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

• Cytoplasm (Predicted from LogP)
• endoplasmic reticulum
• mitochondria
• nucleus

• Blood
• Cerebrospinal Fluid
• Urine

• 125853 (Diabetes mellitus type 2)

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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
16. Wikipedia

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, H3 lysine-4 specific SET7
8. S-adenosylmethionine synthetase isoform type-2
9. Phenylethanolamine N-methyltransferase
10. Probable diphthine synthase
11. Arsenite methyltransferase
12. tRNA
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
19. Hexaprenyldihydroxybenzoate methyltransferase, mitochondrial precursor
20. S-adenosylmethionine synthetase isoform type-1
21. Histone-lysine N-methyltransferase, H3 lysine-9 specific 3
22. S-adenosylmethionine decarboxylase proenzyme
23. Methionine synthase reductase, mitochondrial precursor
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. Lipoic acid synthetase, mitochondrial precursor
37. Protein arginine N-methyltransferase 5
38. Histone-lysine N-methyltransferase, H3 lysine-4 specific SET1
39. rRNA 2'-O-methyltransferase fibrillarin
40. Zinc finger protein HRX
41. Molybdenum cofactor biosynthesis protein 1 A
42. DNA
43. DNA
44. tRNA
45. Histone-lysine N-methyltransferase, H4 lysine-20 specific
46. Myeloid/lymphoid or mixed-lineage leukemia protein 3 homolog
47. Methionine adenosyltransferase 2 subunit beta
48. Histone-lysine N-methyltransferase SETDB2
49. Solute carrier family 25 member 26
50. tRNA
51. Histamine N-methyltransferase
52. Adenosylmethionine decarboxylase 1
53. Ubiquinone biosynthesis methyltransferase COQ5, mitochondrial precursor
54. tRNA wybutosine-synthesizing protein 1 homolog
55. tRNA wybutosine-synthesizing protein 1 homolog B
56. Molybdenum cofactor biosynthesis protein 1 B
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. Enhancer of zeste homolog 2
65. Uncharacterized protein ENSP00000339522
66. Leucine carboxyl methyltransferase 2
67. mRNA cap guanine-N7 methyltransferase
68. Putative S-adenosyl-L-methionine-dependent methyltransferase METT5D1
69. 7SK snRNA methylphosphate capping enzyme
70. Myeloid/lymphoid or mixed-lineage leukemia protein 2
71. WW domain-binding protein 7
72. Myeloid/lymphoid or mixed-lineage leukemia protein 5
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 precursor
85. SET domain-containing protein 1B
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. Mitochondrial dimethyladenosine transferase 1, mitochondrial precursor
93. Mitochondrial dimethyladenosine transferase 2, mitochondrial precursor
94. tRNA guanosine-2'-O-methyltransferase TRM11 homolog
95. Coiled-coil domain-containing protein 76
96. N(2),N(2)-dimethylguanosine tRNA methyltransferase
97. tRNA
98. tRNA
99. Potential tRNA
100. tRNA
101. tRNA wybutosine-synthesizing protein 2 homolog
102. tRNA wybutosine-synthesizing protein 3 homolog
103. Not Available
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. Enhancer of zeste homolog 1
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. Uncharacterized protein PRMT5 (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. cDNA FLJ43496 fis, clone PEBLM2001465, highly similar to Probable diphthine synthase (EC 2.1.1.98)

1. PEAMT
2. PEMT
3. PEMT2

MTRLLGYVDPLDPSFVAAVITITFNPLYWNVVARWEHKTRKLSRAFGSPYLACYSLSVTI
LLLNFLRSHCFTQAMLSQPRMESLDTPAAYSLGLALLGLGVVLVLSSFFALGFAGTFLGD
YFGILKEARVTVFPFNILDNPMYWGSTANYLGWAIMHASPTGLLLTVLVALTYIMALLYE
EPFTAEIYRQKASGSHKRS

• Phospholipid Synthesis (map00564 )
• Glycine, Serine and Threonine Metabolism (map00260 )

• S-adenosyl-L-methionine + phosphatidylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine

• PEMT (PF04191 )

• None

• 13-33 46-66 94-114 158-178

ATGACCCGGCTGCTGGGCTACGTGGACCCCCTGGATCCCAGCTTTGTGGCTGCCGTCATC
ACCATCACCTTCAATCCGCTCTACTGGAATGTGGTTGCACGATGGGAACACAAGACCCGC
AAGCTGAGCAGGGCCTTCGGATCCCCCTACCTGGCCTGCTACTCTCTAAGCGTCACCATC
CTGCTCCTGAACTTCCTGCGCTCGCACTGCTTCACGCAGGCCATGCTGAGCCAGCCCAGG
ATGGAGAGCCTGGACACCCCCGCGGCCTACAGCCTGGGCCTCGCGCTCCTGGGACTGGGC
GTCGTGCTCGTGCTCTCCAGCTTCTTTGCACTGGGGTTCGCTGGAACTTTCCTAGGTGAT
TACTTCGGGATCCTCAAGGAGGCGAGAGTGACCGTGTTCCCCTTCAACATCCTGGACAAC
CCCATGTACTGGGGAAGCACAGCCAACTACTTGGGCTGGGCCATCATGCACGCCAGCCCC
ACGGGCCTGCTCCTGACGGTGCTGGTGGCCCTCACCTACATAATGGCTCTCCTATACGAA
GAGCCCTTCACCGCTGAGATCTACCGGCAGAAAGCCTCCGGGTCCCACAAGAGGAGCTGA

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 ]
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 ]
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 ]

1. HIOMT
2. Acetylserotonin O-methyltransferase
3. ASMT

MGSSEDQAYRLLNDYANGFMVSQVLFAACELGVFDLLAEAPGPLDVAAVAAGVRASAHGT
ELLLDICVSLKLLKVETRGGKAFYRNTELSSDYLTTVSPTSQCSMLKYMGRTSYRCWGHL
ADAVREGRNQYLETFGVPAEELFTAIYRSEGERLQFMQALQEVWSVNGRSVLTAFDLSVF
PLMCDLGGGAGALAKECMSLYPGCKITVFDIPEVVWTAKQHFSFQEEEQIDFQEGDFFKD
PLPEADLYILARVLHDWADGKCSHLLERIYHTCKPGGGILVIESLLDEDRRGPLLTQLYS
LNMLVQTEGQERTPTHYHMLLSSAGFRDFQFKKTGAIYDAILARK

• Tryptophan Metabolism (map00380 )

• S-adenosyl-L-methionine + N-acetylserotonin = S-adenosyl-L-homocysteine + melatonin

• Methyltransf_2 (PF00891 )

• None

• None

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 ]
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 ]

1. 5-methyltetrahydrofolate-- homocysteine methyltransferase
2. Methionine synthase, vitamin-B12 dependent
3. MS

MSPALQDLSQPEGLKKTLRDEINAILQKRIMVLDGGMGTMIQREKLNEEHFRGQEFKDHA
RPLKGNNDILSITQPDVIYQIHKEYLLAGADIIETNTFSSTSIAQADYGLEHLAYRMNMC
SAGVARKAAEEVTLQTGIKRFVAGALGPTNKTLSVSPSVERPDYRNITFDELVEAYQEQA
KGLLDGGVDILLIETIFDTANAKAALFALQNLFEEKYAPRPIFISGTIVDKSGRTLSGQT
GEGFVISVSHGEPLCIGLNCALGAAEMRPFIEIIGKCTTAYVLCYPNAGLPNTFGDYDET
PSMMAKHLKDFAMDGLVNIVGGCCGSTPDHIREIAEAVKNCKPRVPPATAFEGHMLLSGL
EPFRIGPYTNFVNIGERCNVAGSRKFAKLIMAGNYEEALCVAKVQVEMGAQVLDVNMDDG
MLDGPSAMTRFCNLIASEPDIAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEDD
FLEKARKIKKYGAAMVVMAFDEEGQATETDTKIRVCTRAYHLLVKKLGFNPNDIIFDPNI
LTIGTGMEEHNLYAINFIHATKVIKETLPGARISGGLSNLSFSFRGMEAIREAMHGVFLY
HAIKSGMDMGIVNAGNLPVYDDIHKELLQLCEDLIWNKDPEATEKLLRYAQTQGTGGKKV
IQTDEWRNGPVEERLEYALVKGIEKHIIEDTEEARLNQKKYPRPLNIIEGPLMNGMKIVG
DLFGAGKMFLPQVIKSARVMKKAVGHLIPFMEKEREETRVLNGTVEEEDPYQGTIVLATV
KGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILKAALDHKADIIGLSGLITPSLDEM
IFVAKEMERLAIRIPLLIGGATTSKTHTAVKIAPRYSAPVIHVLDASKSVVVCSQLLDEN
LKDEYFEEIMEEYEDIRQDHYESLKERRYLPLSQARKSGFQMDWLSEPHPVKPTFIGTQV
FEDYDLQKLVDYIDWKPFFDVWQLRGKYPNRGFPKIFNDKTVGGEARKVYDDAHNMLNTL
ISQKKLRARGVVGFWPAQSIQDDIHLYAEAAVPQAAEPIATFYGLRQQAEKDSASTEPYY
CLSDFIAPLHSGIRDYLGLFAVACFGVEELSKAYEDDGDDYSSIMVKALGDRLAEAFAEE
LHERVRRELWAYCGSEQLDVADLRRLRYKGIRPAPGYPSQPDHTEKLTMWRLADIEQSTG
IRLTESLAMAPASAVSGLYFSNLKSKYFAVGKISKDQVEDYALRKNISVAEVEKWLGPIL
GYDTD

• Methionine Metabolism (map00271 )
• One Carbon Pool By Folate (map00670 )

• 5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + L-methionine

• B12-binding (PF02310 )
• B12-binding_2 (PF02607 )
• Met_synt_B12 (PF02965 )
• Pterin_bind (PF00809 )
• S-methyl_trans (PF02574 )

• None

• None

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

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 ]
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 ]
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 ]
4. 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 ]

MPEAPPLLLAAVLLGLVLLVVLLLLLRHWGWGLCLIGWNEFILQPIHNLLMGDTKEQRIL
NHVLQHAEPGNAQSVLEAIDTYCEQKEWAMNVGDKKGKIVDAVIQEHQPSVLLELGAYCG
YSAVRMARLLSPGARLITIEINPDCAAITQRMVDFAGVKDKVTLVVGASQDIIPQLKKKY
DVDTLDMVFLDHWKDRYLPDTLLLEECGLLRKGTVLLADNVICPGAPDFLAHVRGSSCFE
CTHYQSFLEYREVVDGLEKAIYKGPGSEAGP

• Tyrosine Metabolism (map00350 )

• S-adenosyl-L-methionine + a catechol = S-adenosyl-L-homocysteine + a guaiacol

• Methyltransf_3 (PF01596 )

• 1-32

ATGCCGGAGGCCCCGCCTCTGCTGTTGGCAGCTGTGTTGCTGGGCCTGGTGCTGCTGGTG
GTGCTGCTGCTGCTTCTGAGGCACTGGGGCTGGGGCCTGTGCCTTATCGGCTGGAACGAG
TTCATCCTGCAGCCCATCCACAACCTGCTCATGGGTGACACCAAGGAGCAGCGCATCCTG
AACCACGTGCTGCAGCATGCGGAGCCCGGGAACGCACAGAGCGTGCTGGAGGCCATTGAC
ACCTACTGCGAGCAGAAGGAGTGGGCCATGAACGTGGGCGACAAGAAAGGCAAGATCGTG
GACGCCGTGATTCAGGAGCACCAGCCCTCCGTGCTGCTGGAGCTGGGGGCCTACTGTGGC
TACTCAGCTGTGCGCATGGCCCGCCTGCTGTCACCAGGGGCGAGGCTCATCACCATCGAG
ATCAACCCCGACTGTGCCGCCATCACCCAGCGGATGGTGGATTTCGCTGGCGTGAAGGAC
AAGGTCACCCTTGTGGTTGGAGCGTCCCAGGACATCATCCCCCAGCTGAAGAAGAAGTAT
GATGTGGACACACTGGACATGGTCTTCCTCGACCACTGGAAGGACCGGTACCTGCCGGAC
ACGCTTCTCTTGGAGGAATGTGGCCTGCTGCGGAAGGGGACAGTGCTACTGGCTGACAAC
GTGATCTGCCCAGGTGCGCCAGACTTCCTAGCACACGTGCGCGGGAGCAGCTGCTTTGAG
TGCACACACTACCAATCGTTCCTGGAATACAGGGAGGTGGTGGACGGCCTGGAGAAGGCC
ATCTACAAGGGCCCAGGCAGCGAAGCAGGGCCCTGA

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 ]
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 ]
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 ]
4. Tilgmann C, Kalkkinen N: Purification and partial sequence analysis of the soluble catechol-O-methyltransferase from human placenta: comparison to the rat liver enzyme. Biochem Biophys Res Commun. 1991 Jan 31;174(2):995-1002. [PubMed ]
5. Ulmanen I, Lundstrom K: Cell-free synthesis of rat and human catechol O-methyltransferase. Insertion of the membrane-bound form into microsomal membranes in vitro. Eur J Biochem. 1991 Dec 18;202(3):1013-20. [PubMed ]
6. Lachman HM, Papolos DF, Saito T, Yu YM, Szumlanski CL, Weinshilboum RM: Human catechol-O-methyltransferase pharmacogenetics: description of a functional polymorphism and its potential application to neuropsychiatric disorders. Pharmacogenetics. 1996 Jun;6(3):243-50. [PubMed ]
7. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed ]

1. Histone H3-K79 methyltransferase
2. H3-K79-HMTase
3. DOT1-like protein

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

• Lysine Degradation (map00310 )

• S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine

• AT_hook (PF02178 )
• DOT1 (PF08123 )

• None

• None

ATGGGGGAGAAGCTGGAGCTGAGACTGAAGTCGCCCGTGGGGGCTGAGCCCGCCGTCTAC
CCGTGGCCGCTGCCGGTCTACGATAAACATCACGATGCTGCTCATGAAATCATCGAGACC
ATCCGATGGGTCTGTGAAGAAATCCCGGATCTCAAGCTCGCTATGGAGAATTACGTTTTA
ATTGACTATGACACCAAAAGCTTCGAGAGCATGCAGAGGCTCTGCGACAAGTACAACCGT
GCCATCGACAGCATCCACCAGCTGTGGAAGGGCACCACGCAGCCCATGAAGCTGAACACG
CGGCCGTCCACTGGACTCCTGCGCCATATCCTGCAGCAGGTCTACAACCACTCGGTGACC
GACCCCGAGAAGCTCAACAACTACGAGCCCTTCTCCCCCGAGGTGTACGGGGAGACCTCC
TTCGACCTGGTGGCCCAGATGATTGATGAGATCAAGATGACCGACGACGACCTGTTTGTG
GACTTGGGGAGCGGTGTGGGCCAGGTCGTGCTCCAGGTTGCTGCTGCCACCAACTGCAAA
CATCACTATGGCGTCGAGAAAGCAGACATCCCGGCCAAGTATGCGGAGACCATGGACCGC
GAGTTCAGGAAGTGGATGAAATGGTATGGAAAAAAGCATGCAGAATACACATTGGAGAGA
GGCGATTTCCTCTCAGAAGAGTGGAGGGAGCGAATCGCCAACACGAGTGTTATATTTGTG
AATAATTTTGCCTTTGGTCCTGAGGTGGATCACCAGCTGAAGGAGCGGTTTGCAAACATG
AAGGAAGGTGGCAGAATCGTGTCCTCGAAACCCTTTGCACCTCTGAACTTCAGAATAAAC
AGTAGAAACTTGAGTGACATCGGCACCATCATGCGCGTGGTGGAGCTCTCGCCCCTGAAG
GGCTCGGTGTCGTGGACGGGGAAGCCAGTCTCCTACTACCTGCACACTATCGACCGCACC
ATACTTGAAAACTATTTTTCTAGTCTGAAAAACCCAAAACTCAGGGAGGAACAGGAGGCA
GCCCGGCGCCGCCAGCAGCGCGAGAGCAAGAGCAACGCGGCCACGCCCACTAAGGGCCCA
GAGGGCAAGGTGGCCGGCCCCGCCGACGCCCCCATGGACTCTGGTGCTGAGGAAGAGAAG
GCGGGAGCAGCCACCGTGAAGAAGCCGTCTCCCTCCAAAGCCCGCAAGAAGAAGCTAAAC
AAGAAGGGGAGGAAGATGGCTGGCCGCAAGCGCGGGCGCCCCAAGAAGATGAACACTGCG
AACCCCGAGCGGAAGCCCAAGAAGAACCAAACTGCACTGGATGCCCTGCACGCTCAGACC
GTGTCTCAGACGGCGGCCTCCTCACCCCAGGATGCCTACAGATCCCCTCACAGCCCGTTC
TACCAGCTACCTCCGAGCGTGCAGCGGCACTCCCCCAACCCGCTGCTGGTGGCGCCCACC
CCGCCCGCGCTGCAGAAGCTTCTAGAGTCCTTCAAGATCCAGTACCTGCAGTTCCTGGCA
TACACAAAGACCCCCCAGTACAAGGCCAGCCTGCAGGAGCTGCTGGGCCAGGAGAAGGAG
AAGAACGCCCAGCTCCTGGGTGCGGCTCAGCAGCTCCTCAGCCACTGCCAGGCCCAGAAG
GAGGAGATCAGGAGGCTGTTTCAGCAAAAATTGGATGAGCTGGGTGTGAAGGCGCTGACC
TACAACGACCTGATTCAAGCGCAGAAGGAGATCTCCGCCCATAACCAGCAGCTGCGGGAG
CAGTCGGAGCAGCTGGAGCAGGACAACCGCGCGCTCCGCGGCCAGAGCTTGCAGCTGCTC
AAGGCTCGCTGCGAGGAGCTGCAGCTGGACTGGGCCACGCTGTCGCTGGAGAAGCTGTTG
AAGGAGAAGCAGGCCCTGAAGAGCCAGATCTCGGAGAAGCAGAGGCACTGCCTGGAGCTG
CAGATCAGCATTGTGGAGCTAGAGAAGAGCCAGCGGCAGCAGGAGCTCCTGCAGCTCAAG
TCCTGTGTGCCGCCTGACGACGCCCTGTCCCTGCACCTGCGTGGGAAGGGCGCCCTGGGC
CGCGAGCTGGAGCCTGACGCCAGCCGGCTGCACCTGGAGCTGGACTGCACCAAGTTCTCG
CTGCCTCACTTGAGCAGCATGAGCCCGGAGCTCTCCATGAACGGCCAGGCTGCTGGCTAT
GAGCTCTGCGGTGTGCTGAGCCGGCCTTCGTCGAAGCAGAACACGCCCCAGTACCTGGCC
TCACCCCTGGACCAGGAGGTGGTGCCCTGTACCCCTAGCCACGTCGGCCGGCCGCGCCTG
GAGAAGCTGTCTGGCCTAGCCGCACCCGACTACACTAGGCTGTCCCCGGCCAAGATTGTG
CTGAGGCGGCACCTGAGCCAGGACCACACGGTGCCCGGCAGGCCGGCTGCCAGTGAGCTG
CATTCGAGAGCTGAGCACACCAAGGAGAACGGCCTTCCCTACCAGAGCCCCAGCGTGCCT
GGCAGCATGAAGCTGAGCCCTCAGGACCCGCGGCCCCTGTCCCCTGGGGCCTTGCAGCTT
GCTGGAGAGAAGAGCAGTGAGAAGGGCCTGAGAGAGCGCGCCTACGGCAGCAGCGGGGAG
CTCATCACCAGCCTGCCCATCAGCATCCCGCTCAGCACCGTGCAGCCCAACAAGCTCCCG
GTCAGCATTCCCCTGGCCAGCGTGGTGCTGCCCAGCCGCGCCGAGAGGGCGAGGAGCACC
CCCAGTCCCGTGCTGCAGCCCCGTGACCCCTCGTCCACACTTGAAAAGCAGATTGGTGCT
AATGCCCACGGTGCTGGGAGCAGAAGCCTTGCCCTGGCCCCCGCAGGCTTCTCCTACGCT
GGCTCGGTGGCCATCAGCGGGGCCTTGGCGGGCAGCCCGGCCTCTCTCACACCTGGAGCC
GAGCCGGCCACCTTGGATGAGTCCTCCAGCTCTGGGAGCCTTTTTGCCACCGTGGGGTCC
CGCAGCTCCACGCCACAGCACCCCCTGCTGCTGGCACAGCCCCGGAACTCGCTTCCTGCC
TCTCCCGCCCACCAGCTCTCCTCCAGTCCCCGGCTTGGTGGGGCCGCCCAGGGCCCGTTG
CCCGAGGCCAGCAAGGGAGACCTGCCCTCCGATTCCGGCTTCTCAGATCCTGAGAGTGAA
GCCAAGAGGAGGATTGTGTTCACCATCACCACTGGTGCGGGCAGTGCCAAGCAGTCGCCC
TCCAGCAAGCACAGCCCCCTGACCGCCAGCGCCCGTGGGGACTGTGTGCCGAGCCACGGG
CAGGACAGTCGCAGGCGCGGCCGGCGGAAGCGAGCATCTGCGGGGACGCCCAGCTTGAGC
GCAGGCGTGTCCCCCAAGCGCCGAGCCCTGCCGTCCGTCGCTGGCCTTTTCACACAGCCT
TCGGGGTCTCCCCTCAACCTCAACTCCATGGTCAGTAACATCAACCAGCCCCTGGAGATT
ACAGCCATCTCGTCCCCGGAGACCTCCCTGAAGAGCTCCCCTGTGCCCTACCAGGACCAC
GACCAGCCCCCCGTGCTCAAGAAGGAGCGGCCTCTGAGCCAGACCAATGGGGCACACTAC
TCCCCACTCACCTCAGACGAGGAGCCAGGCTCTGAGGACGAGCCCAGCAGTGCTCGAATT
GAGAGAAAAATTGCAACAATCTCCTTAGAAAGCAAATCTCCCCCGAAAACCTTGGAAAAT
GGTGGTGGCTTGGCGGGAAGGAAGCCCGCGCCCGCCGGCGAGCCAGTCAATAGCAGCAAG
TGGAAGTCCACCTTCTCGCCCATCTCCGACATCGGCCTGGCCAAGTCGGCGGACAGCCCG
CTGCAGGCCAGCTCCGCCCTCAGCCAGAACTCCCTGTTCACGTTCCGGCCCGCCCTGGAG
GAGCCCTCTGCCGATGCCAAGCTGGCCGCTCACCCCAGGAAAGGCTTTCCCGGCTCCCTG
TCGGGGGCTGACGGACTCAGCCCGGGCACCAACCCTGCCAACGGCTGCACCTTCGGCGGG
GGCCTGGCCGCGGACCTGAGTTTACACAGCTTCAGTGATGGTGCTTCTCTTCCCCACAAG
GGCCCCGAGGCGGCCGGCCTGAGCTCCCCGCTGAGCTTCCCCTCGCAGCGCGGCAAGGAG
GGCTCGGACGCCAACCCTTTCCTGAGCAAGAGGCAGCTGGACGGCCTGGCTGGGCTGAAG
GGCGAGGGCAGCCGCGGCAAGGAGGCAGGGGAGGGCGGCCTACCGCTGTGCGGGCCCACG
GACAAGACCCCACTGCTGAGCGGCAAGGCCGCCAAGGCCCGGGACCGCGAGGTCGACCTC
AAGAATGGCCACAACCTCTTCATCTCTGCGGCGGCCGTGCCTCCCGGAAGCCTCCTCAGC
GGCCCCGGCCTGGCCCCGGCGGCGTCCTCCGCAGGCGGCGCGGCGTCCTCCGCCCAGACG
CACCGGTCCTTCCTGGGCCCCTTCCCGCCGGGACCGCAGTTCGCGCTCGGCCCCATGTCC
CTGCAGGCCAACCTCGGCTCCGTGGCCGGCTCCTCCGTGCTGCAGTCGCTGTTCAGCTCT
GTGCCGGCCGCCGCAGGCCTGGTGCACGTGTCGTCCGCTGCCACCAGACTGACCAACTCG
CACGCCATGGGCAGCTTTTCCGGGGTGGCAGGCGGCACAGTTGGAGGTAACTAG

