Showing drug card for Adenosine-5'-Diphosphate (DB03431)

• EXPT00436

• Experimental
• Small Molecule

1. Deoxycytidine kinase
2. Nucleoside kinase

1. FolC bifunctional protein [Includes: Folylpolyglutamate synthase
2. Glutamate dehydrogenase 1, mitochondrial
3. Glutathione synthetase
4. Apoptotic protease-activating factor 1
5. Riboflavin kinase
6. Mast/stem cell growth factor receptor
7. 3-hydroxy-3-methylglutaryl-coenzyme A reductase
8. Serine/threonine-protein kinase 6
9. Heat shock 70 kDa protein 1
10. Glycogen synthase kinase-3 beta
11. Hexokinase-1
12. Heat shock protein HSP 90-alpha
13. Thymidylate kinase
14. Dephospho-CoA kinase
15. Homoserine kinase
16. [3-methyl-2-oxobutanoate dehydrogenase [lipoamide]] kinase, mitochondrial
17. Protein recA
18. Adenylate kinase
19. UDP-N-acetylmuramoylalanine--D-glutamate ligase
20. Protein recA
21. Dethiobiotin synthetase
22. Pantothenate kinase
23. Uncharacterized protein YML087W
24. Nonsecretory ribonuclease
25. Glucose-1-phosphate adenylyltransferase small subunit, chloroplast
26. Myosin-2 heavy chain, non muscle
27. Ribonuclease pancreatic
28. MAP kinase-activated protein kinase 2
29. Amidophosphoribosyltransferase
30. Thymidine kinase
31. UPF0189 protein AF_1521
32. Chemotaxis protein cheA
33. 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
34. Nucleoside diphosphate kinase, cytosolic
35. Endoplasmin
36. Mono-ADP-ribosyltransferase C3
37. Uridine-cytidine kinase 2
38. S-adenosylmethionine synthetase
39. Holliday junction ATP-dependent DNA helicase ruvB
40. Sulfate adenylyltransferase
41. Phosphoribosylglycinamide formyltransferase 2
42. Nitrogenase iron protein 1
43. Acetylglutamate kinase
44. Glycerol kinase
45. Sarcoplasmic/endoplasmic reticulum calcium ATPase 1
46. Adenylyl-sulfate kinase
47. Inositol-trisphosphate 3-kinase A
48. Phosphoglycerate kinase, glycosomal
49. Myosin-11
50. S-adenosylmethionine synthetase isoform type-1
51. Protein claret segregational
52. Guanylate kinase
53. Kinesin-like protein KIF2C
54. Cytidylate kinase
55. Spliceosome RNA helicase Bat1
56. Probable branched-chain amino acid transport ATP-binding protein livG
57. ABC transporter ATP-binding protein MJ0796
58. Arginine kinase
59. Vanillyl-alcohol oxidase
60. Glutamate--cysteine ligase
61. Actin, alpha skeletal muscle
62. ATP-dependent molecular chaperone HSP82
63. Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase
64. Kinesin-like protein KIF11
65. Aminoglycoside 3'-phosphotransferase
66. Acetate kinase
67. Glutamine synthetase
68. Arsenical pump-driving ATPase
69. Hypothetical protein MG245 homolog
70. Thymidine kinase
71. Acetylglutamate kinase
72. Pyridoxal kinase
73. Ribokinase
74. ATP-dependent Clp protease ATP-binding subunit clpA
75. Inositol-tetrakisphosphate 1-kinase
76. Polynucleotide kinase
77. Riboflavin kinase/FMN adenylyltransferase
78. Adenylate kinase
79. Serine/threonine-protein kinase SKY1
80. Deoxycytidine kinase
81. NTPase P4
82. Phosphoenolpyruvate carboxykinase [ATP]
83. Cag-alfa
84. PMS1 protein homolog 2
85. DNA polymerase III subunit tau
86. Cystic fibrosis transmembrane conductance regulator
87. Trimethylamine dehydrogenase
88. Riboflavin kinase
89. Transcriptional regulator
90. Heat shock cognate 71 kDa protein
91. Phosphoribosylformylglycinamidine synthase
92. Kinesin-like protein KIF1A
93. Protein recA
94. DNA replication protein
95. FtsH
96. Activator of
97. Galactokinase
98. Inositol-trisphosphate 3-kinase A
99. Glutathione synthetase
100. ATP-dependent Clp protease ATP-binding subunit clpX
101. Focal adhesion kinase 1
102. RNase l inhibitor
103. Hypothetical protein APE0152
104. Transitional endoplasmic reticulum ATPase
105. Multidrug resistance ABC transporter ATP-binding and permease protein
106. Chromosomal replication initiator protein dnaA
107. Preprotein translocase subunit secA
108. Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 1
109. Lysine biosynthesis enzyme
110. Kinesin heavy chain
111. Plasmid segregation protein parM
112. 245aa long hypothetical cell division inhibitor MinD
113. D-alanine--D-alanine ligase B
114. Large T antigen
115. Kinesin heavy chain
116. ABC transporter, ATP binding protein
117. Signaling protein
118. Shikimate kinase
119. Phosphopantetheine adenylyltransferase
120. ATP-dependent hsl protease ATP-binding subunit hslU
121. Glycogen synthase 1
122. Putative partitioning protein
123. Shikimate kinase 2
124. Nucleoside diphosphate kinase A
125. 2-keto-3-deoxy-gluconate kinase
126. Cell division control protein 6
127. Kinesin-like protein KAR3
128. ADP-dependent glucokinase
129. D-alanine--D-alanine ligase
130. Antigen peptide transporter 1
131. Thymidine kinase
132. TrwB
133. Myosin II heavy chain
134. UPF0166 protein TM_0021
135. Phosphoribosylaminoimidazole carboxylase ATPase subunit
136. Replication factor C small subunit
137. Cell division inhibitor minD homolog
138. Preprotein translocase secA 1 subunit
139. Carbamate kinase
140. Thermosome subunit alpha
141. Myosin IE heavy chain
142. Kinesin-like protein KIF1A
143. Transient receptor potential cation channel subfamily M member 7
144. UPF0079 ATP-binding protein HI0065
145. Chaperone protein htpG
146. Kinesin heavy chain-like protein
147. [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 2, mitochondrial

MATPPKRSCPSFSASSEGTRIKKISIEGNIAAGKSTFVNILKQLCEDWEVVPEPVARWCN
VQSTQDEFEELTMSQKNGGNVLQMMYEKPERWSFTFQTYACLSRIRAQLASLNGKLKDAE
KPVLFFERSVYSDRYIFASNLYESECMNETEWTIYQDWHDWMNNQFGQSLELDGIIYLQA
TPETCLHRIYLRGRNEEQGIPLEYLEKLHYKHESWLLHRTLKTNFDYLQEVPILTLDVNE
DFKDKYESLVEKVKEFLSTL

MANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFMQASEDLLKEHYVDLKDRPF
FAGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVESAEKEIGLWFHPEELVDYTSCAQNWIYE

1. EC 6.3.2.17
2. FPGS
3. Folylpoly-gamma-glutamate synthetase
4. Tetrahydrofolate synthase

MIIKRTPQAASPLASWLSYLENLHSKTIDLGLERVSLVAARLGVLKPAPFVFTVAGTNGK
GTTCRTLESILMAAGYKVGVYSSPHLVRYTERVRVQGQELPESAHTASFAEIESARGDIS
LTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVTSIALDHTDWLGPD
RESIGREKAGIFRSEKPAIVGEPEMPSTIADVAQEKGALLQRRGVEWNYSVTDHDWAFSD
AHGTLENLPLPLVPQPNAATALAALRASGLEVSENAIRDGIASAILPGRFQIVSESPRVI
FDVAHNPHAAEYLTGRMKALPKNGRVLAVIGMLHDKDIAGTLAWLKSVVDDWYCAPLEGP
RGATAEQLLEHLGNGKSFDSVAQAWDAAMADAKAEDTVLVCGSFHTVAHVMEVIDARRSG
GK

• ATP + 7,8-dihydropteroate + L-glutamate = ADP + phosphate + 7,8-dihydropteroylglutamate

• Mur_ligase_C (PF02875 )
• Mur_ligase_M (PF08245 )

• None

• None

ATGATTATCAAACGCACTCCTCAAGCCGCGTCGCCTCTGGCTTCGTGGCTTTCTTATCTG
GAAAACCTGCACAGTAAAACTATCGATCTCGGCCTTGAGCGCGTGAGCCTGGTCGCGGCG
CGTCTTGGCGTCCTGAAACCAGCGCCATTTGTGTTTACCGTTGCGGGTACGAATGGCAAA
GGCACCACCTGCCGTACGCTGGAGTCGATTCTGATGGCGGCAGGGTACAAAGTGGGCGTC
TACAGTTCGCCTCATCTGGTGCGTTATACCGAGCGCGTACGTGTGCAGGGCCAGGAATTG
CCGGAATCGGCCCACACCGCCTCTTTTGCGGAGATTGAATCGGCACGCGGTGATATTTCC
CTGACCTATTTCGAGTACGGTACGCTGTCGGCGTTGTGGCTGTTCAAGCAGGCACAACTT
GACGTGGTGATTCTGGAAGTAGGGCTGGGCGGTCGTCTGGACGCAACCAATATTGTCGAC
GCCGATGTCGCGGTAGTAACCAGTATTGCGCTGGATCATACCGACTGGCTGGGTCCAGAT
CGCGAAAGTATTGGTCGCGAGAAAGCAGGCATCTTCCGCAGCGAAAAACCGGCAATTGTC
GGTGAGCCGGAAATGCCTTCTACCATTGCTGATGTGGCGCAGGAAAAAGGTGCACTGTTA
CAACGTCGGGGCGTTGAGTGGAACTATTCCGTCACCGATCATGACTGGGCGTTTAGCGAT
GCTCACGGCACGCTGGAAAATCTGCCGTTGCCGCTTGTCCCGCAACCGAATGCCGCAACA
GCGCTGGCGGCACTGCGTGCCAGCGGGCTGGAAGTCAGTGAAAATGCCATTCGCGACGGG
ATTGCCAGCGCAATTTTGCCGGGACGTTTCCAGATTGTGAGCGAGTCGCCACGCGTTATT
TTTGATGTCGCGCATAATCCACATGCGGCGGAATATCTCACCGGGCGTATGAAAGCGCTA
CCGAAAAACGGGCGCATGCTGGCGGTTATCGGTATGCTACATGATAAAGATATTGCCGGA
ACTCTGGCCTGGTTGAAAAGCGTGGTTGATGACTGGTATTGTGCGCCACTGGAAGGGCCG
CGCGGTGCCACGGCAGAACAACTGCTTGAGCATTTGGGTAACGGCAAATCATTTGATAGC
GTTGCGCAGGCATGGGATGCCGCAATGGCGGACGCTAAAGCGGAAGACACCGTGCTGGTG
TGTGGTTCTTTCCACACGGTCGCACATGTCATGGAAGTGATTGACGCGAGGAGAAGCGGT
GGCAAGTAA

1. Kimlova LJ, Pyne C, Keshavjee K, Huy J, Beebakhee G, Bognar AL: Mutagenesis of the folC gene encoding folylpolyglutamate synthetase-dihydrofolate synthetase in Escherichia coli. Arch Biochem Biophys. 1991 Jan;284(1):9-16. [PubMed ]
2. Nonet ML, Marvel CC, Tolan DR: The hisT-purF region of the Escherichia coli K-12 chromosome. Identification of additional genes of the hisT and purF operons. J Biol Chem. 1987 Sep 5;262(25):12209-17. [PubMed ]
3. Bognar AL, Osborne C, Shane B: Primary structure of the Escherichia coli folC gene and its folylpolyglutamate synthetase-dihydrofolate synthetase product and regulation of expression by an upstream gene. J Biol Chem. 1987 Sep 5;262(25):12337-43. [PubMed ]
4. Yamamoto Y, Aiba H, Baba T, Hayashi K, Inada T, Isono K, Itoh T, Kimura S, Kitagawa M, Makino K, Miki T, Mitsuhashi N, Mizobuchi K, Mori H, Nakade S, Nakamura Y, Nashimoto H, Oshima T, Oyama S, Saito N, Sampei G, Satoh Y, Sivasundaram S, Tagami H, Horiuchi T, et al.: Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features. DNA Res. 1997 Apr 28;4(2):91-113. [PubMed ]
5. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-74. [PubMed ]

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. EC 1.4.1.3
2. GDH
3. Glutamate dehydrogenase 1, mitochondrial precursor

MYRYLGEALLLSRAGPAALGSASADSAALLGWARGQPAAAPQPGLALAARRHYSEAVADR
EDDPNFFKMVEGFFDRGASIVEDKLVEDLRTRESEEQKRNRVRGILRIIKPCNHVLSLSF
PIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFG
GAKAGVKINPKNYTDNELEKITRRFTMELAKKGFIGPGIDVPAPDMSTGEREMSWIADTY
ASTIGHYDINAHACVTGKPISQGGIHGRISATGRGVFHGIENFINEASYMSILGMTPGFG
DKTFVVQGFGNVGLHSMRYLHRFGAKCIAVGESDGSIWNPDGIDPKELEDFKLQHGSILG
FPKAKPYEGSILEADCDILIPAASEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLER
NIMVIPDLYLNAGGVTVSYFEWLKNLNHVSYGRLTFKYERDSNYHLLMSVQESLERKFGK
HGGTIPIVPTAEFQDRISGASEKDIVHSGLAYTMERSARQIMRTAMKYNLGLDLRTAAYV
NAIEKVFKVYNEAGVTFT

• L-glutamate + H2O + NAD(P)+ = 2-oxoglutarate + NH3 + NAD(P)H + H+

• ELFV_dehydrog (PF00208 )
• ELFV_dehydrog_N (PF02812 )

• None

• None

• Mitochondrion
• mitochondrial matrix

ATGTACCGCTACCTGGGCGAAGCGCTGTTGCTGTCCCGGGCCGGGCCCGCTGCCCTGGGC
TCGGCGTCCGCCGACTCGGCCGCGTTGCTGGGCTGGGCCCGGGGACAGCCCGCCGCCGCC
CCGCAGCCGGGGCTGGCATTGGCCGCCCGGCGCCACTACAGCGAGGCGGTGGCCGACCGC
GAGGACGACCCCAACTTCTTCAAGATGGTGGAGGGCTTCTTCGATCGCGGCGCCAGCATC
GTGGAGGACAAGCTGGTGGAGGACCTGAGGACCCGGGAGAGCGAGGAGCAGAAGCGGAAC
CGGGTGCGCGGCATCCTGCGGATCATCAAGCCCTGCAACCATGTGCTGAGTCTCTCCTTC
CCCATCCGGCGCGACGACGGCTCCTGGGAGGTCATCGAAGGCTACCGGGCCCAGCACAGC
CAGCACCGCACGCCCTGCAAGGGAGGTATCCGTTACAGCACTGATGTGAGTGTAGATGAA
GTAAAAGCTTTGGCTTCTCTGATGACATACAAGTGTGCAGTGGTTGATGTGCCGTTTGGG
GGTGCTAAAGCTGGTGTTAAGATCAATCCCAAGAACTATACTGATAATGAATTGGAAAAG
ATCACAAGGAGGTTCACCATGGAGCTAGCAAAAAAGGGCTTTATTGGTCCTGGCATTGAT
GTGCCTGCTCCAGACATGAGCACAGGTGAGCGGGAGATGTCCTGGATCGCTGATACCTAT
GCCAGCACCATAGGGCACTATGATATTAATGCACACGCCTGTGTTACTGGTAAACCCATC
AGCCAAGGGGGAATCCATGGACGCATCTCTGCTACTGGCCGTGGTGTCTTCCATGGGATT
GAAAATTTCATCAATGAAGCTTCTTACATGAGCATTTTAGGAATGACACCAGGGTTTGGA
GATAAAACATTTGTTGTTCAGGGATTTGGTAATGTGGGCCTACACTCTATGAGATATTTA
CATCGTTTTGGTGCTAAATGTATTGCTGTTGGTGAGTCTGATGGGAGTATATGGAATCCA
GATGGTATTGACCCAAAGGAACTGGAAGACTTCAAATTGCAACATGGGTCCATTCTGGGC
TTCCCCAAGGCAAAGCCCTATGAAGGAAGCATCTTGGAGGCCGACTGTGACATACTGATC
CCAGCTGCCAGTGAGAAGCAGTTGACCAAATCCAACGCACCCAGAGTCAAAGCCAAGATC
ATTGCTGAAGGTGCCAATGGGCCAACAACTCCAGAAGCTGACAAGATCTTCCTGGAGAGA
AACATTATGGTTATTCCAGATCTCTACTTGAATGCTGGAGGAGTGACAGTATCTTACTTT
GAGTGGCTGAAGAATCTAAATCATGTCAGCTATGGCCGTTTGACCTTCAAATATGAAAGG
GATTCTAACTACCACTTGCTCATGTCTGTTCAAGAGAGTTTAGAAAGAAAATTTGGAAAG
CATGGTGGAACTATTCCCATTGTACCCACGGCAGAGTTCCAAGACAGGATATCGGGTGCA
TCTGAGAAAGACATCGTGCACTCTGGCTTGGCATACACAATGGAGCGTTCTGCCAGGCAA
ATTATGCGCACAGCCATGAAGTATAACCTGGGATTGGACCTGAGAACAGCTGCCTATGTT
AATGCCATTGAGAAAGTCTTCAAAGTGTACAATGAAGCTGGTGTGACCTTCACATAG

1. Meissner T, Beinbrech B, Mayatepek E: Congenital hyperinsulinism: molecular basis of a heterogeneous disease. Hum Mutat. 1999;13(5):351-61. [PubMed ]
2. Miki Y, Taki T, Ohura T, Kato H, Yanagisawa M, Hayashi Y: Novel missense mutations in the glutamate dehydrogenase gene in the congenital hyperinsulinism-hyperammonemia syndrome. J Pediatr. 2000 Jan;136(1):69-72. [PubMed ]
3. Santer R, Kinner M, Passarge M, Superti-Furga A, Mayatepek E, Meissner T, Schneppenheim R, Schaub J: Novel missense mutations outside the allosteric domain of glutamate dehydrogenase are prevalent in European patients with the congenital hyperinsulinism-hyperammonemia syndrome. Hum Genet. 2001 Jan;108(1):66-71. [PubMed ]
4. Smith TJ, Peterson PE, Schmidt T, Fang J, Stanley CA: Structures of bovine glutamate dehydrogenase complexes elucidate the mechanism of purine regulation. J Mol Biol. 2001 Mar 23;307(2):707-20. [PubMed ]
5. MacMullen C, Fang J, Hsu BY, Kelly A, de Lonlay-Debeney P, Saudubray JM, Ganguly A, Smith TJ, Stanley CA: Hyperinsulinism/hyperammonemia syndrome in children with regulatory mutations in the inhibitory guanosine triphosphate-binding domain of glutamate dehydrogenase. J Clin Endocrinol Metab. 2001 Apr;86(4):1782-7. [PubMed ]
6. Fang J, Hsu BY, MacMullen CM, Poncz M, Smith TJ, Stanley CA: Expression, purification and characterization of human glutamate dehydrogenase (GDH) allosteric regulatory mutations. Biochem J. 2002 Apr 1;363(Pt 1):81-7. [PubMed ]
7. Smith TJ, Schmidt T, Fang J, Wu J, Siuzdak G, Stanley CA: The structure of apo human glutamate dehydrogenase details subunit communication and allostery. J Mol Biol. 2002 May 3;318(3):765-77. [PubMed ]
8. Banerjee S, Schmidt T, Fang J, Stanley CA, Smith TJ: Structural studies on ADP activation of mammalian glutamate dehydrogenase and the evolution of regulation. Biochemistry. 2003 Apr 1;42(12):3446-56. [PubMed ]
9. Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [PubMed ]
10. Mavrothalassitis G, Tzimagiorgis G, Mitsialis A, Zannis V, Plaitakis A, Papamatheakis J, Moschonas N: Isolation and characterization of cDNA clones encoding human liver glutamate dehydrogenase: evidence for a small gene family. Proc Natl Acad Sci U S A. 1988 May;85(10):3494-8. [PubMed ]
11. 3377777 Amuro N, Yamaura M, Goto Y, Okazaki T: Molecular cloning and nucleotide sequence of the cDNA for human liver glutamate dehydrogenase precursor. Biochem Biophys Res Commun. 1988 May 16;152(3):1395-400.
12. 3399399 Nakatani Y, Schneider M, Banner C, Freese E: Complete nucleotide sequence of human glutamate dehydrogenase cDNA. Nucleic Acids Res. 1988 Jul 11;16(13):6237.
13. 3426581 Nakatani Y, Banner C, von Herrath M, Schneider ME, Smith HH, Freese E: Comparison of human brain and liver glutamate dehydrogenase cDNAS. Biochem Biophys Res Commun. 1987 Dec 16;149(2):405-10.
14. 3585334 Banner C, Silverman S, Thomas JW, Lampel KA, Vitkovic L, Huie D, Wenthold RJ: Isolation of a human brain cDNA for glutamate dehydrogenase. J Neurochem. 1987 Jul;49(1):246-52.
15. 429360 Julliard JH, Smith EL: Partial amino acid sequence of the glutamate dehydrogenase of human liver and a revision of the sequence of the bovine enzyme. J Biol Chem. 1979 May 10;254(9):3427-38.
16. 8314555 Tzimagiorgis G, Leversha MA, Chroniary K, Goulielmos G, Sargent CA, Ferguson-Smith M, Moschonas NK: Structure and expression analysis of a member of the human glutamate dehydrogenase (GLUD) gene family mapped to chromosome 10p11.2. Hum Genet. 1993 Jun;91(5):433-8.
17. 8486350 Michaelidis TM, Tzimagiorgis G, Moschonas NK, Papamatheakis J: The human glutamate dehydrogenase gene family: gene organization and structural characterization. Genomics. 1993 Apr;16(1):150-60.
18. 9571255 Stanley CA, Lieu YK, Hsu BY, Burlina AB, Greenberg CR, Hopwood NJ, Perlman K, Rich BH, Zammarchi E, Poncz M: Hyperinsulinism and hyperammonemia in infants with regulatory mutations of the glutamate dehydrogenase gene. N Engl J Med. 1998 May 7;338(19):1352-7.

