Methyltransferase 5 domain-containing protein 2
Enzyme 103 Gene Name METT5D2
Enzyme 103 Protein Sequence >Probable S-adenosyl-L-methionine-dependent methyltransferase METT5D2
MLRYPYFCRMYKECLSCWLESGIPNLGVWPKRIHTTAEKYREYEAREQTDQTQVQELHRS
QDRDFETMAKLHIPVMVDEVVHCLSPQKGQIFLDMTFGSGGHTKAILQKESDIVLYALDR
DPTAYALAEHLSELYPKQIRAMLGQFSQAEALLMKAGVQPGTFDGVLMDLGCSSMQLDTP
ERGSSLRKDGPLDIRMDGGRNISSLCYLYTERLTTAIYLYCHQDFPGSSHICEQ
Enzyme 103 Number of Residues 234
Enzyme 103 Molecular Weight 26715.3
Enzyme 103 Theoretical pI 5.84
Enzyme 103 GO Classification
Function
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
Component
Enzyme 103 General Function Involved in methyltransferase activity
Enzyme 103 Specific Function Probable S-adenosyl-L-methionine-dependent methyltransferase
Enzyme 103 Pathways Not Available
Enzyme 103 Reactions Not Available
Enzyme 103 Pfam Domain Function
Enzyme 103 Signals
  • None
Enzyme 103 Transmembrane Regions
  • None
Enzyme 103 Essentiality Not Available
Enzyme 103 GenBank ID Protein Not Available
Enzyme 103 UniProtKB/Swiss-Prot ID P0C7V9 Link Image
Enzyme 103 UniProtKB/Swiss-Prot Entry Name ME5D2_HUMAN Link Image
Enzyme 103 PDB ID Not Available
Enzyme 103 Cellular Location Not Available
Enzyme 103 Gene Sequence Not Available
Enzyme 103 GenBank Gene ID Not Available
Enzyme 103 GeneCard ID METT5D2 Link Image
Enzyme 103 GenAtlas ID METT5D2 Link Image
Enzyme 103 HGNC ID HGNC:31926 Link Image
Enzyme 103 Chromosome Location 3
Enzyme 103 Locus 3q25.31
Enzyme 103 SNPs SNPJam Report Link Image
Enzyme 103 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. Dias Neto E, Correa RG, Verjovski-Almeida S, Briones MR, Nagai MA, da Silva W Jr, Zago MA, Bordin S, Costa FF, Goldman GH, Carvalho AF, Matsukuma A, Baia GS, Simpson DH, Brunstein A, de Oliveira PS, Bucher P, Jongeneel CV, O'Hare MJ, Soares F, Brentani RR, Reis LF, de Souza SJ, Simpson AJ: Shotgun sequencing of the human transcriptome with ORF expressed sequence tags. Proc Natl Acad Sci U S A. 2000 Mar 28;97(7):3491-6. [PubMed Link Image]
Enzyme 103 Metabolite References Not Available
Enzyme 104 [top]
Enzyme 104 ID 15244
Enzyme 104 Name 5-methyltetrahydrofolate-homocysteine methyltransferase reductase
Enzyme 104 Synonyms Not Available
Enzyme 104 Gene Name MTRR
Enzyme 104 Protein Sequence >5-methyltetrahydrofolate-homocysteine methyltransferase reductase
MRRFLLLYATQQGQAKAIAEEICEQAVVHGFSADLHCISESDKYDLKTETAPLVVVVSTT
GTGDPPDTARKFVKEIQNQTLPVDFFAHLRYGLLGLGDSEYTYFCNGGKIIDKRLQELGA
RHFYDTGHADDCVGLELVVEPWIAGLWPALRKHFRSSRGQEEISGALPVASPASSRTDLV
KSELLHIESQVELLRFDDSGRKDSEVLKQNAVNSNQSNVVIEDFESSLTRSVPPLSQASL
NIPGLPPEYLQVHLQESLGQEESQVSVTSADPVFQVPISKAVQLTTNDAIKTTLLVELDI
SNTDFSYQPGDAFSVICPNSDSEVQSLLQRLQLEDKREHCVLLKIKADTKKKGATLPQHI
PAGCSLQFIFTWCLEIRAIPKKAFLRALVDYTSDSAEKRRLQELCSKQGAADYSRFVRDA
CACLLDLLLAFPSCQPPLSLLLEHLPKLQPRPYSCASSSLFHPGKLHFVFNIVEFLSTAT
TEVLRKGVCTGWLALLVASVLQPNIHASHEDSGKALAPKISISPRTTNSFHLPDDPSIPI
IMVGPGTGIAPFIGFLQHREKLQEQHPDGNFGAMWLFFGCRHKDRDYLFRKELRHFLKHG
ILTHLKVSFSRDAPVGEEEAPAKYVQDNIQLHGQQVARILLQENGHIYVCGDAKNMAKDV
HDALVQIISKEVGVEKLEAMKTLATLKEEKRYLQDIWS
Enzyme 104 Number of Residues 698
Enzyme 104 Molecular Weight 77673.0
Enzyme 104 Theoretical pI 6.47
Enzyme 104 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 104 General Function Involved in oxidoreductase activity
Enzyme 104 Specific Function Not Available
Enzyme 104 Pathways Not Available
Enzyme 104 Reactions Not Available
Enzyme 104 Pfam Domain Function
Enzyme 104 Signals
  • None
Enzyme 104 Transmembrane Regions
  • None
Enzyme 104 Essentiality Not Available
Enzyme 104 GenBank ID Protein 127798340 Link Image
Enzyme 104 UniProtKB/Swiss-Prot ID Q7Z4M8 Link Image