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 ]
2. Nagase T, Nakayama M, Nakajima D, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2001 Apr 27;8(2):85-95. [PubMed ]
3. Jikuya H, Takano J, Kikuno R, Hirosawa M, Nagase T, Nomura N, Ohara O: Characterization of long cDNA clones from human adult spleen. II. The complete sequences of 81 cDNA clones. DNA Res. 2003 Feb 28;10(1):49-57. [PubMed ]
4. Min J, Feng Q, Li Z, Zhang Y, Xu RM: Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase. Cell. 2003 Mar 7;112(5):711-23. [PubMed ]

MVDSVYRTRSLGVAAEGLPDQYADGEAARVWQLYIGDTRSRTAEYKAWLLGLLRQHGCQR
VLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYALKERWNRRHEPAFDKWVIEEANWMT
LDKDVPQSAEGGFDAVICLGNSFAHLPDCKGDQSEHRLALKNIASMVRAGGLLVIDHRNY
DHILSTGCAPPGKNIYYKSDLTKDVTTSVLIVNNKAHMVTLDYTVQVPGAGQDGSPGLSK
FRLSYYPHCLASFTELLQAAFGGKCQHSVLGDFKPYKPGQTYIPCYFIHVLKRTD

• Glycine, Serine and Threonine Metabolism (map00260 )

• S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine

• Methyltransf_12 (PF08242 )

• None

• None

ATGGTGGACAGCGTGTACCGGACCCGCTCCCTGGGGGTGGCGGCCGAAGGGCTCCCGGAC
CAGTACGCGGACGGGGAGGCGGCGCGCGTGTGGCAGCTGTATATCGGAGACACCCGCAGC
CGCACCGCCGAGTACAAGGCATGGCTGCTTGGGCTGCTGCGCCAGCACGGCTGCCAGCGG
GTGCTCGACGTAGCCTGTGGCACTGGGGTGGACTCCATTATGCTGGTGGAAGAGGGCTTC
AGTGTGACGAGTGTGGATGCCAGTGACAAGATGCTGAAGTATGCACTTAAGGAGCGCTGG
AACCGGCGGCACGAGCCCGCCTTCGACAAGTGGGTCATCGAAGAAGCCAACTGGATGACT
CTGGACAAAGATGTGCCCCAGTCAGCAGAGGGTGGCTTTGATGCTGTCATCTGCCTTGGA
AACAGTTTCGCTCACTTGCCAGACTGCAAAGGGGACCAGAGTGAGCACCGGCTGGCGCTG
AAAAACATTGCGAGCATGGTGCGGGCAGGGGGCCTACTGGTCATTGATCATCGCAACTAC
GACCACATCCTCAGTACAGGCTGTGCACCCCCAGGGAAGAACATCTACTATAAGAGTGAC
TTGACCAAGGACGTCACAACATCAGTGCTGATAGTGAACAACAAGGCCCACATGGTGACC
CTGGACTATACGGTGCAGGTGCCGGGGGCTGGCCAGGATGGCTCTCCTGGCTTGAGTAAG
TTCCGGCTCTCCTACTACCCACACTGTCTGGCATCCTTCACGGAGCTGCTCCAAGCAGCC
TTCGGAGGTAAGTGCCAGCACAGCGTCCTGGGCGACTTCAAGCCTTACAAGCCAGGCCAA
ACCTACATTCCCTGCTACTTCATCCACGTGCTCAAGAGGACAGACTGA

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 ]
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 ]
3. Luka Z, Cerone R, Phillips JA 3rd, Mudd HS, Wagner C: Mutations in human glycine N-methyltransferase give insights into its role in methionine metabolism. Hum Genet. 2002 Jan;110(1):68-74. Epub 2001 Dec 7. [PubMed ]

1. Histone H3-K4 methyltransferase
2. H3-K4-HMTase
3. SET domain-containing protein 7
4. Set9
5. SET7/9

MDSDDEMVEEAVEGHLDDDGLPHGFCTVTYSSTDRFEGNFVHGEKNGRGKFFFFDGSTLE
GYYVDDALQGQGVYTYEDGGVLQGTYVDGELNGPAQEYDTDGRLIFKGQYKDNIRHGVCW
IYYPDGGSLVGEVNEDGEMTGEKIAYVYPDERTALYGKFIDGEMIEGKLATLMSTEEGRP
HFELMPGNSVYHFDKSTSSCISTNALLPDPYESERVYVAESLISSAGEGLFSKVAVGPNT
VMSFYNGVRITHQEVDSRDWALNGNTLSLDEETVIDVPEPYNHVSKYCASLGHKANHSFT
PNCIYDMFVHPRFGPIKCIRTLRAVEADEELTVAYGYDHSPPGKSGPEAPEWYQVELKAF
QATQQK

• Lysine Degradation (map00310 )

• S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine

• MORN (PF02493 )
• SET (PF00856 )

• None

• None

ATGGATAGCGACGACGAGATGGTGGAGGAGGCGGTGGAAGGGCACCTGGACGATGACGGA
TTACCGCACGGGTTCTGCACAGTCACCTACTCCTCCACAGACAGATTTGAGGGGAACTTT
GTTCACGGAGAAAAGAACGGACGGGGGAAGTTCTTCTTCTTTGATGGCAGCACCCTGGAG
GGGTATTATGTGGATGATGCCTTGCAGGGCCAGGGAGTTTACACTTACGAAGATGGGGGA
GTTCTCCAGGGCACGTATGTAGACGGAGAGCTGAACGGTCCAGCCCAGGAATATGACACA
GATGGGAGACTGATCTTCAAGGGGCAGTATAAAGATAACATTCGTCATGGAGTGTGCTGG
ATATATTACCCAGATGGAGGAAGCCTTGTAGGAGAAGTAAATGAAGATGGGGAGATGACT
GGAGAGAAGATAGCCTATGTGTACCCTGATGAGAGGACCGCACTTTATGGGAAATTTATT
GATGGAGAGATGATAGAAGGCAAACTGGCTACCCTTATGTCCACTGAAGAAGGGAGGCCT
CACTTTGAACTGATGCCTGGAAATTCAGTGTACCACTTTGATAAGTCGACTTCATCTTGC
ATTTCTACCAATGCTCTTCTTCCAGATCCTTATGAATCAGAAAGGGTTTATGTTGCTGAA
TCTCTTATTTCCAGTGCTGGAGAAGGACTTTTTTCAAAGGTAGCTGTGGGACCTAATACT
GTTATGTCTTTTTATAATGGAGTTCGAATTACACACCAAGAGGTTGACAGCAGGGACTGG
GCCCTTAATGGGAACACCCTCTCCCTTGATGAAGAAACGGTCATTGATGTGCCTGAGCCC
TATAACCACGTATCCAAGTACTGTGCCTCCTTGGGACACAAGGCAAATCACTCCTTCACT
CCAAACTGCATCTACGATATGTTTGTCCACCCCCGTTTTGGGCCCATCAAATGCATCCGC
ACCCTGAGAGCAGTGGAGGCCGATGAAGAGCTCACCGTTGCCTATGGCTATGACCACAGC
CCCCCCGGGAAGAGTGGGCCTGAAGCCCCTGAGTGGTACCAGGTGGAGCTGAAGGCCTTC
CAGGCCACCCAGCAAAAGTGA

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 ]
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 ]
3. Nagase T, Kikuno R, Hattori A, Kondo Y, Okumura K, Ohara O: Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Dec 31;7(6):347-55. [PubMed ]
4. Wilson JR, Jing C, Walker PA, Martin SR, Howell SA, Blackburn GM, Gamblin SJ, Xiao B: Crystal structure and functional analysis of the histone methyltransferase SET7/9. Cell. 2002 Oct 4;111(1):105-15. [PubMed ]
5. Jacobs SA, Harp JM, Devarakonda S, Kim Y, Rastinejad F, Khorasanizadeh S: The active site of the SET domain is constructed on a knot. Nat Struct Biol. 2002 Nov;9(11):833-8. [PubMed ]
6. Xiao B, Jing C, Wilson JR, Walker PA, Vasisht N, Kelly G, Howell S, Taylor IA, Blackburn GM, Gamblin SJ: Structure and catalytic mechanism of the human histone methyltransferase SET7/9. Nature. 2003 Feb 6;421(6923):652-6. Epub 2003 Jan 22. [PubMed ]
7. Kwon T, Chang JH, Kwak E, Lee CW, Joachimiak A, Kim YC, Lee J, Cho Y: Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet. EMBO J. 2003 Jan 15;22(2):292-303. [PubMed ]

1. Methionine adenosyltransferase 2
2. AdoMet synthetase 2
3. Methionine adenosyltransferase II
4. MAT-II

MNGQLNGFHEAFIEEGTFLFTSESVGEGHPDKICDQISDAVLDAHLQQDPDAKVACETVA
KTGMILLAGEITSRAAVDYQKVVREAVKHIGYDDSSKGFDYKTCNVLVALEQQSPDIAQG
VHLDRNEEDIGAGDQGLMFGYATDETEECMPLTIVLAHKLNAKLAELRRNGTLPWLRPDS
KTQVTVQYMQDRGAVLPIRVHTIVISVQHDEEVCLDEMRDALKEKVIKAVVPAKYLDEDT
IYHLQPSGRFVIGGPQGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARW
VAKSLVKGGLCRRVLVQVSYAIGVSHPLSISIFHYGTSQKSERELLEIVKKNFDLRPGVI
VRDLDLKKPIYQRTAAYGHFGRDSFPWEVPKKLKY

• Methionine Metabolism (map00271 )
• Selenoamino Acid Metabolism (map00450 )

• ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine

• S-AdoMet_synt_C (PF02773 )
• S-AdoMet_synt_M (PF02772 )
• S-AdoMet_synt_N (PF00438 )

• None

• None

ATGAACGGACAGCTCAACGGCTTCCACGAGGCGTTCATCGAGGAGGGCACATTCCTTTTC
ACCTCAGAGTCGGTCGGGGAAGGCCACCCAGATAAGATTTGTGACCAAATCAGTGATGCT
GTCCTTGATGCCCACCTTCAGCAGGATCCTGATGCCAAAGTAGCTTGTGAAACTGTTGCT
AAAACTGGAATGATCCTTCTTGCTGGGGAAATTACATCCAGAGCTGCTGTTGACTACCAG
AAAGTGGTTCGTGAAGCTGTTAAACACATTGGATATGATGATTCTTCCAAAGGTTTTGAC
TACAAGACTTGTAACGTGCTGGTAGCCTTGGAGCAACAGTCACCAGATATTGCTCAAGGT
GTTCATCTTGACAGAAATGAAGAAGACATTGGTGCTGGAGACCAGGGCTTAATGTTTGGC
TATGCCACTGATGAAACTGAGGAGTGTATGCCTTTAACCATTGTCTTGGCACACAAGCTA
AATGCCAAACTGGCAGAACTACGCCGTAATGGCACTTTGCCTTGGTTACGCCCTGATTCT
AAAACTCAAGTTACTGTGCAGTATATGCAGGATCGAGGTGCTGTGCTTCCCATCAGAGTC
CACACAATTGTTATATCTGTTCAGCATGATGAAGAGGTTTGTCTTGATGAAATGAGGGAT
GCCCTAAAGGAGAAAGTCATCAAAGCAGTTGTGCCTGCGAAATACCTTGATGAGGATACA
ATCTACCACCTACAGCCAAGTGGCAGATTTGTTATTGGTGGGCCTCAGGGTGATGCTGGT
TTGACTGGACGGAAAATCATTGTGGACACTTATGGCGGTTGGGGTGCTCATGGAGGAGGT
GCCTTTTCAGGAAAGGATTATACCAAGGTCGACCGTTCAGCTGCTTATGCTGCTCGTTGG
GTGGCAAAATCCCTTGTTAAAGGAGGTCTGTGCCGGAGGGTTCTTGTTCAGGTCTCTTAT
GCTATTGGAGTTTCTCATCCATTATCTATCTCCATTTTCCATTATGGTACCTCTCAGAAG
AGTGAGAGAGAGCTATTAGAGATTGTGAAGAAGAATTTCGATCTCCGCCCTGGGGTCATT
GTCAGGGATCTGGATCTGAAGAAGCCAATTTATCAGAGGACTGCAGCCTATGGCCACTTT
GGTAGGGACAGCTTCCCATGGGAAGTGCCCAAAAAGCTTAAATATTGA

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 ]
2. 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 ]

1. PNMTase
2. Noradrenaline N-methyltransferase

MSGADRSPNAGAAPDSAPGQAAVASAYQRFEPRAYLRNNYAPPRGDLCNPNGVGPWKLRC
LAQTFATGEVSGRTLIDIGSGPTVYQLLSACSHFEDITMTDFLEVNRQELGRWLQEEPGA
FNWSMYSQHACLIEGKGECWQDKERQLRARVKRVLPIDVHQPQPLGAGSPAPLPADALVS
AFCLEAVSPDLASFQRALDHITTLLRPGGHLLLIGALEESWYLAGEARLTVVPVSEEEVR
EALVRSGYKVRDLRTYIMPAHLQTGVDDVKGVFFAWAQKVGL

• Tyrosine Metabolism (map00350 )

• S-adenosyl-L-methionine + phenylethanolamine = S-adenosyl-L-homocysteine + N-methylphenylethanolamine

• NNMT_PNMT_TEMT (PF01234 )

• None

• None

ATGAGCGGCGCAGACCGTAGCCCCAATGCGGGCGCAGCCCCTGACTCGGCCCCGGGCCAG
GCGGCGGTGGCTTCGGCCTACCAGCGCTTCGAGCCGCGCGCCTACCTCCGCAACAACTAC
GCGCCCCCTCGCGGGGACCTGTGCAACCCGAACGGCGTCGGGCCGTGGAAGCTGCGCTGC
TTGGCGCAGACCTTCGCCACCGGTGAAGTGTCCGGACGCACCCTCATCGACATTGGTTCA
GGCCCCACCGTGTACCAGCTGCTCAGTGCCTGCAGCCACTTTGAGGACATCACCATGACA
GATTTCCTGGAGGTCAACCGCCAGGAGCTGGGGCGCTGGCTGCAGGAGGAGCCGGGGGCC
TTCAACTGGAGCATGTACAGCCAACATGCCTGCCTCATTGAGGGCAAGGGGGAATGCTGG
CAGGATAAGGAGCGCCAGCTGCGAGCCAGGGTGAAACGGGTCCTGCCCATCGACGTGCAC
CAGCCCCAGCCCCTGGGTGCTGGGAGCCCAGCTCCCCTGCCTGCTGACGCCCTGGTCTCT
GCCTTCTGCTTGGAGGCTGTGAGCCCAGATCTTGCCAGCTTTCAGCGGGCCCTGGACCAC
ATCACCACGCTGCTGAGGCCTGGGGGGCACCTCCTCCTCATCGGGGCCCTGGAGGAGTCG
TGGTACCTGGCTGGGGAGGCCAGGCTGACGGTGGTGCCAGTGTCTGAGGAGGAGGTGAGG
GAGGCCCTGGTGCGTAGTGGCTACAAGGTCCGGGACCTCCGCACCTATATCATGCCTGCC
CACCTTCAGACAGGCGTAGATGATGTCAAGGGCGTCTTCTTCGCCTGGGCTCAGAAGGTT
GGGCTGTGA

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 ]
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 ]

1. Diphthamide biosynthesis methyltransferase

MLYLIGLGLGDAKDITVKGLEVVRRCSRVYLEAYTSVLTVGKEALEEFYGRKLVVADREE
VEQEADNILKDADISDVAFLVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAVGCC
GLQLYKFGETVSIVFWTDTWRPESFFDKVKKNRQNGMHTLCLLDIKVKEQSLENLIKGRK
IYEPPRYMSVNQAAQQLLEIVQNQRIRGEEPAVTEETLCVGLARVGADDQKIAAGTLRQM
CTVDLGEPLHSLIITGGSIHPMEMEMLSLFSIPENSSESQSINGL

• S-adenosyl-L-methionine + 2-(3-carboxy-3-aminopropyl)-L-histidine = S-adenosyl-L-homocysteine + 2-[3-carboxy-3-(methylammonio)propyl]-L-histidine

• TP_methylase (PF00590 )