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. EC 6.3.2.3
2. GSH synthetase
3. GSH-S
4. Glutathione synthase

MATNWGSLLQDKQQLEELARQAVDRALAEGVLLRTSQEPTSSEVVSYAPFTLFPSLVPSA
LLEQAYAVQMDFNLLVDAVSQNAAFLEQTLSSTIKQDDFTARLFDIHKQVLKEGIAQTVF
LGLNRSDYMFQRSADGSPALKQIEINTISASFGGLASRTPAVHRHVLSVLSKTKEAGKIL
SNNPSKGLALGIAKAWELYGSPNALVLLIAQEKERNIFDQRAIENELLARNIHVIRRTFE
DISEKGSLDQDRRLFVDGQEIAVVYFRDGYMPRQYSLQNWEARLLLERSHAAKCPDIATQ
LAGTKKVQQELSRPGMLEMLLPGQPEAVARLRATFAGLYSLDVGEEGDQAIAEALAAPSR
FVLKPQREGGGNNLYGEEMVQALKQLKDSEERASYILMEKIEPEPFENCLLRPGSPARVV
QCISELGIFGVYVRQEKTLVMNKHVGHLLRTKAIEHADGGVAAGVAVLDNPYPV

• ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione

• GSH_synthase (PF03199 )
• GSH_synth_ATP (PF03917 )

• None

• None

ATGGCCACCAACTGGGGGAGCCTCTTGCAGGATAAACAGCAGCTAGAGGAGCTGGCACGG
CAGGCCGTGGACCGGGCCCTGGCTGAGGGAGTATTGCTGAGGACCTCACAGGAGCCCACT
TCCTCGGAGGTGGTGAGCTATGCCCCATTCACGCTCTTCCCCTCACTGGTCCCCAGTGCC
CTGCTGGAGCAAGCCTATGCTGTGCAGATGGACTTCAACCTGCTAGTGGATGCTGTCAGC
CAGAACGCTGCCTTCCTGGAGCAAACTCTTTCCAGCACCATCAAACAGGATGACTTTACC
GCTCGTCTCTTTGACATCCACAAGCAAGTCCTAAAAGAGGGCATTGCCCAGACTGTGTTC
CTGGGCCTGAATCGCTCAGACTACATGTTCCAGCGCAGCGCAGATGGCTCCCCAGCCCTG
AAACAGATCGAAATCAACACCATCTCTGCCAGCTTTGGGGGCCTGGCCTCCCGGACCCCA
GCTGTGCACCGACATGTTCTCAGTGTCCTGAGTAAGACCAAAGAAGCTGGCAAGATCCTC
TCTAATAATCCCAGCAAGGGACTGGCCCTGGGAATTGCCAAAGCCTGGGAGCTCTACGGC
TCACCCAATGCTCTGGTGCTACTGATTGCTCAAGAGAAGGAAAGAAACATATTTGACCAG
CGTGCCATAGAGAATGAGCTACTGGCCAGGAACATCCATGTGATCCGACGAACATTTGAA
GATATCTCTGAAAAGGGGTCTCTGGACCAAGACCGAAGGCTGTTTGTGGATGGCCAGGAA
ATTGCTGTGGTTTACTTCCGGGATGGCTACATGCCTCGTCAGTACAGTCTACAGAATTGG
GAAGCACGTCTACTGCTGGAGAGGTCACATGCTGCCAAGTGCCCAGACATTGCCACCCAG
CTGGCTGGGACTAAGAAGGTGCAGCAGGAGCTAAGCAGGCCGGGCATGCTGGAGATGTTG
CTCCCTGGCCAGCCTGAGGCTGTGGCCCGCCTCCGCGCCACCTTTGCTGGCCTCTACTCA
CTGGATGTGGGTGAAGAAGGGGACCAGGCCATCGCCGAGGCCCTTGCTGCCCCTAGCCGG
TTTGTGCTAAAGCCCCAGAGAGAGGGTGGAGGTAACAACCTATATGGGGAGGAAATGGTA
CAGGCCCTGAAACAGCTGAAGGACAGTGAGGAGAGGGCCTCCTACATCCTCATGGAGAAG
ATCGAACCTGAGCCTTTTGAGAATTGCCTGCTACGGCCTGGCAGCCCTGCCCGAGTGGTC
CAGTGCATTTCAGAGCTGGGCATCTTTGGGGTCTATGTCAGGCAGGAAAAGACACTCGTG
ATGAACAAGCACGTGGGGCATCTACTTCGAACCAAAGCCATCGAGCATGCAGATGGTGGT
GTGGCAGCGGGAGTGGCAGTCCTGGACAACCCATACCCTGTGTGA

1. 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 ]
2. Gali RR, Board PG: Sequencing and expression of a cDNA for human glutathione synthetase. Biochem J. 1995 Aug 15;310 ( Pt 1):353-8. [PubMed ]
3. Shi ZZ, Habib GM, Rhead WJ, Gahl WA, He X, Sazer S, Lieberman MW: Mutations in the glutathione synthetase gene cause 5-oxoprolinuria. Nat Genet. 1996 Nov;14(3):361-5. [PubMed ]
4. Dahl N, Pigg M, Ristoff E, Gali R, Carlsson B, Mannervik B, Larsson A, Board P: Missense mutations in the human glutathione synthetase gene result in severe metabolic acidosis, 5-oxoprolinuria, hemolytic anemia and neurological dysfunction. Hum Mol Genet. 1997 Jul;6(7):1147-52. [PubMed ]

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. Apaf-1

MDAKARNCLLQHREALEKDIKTSYIMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMI
LKKDNDSYVSFYNALLHEGYKDLAALLHDGIPVVSSSSGKDSVSGITSYVRTVLCEGGVP
QRPVVFVTRKKLVNAIQQKLSKLKGEPGWVTIHGMAGCGKSVLAAEAVRDHSLLEGCFPG
GVHWVSVGKQDKSGLLMKLQNLCTRLDQDESFSQRLPLNIEEAKDRLRILMLRKHPRSLL
ILDDVWDSWVLKAFDSQCQILLTTRDKSVTDSVMGPKYVVPVESSLGKEKGLEILSLFVN
MKKADLPEQAHSIIKECKGSPLVVSLIGALLRDFPNRWEYYLKQLQNKQFKRIRKSSSYD
YEALDEAMSISVEMLREDIKDYYTDLSILQKDVKVPTKVLCILWDMETEEVEDILQEFVN
KSLLFCDRNGKSFRYYLHDLQVDFLTEKNCSQLQDLHKKIITQFQRYHQPHTLSPDQEDC
MYWYNFLAYHMASAKMHKELCALMFSLDWIKAKTELVGPAHLIHEFVEYRHILDEKDCAV
SENFQEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYQQAKLQAKQEVDNGMLYLEWINK
KNITNLSRLVVRPHTDAVYHACFSEDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEV
LCCAFSTDDRFIATCSVDKKVKIWNSMTGELVHTYDEHSEQVNCCHFTNSSHHLLLATGS
SDCFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDKLLASCSADGTLKLWDATSANERKS
INVKQFFLNLEDPQEDMEVIVKCCSWSADGARIMVAAKNKIFLFDIHTSGLLGEIHTGHH
STIQYCDFSPQNHLAVVALSQYCVELWNTDSRSKVADCRGHLSWVHGVMFSPDGSSFLTS
SDDQTIRLWETKKVCKNSAVMLKQEVDVVFQENEVMVLAVDHIRRLQLINGRTGQIDYLT
EAQVSCCCLSPHLQYIAFGDENGAIEILELVNNRIFQSRFQHKKTVWHIQFTADEKTLIS
SSDDAEIQVWNWQLDKCIFLRGHQETVKDFRLLKNSRLLSWSFDGTVKVWNIITGNKEKD
FVCHQGTVLSCDISHDATKFSSTSADKTAKIWSFDLLLPLHELRGHNGCVRCSAFSVDST
LLATGDDNGEIRIWNVSNGELLHLCAPLSEEGAATHGGWVTDLCFSPDGKMLISAGGYIK
WWNVVTGESSQTFYTNGTNLKKIHVSPDFKTYVTVDNLGILYILQTLE

• WD40 (PF00400 )
• CARD (PF00619 )
• NB-ARC (PF00931 )

• None

• None

• Cytoplasm

ATGGATGCAAAAGCTCGAAATTGTTTGCTTCAACATAGAGAAGCTCTGGAAAAGGACATC
AAGACATCCTACATCATGGATCACATGATTAGTGATGGATTTTTAACAATATCAGAAGAG
GAAAAAGTAAGAAATGAGCCCACTCAACAGCAAAGAGCAGCTATGCTGATTAAAATGATA
CTTAAAAAAGATAATGATTCCTACGTATCATTCTACAATGCTCTACTACATGAAGGATAT
AAAGATCTTGCTGCCCTTCTCCATGATGGCATTCCTGTTGTCTCTTCTTCCAGTGGTAAA
GATTCAGTTAGTGGAATAACTTCGTATGTAAGGACAGTCCTGTGTGAAGGTGGAGTACCA
CAGAGGCCAGTTGTTTTTGTCACAAGGAAGAAGCTGGTGAATGCAATTCAGCAGAAGCTC
TCCAAATTGAAAGGTGAACCAGGATGGGTCACCATACATGGAATGGCAGGCTGTGGGAAG
TCTGTATTAGCTGCAGAAGCTGTTAGAGATCATTCCCTTTTAGAAGGTTGTTTCCCAGGG
GGAGTGCATTGGGTTTCAGTTGGGAAACAAGACAAATCTGGGCTTCTGATGAAACTGCAG
AATCTTTGCACACGGTTGGATCAGGATGAGAGTTTTTCCCAGAGGCTTCCACTTAATATT
GAAGAGGCTAAAGACCGTCTCCGCATTCTGATGCTTCGCAAACACCCAAGGTCTCTCTTG
ATCTTGGATGATGTTTGGGACTCTTGGGTGTTGAAAGCTTTTGACAGTCAGTGTCAGATT
CTTCTTACAACCAGAGACAAGAGTGTTACAGATTCAGTAATGGGTCCTAAATATGTAGTC
CCTGTGGAGAGTTCCTTAGGAAAGGAAAAAGGACTTGAAATTTTATCCCTTTTTGTTAAT
ATGAAGAAGGCAGATTTGCCAGAACAAGCTCATAGTATTATAAAAGAATGTAAAGGCTCT
CCCCTTGTAGTATCTTTAATTGGTGCACTTTTACGTGATTTTCCCAATCGCTGGGAGTAC
TACCTCAAACAGCTTCAGAATAAGCAGTTTAAGAGAATAAGGAAATCTTCGTCTTATGAT
TATGAGGCTCTAGATGAAGCCATGTCTATAAGTGTTGAAATGCTCAGAGAAGACATCAAA
GATTATTACACAGATCTTTCCATCCTTCAGAAGGACGTTAAGGTGCCTACAAAGGTGTTA
TGTATTCTCTGGGACATGGAAACTGAAGAAGTTGAAGACATACTGCAGGAGTTTGTAAAT
AAGTCTCTTTTATTCTGTGATCGGAATGGAAAGTCGTTTCGTTATTATTTACATGATCTT
CAAGTAGATTTTCTTACAGAGAAGAATTGCAGCCAGCTTCAGGATCTACATAAGAAGATA
ATCACTCAGTTTCAGAGATATCACCAGCCGCATACTCTTTCACCAGATCAGGAAGACTGT
ATGTATTGGTACAACTTTCTGGCCTATCACATGGCCAGTGCCAAGATGCACAAGGAACTT
TGTGCTTTAATGTTTTCCCTGGATTGGATTAAAGCAAAAACAGAACTTGTAGGCCCTGCT
CATCTGATTCATGAATTTGTGGAATACAGACATATACTAGATGAAAAGGATTGTGCAGTC
AGTGAGAATTTTCAGGAGTTTTTATCTTTAAATGGACACCTTCTTGGACGACAGCCATTT
CCTAATATTGTACAACTGGGTCTCTGTGAGCCGGAAACTTCAGAAGTTTATCAGCAAGCT
AAGCTGCAGGCCAAGCAGGAGGTCGATAATGGAATGCTTTACCTGGAATGGATAAACAAA
AAAAACATCACGAATCTTTCCTGCTTAGTTGTCCGCCCCCACACAGATGCTGTTTACCAT
GCCTGCTTTTCTGAGGATGGTCAGAGAATAGCTTCTTGTGGAGCTGATAAAACCTTACAG
GTGTTCAAAGCTGAAACAGGAGAGAAACTTCTAGAAATCAAGGCTCATGAGGATGAAGTG
CTTTGTTGTGCATTCTCTACAGATGACAGATTTATAGCAACCTGCTCAGTGGATAAAAAA
GTGAAGATTTGGAATTCTATGACTGGGGAACTAGTACACACCTATGATGAGCACTCAGAG
CAAGTCAATTGCTGCCATTTCACCAACAGTAGTCATCATCTTCTCTTAGCCACTGGGTCA
AGTGACTGCTTCCTCAAACTTTGGGATTTGAATCAAAAAGAATGTCGAAATACCATGTTT
GGTCATACAAATTCAGTCAATCACTGCAGATTTTCACCAGATGATAAGCTTTTGGCTAGT
TGTTCAGCTGATGGAACCTTAAAGCTTTGGGATGCGACATCAGCAAATGAGAGGAAAAGC
ATTAATGTGAAACAGTTCTTCCTAAATTTGGAGGACCCTCAAGAGGATATGGAAGTGATA
GTGAAGTGTTGTTCGTGGTCTGCTGATGGTGCAAGGATAATGGTGGCAGCAAAAAATAAA
ATCTTTCTTTTTGCCATTCATACTAGTGGCCTATTGGGAGAAATCCACACGGGCCATCAC
AGCACCATCCAGTACTGTGACTTCTCCCCACAAAACCATTTGGCAGTGGTTGCTTTGTCC
CAGTACTGTGTAGAGTTGTGGAATACAGACTCACGTTCAAAGGTGGCTGATTGCAGAGGA
CATTTAAGTTGGGTTCATGGTGTGATGTTTTCTCCTGATGGATCATCATTTTTGACATCT
TCTGATGACCAGACAATCAGGCTCTGGGAGACAAAGAAAGTATGTAAGAACTCTGCTGTA
ATGTTAAAGCAAGAAGTAGATGTTGTGTTTCAAGAAAATGAAGTGATGGTCCTTGCAGTT
GACCATATAAGACGTCTGCAACTCGTTAATGGAAGAACAGGTCAGATTGATTATCTGACT
GAAGCTCAAGTTAGCTGCTGTTGCTTAAGTCCACATCTTCAGTACATTGCATTTGGAGAT
GAAAATGGAGCCATTGAGATTTTAGAACTTGTAAACAATAGAATCTTCCAGTCCAGGTTT
CAGCACAAGAAAACTGTATGGCACATCCAGTTCACAGCCGATGAGAAGACTCTTATTTCA
AGTTCTGATGATGCTGAAATTCAGGTATGGAATTGGCAATTGGACAAATGTATCTTTCTA
CGAGGCCATCAGGAAACAGTGAAAGACTTTAGACTCTTGAAAAATTCAAGACTGCTTTCT
TGGTCATTTGATGGAACAGTGAAGGTATGGAATATTATTACTGGAAATAAAGAAAAAGAC
TTTGTCTGTCACCAGGGTACAGTACTTTCTTGTGACATTTCTCACGATGCTACCAAGTTT
TCATCTACCTCTGCTGACAAGACTGCAAAGATCTGGAGTTTTGATCTCCTTTTGCCACTT
CATGAATTGAGGGGCCACAACGGCTGTGTGCGCTGCTCTGCCTTCTCTGTGGACAGTACC
CTGCTGGCAACGGGAGATGACAATGGAGAAATCAGGATATGGAATGTCTCAAACGGTGAG
CTTCTTCATTTGTGTGCTCCGCTTTCAGAAGAAGGAGCTGCTACCCATGGAGGCTGGGTG
ACTGACCTTTGCTTTTCTCCAGATGGCAAAATGCTTATCTCTGCTGGAGGATATATTAAG
TGGTGGAACGTTGTCACTGGGGAATCCTCACAGACCTTCTACACAAATGGAACCAATCTT
AAGAAAATACACGTGTCCCCTGACTTCAAAACATATGTGACTGTGGATAATCTTGGTATT
TTATATATTTTACAGACTTTAGAATAA

1. Saleh A, Srinivasula SM, Acharya S, Fishel R, Alnemri ES: Cytochrome c and dATP-mediated oligomerization of Apaf-1 is a prerequisite for procaspase-9 activation. J Biol Chem. 1999 Jun 18;274(25):17941-5. [PubMed ]
2. Hu Y, Benedict MA, Ding L, Nunez G: Role of cytochrome c and dATP/ATP hydrolysis in Apaf-1-mediated caspase-9 activation and apoptosis. EMBO J. 1999 Jul 1;18(13):3586-95. [PubMed ]
3. Hahn C, Hirsch B, Jahnke D, Durkop H, Stein H: Three new types of Apaf-1 in mammalian cells. Biochem Biophys Res Commun. 1999 Aug 11;261(3):746-9. [PubMed ]
4. Vaughn DE, Rodriguez J, Lazebnik Y, Joshua-Tor L: Crystal structure of Apaf-1 caspase recruitment domain: an alpha-helical Greek key fold for apoptotic signaling. J Mol Biol. 1999 Oct 29;293(3):439-47. [PubMed ]
5. Day CL, Dupont C, Lackmann M, Vaux DL, Hinds MG: Solution structure and mutagenesis of the caspase recruitment domain (CARD) from Apaf-1. Cell Death Differ. 1999 Nov;6(11):1125-32. [PubMed ]
6. Moroni MC, Hickman ES, Lazzerini Denchi E, Caprara G, Colli E, Cecconi F, Muller H, Helin K: Apaf-1 is a transcriptional target for E2F and p53. Nat Cell Biol. 2001 Jun;3(6):552-8. [PubMed ]
7. 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 ]
8. Ogawa T, Shiga K, Hashimoto S, Kobayashi T, Horii A, Furukawa T: APAF-1-ALT, a novel alternative splicing form of APAF-1, potentially causes impeded ability of undergoing DNA damage-induced apoptosis in the LNCaP human prostate cancer cell line. Biochem Biophys Res Commun. 2003 Jun 27;306(2):537-43. [PubMed ]
9. Zou H, Henzel WJ, Liu X, Lutschg A, Wang X: Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell. 1997 Aug 8;90(3):405-13. [PubMed ]
10. Ishikawa K, Nagase T, Nakajima D, Seki N, Ohira M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1997 Oct 31;4(5):307-13. [PubMed ]
11. 9651578 Srinivasula SM, Ahmad M, Fernandes-Alnemri T, Alnemri ES: Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization. Mol Cell. 1998 Jun;1(7):949-57.