Enzyme 104 UniProtKB/Swiss-Prot Entry Name Q7Z4M8_HUMAN Link Image
Enzyme 104 PDB ID Not Available
Enzyme 104 Cellular Location Not Available
Enzyme 104 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 104 GenBank Gene ID BC054816 Link Image
Enzyme 104 GeneCard ID MTRR Link Image
Enzyme 104 GenAtlas ID MTRR Link Image
Enzyme 104 HGNC ID HGNC:7473 Link Image
Enzyme 104 Chromosome Location 5
Enzyme 104 Locus 5p15.31
Enzyme 104 SNPs SNPJam Report Link Image
Enzyme 104 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 104 Metabolite References Not Available
Enzyme 105 [top]
Enzyme 105 ID 15862
Enzyme 105 Name DNA (cytosine-5)-methyltransferase 3-like
Enzyme 105 Synonyms Not Available
Enzyme 105 Gene Name DNMT3L
Enzyme 105 Protein Sequence >DNA (cytosine-5)-methyltransferase 3-like
MAAIPALDPEAEPSMDVILVGSSELSSSVSPGTGRDLIAYEVKANQRNIEDICICCGSLQ
VHTQHPLFEGGICAPCKDKFLDALFLYDDDGYQSYCSICCSGETLLICGNPDCTRCYCFE
CVDSLVGPGTSGKVHAMSNWVCYLCLPSSRSGLLQRRRKWRSQLKAFYDRESENPLEMFE
TVPVWRRQPVRVLSLFEDIKKELTSLGFLESGSDPGQLKHVVDVTDTVRKDVEEWGPFDL
VYGATPPLGHTCDRPPSWYLFQFHRLLQYARPKPGSPRPFFWMFVDNLVLNKEDLDVASR
FLEMEPVTIPDVHGGSLQNAVRVWSNIPAIRSSRHWALVSEEELSLLAQNKQSSKLAAKW
PTKLVKNCFLPLREYFKYFSTELTSSL
Enzyme 105 Number of Residues 387
Enzyme 105 Molecular Weight 43669.5
Enzyme 105 Theoretical pI 5.67
Enzyme 105 GO Classification
Function
  • binding
  • cation binding
  • ion binding
  • metal ion binding
  • transition metal ion binding
  • zinc ion binding
Process
Component
Enzyme 105 General Function Involved in zinc ion binding
Enzyme 105 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 105 Pathways Not Available
Enzyme 105 Reactions Not Available
Enzyme 105 Pfam Domain Function Not Available
Enzyme 105 Signals
  • None
Enzyme 105 Transmembrane Regions
  • None
Enzyme 105 Essentiality Not Available
Enzyme 105 GenBank ID Protein 6180116 Link Image
Enzyme 105 UniProtKB/Swiss-Prot ID Q9UJW3 Link Image
Enzyme 105 UniProtKB/Swiss-Prot Entry Name DNM3L_HUMAN Link Image
Enzyme 105 PDB ID Not Available
Enzyme 105 Cellular Location Not Available
Enzyme 105 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 105 GenBank Gene ID AF194032 Link Image
Enzyme 105 GeneCard ID DNMT3L Link Image
Enzyme 105 GenAtlas ID DNMT3L Link Image
Enzyme 105 HGNC ID HGNC:2980 Link Image
Enzyme 105 Chromosome Location 2
Enzyme 105 Locus 21q22.3
Enzyme 105 SNPs SNPJam Report Link Image
Enzyme 105 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 105 Metabolite References Not Available
Enzyme 106 [top]
Enzyme 106 ID 15863
Enzyme 106 Name Euchromatic histone-lysine N-methyltransferase 2 (Euchromatic histone- lysine N-methyltransferase 2, isoform CRA_c) (HLA-B associated transcript 8)
Enzyme 106 Synonyms Not Available
Enzyme 106 Gene Name EHMT2
Enzyme 106 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 106 Number of Residues 1210
Enzyme 106 Molecular Weight 132372
Enzyme 106 Theoretical pI 5.14
Enzyme 106 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 106 General Function Not Available
Enzyme 106 Specific Function S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N(6)-methyl-L-lysine
Enzyme 106 Pathways Not Available
Enzyme 106 Reactions Not Available
Enzyme 106 Pfam Domain Function
Enzyme 106 Signals
  • None
Enzyme 106 Transmembrane Regions
  • None
Enzyme 106 Essentiality Not Available
Enzyme 106 GenBank ID Protein Not Available
Enzyme 106 UniProtKB/Swiss-Prot ID Q5JQ92 Link Image
Enzyme 106 UniProtKB/Swiss-Prot Entry Name Q5JQ92_HUMAN Link Image
Enzyme 106 PDB ID Not Available
Enzyme 106 Cellular Location Not Available
Enzyme 106 Gene Sequence Not Available
Enzyme 106 GenBank Gene ID AL662834 Link Image
Enzyme 106 GeneCard ID Q5JQ92 Link Image