• None

• None

ATGCTTTATCTCATCGGGTTGGGCCTGGGAGATGCCAAGGACATCACAGTCAAGGGCCTG
GAAGTTGTTAGACGCTGCAGTCGAGTGTATCTGGAAGCCTACACCTCAGTCCTAACTGTA
GGGAAGGAAGCCTTGGAAGAGTTTTATGGAAGAAAATTGGTTGTTGCTGATAGAGAAGAA
GTGGAACAAGAAGCAGATAATATTTTAAAGGATGCTGATATCAGTGATGTTGCATTCCTT
GTGGTTGGTGATCCATTTGGGGCCACAACACACAGTGATCTTGTTCTAAGAGCAACAAAG
CTGGGAATTCCTTATAGAGTTATTCACAATGCCTCCATAATGAATGCTGTAGGCTGCTGT
GGTTTACAGTTATATAAGTTTGGAGAGACAGTTTCTATTATGCTGATATCAGTGATGTTG
CATTCCTTGTGGTTGGTGATCCATTTGGACACTTGGAGACCAGAAAGCTTCTTTGACAAA
GTGAAGAAGAACAGACAAAATGGCATGCACACATTATGTTTACTAGACATCAAAGTAAAG
GAGCAGTCTTTGGAAAATCTAATCAAGGGAAGGAAGATCTATGAACCTCCACGGTATATG
AGTGTAAACCAAGCAGCCCAGCAGCTTCTGGAGATTGTTCAAAATCAAAGAATACGAGGA
GAAGAACCAGCAGTTACCGAGGAGACACTTTGTGTTGGCTTAGCCAGGGTTGGAGCCGAC
GACCAGAAAATTGCAGCAGGCACTTTAAGGCAAATGTGCACTGTGGACTTGGGAGAACCA
TTGCATTCCTTGATCATCACAGGAGGCAGCATACATCCAATGGAGATGGAGATGCTAAGT
CTGTTTTCCATACCAGAAAATAGCTCAGAATCTCAAAGCATCAATGGACTTTGA

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 ]
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 ]
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 ]

1. S-adenosyl-L- methionine:arsenic(IIImethyltransferase
2. Methylarsonite methyltransferase

MAALRDAEIQKDVQTYYGQVLKRSADLQTNGCVTTARPVPKHIREALQNVHEEVALRYYG
CGLVIPEHLENCWILDLGSGSGRDCYVLSQLVGEKGHVTGIDMTKGQVEVAEKYLDYHME
KYGFQASNVTFFHGNIEKLAEAGIKNESHDIVVSNCVINLVPDKQQVLQEAYRVLKHGGE
LYFSDVYTSLELPEEIRTHKVLWGECLGGALYWKELAVLAQKIGFCPPRLVTANLITIQN
KELERVIGDCRFVSATFRLFKHSKTGPTKRCQVIYNGGITGHEKELMFDANFTFKEGEIV
EVDEETAAILKNSRFAQDFLIRPIGEKLPTSGGCSALELKDIITDPFKLAEESDSMKSRC
VPDAAGGCCGTKKSC

• (1) S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + methylarsonate
• (2) S-adenosyl-L-methionine + methylarsonite = S-adenosyl-L-homocysteine + dimethylarsinate

• Methyltransf_11 (PF08241 )

• None

• None

ATGGCTGCACTTCGTGACGCTGAGATACAGAAGGACGTGCAGACCTACTACGGGCAGGTG
CTGAAGAGATCGGCAGACCTCCAGACCAACGGCTGTGTCACCACAGCCAGGCCGGTCCCC
AAGCACATCCGGGAAGCCTTGCAAAATGTACACGAAGAAGTAGCCCTAAGATATTATGGC
TGTGGTCTGGTGATCCCTGAGCATCTAGAAAACTGCTGGATTTTGGATCTGGGTAGTGGA
AGTGGCAGAGATTGCTATGTACTTAGCCAGCTGGTTGGTGAAAAAGGACACGTGACTGGA
ATAGACATGACCAAAGGCCAGGTGGAAGTGGCTGAAAAGTATCTTGACTATCACATGGAA
AAATATGGCTTCCAGGCATCTAATGTGACTTTTTTCCATGGCAACATTGAGAAGTTGGCA
GAGGCTGGAATCAAGAATGAGAGCCATGATATTGTTGTATCAAACTGTGTTATTAACCTT
GTGCCTGATAAACAACAAGTGCTTCAGGAGGCATATCGGGTGCTGAAGCATGGTGGGGAG
TTATATTTCAGTGACGTCTATACGAGCCTTGAACTGCCAGAAGAAATCAGGACACACAAA
GTTTTATGGGGTGAGTGTCTGGGTGGTGCTTTATACTGGAAGGAACTTGCTGTCCTTGCT
CAAAAAATTGGGTTCTGCCCTCCACGTTTGGTCACTGCCAATCTCATTACAATTCAAAAC
AAGGAACTGGAAAGAGTTATCGGTGACTGTCGTTTTGTTTCTGCAACATTTCGCCTCTTC
AAACACTCTAAGACAGGACCAACCAAGAGATGCCAAGTTATTTACAATGGAGGAATTACA
GGACATGAAAAAGAACTAATGTTTGATGCCAATTTTACATTTAAGGAAGGTGAAATTGTT
GAAGTGGATGAAGAAACAGCAGCTATCTTGAAGAATTCAAGATTTGCTCAAGATTTTCTG
ATCAGACCAATTGGAGAGAAGTTGCCAACATCTGGAGCTGTTCTGCTTTGGAGTTAA

1. 5-methylaminomethyl-2-thiouridylate-methyltransferase
2. Mitochondrial tRNA-specific 2-thiouridylase 1
3. MTO2 homolog

MQALRHVVCALSGGVDSAVAALLLRRRGYQVTGVFMKNWDSLDEHGVCTADKDCEDAYRV
CQILDIPFHQVSYVKEYWNDVFSDFLNEYEKGRTPNPDIVCNKHIKFSCFFHYAVDNLGA
DAIATGHYARTSLEDEEVFEQKHVKKPEGLFRNRFEVRNAVKLLQAADSFKDQTFFLSQV
SQDALRRTIFPLGGLTKEFVKKIAAENRLHHVLQKKESMGMCFIGKRNFEHFLLQYLQPR
PGHFISIEDNKVLGTHKGWFLYTLGQRANIGGLREPWYVVEKDSVKGDVFVAPRTDHPAL
YRDLLRTSRVHWIAEEPPAALVRDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTAVQAV
RALATGQFAVFYKGDECLGSGKILRLGPSAYTLQKGQRRAGMATESPSDSPEDGPGLSPL
L

• S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing 5-methylaminomethyl-2-thiouridylate

• tRNA_Me_trans (PF03054 )

• 1-20

ATGCAGGCCTTGCGGCACGTCGTGTGCGCCCTGTCCGGCGGCGTGGACAGCGCCGTGGCC
GCGCTGCTGCTGAGGCGGAGAGGTTACCAGGTGACAGGGGTGTTTATGAAGAACTGGGAC
TCACTGGATGAACATGGGGTCTGTACTGCCGACAAAGACTGTGAAGATGCTTACAGAGTT
TGCCAGATCTTAGACATCCCTTTCCATCAAGTGTCCTACGTAAAGGAGTATTGGAATGAT
GTGTTCAGTGACTTTTTGAATGAGTATGAAAAAGGAAGGACTCCCAATCCTGACATAGTT
TGCAACAAGCACATCAAATTTAGTTGCTTTTTTCATTATGCTGTGGATAATCTTGGGGCA
GATGCCATTGCCACAGGTCACTATGCAAGAACTTCCCTGGAAGATGAAGAAGTCTTTGAG
CAGAAGCACGTTAAGAAGCCCGAAGGGCTTTTCAGAAATCGGTTTGAAGTTAGAAATGCG
GTAAAACTCCTCCAGGCAGCTGACAGCTTTAAAGACCAGACCTTCTTTCTCAGCCAGGTT
TCCCAGGATGCCCTGAGGAGAACCATCTTCCCTCTGGGGGGATTAACGAAAGAGTTTGTA
AAGAAAATCGCTGCTGAGAATAGACTTCATCATGTGCTTCAGAAGAAAGAGAGCATGGGC
ATGTGTTTCATCGGGAAGAGGAATTTTGAACATTTCCTTCTTCAGTATCTGCAGCCTCGA
CCTGGTCACTTTATTTCCATAGAAGACAATAAGGTTCTGGGAACACATAAAGGTTGGTTC
CTGTATACCTTGGGCCAGAGAGCAAACATAGGTGGCCTGAGAGAGCCCTGGTACGTGGTG
GAGAAGGACAGCGTCAAGGGTGACGTGTTTGTGGCCCCCCGGACAGACCACCCAGCCCTG
TACAGGGACCTGCTGAGGACCAGCCGCGTGCACTGGATTGCGGAGGAGCCTCCCGCAGCA
CTGGTCCGGGACAAGATGATGGAGTGCCACTTCCGATTCCGCCACCAGATGGCACTAGTG
CCCTGTGTGCTGACCCTCAATCAAGATGGCACCGTGTGGGTGACAGCTGTGCAGGCTGTG
CGTGCCCTTGCCACAGGACAGTTTGCTGTGTTCTACAAGGGGGACGAGTGCCTGGGCAGC
GGGAAGATCCTGCGGCTGGGGCCGTCTGCCTACACGCTCCAGAAGGGCCAGCGCAGAGCT
GGGATGGCCACTGAGAGCCCCAGTGACAGCCCAGAAGATGGTCCAGGCCTGAGTCCCTTG
CTCTGA

1. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed ]

1. H3-K36-HMTase
2. H4-K20-HMTase
3. Nuclear receptor-binding SET domain-containing protein 1
4. NR-binding SET domain-containing protein
5. Androgen receptor-associated coregulator 267

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

• Lysine Degradation (map00310 )

• S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine

• PHD (PF00628 )
• PWWP (PF00855 )
• SET (PF00856 )

• None

• None

ATGCCCCTGAAGACAAGGACAGCCCTTTCGGATGATCCAGATTCCAGTACCAGTACATTA
GGAAACATGCTAGAATTACCTGGAACTTCATCATCATCTACTTCACAGGAATTGCCATTT
TGTCAACCTAAGAAAAAGTCTACGCCACTGAAGTATGAAGTTGGAGATCTCATCTGGGCA
AAATTCAAGAGACGCCCATGGTGGCCCTGCAGGATTTGTTCTGATCCGTTGATTAACACA
CATTCAAAAATGAAAGTTTCCAACCGGAGGCCCTATCGGCAGTACTACGTGGAGGCTTTT
GGAGATCCTTCTGAGAGAGCCTGGGTGGCTGGAAAAGCAATCGTCATGTTTGAAGGCAGA
CATCAATTCGAAGAGCTACCTGTCCTTAGGAGAAGAGGGAAACAGAAAGAAAAAGGATAT
AGGCATAAGGTTCCTCAGAAAATTTTGAGTAAATGGGAAGCCAGTGTTGGACTTGCAGAA
CAGTATGATGTTCCCAAGGGGTCAAAGAACCGAAAATGTATTCCTGGTTCAATCAAGTTG
GACAGTGAAGAAGATATGCCATTTGAAGACTGCACAAATGATCCTGAGTCAGAACATGAC
CTGTTGCTTAATGGCTGTTTGAAATCACTGGCTTTTGATTCTGAACATTCTGCAGATGAG
AAGGAAAAGCCTTGTGCTAAATCTCGAGCCAGAAAGAGCTCTGATAATCCAAAAAGGACT
AGTGTGAAAAAGGGCCACATACAATTTGAAGCACATAAAGATGAACGGAGGGGAAAGATT
CCAGAGAACCTTGGCCTAAACTTTATCTCTGGGGATATATCTGATACGCAGGCCTCTAAT
GAACTTTCCAGGATAGCAAATAGCCTCACAGGGTCCAACACTGCCCCAGGAAGTTTTCTG
TTTTCTTCCTGTGGAAAAAACACTGCAAAGAAAGAATTTGAGACTTCAAATGGTGACTCT
TTATTGGGCTTGCCTGAGGGTGCTTTGATCTCAAAGTGTTCTCGAGAGAAGAATAAACCC
CAACGAAGCCTGGTGTGTGGTTCAAAAGTGAAGCTCTGCTATATTGGAGCAGGTGATGAG
GAAAAGCGAAGTGATTCCATTAGTATCTGTACCACTTCTGATGATGGAAGCAGTGACCTG
GATCCCATAGAACACAGCTCAGAGTCTGATAACAGTGTCCTTGAAATTCCAGATGCTTTC
GATAGAACAGAGAACATGTTATCTATGCAGAAAAATGAAAAGATAAAGTATTCTAGGTTT
GCTGCCACAAACACTAGGGTAAAAGCAAAACAGAAGCCTCTCATTAGTAACTCACATACA
GACCACTTAATGGGTTGTACTAAGAGTGCAGAGCCTGGAACCGAGACGTCTCAGGTTAAT
CTCTCTGATCTGAAGGCATCTACTCTTGTTCACAAACCCCAGTCAGATTTTACAAATGAT
GCTCTCTCTCCAAAATTCAACCTGTCATCAAGCATATCCAGTGAGAACTCGTTAATAAAG
GGTGGGGCAGCAAATCAAGCTCTATTACATTCGAAAAGCAAACAGCCCAAGTTCCGAAGT
ATAAAGTGCAAACACAAAGAAAATCCAGTTATGGCAGAACCCCCAGTTATAAATGAGGAG
TGCAGTTTGAAATGCTGCTCTTCTGATACCAAAGGCTCTCCTTTGGCCAGCATTTCTAAA
AGTGGGAAAGTGGATGGTCTAAAACTACTGAACAATATGCATGAGAAAACCAGGGATTCA
AGTGACATAGAAACAGCAGTGGTGAAACATGTTTTATCCGAGTTGAAGGAACTCTCTTAC
AGATCCTTAGGTGAGGATGTCAGTGACTCTGGAACATCAAAGCCATCAAAACCATTACTT
TTCTCTTCTGCTTCTAGTCAGAATCACATACCTATTGAACCAGACTACAAATTCAGTACA
TTGCTAATGATGTTGAAAGATATGCATGATAGTAAGACGAAGGAGCAGCGGTTGATGACT
GCTCAAAACCTGGTCTCTTACCGGAGTCCTGGTCGTGGGGACTGTTCTACTAATAGTCCT
GTAGGAGTCTCTAAGGTTTTGGTTTCAGGAGGCTCCACACACAATTCAGAGAAAAAGGGA
GATGGCACTCAGAACTCCGCCAATCCTAGCCCTAGTGGGGGTGACTCTGCATTATCTGGC
GAGTTGTCTGCTTCCCTACCTGGCTTACTGTCCGACAAGAGAGACCTCCCTGCTTCTGGT
AAAAGTCGTTCAGACTGTGTTACTAGGCGCAACTGTGGACGATCAAAGCCTTCATCCAAA
TTGCGAGATGCTTTTTCAGCCCAAATGGTAAAGAACACAGTGAACCGTAAAGCCTTAAAG
ACCGAGCGCAAAAGAAAACTGAATCAGCTTCCAAGTGTGACTCTTGATGCTGTACTGCAG
GGAGACCGAGAACGTGGAGGTTCATTGAGAGGTGGGGCAGAAGATCCTAGTAAAGAGGAT
CCCCTTCAGATAATGGGCCACTTAACAAGTGAAGATGGTGACCATTTTTCTGATGTGCAT
TTCGATAGCAAGGTTAAGCAATCTGATCCTGGTAAAATTTCTGAAAAAGGACTCTCTTTT
GAAAACGGAAAAGGCCCAGAGCTGGACTCTGTAATGAACAGTGAGAATGATGAACTCAAT
GGTGTAAATCAAGTGGTGCCTAAAAAGCGGTGGCAGCGTTTAAACCAAAGGCGCACTAAA
CCTCGTAAGCGCATGAACAGATTTAAAGAGAAAGAAAACTCTGAGTGTGCCTTTAGGGTC
TTACTTCCTAGTGACCCTGTGCAGGAGGGGCGGGATGAGTTTCCAGAGCATAGAACTCCT
TCAGCAAGCATACTTGAGGAACCACTGACAGAGCAAAATCATGCTGACTGCTTAGATTCA
GCTGGGCCACGGTTAAATGTTTGTGATAAATCCAGTGCCAGCATTGGTGACATGGAAAAG
GAGCCAGGAATTCCCAGTTTGACACCACAGGCTGAGCTCCCTGAACCAGCTGTGCGGTCA
GAGAAGAAACGCCTTAGGAAGCCAAGCAAGTGGCTTTTGGAATATACAGAAGAATATGAT
CAGATATTTGCTCCTAAGAAAAAACAAAAGAAGGTACAGGAGCAGGTGCACAAGGTAAGT
TCCCGCTGTGAAGAGGAAAGCCTTCTAGCCCGAGGTCGATCTAGTGCTCAGAACAAGCAG
GTGGACGAGAATTCTTTGATTTCAACCAAAGAAGAGCCTCCAGTTCTTGAAAGGGAGGCT
CCGTTTTTGGAGGGCCCCTTGGCTCAGTCAGAACTTGGAGGTGGACATGCTGAGTTGCCG
CAGCTGACCTTGTCTGTGCCTGTGGCTCCGGAAGTCTCTCCACGGCCTGCCCTTGAGTCT
GAGGAATTGCTAGTTAAAACGCCAGGAAATTATGAAAGTAAACGTCAAAGAAAACCAACT
AAGAAACTTCTTGAATCCAATGATTTAGACCCTGGATTTATGCCCAAGAAGGGGGACCTT
GGCCTTTCTAAAAAGTGCTATGAAGCTGGTCACCTGGAGAATGGCATAACTGAATCTTGT
GCCACATCTTATTCAAAAGATTTTGGTGGAGGCACTACCAAGATATTTGACAAGCCAAGG
AAGCGAAAACGACAGAGGCATGCTGCAGCCAAGATGCAGTGTAAAAAAGTGAAAAATGAT
GACTCGTCAAAAGAGATTCCAGGCTCAGAGGGAGAACTAATGCCTCACAGGACGGCCACA
AGCCCCAAGGAGACTGTTGAGGAAGGTGTAGAACACGATCCCGGGATGCCTGCCTCTAAA
AAAATGCAGGGTGAACGCGGTGGAGGAGCTGCACTCAAGGAGAATGTCTGTCAGAATTGT
GAAAAATTGGGTGAGCTGCTGTTATGTGAGGCTCAGTGCTGTGGGGCTTTCCACCTGGAG
TGCCTTGGATTGACTGAGATGCCAAGAGGAAAATTTATCTGCAATGAATGTCGCACAGGA
ATCCATACCTGTTTTGTATGTAAGCAGAGTGGGGAAGATGTTAAAAGGTGCCTTCTACCC
TTGTGTGGAAAGTTTTACCATGAAGAGTGTGTCCAGAAGTACCCACCCACTGTTATGCAG
AACAAGGGCTTCCGGTGCTCCCTCCACATCTGTATAACCTGTCATGCTGCTAATCCAGCC
AATGTTTCTGCATCTAAAGGTCGGTTGATGCGCTGTGTCCGCTGTCCTGTGGCATACCAC
GCCAATGACTTTTGCCTGGCTGCTGGGTCAAAGATCCTTGCATCTAATAGTATCATCTGC
CCTAATCACTTTACCCCTAGGCGGGGCTGCCGAAATCATGAGCATGTTAATGTTAGCTGG
TGCTTTGTGTGCTCAGAAGGAGGCAGCCTTCTGTGCTGTGATTCTTGCCCTGCTGCTTTT
CATCGTGAATGCCTGAACATTGATATCCCTGAAGGAAACTGGTATTGCAATGACTGTAAA
GCAGGCAAAAAGCCACACTACAGGGAGATTGTCTGGGTAAAAGTTGGACGATACAGGTGG
TGGCCAGCTGAGATCTGCCATCCTCGAGCTGTTCCTTCCAACATTGATAAGATGAGACAT
GATGTGGGAGAGTTCCCAGTCCTCTTTTTTGGATCTAATGACTATTTGTGGACTCACCAG
GCCCGAGTCTTCCCTTACATGGAGGGTGACGTGAGCAGCAAGGATAAGATGGGCAAAGGA
GTGGATGGGACATATAAAAAAGCTCTTCAGGAAGCTGCAGCAAGGTTTGAGGAATTAAAG
GCCCAAAAAGAGCTAAGACAGCTGCAGGAAGACCGAAAGAATGACAAGAAGCCACCACCT
TATAAACATATAAAGGTAAACCGTCCTATTGGCAGGGTACAGATCTTCACTGCAGACTTA
TCTGAAATACCCCGTTGCAACTGTAAAGCTACTGATGAGAACCCCTGTGGGATAGACTCT
GAATGCATCAACCGCATGCTGCTCTATGAGTGCCACCCCACAGTGTGTCCTGCCGGAGGG
CGCTGTCAAAACCAGTGCTTTTCCAAGCGCCAATATCCAGAGGTTGAAATTTTCCGCACA
TTACAGCGGGGTTGGGGTCTACGGACAAAAACAGATATTAAAAAGGGTGAATTTGTGAAT
GAGTATGTGGGTGAGCTTATAGATGAAGAAGAATGCAGAGCTCGAATTCGCTATGCTCAA
GAACATGATATCACTAATTTCTATATGCTCACCCTAGACAAAGACCGAATCATTGATGCT
GGTCCCAAAGGAAACTATGCTCGGTTCATGAATCATTGCTGCCAGCCCAACTGTGAAACA
CAGAAGTGGTCTGTGAATGGAGATACCCGTGTAGGCCTTTTTGCACTAAGTGACATTAAA
GCAGGCACTGAACTTACCTTCAACTACAACCTAGAATGTCTTGGGAATGGAAAGACTGTT
TGCAAATGTGGAGCCCCGAACTGCAGTGGCTTCTTGGGTGTAAGGCCAAAGAATCAACCC
ATTGCCACGGAAGAAAAGTCAAAGAAATTCAAGAAGAAGCAACAGGGAAAGCGCAGGACC
CAGGGTGAAATCACAAAGGAGCGAGAAGATGAGTGTTTTAGTTGTGGGGATGCTGGCCAG
CTCGTCTCCTGCAAGAAACCAGGCTGCCCAAAAGTTTACCACGCAGACTGTCTCAATCTG
ACCAAGCGACCAGCAGGGAAATGGGAATGTCCGTGGCATCAGTGTGACATCTGCGGGAAG
GAAGCAGCCTCCTTCTGTGAGATGTGCCCCAGCTCCTTTTGTAAGCAGCATCGAGAAGGG
ATGCTTTTCATTTCCAAACTGGATGGGCGTCTGTCTTGTACTGAGCATGACCCCTGTGGG
CCCAATCCTCTGGAACCTGGGGAGATCCGTGAGTATGTGCCTCCCCCAGTACCGCTGCCT
CCAGGGCCAAGCACTCACCTGGCAGAGCAATCAACAGGAATGGCTGCTCAGGCACCCAAA
ATGTCAGATAAACCTCCTGCTGACACCAACCAGATGCTGTCGCTCTCCAAAAAAGCTCTG
GCAGGGACTTGTCAGAGGCCACTGCTACCTGAAAGACCTCTTGAGAGAACTGACTCCAGG
CCCCAGCCTTTAGATAAGGTCAGAGACCTCGCTGGCTCAGGGACCAAATCCCAATCCTTG
GTTTCCAGCCAGAGGCCACTGGACAGGCCACCAGCAGTGGCAGGACCAAGACCCCAGCTA
AGCGACAAACCCTCTCCAGTGACCAGCCCAAGCTCCTCACCCTCAGTCAGGTCCCAACCA
CTGGAAAGACCTCTGGGGACGGCTGACCCAAGGCTGGATAAATCCATAGGTGCTGCCAGC
CCAAGGCCCCAGTCACTGGAGAAAACCTCAGTTCCCACTGGCCTGAGACTTCCGCCGCCA
GACAGACTGCTCATTACTAGCAGTCCCAAACCCCAGACTTCAGACAGGCCTACTGACAAA
CCCCATGCCTCTTTGTCCCAGAGACTCCCACCTCCTGAGAAAGTACTATCAGCTGTGGTC
CAGACCCTTGTAGCTAAAGAAAAAGCACTGAGGCCTGTGGACCAGAATACTCAGTCAAAA
AATAGAGCTGCTTTGGTGATGGATCTCATAGACCTAACTCCTCGCCAGAAGGAGCGGGCA
GCTTCACCTCATCAGGTCACACCACAGGCTGATGAGAAGATGCCAGTGTTGGAGTCAAGT
TCATGGCCTGCCAGCAAAGGTCTGGGGCATATGCCGAGAGCTGTTGAGAAAGGCTGTGTG
TCAGATCCTCTTCAGACATCTGGGAAAGCAGCAGCCCCTTCAGAGGACCCCTGGCAAGCT
GTTAAATCACTCACCCAGGCCAGACTTCTTTCTCAGCCTCCTGCCAAGGCCTTTTTATAT
GAGCCAACAACTCAGGCCTCAGGAAGAGCTTCTGCAGGGGCTGAGCAGACCCCAGGGCCT
CTTAGCCAATCCCCGGGCCTGGTGAAGCAGGCGAAGCAGATGGTCGGAGGCCAGCAACTA
CCTGCACTTGCCGCCAAGAGTGGGCAATCTTTTAGGTCTCTCGGGAAGGCCCCAGCCTCC
CTCCCCACTGAAGAAAAGAAGTTGGTAACCACAGAGCAAAGTCCCTGGGCCCTGGGAAAA
GCCTCATCACGGGCAGGGCTCTGGCCCATAGTGGCTGGACAGACACTGGCACAGTCTTGC
TGGTCTGCTGGGAGCACACAGACATTGGCACAGACTTGCTGGTCTCTTGGAAGAGGGCAA
GACCCCAAACCAGAGCAAAATACACTTCCAGCTCTTAACCAGGCTCCTTCCAGTCACAAG
TGTGCAGAATCAGAACAGAAGTAG