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. ATP:riboflavin 5'-phosphotransferase
2. EC 2.7.1.26
3. Flavokinase

MPRADCIMRHLPYFCRGQVVRGFGRGSKQLGIPTANFPEQVVDNLPADISTGIYYGWASV
GSGDVHKMVVSIGWNPYYKNTKKSMETHIMHTFKEDFYGEILNVAIVGYLRPEKNFDSLE
SLISAIQGDIEEAKKRLELPEHLKIKEDNFFQVSKSKIMNGH

• ATP + riboflavin = ADP + FMN

• Flavokinase (PF01687 )

• None

• None

• Cytoplasm

ATGCCCCGAGCGGACTGCATTATGAGGCACCTGCCTTACTTCTGCCGGGGTCAAGTGGTG
CGGGGCTTCGGCCGCGGCTCCAAGCAGCTGGGCATCCCCACAGCTAATTTTCCTGAGCAA
GTGGTAGATAATCTTCCAGCTGATATATCCACTGGTATTTACTATGGTTGGGCCAGTGTT
GGAAGTGGAGATGTCCATAAGATGGTGGTGAGCATAGGATGGAACCCATATTACAAGAAT
ACGAAGAAGTCTATGGAAACACATATCATGCATACCTTCAAAGAGGACTTCTATGGGGAA
ATCCTCAGTGTGGCCATTGTTGGCTACCTGAGACCAGAAAAGAACTTTGATTCTTTAGAG
TCACTTATTTCAGCAATTCAAGGTGATATTGAAGAAGCTAAGAAACGACTAGAGTTACCA
GAACATTTGAAAATCAAAGAAGACAATTTCTTCCAGGTTTCTAAAAGCAAAATAATGAAT
GGCCACTGA

1. Karthikeyan S, Zhou Q, Mseeh F, Grishin NV, Osterman AL, Zhang H: Crystal structure of human riboflavin kinase reveals a beta barrel fold and a novel active site arch. Structure. 2003 Mar;11(3):265-73. [PubMed ]

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. CD117 antigen
2. EC 2.7.10.1
3. Mast/stem cell growth factor receptor precursor
4. Proto-oncogene tyrosine-protein kinase Kit
5. SCFR
6. c-kit

MRGARGAWDFLCVLLLLLRVQTGSSQPSVSPGEPSPPSIHPGKSDLIVRVGDEIRLLCTD
PGFVKWTFEILDETNENKQNEWITEKAEATNTGKYTCTNKHGLSNSIYVFVRDPAKLFLV
DRSLYGKEDNDTLVRCPLTDPEVTNYSLKGCQGKPLPKDLRFIPDPKAGIMIKSVKRAYH
RLCLHCSVDQEGKSVLSEKFILKVRPAFKAVPVVSVSKASYLLREGEEFTVTCTIKDVSS
SVYSTWKRENSQTKLQEKYNSWHHGDFNYERQATLTISSARVNDSGVFMCYANNTFGSAN
VTTTLEVVDKGFINIFPMINTTVFVNDGENVDLIVEYEAFPKPEHQQWIYMNRTFTDKWE
DYPKSENESNIRYVSELHLTRLKGTEGGTYTFLVSNSDVNAAIAFNVYVNTKPEILTYDR
LVNGMLQCVAAGFPEPTIDWYFCPGTEQRCSASVLPVDVQTLNSSGPPFGKLVVQSSIDS
SAFKHNGTVECKAYNDVGKTSAYFNFAFKGNNKEQIHPHTLFTPLLIGFVIVAGMMCIIV
MILTYKYLQKPMYEVQWKVVEEINGNNYVYIDPTQLPYDHKWEFPRNRLSFGKTLGAGAF
GKVVEATAYGLIKSDAAMTVAVKMLKPSAHLTEREALMSELKVLSYLGNHMNIVNLLGAC
TIGGPTLVITEYCCYGDLLNFLRRKRDSFICSKQEDHAEAALYKNLLHSKESSCSDSTNE
YMDMKPGVSYVVPTKADKRRSVRIGSYIERDVTPAIMEDDELALDLEDLLSFSYQVAKGM
AFLASKNCIHRDLAARNILLTHGRITKICDFGLARDIKNDSNYVVKGNARLPVKWMAPES
IFNCVYTFESDVWSYGIFLWELFSLGSSPYPGMPVDSKFYKMIKEGFRMLSPEHAPAEMY
DIMKTCWDADPLKRPTFKQIVQLIEKQISESTNHIYSNLANCSPNRQKPVVDHSVRINSV
GSTASSSQPLLVHDDV

• ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate

• ig (PF00047 )
• Pkinase_Tyr (PF07714 )

• 1-25

• 525-545

• Membrane
• single-pass type I membrane protein

ATGAGAGGCGCTCGCGGCGCCTGGGATTTTCTCTGCGTTCTGCTCCTACTGCTTCGCGTC
CAGACAGGCTCTTCTCAACCATCTGTGAGTCCAGGGGAACCGTCTCCACCATCCATCCAT
CCAGGAAAATCAGACTTAATAGTCCGCGTGGGCGACGAGATTAGGCTGTTATGCACTGAT
CCGGGCTTTGTCAAATGGACTTTTGAGATCCTGGATGAAACGAATGAGAATAAGCAGAAT
GAATGGATCACGGAAAAGGCAGAAGCCACCAACACCGGCAAATACACGTGCACCAACAAA
CACGGCTTAAGCAATTCCATTTATGTGTTTGTTAGAGATCCTGCCAAGCTTTTCCTTGTT
GACCGCTCCTTGTATGGGAAAGAAGACAACGACACGCTGGTCCGCTGTCCTCTCACAGAC
CCAGAAGTGACCAATTATTCCCTCAAGGGGTGCCAGGGGAAGCCTCTTCCCAAGGACTTG
AGGTTTATTCCTGACCCCAAGGCGGGCATCATGATCAAAAGTGTGAAACGCGCCTACCAT
CGGCTCTGTCTGCATTGTTCTGTGGACCAGGAGGGCAAGTCAGTGCTGTCGGAAAAATTC
ATCCTGAAAGTGAGGCCAGCCTTCAAAGCTGTGCCTGTTGTGTCTGTGTCCAAAGCAAGC
TATCTTCTTAGGGAAGGGGAAGAATTCACAGTGACGTGCACAATAAAAGATGTGTCTAGT
TCTGTGTACTCAACGTGGAAAAGAGAAAACAGTCAGACTAAACTACAGGAGAAATATAAT
AGCTGGCATCACGGTGACTTCAATTATGAACGTCAGGCAACGTTGACTATCAGTTCAGCG
AGAGTTAATGATTCTGGAGTGTTCATGTGTTATGCCAATAATACTTTTGGATCAGCAAAT
GTCACAACAACCTTGGAAGTAGTAGATAAAGGATTCATTAATATCTTCCCCATGATAAAC
ACTACAGTATTTGTAAACGATGGAGAAAATGTAGATTTGATTGTTGAATATGAAGCATTC
CCCAAACCTGAACACCAGCAGTGGATCTATATGAACAGAACCTTCACTGATAAATGGGAA
GATTATCCCAAGTCTGAGAATGAAAGTAATATCAGATACGTAAGTGAACTTCATCTAACG
AGATTAAAAGGCACCGAAGGAGGCACTTACACATTCCTAGTGTCCAATTCTGACGTCAAT
GCTGCCATAGCATTTAATGTTTATGTGAATACAAAACCAGAAATCCTGACTTACGACAGG
CTCGTGAATGGCATGCTCCAATGTGTGGCAGCAGGATTCCCAGAGCCCACAATAGATTGG
TATTTTTGTCCAGGAACTGAGCAGAGATGCTCTGCTTCTGTACTGCCAGTGGATGTGCAG
ACACTAAACTCATCTGGGCCACCGTTTGGAAAGCTAGTGGTTCAGAGTTCTATAGATTCT
AGTGCATTCAAGCACAATGGCACGGTTGAATGTAAGGCTTACAACGATGTGGGCAAGACT
TCTGCCTATTTTAACTTTGCATTTAAAGGTAACAACAAAGAGCAAATCCATCCCCACACC
CTGTTCACTCCTTTGCTGATTGGTTTCGTAATCGTAGCTGGCATGATGTGCATTATTGTG
ATGATTCTGACCTACAAATATTTACAGAAACCCATGTATGAAGTACAGTGGAAGGTTGTT
GAGGAGATAAATGGAAACAATTATGTTTACATAGACCCAACACAACTTCCTTATGATCAC
AAATGGGAGTTTCCCAGAAACAGGCTGAGTTTTGGGAAAACCCTGGGTGCTGGAGCTTTC
GGGAAGGTTGTTGAGGCAACTGCTTATGGCTTAATTAAGTCAGATGCGGCCATGACTGTC
GCTGTAAAGATGCTCAAGCCGAGTGCCCATTTGACAGAACGGGAAGCCCTCATGTCTGAA
CTCAAAGTCCTGAGTTACCTTGGTAATCACATGAATATTGTGAATCTACTTGGAGCCTGC
ACCATTGGAGGGCCCACCCTGGTCATTACAGAATATTGTTGCTATGGTGATCTTTTGAAT
TTTTTGAGAAGAAAACGTGATTCATTTATTTGTTCAAAGCAGGAAGATCATGCAGAAGCT
GCACTTTATAAGAATCTTCTGCATTCAAAGGAGTCTTCCTGCAGCGATAGTACTAATGAG
TACATGGACATGAAACCTGGAGTTTCTTATGTTGTCCCAACCAAGGCCGACAAAAGGAGA
TCTGTGAGAATAGGCTCATACATAGAAAGAGATGTGACTCCCGCCATCATGGAGGATGAC
GAGTTGGCCCTAGACTTAGAAGACTTGCTGAGCTTTTCTTACCAGGTGGCAAAGGGCATG
GCTTTCCTCGCCTCCAAGAATTGTATTCACAGAGACTTGGCAGCCAGAAATATCCTCCTT
ACTCATGGTCGGATCACAAAGATTTGTGATTTTGGTCTAGCCAGAGACATCAAGAATGAT
TCTAATTATGTGGTTAAAGGAAACGCTCGACTACCTGTGAAGTGGATGGCACCTGAAAGC
ATTTTCAACTGTGTATACACGTTTGAAAGTGACGTCTGGTCCTATGGGATTTTTCTTTGG
GAGCTGTTCTCTTTAGGAAGCAGCCCCTATCCTGGAATGCCGGTCGATTCTAAGTTCTAC
AAGATGATCAAGGAAGGCTTCCGGATGCTCAGCCCTGAACACGCACCTGCTGAAATGTAT
GACATAATGAAGACTTGCTGGGATGCAGATCCCCTAAAAAGACCAACATTCAAGCAAATT
GTTCAGCTAATTGAGAAGCAGATTTCAGAGAGCACCAATCATATTTACTCCAACTTAGCA
AACTGCAGCCCCAACCGACAGAAGCCCGTGGTAGACCATTCTGTGCGGATCAATTCTGTC
GGCAGCACCGCTTCCTCCTCCCAGCCTCTGCTTGTGCACGACGATGTCTGA

1. Mancini A, Koch A, Stefan M, Niemann H, Tamura T: The direct association of the multiple PDZ domain containing proteins (MUPP-1) with the human c-Kit C-terminus is regulated by tyrosine kinase activity. FEBS Lett. 2000 Sep 29;482(1-2):54-8. [PubMed ]
2. Wollberg P, Lennartsson J, Gottfridsson E, Yoshimura A, Ronnstrand L: The adapter protein APS associates with the multifunctional docking sites Tyr-568 and Tyr-936 in c-Kit. Biochem J. 2003 Mar 15;370(Pt 3):1033-8. [PubMed ]
3. Giebel LB, Strunk KM, Holmes SA, Spritz RA: Organization and nucleotide sequence of the human KIT (mast/stem cell growth factor receptor) proto-oncogene. Oncogene. 1992 Nov;7(11):2207-17. [PubMed ]
4. Spritz RA, Giebel LB, Holmes SA: Dominant negative and loss of function mutations of the c-kit (mast/stem cell growth factor receptor) proto-oncogene in human piebaldism. Am J Hum Genet. 1992 Feb;50(2):261-9. [PubMed ]
5. Fleischman RA: Human piebald trait resulting from a dominant negative mutant allele of the c-kit membrane receptor gene. J Clin Invest. 1992 Jun;89(6):1713-7. [PubMed ]
6. Giebel LB, Spritz RA: Mutation of the KIT (mast/stem cell growth factor receptor) protooncogene in human piebaldism. Proc Natl Acad Sci U S A. 1991 Oct 1;88(19):8696-9. [PubMed ]
7. Yarden Y, Kuang WJ, Yang-Feng T, Coussens L, Munemitsu S, Dull TJ, Chen E, Schlessinger J, Francke U, Ullrich A: Human proto-oncogene c-kit: a new cell surface receptor tyrosine kinase for an unidentified ligand. EMBO J. 1987 Nov;6(11):3341-51. [PubMed ]
8. Spritz RA, Holmes SA, Itin P, Kuster W: Novel mutations of the KIT (mast/stem cell growth factor receptor) proto-oncogene in human piebaldism. J Invest Dermatol. 1993 Jul;101(1):22-5. [PubMed ]
9. Furitsu T, Tsujimura T, Tono T, Ikeda H, Kitayama H, Koshimizu U, Sugahara H, Butterfield JH, Ashman LK, Kanayama Y, et al.: Identification of mutations in the coding sequence of the proto-oncogene c-kit in a human mast cell leukemia cell line causing ligand-independent activation of c-kit product. J Clin Invest. 1993 Oct;92(4):1736-44. [PubMed ]
10. Riva P, Milani N, Gandolfi P, Larizza L: A 12-bp deletion (7818del12) in the c-kit protooncogene in a large Italian kindred with piebaldism. Hum Mutat. 1995;6(4):343-5. [PubMed ]
11. 9027509 Andre C, Hampe A, Lachaume P, Martin E, Wang XP, Manus V, Hu WX, Galibert F: Sequence analysis of two genomic regions containing the KIT and the FMS receptor tyrosine kinase genes. Genomics. 1997 Jan 15;39(2):216-26.
12. 9697690 Nishida T, Hirota S, Taniguchi M, Hashimoto K, Isozaki K, Nakamura H, Kanakura Y, Tanaka T, Takabayashi A, Matsuda H, Kitamura Y: Familial gastrointestinal stromal tumours with germline mutation of the KIT gene. Nat Genet. 1998 Aug;19(4):323-4.

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. EC 1.1.1.34
2. HMG-CoA reductase

MLSRLFRMHGLFVASHPWEVIVGTVTLTICMMSMNMFTGNNKICGWNYECPKFEEDVLSS
DIIILTITRCIAILYIYFQFQNLRQLGSKYILGIAGLFTIFSSFVFSTVVIHFLDKELTG
LNEALPFFLLLIDLSRASTLAKFALSSNSQDEVRENIARGMAILGPTFTLDALVECLVIG
VGTMSGVRQLEIMCCFGCMSVLANYFVFMTFFPACVSLVLELSRESREGRPIWQLSHFAR
VLEEEENKPNPVTQRVKMIMSLGLVLVHAHSRWIADPSPQNSTADTSKVSLGLDENVSKR
IEPSVSLWQFYLSKMISMDIEQVITLSLALLLAVKYIFFEQTETESTLSLKNPITSPVVT
QKKVPDNCCRREPMLVRNNQKCDSVEEETGINRERKVEVIKPLVAETDTPNRATFVVGNS
SLLDTSSVLVTQEPEIELPREPRPNEECLQILGNAEKGAKFLSDAEIIQLVNAKHIPAYK
LETLMETHERGVSIRRQLLSKKLSEPSSLQYLPYRDYNYSLVMGACCENVIGYMPIPVGV
AGPLCLDEKEFQVPMATTEGCLVASTNRGCRAIGLGGGASSRVLADGMTRGPVVRLPRAC
DSAEVKAWLETSEGFAVIKEAFDSTSRFARLQKLHTSIAGRNLYIRFQSRSGDAMGMNMI
SKGTEKALSKLHEYFPEMQILAVSGNYCTDKKPAAINWIEGRGKSVVCEAVIPAKVVREV
LKTTTEAMIEVNINKNLVGSAMAGSIGGYNAHAANIVTAIYIACGQDAAQNVGSSNCITL
MEASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQMLGVQGACKDNPGENARQLAR
IVCGTVMAGELSLMAALAAGHLVKSHMIHNRSKINLQDLQGACTKKTA

• (R)-mevalonate + CoA + 2 NADP+ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+

• HMG-CoA_red (PF00368 )

• None

• 10-39
• 57-78
• 90-114
• 124-149
• 160-187
• 192-220
• 315-339

• Endoplasmic reticulum
• endoplasmic reticulum membrane
• multi-pass membrane protein. Peroxisome
• pero

ATGTTGTCAAGACTTTTTCGAATGCATGGCCTCTTTGTGGCCTCCCATCCCTGGGAAGTC
ATAGTGGGGACAGTGACACTGACCATCTGCATGATGTCCATGAACATGTTTACTGGTAAC
AATAAGATCTGTGGTTGGAATTATGAATGTCCAAAGTTTGAAGAGGATGTTTTGAGCAGT
GACATTATAATTCTGACAATAACACGATGCATAGCCATCCTGTATATTTACTTCCAGTTC
CAGAATTTACGTCAACTTGGATCAAAATATATTTTGGGTATTGCTGGCCTTTTCACAATT
TTCTCAAGTTTTGTATTCAGTACAGTTGTCATTCACTTCTTAGACAAAGAATTGACAGGC
TTGAATGAAGCTTTGCCCTTTTTCCTACTTTTGATTGACCTTTCCAGAGCAAGCACATTA
GCAAAGTTTGCCCTCAGTTCCAACTCACAGGATGAAGTAAGGGAAAATATTGCTCGTGGA
ATGGCAATTTTAGGTCCTACGTTTACCCTCGATGCTCTTGTTGAATGTCTTGTGATTGGA
GTTGGTACCATGTCAGGGGTACGTCAGCTTGAAATTATGTGCTGCTTTGGCTGCATGTCA
GTTCTTGCCAACTACTTCGTGTTCATGACTTTCTTCCCAGCTTGTGTGTCCTTGGTATTA
GAGCTTTCTCGGGAAAGCCGCGAGGGTCGTCCAATTTGGCAGCTCAGCCATTTTGCCCGA
GTTTTAGAAGAAGAAGAAAATAAGCCGAATCCTGTAACTCAGAGGGTCAAGATGATTATG
TCTCTAGGCTTGGTTCTTGTTCATGCTCACAGTCGCTGGATAGCTGATCCTTCTCCTCAA
AACAGTACAGCAGATACTTCTAAGGTTTCATTAGGACTGGATGAAAATGTGTCCAAGAGA
ATTGAACCAAGTGTTTCCCTCTGGCAGTTTTATCTCTCTAAAATGATCAGCATGGATATT
GAACAAGTTATTACCCTAAGTTTAGCTCTCCTTCTGGCTGTCAAGTACATCTTCTTTGAA
CAAACAGAGACAGAATCTACACTCTCATTAAAAAACCCTATCACATCTCCTGTAGTGACA
CAAAAGAAAGTCCCAGACAATTGTTGTAGACGTGAACCTATGCTGGTCAGAAATAACCAG
AAATGTGATTCAGTAGAGGAAGAGACAGGGATAAACCGAGAAAGAAAAGTTGAGGTTATA
AAACCCTTAGTGGCTGAAACAGATACCCCAAACAGAGCTACATTTGTGGTTGGTAACTCC
TCCTTACTCGATACTTCATCAGTACTGGTGACACAGGAACCTGAAATTGAACTTCCCAGG
GAACCTCGGCCTAATGAAGAATGTCTACAGATACTTGGGAATGCAGAGAAAGGTGCAAAA
TTCCTTAGTGATGCTGAGATCATCCAGTTAGTCAATGCTAAGCATATCCCAGCCTACAAG
TTGGAAACTCTGATGGAAACTCATGAGCGTGGTGTATCTATTCGCCGACAGTTACTTTCC
AAGAAGCTTTCAGAACCTTCTTCTCTCCAGTACCTACCTTACAGGGATTATAATTACTCC
TTGGTGATGGGAGCTTGTTGTGAGAATGTTATTGGATATATGCCCATCCCTGTTGGAGTG
GCAGGACCCCTTTGCTTAGATGAAAAAGAATTTCAGGTTCCAATGGCAACAACAGAAGGT
TGTCTTGTGGCCAGCACCAATAGAGGCTGCAGAGCAATAGGTCTTGGTGGAGGTGCCAGC
AGCCGAGTCCTTGCAGATGGGATGACTCGTGGCCCAGTTGTGCGTCTTCCACGTGCTTGT
GACTCTGCAGAAGTGAAAGCCTGGCTCGAAACATCTGAAGGGTTCGCAGTGATAAAGGAG
GCATTTGACAGCACTAGCAGATTTGCACGTCTACAGAAACTTCATACAAGTATAGCTGGA
CGCAACCTTTATATCCGTTTCCAGTCCAGGTCAGGGGATGCCATGGGGATGAACATGATT
TCAAAGGGTACAGAGAAAGCACTTTCAAAACTTCACGAGTATTTCCCTGAAATGCAGATT
CTAGCCGTTAGTGGTAACTATTGTACTGACAAGAAACCTGCTGCTATAAATTGGATAGAG
GGAAGAGGAAAATCTGTTGTTTGTGAAGCTGTCATTCCAGCCAAGGTTGTCAGAGAAGTA
TTAAAGACTACCACAGAGGCTATGATTGAGGTCAACATTAACAAGAATTTAGTGGGCTCT
GCCATGGCTGGGAGCATAGGAGGCTACAACGCCCATGCAGCAAACATTGTCACCGCCATC
TACATTGCCTGTGGACAGGATGCAGCACAGAATGTTGGTAGTTCAAACTGTATTACTTTA
ATGGAAGCAAGTGGTCCCACAAATGAAGATTTATATATCAGCTGCACCATGCCATCTATA
GAGATAGGAACGGTGGGTGGTGGGACCAACCTACTACCTCAGCAAGCCTGTTTGCAGATG
CTAGGTGTTCAAGGAGCATGCAAAGATAATCCTGGGGAAAATGCCCGGCAGCTTGCCCGA
ATTGTGTGTGGGACCGTAATGGCTGGGGAATTGTCACTTATGGCAGCATTGGCAGCAGGA
CATCTTGTCAAAAGTCACATGATTCACAACAGGTCGAAGATCAATTTACAAGACCTCCAA
GGAGCTTGCACCAAGAAGACAGCCTGA