Enzyme 106 GenAtlas ID EHMT2 Link Image
Enzyme 106 HGNC ID HGNC:14129 Link Image
Enzyme 106 Chromosome Location Not Available
Enzyme 106 Locus Not Available
Enzyme 106 SNPs SNPJam Report Link Image
Enzyme 106 General References Not Available
Enzyme 106 Metabolite References Not Available
Enzyme 107 [top]
Enzyme 107 ID 15864
Enzyme 107 Name Histone-lysine N-methyltransferase EZH1
Enzyme 107 Synonyms
  1. ENX-2
  2. Enhancer of zeste homolog 1
Enzyme 107 Gene Name EZH1
Enzyme 107 Protein Sequence >Histone-lysine N-methyltransferase EZH1
MEIPNPPTSKCITYWKRKVKSEYMRLRQLKRLQANMGAKALYVANFAKVQEKTQILNEEW
KKLRVQPVQSMKPVSGHPFLKKCTIESIFPGFASQHMLMRSLNTVALVPIMYSWSPLQQN
FMVEDETVLCNIPYMGDEVKEEDETFIEELINNYDGKVHGEEEMIPGSVLISDAVFLELV
DALNQYSDEEEEGHNDTSDGKQDDSKEDLPVTRKRKRHAIEGNKKSSKKQFPNDMIFSAI
ASMFPENGVPDDMKERYRELTEMSDPNALPPQCTPNIDGPNAKSVQREQSLHSFHTLFCR
RCFKYDCFLHPFHATPNVYKRKNKEIKIEPEPCGTDCFLLLEGAKEYAMLHNPRSKCSGR
RRRRHHIVSASCSNASASAVAETKEGDSDRDTGNDWASSSSEANSRCQTPTKQKASPAPP
QLCVVEAPSEPVEWTGAEESLFRVFHGTYFNNFCSIARLLGTKTCKQVFQFAVKESLILK
LPTDELMNPSQKKKRKHRLWAAHCRKIQLKKDNSSTQVYNYQPCDHPDRPCDSTCPCIMT
QNFCEKFCQCNPDCQNRFPGCRCKTQCNTKQCPCYLAVRECDPDLCLTCGASEHWDCKVV
SCKNCSIQRGLKKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKVYD
KYMSSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVVMVNGDHRIGIFAKRAIQAG
EELFFDYRYSQADALKYVGIERETDVL
Enzyme 107 Number of Residues 747
Enzyme 107 Molecular Weight 85270.4
Enzyme 107 Theoretical pI 7.77
Enzyme 107 GO Classification
Function
  • DNA binding
  • binding
  • nucleic acid binding
Process
Component
Enzyme 107 General Function Involved in DNA binding
Enzyme 107 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 107 Pathways Not Available
Enzyme 107 Reactions
  • S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
Enzyme 107 Pfam Domain Function
Enzyme 107 Signals
  • None
Enzyme 107 Transmembrane Regions
  • None
Enzyme 107 Essentiality Not Available
Enzyme 107 GenBank ID Protein 19923202 Link Image
Enzyme 107 UniProtKB/Swiss-Prot ID Q92800 Link Image
Enzyme 107 UniProtKB/Swiss-Prot Entry Name EZH1_HUMAN Link Image
Enzyme 107 PDB ID Not Available
Enzyme 107 Cellular Location Not Available
Enzyme 107 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 107 GenBank Gene ID NM_001991.3 Link Image
Enzyme 107 GeneCard ID EZH1 Link Image
Enzyme 107 GenAtlas ID EZH1 Link Image
Enzyme 107 HGNC ID HGNC:3526 Link Image
Enzyme 107 Chromosome Location 1
Enzyme 107 Locus 17q21.1-q21.3
Enzyme 107 SNPs SNPJam Report Link Image
Enzyme 107 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 107 Metabolite References Not Available
Enzyme 108 [top]
Enzyme 108 ID 15865
Enzyme 108 Name Enhancer of zeste homolog 2 (Drosophila) (Enhancer of zeste homolog 2 (Drosophila), isoform CRA_a)
Enzyme 108 Synonyms Not Available
Enzyme 108 Gene Name EZH2
Enzyme 108 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 108 Number of Residues 751
Enzyme 108 Molecular Weight 86019
Enzyme 108 Theoretical pI 7.22
Enzyme 108 GO Classification
Function
  • DNA binding
  • binding
  • nucleic acid binding
Process
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 108 General Function Not Available
Enzyme 108 Specific Function Not Available
Enzyme 108 Pathways Not Available
Enzyme 108 Reactions Not Available
Enzyme 108 Pfam Domain Function
Enzyme 108 Signals
  • None
Enzyme 108 Transmembrane Regions
  • None
Enzyme 108 Essentiality Not Available
Enzyme 108 GenBank ID Protein Not Available
Enzyme 108 UniProtKB/Swiss-Prot ID Q96FI6 Link Image
Enzyme 108 UniProtKB/Swiss-Prot Entry Name Q96FI6_HUMAN Link Image
Enzyme 108 PDB ID Not Available
Enzyme 108 Cellular Location Not Available
Enzyme 108 Gene Sequence Not Available