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 ]
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 ]
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 ]
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 ]
5. Douglas J, Hanks S, Temple IK, Davies S, Murray A, Upadhyaya M, Tomkins S, Hughes HE, Cole TR, Rahman N: NSD1 mutations are the major cause of Sotos syndrome and occur in some cases of Weaver syndrome but are rare in other overgrowth phenotypes. Am J Hum Genet. 2003 Jan;72(1):132-43. Epub 2002 Dec 2. [PubMed ]
6. Rio M, Clech L, Amiel J, Faivre L, Lyonnet S, Le Merrer M, Odent S, Lacombe D, Edery P, Brauner R, Raoul O, Gosset P, Prieur M, Vekemans M, Munnich A, Colleaux L, Cormier-Daire V: Spectrum of NSD1 mutations in Sotos and Weaver syndromes. J Med Genet. 2003 Jun;40(6):436-40. [PubMed ]

1. SET domain bifurcated 1
2. ERG-associated protein with SET domain
3. ESET
4. Histone H3-K9 methyltransferase 4
5. H3-K9-HMTase 4

MSSLPGCIGLDAATATVESEEIAELQQAVVEELGISMEELRHFIDEELEKMDCVQQRKKQ
LAELETWVIQKESEVAHVDQLFDDASRAVTNCESLVKDFYSKLGLQYRDSSSEDESSRPT
EIIEIPDEDDDVLSIDSGDAGSRTPKDQKLREAMAALRKSAQDVQKFMDAVNKKSSSQDL
HKGTLSQMSGELSKDGDLIVSMRILGKKRTKTWHKGTLIAIQTVGPGKKYKVKFDNKGKS
LLSGNHIAYDYHPPADKLYVGSRVVAKYKDGNQVWLYAGIVAETPNVKNKLRFLIFFDDG
YASYVTQSELYPICRPLKKTWEDIEDISCRDFIEEYVTAYPNRPMVLLKSGQLIKTEWEG
TWWKSRVEEVDGSLVRILFLDDKRCEWIYRGSTRLEPMFSMKTSSASALEKKQGQLRTRP
NMGAVRSKGPVVQYTQDLTGTGTQFKPVEPPQPTAPPAPPFPPAPPLSPQAGDSDLESQL
AQSRKQVAKKSTSFRPGSVGSGHSSPTSPALSENVSGGKPGINQTYRSPLGSTASAPAPS
ALPAPPAPPVFHGMLERAPAEPSYRAPMEKLFYLPHVCSYTCLSRVRPMRNEQYRGKNPL
LVPLLYDFRRMTARRRVNRKMGFHVIYKTPCGLCLRTMQEIERYLFETGCDFLFLEMFCL
DPYVLVDRKFQPYKPFYYILDITYGKEDVPLSCVNEIDTTPPPQVAYSKERIPGKGVFIN
TGPEFLVGCDCKDGCRDKSKCACHQLTIQATACTPGGQINPNSGYQYKRLEECLPTGVYE
CNKRCKCDPNMCTNRLVQHGLQVRLQLFKTQNKGWGIRCLDDIAKGSFVCIYAGKILTDD
FADKEGLEMGDEYFANLDHIESVENFKEGYESDAPCSSDSSGVDLKDQEDGNSGTEDPEE
SNDDSSDDNFCKDEDFSTSSVWRSYATRRQTRGQKENGLSETTSKDSHPPDLGPPHIPVP
PSIPVGGCNPPSSEETPKNKVASWLSCNSVSEGGFADSDSHSSFKTNEGGEGRAGGSRME
AEKASTSGLGIKDEGDIKQAKKEDTDDRNKMSVVTESSRNYGYNPSPVKPEGLRRPPSKT
SMHQSRRLMASAQSNPDDVLTLSSSTESEGESGTSRKPTAGQTSATAVDSDDIQTISSGS
EGDDFEDKKNMTGPMKRQVAVKSTRGFALKSTHGIAIKSTNMASVDKGESAPVRKNTRQF
YDGEESCYIIDAKLEGNLGRYLNHSCSPNLFVQNVFVDTHDLRFPWVAFFASKRIRAGTE
LTWDYNYEVGSVEGKELLCCCGAIECRGRLL

• Lysine Degradation (map00310 )

• S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine

• MBD (PF01429 )
• Pre-SET (PF05033 )
• SET (PF00856 )

• None

• None

AGCTGGAAGACGGGAGAGGACAAAAGCATGTCTTCCCTTCCTGGGTGCATTGGTTTGGAT
GCAGCAACAGCTACAGTGGAGTCTGAAGAGATTGCAGAGCTGCAACAGGCAGTGGTTGAG
GAACTGGGTATCTCTATGGAGGAACTTCGGCATTTCATCGATGAGGAACTGGAGAAGATG
GATTGTGTACAGCAACGCAAGAAGCAGCTAGCAGAGTTAGAGACATGGGTAATACAGAAA
GAATCTGAGGTGGCTCACGTTGACCAACTCTTTGATGATGCATCCAGGGCAGTGACTAAT
TGTGAGTCTTTGGTGAAGGACTTCTACTCCAAGCTGGGACTACAATACCGGGACAGTAGC
TCTGAGGACGAATCTTCCCGGCCTACAGAAATAATTGAGATTCCTGATGAAGATGATGAT
GTCCTCAGTATTGATTCAGGTGATGCTGGGAGCAGAACTCCAAAAGACCAGAAGCTCCGT
GAAGCTATGGCTGCCTTAAGAAAGTCAGCTCAAGATGTTCAGAAGTTCATGGATGCTGTC
AACAAGAAGAGCAGTTCCCAGGATCTGCATAAAGGAACCTTGAGTCAGATGTCTGGAGAA
CTAAGCAAAGATGGTGACCTGATAGTCAGCATGCGAATTCTGGGCAAGAAGAGAACTAAG
ACTTGGCACAAAGGCACCCTTATTGCCATCCAGACAGTTGGGCCAGGGAAGAAATACAAG
GTGAAATTTGACAACAAAGGAAAGAGTCTACTGTCGGGGAACCATATTGCCTATGATTAC
CACCCTCCTGCTGACAAGCTGTATGTGGGCAGTCGGGTGGTCGCCAAATACAAAGATGGG
AATCAGGTCTGGCTCTATGCTGGCATTGTAGCTGAGACACCAAACGTCAAAAACAAGCTC
AGGTTTCTCATTTTCTTTGATGATGGCTATGCTTCCTATGTCACACAGTCGGAACTGTAT
CCCATTTGCCGGCCACTGAAAAAGACTTGGGAGGACATAGAAGACATCTCCTGCCGTGAC
TTCATAGAGGAGTATGTCACTGCCTACCCCAACCGCCCCATGGTACTGCTCAAGAGTGGC
CAGCTTATCAAGACTGAGTGGGAAGGCACGTGGTGGAAGTCCCGAGTTGAGGAGGTGGAT
GGCAGCCTAGTCAGGATCCTCTTCCTGGATGACAAAAGATGTGAGTGGATCTATCGAGGC
TCTACACGGCTGGAGCCCATGTTCAGCATGAAAACATCCTCAGCCTCTGCACTGGAGAAG
AAGCAAGGACAGCTCAGGACACGTCCAAATATGGGTGCTGTGAGGAGCAAAGGCCCTGTT
GTCCAGTACACACAGGATCTGACCGGTACTGGAACCCAGTTCAAGCCAGTGGAACCCCCA
CAGCCTACAGCTCCACCTGCCCCACCTTTCCCACCTGCTCCACCTCTATCCCCCCAAGCA
GGTGACAGTGACTTGGAAAGCCAGCTTGCCCAGTCACGGAAGCAGGTAGCCAAAAAGAGC
ACGTCCTTTCGACCAGGATCTGTGGGCTCTGGTCATTCCTCCCCTACATCTCCTGCACTC
AGTGAAAATGTCTCTGGTGGGAAACCTGGGATCAACCAGACATATAGATCACCTTTAGGC
TCCACAGCCTCTGCCCCAGCACCCTCAGCACTCCCGGCCCCTCCAGCACCCCCAGTCTTC
CATGGCATGCTGGAGCGGGCCCCAGCAGAGCCCTCCTACCGTGCTCCCATGGAGAAGCTT
TTCTACTTACCTCATGTCTGCAGCTATACCTGTCTGTCTCGAGTCAGACCTATGAGGAAT
GAGCAGTACCGGGGCAAGAACCCTCTGCTGGTCCCGTTACTATATGACTTCCGGCGGATG
ACAGCCCGGCGTCGAGTTAACCGCAAGATGGGCTTTCATGTTATCTATAAGACACCTTGT
GGTCTCTGCCTTCGGACAATGCAGGAGATAGAACGCTACCTTTTCGAGACTGGCTGTGAC
TTCCTCTTCCTGGAGATGTTCTGTTTGGATCCATATGTTCTTGTGGACCGAAAGTTTCAG
CCCTATAAGCCTTTTTACTATATTTTGGACATCACTTATGGGAAGGAAGATGTTCCCCTA
TCCTGTGTCAATGAGATTGACACAACCCCTCCACCCCAGGTGGCCTACAGCAAGGAACGT
ATCCCGGGCAAGGGTGTTTTCATTAACACAGGCCCTGAATTTCTGGTTGGCTGTGACTGC
AAGGATGGGTGTCGGGACAAGTCCAAGTGTGCCTGCCATCAACTAACTATCCAGGCTACA
GCCTGTACCCCAGGAGGCCAAATCAACCCTAACTCTGGCTACCAGTACAAGAGACTAGAA
GAGTGTCTACCCACAGGGGTATATGAGTGTAACAAACGCTGCAAATGTGACCCAAACATG
TGCACAAACCGGTTGGTGCAACATGGACTACAAGTTCGGCTACAGCTATTCAAGACACAG
AACAAGGGCTGGGGTATCCGCTGCTTGGATGACATTGCCAAAGGCTCTTTTGTTTGTATT
TATGCAGGCAAAATCCTGACAGATGACTTTGCAGACAAGGAGGGTCTGGAAATGGGTGAT
GAGTACTTTGCAAATCTGGACCATATCGAGAGCGTGGAGAACTTCAAAGAAGGATATGAG
AGTGATGCCCCCTGTTCCTCTGACAGCAGTGGTGTAGACTTGAAGGACCAGGAAGATGGC
AACAGCGGTACAGAGGACCCTGAAGAGTCCAATGATGATAGCTCAGATGATAACTTCTGT
AAGGATGAGGACTTCAGCACCAGTTCAGTGTGGCGGAGCTATGCTACCCGGAGGCAGACC
CGGGGCCAGAAAGAGAACGGACTCTCTGAGACAACTTCCAAGGACTCCCACCCCCCAGAT
CTTGGACCCCCACATATTCCTGTTCCTCCCTCAATCCCTGTAGGTGGCTGCAATCCACCT
TCCTCCGAAGAGACACCCAAGAACAAGGTGGCCTCATGGTTGAGCTGCAATAGTGTCAGT
GAAGGTGGTTTTGCTGACTCTGATAGCCATTCATCCTTCAAGACTAATGAAGGTGGGGAG
GGCCGGGCTGGGGGAAGCCGAATGGAGGCTGAGAAGGCCTCCACCTCAGGACTAGGCATC
AAGGATGAGGGAGACATCAAACAGGCCAAGAAAGAGGACACTGACGACCGAAACAAGATG
TCAGTAGTTACTGAAAGCTCTCGAAATTACGGTTACAATCCTTCTCCTGTGAAGCCTGAA
GGACTTCGCCGCCCACCTAGTAAGACTAGTATGCATCAAAGCCGAAGACTCATGGCTTCT
GCTCAGTCCAACCCTGATGATGTCCTGACACTGTCCAGCAGCACAGAAAGTGAGGGGGAA
AGTGGGACCAGCCGAAAGCCCACTGCTGGTCAGACTTCGGCTACAGCGGTTGACAGTGAT
GATATCCAGACCATATCCTCTGGCTCTGAAGGGGATGACTTTGAGGACAAGAAGAACATG
ACTGGTCCAATGAAGCGTCAAGTGGCAGTAAAATCAACCCGAGGCTTTGCTCTTAAATCA
ACCCATGGGATTGCAATTAAATCAACCAACATGGCCTCTGTGGACAAGGGGGAGAGCGCA
CCTGTTCGTAAGAACACACGCCAATTCTATGATGGCGAGGAGTCTTGCTACATCATTGAT
GCCAAGCTTGAAGGCAACCTGGGCCGCTACCTCAACCACAGTTGCAGCCCCAACCTGTTT
GTCCAGAATGTCTTCGTGGATACCCATGATCTTCGCTTCCCCTGGGTGGCCTTCTTTGCC
AGCAAAAGAATCCGGGCTGGGACAGAACTTACTTGGGACTACAACTACGAGGTGGGCAGT
GTGGAAGGCAAGGAGCTACTCTGTTGCTGTGGGGCCATTGAATGCAGAGGACGTCTTCTT
TAG

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 ]
2. Schultz DC, Ayyanathan K, Negorev D, Maul GG, Rauscher FJ 3rd: SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-finger proteins. Genes Dev. 2002 Apr 15;16(8):919-32. [PubMed ]

1. Protein-beta-aspartate methyltransferase
2. PIMT
3. Protein L- isoaspartyl/D-aspartyl methyltransferase
4. L-isoaspartyl protein carboxyl methyltransferase

MAWKSGGASHSELIHNLRKNGIIKTDKVFEVMLATDRSHYAKCNPYMDSPQSIGFQATIS
APHMHAYALELLFDQLHEGAKALDVGSGSGILTACFARMVGCTGKVIGIDHIKELVDDSI
NNVRKDDPTLLSSGRVQLVVGDGRMGYAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLI
LPVGPAGGNQMLEQYDKLQDGSIKMKPLMGVIYVPLTDKEKQWSRWK

• S-adenosyl-L-methionine + protein L-isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester

• PCMT (PF01135 )

• None

• None

ATGGCCTGGAAATCCGGCGGCGCCAGCCACTCGGAGCTAATCCACAATCTCCGCAAAAAT
GGAATCATCAAGACAGATAAAGTATTTGAAGTGATGCTGGCTACAGACCGCTCCCACTAT
GCAAAATGTAACCCATACATGGATTCTCCACAATCAATAGGTTTCCAAGCAACAATCAGT
GCTCCACACATGCATGCATATGCGCTAGAACTTCTATTTGATCAGTTGCATGAAGGAGCT
AAAGCTCTTGATGTAGGATCTGGAAGTGGAATCCTTACTGCATGTTTTGCACGTATGGTT
GGATGTACTGGAAAAGTCATAGGAATTGATCACATTAAAGAGCTAGTAGATGACTCAGTA
AATAATGTCAGGAAGGACGATCCAACACTTCTGTCTTCAGGGAGAGTACAGCTTGTTGTG
GGGGATGGAAGAATGGGATATGCTGAAGAAGCCCCTTATGATGCCATTCATGTGGGAGCT
GCAGCCCCTGTTGTACCCCAGGCGCTAATAGATCAGTTAAAGCCCGGAGGAAGATTGATA
TTGCCTGTTGGTCCTGCAGGCGGAAACCAAATGTTGGAGCAGTATGACAAGCTACAAGAT
GGCAGCATCAAAATGAAGCCTCTGATGGGGGTGATATACGTGCCTTTAACAGATAAAGAA
AAGCAGTGGTCCAGGGATGAATTGTAA

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 ]
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 ]
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 ]
4. 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 ]
5. 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 ]
6. 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 ]
7. 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 ]
8. 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 ]

1. Isoprenylcysteine carboxylmethyltransferase
2. Prenylcysteine carboxyl methyltransferase
3. pcCMT
4. Prenylated protein carboxyl methyltransferase
5. PPMT

MAGCAARAPPGSEARLSLATFLLGASVLALPLLTRAGLQGRTGLALYVAGLNALLLLLYR
PPRYQIAIRACFLGFVFGCGTLLSFSQSSWSHFGWYMCSLSLFHYSEYLVTAVNNPKSLS
LDSFLLNHSLEYTVAALSSWLEFTLENIFWPELKQITWLSVTGLLMVVFGECLRKAAMFT
AGSNFNHVVQNEKSDTHTLVTSGVYAWFRHPSYVGWFYWSIGTQVMLCNPICGVSYALTV
WRFFRDRTEEEEISLIHFFGEEYLEYKKRVPTGLPFIKGVKVDL