1. 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 ]
2. Istvan ES, Palnitkar M, Buchanan SK, Deisenhofer J: Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis. EMBO J. 2000 Mar 1;19(5):819-30. [PubMed ]
3. Luskey KL, Stevens B: Human 3-hydroxy-3-methylglutaryl coenzyme A reductase. Conserved domains responsible for catalytic activity and sterol-regulated degradation. J Biol Chem. 1985 Aug 25;260(18):10271-7. [PubMed ]

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. Aurora kinase A
2. Aurora-A
3. Aurora-related kinase 1
4. Aurora/IPL1-related kinase 1
5. Breast-tumor-amplified kinase
6. EC 2.7.11.1
7. Serine/threonine kinase 15
8. hARK1

MDRSKENCISGPVKATAPVGGPKRVLVTQQFPCQNPLPVNSGQAQRVLCPSNSSQRVPLQ
AQKLVSSHKPVQNQKQKQLQATSVPHPVSRPLNNTQKSKQPLPSAPENNPEEELASKQKN
EESKKRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRR
EVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITEL
ANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRTTLCGTLDYLPPEM
IEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLI
SRLLKHNPSQRPMLREVLEHPWITANSSKPSNCQNKESASKQS

• ATP + a protein = ADP + a phosphoprotein

• Pkinase (PF00069 )

• None

• None

• Centrosome. Spindle. Note=Localizes on centrosomes in interphase cells and at each spindle pole in m

ATGGACCGATCTAAAGAAAACTGCATTTCAGGACCTGTTAAGGCTACAGCTCCAGTTGGA
GGTCCAAAACGTGTTCTCGTGACTCAGCAATTTCCTTGTCAGAATCCATTACCTGTAAAT
AGTGGCCAGGCTCAGCGGGTCTTGTGTCCTTCAAATTCTTCCCAGCGCGTTCCTTTGCAA
GCACAAAAGCTTGTCTCCAGTCACAAGCCGGTTCAGAATCAGAAGCAGAAGCAATTGCAG
GCAACCAGTGTACCTCATCCTGTCTCCAGGCCACTGAATAACACCCAAAAGAGCAAGCAG
CCCCTGCCATCGCACCTGAAAATAATCCTGAGGAGGAACTGGCATCAAAACAGAAAAATG
AAGAATCAAAAAGAGGCAGTGGCTTTGGAAGACTTTGAAATTGGTCGCCCTCTGGGTAAA
GGAAAGTTTGGTAATGTTTATTTGGCAAGAGAAAAGCAAAGCAAGTTTATTCTGGCTCTT
AAAGTGTTATTTAAAGCTCAGCTGGAGAAAGCCGGAGTGGAGCATCAGCTCAGAAGAGAA
GTAGAAATACAGTCCCACCTTCGGCATCCTAATATTCTTAGACTGTATGGTTATTTCCAT
GATGCTACCAGAGTCTACCTAATTCTGGAATATGCACCACTTGGAACAGTTTATAGAGAA
CTTCAGAAACTTTCAAAGTTTGATGAGCAGAGAACTGCTAACTTATATAACAGAATTGCA
AATGCCCTGTCTTACTGTCATTCGAAGAGAGTTATTCATAGAGACATTAAGCCAGAGAAC
TTACTTCTTGGATCAGCTGGAGAGCTTAAAATTGCAGATTTTGGGTGGTCAGTACATGCT
CCATCTTCCAGGAGGACCACTCTCTGTGGCACCCTGGACTACCTGCCCCCTGAAATGATT
GAAGGTCGGATGCATGATGAGAAGGTGGATCTCTGGAGCCTTGGAGTTCTTTGCTATGAA
TTTTTAGTTGGGAAGCCTCCTTTTGAGGCAAACACATACCAAGAGACCTACAAAAGAATA
TCACGGGTTGAATTCACATTCCCTGACTTTGTAACAGAGGGAGCCAGGGACCTCATTTCA
AGACTGTTGAAGCATAATCCCAGCCAGAGGCCAATGCTCAGAGAAGTACTTGAACACCCC
TGGATCACAGCAAATTCATCAAAACCATCAAATTGCCAAAACAAAGAATCAGCTAGCAAA
CAGTCTTAG

1. Nigg EA: Mitotic kinases as regulators of cell division and its checkpoints. Nat Rev Mol Cell Biol. 2001 Jan;2(1):21-32. [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. Tanaka M, Ueda A, Kanamori H, Ideguchi H, Yang J, Kitajima S, Ishigatsubo Y: Cell-cycle-dependent regulation of human aurora A transcription is mediated by periodic repression of E4TF1. J Biol Chem. 2002 Mar 22;277(12):10719-26. Epub 2002 Jan 14. [PubMed ]
4. Nowakowski J, Cronin CN, McRee DE, Knuth MW, Nelson CG, Pavletich NP, Rogers J, Sang BC, Scheibe DN, Swanson RV, Thompson DA: Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography. Structure. 2002 Dec;10(12):1659-67. [PubMed ]
5. Kimura M, Kotani S, Hattori T, Sumi N, Yoshioka T, Todokoro K, Okano Y: Cell cycle-dependent expression and spindle pole localization of a novel human protein kinase, Aik, related to Aurora of Drosophila and yeast Ipl1. J Biol Chem. 1997 May 23;272(21):13766-71. [PubMed ]
6. Shindo M, Nakano H, Kuroyanagi H, Shirasawa T, Mihara M, Gilbert DJ, Jenkins NA, Copeland NG, Yagita H, Okumura K: cDNA cloning, expression, subcellular localization, and chromosomal assignment of mammalian aurora homologues, aurora-related kinase (ARK) 1 and 2. Biochem Biophys Res Commun. 1998 Mar 6;244(1):285-92. [PubMed ]
7. Zhou H, Kuang J, Zhong L, Kuo WL, Gray JW, Sahin A, Brinkley BR, Sen S: Tumour amplified kinase STK15/BTAK induces centrosome amplification, aneuploidy and transformation. Nat Genet. 1998 Oct;20(2):189-93. [PubMed ]

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. HSP70-1/HSP70-2
2. HSP70.1

MAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVA
LNPQNTVFDAKRLIGRKFGDPVVQSDMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEIS
SMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAA
IAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNH
FVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRA
RFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLN
KSINPDEAVAYGAAVQAAILMGDKSENVQDLLLLDVAPLSLGLETAGGVMTALIKRNSTI
PTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDI
DANGILNVTATDKSTGKANKITITNDKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKN
ALESYAFNMKSAVEDEGLKGKISEADKKKVLDKCQEVISWLDANTLAEKDEFEHKRKELE
QVCNPIISGLYQGAGGPGPGGFGAQGPKGGSGSGPTIEEVD

• HSP70 (PF00012 )

• None

• None

ATGGCCAAAGCCGCGGCGATCGGCATCGACCTGGGCACCACCTACTCCTGCGTGGGGGTG
TTCCAACACGGCAAGGTGGAGATCATCGCCAACGACCAGGGCAACCGCACCACCCCCAGC
TACGTGGCCTTCACGGACACCGAGCGGCTCATCGGGGATGCGGCCAAGAACCAGGTGGCG
CTGAACCCGCAGAACACCGTGTTTGACGCGAAGCGCCTGATTGGCCGCAAGTTCGGCGAC
CCGGTGGTGCAGTCGGACATGAAGCACTGGCCTTTCCAGGTGATCAACGACGGAGACAAG
CCCAAGGTGCAGGTGAGCTACAAGGGGGAGACCAAGGCATTCTACCCCGAGGAGATCTCG
TCCATGGTGCTGACCAAGATGAAGGAGATCGCCGAGGCGTACCTGGGCTACCCGGTGACC
AACGCGGTGATCACCGTGCCGGCCTACTTCAACGACTCGCAGCGCCAGGCCACCAAGGAT
GCGGGTGTGATCGCGGGGCTCAACGTGCTGCGGATCATCAACGAGCCCACGGCCGCCGCC
ATCGCCTACGGCCTGGACAGAACGGGCAAGGGGGAGCGCAACGTGCTCATCTTTGACCTG
GGCGGGGGCACCTTCGACGTGTCCATCCTGACGATCGACGACGGCATCTTCGAGGTGAAG
GCCACGGCCGGGGACACCCACCTGGGTGGGGAGGACTTTGACAACAGGCTGGTGAACCAC
TTCGTGGAGGAGTTCAAGAGAAAACACAAGAAGGACATCAGCCAGAACAAGCGAGCCGTG
AGGCGGCTGCGCACCGCCTGCGAGAGGGCCAAGAGGACCCTGTCGTCCAGCACCCAGGCC
AGCCTGGAGATCGACTCCCTGTTTGAGGGCATCGACTTCTACACGTCCATCACCAGGGCG
AGGTTCGAGGAGCTGTGCTCCGACCTGTTCCGAAGCACCCTGGAGCCCGTGGAGAAGGCT
CTGCGCGACGCCAAGCTGGACAAGGCCCAGATTCACGACCTGGTCCTGGTCGGGGGCTCC
ACCCGCATCCCCAAGGTGCAGAAGCTGCTGCAGGACTTCTTCAACGGGCGCGACCTGAAC
AAGAGCATCAACCCCGACGAGGCTGTGGCCTACGGGGCGGCGGTGCAGGCGGCCATCCTG
ATGGGGGACAAGTCCGAGAACGTGCAGGACCTGCTGCTGCTGGACGTGGCTCCCCTGTCG
CTGGGGCTGGAGACGGCCGGAGGCGTGATGACTGCCCTGATCAAGCGCAACTCCACCATC
CCCACCAAGCAGACGCAGATCTTCACCACCTACTCCGACAACCAACCCGGGGTGCTGATC
CAGGTGTACGAGGGCGAGAGGGCCATGACGAAAGACAACAATCTGTTGGGGCGCTTCGAG
CTGAGCGGCATCCCTCCGGCCCCCAGGGGCGTGCCCCAGATCGAGGTGACCTTCGACATC
GATGCCAACGGCATCCTGAACGTCACGGCCACGGACAAGAGCACCGGCAAGGCCAACAAG
ATCACCATCACCAACGACAAGGGCCGCCTGAGCAAGGAGGAGATCGAGCGCATGGTGCAG
GAGGCGGAGAAGTACAAAGCGGAGGACGAGGTGCAGCGCGAGAGGGTGTCAGCCAAGAAC
GCCCTGGAGTCCTACGCCTTCAACATGAAGAGCGCCGTGGAGGATGAGGGGCTCAAGGGC
AAGATCAGCGAGGCCGACAAGAAGAAGGTGCTGGACAAGTGTCAAGAGGTCATCTCGTGG
CTGGACGCCAACACCTTGGCCGAGAAGGACGAGTTTGAGCACAAGAGGAAGGAGCTGGAG
CAGGTGTGTAACCCCATCATCAGCGGACTGTACCAGGGTGCCGGTGGTCCCGGGCCTGGG
GGCTTCGGGGCTCAGGGTCCCAAGGGAGGGTCTGGGTCAGGCCCCACCATTGAGGAGGTA
GATTAG

1. Osipiuk J, Walsh MA, Freeman BC, Morimoto RI, Joachimiak A: Structure of a new crystal form of human Hsp70 ATPase domain. Acta Crystallogr D Biol Crystallogr. 1999 May;55(Pt 5):1105-7. [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. Milner CM, Campbell RD: Structure and expression of the three MHC-linked HSP70 genes. Immunogenetics. 1990;32(4):242-51. [PubMed ]
4. Sargent CA, Dunham I, Trowsdale J, Campbell RD: Human major histocompatibility complex contains genes for the major heat shock protein HSP70. Proc Natl Acad Sci U S A. 1989 Mar;86(6):1968-72. [PubMed ]
5. Drabent B, Genthe A, Benecke BJ: In vitro transcription of a human hsp 70 heat shock gene by extracts prepared from heat-shocked and non-heat-shocked human cells. Nucleic Acids Res. 1986 Nov 25;14(22):8933-48. [PubMed ]
6. Hunt C, Morimoto RI: Conserved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70. Proc Natl Acad Sci U S A. 1985 Oct;82(19):6455-9. [PubMed ]

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. EC 2.7.11.26
2. GSK-3 beta

MSGRPRTTSFAESCKPVQQPSAFGSMKVSRDKDGSKVTTVVATPGQGPDRPQEVSYTDTK
VIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSG
EKKDEVYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHR
DIKPQNLLLDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDV
WSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHP
WTKVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPNVKLPNGRDTPALF
NFTTQELSSNPPLATILIPPHARIQAAASTPTNATAASDANTGDRGQTNNAASASASNST

• ATP + [tau-protein] = ADP + O-phospho-[tau-protein] ALL_REAC (other) R03744

• Pkinase (PF00069 )

• None

• None

ATGTCAGGGCGGCCCAGAACCACCTCCTTTGCGGAGAGCTGCAAGCCGGTGCAGCAGCCT
TCAGCTTTTGGCAGCATGAAAGTTAGCAGAGACAAGGACGGCAGCAAGGTGACAACAGTG
GTGGCAACTCCTGGGCAGGGTCCAGACAGGCCACAAGAAGTCAGCTATACAGACACTAAA
GTGATTGGAAATGGATCATTTGGTGTGGTATATCAAGCCAAACTTTGTGATTCAGGAGAA
CTGGTCGCCATCAAGAAAGTATTGCAGGACAAGAGATTTAAGAATCGAGAGCTCCAGATC
ATGAGAAAGCTAGATCACTGTAACATAGTCCGATTGCGTTATTTCTTCTACTCCAGTGGT
GAGAAGAAAGATGAGGTCTATCTTAATCTGGTGCTGGACTATGTTCCGGAAACAGTATAC
AGAGTTGCCAGACACTATAGTCGAGCCAAACAGACGCTCCCTGTGATTTATGTCAAGTTG
TATATGTATCAGCTGTTCCGAAGTTTAGCCTATATCCATTCCTTTGGAATCTGCCATCGG
GATATTAAACCGCAGAACCTCTTGTTGGATCCTGATACTGCTGTATTAAAACTCTGTGAC
TTTGGAAGTGCAAAGCAGCTGGTCCGAGGAGAACCCAATGTTTCGTATATCTGTTCTCGG
TACTATAGGGCACCAGAGTTGATCTTTGGAGCCACTGATTATACCTCTAGTATAGATGTA
TGGTCTGCTGGCTGTGTGTTGGCTGAGCTGTTACTAGGACAACCAATATTTCCAGGGGAT
AGTGGTGTGGATCAGTTGGTAGAAATAATCAAGGTCCTGGGAACTCCAACAAGGGAGCAA
ATCAGAGAAATGAACCCAAACTACACAGAATTTAAATTCCCTCAAATTAAGGCACATCCT
TGGACTAAGGTCTTCCGACCCCGAACTCCACCGGAGGCAATTGCACTGTGTAGCCGTCTG
CTGGAGTATACACCAACTGCCCGACTAACACCACTGGAAGCTTGTGCACATTCATTTTTT
GATGAATTACGGGACCCAAATGTCAAACATCCAAATGGGCGAGACACACCTGCACTCTTC
AACTTCACCACTCAAGAACTGTCAAGTAATCCACCTCTGGCTACCATCCTTATTCCTCCT
CATGCTCGGATTCAAGCAGCTGCTTCAACCCCCACAAATGCCACAGCAGCGTCAGATGCT
AATACTGGAGACCGTGGACAGACCAATAATGCTGCTTCTGCATCAGCTTCCAACTCCACC
TGA

1. Lau KF, Miller CC, Anderton BH, Shaw PC: Molecular cloning and characterization of the human glycogen synthase kinase-3beta promoter. Genomics. 1999 Sep 1;60(2):121-8. [PubMed ]
2. Rhoads AR, Karkera JD, Detera-Wadleigh SD: Radiation hybrid mapping of genes in the lithium-sensitive wnt signaling pathway. Mol Psychiatry. 1999 Sep;4(5):437-42. [PubMed ]
3. Hong YR, Chen CH, Chang JH, Wang S, Sy WD, Chou CK, Howng SL: Cloning and characterization of a novel human ninein protein that interacts with the glycogen synthase kinase 3beta. Biochim Biophys Acta. 2000 Jul 24;1492(2-3):513-6. [PubMed ]
4. Dajani R, Fraser E, Roe SM, Young N, Good V, Dale TC, Pearl LH: Crystal structure of glycogen synthase kinase 3 beta: structural basis for phosphate-primed substrate specificity and autoinhibition. Cell. 2001 Jun 15;105(6):721-32. [PubMed ]
5. Bax B, Carter PS, Lewis C, Guy AR, Bridges A, Tanner R, Pettman G, Mannix C, Culbert AA, Brown MJ, Smith DG, Reith AD: The structure of phosphorylated GSK-3beta complexed with a peptide, FRATtide, that inhibits beta-catenin phosphorylation. Structure. 2001 Dec;9(12):1143-52. [PubMed ]
6. Stambolic V, Woodgett JR: Mitogen inactivation of glycogen synthase kinase-3 beta in intact cells via serine 9 phosphorylation. Biochem J. 1994 Nov 1;303 ( Pt 3):701-4. [PubMed ]
7. Delcommenne M, Tan C, Gray V, Rue L, Woodgett J, Dedhar S: Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase. Proc Natl Acad Sci U S A. 1998 Sep 15;95(19):11211-6. [PubMed ]

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. Brain form hexokinase
2. EC 2.7.1.1
3. HK I
4. Hexokinase type I

MIAAQLLAYYFTELKDDQVKKIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTAT
VKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTPENIVH
GSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGV
EGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYME
ELRHIDLVEGDEGRMCINTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGM
YLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGLHNAKEILTRLG
VEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTH
PQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETLAHFHLT
KDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRV
LLVKIRSGKKRTVEMHNKIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGF
TFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLLRDAIKRREEFDLDVVAVVNDTVG
TMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGCLDD
IRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRG
IFETKFLSQIESDRLALLQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAA
VVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQTVKELSPKCNVSFLLSEDGSGKG
AALITAVGVRLRTEASS

• ATP + D-hexose = ADP + D-hexose 6-phosphate

• Hexokinase_1 (PF00349 )
• Hexokinase_2 (PF03727 )

• None

• None

• Mitochondrion
• mitochondrial outer membrane. Note=Its hydrophobic N-terminal sequence may be involve