Enzyme 108 GenBank Gene ID BC010858 Link Image
Enzyme 108 GeneCard ID Q96FI6 Link Image
Enzyme 108 GenAtlas ID EZH2 Link Image
Enzyme 108 HGNC ID HGNC:3527 Link Image
Enzyme 108 Chromosome Location Not Available
Enzyme 108 Locus Not Available
Enzyme 108 SNPs SNPJam Report Link Image
Enzyme 108 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 108 Metabolite References Not Available
Enzyme 109 [top]
Enzyme 109 ID 15866
Enzyme 109 Name cDNA FLJ75818, highly similar to Homo sapiens PR/SET domain containing protein 8 (SET8), mRNA
Enzyme 109 Synonyms Not Available
Enzyme 109 Gene Name Not Available
Enzyme 109 Protein Sequence >cDNA FLJ75818, highly similar to Homo sapiens PR/SET domain containing protein 8 (SET8), mRNA
MARGRKMSKPRAVEAAAAAAAVAATAPGPEMVERRGPGRPRTDGENVFTGQSKIYSYMSP
NKCSGMRFPLQEENSVTHHEVKCQGKPLAGIYRKREEKRNAGNAVRSAMKSEEQKIKDAR
KGPLVPFPNQKSEAAEPPKTPPSSCDSTNAAIAKQALKKPIKGKQAPRKKAQGKTQQNRK
LTDFYPVRRSSRKSKAELQSEERKRIDELIESGKEEGMKIDLIDGKGRGVIATKQFSRGD
FVVEYHGDLIEITDAKKREALYAQDPSTGCYMYYFQYLSKTYCVDATRETNRLGRLINHS
KCGNCQTKLHDIDGVPHLILIASRDIAAGEELLYDYGDRSKASIEAHPWLKH
Enzyme 109 Number of Residues 352
Enzyme 109 Molecular Weight 39223
Enzyme 109 Theoretical pI 10.12
Enzyme 109 GO Classification Not Available
Enzyme 109 General Function Not Available
Enzyme 109 Specific Function Not Available
Enzyme 109 Pathways Not Available
Enzyme 109 Reactions Not Available
Enzyme 109 Pfam Domain Function Not Available
Enzyme 109 Signals
  • None
Enzyme 109 Transmembrane Regions
  • None
Enzyme 109 Essentiality Not Available
Enzyme 109 GenBank ID Protein Not Available
Enzyme 109 UniProtKB/Swiss-Prot ID A8K9D0 Link Image
Enzyme 109 UniProtKB/Swiss-Prot Entry Name A8K9D0_HUMAN Link Image
Enzyme 109 PDB ID Not Available
Enzyme 109 Cellular Location Not Available
Enzyme 109 Gene Sequence Not Available
Enzyme 109 GenBank Gene ID AK292645 Link Image
Enzyme 109 GeneCard ID A8K9D0 Link Image
Enzyme 109 GenAtlas ID Not Available
Enzyme 109 HGNC ID Not Available
Enzyme 109 Chromosome Location Not Available
Enzyme 109 Locus Not Available
Enzyme 109 SNPs Not Available
Enzyme 109 General References Not Available
Enzyme 109 Metabolite References Not Available
Enzyme 110 [top]
Enzyme 110 ID 15867
Enzyme 110 Name Wolf-Hirschhorn syndrome candidate 1 (Wolf-Hirschhorn syndrome candidate 1, isoform CRA_e)
Enzyme 110 Synonyms Not Available
Enzyme 110 Gene Name WHSC1
Enzyme 110 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 110 Number of Residues 1365
Enzyme 110 Molecular Weight 152259
Enzyme 110 Theoretical pI 8.81
Enzyme 110 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 110 General Function Not Available
Enzyme 110 Specific Function Not Available
Enzyme 110 Pathways Not Available
Enzyme 110 Reactions Not Available
Enzyme 110 Pfam Domain Function
Enzyme 110 Signals
  • None
Enzyme 110 Transmembrane Regions
  • None
Enzyme 110 Essentiality Not Available
Enzyme 110 GenBank ID Protein Not Available
Enzyme 110 UniProtKB/Swiss-Prot ID A2A2T3 Link Image
Enzyme 110 UniProtKB/Swiss-Prot Entry Name A2A2T3_HUMAN Link Image
Enzyme 110 PDB ID Not Available
Enzyme 110 Cellular Location Not Available
Enzyme 110 Gene Sequence Not Available
Enzyme 110 GenBank Gene ID AL132868 Link Image
Enzyme 110 GeneCard ID A2A2T3 Link Image
Enzyme 110 GenAtlas ID Not Available
Enzyme 110 HGNC ID Not Available
Enzyme 110 Chromosome Location Not Available
Enzyme 110 Locus Not Available
Enzyme 110 SNPs SNPJam Report Link Image
Enzyme 110 General References Not Available
Enzyme 110 Metabolite References Not Available
Enzyme 111 [top]
Enzyme 111 ID 15868
Enzyme 111 Name EHMT1 protein
Enzyme 111 Synonyms Not Available
Enzyme 111 Gene Name EHMT1