• S-adenosyl-L-methionine + protein C-terminal S-farnesyl-L-cysteine = S-adenosyl-L-homocysteine + protein C-terminal S-farnesyl-L-cysteine methyl ester

• ICMT (PF04140 )

• 1-29

ATGGCGGGCTGCGCGGCGCGGGCTCCGCCGGGCTCTGAGGCGCGTCTCAGCCTCGCCACC
TTCCTGCTGGGCGCCTCGGTGCTCGCGCTGCCGCTGCTCACGCGCGCCGGCCTGCAGGGC
CGCACCGGGCTGGCGCTCTACGTGGCCGGGCTCAACGCGCTGCTGCTGCTGCTCTATCGG
CCGCCTCGCTACCAGATAGCCATCCGAGCTTGTTTCCTGGGGTTTGTGTTCGGCTGCGGC
ACGCTGCTAAGTTTTAGCCAGTCTTCTTGGAGTCACTTTGGCTGGTACATGTGCTCCCTG
TCATTGTTCCACTATTCTGAATACTTGGTGACAGCAGTCAATAATCCCAAAAGTCTGTCC
TTGGATTCCTTTCTCCTGAATCACAGCCTGGAGTATACAGTAGCTGCTCTTTCTTCTTGG
TTAGAGTTCACACTTGAAAATATCTTTTGGCCAGAACTGAAGCAGATTACCTGGCTCAGT
GTCACAGGGCTGCTGATGGTGGTCTTCGGAGAATGTCTGAGGAAGGCGGCCATGTTTACA
GCTGGCTCCAATTTCAACCACGTGGTACAGAATGAAAAATCAGATACACATACTCTGGTG
ACCAGTGGAGTGTACGCTTGGTTTCGGCATCCTTCTTACGTCGGGTGGTTTTACTGGAGT
ATTGGAACTCAGGTGATGCTGTGTAACCCCATCTGCGGCGTCAGCTATGCCCTGACAGTG
TGGCGATTCTTCCGCGATCGAACAGAAGAAGAAGAAATCTCACTAATTCACTTTTTTGGA
GAGGAGTACCTGGAGTATAAGAAGAGGGTGCCCACGGGCCTGCCTTTCATAAAGGGGGTC
AAGGTGGACCTGTGA

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 ]
2. Lin X, Antalffy B, Kang D, Orr HT, Zoghbi HY: Polyglutamine expansion down-regulates specific neuronal genes before pathologic changes in SCA1. Nat Neurosci. 2000 Feb;3(2):157-63. [PubMed ]

1. Aromatic alkylamine N-methyltransferase
2. Indolamine N-methyltransferase
3. Arylamine N- methyltransferase
4. Amine N-methyltransferase

MKGGFTGGDEYQKHFLPRDYLATYYSFDGSPSPEAEMLKFNLECLHKTFGPGGLQGDTLI
DIGSGPTIYQVLAACDSFQDITLSDFTDRNREELEKWLKKEPGAYDWTPAVKFACELEGN
SGRWEEKEEKLRAAVKRVLKCDVHLGNPLAPAVLPLADCVLTLLAMECACCSLDAYRAAL
CNLASLLKPGGHLVTTVTLRLPSYVVGKREFSCVALEKEEVEQAVLDAGFDIEQLLHSPQ
SYSVTNAANNGVCCIVARKKPGP

• Tryptophan Metabolism (map00380 )

• S-adenosyl-L-methionine + an amine = S-adenosyl-L-homocysteine + a methylated amine

• NNMT_PNMT_TEMT (PF01234 )

• None

• None

ATGAAGGGTGGCTTCACTGGGGGTGATGAGTACCAGAAGCACTTCCTGCCCAGGGACTAC
TTGGCTACTTACTACAGCTTCGATGGCAGCCCCTCACCCGAGGCCGAGATGCTGAAGTTT
AACTTGGAATGTCTCCACAAGACCTTCGGCCCTGGAGGCCTCCAAGGGGACACGCTGATT
GACATTGGCTCAGGTCCTACCATCTACCAAGTTCTTGCTGCCTGTGATTCCTTCCAAGAC
ATCACTCTCTCCGACTTTACCGACCGCAACCGGGAGGAGCTGGAAAAGTGGCTGAAGAAG
GAGCCGGGGGCCTATGACTGGACCCCAGCGGTGAAATTCGCCTGTGAGCTGGAAGGAAAC
AGCGGCCGATGGGAGGAGAAGGAGGAGAAGCTGCGGGCAGCGGTGAAGCGGGTGCTCAAG
TGCGATGTCCACCTGGGCAACCCGCTGGCCCCGGCTGTGTTGCCTCTCGCCGACTGTGTG
CTCACCCTGCTGGCCATGGAGTGTGCCTGCTGTAGCCTTGATGCCTACCGCGCTGCCCTG
TGCAACCTTGCCTCACTGCTCAAGCCGGGTGGCCACCTGGTGACCACTGTCACGCTTCGG
CTCCCGTCCTACGTGGTGGGGAAGCGTGAATTTTCCTGCGTGGCCCTGGAGAAAGAGGAG
GTGGAGCAGGCTGTCCTGGATGCTGGCTTTGACATTGAACAGCTCCTACACAGTCCCCAG
AGCTACTCTGTCACCAATGCTGCCAACAATGGGGTCTGCTGCATTGTGGCTCGCAAGAAG
CCTGGGCCCTGA

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 ]
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 ]

1. cytosine-5-methyltransferase 3A
2. Dnmt3a
3. DNA methyltransferase HsaIIIA
4. DNA MTase HsaIIIA
5. M.HsaIIIA

MPSSGPGDTSSSAAEREEDRKDGEEQEEPRGKEERQEPSTTARKVGRPGRKRKHPPVESG
DTPKDPAVISKSPSMAQDSGASELLPNGDLEKRSEPQPEEGSPAGGQKGGAPAEGEGAAE
TLPEASRAVENGCCTPKEGRGAPAEAGKEQKETNIESMKMEGSRGRLRGGLGWESSLRQR
PMPRLTFQAGDPYYISKRKRDEWLARWKREAEKKAKVIAGMNAVEENQGPGESQKVEEAS
PPAVQQPTDPASPTVATTPEPVGSDAGDKNATKAGDDEPEYEDGRGFGIGELVWGKLRGF
SWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNKQP
MYRKAIYEVLQVASSRAGKLFPVCHDSDESDTAKAVEVQNKPMIEWALGGFQPSGPKGLE
PPEEEKNPYKEVYTDMWVEPEAAAYAPPPPAKKPRKSTAEKPKVKEIIDERTRERLVYEV
RQKCRNIEDICISCGSLNVTLEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGG
REVLMCGNNNCCRCFCVECVDLLVGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPS
RLQMFFANNHDQEFDPPKVYPPVPAEKRKPIRVLSLFDGIATGLLVLKDLGIQVDRYIAS
EVCEDSITVGMVRHQGKIMYVGDVRSVTQKHIQEWGPFDLVIGGSPCNDLSIVNPARKGL
YEGTGRLFFEFYRLLHDARPKEGDDRPFFWLFENVVAMGVSDKRDISRFLESNPVMIDAK
EVSAAHRARYFWGNLPGMNRPLASTVNDKLELQECLEHGRIAKFSKVRTITTRSNSIKQG
KDQHFPVFMNEKEDILWCTEMERVFGFPVHYTDVSNMSRLARQRLLGRSWSVPVIRHLFA
PLKEYFACV

• Methionine Metabolism (map00271 )

• S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine

• DNA_methylase (PF00145 )
• PWWP (PF00855 )

• None

• None

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

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 ]
2. Robertson KD, Uzvolgyi E, Liang G, Talmadge C, Sumegi J, Gonzales FA, Jones PA: The human DNA methyltransferases (DNMTs) 1, 3a and 3b: coordinate mRNA expression in normal tissues and overexpression in tumors. Nucleic Acids Res. 1999 Jun 1;27(11):2291-8. [PubMed ]

1. Dihydroxyhexaprenylbenzoate methyltransferase
2. 3,4- dihydroxy-5-hexaprenylbenzoate methyltransferase
3. DHHB methyltransferase
4. DHHB-MT
5. DHHB-MTase

MWSGRKLGSSGGWFLRVLGPGGCNTKAARPLISSAVYVKNQLSGTLQIKPGVFNEYRTIW
FKSYRTIFSCLNRIKSFRYPWARLYSTSQTTVDSGEVKTFLALAHKWWDEQGVYAPLHSM
NDLRVPFIRDNLLKTIPNHQPGKPLLGMKILDVGCGGGLLTEPLGRLGASVIGIDPVDEN
IKTAQCHKSFDPVLDKRIEYRVCSLEEIVEETAETFDAVVASEVVEHVIDLETFLQCCCQ
VLKPGGSLFITTINKTQLSYALGIVFSEQIAGIVPKGTHTWEKFVSPETLESILESNGLS
VQTVVGMLYNPFSGYWHWSENTSLNYAAHAVKSRVQEHPASAEFVLKGETEELQANACTN
PAVHEKLKK

• Ubiquinone Biosynthesis (map00130 )

• S-adenosyl-L-methionine + 3-hexaprenyl-4,5-dihydroxybenzoate = S-adenosyl-L-homocysteine + 3-hexaprenyl-4-hydroxy-5-methoxybenzoate

• Methyltransf_11 (PF08241 )

• None

• None

ATGTGGAGTGGCCGTAAGCTGGGCTCCTCCGGGGGTTGGTTTTTAAGAGTGCTGGGGCCT
GGAGGCTGTAATACAAAAGCTGCGCGTCCCTTAATTTCCTCGGCGGTTTATGTGAAGAAC
CAGCTCAGTGGGACTCTACAGATTAAACCAGGGGTTTTCAATGAATACAGAACCATATGG
TTCAAATCCTACAGGACGATCTTTTCCTGTTTGAACAGAATAAAGAGTTTCAGGTACCCT
TGGGCGAGACTGTACAGTACTTCCCAAACCACTGTCGACAGCGGTGAGGTAAAAACCTTC
TTGGCCCTGGCTCACAAATGGTGGGATGAACAAGGAGTATATGCACCTCTTCATTCCATG
AATGACCTGAGGGTGCCATTTATTAGGGACAATCTTCTGGAAACAATTCCTAATCACCAG
CCAGGAAAACCTTTGTTGGGGATGAAGATTCTTGACGTTGGCTGTGGTGGTGGGCTGTTA
ACTGAACCTCTAGGCCGGCTTGGGGCTTCAGTTATTGGAATCGACCCTGTGGATGAGAAC
ATTAAAACAGCACAATGCCATAAATCATTTGATCCAGTCCTGGATAAGAGAATAGAGTAC
AGAGTGTGTTCCCTGGAAGAGATTGTGGAAGAGACTGCAGAAACATTTGATGCTGTTGTA
GCTTCTGAAGTTGTAGAACATGTGATTGATCTAGAAACATTTTTACAGTGCTGCTGTCAA
GTGTTAAAACCCGGTGGTTCTTTATTCATTACTACAATCAACAAAACACAACTTTCCTAT
GCCTTGGGAATTGTTTTTTCAGAGCAAATTGCAGGTATTGTACCAAAAGGTACTCATACA
TGGGAGAAGTTTGTTTCACTTGAACCACTAGAGAGCATTCTGGAATCAAATGGTCTGTCA
GTTCAAACAGTGGTAGGAATGCTCTATAACCCCTTCTCAGGTTACTGGCATTGGAGTGAA
GATACCAGCCTTAACTATGCAGCTCATGCTGTGAAATCCAGGGTCCAGGAACACCCAGCC
TCTGCTGAGTTTGTTTTAAAGGGAGAAACAGAAGAGCTCCAAGCTAATGCCTGCACCAAT
CCAGCTGTGCATGAAAAGCTGAAGAAATGA

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 ]
2. Jonassen T, Clarke CF: Isolation and functional expression of human COQ3, a gene encoding a methyltransferase required for ubiquinone biosynthesis. J Biol Chem. 2000 Apr 28;275(17):12381-7. [PubMed ]

1. Methionine adenosyltransferase 1
2. AdoMet synthetase 1
3. Methionine adenosyltransferase I/III
4. MAT-I/III

MNGPVDGLCDHSLSEGVFMFTSESVGEGHPDKICDQISDAVLDAHLKQDPNAKVACETVC
KTGMVLLCGEITSMAMVDYQRVVRDTIKHIGYDDSAKGFDFKTCNVLVALEQQSPDIAQC
VHLDRNEEDVGAGDQGLMFGYATDETEECMPLTIILAHKLNARMADLRRSGLLPWLRPDS
KTQVTVQYMQDNGAVIPVRIHTIVISVQHNEDITLEEMRRALKEQVIRAVVPAKYLDEDT
VYHLQPSGRFVIGGPQGDAGVTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARW
VAKSLVKAGLCRRVLVQVSYAIGVAEPLSISIFTYGTSQKTERELLDVVHKNFDLRPGVI
VRDLDLKKPIYQKTACYGHFGRSEFPWEVPRKLVF

• Methionine Metabolism (map00271 )
• Selenoamino Acid Metabolism (map00450 )

• ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine

• S-AdoMet_synt_C (PF02773 )
• S-AdoMet_synt_M (PF02772 )
• S-AdoMet_synt_N (PF00438 )

• None

• None

ATGAATGGACCGGTGGATGGCTTGTGTGACCACTCTCTAAGTGAAGGAGTCTTCATGTTC
ACATCGGAGTCTGTGGGAGAGGGACACCCGGATAAGATCTGTGACCAGATCAGTGATGCA
GTGCTGGATGCCCATCTCAAGCAAGACCCCAATGCCAAGGTGGCCTGTGAGACAGTGTGC
AAGACCGGCATGGTGCTGCTGTGTGGTGAGATCACCTCAATGGCCATGGTGGACTACCAG
CGGGTGGTGAGGGACACCATCAAGCACATCGGCTACGATGACTCAGCCAAGGGCTTTGAC
TTCAAGACTTGCAACGTGCTGGTGGCTTTGGAGCAGCAATCCCCAGATATTGCCCAGTGC
GTCCATCTGGACAGAAATGAGGAGGATGTGGGGGCAGGAGATCAGGGTTTGATGTTCGGC
TATGCCACCGACGAGACAGAGGAGTGCATGCCCCTCACCATCATCCTTGCTCACAAGCTC
AACGCCCGGATGGCAGACCTCAGGCGCTCCGGCCTCCTCCCCTGGCTGCGGCCTGACTCT
AAGACTCAGGTGACAGTTCAGTACATGCAGGACAATGGCGCAGTCATCCCTGTGCGCATC
CACACCATCGTCATCTCTGTGCAGCACAACGAAGACATCACGCTGGAGGAGATGCGCAGG
GCCCTGAAGGAGCAAGTCATCAGGGCCGTGGTGCCGGCCAAGTACCTGGACGAAGACACC
GTCTACCACCTGCAGCCCAGTGGGCGGTTTGTCATCGGAGGTCCCCAGGGGGATGCGGGT
GTCACTGGCCGTAAGATTATTGTGGACACCTATGCGGCCTGGGGGGCTCATGGTGGTGGG
GCCTTCTCTGGGAAGGACTACACCAAGGTGGACCGCTCAGCCGCATATGCTGCCCGCTGG
GTGGCCAAGTCTCTGGTGAAAGCAGGGCTCTGCCGGAGAGTGCTTGTCCAGGTTTCCTAT
GCCATTGGTGTGGCCGAGCCGCTGTCCATTTCCATCTTCACCTACGGAACCTCTCAGAAG
ACAGAGCGAGAGCTGCTGGATGTGGTGCATAAGAACTTCGACCTCCGGCCGGGCGTCATT
GTCAGGGACTTGGATTTGAAGAAGCCCATCTACCAGAAGACAGCATGCTACGGCCATTTC
GGAAGAAGCGAGTTCCCATGGGAGGTTCCCAGGAAGCTTGTATTTTAG

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 ]
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 ]
3. Ubagai T, Lei KJ, Huang S, Mudd SH, Levy HL, Chou JY: Molecular mechanisms of an inborn error of methionine pathway. Methionine adenosyltransferase deficiency. J Clin Invest. 1995 Oct;96(4):1943-7. [PubMed ]
4. 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 ]
5. 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 ]
6. 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 ]

1. Histone H3-K9 methyltransferase 3
2. H3-K9-HMTase 3
3. Euchromatic histone-lysine N-methyltransferase 2
4. HLA-B-associated transcript 8
5. Protein G9a

MAAAAGAAAAAAAEGEAPAEMGALLLEKETRGATERVHGSLGDTPRSEETLPKATPDSLE
PAGPSSPASVTVTVGDEGADTPVGATPLIGDESENLEGDGDLRGGRILLGHATKSFPSSP
SKGGSCPSRAKMSMTGAGKSPPSVQSLAMRLLSMPGAQGAAAAGSEPPPATTSPEGQPKV
HRARKTMSKPGNGQPPVPEKRPPEIQHFRMSDDVHSLGKVTSDLAKRRKLNSGGGLSEEL
GSARRSGEVTLTKGDPGSLEEWETVVGDDFSLYYDSYSVDERVDSDSKSEVEALTEQLSE
EEEEEEEEEEEEEEEEEEEEEEEDEESGNQSDRSGSSGRRKAKKKWRKDSPWVKPSRKRR
KREPPRAKEPRGVNGVGSSGPSEYMEVPLGSLELPSEGTLSPNHAGVSNDTSSLETERGF
EELPLCSCRMEAPKIDRISERAGHKCMATESVDGELSGCNAAILKRETMRPSSRVALMVL
CETHRARMVKHHCCPGCGYFCTAGTFLECHPDFRVAHRFHKACVSQLNGMVFCPHCGEDA
SEAQEVTIPRGDGVTPPAGTAAPAPPPLSQDVPGRADTSQPSARMRGHGEPRRPPCDPLA
DTIDSSGPSLTLPNGGCLSAVGLPLGPGREALEKALVIQESERRKKLRFHPRQLYLSVKQ
GELQKVILMLLDNLDPNFQSDQQSKRTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRT
PLMEAVVNNHLEVARYMVQRGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGQVDVNA
QDSGGWTPIIWAAEHKHIEVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNA
RCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTAWDLTPERSDVWFA
LQLNRKLRLGVGNRAIRTEKIICRDVARGYENVPIPCVNGVDGEPCPEDYKYISENCETS
TMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQA
CSCWRNCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVR
EDDSYLFDLDNKDGEVYCIDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFS
SRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQSRLARLDPHPELLP
ELGSLPPVNT

• Lysine Degradation (map00310 )

• S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine

• Ank (PF00023 )
• Pre-SET (PF05033 )
• SET (PF00856 )

• None

• None

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 ]
2. 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 ]
3. 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 ]
4. 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 ]

1. AdoMetDC
2. SamDC[Contains: S-adenosylmethionine decarboxylase alpha chain
3. S- adenosylmethionine decarboxylase beta chain]

MEAAHFFEGTEKLLEVWFSRQQPDANQGSGDLRTIPRSEWDILLKDVQCSIISVTKTDKQ
EAYVLSESSMFVSKRRFILKTCGTTLLLKALVPLLKLARDYSGFDSIQSFFYSRKNFMKP
SHQGYPHRNFQEEIEFLNAIFPNGAAYCMGRMNSDCWYLYTLDFPESRVISQPDQTLEIL
MSELDPAVMDQFYMKDGVTAKDVTRESGIRDLIPGSVIDATMFNPCGYSMNGMKSDGTYW
TIHITPEPEFSYVSFETNLSQTSYDDLIRKVVEVFKPGKFVTTLFVNQSSKCRTVLASPQ
KIEGFKRLDCQSAMFNDYNFVFTSFAKKQQQQQS

• Arginine and Proline Metabolism (map00330 )

• S-adenosyl-L-methionine = (5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2

• SAM_decarbox (PF01536 )