ATGATCGCCGCGCAGCTCCTGGCCTATTACTTCACGGAGCTGAAGGATGACCAGGTCAAA
AAGATTGACAAGTATCTGTATGCCATGCGGCTCTCCGATGAAACTCTCATAGATATCATG
ACTCGCTTCAGGAAGGAGATGAAGAATGGCCTCTCCCGGGATTTTAATCCAACAGCCACA
GTCAAGATGTTGCCAACATTCGTAAGGTCCATTCCTGATGGCTCTGAAAAGGGAGATTTC
ATTGCCCTGGATCTTGGTGGGTCTTCCTTTCGAATTCTGCGGGTGCAAGTGAATCATGAG
AAAAACCAGAATGTTCACATGGAGTCCGAGGTTTATGACACCCCAGAGAACATCGTGCAC
GGCAGTGGAAGCCAGCTTTTTGATCATGTTGCTGAGTGCCTGGGAGATTTCATGGAGAAA
AGGAAGATCAAGGACAAGAAGTTACCTGTGGGATTCACGTTTTCTTTTCCTTGCCAACAA
TCCAAAATAGATGAGGCCATCCTGATCACCTGGACAAAGCGATTTAAAGCGAGCGGAGTG
GAAGGAGCAGATGTGGTCAAACTGCTTAACAAAGCCATCAAAAAGCGAGGGGACTATGAT
GCCAACATCGTAGCTGTGGTGAATGACACAGTGGGCACCATGATGACCTGTGGCTATGAC
GACCAGCACTGTGAAGTCGGCCTGATCATCGGCACTGGCACCAATGCTTGCTACATGGAG
GAACTGAGGCACATTGATCTGGTGGAAGGAGACGAGGGGAGGATGTGTATCAATACAGAA
TGGGGAGCCTTTGGAGACGATGGATCATTAGAAGACATCCGGACAGAGTTTGACAGGGAG
ATAGACCGGGGATCCCTCAACCCTGGAAAACAGCTGTTTGAGAAGATGGTCAGTGGCATG
TACTTGGGAGAGCTGGTTCGACTGATCCTAGTCAAGATGGCCAAGGAGGGCCTCTTATTT
GAAGGGCGGATCACCCCGGAGCTGCTCACCCGAGGGAAGTTTAACACCAGTGATGTGTCA
GCCATCGAAAAGAATAAGGAAGGCCTCCACAATGCCAAAGAAATCCTGACCCGCCTGGGA
GTGGAGCCGTCCGATGATGACTGTGTCTCAGTCCAGCACGTTTGCACCATTGTCTCATTT
CGCTCAGCCAACTTGGTGGCTGCCACACTGGGCGCCATCTTGAACCGCCTGCGTGATAAC
AAGGGCACACCCAGGCTGCGGACCACGGTTGGTGTCGACGGATCTCTTTACAAGACGCAC
CCACAGTATTCCCGGCGTTTCCACAAGACTCTAAGGCGCTTGGTGCCAGACTCCGATGTG
CGCTTCCTCCTCTCGGAGAGTGGCAGCGGCAAGGGGGCTGCCATGGTGACGGCGGTGGCC
TACCGCTTGGCCGAGCAGCACCGGCAGATAGAGGAGACCCTGGCTCATTTCCACCTCACC
AAAGACATGCTGCTGGAGGTGAAGAAGAGGATGCGGGCCGAGATGGAGCTGGGGCTGAGG
AAGCAGACGCACAACAATGCCGTGGTTAAGATGCTGCCCTCCTTCGTCCGGAGAACTCCC
GACGGGACCGAGAATGGTGACTTCTTGGCCCTGGATCTTGGAGGAACCAATTTCCGTGTG
CTGCTGGTGAAAATCCGTAGTGGGAAAAAGAGAACGGTGGAAATGCACAACAAGATCTAC
GCCATTCCTATTGAAATCATGCAGGGCACTGGGGAAGAGCTGTTTGATCACATTGTCTCC
TGCATCTCTGACTTCTTGGACTACATGGGGATCAAAGGCCCCAGGATGCCTCTGGGCTTC
ACGTTCTCATTTCCCTGCCAGCAGACGAGTCTGGACGCGGGAATCTTGATCACGTGGACA
AAGGGTTTTAAGGCAACAGACTGCGTGGGCCACGATGTAGTCACCTTACTAAGGGATGCG
ATAAAAAGGAGAGAGGAATTTGACCTGGACGTGGTGGCTGTGGTCAACGACACAGTGGGC
ACCATGATGACCTGTGCTTATGAGGAGCCCACCTGTGAGGTTGGACTCATTGTTGGGACC
GGCAGCAATGCCTGCTACATGGAGGAGATGAAGAACGTGGAGATGGTGGAGGGGGACCAG
GGGCAGATGTGCATCAACATGGAGTGGGGGGCCTTTGGGGACAACGGGTGTCTGGATGAT
ATCAGGACACACTACGACAGACTGGTGAACGAATATTCCCTAAATGCTGGGAAACAAAGG
TATGAGAAGATGATCAGTGGTATGTACCTGGGTGAAATCGTCCGCAACATCTTAATCGAC
TTCACCAAGAAGGGATTCCTCTTCCGAGGGCAGATCTCTGAGACGATGAAGACCCGGGGC
ATCTTTGAGACCAAGTTTCTCTCTCAGATCGAGAGTGACCGATTAGCACTGCTCCAGGTC
CGGGCTATCCTCCAGCAGCTAGGTCTGAATAGCACCTGCGATGACAGTATCCTCGTCAAG
ACAGTGTGCGGGGTGGTGTCCAGGAGGGCCGCACAGCTGTGTGGCGCAGGCATGGCTGCG
GTTGTGGATAAGATCCGCGAGAACAGAGGACTGGACCGTCTGAATGTGACTGTGGGAGTG
GACGGGACACTCTACAAGCTTCATCCACACTTCTCCAGAATCATGCACCAGACGGTGAAG
GAACTGTCACCAAAATGTAACGTGTCCTTCCTCCTGTCTGAGGATGGCAGCGGCAAGGGG
GCCGCCCTCATCACGGCCGTGGGCGTGCGGTTACGCACAGAGGCAAGCAGCTAA

1. Rosano C, Sabini E, Rizzi M, Deriu D, Murshudov G, Bianchi M, Serafini G, Magnani M, Bolognesi M: Binding of non-catalytic ATP to human hexokinase I highlights the structural components for enzyme-membrane association control. Structure. 1999 Nov 15;7(11):1427-37. [PubMed ]
2. Aleshin AE, Kirby C, Liu X, Bourenkov GP, Bartunik HD, Fromm HJ, Honzatko RB: Crystal structures of mutant monomeric hexokinase I reveal multiple ADP binding sites and conformational changes relevant to allosteric regulation. J Mol Biol. 2000 Mar 3;296(4):1001-15. [PubMed ]
3. Andreoni F, Ruzzo A, Magnani M: Structure of the 5' region of the human hexokinase type I (HKI) gene and identification of an additional testis-specific HKI mRNA. Biochim Biophys Acta. 2000 Sep 7;1493(1-2):19-26. [PubMed ]
4. Magnani M, Bianchi M, Casabianca A, Stocchi V, Daniele A, Altruda F, Ferrone M, Silengo L: A recombinant human 'mini'-hexokinase is catalytically active and regulated by hexose 6-phosphates. Biochem J. 1992 Jul 1;285 ( Pt 1):193-9. [PubMed ]
5. Magnani M, Serafini G, Bianchi M, Casabianca A, Stocchi V: Human hexokinase type I microheterogeneity is due to different amino-terminal sequences. J Biol Chem. 1991 Jan 5;266(1):502-5. [PubMed ]
6. Nishi S, Seino S, Bell GI: Human hexokinase: sequences of amino- and carboxyl-terminal halves are homologous. Biochem Biophys Res Commun. 1988 Dec 30;157(3):937-43. [PubMed ]
7. Bianchi M, Magnani M: Hexokinase mutations that produce nonspherocytic hemolytic anemia. Blood Cells Mol Dis. 1995;21(1):2-8. [PubMed ]
8. Aleshin AE, Zeng C, Fromm HJ, Honzatko RB: Crystallization and preliminary X-ray analysis of human brain hexokinase. FEBS Lett. 1996 Aug 5;391(1-2):9-10. [PubMed ]
9. Murakami K, Piomelli S: Identification of the cDNA for human red blood cell-specific hexokinase isozyme. Blood. 1997 Feb 1;89(3):762-6. [PubMed ]
10. Aleshin AE, Zeng C, Bourenkov GP, Bartunik HD, Fromm HJ, Honzatko RB: The mechanism of regulation of hexokinase: new insights from the crystal structure of recombinant human brain hexokinase complexed with glucose and glucose-6-phosphate. Structure. 1998 Jan 15;6(1):39-50. [PubMed ]
11. 9531504 Ruzzo A, Andreoni F, Magnani M: Structure of the human hexokinase type I gene and nucleotide sequence of the 5' flanking region. Biochem J. 1998 Apr 15;331 ( Pt 2):607-13.
12. 9735292 Aleshin AE, Zeng C, Bartunik HD, Fromm HJ, Honzatko RB: Regulation of hexokinase I: crystal structure of recombinant human brain hexokinase complexed with glucose and phosphate. J Mol Biol. 1998 Sep 18;282(2):345-57.

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. HSP 86
2. Renal carcinoma antigen NY- REN-38

MPEETQTQDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIR
YESLTDPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTKAFME
ALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVRTDTGEPM
GRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAEEKED
KEEEKEKEEKESEDKPEIEDVGSDEEEEKKDGDKKKKKKIKEKYIDQEELNKTKPIWTRN
PDDITNEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFVPRRAPFDLFENRKKKNN
IKLYVRRVFIMDNCEELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKC
LELFTELAEDKENYKKFYEQFSKNIKLGIHEDSQNRKKLSELLRYYTSASGDEMVSLKDY
CTRMKENQKHIYYITGETKDQVANSAFVERLRKHGLEVIYMIEPIDEYCVQQLKEFEGKT
LVSVTKEGLELPEDEEEKKKQEEKKTKFENLCKIMKDILEKKVEKVVVSNRLVTSPCCIV
TSTYGWTANMERIMKAQALRDNSTMGYMAAKKHLEINPDHSIIETLRQKAEADKNDKSVK
DLVILLYETALLSSGFSLEDPQTHANRIYRMIKLGLGIDEDDPTADDTSAAVTEEMPPLE
GDDDTSRMEEVD

• HSP90 (PF00183 )
• HATPase_c (PF02518 )

• None

• None

• Cytoplasm. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to

ATGCCTGAGGAAACCCAGACCCAAGACCAACCGATGGAGGAGGAGGAGGTTGAGACGTTC
GCCTTTCAGGCAGAAATTGCCCAGTTGATGTCATTGATCATCAATACTTTCTACTCGAAC
AAAGAGATCTTTCTGAGAGAGCTCATTTCAAATTCATCAGATGCATTGGACAAAATCCGG
TATGAAACTTTGACAGATCCCAGTAAATTAGACTCTGGGAAAGAGCTGCATATTAACCTT
ATACCGAACAAACAAGATCGAACTCTCACTATTGTGGATACTGGAATTGGAATGACCAAG
GCTGACTTGATCAATAACCTTGGTACTATCGCCAAGTCTGGGACCAAAGCGTTCATGGAA
GCTTTGCAGGCTGGTGCAGATATCTCTATGATTGGCCAGTTCGGTGTTGGTTTTTATTCT
GCTTATTTGGTTGCTGAGAAAGTAACTGTGATCACCAAACATAACGATGATGAGCAGTAC
GCTTGGGAGTCCTCAGCAGGGGGATCATTCACAGTGAGGACAGACACAGGTGAACCTATG
GGTCGTGGAACAAAAGTTATCCTACACCTGAAAGAAGACCAAACTGAGTACTTGGAGGAA
CGAAGAATAAAGGAGATTGTGAAGAAACATTCTCAGTTTATTGGATATCCCATTACTCTT
TTTGTGGAGAAGGAACGTGATAAAGAAGTAAGCGATGATGAGGCTGAAGAAAAGGAAGAC
AAAGAAGAAGAAAAAGAAAAAGAAGAGAAAGAGTCGGAAGACAAACCTGAAATTGAAGAT
GTTGGTTCTGATGAGGAAGAAGAAAAGAAGGATGGTGACAAGAAGAAGAAGAAGAAGATT
AAGGAAAAGTACATCGATCAAGAAGAGCTCAACAAAACAAAGCCCATCTGGACCAGAAAT
CCCGACGATATTACTAATGAGGAGTACGGAGAATTCTATAAGAGCTTGACCAATGACTGG
GAAGATCACTTGGCAGTGAAGCATTTTTCAGTTGAAGGACAGTTGGAATTCAGAGCCCTT
CTATTTGTCCCACGACGTGCTCCTTTTGATCTGTTTGAAAACAGAAAGAAAAAGAACAAT
ATCAAATTGTATGTACGCAGAGTTTTCATCATGGATAACTGTGAGGAGCTAATCCCTGAA
TATCTGAACTTCATTAGAGGGGTGGTAGACTCGGAGGATCTCCCTCTAAACATATCCCGT
GAGATGTTGCAACAAAGCAAAATTTTGAAAGTTATCAGGAAGAATTTGGTCAAAAAATGC
TTAGAACTCTTTACTGAACTGGCGGAAGATAAAGAGAACTACAAGAAATTCTATGAGCAG
TTCTCTAAAAACATAAAGCTTGGAATACACGAAGACTCTCAAAATCGGAAGAAGCTTTCA
GAGCTGTTAAGGTACTACACATCTGCCTCTGGTGATGAGATGGTTTCTCTCAAGGACTAC
TGCACCAGAATGAAGGAGAACCAGAAACATATCTATTATATCACAGGTGAGACCAAGGAC
CAGGTAGCTAACTCAGCCTTTGTGGAACGTCTTCGGAAACATGGCTTAGAAGTGATCTAT
ATGATTGAGCCCATTGATGAGTACTGTGTCCAACAGCTGAAGGAATTTGAGGGGAAGACT
TTAGTGTCAGTCACCAAAGAAGGCCTGGAACTTCCAGAGGATGAAGAAGAGAAAAAGAAG
CAGGAAGAGAAAAAAACAAAGTTTGAGAACCTCTGCAAAATCATGAAAGACATATTGGAG
AAAAAAGTTGAAAAGGTGGTTGTGTCAAACCGATTGGTGACATCTCCATGCTGTATTGTC
ACAAGCACATATGGCTGGACAGCAAACATGGAGAGAATCATGAAAGCTCAAGCCCTAAGA
GACAACTCAACAATGGGTTACATGGCAGCAAAGAAACACCTGGAGATAAACCCTGACCAT
TCCATTATTGAGACCTTAAGGCAAAAGGCAGAGGCTGATAAGAACGACAAGTCTGTGAAG
GATCTGGTCATCTTGCTTTATGAAACTGCGCTCCTGTCTTCTGGCTTCAGTCTGGAAGAT
CCCCAGACACATGCTAACAGGATCTACAGGATGATCAAACTTGGTCTGGGTATTGATGAA
GATGACCCTACTGCTGATGATACCAGTGCTGCTGTAACTGAAGAAATGCCACCCCTTGAA
GGAGATGACGACACATCACGCATGGAAGAAGTAGACTAA

1. Scanlan MJ, Gordan JD, Williamson B, Stockert E, Bander NH, Jongeneel V, Gure AO, Jager D, Jager E, Knuth A, Chen YT, Old LJ: Antigens recognized by autologous antibody in patients with renal-cell carcinoma. Int J Cancer. 1999 Nov 12;83(4):456-64. [PubMed ]
2. Lotz GP, Lin H, Harst A, Obermann WM: Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone. J Biol Chem. 2003 May 9;278(19):17228-35. Epub 2003 Feb 24. [PubMed ]
3. Yamazaki M, Tashiro H, Yokoyama K, Soeda E: Molecular cloning of cDNA encoding a human heat-shock protein whose expression is induced by adenovirus type 12 E1A in HeLa cells. Agric Biol Chem. 1990 Dec;54(12):3163-70. [PubMed ]
4. Hoffmann T, Hovemann B: Heat-shock proteins, Hsp84 and Hsp86, of mice and men: two related genes encode formerly identified tumour-specific transplantation antigens. Gene. 1988 Dec 30;74(2):491-501. [PubMed ]
5. Lees-Miller SP, Anderson CW: Two human 90-kDa heat shock proteins are phosphorylated in vivo at conserved serines that are phosphorylated in vitro by casein kinase II. J Biol Chem. 1989 Feb 15;264(5):2431-7. [PubMed ]
6. Lees-Miller SP, Anderson CW: The human double-stranded DNA-activated protein kinase phosphorylates the 90-kDa heat-shock protein, hsp90 alpha at two NH2-terminal threonine residues. J Biol Chem. 1989 Oct 15;264(29):17275-80. [PubMed ]
7. Hickey E, Brandon SE, Smale G, Lloyd D, Weber LA: Sequence and regulation of a gene encoding a human 89-kilodalton heat shock protein. Mol Cell Biol. 1989 Jun;9(6):2615-26. [PubMed ]
8. Walter T, Drabent B, Krebs H, Tomalak M, Heiss S, Benecke BJ: Cloning and analysis of a human 86-kDa heat-shock-protein-encoding gene. Gene. 1989 Nov 15;83(1):105-15. [PubMed ]
9. Yamazaki M, Akaogi K, Miwa T, Imai T, Soeda E, Yokoyama K: Nucleotide sequence of a full-length cDNA for 90 kDa heat-shock protein from human peripheral blood lymphocytes. Nucleic Acids Res. 1989 Sep 12;17(17):7108. [PubMed ]
10. Nemoto T, Ohara-Nemoto Y, Ota M, Takagi T, Yokoyama K: Mechanism of dimer formation of the 90-kDa heat-shock protein. Eur J Biochem. 1995 Oct 1;233(1):1-8. [PubMed ]
11. 9108479 Stebbins CE, Russo AA, Schneider C, Rosen N, Hartl FU, Pavletich NP: Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell. 1997 Apr 18;89(2):239-50.
12. 9660753 Young JC, Obermann WM, Hartl FU: Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90. J Biol Chem. 1998 Jul 17;273(29):18007-10.
13. 9817749 Obermann WM, Sondermann H, Russo AA, Pavletich NP, Hartl FU: In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis. J Cell Biol. 1998 Nov 16;143(4):901-10.

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. EC 2.7.4.9
2. dTMP kinase

MAARRGALIVLEGVDRAGKSTQSRKLVEALCAAGHRAELLRFPERSTEIGKLLSSYLQKK
SDVEDHSVHLLFSANRWEQVPLIKEKLSQGVTLVVDRYAFSGVAFTGAKENFSLDWCKQP
DVGLPKPDLVLFLQLQLADAAKRGAFGHERYENGAFQERALRCFHQLMKDTTLNWKMVDA
SKSIEAVHEDIRVLSEDAIRTATEKPLGELWK

• ATP + dTMP = ADP + dTDP

• Thymidylate_kin (PF02223 )

• None

• None

ATGGCGGCCCGGCGCGGGGCTCTCATAGTGCTGGAGGGCGTGGACCGCGCCGGGAAGAGC
ACGCAGAGCCGCAAGCTGGTGGAAGCGCTGTCGCGCGGGCCACCGCCCGAACTGCTCCGG
TTCCCGGAAAGATCAACTGAAATCGGCAAACTTCTGAGTTCCTACTTGCAAAAGAAAAGT
GACGTGGAGGATCACTCGGTGCACCTGCTTTTTTCTGCAAATCGCTGGGAACAAGTGCCG
TTAATTAAGGAAAAGTTGAGCCAGGGCGTGACCCTCGTCGTGGACAGATACGCATTTTCT
GGTGTGGCCTTCACCGGTGCCAAGGAGAATTTTTCCCTAGACTGGTGTAAACAGCCAGAC
GTGGGCCTTCCCAAACCCGACCTGGTCCTGTTCCTCCAGTTACAGCTGGCGGATGCTGCC
AAGCGGGGAGCGTTTGGCCATGAGCGCTATGAGAACGGGGCTTTCCAGGAGCGGGCGCTC
CGGTGTTTCCACCAGCTCATGAAAGACACGACTTTGAACTGGAAGATGGTGGATGCTTCC
AAAAGACTCGAAGCTGTCCATGAGGAACTCCGCGTGCTCTCTGAGGACGCCATCCGCACT
GCCACAGAGAAGCCGCTGGGGGAGCTATGGAAGTGA

1. Su JY, Sclafani RA: Molecular cloning and expression of the human deoxythymidylate kinase gene in yeast. Nucleic Acids Res. 1991 Feb 25;19(4):823-7. [PubMed ]
2. Huang SH, Tang A, Drisco B, Zhang SQ, Seeger R, Li C, Jong A: Human dTMP kinase: gene expression and enzymatic activity coinciding with cell cycle progression and cell growth. DNA Cell Biol. 1994 May;13(5):461-71. [PubMed ]

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. Dephosphocoenzyme A kinase
2. EC 2.7.1.24

MRYIVALTGGIGSGKSTVANAFADLGINVIDADIIARQVVEPGAPALHAIADHFGANMIA
ADGTLQRRALRERIFANPEEKNWLNALLHPLIQQETQHQIQQATSPYVLWVVPLLVENSL
YKKANRVLVVDVSPETQLKRTMQRDDVTREHVEQILAAQATREARLAVADDVIDNNGAPD
AIASDVARLHAHYLQLASQFVSQEKP

• ATP + dephospho-CoA = ADP + CoA

• CoaE (PF01121 )

• None

• None

• Cytoplasm (Probable)

TTACGGTTTTTCCTGTGAGACAAACTGCGACGCAAGCTGCAAATAGTGTGCGTGCAGGCG
GGCAACATCCGATGCGATAGCATCCGGTGCGCCGTTATTATCAATGACGTCATCTGCCAC
GGCAAGGCGGGCTTCGCGCGTTGCCTGAGCAGCAAGGATTTGTTCGACATGCTCGCGAGT
TACATCATCGCGCTGCATGGTGCGCTTAAGTTGCGTTTCTGGGCTGACATCCACCACAAG
CACTCGATTCGCTTTTTTATACAGTGAGTTTTCTACCAGCAATGGCACAACCCACAGTAC
ATAGGGGGAAGTAGCTTGCTGGATCTGGTGTTGCGTCTCTTGCTGAATCAGCGGATGCAG
CAGGGCGTTAAGCCAGTTTTTCTCTTCCGGGTTGGCGAAGATCCGCTCGCGCAAGGCCCG
GCGCTGCAATGTTCCATCAGCAGCAATCATGTTAGCGCCAAAGTGATCAGCAATGGCATG
TAGCGCAGGTGCACCTGGTTCAACCACCTGACGCGCAATAATATCGGCATCAATGACGTT
AATTCCGAGATCAGCAAACGCATTGGCAACGGTACTCTTGCCACTGCCAATGCCTCCCGT
TAAGGCAACTATATACCTCAT