Enzyme 111 Protein Sequence >EHMT1 protein
MAAADAEAVPARGEPQQDCCVKTELLGEETPMAADEGSAEKQAGEAHMAADGETNGSCEN
SDASSHANAAKHTQDSARVNPQDGTNTLTRIAENGVSERDSEAAKQNHVTADDFVQTSVI
GSNGYILNKPALQAQPLRTTSTLASSLPGHAAKTLPGGAGKGRTPSAFPQTPAAPPATLG
EGSADTEDRKLPAPGADVKVHRARKTMPKSVVGLHAASKDPREVREARDHKEPKEEINKN
ISDFGRQQLLPPFPSLHQSLPQNQCYMATTKSQTACLPFVLAAAVSRKKKRRMGTYSLVP
KKKTKVLKQRTVIEMFKSITHSTVGSKGEKDLGASSLHVNGESLEMDSDEDDSEELEEDD
GHGAEQAAAFPTEDSRTSKESMSEADRAQKMDGESEEEQESVDTGEEEEGGDESDLSSES
SIKKKFLKRKGKTDSPWIKPARKRRRRSRKKPSGALGSESYKSSAGSAEQTAPGDSTGYM
EVSLDSLDLRVKGILSSQAEGLANGPDVLETDGLQEVPLCSCRMETPKSREITTLANNQC
MATESVDHELGRCTDSVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCGYFCTAGNF
MECQPESSISHRFHKDCASRVNNASYCPHCGEESSKAKEVTIAKADTTSTVTPVPGQEKG
SALEGRADTTTGSAAGPPLSEDDKLQGAASHVPEGFDPTGPAGLGRPTPGLSQGPGKETL
ESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQNKRSPLHAA
AEAGHVDICHMLVQFCRLGSPRSRGCLW
Enzyme 111 Number of Residues 808
Enzyme 111 Molecular Weight 86703.8
Enzyme 111 Theoretical pI 6.18
Enzyme 111 GO Classification Not Available
Enzyme 111 General Function Not Available
Enzyme 111 Specific Function Not Available
Enzyme 111 Pathways Not Available
Enzyme 111 Reactions Not Available
Enzyme 111 Pfam Domain Function Not Available
Enzyme 111 Signals
  • None
Enzyme 111 Transmembrane Regions
  • None
Enzyme 111 Essentiality Not Available
Enzyme 111 GenBank ID Protein 28704074 Link Image
Enzyme 111 UniProtKB/Swiss-Prot ID Q86X08 Link Image
Enzyme 111 UniProtKB/Swiss-Prot Entry Name Q86X08_HUMAN Link Image
Enzyme 111 PDB ID Not Available
Enzyme 111 Cellular Location Not Available
Enzyme 111 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 111 GenBank Gene ID BC047504 Link Image
Enzyme 111 GeneCard ID EHMT1 Link Image
Enzyme 111 GenAtlas ID EHMT1 Link Image
Enzyme 111 HGNC ID HGNC:24650 Link Image
Enzyme 111 Chromosome Location 9
Enzyme 111 Locus 9q34.3
Enzyme 111 SNPs SNPJam Report Link Image
Enzyme 111 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 111 Metabolite References Not Available
Enzyme 112 [top]
Enzyme 112 ID 15869
Enzyme 112 Name cDNA FLJ78356, highly similar to Homo sapiens PIMT isozyme I
Enzyme 112 Synonyms Not Available
Enzyme 112 Gene Name Not Available
Enzyme 112 Protein Sequence >cDNA FLJ78356, highly similar to Homo sapiens PIMT isozyme I
MAWKSGGASHSELIHNLRKNGIIKTDKVFEVMLATDRSHYAKCNPYMDSPQSIGFQATIS
APHMHAYALELLFDQLHEGAKALDVGSGSGILTACFARMVGCTGKVIGIDHIKELVDDSV
NNVRKDDPTLLSSGRVQLVVGDGRMGYAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLI
LPVGPAGGNQMLEQYDKLQDGSIKMKPLMGVIYVPLTDKEKQWSRWK
Enzyme 112 Number of Residues 227
Enzyme 112 Molecular Weight 24637
Enzyme 112 Theoretical pI 7.25
Enzyme 112 GO Classification Not Available
Enzyme 112 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 112 Specific Function Not Available
Enzyme 112 Pathways Not Available
Enzyme 112 Reactions Not Available
Enzyme 112 Pfam Domain Function Not Available
Enzyme 112 Signals
  • None
Enzyme 112 Transmembrane Regions
  • None
Enzyme 112 Essentiality Not Available
Enzyme 112 GenBank ID Protein Not Available
Enzyme 112 UniProtKB/Swiss-Prot ID A8K109 Link Image
Enzyme 112 UniProtKB/Swiss-Prot Entry Name A8K109_HUMAN Link Image
Enzyme 112 PDB ID 1KR5 Link Image
Enzyme 112 PDB File Show
Enzyme 112 3D Structure
Enzyme 112 Cellular Location Not Available
Enzyme 112 Gene Sequence Not Available
Enzyme 112 GenBank Gene ID AK289724 Link Image
Enzyme 112 GeneCard ID A8K109 Link Image
Enzyme 112 GenAtlas ID Not Available
Enzyme 112 HGNC ID Not Available
Enzyme 112 Chromosome Location Not Available
Enzyme 112 Locus Not Available
Enzyme 112 SNPs Not Available
Enzyme 112 General References Not Available