• None

• None

ATGGAAGCTGCACATTTTTTCGAAGGGACCGAGAAGCTGCTGGAGGTTTGGTTCTCCCGG
CAGCAGCCCGACGCAAACCAAGGATCTGGGGATCTTCGCACTATCCCAAGATCTGAGTGG
GACATACTTTTGAAGGATGTGCAATGTTCAATCATAAGTGTGACAAAAACTGACAAGCAG
GAAGCTTATGTACTCAGTGAGAGTAGCATGTTTGTCTCCAAGAGACGTTTCATTTTGAAG
ACATGTGGTACCACCCTCTTGCTGAAAGCACTGGTTCCCCTGTTGAAGCTTGCTAGGGAT
TACAGTGGGTTTGACTCAATTCAAAGCTTCTTTTATTCTCGTAAGAATTTCATGAAGCCT
TCTCACCAAGGGTACCCACACCGGAATTTCCAGGAAGAAATAGAGTTTCTTAATGCAATT
TTCCCAAATGGAGCAGGATATTGTATGGGACGTATGAATTCTGACTGTTGGTACTTATAT
ACTCTGGATTTCCCAGAGAGTCGGGTAATCAGTCAGCCAGATCAAACCTTGGAAATTCTG
ATGAGTGAGCTTGACCCAGCAGTTATGGACCAGTTCTACATGAAAGATGGTGTTACTGCA
AAGGATGTCACTCGTGAGAGTGGAATTCGTGACCTGATACCAGGTTCTGTCATTGATGCC
ACAATGTTCAATCCTTGTGGGTATTCGATGAATGGAATGAAATCGGATGGAACTTATTGG
ACTATTCACATCACTCCAGAACCAGAATTTTCTTATGTTAGCTTTGAAACAAACTTAAGT
CAGACCTCCTATGATGACCTGATCAGGAAAGTTGTAGAAGTCTTCAAGCCAGGAAAATTT
GTGACCACCTTGTTTGTTAATCAGAGTTCTAAATGTCGCACAGTGCTTGCTTCGCCCCAG
AAGATTGAAGGTTTTAAGCGTCTTGATTGCCAGAGTGCTATGTTCAATGATTACAATTTT
GTTTTTACCAGTTTTGCTAAGAAGCAGCAACAACAGCAGAGTTGA

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 ]
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 ]
3. 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 ]
4. 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 ]
5. 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 ]
6. 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 ]
7. 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 ]

1. MSR

MGAASVRAGARLVEVALCSFTVTCLEVMRRFLLLYATQQGQAKAIAEEICEQAVVHGFSA
DLHCISESDKYDLKTETAPLVVVVSTTGTGDPPDTARKFVKEIQNQTLPVDFFAHLRYGL
LGLGDSEYTYFCNGGKIIDKRLQELGARHFYDTGHADDCVGLELVVEPWIAGLWPALRKH
FRSSRGQEEISGALPVASPASLRTDLVKSELLHIESQVELLRFDDSGRKDSEVLKQNAVN
SNQSNVVIEDFESSLTRSVPPLSQASLNIPGLPPEYLQVHLQESLGQEESQVSVTSADPV
FQVPISKAVQLTTNDAIKTTLLVELDISNTDFSYQPGDAFSVICPNSDSEVQSLLQRLQL
EDKREHCVLLKIKADTKKKGATLPQHIPAGCSLQFIFTWCLEIRAIPKKAFLRALVDYTS
DSAEKRRLQELCSKQGAADYSRFVRDACACLLDLLLAFPSCQPPLSLLLEHLPKLQPRPY
SCASSSLFHPGKLHFVFNIVEFLSTATTEVLRKGVCTGWLALLVASVLQPNIHASHEDSG
KALAPKISISPRTTNSFHLPDDPSIPIIMVGPGTGIAPFIGFLQHREKLQEQHPDGNFGA
MWLFFGCRHKDRDYLFRKELRHFLKHGILTHLKVSFSRDAPVGEEEAPAKYVQDNIQLHG
QQVARILLQENGHIYVCGDAKNMAKDVHDALVQIISKEVGVEKLEAMKTLATLKEEKRYL
QDIWS

• 2 [methionine synthase]-methylcob(I)alamin + 2 S-adenosylhomocysteine + NADP+ = 2 [methionine synthase]-cob(I)alamin + NADPH + H+ + 2 S-adenosylLmethionine

• FAD_binding_1 (PF00667 )
• Flavodoxin_1 (PF00258 )
• NAD_binding_1 (PF00175 )

• 1-24

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

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 ]
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 ]
3. Wilson A, Leclerc D, Rosenblatt DS, Gravel RA: Molecular basis for methionine synthase reductase deficiency in patients belonging to the cblE complementation group of disorders in folate/cobalamin metabolism. Hum Mol Genet. 1999 Oct;8(11):2009-16. [PubMed ]
4. Wilson A, Platt R, Wu Q, Leclerc D, Christensen B, Yang H, Gravel RA, Rozen R: A common variant in methionine synthase reductase combined with low cobalamin (vitamin B12) increases risk for spina bifida. Mol Genet Metab. 1999 Aug;67(4):317-23. [PubMed ]

1. Suppressor of variegation 3-9 homolog 1
2. Su(var3-9 homolog 1
3. Position-effect variegation 3-9 homolog
4. Histone H3-K9 methyltransferase 1
5. H3-K9- HMTase 1

MAENLKGCSVCCKSSWNQLQDLCRLAKLSCPALGISKRNLYDFEVEYLCDYKKIREQEYY
LVKWRGYPDSESTWEPRQNLKCVRILKQFHKDLERELLRRHHRSKTPRHLDPSLANYLVQ
KAKQRRALRRWEQELNAKRSHLGRITVENEVDLDGPPRAFVYINEYRVGEGITLNQVAVG
CECQDCLWAPTGGCCPGASLHKFAYNDQGQVRLRAGLPIYECNSRCRCGYDCPNRVVQKG
IRYDLCIFRTDDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFD
LDYVEDVYTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIRAGEE
LTFDYNMQVDPVDMESTRMDSNFGLAGLPGSPKKRVRIECKCGTESCRKYLF

• Lysine Degradation (map00310 )

• S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine

• Chromo (PF00385 )
• Pre-SET (PF05033 )
• SET (PF00856 )

• None

• None

ATGGCGGAAAATTTAAAAGGCTGCAGCGTGTGTTGCAAGTCTTCTTGGAATCAGCTGCAG
GACCTGTGCCGCCTGGCCAAGCTCTCCTGCCCTGCCCTCGGTATCTCTAAGAGGAACCTC
TATGACTTTGAAGTCGAGTACCTGTGCGATTACAAGAAGATCCGCGAACAGGAATATTAC
CTGGTGAAATGGCGTGGATATCCAGACTCAGAGAGCACCTGGGAGCCACGGCAGAATCTC
AAGTGTGTGCGTATCCTCAAGCAGTTCCACAAGGACTTAGAAAGGGAGCTGCTCCGGCGG
CACCACCGGTCAAAGACCCCCCGGCACCTGGACCCAAGCTTGGCCAACTACCTGGTGCAG
AAGGCCAAGCAGAGGCGGGCGCTCCGTCGCTGGGAGCAGGAGCTCAATGCCAAGCGCAGC
CATCTGGGACGCATCACTGTAGAGAATGAGGTGGACCTGGACGGCCCTCCGCGGGCCTTC
GTGTACATCAATGAGTACCGTGTTGGTGAGGGCATCACCCTCAACCAGGTGGCTGTGGGC
TGCGAGTGCCAGGACTGTCTGTGGGCACCCACTGGAGGCTGCTGCCCGGGGGCGTCACTG
CACAAGTTTGCCTACAATGACCAGGGCCAGGTGCGGCTTCGAGCCGGGCTGCCCATCTAC
GAGTGCAACTCCCGCTGCCGCTGCGGCTATGACTGCCCAAATCGTGTGGTACAGAAGGGT
ATCCGATATGACCTCTGCATCTTCCGGACGGATGATGGGCGTGGCTGGGGCGTCCGCACC
CTGGAGAAGATTCGCAAGAACAGCTTCGTCATGGAGTACGTGGGAGAGATCATTACCTCA
GAGGAGGCAGAGCGGCGGGGCCAGATCTACGACCGTCAGGGCGCCACCTACCTCTTTGAC
CTGGACTACGTGGAGGACGTGTACACCGTGGATGCCGCCTACTATGGCAACATCTCCCAC
TTTGTCAACCACAGTTGTGACCCCAACCTGCAGGTGTACAACGTCTTCATAGACAACCTT
GACGAGCGGCTGCCCCGCATCGCTTTCTTTGCCACAAGAACCATCCGGGCAGGCGAGGAG
CTCACCTTTGATTACAACATGCAAGTGGACCCCGTGGACATGGAGAGCACCCGCATGGAC
TCCAACTTTGGCCTGGCTGGGCTCCCTGGCTCCCCTAAGAAGCGGGTCCGTATTGAATGC
AAGTGTGGGACTGAGTCCTGCCGCAAATACCTCTTCTAG

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 ]
2. 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 ]
3. 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 ]
4. 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 ]
5. 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 ]
6. 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 ]
7. 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 ]

MESGFTSKDTYLSHFNPRDYLEKYYKFGSRHSAESQILKHLLKNLFKIFCLDGVKGDLLI
DIGSGPTIYQLLSACESFKEIVVTDYSDQNLQELEKWLKKEPEAFDWSPVVTYVCDLEGN
RVKGPEKEEKLRQAVKQVLKCDVTQSQPLGAVPLPPADCVLSTLCLDAACPDLPTYCRAL
RNLGSLLKPGGFLVIMDALKSSYYMIGEQKFSSLPLGREAVEAAVKEAGYTIEWFEVISQ
SYSSTMANNEGLFSLVARKLSRPL

• Nicotinate and Nicotinamide Metabolism (map00760 )

• S-adenosyl-L-methionine + nicotinamide = S-adenosyl-L-homocysteine + 1-methylnicotinamide

• NNMT_PNMT_TEMT (PF01234 )

• None

• None

ATGGAATCAGGCTTCACCTCCAAGGACACCTATCTAAGCCATTTTAACCCTCGGGATTAC
CTAGAAAAATATTACAAGTTTGGTTCTAGGCACTCTGCAGAAAGCCAGATTCTTAAGCAC
CTTCTGAAAAATCTTTTCAAGATATTCTGCCTAGACGGTGTGAAGGGAGACCTGCTGATT
GACATCGGCTCTGGCCCCACTATCTATCAGCTCCTCTCTGCTTGTGAATCCTTTAAGGAG
ATCGTCGTCACTGACTACTCAGACCAGAACCTGCAGGAGCTGGAGAAGTGGCTGAAGAAA
GAGCCAGAGGCCTTTGACTGGTCCCCAGTGGTGACCTATGTGTGTGATCTTGAAGGGAAC
AGAGTCAAGGGTCCAGAGAAGGAGGAGAAGTTGAGACAGGCGGTCAAGCAGGTGCTGAAG
TGTGATGTGACTCAGAGCCAGCCACTGGGGGCCGTCCCCTTACCCCCGGCTGACTGCGTG
CTCAGCACACTGTGTCTGGATGCCGCCTGCCCAGACCTCCCCACCTACTGCAGGGCGCTC
AGGAACCTCGGCAGCCTACTGAAGCCAGGGGGCTTCCTGGTGATCATGGATGCGCTCAAG
AGCAGCTACTACATGATTGGTGAGCAGAAGTTCTCCAGCCTCCCCCTGGGCCGGGAGGCA
GTAGAGGCTGCTGTGAAAGAGGCTGGCTACACAATCGAATGGTTTGAGGTGATCTCGCAA
AGTTATTCTTCCACCATGGCCAACAACGAAGGACTTTTCTCCCTGGTGGCGAGGAAGCTG
AGCAGACCCCTGTGA

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 ]
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 ]
3. Hubbard MJ, McHugh NJ: Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping. Electrophoresis. 2000 Nov;21(17):3785-96. [PubMed ]

1. Suppressor of variegation 3-9 homolog 2
2. Su(var3-9 homolog 2
3. Histone H3-K9 methyltransferase 2
4. H3-K9-HMTase 2

MAAVGAEARGAWCVPCLVSLDTLQELCRKEKLTCKSIGITKRNLNNYEVEYLCDYKVVKD
MEYYLVKWKGWPDSTNTWEPLQNLKCPLLLQQFSNDKHNYLSQVKKGKAITPKDNNKTLK
PAIAEYIVKKAKQRIALQRWQDELNRRKNHKGMIFVENTVDLEGPPSDFYYINEYKPAPG
ISLVNEATFGCSCTDCFFQKCCPAEAGVLLAYNKNQQIKIPPGTPIYECNSRCQCGPDCP
NRIVQKGTQYSLCIFRTSNGRGWGVKTLVKIKRMSFVMEYVGEVITSEEAERRGQFYDNK
GITYLFDLDYESDEFTVDAARYGNVSHFVNHSCDPNLQVFNVFIDNLDTRLPRIALFSTR
TINAGEELTFDYQMKGSGDISSDSIDHSPAKKRVRTVCKCGAVTCRGYLN

• Lysine Degradation (map00310 )

• S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine

• Chromo (PF00385 )
• Pre-SET (PF05033 )
• SET (PF00856 )

• 1-13

ATGGAATATTATCTTGTAAAATGGAAAGGATGGCCAGATTCTACAAATACTTGGGAACCT
TTGCAAAATCTGAAGTGCCCGTTACTGCTTCAGCAATTCTCTAATGACAAGCATAATTAT
TTATCTCAGGTAAAGAAAGGCAAAGCAATAACTCCAAAAGACAATAACAAAACTTTGAAA
CCTGCCATTGCTGAGTACATTGTGAAGAAGGCTAAACAAAGGATAGCTCTGCAGAGATGG
CAAGATGAACTCAACAGAAGAAAGAATCATAAAGGAATGATATTTGTTGAAAATACTGTT
GATTTAGAGGGCCCACCTTCAGACTTCTATTACATTAACGAATACAAACCAGCTCCTGGA
ATCAGCTTAGTCAATGAAGCTACCTTTGGTTGTTCATGCACAGATTGCTTCTTTCAAAAA
TGTTGTCCTGCTGAAGCTGGAGTTCTTTTGGCTTATAATAAAAACCAACAAATTAAAATC
CCACCTGGTACTCCCATCTATGAATGCAACTCAAGGTGTCAGTGTGGTCCTGATTGTCCC
AATAGGATTGTACAAAAAGGCACACAGTATTCGCTTTGCATCTTTCGAACTAGCAATGGA
CGTGGCTGGGGTGTAAAGACCCTTGTGAAGATTAAAAGAATGAGTTTTGTCATGGAATAT
GTTGGAGAGGTAATCACAAGTGAAGAAGCTGAAAGACGAGGACAGTTCTATGACAACAAG
GGAATCACGTATCTCTTTGATCTGGACTATGAGTCTGATGAATTCACAGTGGATGCGGCT
CGATACGGCAATGTGTCTCATTTTGTGAATCACAGCTGTGACCCAAATCTTCAGGTGTTC
AATGTTTTCATTGATAACCTCGATACTCGTCTTCCCCGAATAGCATTGTTTTCCACAAGA
ACCATAAATGCTGGAGAAGAGCTGACTTTTGATTATCAAATGAAAGGTTCTGGAGATATA
TCTTCAGATTCTATTGACCACAGCCCAGCCAAAAAGAGGGTCAGAACAGTATGTAAATGT
GGAGCTGTGACTTGCAGAGGTTACCTCAACTGA

1. Histone H3-K9 methyltransferase 5
2. H3-K9-HMTase 5
3. Euchromatic histone-lysine N-methyltransferase 1
4. Eu-HMTase1
5. G9a- like protein 1
6. GLP1

MAADEGSAEKQAGEAHMAADGETNGSCENSDASSHANAAKHTQDSARVNPQDGTNTLTRI
AENGVSERDSEAAKQNHVTADDFVQTSVIGSNGYILNKPALQAQPLRTTSTLASSLPGHA
AKTLPGGAGKGRTPSAFPQTPAAPPATLGEGSADTEDRKLPAPGADVKVHRARKTMPKSV
VGLHAASKDPREVREARDHKEPKEEINKNISDFGRQQLLPPFPSLHQSLPQNQCYMATTK
SQTACLPFVLAAAVSRKKKRRMGTYSLVPKKKTKVLKQRTVIEMFKSITHSTVGSKGEKD
LGASSLHVNGESLEMDSDEDDSEELEEDDGHGAEQAAAFPTEDSRTSKESMSEADRAQKM
DGESEEEQESVDTGEEEEGGDESDLSSESSIKKKFLKRKGKTDSPWIKPARKRRRRSRKK
PSGALGSESYKSSAGSAEQTAPGDSTGYMEVSLDSLDLRVKGILSSQAEGLANGPDVLET
DGLQEVPLCSCRMETPKSREITTLANNQCMATESVDHELGRCTNSVVKYELMRPSNKAPL
LVLCEDHRGRMVKHQCCPGCGYFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCG
EESSKAKEVTIAKADTTSTVTPVPGQEKGSALEGRADTTTGSAAGPPLSEDDKLQGAASH
VPEGFDPTGPAGLGRPTPGLSQGPGKETLESALIALDSEKPKKLRFHPKQLYFSARQGEL
QKVLLMLVDGIDPNFKMEHQNKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLM
EAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQMDVNCQDD
GGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCD
LHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLNSQVWSALQM
SKALQDSAPDRPSPVERIVSRDIARGYERIPIPCVNAVDSEPCPSNYKYVSQNCVTSPMN
IDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSC
WRNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREED
SYLFDLDNKDGEVYCIDARFYGNVSRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRL
IEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHSSAALAQRQASAAQEAQEDGLPDTSS
AAAADPL

• Lysine Degradation (map00310 )

• S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine

• Ank (PF00023 )
• Pre-SET (PF05033 )
• SET (PF00856 )