1. Fountoulakis M, Takacs MF, Berndt P, Langen H, Takacs B: Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite chromatography. Electrophoresis. 1999 Aug;20(11):2181-95. [PubMed ]
2. Mishra P, Park PK, Drueckhammer DG: Identification of yacE (coaE) as the structural gene for dephosphocoenzyme A kinase in Escherichia coli K-12. J Bacteriol. 2001 May;183(9):2774-8. [PubMed ]
3. Fujita N, Mori H, Yura T, Ishihama A: Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region. Nucleic Acids Res. 1994 May 11;22(9):1637-9. [PubMed ]
4. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-74. [PubMed ]

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. EC 2.7.1.39
2. HK
3. HSK

MKVRVKAPCTSANLGVGFDVFGLCLKEPYDVIEVEAIDDKEIIIEVDDKNIPTDPDKNVA
GIVAKKMIDDFNIGKGVKITIKKGVKAGSGLGSSAASSAGTAYAINELFKLNLDKLKLVD
YASYGELASSGAKHADNVAPAIFGGFTMVTNYEPLEVLHIPIDFKLDILIAIPNISINTK
EAREILPKAVGLKDLVNNVGKACGMVYALYNKDKSLFGRYMMSDKVIEPVRGKLIPNYFK
IKEEVKDKVYGITISGSGPSIIAFPKEEFIDEVENILRDYYENTIRTEVGKGVEVV

• ATP + L-homoserine = ADP + O-phospho-L-homoserine

• GHMP_kinases_N (PF00288 )
• GHMP_kinases_C (PF08544 )

• None

• None

• Cytoplasm (Potential)

TTAAACAACTTCAACTCCTTTACCAACTTCTGTTCTTATTGTATTTTCATAATAATCTCT
CAAAATATTTTCAACCTCATCAATAAATTCTTCTTTTGGAAATGCAATTATTGAAGGGCC
AGAACCACTTATTGTTATGCCATAAACTTTGTCTTTAACTTCTTCTTTAATTTTGAAATA
ATTTGGGATGAGTTTTCCTCTAACTGGCTCTATAACCTTGTCAGACATCATATATCTTCC
AAATAATGATTTATCTTTATTATATAGGGCATAAACCATTCCACAGGCCTTTCCAACGTT
ATTTACTAAATCTTTTAGTCCAACAGCTTTTGGCAATATCTCTCTTGCTTCTTTTGTGTT
TATTGAGATGTTTGGGATAGCTATTAAAATATCAAGCTTAAAATCTATTGGTATATGTAA
AACTTCCAATGGCTCATAATTGGTTACCATCGTAAAGCCTCCAAATATAGCTGGAGCTAC
ATTATCAGCGTGTTTAGCTCCGGAAGAGGCAAGTTCTCCATAAGAAGCATAATCCACCAA
CTTTAACTTATCTAAATTAAGCTTAAATAGCTCATTTATAGCATAAGCAGTTCCTGCTGA
TGAAGCTGCTGAACTTCCCAAACCACTACCAGCTTTAACACCTTTTTTTATTGTTATTTT
AACTCCTTTACCAATATTAAAATCATCTATCATCTTTTTTGCTACAATTCCTGCAACATT
TTTATCTGGGTCTGTAGGGATGTTTTTATCATCTACTTCAATAATAATCTCTTTATCATC
TATTGCTTCAACCTCTATAACATCATAAGGTTCTTTTAAACATAAACCAAACACATCAAA
ACCAACTCCTAAATTTGCTGATGTGCAGGGAGCTTTCACTCTAACTTTCATGATTTCCCT
CAT

1. Bult CJ, White O, Olsen GJ, Zhou L, Fleischmann RD, Sutton GG, Blake JA, FitzGerald LM, Clayton RA, Gocayne JD, Kerlavage AR, Dougherty BA, Tomb JF, Adams MD, Reich CI, Overbeek R, Kirkness EF, Weinstock KG, Merrick JM, Glodek A, Scott JL, Geoghagen NS, Venter JC: Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii. Science. 1996 Aug 23;273(5278):1058-73. [PubMed ]

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. BCKD-kinase
2. BCKDHKIN
3. Branched-chain alpha-ketoacid dehydrogenase kinase
4. EC 2.7.11.4
5. kinase, mitochondrial precursor

MILTSVLGSGPRSGSSLWPLLGSSLSLRVRSTSATDTHHVELARERSKTVTSFYNQSAID
VVAEKPSVRLTPTMMLYSGRSQDGSHLLKSGRYLQQELPVRIAHRIKGFRSLPFIIGCNP
TILHVHELYIRAFQKLTDFPPIKDQADEAQYCQLVRQLLDDHKDVVTLLAEGLRESRKHI
EDEKLVRYFLDKTLTSRLGIRMLATHHLALHEDKPDFVGIICTRLSPKKIIEKWVDFARR
LCEHKYGNAPRVRINGHVAARFPFIPMPLDYILPELLKNAMRATMESHLDTPYNVPDVVI
TIANNDVDLIIRISDRGGGIAHKDLDRVMDYHFTTAEASTQDPRISPLFGHLDMHSGGQS
GPMHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRLRHIDGREESFRI

• ATP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] = ADP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphate ALL_REAC (other) R03516

• HATPase_c (PF02518 )

• None

• None

• Mitochondrion
• mitochondrial matrix

ATGATACTGACTTCAGTGCTGGGCAGCGGCCCTCGGAGCGGGTCTTCACTTTGGCCCCTC
TTGGGGTCCTCACTGTCACTCCGGGTTCGCTCAACATCAGCCACCGATACACACCATGTA
GAGCTGGCCAGGGAACGCTCCAAGACTGTTACCTCCTTTTACAACCAGTCAGCTATTGAC
GTGGTAGCAGAGAAGCCCTCAGTCCGCCTCACTCCCACCATGATGCTCTATTCTGGTCGC
TCACAGGATGGCAGCCACCTTCTGAAAAGTGGTCGCTACTTGCAGCAAGAGTTACCGGTG
AGGATCGCTCACCGCATCAAGGGCTTCGTAGTCTTCCTTTCATCATTGGTTGCAACCCTA
CCATACTGCACTGTGCACGAGCTATACATCCGGGCCTTCCAGAAGTTGACAGACTTCCCT
CCGATCAAGGACCAGGCAGACGAAGCCCAGTATTGCCAGCTGGTGCGACAGCTGCTAGAT
GACCACAAGGATGTGGTAACCCTGTTAGCTGAGGGTCTGCGTGAGAGCCGGAAACACATA
GAGGATGAAAAGCTGGTCCGCTACTTCCTGGATAAAACACTAACGTCCAGACTTGGGATC
CGAATGCTGGCTACTCACCACTTGGCGCTACATGAAGACAAGCCTGATTTTGTTGGCATC
ATCTCGACTCGTCTGTCACCCAAGAAGATTATTGAGAAGTGGGTGGATTTTGCCAGACGC
CTGTGCGAGCACAAGTATGGCAATGCCCCTAGAGTCCGCATCAATGGGCACGTGGCTGCC
CGTTTCCCCTTCATTCCTATGCCGCTGGACTATATCCTGCCTGAGCTGCTCAAGAACGCC
ATGAGAGCCACAATGGAGAGTCACCTAGACACGCCCTACAATGTTCCTGATGTGGTCATC
ACCATCGCCAATAACGATGTGGATCTCATCATCAGGATCTCAGACCGGGGTGGAGGAATC
GCTCATAAGGACCTGGATCGGGTCATGGACTACCACTTCACCACAGCTGAGGCCAGCACC
CAGGACCCCCGAATCAGCCCCCTCTTCGGCCACCTGGATATGCACAGTGGTGGCCAATCA
GGACCTATGCATGGCTTTGGCTTCGGGTTGCCCACGTCCAGGGCCTATGCGGAGTATCTC
GGTGGCTCCCTGCAGCTGCAGTCCCTGCAGGGCATTGGCACAGATGTCTACCTACGGCTC
CGCCACATTGATGGCCGGGAGGAAAGCTTCAGAATCTGA

1. Popov KM, Zhao Y, Shimomura Y, Kuntz MJ, Harris RA: Branched-chain alpha-ketoacid dehydrogenase kinase. Molecular cloning, expression, and sequence similarity with histidine protein kinases. J Biol Chem. 1992 Jul 5;267(19):13127-30. [PubMed ]
2. Harris RA, Popov KM, Shimomura Y, Zhao Y, Jaskiewicz J, Nanaumi N, Suzuki M: Purification, characterization, regulation and molecular cloning of mitochondrial protein kinases. Adv Enzyme Regul. 1992;32:267-84. [PubMed ]
3. Davie JR, Wynn RM, Meng M, Huang YS, Aalund G, Chuang DT, Lau KS: Expression and characterization of branched-chain alpha-ketoacid dehydrogenase kinase from the rat. Is it a histidine-protein kinase? J Biol Chem. 1995 Aug 25;270(34):19861-7. [PubMed ]

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. Recombinase A

MAQQAPDREKALELAMAQIDKNFGKGSVMRLGEEVRQPISVIPTGSISLDVALGIGGLPR
GRVIEIYGPESSGKTTVALHAVANAQAAGGIAAFIDAEHALDPEYAKKLGVDTDSLLVSQ
PDTGEQALEIADMLVRSGALDIIVIDSVAALVPRAEIEGEMGDSHVGLQARLMSQALRKM
TGALNNSGTTAIFINQLREKIGVMFGSPETTTGGKALKFYASVRLDVRRIETLKDGTDAV
GNRTRVKVVKNKVSPPFKQAEFDILYGQGISREGSLIDMGVEHGFIRKSGSWFTYEGEQL
GQGKENARKFLLENTDVANEIEKKIKEKLGIGAVVTAEADDVLPAPVDF

• RecA (PF00154 )

• None

• None

• Cytoplasm

ATGGCGCAGCAGGCCCCAGATCGCGAAAAGGCCCTCGAACTGGCGATGGCCCAGATCGAC
AAGAATTTCGGCAAAGGCTCGGTGATGCGCCTCGGCGAAGAGGTGCGCCAGCCGATCTCG
GTGATCCCCACCGGCTCCATCTCGCTGGATGTGGCGCTCGGCATCGGCGGCCTGCCGCGG
GGCCGCGTCATCGAGATCTACGGCCCGGAGTCCTCGGGTAAGACCACCGTGGCCCTGCAT
GCCGTCGCCAACGCGCAGGCCGCGGGCGGTATCGCGGCGTTCATCGACGCCGAGCACGCG
CTGGATCCCGAGTACGCCAAGAAGCTGGGTGTGGACACCGACTCGCTGCTGGTGTCGCAG
CCCGACACCGGTGAGCAGGCGCTGGAGATCGCCGACATGCTGGTGCGGTCCGGCGCGCTG
GACATCATCGTCATCGACTCGGTCGCCGCCCTGGTGCCGCGCGCCGAGATCGAGGGCGAG
ATGGGTGACAGCCACGTCGGCCTGCAGGCCCGCCTGATGAGCCAGGCGCTGCGCAAGATG
ACCGGCGCGTTGAACAACTCGGGCACCACCGCGATCTTCATCAACCAGCTCCGCGAGAAG
ATCGGTGTGATGTTCGGCTCGCCCGAGACCACCACGGGCGGTAAGGCACTGAAGTTCTAC
GCCTCGGTCCGCCTCGACGTGCGCCGTATCGAGACGCTCAAGGACGGCACCGACGCGGTC
GGTAACCGCACCCGCGTCAAGGTCGTCAAGAACAAGGTCTCCCCGCCGTTCAAGCAGGCC
GAGTTCGACATCCTCTACGGCCAGGGCATCAGCCGCGAGGGTTCGCTCATCGACATGGGC
GTCGAGCACGGCTTCATCCGCAAGTCCGGGTCCTGGTTCACCTACGAGGGTGAGCAGCTG
GGCCAGGGCAAGGAGAACGCCCGCAAGTTCCTGCTGGAGAACACCGACGTCGCCAACGAG
ATCGAGAAGAAGATCAAAGAGAAGCTCGGTATCGGCGCCGTCGTGACCGCTGAAGCCGAT
GACGTCCTCCCGGCCCCGGTTGACTTCTGA

1. Papavinasasundaram KG, Colston MJ, Davis EO: Construction and complementation of a recA deletion mutant of Mycobacterium smegmatis reveals that the intein in Mycobacterium tuberculosis recA does not affect RecA function. Mol Microbiol. 1998 Nov;30(3):525-34. [PubMed ]

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. AK
2. ATP-AMP transphosphorylase
3. EC 2.7.4.3

MRIILLGAPGAGKGTQAQFIMEKYGIPQISTGDMLRAAVKSGSELGKQAKDIMDAGKLVT
DELVIALVKERIAQEDCRNGFLLDGFPRTIPQADAMKEAGINVDYVLEFDVPDELIVDRI
VGRRVHAPSGRVYHVKFNPPKVEGKDDVTGEELTTRKDDQEETVRKRLVEYHQMTAPLIG
YYSKEAEAGNTKYAKVDGTKPVAEVRADLEKILG

• ATP + AMP = 2 ADP

• ADK (PF00406 )
• ADK_lid (PF05191 )

• None

• None

• Cytoplasm

ATGCGTATCATTCTGCTTGGCGCTCCGGGCGCGGGGAAAGGGACTCAGGCTCAGTTCATC
ATGGAGAAATATGGTATTCCGCAAATCTCCACTGGCGATATGCTGCGTGCTGCGGTCAAA
TCTGGCTCCGAGCTGGGTAAACAAGCAAAAGACATTATGGATGCTGGCAAACTGGTCACC
GACGAACTGGTGATCGCGCTGGTTAAAGAGCGCATTGCTCAGGAAGACTGCCGTAATGGT
TTCCTGTTGGACGGCTTCCCGCGTACCATTCCGCAGGCAGACGCGATGAAAGAAGCGGGC
ATCAATGTTGATTACGTTCTGGAATTCGACGTACCGGACGAACTGATCGTTGACCGTATC
GTCGGTCGCCGCGTTCATGCGCCGTCTGGTCGTGTTTATCACGTTAAATTCAATCCGCCG
AAAGTAGAAGGCAAAGACGACGTTACCGGTGAAGAACTGACTACCCGTAAAGATGATCAG
GAAGAGACCGTACGTAAACGTCTGGTTGAATACCATCAGATGACAGCACCGCTGATCGGC
TACTACTCCAAAGAAGCAGAAGCGGGTAATACCAAATACGCGAAAGTTGACGGCACCAAG
CCGGTTGCTGAAGTTCGCGCTGATCTGGAAAAAATCCTCGGCTAA

1. Muller CW, Schulz GE: Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state. J Mol Biol. 1992 Mar 5;224(1):159-77. [PubMed ]
2. Miyamoto K, Nakahigashi K, Nishimura K, Inokuchi H: Isolation and characterization of visible light-sensitive mutants of Escherichia coli K12. J Mol Biol. 1991 Jun 5;219(3):393-8. [PubMed ]
3. Reinstein J, Schlichting I, Wittinghofer A: Structurally and catalytically important residues in the phosphate binding loop of adenylate kinase of Escherichia coli. Biochemistry. 1990 Aug 14;29(32):7451-9. [PubMed ]
4. Reinstein J, Brune M, Wittinghofer A: Mutations in the nucleotide binding loop of adenylate kinase of Escherichia coli. Biochemistry. 1988 Jun 28;27(13):4712-20. [PubMed ]
5. Brune M, Schumann R, Wittinghofer F: Cloning and sequencing of the adenylate kinase gene (adk) of Escherichia coli. Nucleic Acids Res. 1985 Oct 11;13(19):7139-51. [PubMed ]
6. Bardwell JC, Craig EA: Eukaryotic Mr 83,000 heat shock protein has a homologue in Escherichia coli. Proc Natl Acad Sci U S A. 1987 Aug;84(15):5177-81. [PubMed ]
7. Berry MB, Meador B, Bilderback T, Liang P, Glaser M, Phillips GN Jr: The closed conformation of a highly flexible protein: the structure of E. coli adenylate kinase with bound AMP and AMPPNP. Proteins. 1994 Jul;19(3):183-98. [PubMed ]
8. Muller CW, Schulz GE: Crystal structures of two mutants of adenylate kinase from Escherichia coli that modify the Gly-loop. Proteins. 1993 Jan;15(1):42-9. [PubMed ]
9. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-74. [PubMed ]
10. Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [PubMed ]
11. 9600841 Wilkins MR, Gasteiger E, Tonella L, Ou K, Tyler M, Sanchez JC, Gooley AA, Walsh BJ, Bairoch A, Appel RD, Williams KL, Hochstrasser DF: Protein identification with N and C-terminal sequence tags in proteome projects. J Mol Biol. 1998 May 8;278(3):599-608.

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. D-glutamic acid- adding enzyme
2. EC 6.3.2.9
3. UDP-N- acetylmuramoyl-L-alanyl-D-glutamate synthetase

MADYQGKNVVIIGLGLTGLSCVDFFLARGVTPRVMDTRMTPPGLDKLPEAVERHTGSLND
EWLMAADLIVASPGIALAHPSLSAAADAGIEIVGDIELFCREAQAPIVAITGSNGKSTVT
TLVGEMAKAAGVNVGVGGNIGLPALMLLDDECELYVLELSSFQLETTSSLQAVAATILNV
TEDHMDRYPFGLQQYRAAKLRIYENAKVCVVNADDALTMPIRGADERCVSFGVNMGDYHL
NHQQGETWLRVKGEKVLNVKEMKLSGQHNYTNALAALALADAAGLPRASSLKALTTFTGL
PHRFEVVLEHNGVRWINDSKATNVGSTEAALNGLHVDGTLHLLLGGDGKSADFSPLARYL
NGDNVRLYCFGRDGAQLAALRPEVAEQTETMEQAMRLLAPRVQPGDMVLLSPACASLDQF
KNFEQRGNEFARLAKELG

• ATP + UDP-N-acetylmuramoyl-L-alanine + D-glutamate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate

• Mur_ligase_C (PF02875 )
• Mur_ligase_M (PF08245 )

• None

• None

• Cytoplasm

ATGGCTGATTATCAGGGTAAAAATGTCGTCATTATCGGCCTGGGCCTCACCGGGCTTTCC
TGCGTGGACTTTTTCCTCGCTCGCGGTGTGACGCCGCGCGTTATGGATACGCGTATGACA
CCGCCTGGCCTGGATAAATTACCCGAAGCCGTAGAACGCCACACGGGCAGTCTGAATGAT
GAATGGCTGATGGCGGCAGATCTGATTGTCGCCAGTCCCGGTATTGCACTGGCGCATCCA
TCCTTAAGCGCTGCCGCTGATGCCGGAATCGAAATCGTTGGCGATATCGAGCTGTTCTGT
CGCGAAGCACAAGCACCGATTGTGGCGATTACCGGTTCTAACGGCAAAAGCACGGTCACC
ACGCTAGTGGGTGAAATGGCGAAAGCGGCGGGGGTTAACGTTGGTGTGGGTGGCAATATT
GGCCTGCCTGCGTTGATGCTACTGGATGATGAGTGTGAACTGTACGTGCTGGAACTGTCG
AGCTTCCAGCTGGAAACCACCTCCAGCTTACAGGCGGTAGCAGCGACCATTCTGAACGTG
ACTGAAGATCATATGGATCGCTATCCGTTTGGTTTACAACAGTATCGTGCAGCAAAACTG
CGCATTTACGAAAACGCGAAAGTTTGCGTGGTTAATGCTGATGATGCCTTAACAATGCCG
ATTCGCGGTGCGGATGAACGCTGCGTCAGCTTTGGCGTCAACATGGGTGACTATCACCTG
AATCATCAGCAGGGCGAAACCTGGCTGCGGGTTAAAGGCGAGAAAGTGCTGAATGTGAAA
GAGATGAAACTTTCCGGGCAGCATAACTACACCAATGCGCTGGCGGCGCTGGCGCTGGCA
GATGCTGCAGGGTTACCGCGTGCCAGCAGCCTGAAAGCGTTAACCACATTCACTGGTCTG
CCGCATCGCTTTGAAGTTGTGCTGGAGCATAACGGCGTACGTTGGATTAACGATTCGAAA
GCGACCAACGTCGGCAGTACGGAAGCGGCGCTGAATGGCCTGCACGTAGACGGCACACTG
CATTTGTTGCTGGGTGGCGATGGTAAATCGGCGGACTTTAGCCCACTGGCGCGTTACCTG
AATGGCGATAACGTACGTCTGTATTGTTTCGGTCGTGACGGCGCGCAGCTGGCGGCGCTA
CGCCCGGAAGTGGCAGAACAAACCGAAACTATGGAACAGGCGATGCGCTTGCTGGCTCCG
CGTGTTCAGCCGGGCGATATGGTTCTGCTCTCCCCAGCCTGTGCCAGCCTTGATCAGTTC
AAGAACTTTGAACAACGAGGCAATGAGTTTGCCCGTCTGGCGAAGGAGTTAGGTTGA