Enzyme 112 Metabolite References Not Available
Enzyme 113 [top]
Enzyme 113 ID 15870
Enzyme 113 Name Protein arginine methyltransferase 5, isoform CRA_d
Enzyme 113 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 113 Gene Name PRMT5
Enzyme 113 Protein Sequence >Protein arginine methyltransferase 5, isoform CRA_d
MRGPNSGTEKGRLVIPEKQGFDFLCMPVFHPRFKREFIQEPAKNRPGPQTRSDLLLSGRD
WNTLIVGKLSPWIRPDSKVEKIRRNSEAAMLQELNFGAYLGLPAFLLPLNQEDNTNLARV
LTNHIHTGHHSSMFWMRVPLVAPEDLRDDIIENAPTTHTEEYSGEEKTWMWWHNFRTLCD
YSKRIAVALEIGADLPSNHVIDRWLGEPIKAAILPTSIFLTNKKGFPVLSKMHQRLIFRL
LKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELFAKGYEDYLQSPLQPLMD
NLESQTYEVFEKDPIKYSQYQQAIYKCLLDRVPEEEKDTNVQVLMVLGAGRGPLVNASLR
AAKQADRRIKLYAVEKNPNAVVTLENWQFEEWGSQVTVVSSDMREWVAPEKADIIVSELL
GSFADNELSPECLDGAQHFLKDDGVSIPGEYTSFLAPISSSKLYNEVRACREKDRDPEAQ
FEMPYVVRLHNFHQLSAPQPCFTFSHPNRDPMIDNNRYCTLEFPVEVNTVLHGFAGYFET
VLYQDITLSIRPETHSPGMFSWFPILFPIKQPITVREGQTICVRFWRCSNSKKVWYEWAV
TAPVCSAIHNPTGRSYTIGL
Enzyme 113 Number of Residues 620
Enzyme 113 Molecular Weight 71319.8
Enzyme 113 Theoretical pI 6.42
Enzyme 113 GO Classification
Function
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 113 General Function Involved in methyltransferase activity
Enzyme 113 Specific Function Not Available
Enzyme 113 Pathways Not Available
Enzyme 113 Reactions Not Available
Enzyme 113 Pfam Domain Function
Enzyme 113 Signals
  • None
Enzyme 113 Transmembrane Regions
  • None
Enzyme 113 Essentiality Not Available
Enzyme 113 GenBank ID Protein 193786772 Link Image
Enzyme 113 UniProtKB/Swiss-Prot ID A8MZ91 Link Image
Enzyme 113 UniProtKB/Swiss-Prot Entry Name A8MZ91_HUMAN Link Image
Enzyme 113 PDB ID Not Available
Enzyme 113 Cellular Location Not Available
Enzyme 113 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 113 GenBank Gene ID AK075251 Link Image
Enzyme 113 GeneCard ID PRMT5 Link Image
Enzyme 113 GenAtlas ID PRMT5 Link Image
Enzyme 113 HGNC ID HGNC:10894 Link Image
Enzyme 113 Chromosome Location 1
Enzyme 113 Locus 14q11.2
Enzyme 113 SNPs SNPJam Report Link Image
Enzyme 113 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 113 Metabolite References Not Available
Enzyme 114 [top]
Enzyme 114 ID 15871
Enzyme 114 Name Uncharacterized protein CARM1 (Coactivator-associated arginine methyltransferase 1, isoform CRA_b)
Enzyme 114 Synonyms Not Available
Enzyme 114 Gene Name CARM1
Enzyme 114 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 114 Number of Residues 608
Enzyme 114 Molecular Weight 65854
Enzyme 114 Theoretical pI 6.73
Enzyme 114 GO Classification Not Available
Enzyme 114 General Function Not Available
Enzyme 114 Specific Function Not Available
Enzyme 114 Pathways Not Available
Enzyme 114 Reactions Not Available
Enzyme 114 Pfam Domain Function
Enzyme 114 Signals
  • None
Enzyme 114 Transmembrane Regions
  • None
Enzyme 114 Essentiality Not Available
Enzyme 114 GenBank ID Protein Not Available
Enzyme 114 UniProtKB/Swiss-Prot ID A6NN38 Link Image
Enzyme 114 UniProtKB/Swiss-Prot Entry Name A6NN38_HUMAN Link Image
Enzyme 114 PDB ID Not Available
Enzyme 114 Cellular Location Not Available
Enzyme 114 Gene Sequence Not Available
Enzyme 114 GenBank Gene ID AC011442 Link Image
Enzyme 114 GeneCard ID A6NN38 Link Image
Enzyme 114 GenAtlas ID CARM1 Link Image
Enzyme 114 HGNC ID HGNC:23393 Link Image
Enzyme 114 Chromosome Location 19
Enzyme 114 Locus 19p13.2
Enzyme 114 SNPs SNPJam Report Link Image
Enzyme 114 General References Not Available
Enzyme 114 Metabolite References Not Available
Enzyme 115 [top]
Enzyme 115 ID 16535
Enzyme 115 Name Methionine adenosyltransferase II, beta, isoform CRA_a
Enzyme 115 Synonyms