• None

• None

ATGGCTGCCGATGAAGGCTCAGCAGAGAAACAGGCAGGAGAGGCCCACATGGCTGCGGAC
GGTGAGACCAATGGGTCTTGTGAAAACAGCGATGCCAGCAGTCATGCAAATGCTGCAAAG
CACACTCAGGACAGCGCAAGGGTCAACCCCCAGGATGGCACCAACACACTAACTCGGATA
GCGGAAAATGGGGTTTCAGAAAGAGACTCAGAAGCGGCGAAGCAAAACCACGTCACTGCC
GACGACTTTGTGCAGACTTCTGTCATCGGCAGCAACGGATACATCTTAAATAAGCCGGCC
CTACAGGCACAGCCCTTGAGGACTACCAGCACTCTGGCCTCTTCGCTGCCTGGCCATGCT
GCAAAAACCCTTCCTGGAGGGGCTGGCAAAGGCAGGACTCCAAGCGCTTTTCCCCAGACG
CCAGCCGCCCCACCAGCCACCCTTGGGGAGGGGAGTGCTGACACAGAGGACAGGAAGCTC
CCGGCCCCTGGCGCCGACGTCAAGGTCCACAGGGCACGCAAGACCATGCCGAAGTCCGTC
GTGGGCCTGCATGCAGCCAGTAAAGATCCCAGAGAAGTTCGAGAAGCTAGAGATCATAAG
GAACCAAAAGAGGAGATCAACAAAAACATTTCTGACTTTGGACGACAGCAGCTTTTACCC
CCCTTCCCATCCCTTCATCAGTCGCTACCTCAGAACCAGTGCTACATGGCCACCACAAAA
TCACAGACAGCTTGCTTGCCTTTTGTTTTAGCAGCTGCAGTATCTCGGAAGAAAAAACGA
AGAATGGGAACCTATAGCCTGGTTCCTAAGAAAAAGACCAAAGTATTAAAACAGAGGACG
GTGATTGAGATGTTTAAGAGCATAACTCATTCCACTGTGGGTTCCAAGGGGGAGAAGGAC
CTGGGCGCCAGCAGCCTGCACGTGAATGGGGAGAGCCTGGAGATGGACTCGGATGAGGAC
GACTCAGAGGAGCTCGAGGAGGACGACGGCCATGGTGCAGAGCAGGCGGCCGCGTTCCCC
ACAGAGGACAGCAGGACTTCCAAGGAGAGCATGTCGGAGGCTGATCGCGCCCAGAAGATG
GACGGGGAGTCCGAGGAGGAGCAGGAGTCCGTGGACACCGGGGAGGAGGAGGAAGGCGGT
GACGAGTCTGACCTGAGTTCGGAATCCAGCATTAAGAAGAAATTTCTCAAGAGGAAAGGA
AAGACCGACAGTCCCTGGATCAAGCCAGCCAGGAAAAGGAGGCGGAGAAGTAGAAAGAAG
CCCAGCGGTGCCCTCGGTTCTGAGTCGTATAAGTCATCTGCAGGAAGCGCTGAGCAGACG
GCACCAGGAGACAGCACAGGGTACATGGAAGTTTCTCTGGACTCCCTGGATCTCCGAGTC
AAAGGAATTCTGTCTTCACAAGCAGAAGGGTTGGCCAACGGTCCAGATGTGCTGGAGACA
GACGGCCTCCAGGAAGTGCCTCTCTGCAGCTGCCGGATGGAAACACCGAAGAGTCGAGAG
ATCACCACACTGGCCAACAACCAGTGCATGGCTACAGAGAGCGTGGACCATGAATTGGGC
CGGTGCACAAACAGCGTGGTCAAGTATGGGCTGATGCGCCCCTCCAACAAGGCCCCGCTC
CTCGTGCTGTGTGAAGACCACCGGGGCCGCATGGTGAAGCACCAGTGCTGTCCTGGCTGT
GGCTACTTCTGCACAGCGGGTAATTTTATGGAGTGTCAGCCCGAGAGCAGCATCTCTCAC
CGTTTCCACAAAGACTGTGCCTCTCGAGTCAATAACGCCAGCTATTGTCCCCACTGTGGG
GAGGAGAGCTCCAAGGCCAAAGAGGTGACGATAGCTAAAGCAGACACCACCTCGACCGTG
ACACCAGTCCCCGGGCAGGAGAAGGGCTCGGCCCTGGAGGGCAGGGCCGACACCACAACG
GGCAGTGCTGCCGGGCCACCACTCTCGGAGGACGACAAGCTGCAGGGTGCAGCCTCCCAC
GTGCCCGAGGGCTTTGATCCAACGGGACCTGCTGGGCTTGGGAGGCCAACTCCCGGCCTT
TCCCAGGGACCAGGGAAGGAAACCTTGGAGAGCGCTCTCATCGCCCTCGACTCGGAAAAA
CCCAAGAAGCTTCGCTTCCACCCAAAGCAGCTGTACTTCTCCGCCAGGCAAGGGGAGCTT
CAGAAGGTGCTCCTCATGCTGGTGGACGGAATTGACCCCAACTTCAAAATGGAGCACCAG
AATAAGCGCTCTCCACTGCACGCCGCGGCAGAGGCTGGACACGTGGACATCTGCCACATG
CTGGTTCAGGCGGGCGCTAATATTGACACCTGCTCAGAAGACCAGAGGACCCCGTTGATG
GAAGCAGCCGAAAACAACCATCTGGAAGCAGTGAAGTACCTCATCAAGGCTGGGGCCCTG
GTGGATCCCAAGGACGCAGAGGGCTCTACGTGTTTGCACCTGGCTGCCAAGAAAGGCCAC
TACGAAGTGGTCCAGTACCTGCTTTCGAATGGACAGATGGACGTCAACTGTCAGGATGAC
GGAGGCTGGACACCCATGATCTGGGCCACAGAGTACAAGCACGTGGACCTCGTGAAGCTG
CTGCTGTCCAAGGGCTCTGACATCAACATCCGAGACAACGAGGAGAACATTTGCCTGCAC
TGGGCGGCGTTCTCCGGCTGCGTGGACATAGCCGAGATCCTGCTGGCTGCCAAGTGCGAC
CTCCACGCCGTGAACATCCACGGAGACTCGCCACTGCACATTGCCGCCCGGGAGAACCGC
TACGACTGTGTCGTCCTCTTTCTTTCTCGGGATTCAGATGTCACCTTAAAGAACAAGGAA
GGAGAGACGCCCCTGCAGTGTGCGAGCCTCAACTCTCAGGTGTGGAGCGCTCTGCAGATG
AGCAAGGCTCTGCAGGACTCGGCCCCCGACAGGCCCAGCCCCGTGGAGAGGATAGTGAGC
AGGGACATCGCTCGAGGCTACGAGCGCATCCCCATCCCCTGTGTCAACGCCGTAGACAGC
GAGCCATGCCCCAGCAACTACAAGTACGTCTCTCAGAACTGCGTGACGTCCCCCATGAAC
ATCGACAGAAATATCACTCATCTGCAGTACTGCGTGTGCATCGACGACTGCTCCTCCAGC
AACTGCATGTGCGGCCAGCTCAGCATGCGCTGCTGGTACGACAAGGATGGCCGGCTCCTG
CCAGAGTTCAACATGGCGGAGCCTCCCTTGATCTTCGAATGCAACCACGCGTGCTCCTGC
TGGAGGAACTGCCGAAATCGCGTCGTACAGAATGGTCTCAGGGCAAGGCTGCAGCTCTAC
CGGACGCGGGACATGGGCTGGGGCGTGCGGTCCCTGCAGGACATCCCACCAGGCACCTTT
GTCTGCGAGTATGTTGGGGAGCTGATTTCAGACTCAGAAGCCGACGTTCGAGAGGAAGAT
TCTTACCTCTTTGATCTCGACAATAAGGACGGGGAGGTTTACTGCATCGACGCGCGGTTC
TACGGGAACGTCAGCCGGTTCATCAACCACCACTGCGAGCCCAACCTGGTGCCCGTGCGC
GTGTTCATGGCCCACCAGGACCTGCGGTTCCCCCGGATCGCCTTCTTCAGCACCCGCCTG
ATCGAGGCCGGCGAGCAGCTCGGGTTTGACTATGGAGAGCGCTTCTGGGACATCAAAGGC
AAGCTCTTCAGCTGCCGCTGCGGCTCCCCCAAGTGCCGGCACTCGAGCGCGGCCCTGGCC
CAGCGTCAGGCCAGCGCGGCCCAGGAGGCCCAGGAGGACGGCTTGCCCGACACCAGCTCC
GCGGCTGCCGCCGACCCCCTATGA

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 ]
2. Nagase T, Nakayama M, Nakajima D, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2001 Apr 27;8(2):85-95. [PubMed ]
3. 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 ]

MSAPSATPIFAPGENCSPAWGAAPAAYDAADTHLRILGKPVMERWETPYMHALAAAASSK
GGRVLEVGFGMAIAASKVQEAPIDEHWIIECNDGVFQRLRDWAPRQTHKVIPLKGLWEDV
APTLPDGHFDGILYDTYPLSEETWHTHQFNFIKNHAFRLLKPGGVLTYCNLTSWGELMKS
KYSDITIMFEETQVPALLEAGFRRENIRTEVMALVPPADCRYYAFPQMITPLVTKG

• Arginine and Proline Metabolism (map00330 )
• Glycine, Serine and Threonine Metabolism (map00260 )

• S-adenosyl-L-methionine + guanidinoacetate = S-adenosyl-L-homocysteine + creatine

• None

• None

ATGAGCGCCCCCAGCGCGACCCCCATCTTCGCGCCCGGCGAGAACTGCAGCCCCGCGTGG
GGGGCGGCGCCCGCGGCCTACGACGCAGCGGACACGCACCTGCGCATCCTGGGCAAGCCG
GTGATGGAGCGCTGGGAGACCCCCTATATGCACGCGCTGGCCGCCGCCGCCTCCTCCAAA
GGGGGCCGGGTCCTGGAGGTGGGCTTTGGCATGGCCATCGCAGCGTCAAAGGTGCAGGAG
GCGCCCATTGATGAGCATTGGATCATCGAGTGCAATGACGGCGTCTTCCAGCGGCTCCGG
GACTGGGCCCCACGGCAGACACACAAGGTCATCCCCTTGAAAGGCCTGTGGGAGGATGTG
GCACCCACCCTGCCTGACGGTCACTTTGATGGGATCCTGTACGACACGTACCCACTCTCG
GAGGAGACCTGGCACACACACCAGTTCAACTTCATCAAGAACCACGCCTTTCGCCTGCTG
AAGCCGGGGGGCGTCCTCACCTACTGCAACCTCACCTCCTGGGGGGAGCTGATGAAGTCC
AAGTACTCAGACATCACCATCATGTTTGAGGAGACGCAGGTGCCCGCGCTGCTGGAGGCC
GGCTTCCGGAGGGAGAACATCCGTACGGAGGTGATGGCGCTGGTCCCACCGGCCGACTGC
CGCTACTACGCCTTCCCACAGATGATCACGCCCCTGGTGACCAAAGGCTGA

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 ]
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 ]

1. HMT

MASSMRSLFSDHGKYVESFRRFLNHSTEHQCMQEFMDKKLPGIIGRIGDTKSEIKILSIG
GGAGEIDLQILSKVQAQYPGVCINNEVVEPSAEQIAKYKELVAKTSNLENVKFAWHKETS
SEYQSRMLEKKELQKWDFIHMIQMLYYVKDIPATLKFFHSLLGTNAKMLIIVVSGSSGWD
KLWKKYGSRFPQDDLCQYITSDDLTQMLDNLGLKYECYDLLSTMDISDCFIDGNENGDLL
WDFLTETCNFNATAPPDLRAELGKDLQEPEFSAKKEGKVLFNNTLSFIVIEA

• Histidine Metabolism (map00340 )

• S-adenosyl-L-methionine + histamine = S-adenosyl-L-homocysteine + N(tau)-methylhistamine

• None

• None

ATGGCATCTTCCATGAGGAGCTTGTTTTCTGACCACGGGAAATATGTTGAATCTTTCCGG
AGGTTTCTCAACCATTCCACGGAACACCAGTGCATGCAGGAATTCATGGACAAGAAGCTG
CCAGGCATAATAGGAAGGATTGGAGACACAAAATCAGAAATTAAGATTCTAAGCATAGGC
GGAGGTGCAGGTGAAATTGATCTTCAAATTCTCTCCAAAGTTCAGGCTCAATACCCAGGA
GTTTGTATCAACAATGAAGTTGTTGAGCCAAGTGCTGAACAAATTGCCAAATACAAAGAG
CTTGTAGCCAAGACATCGAACCTCGAGAACGTAAAGTTTGCTTGGCATAAGGAGACATCA
TCTGAATACCAAAGTAGAATGTTGGAGAAAAAGGAGCTTCAAAAGTGGGACTTTATTCAT
ATGATTCAAATGCTGTATTATGTAAAAGACATCCCAGCTACCCTGAAATTCTTCCATAGT
CTCTTAGGTACCAATGCTAAGATGCTCATTATTGTTGTGTCAGGAAGCAGTGGCTGGGAC
AAGCTGTGGAAAAAGTACGGATCACGCTTTCCCCAGGATGACCTCTGCCAGTATGTCACA
TCAGATGACCTCACTCAGATGCTGGACAACCTAGGGCTTAAGTATGAGTGCTATGACCTT
TTGTCCACCATGGATATATCTGACTGCTTTATTGATGGTAATGAAAATGGAGACCTGCTT
TGGGATTTTTTGACTGAAACCTGCAACTTTAATGCCACAGCACCACCTGATCTCAGAGCA
GAGCTTGGGAAAGATCTACAAGAGCCTGAATTTAGTGCTAAGAAAGAGGGGAAGGTTCTT
TTTAATAATACTCTGAGTTTCATAGTGATTGAGGCATAA

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 ]
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 ]
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 ]
4. 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 ]
5. 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 ]

1. Thiopurine methyltransferase

MDGTRTSLDIEEYSDTEVQKNQVLTLEEWQDKWVNGKTAFHQEQGHQLLKKHLDTFLKGK
SGLRVFFPLCGKAVEMKWFADRGHSVVGVEISELGIQEFFTEQNLSYSEEPITEIPGTKV
FKSSSGNISLYCCSIFDLPRTNIGKFDMIWDRGALVAINPGDRKCYADTMFSLLGKKFQY
LLCVLSYDPTKHPGPPFYVPHAEIERLFGKICNIRCLEKVDAFEERHKSWGIDCLFEKLY
LLTEK

• S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether

• TPMT (PF05724 )

• None

• None

ATGGATGGTACAAGAACTTCACTTGACATTGAAGAGTACTCGGATACTGAGGTACAGAAA
AACCAAGTACTAACTCTGGAAGAATGGCAAGACAAGTGGGTGAACGGCAAGACTGCTTTT
CATCAGGAACAAGGACATCAGCTATTAAAGAAGCATTTAGATACTTTCCTTAAAGGCAAG
AGTGGACTGAGGGTATTTTTTCCTCTTTGCGGAAAAGCGGTTGAGATGAAATGGTTTGCA
GACCGGGGACACAGTGTAGTTGGTGTGGAAATCAGTGAACTTGGGATACAAGAATTTTTT
ACAGAGCAGAATCTTTCTTACTCAGAAGAACCAATCACCGAAATTCCTGGAACCAAAGTA
TTTAAGAGTTCTTCGGGGAACATTTCATTGTACTGTTGCAGTATTTTTGATCTTCCCAGG
ACAAATATTGGCAAATTTGACATGATTTGGGATAGAGGAGCATTAGTTGCCATTAATCCA
GGTGATCGCAAATGCTATGCAGATACAATGTTTTCCCTCCTGGGAAAGAAGTTTCAGTAT
CTCCTGTGTGTTCTTTCTTATGATCCAACTAAACATCCAGGTCCACCATTTTATGTTCCA
CATGCTGAAATTGAAAGGTTGTTTGGTAAAATATGCAATATACGTTGTCTTGAGAAGGTT
GATGCTTTTGAAGAACGACATAAAAGTTGGGGAATTGACTGTCTTTTTGAAAAGTTATAT
CTACTTACAGAAAAGTAA

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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
7. Spire-Vayron de la Moureyre C, Debuysere H, Sabbagh N, Marez D, Vinner E, Chevalier ED, Lo Guidice JM, Broly F: Detection of known and new mutations in the thiopurine S-methyltransferase gene by single-strand conformation polymorphism analysis. Hum Mutat. 1998;12(3):177-85. [PubMed ]
8. Krynetski EY, Schuetz JD, Galpin AJ, Pui CH, Relling MV, Evans WE: A single point mutation leading to loss of catalytic activity in human thiopurine S-methyltransferase. Proc Natl Acad Sci U S A. 1995 Feb 14;92(4):949-53. [PubMed ]
9. Tai HL, Krynetski EY, Yates CR, Loennechen T, Fessing MY, Krynetskaia NF, Evans WE: Thiopurine S-methyltransferase deficiency: two nucleotide transitions define the most prevalent mutant allele associated with loss of catalytic activity in Caucasians. Am J Hum Genet. 1996 Apr;58(4):694-702. [PubMed ]
10. Hon YY, Fessing MY, Pui CH, Relling MV, Krynetski EY, Evans WE: Polymorphism of the thiopurine S-methyltransferase gene in African-Americans. Hum Mol Genet. 1999 Feb;8(2):371-6. [PubMed ]

1. MT-A70
2. Methyltransferase-like protein 3

MSDTWSSIQAHKKQLDSLRERLQRRRKQDSGHLDLRNPEAALSPTFRSDSPVPTAPTSGG
PKPSTASAVPELATDPELEKKLLHHLSDLALTLPTDAVSICLAISTPDAPATQDGVESLL
QKFAAQELIEVKRGLLQDDAHPTLVTYADHSKLSAMMGAVAEKKGPGEVAGTVTGQKRRA
EQDSTTVAAFASSLVSGLNSSASEPAKEPAKKSRKHAASDVDLEIESLLNQQSTKEQQSK
KVSQEILELLNTTTAKEQSIVEKFRSRGRAQVQEFCDYGTKEECMKASDADRPCRKLHFR
RIINKHTDESLGDCSFLNTCFHMDTCKYVHYEIDACMDSEAPGSKDHTPSQELALTQSVG
GDSSADRLFPPQWICCDIRYLDVSILGKFAVVMADPPWDIHMELPYGTLTDDEMRRLNIP
VLQDDGFLFLWVTGRAMELGRECLNLWGYERVDEIIWVKTNQLQRIIRTGRTGHWLNHGK
EHCLVGVKGNPQGFNQGLDCDVIVAEVRSTSHKPDEIYGMIERLSPGTRKIELFGRPHNV
QPNWITLGNQLDGIHLLDPDVVARFKQRYPDGIISKPKNL

• S-adenosyl-L-methionine + m7G(5')pppAm = S-adenosyl-L-homocysteine + m7G(5')pppm6Am (mRNA containing an N6,2'-O-dimethyladenosine cap)

• MT-A70 (PF05063 )

• None

• None

ATGTCGGACACGTGGAGCTCTATCCAGGCCCACAAGAAGCAGCTGGACTCTCTGCGGGAG
AGGCTGCAGCGGAGGCGGAAGCAGGACTCGGGGCACTTGGATCTACGGAATCCAGAGGCA
GCATTGTCTCCAACCTTCCGTAGTGACAGCCCAGTGCCTACTGCACCCACCTCTGGTGGC
CCTAAGCCCAGCACAGCTTCAGCAGTTCCTGAATTAGCTACAGATCCTGAGTTAGAGAAG
AAGTTGCTACACCACCTCTCTGATCTGGCCTTAACATTGCCCACTGATGCTGTGTCCATC
TGTCTTGCCATCTCCACGCCAGATGCTCCTGCCACTCAAGATGGGGTAGAAAGCCTCCTG
CAGAAGTTTGCAGCTCAGGAGTTGATTGAGGTAAAGCGAGGTCTCCTACAAGATGATGCA
CATCCTACTCTTGTAACCTATGCTGACCATTCCAAGCTCTCTGCCATGATGGGTGCTGTG
GCAGAAAAGAAGGGCCCTGGGGAGGTAGCAGGGACTGTCACAGGGCAGAAGCGGCGTGCA
GAACAGGACTCGACTACAGTAGCTGCCTTTGCCAGTTCGTTAGTCTCTGGTCTGAACTCT
TCAGCATCGGAACCAGCAAAGGAGCCAGCCAAGAAATCAAGGAAACATGCTGCCTCAGAT
GTTGATCTGGAGATAGAGAGCCTTCTGAACCAACAGTCCACTAAGGAACAACAGAGCAAG
AAGGTCAGTCAGGAGATCCTAGAGCTATTAATTACTACAACAGCCAAGGAACAATCCATT
GTTGAAATTCGCTCTCGAGGTCGGGCCCAAGTGCAAGAATTCTGTGACTATGGAACCAAG
GAGGAGTGCATGAAAGCCAGTGATGCTGATCGACCCTGTCGCAAGCTGCACTTCAGACGA
ATTATCAATAAACACACTGATGAGTCTTTAGGTGACTGCTCTTTCCTTAATACATGTTTC
CACATGGATACCTGCAAGTATGTTCACTATGAAATTGATGCTTGCATGGATTCTGAGGCC
CCTGGCAGCAAAGACCACACGCCAAGCCAGGAGCTTGCTCTTACACAGAGTGTCGGAGGT
GATTCCAGTGCAGACCGACTCTTCCCACCTCAGTGGATCTGTTGTGATATCCGCTACCTG
GTCGTCAGTATCTTGGGCAAGTTTGCAGTTGTGATGGCTGACCCACCCTGGGATATTCAC
ATGGAACTGCCCTATGGGACCCTGACAGATGATGAGATGCGCAGGCTCAACATACCCGTA
CTACAGGATGATGGCTTTCTCTTCCTCTGGGTCACAGGCAGGGCCATGGAGTTGGGGAGA
GAATGTCTAAACCTCTGGGGGTATGAACGGGTAGATGAAATTATTTGGGTGAAGACAAAT
CAACTGCAACGCATCATTCGGACAGGCCGTACAGGTCACTGGTTGAACCATGGGAAGGAA
CACTGCTTGGTTGGTGTCAAAGGAAATCCCCAAGGCTTCAACCAGGGTCTGGATTGTGAT
GTGATCGTAGCTGAGGTTCGTTCCACCAGTCATAAACCAGATGAAATCTATGGCATGATT
GAAAGACTATCTCCTGGCACTCGCAAGATTGAGTTATTTGGACGACCACACAATGTGCAA
CCCAACTGGATCACCCTTGGAAACCAACTGGATGGGATCCACCTACTAGACCCAGATGTG
GTTGCACGGTTCAAGCAAAGGTACCCAGATGGTATCATCTCTAAACCTAAGAATTTATAG

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 ]
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 ]

1. S-adenosyl-L- homocysteine hydrolase 3
2. AdoHcyase 3

MSVQVVSAAAAAKVPEVELKDLSPSEAESQLGLSTAAVGAMAPPAGGGDPEAPAPAAERP
PVPGPGSGPAAALSPAAGKVPQASAMKRSDPHHQHQRHRDGGEALVSPDGTVTEAPRTVK
KQIQFADQKQEFNKRPTKIGRRSLSRSISQSSTDSYSSAASYTDSSDDETSPRDKQQKNS
KGSSDFCVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTA
VLMETLGALGAQCRWAACNIYSTLNEVAAALAESGFPVFAWKGESEDDFWWCIDRCVNVE
GWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVN
DSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYV
TEIDPICALQACMDGFRLVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGH
SNTEIDVASLRTPELTWERVRSQVDHVIWPDGKRIVLLAEGRLLNLSCSTVPTFVLSITA
TTQALALIELYNAPEGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQAKYLGLNK
NGPFKPNYYRY

• Methionine Metabolism (map00271 )
• Selenoamino Acid Metabolism (map00450 )

• S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine

• AdoHcyase (PF05221 )
• AdoHcyase_NAD (PF00670 )