1. Bertrand JA, Fanchon E, Martin L, Chantalat L, Auger G, Blanot D, van Heijenoort J, Dideberg O: "Open" structures of MurD: domain movements and structural similarities with folylpolyglutamate synthetase. J Mol Biol. 2000 Sep 1;301(5):1257-66. [PubMed ]
2. Yura T, Mori H, Nagai H, Nagata T, Ishihama A, Fujita N, Isono K, Mizobuchi K, Nakata A: Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region. Nucleic Acids Res. 1992 Jul 11;20(13):3305-8. [PubMed ]
3. Pratviel-Sosa F, Mengin-Lecreulx D, van Heijenoort J: Over-production, purification and properties of the uridine diphosphate N-acetylmuramoyl-L-alanine:D-glutamate ligase from Escherichia coli. Eur J Biochem. 1991 Dec 18;202(3):1169-76. [PubMed ]
4. Mengin-Lecreulx D, van Heijenoort J: Nucleotide sequence of the murD gene encoding the UDP-MurNAc-L-Ala-D-Glu synthetase of Escherichia coli. Nucleic Acids Res. 1990 Jan 11;18(1):183. [PubMed ]
5. Ikeda M, Wachi M, Ishino F, Matsuhashi M: Nucleotide sequence involving murD and an open reading frame ORF-Y spacing murF and ftsW in Escherichia coli. Nucleic Acids Res. 1990 Feb 25;18(4):1058. [PubMed ]
6. Ikeda M, Sato T, Wachi M, Jung HK, Ishino F, Kobayashi Y, Matsuhashi M: Structural similarity among Escherichia coli FtsW and RodA proteins and Bacillus subtilis SpoVE protein, which function in cell division, cell elongation, and spore formation, respectively. J Bacteriol. 1989 Nov;171(11):6375-8. [PubMed ]
7. Bertrand JA, Auger G, Fanchon E, Martin L, Blanot D, van Heijenoort J, Dideberg O: Crystal structure of UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase from Escherichia coli. EMBO J. 1997 Jun 16;16(12):3416-25. [PubMed ]
8. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-74. [PubMed ]

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. Recombinase A

MTQAPDREKALELAMAQIEKSYGKGSVMRLGDEMRQPISVIPTGSIALDVALGIGGLPRG
RVVEIYGPESSGKTTVALHAVANAQAAGGVAAFIDAEHALDPEYAKKLGVDTDSLLVSQP
DTGEQALEIADMLIRSGALDILVIDSVAALVPRAELEGEMGDSHVGLQARLMSQALRKMT
GALNNSGTTAIFINQLREKIGVMFGSPETTTGGKALKFYASVRMDVRRIETLKDGTNAVG
NRTRVKIVKNKVSPPFKQAEFDILYGRGISREGSLIDMGVDQGFIRKSGSWFTYEGEQLG
QGKENARTFLMENDEVANEIEKKIKEKLGIGAVVTDDLSDDGVLPAPVDF

• RecA (PF00154 )

• None

• None

• Cytoplasm

TCAGAAGTCGACGGGGGCGGGCAGGACGCCGTCATCGGACAAGTCATCGGTCACGACCGC
GCCAATGCCGAGCTTTTCCTTGATCTTCTTCTCGATCTCGTTGGCGACCTCGTCGTTCTC
CATCAAGAAGGTGCGGGCGTTCTCCTTGCCCTGGCCGAGCTGCTCGCCCTCATAGGTGAA
CCAGGAACCGGACTTGCGGATGAAGCCCTGATCCACACCCATGTCGATCAGCGAGCCCTC
CCGGCTGATCCCGCGGCCGTAGAGGATGTCGAACTCGGCCTGCTTGAACGGCGGCGACAC
CTTGTTCTTGACGATCTTGACCCGGGTGCGGTTGCCGACCGCGTTGGTGCCGTCCTTGAG
CGTCTCGATCCGGCGCACGTCCATGCGCACCGAGGCGTAGAACTTCAACGCCTTGCCACC
CGTCGTGGTCTCCGGGCTGCCGAACATCACCCCGATCTTCTCCCGCAGCTGGTTGATGAA
GATCGCGGTGGTGCCCGAATTGTTCAGCGCGCCAGTCATTTTCCGCAGCGCCTGGCTCAT
CAGCCGGGCCTGCAGCCCGACGTGGCTGTCCCCCATCTCGCCCTCCAGCTCGGCGCGCGG
CACCAGCGCGGCCACCGAGTCGATGACCAGGATGTCCAGCGCGCCGGAGCGGATCAGCAT
GTCGGCGATCTCGAGCGCCTGCTCCCCCGTGTCCGGCTGGCTGACCAGCAGCGAATCGGT
GTCCACGCCGAGCTTCTTGGCGTACTCGGGGTCCAGCGCGTGCTCGGCGTCGATGAACGC
CGCGACACCGCCGGCGGCCTGGGCGTTGGCCACCGCGTGCAGGGCGACGGTGGTCTTACC
CGAGGATTCCGGGCCGTAGATCTCCACGACCCGGCCGCGGGGCAGGCCGCCGATGCCCAG
GGCGACGTCCAGGGCGATGGATCCGGTCGGGATGACCGAGATCGGTTGACGCATCTCGTC
GCCGAGACGCATCACCGAGCCTTTCCCGTAGCTCTTTTCGATCTGGGCCATCGCCAGTTC
GAGAGCCTTCTCGCGGTCGGGGGCTTGCGTCATGGTGCCTCTCCTATAGTCGGTGTGTCT
TCTGACCGGTATCGGTCGGTTGGCGGTGACACTAGAGAAGGCCACCGACAAGTTGACGCT
GCGAACGTCCCCCACAGTAGCCGAACAGGTGTTCGATTCAAGTTCGACACGCCGCGGGCG
TCGCAGCAGCCGCGAAAGGCCGGCCGACAT

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. DTB synthetase
2. DTBS
3. Dethiobiotin synthase
4. EC 6.3.3.3

MSKRYFVTGTDTEVGKTVASCALLQAAKAAGYRTAGYKPVASGSEKTPEGLRNSDALALQ
RNSSLQLDYATVNPYTFAEPTSPHIISAQEGRPIESLVMSAGLRALEQQADWVLVEGAGG
WFTPLSDTFTFADWVTQEQLPVILVVGVKLGCINHAMLTAQVIQHAGLTLAGWVANDVTP
PGKRHAEYMTTLTRMIPAPLLGEIPWLAENPENAATGKYINLALL

• ATP + 7,8-diaminononanoate + CO2 = ADP + phosphate + dethiobiotin

• CbiA (PF01656 )

• None

• None

• Cytoplasm

GTGAGTAAACGTTATTTTGTCACCGGAACGGATACCGAAGTGGGGAAAACTGTCGCCAGT
TGTGCACTTTTACAAGCCGCAAAGCGAGCAGGCTACCGGACGGCAGGTTATAAACCGGTC
GCCTCTGGCAGCGAAAAGACCCCGGAAGGTTTACGCAATAGCGACGCGCTGGCGTTACAG
CGCAACAGCAGCCTGCAGCTGGATTACGCAACAGTAAATCCTTACACCTTCGCAGAACCC
ACTTCGCCGCACATCATCAGCGCGCAAGAGGGCAGACCGATAGAATCATTGGTAATGAGC
GCCGGATTACGCGCGCTTGAACAACAGGCTGACTGGGTGTTAGTGGAAGGTGCTGGCGGC
TGGTTTACGCCGCTTTCTGACACTTTCACTTTTGCAGATTGGGTAACACAGGAACAACTG
CCGGTGATACTGGTAGTTGGTGTGAAACTCGGCTGTATTAATCACGCGATGTTGACTGCA
CAGGTAATACAACACGCCGGACTGACTCTGGCGGGTTGGGTGGCGAACGATGTTACGCCT
CCGGGAAAACGTCACGCTGAATATATGACCACGCTCACCCGCATGATTCCGCGCCGCTGC
TGGGAGAGATCCCCTGGCTTGCAGAAAATCCAGAAAATGCGGCAACCGGAAAGTACATAA

1. Sandalova T, Schneider G, Kack H, Lindqvist Y: Structure of dethiobiotin synthetase at 0.97 A resolution. Acta Crystallogr D Biol Crystallogr. 1999 Mar;55(Pt 3):610-24. [PubMed ]
2. Otsuka AJ, Buoncristiani MR, Howard PK, Flamm J, Johnson C, Yamamoto R, Uchida K, Cook C, Ruppert J, Matsuzaki J: The Escherichia coli biotin biosynthetic enzyme sequences predicted from the nucleotide sequence of the bio operon. J Biol Chem. 1988 Dec 25;263(36):19577-85. [PubMed ]
3. Alexeev D, Baxter RL, Sawyer L: Mechanistic implications and family relationships from the structure of dethiobiotin synthetase. Structure. 1994 Nov 15;2(11):1061-72. [PubMed ]
4. Huang W, Lindqvist Y, Schneider G, Gibson KJ, Flint D, Lorimer G: Crystal structure of an ATP-dependent carboxylase, dethiobiotin synthetase, at 1.65 A resolution. Structure. 1994 May 15;2(5):407-14. [PubMed ]
5. Alexeev D, Bury SM, Boys CW, Turner MA, Sawyer L, Ramsey AJ, Baxter HC, Baxter RL: Sequence and crystallization of Escherichia coli dethiobiotin synthetase, the penultimate enzyme of biotin biosynthesis. J Mol Biol. 1994 Jan 14;235(2):774-6. [PubMed ]
6. Yang G, Sandalova T, Lohman K, Lindqvist Y, Rendina AR: Active site mutants of Escherichia coli dethiobiotin synthetase: effects of mutations on enzyme catalytic and structural properties. Biochemistry. 1997 Apr 22;36(16):4751-60. [PubMed ]
7. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-74. [PubMed ]
8. Kack H, Gibson KJ, Lindqvist Y, Schneider G: Snapshot of a phosphorylated substrate intermediate by kinetic crystallography. Proc Natl Acad Sci U S A. 1998 May 12;95(10):5495-500. [PubMed ]
9. Kack H, Sandmark J, Gibson KJ, Schneider G, Lindqvist Y: Crystal structure of two quaternary complexes of dethiobiotin synthetase, enzyme-MgADP-AlF3-diaminopelargonic acid and enzyme-MgADP-dethiobiotin-phosphate; implications for catalysis. Protein Sci. 1998 Dec;7(12):2560-6. [PubMed ]

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. EC 2.7.1.33
2. Pantothenic acid kinase
3. Rts protein

MSIKEQTLMTPYLQFDRNQWAALRDSVPMTLSEDEIARLKGINEDLSLEEVAEIYLPLSR
LLNFYISSNLRRQAVLEQFLGTNGQRIPYIISIAGSVAVGKSTTARVLQALLSRWPEHRR
VELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVPNVTAPVYSHLIY
DVIPDGDKTVVQPDILILEGLNVLQSGMDYPHDPHHVFVSDFVDFSIYVDAPEDLLQTWY
INRFLKFREGAFTDPDSYFHNYAKLTKEEAIKTAMTLWKEINWLNLKQNILPTRERASLI
LTKSANHAVEEVRLRK

• ATP + (R)-pantothenate = ADP + (R)-4'-phosphopantothenate

• PRK (PF00485 )

• None

• None

• Cytoplasm (Probable)

GTGACGCGCCATGGCAAATATCGCTTTGCCGATAGAGCTATGACCGCCAGAAACATGCTT
ATGAGTATAAAAGAGCAAACGTTAATGACGCCTTACCTACAGTTTGACCGCAACCAGTGG
GCAGCTCTGCGTGATTCCGTACCTATGACGTTATCGGAAGATGAGATCGCCCGTCTCAAA
GGTATTAATGAAGATCTCTCGTTAGAAGAAGTTGCCGAGATCTATTTACCTTTGTCACGT
TTGCTGAACTTCTATATAAGCTCGAATCTGCGCCGTCAGGCAGTTCTGGAACAGTTTCTT
GGTACCAACGGGCAACGCATTCCTTACATTATCAGTATTGCTGGCAGTGTCGCGGTGGGG
AAAAGTACAACCGCCCGTGTATTGCAGGCGCTATTAAGCCGTTGGCCGGAACATCGTCGT
GTTGAACTGATCACTACAGATGGCTTCCTTCACCCTAATCAGGTTCTGAAAGAACGTGGT
CTGATGAAGAAGAAAGGCTTCCCGGAATCGTATGATATGCATCGCCTGGTGAAGTTTGTT
TCCGATCTCAAATCCGGCGTGCCAAACGTTACAGCACCTGTTTACTCACATCTTATTTAT
GATGTGATCCCGGATGGAGATAAAACGGTTGTTCAGCCTGATATTTTAATTCTTGAAGGG
TTAAATGTCTTACAGAGCGGGATGGATTATCCACACGATCCACATCATGTATTTGTTTCT
GATTTTGTCGATTTTTCGATATATGTTGATGCACCGGAAGACTTACTTCAGACATGGTAT
ATCAACCGTTTTCTGAAATTCCGCGAAGGGGCTTTTACCGACCCGGATTCCTATTTTCAT
AACTACGCGAAATTAACTAAAGAAGAAGCGATTAAGACTGCCATGACATTGTGGAAAGAG
ATCAACTGGCTGAACTTAAAGCAAAATATTCTACCTACTCGTGAGCGCGCCAGTTTAATC
CTGACGAAAAGTGCTAATCATGCGGTAGAAGAGGTCAGACTACGCAAATAA

1. Song WJ, Jackowski S: coaA and rts are allelic and located at kilobase 3532 on the Escherichia coli physical map. J Bacteriol. 1992 Mar;174(5):1705-6. [PubMed ]
2. Song WJ, Jackowski S: Cloning, sequencing, and expression of the pantothenate kinase (coaA) gene of Escherichia coli. J Bacteriol. 1992 Oct;174(20):6411-7. [PubMed ]
3. Flamm JA, Friesen JD, Otsuka AJ: The nucleotide sequence of the Escherichia coli rts gene. Gene. 1988 Dec 30;74(2):555-8. [PubMed ]
4. Blattner FR, Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL: Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes. Nucleic Acids Res. 1993 Nov 25;21(23):5408-17. [PubMed ]
5. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-74. [PubMed ]

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

MTGSLNRHSLLNGVKKMRIILCDTNEVVTNLWQESIPHAYIQNDKYLCIHHGHLQSLMDS
MRKGDAIHHGHSYAIVSPGNSYGYLGGGFDKALYNYFGGKPFETWFRNQLGGRYHTVGSA
TVVDLQRCLEEKTIECRDGIRYIIHVPTVVAPSAPIFNPQNPLKTGFEPVFNAMWNALMH
SPKDIDGLIIPGLCTGYAGVPPIISCKSMAFALRLYMAGDHISKELKNVLIMYYLQYPFE
PFFPESCKIECQKLGIDIEMLKSFNVEKDAIELLIPRRILTLDL

• None

• None

ATGACAGGATCTTTAAACAGACACTCACTTTTGAACGGGGTAAAAAAAATGAGAATAATA
TTATGCGATACAAACGAAGTAGTTACCAATCTCTGGCAGGAATCTATACCCCATGCATAT
ATTCAAAATGATAAGTATCTTTGTATTCATCATGGGCACCTTCAATCTCTTATGGATTCA
ATGCGTAAAGGTGATGCAATCCATCATGGCCACTCTTACGCAATTGTTTCACCTGGTAAC
TCGTATGGCTATCTTGGAGGAGGGTTCGATAAAGCTTTGTATAATTATTTCGGGGGAAAG
CCCTTTGAAACATGGTTCAGGAATCAGCTTGGAGGAAGATATCACACGGTCGGATCTGCT
ACAGTGGTTGACCTACAGCGATGTCTTGAAGAGAAAACAATTGAATGTAGAGATGGTATT
AGGTATATTATTCATGTTCCGACCGTTGTAGCCCCATCAGCTCCTATATTTAATCCGCAG
AATCCCCTCAAGACAGGGTTTGAACCGGTTTTCAACGCCATGTGGAATGCCTTGATGCAT
TCTCCAAAAGACATTGATGGTCTTATTATTCCTGGATTATGTACTGGGTATGCAGGTGTA
CCACCCATTATCAGTTGCAAGAGTATGGCCTTTGCGTTAAGACTATATATGGCGGGAGAT
CACATAAGCAAAGAATTGAAAAATGTGCTGATCATGTATTATTTGCAATATCCGTTTGAA
CCTTTTTTCCCGGAAAGTTGCAAAATAGAGTGCCAAAAACTAGGAATAGATATCGAAATG
CTGAAATCCTTTAATGTAGAAAAAGATGCAATAGAATTGCTCATTCCTAGAAGGATTTTG
ACCTTGGATTTATAA

1. Bowman S, Churcher C, Badcock K, Brown D, Chillingworth T, Connor R, Dedman K, Devlin K, Gentles S, Hamlin N, Hunt S, Jagels K, Lye G, Moule S, Odell C, Pearson D, Rajandream M, Rice P, Skelton J, Walsh S, Whitehead S, Barrell B: The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII. Nature. 1997 May 29;387(6632 Suppl):90-3. [PubMed ]

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. EC 3.1.27.5
2. Eosinophil-derived neurotoxin
3. Nonsecretory ribonuclease precursor
4. RNase 2
5. RNase UpI-2
6. Ribonuclease 2
7. Ribonuclease US

MVPKLFTSQICLLLLLGLLAVEGSLHVKPPQFTWAQWFETQHINMTSQQCTNAMQVINNY
QRRCKNQNTFLLTTFANVVNVCGNPNMTCPSNKTRKNCHHSGSQVPLIHCNLTTPSPQNI
SNCRYAQTPANMFYIVACDNRDQRRDPPQYPVVPVHLDRII

• Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates REFERENCE 1 AUTHORS Anfinsen, C.B. and White, F.H., Jr. TITLE The ribonucleases: occurrence, structure, and properties. JOURNAL In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 5, Academic Press, New York, 1961, p. 95-122. REFERENCE 2 [PMID:14247667] AUTHORS BEARD JR, RAZZELL WE. TITLE PURIFICATION OF ALKALINE RIBONUCLEASE II FROM MITOCHONDRIAL AND SOLUBLE FRACTIONS OF LIVER. JOURNAL J. Biol. Chem. 239 (1964) 4186-93. ORGANISM pig [GN:ssc], rat [GN:rno], cow [GN:bta]

• RnaseA (PF00074 )

• 1-27

• None

• Lysosome (Probable). Cytoplasmic granule. Note=Matrix of eosinophil's large specific granule

ATGGTTCCAAAACTGTTCACTTCCCAAATTTGTCTGCTTCTTCTGTTGGGGCTTCTGGCT
GTGGAGGGCTCACTCCATGTCAAACCTCCACAGTTTACCTGGGCTCAATGGTTTGAAACC
CAGCACATCAATATGACCTCCCAGCAATGCACCAATGCAATGCAGGTCATTAACAATTAT
CAACGGCGATGCAAAAACCAAAATACTTTCCTTCTTACAACTTTTGCTAACGTAGTTAAT
GTTTGTGGTAACCCAAATATGACCTGTCCTAGTAACAAAACTCGCAAAAATTGTCACCAC
AGTGGAAGCCAGGTGCCTTTAATCCACTGTAACCTCACAACTCCAAGTCCACAGAATATT
TCAAACTGCAGGTATGCGCAGACACCAGCAAACATGTTCTATATAGTTGCATGTGACAAC
AGAGATCAACGACGAGACCCTCCACAGTATCCGGTGGTTCCAGTTCACCTGGATAGAATC
ATCTAA