  1. SubName: cDNA, FLJ92687, Homo sapiens methionine adenosyltransferase II, beta (MAT2B), mRNA
Enzyme 115 Gene Name MAT2B
Enzyme 115 Protein Sequence >Methionine adenosyltransferase II, beta, isoform CRA_a
MVGREKELSIHFVPGSCRLVEEEVNIPNRRVLVTGATGLLGRAVHKEFQQNNWHAVGCGF
RRARPKFEQVNLLDSNAVHHIIHDFQPHVIVHCAAERRPDVVENQPDAASQLNVDASGNL
AKEAAAVGAFLIYISSDYVFDGTNPPYREEDIPAPLNLYGKTKLDGEKAVLENNLGAAVL
RIPILYGEVEKLEESAVTVMFDKVQFSNKSANMDHWQQRFPTHVKDVATVCRQLAEKRML
DPSIKGTFHWSGNEQMTKYEMACAIADAFNLPSSHLRPITDSPVLGAQRPRNAQLDCSKL
ETLGIGQRTPFRIGIKESLWPFLIDKRWRQTVFH
Enzyme 115 Number of Residues 334
Enzyme 115 Molecular Weight 37552
Enzyme 115 Theoretical pI 7.39
Enzyme 115 GO Classification
Function
  • catalytic activity
  • dTDP-4-dehydrorhamnose reductase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • carbohydrate biosynthesis
  • extracellular polysaccharide biosynthesis
  • macromolecule biosynthesis
  • macromolecule metabolism
  • metabolism
  • physiological process
  • polysaccharide biosynthesis
Component
Enzyme 115 General Function Cell wall/membrane/envelope biogenesis
Enzyme 115 Specific Function Not Available
Enzyme 115 Pathways Not Available
Enzyme 115 Reactions Not Available
Enzyme 115 Pfam Domain Function
Enzyme 115 Signals
  • None
Enzyme 115 Transmembrane Regions
  • None
Enzyme 115 Essentiality Not Available
Enzyme 115 GenBank ID Protein Not Available
Enzyme 115 UniProtKB/Swiss-Prot ID B2R5Y6 Link Image
Enzyme 115 UniProtKB/Swiss-Prot Entry Name B2R5Y6_HUMAN Link Image
Enzyme 115 PDB ID Not Available
Enzyme 115 Cellular Location Not Available
Enzyme 115 Gene Sequence Not Available
Enzyme 115 GenBank Gene ID AK312365 Link Image
Enzyme 115 GeneCard ID B2R5Y6 Link Image
Enzyme 115 GenAtlas ID Not Available
Enzyme 115 HGNC ID Not Available
Enzyme 115 Chromosome Location Not Available
Enzyme 115 Locus Not Available
Enzyme 115 SNPs SNPJam Report Link Image
Enzyme 115 General References Not Available
Enzyme 115 Metabolite References Not Available
Enzyme 116 [top]
Enzyme 116 ID 16701
Enzyme 116 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 116 Synonyms Not Available
Enzyme 116 Gene Name SUV39H1
Enzyme 116 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 116 Number of Residues 412
Enzyme 116 Molecular Weight 47908
Enzyme 116 Theoretical pI 8.07
Enzyme 116 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 116 General Function Not Available
Enzyme 116 Specific Function S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N(6)-methyl-L-lysine
Enzyme 116 Pathways Not Available
Enzyme 116 Reactions Not Available
Enzyme 116 Pfam Domain Function
Enzyme 116 Signals
  • None
Enzyme 116 Transmembrane Regions
  • None
Enzyme 116 Essentiality Not Available
Enzyme 116 GenBank ID Protein Not Available
Enzyme 116 UniProtKB/Swiss-Prot ID B2R6E8 Link Image
Enzyme 116 UniProtKB/Swiss-Prot Entry Name B2R6E8_HUMAN Link Image
Enzyme 116 PDB ID Not Available
Enzyme 116 Cellular Location Not Available
Enzyme 116 Gene Sequence Not Available
Enzyme 116 GenBank Gene ID AK312547 Link Image
Enzyme 116 GeneCard ID B2R6E8 Link Image
Enzyme 116 GenAtlas ID Not Available
Enzyme 116 HGNC ID Not Available
Enzyme 116 Chromosome Location Not Available
Enzyme 116 Locus Not Available
Enzyme 116 SNPs SNPJam Report Link Image
Enzyme 116 General References Not Available
Enzyme 116 Metabolite References Not Available
Enzyme 117 [top]
Enzyme 117 ID 16702
Enzyme 117 Name RNA (Guanine-7-) methyltransferase
Enzyme 117 Synonyms
  1. SubName: RNA (Guanine-7-) methyltransferase, isoform CRA_a
Enzyme 117 Gene Name RNMT
Enzyme 117 Protein Sequence >RNA (Guanine-7-) methyltransferase
MANSAKAEEYEKMSLEQAKASVNSETESSFNINENTTASGTGLSEKTSVCRQVDIARKRK
EFEDDLVKESSSCGKDTPSKKRKLDPEIVPEEKDCGDAEGNSKKRKRETEDVPKDKSSTG