• None

• None

GAGCCGGTGGTTGCAGCGGAGGCGGTGATGTCGGTGCAGGTTGTGTCAGCCGCGGCTGCC
GCCAAGGTGCCTGAGGTGGAGCTGAAGGACCTGAGCCCCTCCGAGGCGGAGTCGCAACTA
GGACTGAGCACGGCCGCCGTGGGCGCCATGGCCCCCCCGGCGGGCGGTGGAGACCCTGAG
GCTCCAGCTCCCGCCGCGGAGCGGCCCCCGGTCCCCGGCCCGGGCTCGGGGCCCGCCGCC
GCTCTCAGCCCCGCCGCCGGGAAGGTGCCTCAGGCGTCGGCCATGAAGCGGAGCGACCCA
CATCACCAGCACCAGCGGCACCGCGACGGCGGCGAGGCCCTGGTCAGCCCCGACGGCACC
GTCACCGAGGCGCCGCGCACAGTCAAGAAGATCCAGTTTGCTGACCAGAAGCAAGAATTC
AACAAACGTCCCACCAAAATTGGACGTCGCTCTTTGTCTCGTTCCATTTCTCAGTCATCT
ACTGACAGCTACAGCTCAGCGGCTTCATATACAGATAGCTCTGATGATGAGACATCGCCC
AGGGACAAGCAGCAAAAGAACTCTAAGGGAAGCAGTGACTTCTGTGTTAAGAACATCAAA
CAGGCAGAGTTTGGACGAAGAGAAATTGAAATTGCTGAACAAGAAATGCCTGCATTGATG
GCTTTGAGGAAGAGAGCTCAAGGAGAAAAGCCTTTGGCTGGAGCCAAAATCGTGGGTTGC
ACACACATCACTGCTCAGACTGCTGTGCTTATGGAAACTCTGGGTGCTCTGGGGGCCCAG
TGCCGATGGGCTGCCTGCAACATCTATTCCACTCTCAATGAAGTGGCTGCTGCTCTAGCA
GAAAGTGGATTTCCTGTTTTTGCCTGGAAGGGAGAGTCAGAAGATGACTTTTGGTGGTGT
ATCGATAGATGTGTGAATGTGGAGGGCTGGCAGCCAAACATGATCTTGGATGATGGAGGG
GATCTTACCCACTGGATTTATAAAAAGTATCCCAACATGTTTAAGAAAATCAAGGGCATA
GTAGAGGAGAGTGTTACTGGAGTTCACAGGCTGTACCAACTGTCCAAAGCTGGGAAGCTG
TGTGTTCCAGCCATGAATGTCAATGACTCAGTCACCAAACAGAAATTTGACAACCTCTAC
TGTTGCCGTGAATCAATTCTTGATGGACTTAAAAGGACAACAGACATGATGTTTGGTGGA
AAGCAAGTGGTAGTCTGTGGCTATGGAGAGGTGGGGAAAGGGTGCTGTGCTGCCCTGAAA
GCCATGGGCTCCATTGTGTATGTAACTGAAATTGACCCCATCTGTGCCCTGCAAGCCTGT
ATGGATGGATTTCGACTGGTGAAATTAAATGAGGTCATCCGACAAGTGGACATTGTTATT
ACCTGTACAGGTAACAAGAATGTGGTAACCAGAGAGCACTTGGACCGTATGAAGAATAGC
TGCATCGTTTGTAACATGGGACATTCCAACACAGAGATTGACGTGGCGAGTCTGCGGACA
CCAGAACTGACCTGGGAGCGAGTGAGATCTCAAGTTGACCATGTGATATGGCCTGATGGC
AAGAGGATAGTACTGCTGGCAGAGGGCCGCCTGCTGAACCTTAGCTGCTCCACAGTGCCT
ACATTTGTGCTCTCAATCACTGCTACTACTCAGGCTCTTGCCTTGATAGAGCTTTACAAT
GCTCCTGAGGGTCGCTATAAGCAGGATGTCTACCTGTTGCCCAAGAAGATGGATGAGTAT
GTGGCCAGCCTACACCTGCCTACCTTTGATGCCCACTTGACAGAGCTGACAGATGAACAG
GCCAAGTATCTGGGACTCAACAAGAATGGGCCCTTCAAGCCTAATTACTACAGGTATTAA

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 ]

1. S-adenosyl-L-homocysteine hydrolase
2. AdoHcyase

MSDKLPYKVADIGLAAWGRKALDIAENEMPGLMRMRERYSASKPLKGARIAGCLHMTVET
AVLIETLVTLGAEVQWSSCNIFSTQDHAAAAIAKAGIPVYAWKGETDEEYLWCIEQTLYF
KDGPLNMILDDGGDLTNLIHTKYPQLLPGIRGISEETTTGVHNLYKMMANGILKVPAINV
NDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVI
ITEIDPINALQAAMEGYEVTTMDEACQEGNIFVTTTGCIDIILGRHFEQMKDDAIVCNIG
HFDVEIDVKWLNENAVEKVNIKPQVDRYRLKNGRRIILLAEGRLVNLGCAMGHPSFVMSN
SFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVAEAHLGKLNVKLTKLTEKQAQYLGMS
CDGPFKPDHYRY

• Methionine Metabolism (map00271 )
• Selenoamino Acid Metabolism (map00450 )

• S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine

• AdoHcyase (PF05221 )
• AdoHcyase_NAD (PF00670 )

• None

• None

ATGTCTGACAAACTGCCCTACAAAGTCGCCGACATCGGCCTGGCTGCCTGGGGACGCAAG
GCCCTGGACATTGCTGAGAACGAGATGCCGGGCCTGATGCGTATGCGGGAGCGGTACTCG
GCCTCCAAGCCACTGAAGGGCGCCCGCATCGCTGGCTGCCTGCACATGACCGTGGAGACG
GCCGTCCTCATTGAGACCCTCGTCACCCTGGGTGCTGAGGTGCAGTGGTCCAGCTGCAAC
ATCTTCTCCACCCAGAACCATGCGGCGGCTGCCATTGCCAAGGCTGGCATTCCGGTGTAT
GCCTGGAAGGGCGAAACGGACGAGGAGTACCTGTGGTGCATTGAGCAGACCCTGTACTTC
AAGGACGGGCCCCTCAACATGATTCTGGACGACGGGGGCGACCTCACCAACCTCATCCAC
ACCAAGTACCCGCAGCTTCTGCCAGGCATCCGAGGCATCTCTGAGGAGACCACGACTGGG
GTCCACAACCTCTACAAGATGATGGCCAATGGGATCCTCAAGGTGCCTGCCATCAATGTC
AATGACTCCGTCACCAAGAGCAAGTTTGACAACCTCTATGGCTGCCGGGAGTCCCTCATA
GATGGCATCAAGCGGGCCACAGATGTGATGATTGCCGGCAAGGTAGCGGTGGTAGCAGGC
TATGGTGATGTGGGCAAGGGCTGTGCCCAGGCCCTGCGGGGTTTCGGAGCCCGCGTCATC
ATCACCGAGATTGACCCCATCAACGCACTGCAGGCTGCCATGGAGGGCTATGAGGTGACC
ACCATGGATGAGGCCTGTCAGGAGGGCAACATCTTTGTCACCACCACAGGCTGTATTGAC
ATCATCCTTGGCCGGCACTTTGAGCAGATGAAGGATGATGCCATTGTGTGTAACATTGGA
CACTTTGACGTGGAGATCGATGTCAAGTGGCTCAACGAGAACGCCGTGGAGAAGGTGAAC
ATCAAGCCGCAGGTGGACCGGTATCGGTTGAAGAATGGGCGCCGCATCATCCTGCTGGCC
GAGGGTCGGCTGGTCAACCTGGGTTGTGCCATGGGCCACCCCAGCTTCGTGATGAGTAAC
TCCTTCACCAACCAGGTGATGGCGCAGATCGAGCTGTGGACCCATCCAGACAAGTACCCC
GTTGGGGTTCATTTCCTGCCCAAGAAGCTGGATGAGGCAGTGGCTGAAGCCCACCTGGGC
AAGCTGAATGTGAAGTTGACCAAGCTAACTGAGAAGCAAGCCCAGTACCTGGGCATGTCC
TGTGATGGCCCCTTCAAGCCGGATCACTACCGCTACTGA

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 ]
2. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed ]
3. Turner MA, Yuan CS, Borchardt RT, Hershfield MS, Smith GD, Howell PL: Structure determination of selenomethionyl S-adenosylhomocysteine hydrolase using data at a single wavelength. Nat Struct Biol. 1998 May;5(5):369-76. [PubMed ]

1. S-adenosyl-L- homocysteine hydrolase 2
2. AdoHcyase 2
3. S-adenosylhomocysteine hydrolase-like 1
4. DC-expressed AHCY-like molecule

MSMPDAMPLPGVGEELKQAKEIEDAEKYSFMATVTKAPKKQIQFADDMQEFTKFPTKTGR
RSLSRSISQSSTDSYSSAASYTDSSDDEVSPREKQQTNSKGSSNFCVKNIKQAEFGRREI
EIAEQDMSALISLRKRAQGEKPLAGAKIVGCTHITAQTAVLIETLCALGAQCRWSACNIY
STQNEVAAALAEAGVAVFAWKGESEDDFWWCIDRCVNMDGWQANMILDDGGDLTHWVYKK
YPNVFKKIRGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDG
LKRTTDVMFGGKQVVVCGYGEVGKGCCAALKALGAIVYITEIDPICALQACMDGFRVVKL
NEVIRQVDVVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVTSLRTPELTWERVR
SQVDHVIWPDGKRVVLLAEGRLLNLSCSTVPTFVLSITATTQALALIELYNAPEGRYKQD
VYLLPKKMDEYVASLHLPSFDAHLTELTDDQAKYLGLNKNGPFKPNYYRY

• Methionine Metabolism (map00271 )
• Selenoamino Acid Metabolism (map00450 )

• S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine

• AdoHcyase (PF05221 )
• AdoHcyase_NAD (PF00670 )

• None

• None

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

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 ]

1. Serine sulfhydrase
2. Beta- thionase

MPSETPQAEVGPTGCPHRSGPHSAKGSLEKGSPEDKEAKEPLWIRPDAPSRCTWQLGRPA
SESPHHHTAPAKSPKILPDILKKIGDTPMVRINKIGKKFGLKCELLAKCEFFNAGGSVKD
RISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDV
LRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEI
LQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILAEPEELNQTEQTT
YEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKA
AQELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKEEDLTEKKPWWWHLRVQELGLS
APLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVG
KVIYKQFKQIRLTDTLGRLSHILEMDHFALVVHEQIQYHSTGKSSQRQMVFGVVTAIDLL
NFVAAQERDQK

• Glycine, Serine and Threonine Metabolism (map00260 )
• Methionine Metabolism (map00271 )
• Selenoamino Acid Metabolism (map00450 )

• L-serine + L-homocysteine = cystathionine + H2O

• CBS (PF00571 )
• PALP (PF00291 )

• None

• None

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

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 ]
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 ]
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 ]
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 ]
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 ]
6. 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 ]
7. 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 ]
8. 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 ]
9. 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 ]
10. 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 ]
11. 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 ]
12. 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 ]
13. 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 ]
14. 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 ]
15. Kraus JP: Komrower Lecture. Molecular basis of phenotype expression in homocystinuria. J Inherit Metab Dis. 1994;17(4):383-90. [PubMed ]
16. 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 ]
17. 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 ]
18. 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 ]
19. 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 ]
20. 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 ]
21. 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 ]
22. 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 ]
23. 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 ]
24. 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 ]
25. 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 ]
26. 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 ]
27. 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 ]

1. Lip-syn
2. Lipoate synthase

MSLRCGDAARTLGPRVFGRYFCSPVRPLSSLPDKKKELLQNGPDLQDFVSGDLADRSTWD
EYKGNLKRQKGERLRLPPWLKTEIPMGKNYNKLKNTLRNLNLHTVCEEARCPNIGECWGG
GEYATATATIMLMGDTCTRGCRFCSVKTARNPPPLDASEPYNTAKAIAEWGLDYVVLTSV
DRDDMPDGGAEHIAKTVSYLKERNPKILVECLTPDFRGDLKAIEKVALSGLDVYAHNVET
VPELQSKVRDPRVNFDQSLRVLKHAKKVQPDVISKTSIMLGLGENDEQVYATMKALREAD
VDCLTLGQYMQPTRRHLKVEEYITPEKFKYWEKVGNELGFHYTASGPLVRSSYKAGEFFL
KNLVAKRKTKDL

• Radical_SAM (PF04055 )

• None

• None

ATGTCTCTACGCTGCGGGGATGCAGCCCGCACCCTGGGGCCCCGGGTATTTGGGAGATAT
TTTTGCAGCCCAGTCAGACCGTTAAGCTCCTTGCCAGATAAAAAAAAGGAACTCCTACAG
AATGGACCAGACCTTCAAGATTTTGTATCTGGTGATCTTGCAGACAGGAGCACCTGGGAT
GAATATAAAGGAAACCTAAAACGCCAGAAAGGAGAAAGGTTAAGACTACCTCCATGGCTA
AAGACAGAGATTCCCATGGGGAAAAATTACAATAAACTGAAAAATACTTTGCGGAATTTA
AATCTCCATACAGTATGTGAGGAAGCTCGATGTCCCAATATTGGAGAGTGTTGGGGAGGT
GGAGAATATGCCACCGCCACAGCCACGATCATGTTGATGGGTGACACATGTACAAGAGGT
TGCAGATTTTGTTCTGTTAAGACTGCAAGAAATCCTCCTCCACTGGATGCCAGTGAGCCC
TACAATACTGCAAAGGCAATTGCAGAATGGGGTCTGGATTATGTTGTCCTGACATCTGTG
GATCGAGATGATATGCCTGATGGGGGAGCTGAACACATTGCAAAGACCGTATCATATTTA
AAGGAAAGGAATCCAAAAATCCTTGTGGAGTGTCTTACTCCTGATTTTCGAGGTGATCTC
AAAGCAATAGAAAAAGTTGCTCTGTCAGGATTAGATGTGTATGCACATAATGTAGAAACA
GTCCCGGAATTACAGAGTAAGGTTCGTGATCCTCGGGTCAATTTTGATCAGTCCCTACGT
GTACTGAAACATGCCAAGAAGGTTCAGCCTGATGTTATTTCTAAAACATCTATAATGTTG
GGTTTAGGCGAGAATGATGAGCAAGTATATGCAACAATGAAAGCACTTCGTGAGGCAGAT
GTAGACTGCTTGACTTTAGGACAATATATGCAGCCAACAAGGCGTCACCTTAAGGTTGAA
GAATATATTACTCCTGAAAAATTCAAATACTGGGAAAAAGTAGGAAATGAACTTGGATTT
CATTATACTGCAAGTGGCCCTTTGGTGCGTTCTTCATATAAAGCAGGTGAATTTTTCCTG
AAAAATCTAGTGGCTAAAAGAAAAACAAAAGACCTCTAA

1. 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 ]

1. Shk1 kinase-binding protein 1 homolog
2. SKB1Hs
3. Jak-binding protein 1
4. 72 kDa ICln-binding protein

MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVAKQGFDFLCMPVFHPRFKREFIQEPAK
NRPGPQTRSDLLLSGRDWNTLIVGKLSPWIRPDSKVEKIRRNSEAAMLQELNFGAYLGLP
AFLLPLNQEDNTNLARVLTNHIHTGHHSSMFWMRVPLVAPEDLRDDIIENAPTTHTEEYS
GEEKTWMWWHNFRTLCDYSKRIAVALEIGADLPSNHVIDRWLGEPIKAAILPTSIFLTNK
KGFPVLSKMHQRLIFRLLKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELF
AKGYEDYLQSPLQPLMDNLESQTYEVFEKDPIKYSQYQQAIYKCLLDRVPEEEKDTNVQV
LMVLGAGRGPLVNASLRAAKQADRRIKLYAVEKNPNAVVTLENWQFEEWGSQVTVVSSDM
REWVAPEKADIIVSELLGSFADNELSPECLDGAQHFLKDDGVSIPGEYTSFLAPISSSKL
YNEVRACREKDRDPEAQFEMPYVVRLHNFHQLSAPQPCFTFSHPNRDPMIDNNRYCTLEF
PVEVNTVLHGFAGYFETVLYQDITLSIRPETHSPGMFSWFPILFPIKQPITVREGQTICV
RFWRCSNSKKVWYEWAVTAPVCSAIHNPTGRSYTIGL

• S-adenosyl-L-methionine + histone-arginine = S-adenosyl-L-homocysteine + histone-N(omega)-methyl-arginine

• PRMT5 (PF05185 )

• None

• None

ATGGCGGCGATGGCGGTCGGGGGTGCTGGTGGGAGCCGCGTGTCCAGCGGGAGGGACCTG
AATTGCGTCCCCGAAATAGCTGACACACTAGGGGCTGTGGCCAAGCAGGGGTTTGATTTC
CTCTGCATGCCTGTCTTCCATCCGCGTTTCAAGAGGGAGTTCATTCAGGAACCTGCTAAG
AATCGGCCCGGTCCCCAGACACGATCAGACCTACTGCTGTCAGGAAGGGACTGGAATACG
CTAATTGTGGGAAAGCTTTCTCCATGGATTCGTCCAGACTCAAAAGTGGAGAAAATTCGC
AGGAACTCCGAGGCGGCCATGTTACAGGAGCTGAATTTTGGTGCATATTTGGGTCTTCCA
GCTTTCCTGCTGCCCCTTAATCAGGAAGATAACACCAACCTGGCCAGAGTTTTGACCAAC
CACATCCACACTGGCCATCACTCTTCCATGTTCTGGATGCGGGTACCCTTGGTGGCACCA
GAGGACCTGAGAGATGATATAATTGAGAATGCACCAACTACACACACAGAGGAGTACAGT
GGGGAGGAGAAAACGTGGATGTGGTGGCACAACTTCCGGACTTTGTGTGACTATAGTAAG
AGGATTGCAGTGGCTCTTGAAATTGGGGCTGACCTCCCATCTAATCATGTCATTGATCGC
TGGCTTGGGGAGCCCATCAAAGCAGCCATTCTCCCCACTAGCATTTTCCTGACCAATAAG
AAGGGATTTCCTGTTCTTTTCAAGATGCACCAGAGGCTCATCTTCCGGCTCCTCAAGTTG
GAGGTGCAGTTCATCATCACAGGCACCAACCACCACTCAGAGAAGGAGTTCTGCTCCTAC
CTCCAATACCTGGAATACTTAAGCCAGAACCGTCCTCCACCTAATGCCTATGAACTCTTT
GCCAAGGGCTATGAAGACTATCTGCAGTCCCCGCTTCAGCCACTGATGGACAATCTGGAA
TCTCAGACATATGAAGTGTTTGAAAAGGACCCCATCAAATACTCTCAGTACCAGCAGGCC
ATCTATAAATGTCTGCTAGACCGAGTACCAGAAGAGGAGAAGGATACCAATGTCCAGGTA
CTGATGGTGCTGGGAGCAGGACGGGGACCCCTGGTGAACGCTTCCCTGCGGGCAGCCAAG
CAGGCCGACCGGCGGATAAAGCTGTATGCTGTGGAGAAAAACCCAAATGCCGTGGTGACG
CTAGAGAACTGGCAGTTTGAAGAATGGGGAAGCCAAGTGACCGTAGTCTCATCAGACATG
AGGGAATGGGTGGCTCCAGAGAAAGCAGACATCATTGTCAGTGAGCTTCTGGGCTCATTT
GCTGACAATGAATTGTCGCCTGAGTGCCTGGATGGAGCCCAGCACTTCCTAAAAGATGAT
GGTGTGAGCATCCCCGGGGAGTACACTTCCTTTCTGGCTCCCATCTCTTCCTCCAAGCTG
TACAATGAGGTCCGAGCCTGTAGGGAGAAGGACCGTGACCCTGAGGCCCAGTTTGAGATG
CCTTATGTGGTACGGCTGCACAACTTCCACCAGCTCTCTGCACCCCAGCCCTGTTTCACC
TTCAGCCATCCCAACAGAGATCCTATGATTGACAACAACCGCTATTGCACCTTGGAATTT
CCTGTGGAGGTGAACACAGTACTACATGGCTTTGCGGTCTACTTTGAGACTGTGCTTTAT
CAGGACATCACTCTGAGTATCCGTCCAGAGACTCACTCTCCTGGGATGTTCTCATGGTTT
CCCATCCTCTTCCCTATTAAGCAGCCCATAACGGTACGTGAAGGCCAAACCATCTGTGTG
CGTTTCTGGCGATGCAGCAATTCCAAGAAGGTGTGGTATGAGTGGGCTGTGACAGCACCA
GTCTGTTCTGCTATTCATAACCCCACAGGCCGCTCATATACCATTGGCCTCTAG