DGTQNKRKIALEDVPEKQKNLEEGHSSTVAAHYNELQEVGLEKRSQSRIFYLRNFNNWMK
SVLIGEFLEKVRQKKKRDITVLDLGCGKGGDLLKWKKGRINKLVCTDIADVSVKQCQQRY
EDMKNRRDSEYIFSAEFITADSSKELLIDKFRDPQMCFDICSCQFVCHYSFESYEQADMM
LRNACERLSPGGYFIGTTPNSFELIRRLEASETESFGNEIYTVKFQKKGDYPLFGCKYDF
NLEGVVDVPEFLVYFPLLNEMAKKYNMKLVYKKTFLEFYEEKIKNNENKMLLKRMQALEP
YPANESSKLVSEKVDDYEHAAKYMKNSQVRLPLGTLSKSEWEATSIYLVFAFEKQQ
Enzyme 117 Number of Residues 476
Enzyme 117 Molecular Weight 54845
Enzyme 117 Theoretical pI 6.54
Enzyme 117 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 117 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 117 Specific Function Not Available
Enzyme 117 Pathways Not Available
Enzyme 117 Reactions Not Available
Enzyme 117 Pfam Domain Function
Enzyme 117 Signals
  • None
Enzyme 117 Transmembrane Regions
  • None
Enzyme 117 Essentiality Not Available
Enzyme 117 GenBank ID Protein Not Available
Enzyme 117 UniProtKB/Swiss-Prot ID B0YJ90 Link Image
Enzyme 117 UniProtKB/Swiss-Prot Entry Name B0YJ90_HUMAN Link Image
Enzyme 117 PDB ID Not Available
Enzyme 117 Cellular Location Not Available
Enzyme 117 Gene Sequence Not Available
Enzyme 117 GenBank Gene ID EF445026 Link Image
Enzyme 117 GeneCard ID B0YJ90 Link Image
Enzyme 117 GenAtlas ID Not Available
Enzyme 117 HGNC ID Not Available
Enzyme 117 Chromosome Location 18
Enzyme 117 Locus 18p11.22-p11.23
Enzyme 117 SNPs SNPJam Report Link Image
Enzyme 117 General References Not Available
Enzyme 117 Metabolite References Not Available
Enzyme 118 [top]
Enzyme 118 ID 16703
Enzyme 118 Name DPH5 homolog (S. cerevisiae), isoform CRA_e
Enzyme 118 Synonyms
  1. SubName: cDNA FLJ43496 fis, clone PEBLM2001465, highly similar to Probable diphthine synthase (EC 2.1.1.98)
Enzyme 118 Gene Name DPH5
Enzyme 118 Protein Sequence >DPH5 homolog (S. cerevisiae), isoform CRA_e
MNAVGCCGLQLYKFGETVSIVFWTDTWRPESFFDKVKKNRQNGMHTLCLLDIKVKEQSLE
NLIKGRKIYEPPRYMSVNQAAQQLLEIVQNQRIRGEEPAVTEETLCVGLARVGADDQKIA
AGTLRQMCTVDLGEPLHSLIITGGSIHPMEMEMLSLFSIPENSSESQSINGL
Enzyme 118 Number of Residues 172
Enzyme 118 Molecular Weight 19244.0
Enzyme 118 Theoretical pI 5.29
Enzyme 118 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 118 General Function Involved in methyltransferase activity
Enzyme 118 Specific Function Not Available
Enzyme 118 Pathways Not Available
Enzyme 118 Reactions Not Available
Enzyme 118 Pfam Domain Function Not Available
Enzyme 118 Signals
  • None
Enzyme 118 Transmembrane Regions
  • None
Enzyme 118 Essentiality Not Available
Enzyme 118 GenBank ID Protein 193785050 Link Image
Enzyme 118 UniProtKB/Swiss-Prot ID B3KWP1 Link Image
Enzyme 118 UniProtKB/Swiss-Prot Entry Name B3KWP1_HUMAN Link Image
Enzyme 118 PDB ID Not Available
Enzyme 118 Cellular Location Not Available
Enzyme 118 Gene Sequence >519 bp
ATGAATGCTGTAGGCTGCTGTGGTTTACAGTTATATAAGTTTGGAGAGACAGTTTCTATT
GTTTTTTGGACAGACACTTGGAGACCAGAAAGCTTCTTTGACAAAGTGAAGAAGAACAGA
CAAAATGGCATGCACACATTATGTTTACTAGACATCAAAGTAAAGGAGCAGTCTTTGGAA
AATCTAATCAAGGGAAGGAAGATCTATGAACCTCCACGGTATATGAGTGTAAACCAAGCA
GCCCAGCAGCTTCTGGAGATTGTTCAAAATCAAAGAATACGAGGAGAAGAACCAGCAGTT
ACCGAGGAGACACTTTGTGTTGGCTTAGCCAGGGTTGGAGCCGACGACCAGAAAATTGCA
GCAGGCACTTTAAGGCAAATGTGCACTGTGGACTTGGGAGAACCATTGCATTCCTTGATC
ATCACAGGAGGCAGCATACATCCAATGGAGATGGAGATGCTAAGTCTGTTTTCCATACCA
GAAAATAGCTCAGAATCTCAAAGCATCAATGGACTTTGA
Enzyme 118 GenBank Gene ID AK125485 Link Image
Enzyme 118 GeneCard ID DPH5 Link Image
Enzyme 118 GenAtlas ID DPH5 Link Image
Enzyme 118 HGNC ID HGNC:24270 Link Image
Enzyme 118 Chromosome Location 1
Enzyme 118 Locus 1p21.2
Enzyme 118 SNPs SNPJam Report Link Image
Enzyme 118 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 118 Metabolite References Not Available