1. Zhang J, Rosenberg HF: Sequence variation at two eosinophil-associated ribonuclease loci in humans. Genetics. 2000 Dec;156(4):1949-58. [PubMed ]
2. Leonidas DD, Boix E, Prill R, Suzuki M, Turton R, Minson K, Swaminathan GJ, Youle RJ, Acharya KR: Mapping the ribonucleolytic active site of eosinophil-derived neurotoxin (EDN). High resolution crystal structures of EDN complexes with adenylic nucleotide inhibitors. J Biol Chem. 2001 May 4;276(18):15009-17. Epub 2001 Jan 11. [PubMed ]
3. Yang D, Rosenberg HF, Chen Q, Dyer KD, Kurosaka K, Oppenheim JJ: Eosinophil-derived neurotoxin (EDN), an antimicrobial protein with chemotactic activities for dendritic cells. Blood. 2003 Nov 1;102(9):3396-403. Epub 2003 Jul 10. [PubMed ]
4. Sakakibara R, Hashida K, Kitahara T, Ishiguro M: Characterization of a unique nonsecretory ribonuclease from urine of pregnant women. J Biochem (Tokyo). 1992 Mar;111(3):325-30. [PubMed ]
5. Hamann KJ, Ten RM, Loegering DA, Jenkins RB, Heise MT, Schad CR, Pease LR, Gleich GJ, Barker RL: Structure and chromosome localization of the human eosinophil-derived neurotoxin and eosinophil cationic protein genes: evidence for intronless coding sequences in the ribonuclease gene superfamily. Genomics. 1990 Aug;7(4):535-46. [PubMed ]
6. Hamann KJ, Barker RL, Loegering DA, Pease LR, Gleich GJ: Sequence of human eosinophil-derived neurotoxin cDNA: identity of deduced amino acid sequence with human nonsecretory ribonucleases. Gene. 1989 Nov 15;83(1):161-7. [PubMed ]
7. Rosenberg HF, Tenen DG, Ackerman SJ: Molecular cloning of the human eosinophil-derived neurotoxin: a member of the ribonuclease gene family. Proc Natl Acad Sci U S A. 1989 Jun;86(12):4460-4. [PubMed ]
8. Barker RL, Loegering DA, Ten RM, Hamann KJ, Pease LR, Gleich GJ: Eosinophil cationic protein cDNA. Comparison with other toxic cationic proteins and ribonucleases. J Immunol. 1989 Aug 1;143(3):952-5. [PubMed ]
9. Beintema JJ, Hofsteenge J, Iwama M, Morita T, Ohgi K, Irie M, Sugiyama RH, Schieven GL, Dekker CA, Glitz DG: Amino acid sequence of the nonsecretory ribonuclease of human urine. Biochemistry. 1988 Jun 14;27(12):4530-8. [PubMed ]
10. Sorrentino S, Tucker GK, Glitz DG: Purification and characterization of a ribonuclease from human liver. J Biol Chem. 1988 Nov 5;263(31):16125-31. [PubMed ]
11. 3458170 Gleich GJ, Loegering DA, Bell MP, Checkel JL, Ackerman SJ, McKean DJ: Biochemical and functional similarities between human eosinophil-derived neurotoxin and eosinophil cationic protein: homology with ribonuclease. Proc Natl Acad Sci U S A. 1986 May;83(10):3146-50.
12. 3926759 Niwata Y, Ohgi K, Sanda A, Takizawa Y, Irie M: Purification and properties of bovine kidney ribonucleases. J Biochem (Tokyo). 1985 Mar;97(3):923-34.
13. 7547911 de Beer T, Vliegenthart JF, Loffler A, Hofsteenge J: The hexopyranosyl residue that is C-glycosidically linked to the side chain of tryptophan-7 in human RNase Us is alpha-mannopyranose. Biochemistry. 1995 Sep 19;34(37):11785-9.
14. 7947762 Hofsteenge J, Muller DR, de Beer T, Loffler A, Richter WJ, Vliegenthart JF: New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us. Biochemistry. 1994 Nov 22;33(46):13524-30.
15. 8759319 Mosimann SC, Newton DL, Youle RJ, James MN: X-ray crystallographic structure of recombinant eosinophil-derived neurotoxin at 1.83 A resolution. J Mol Biol. 1996 Jul 26;260(4):540-52.
16. 9450956 Krieg J, Hartmann S, Vicentini A, Glasner W, Hess D, Hofsteenge J: Recognition signal for C-mannosylation of Trp-7 in RNase 2 consists of sequence Trp-x-x-Trp. Mol Biol Cell. 1998 Feb;9(2):301-9.

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. ADP-glucose pyrophosphorylase
2. ADP-glucose synthase
3. AGPase B
4. Alpha-D-glucose-1-phosphate adenyl transferase
5. EC 2.7.7.27
6. Glucose-1-phosphate adenylyltransferase small subunit, chloroplast precursor

MAASIGALKSSPSSNNCINERRNDSTRAVSSRNLSFSSSHLAGDKLMPVSSLRSQGVRFN
VRRSPMIVSPKAVSDSQNSQTCLDPDASRSVLGIILGGGAGTRLYPLTKKRAKPAVPLGA
NYRLIDIPVSNCLNSNISKIYVLTQFNSASLNRHLSRAYASNMGGYKNEGFVEVLAAQQS
PENPDWFQGTADAVRQYLWLFEEHTVLEYLILAGDHLYRMDYEKFIQAHRETDADITVAA
LPMDEKRATAFGLMKIDEEGRIIEFAEKPQGEQLQAMKVDTTILGLDDKRAKEMPFIASM
GIYVISKDVMLNLLRDKFPGANDFGSEVIPGATSLGMRVQAYLYDGYWEDIGTIEAFYNA
NLGITKKPVPDFSFYDRSAPIYTQPRYLPPSKMLDADVTDSVIGEGCVIKNCKIHHSVVG
LRSCISEGAIIEDSLLMGADYYETDADRKLLAAKGSVPIGIGKNCHIKRAIIDKNARIGD
NVKIINKDNVQEAARETDGYFIKSGIVTVIKDALIPSGIII

• ATP + alpha-D-glucose 1-phosphate = diphosphate + ADP-glucose

• NTP_transferase (PF00483 )

• None

• None

• Plastid
• amyloplast. Note=Found in the chloroplast in leaf. Found in the plast
• chloroplast. Plastid

ATGGCGGCTTCCATTGGAGCCTTAAAATCTTCACCTTCTTCTAACAATTGCATCAATGAG
AGAAGAAATGATTCTACACGTGCTGTATCCAGCAGAAATCTCTCATTTTCATCTTCTCAT
CTCGCCGGAGACAAGTTGATGCCTGTATCGTCCTTACGTTCCCAAGGAGTCCGATTCAAT
GTGAGAAGAAGTCCAATGATTGTGTCGCCAAAGGCTGTTTCTGATTCGCAGAATTCACAG
ACATGTCTAGACCCAGATGCTAGCCGGAGTGTTTTGGGAATTATTCTTGGAGGTGGAGCT
GGGACCCGACTTTATCCTCTAACTAAAAAAAGAGCAAAGCCAGCTGTTCCACTTGGAGCA
AATTATCGTCTGATTGACATTCCTGTAAGCAACTGCTTGAACAGTAACATATCCAAGATC
TATGTTCTCACACAATTCAACTCTGCCTCTCTGAATCGCCACCTTTCACGAGCATATGCT
AGCAACATGGGAGGATACAAAAACGAGGGCTTTGTGGAAGTTCTTGCTGCTCAACAAAGT
CCAGAGAACCCCGATTGGTTCCAGGGCACGGCTGATGCTGTCAGACAATATCTGTGGTTG
TTTGAGGAGCATACTGTTCTTGAATACCTTATACTTGCTGGAGATCATCTGTATCGAATG
GATTATGAAAAGTTTATTCAAGCCCACAGAGAAACAGATGCTGATATTACCGTTGCCGCA
CTGCCAATGGACGAGAAGCGTGCCACTGCATTTGGTCTCATGAAGATTGACGAAGAAGGA
CGCATTATTGAATTTGCAGAGAAACCGCAAGGAGAGCAATTGCAAGCAATGAAAGTGGAT
ACTACCATTTTAGGTCTTGATGACAAGAGAGCTAAAGAAATGCCTTTCATTGCCAGTATG
GGTATATATGTCATTAGCAAAGACGTGATGTTAAACCTACTTCGTGACAAGTTCCCTGGG
GCCAATGATTTTGGTAGTGAAGTTATTCCTGGTGCAACTTCACTTGGGATGAGAGTGCAA
GCTTATTTATATGATGGGTACTGGGAAGATATTGGTACCATTGAAGCTTTCTACAATGCC
AATTTGGGCATTACAAAAAAGCCGGTGCCAGATTTTAGCTTTTACGACCGATCAGCCCCA
ATCTACACCCAACCTCGATATCTACCACCATCAAAAATGCTTGATGCTGATGTCACAGAT
AGTGTCATTGGTGAAGGTTGTGTGATCAAGAACTGTAAGATTCATCATTCCGTGGTTGGA
CTCAGATCATGCATATCAGAGGGAGCAATTATAGAAGACTCACTTTTGATGGGGGCAGAT
TACTATGAGACTGATGCTGACAGGAAGTTGTTGGCTGCAAAGGGCAGTGTCCCAATTGGC
ATCGGCAAGAATTGTCACATTAAAAGAGCCATTATCGACAAGAATGCCCGTATAGGGGAC
AATGTGAAGATCATTAACAAAGACAACGTTCAAGAAGCGGCTAGGGAAACAGATGGATAC
TTCATCAAGAGTGGGATTGTCACCGTCATCAAGGATGCTTTGATTCCAAGTGGAATCATC
ATCTGA

1. du Jardin P, Berhin A: Isolation and sequence analysis of a cDNA clone encoding a subunit of the ADP-glucose pyrophosphorylase of potato tuber amyloplasts. Plant Mol Biol. 1991 Feb;16(2):349-51. [PubMed ]
2. Nakata PA, Greene TW, Anderson JM, Smith-White BJ, Okita TW, Preiss J: Comparison of the primary sequences of two potato tuber ADP-glucose pyrophosphorylase subunits. Plant Mol Biol. 1991 Nov;17(5):1089-93. [PubMed ]
3. Muller-Rober BT, Kossmann J, Hannah LC, Willmitzer L, Sonnewald U: One of two different ADP-glucose pyrophosphorylase genes from potato responds strongly to elevated levels of sucrose. Mol Gen Genet. 1990 Oct;224(1):136-46. [PubMed ]
4. Nakata PA, Anderson JM, Okita TW: Structure and expression of the potato ADP-glucose pyrophosphorylase small subunit. J Biol Chem. 1994 Dec 9;269(49):30798-807. [PubMed ]

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. Myosin II heavy chain, non muscle

MNPIHDRTSDYHKYLKVKQGDSDLFKLTVSDKRYIWYNPDPKERDSYECGEIVSETSDSF
TFKTVDGQDRQVKKDDANQRNPIKFDGVEDMSELSYLNEPAVFHNLRVRYNQDLIYTYSG
LFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGE
SGAGKTENTKKVIQYLASVAGRNQANGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFG
KFIEIQFNSAGFISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAG
PESFNYLNQSGCVDIKGVSDSEEFKITRQAMDIVGFSQEEQMSIFKIIAGILHLGNIKFE
KGAGEGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSSSSRDA
LVKALYGRLFLWLVKKINNVLCQERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQ
FFNHHMFKLEQEEYLKEKINWTFIDFGLDSQATIDLIDGRQPPGILALLDEQSVFPNATD
NTLITKLHSHFSKKNAKYEEPRFSKTEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCF
KDSSDNVVTKLFNDPNIASRAKKGANFITVAAQYKEQLASLMATLETTNPHFVRCIIPNN
KQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRDAEDSQ
KATDAVLKHLNIDPEQYRFGITKIFFRAGQLARIEEAREQRISEIIKAIQAATRGWIARK
VYKQAREHTVAARIIQQNLRAYIDFKSWPWWKLFSKARPLLKRRNFEKEIKEKEREILEL
KSNLTDSTTQKDKLEKSLKDTESNVLDLQRQLKAEKETLKAMYDSKDALEAQKRELEIRV
EDMESELDEKKLALENLQNQKRSVEEKVRDLEEELQEEQKLRNTLEKLKKKYEEELEEMK
RVNDGQSDTISRLEKIKDELQKEVEELTESFSEESKDKGVLEKTRVRLQSELDDLTVRLD
SETKDKSELLRQKKKLEEELKQVQEALAAETAAKLAQEAANKKLQGEYTELNEKFNSEVT
ARSNVEKSKKTLESQLVAVNNELDEEKKNRDALEKKKKALDAMLEEMKDQLESTGGEKKS
LYDLKVKQESDMEALRNQISELQSTIAKLEKIKSTLEGEVARLQGELEAEQLAKSNVEKQ
KKKVELDLEDKSAQLAEETAAKQALDKLKKKLEQELSEVQTQLSEANNKNVNSDSTNKHL
ETSFNNLKLELEAEQKAKQALEKKRLGLESELKHVNEQLEEEKKQKESNEKRKVDLEKEV
SELKDQIEEEVASKKAVTEAKNKKESELDEIKRQYADVVSSRDKSVEQLKTLQAKNEELR
NTAEEAEGQLDRAERSKKKAEFDLEEAVKNLEEETAKKVKAEKAMKKAETDYRSTKSELD
DAKNVSSEQYVQIKRLNEELSELRSVLEEADERCNSAIKAKKTAESALESLKDEIDAANN
AKAKAERKSKELEVRVAELEESLEDKSGTVNVEFIRKKDAEIDDLRARLDRETESRIKSD
EDKKNTRKQFADLEAKVEEAQREVVTIDRLKKKLESDIIDLSTQLDTETKSRIKIEKSKK
KLEQTLAERRAAEEGSSKAADEEIRKQVWQEVDELRAQLDSERAALNASEKKIKSLVAEV
DEVKEQLEDEILAKDKLVKAKRALEVELEEVRDQLEEEEDSRSELEDSKRRLTTEVEDIK
KKYDAEVEQNTKLDEAKKKLTDDVDTLKKQLEDEKKKLNESERAKKRLESENEDFLAKLD
AEVKNRSRAEKDRKKYEKDLKDTKYKLNDEAATKTQTEIGAAKLEDQIDELRSKLEQEQA
KATQADKSKKTLEGEIDNLRAQIEDEGKIKMRLEKEKRALEGELEELRETVEEAEDSKSE
AEQSKRLVELELEDARRNLQKEIDAKEIAEDAKSNLQREIVEAKGRLEEESIARTNSDRS
RKRLEAEIDALTAQVDAEQKAKNQQIKENKKIETELKEYRKKFGESEKTKTKEFLVVEKL
ETDYKRAKKEAADEQQQRLTVENDLRKHLSEISLLKDAIDKLQRDHDKTKRELETETASK
IEMQRKMADFFGGFKA

• Myosin_head (PF00063 )
• IQ (PF00612 )
• Myosin_tail_1 (PF01576 )
• Myosin_N (PF02736 )

• None

• None

• Cytoplasm
• cell cortex. Note=Highest concentration in the posterior cell cortex

ATGAATCCAATTCATGATAGAACTTCAGATTATCACAAATACTTAAAAGTTAAACAAGGT
GATTCTGATTTATTTAAACTTACTGTTTCAGATAAGAGATACATTTGGTATAATCCAGAT
CCAAAAGAAAGAGATTCATATGAATGTGGTGAAATTGTTTCAGAAACCTCTGATTCTTTC
ACATTCAAAACCGTTGATGGTCAAGACAGACAAGTCAAAAAGGATGATGCCAATCAACGT
AATCCAATCAAATTCGATGGTGTCGAAGATATGTCTGAATTATCATACCTCAATGAACCA
GCAGTTTTCCACAATCTCCGTGTTCGTTACAATCAAGATTTAATTTACACCTATTCAGGT
CTCTTTTTGGTTGCCGTCAATCCATTCAAGAGAATTCCAATCTACACTCAAGAGATGGTT
GATATCTTCAAAGGTCGTAGAAGAAATGAAGTTGCCCCACATATTTTCGCCATTTCTGAT
GTTGCCTATCGTTCAATGTTAGATGATCGTCAAAATCAATCACTCTTAATCACTGGTGAA
TCTGGTGCTGGTAAGACTGAAAACACCAAAAAGGTCATTCAATATCTTGCATCTGTCGCT
GGTCGTAATCAAGCCAATGGTAGTGGTGTATTGGAACAACAAATTCTCCAAGCCAATCCA
ATCCTTGAAGCTTTTGGTAATGCCAAAACCACCCGTAACAACAATTCATCTCGTTTCGGT
AAATTCATTGAAATTCAATTCAACAATGCTGGTTTCATTAGTGGTGCTTCAATTCAATCC
TACCTTTTAGAGAAATCACGTGTCGTTTTCCAATCTGAAACCGAACGTAATTATCACATT
TTCTATCAACTCTTAGCTGGTGCCACCGCCGAAGAAAAGAAAGCTCTTCACTTGGCTGGT
CCAGAATCATTCAACTACTTAAATCAAAGTGGTTATGTTGATATCAAAGGTGTCTCTGAT
AGTGAAGAATTCAAAATCACTCGTCAAGCTATGGACATTGTTGGTTTCTCACAAGAAGAA
CAAATGTCAATCTTTAAGATCATTGCTGGTATCTTACATTTAGGTAACATCAAATTCGAA
AAAGGTGCTGGTGAAGGTGCTGTCCTCAAAGACAAAACCGCCCTCAACGCTGCTTCAACC
GTCTTTGGTGTCAATCCATCAGTCCTTGAAAAGGCTCTCATGGAACCACGTATTTTAGCC
GGTCGTGATTTAGTTGCTCAACATCTCAACGTTGAAAAATCCTCATCATCAAGAGACGCT
CTTGTCAAAGCTCTCTATGGTCGTCTTTTCCTCTGGTTGGTCAAAAAGATCAACAATGTC
CTCTGTCAAGAGAGAAAAGCTTACTTTATTGGTGTTTTGGATATTTCAGGTTTTGAAATT
TTCAAAGTCAATTCATTCGAACAATTATGTATCAATTATACCAATGAAAAACTCCAACAA
TTCTTCAATCACCATATGTTCAAATTGGAACAAGAAGAATATCTTAAAGAGAAAATCAAT
TGGACTTTCATCGATTTTGGTCTTGATTCACAAGCCACTATCGATTTAATTGATGGTCGT
CAACCACCAGGTATTTTAGCTCTTTTGGATGAACAATCTGTTTTCCCAAATGCCACCGAT
AATACTTTAATCACCAAACTCCACAGTCACTTTAGCAAGAAGAACGCCAAATACGAAGAA
CCACGTTTCTCCAAAACCGAATTTGGTGTTACCCATTATGCTGGTCAAGTCATGTATGAG
ATTCAAGATTGGTTAGAAAAGAACAAAGATCCATTACAACAAGATCTCGAACTTTGCTTC
AAAGATTCATCAGACAACGTTGTCACCAAACTTTTCAATGATCCAAACATTGCCAGTCGT
GCAAAGAAAGGTGCAAACTTTATCACTGTCGCCGCTCAATACAAGGAACAATTAGCCTCA
CTCATGGCNACCCTTGAAACCACCAACCCACATTTCGTTCGTTGTATCATTCCAAACAAC
AAACAATTACCAGCCAAACTCGAAGATAAAGTTGTCCTCGACCAATTACGTTGCAATGGT
GTCCTCGAAGGTATTCGTATTACTCGTAAAGGTTTCCCAAATCGTATTATCTATGCCGAT
TTCGTCAAACGTTACTATTTATTAGCTCCAAACGTTCCAAGAGACGCTGAAGACTCACAA
AAAGCCACCGATGCTGTTCTCAAACATCTTAACATTGATCCAGAACAATATCGTTTCGGT
ATCACCAAGATTTTCTTCCGTGCCGGTCAATTAGCTCGTATTGAAGAAGCTCGTGAACAA
CGTATCTCTGAAATCATCAAAGCCATTCAAGCTGCCACTCGTGGTTGGATCGCTCGTAAA
GTCTACAAACAAGCACGTGAACACACTGTTGCTGCTCGTATCATCCAACAAAATCTCCGT
GCTTACATTGATTTCAAATCATGGCCATGGTGGAAACTCTTCTCAAAGGCTCGTCCATTA
TTAAAGAGAAGAAACTTTGAAAAGGAAATCAAAGAAAAGGAAAGAGAAATCTTAGAACTC
AAATCTAATCTCACCGACTCTACCACTCAAAAGGATAAATTAGAGAAATCACTCAAAGAT
ACTGAATCCAATGTACTCGATCTCCAACGTCAACTCAAAGCTGAAAAAGAAACCCTCAAA
GCTATGTACGATAGCAAGGATGCCTTAGAAGCTCAAAAACGTGAATTAGAAATCCGTGTT
GAAGATATGGAATCTGAACTCGACGAAAAGAAATTAGCTTTGGAAAACCTCCAAAACCAA
AAACGTTCAGTCGAAGAAAAAGTCAGAGACTTGGAAGAAGAATTACAAGAGGAACAAAAA
TTACGTAATACCCTTGAAAAATTAAAGAAGAAATACGAAGAGGAATTAGAAGAAATGAAA
CGTGTCAATGACGGTCAATCTGATACCATCTCTCGTTTAGAAAAAATCAAGGATGAATTA
CAAAAAGAAGTTGAAGAATTAACTGAAAGCTTCTCTGAAGAATCCAAAGATAAAGGTGTT
TTAGAAAAGACTCGTGTCAGATTACAAAGTGAATTGGATGATTTAACCGTAAGATTAGAT
AGTGAAACCAAAGACAAATCTGAATTACTCCGTCAAAAGAAGAAACTCGAAGAAGAACTC
AAACAAGTTCAAGAAGCTCTCGCTGCTGAAACTGCTGCTAAATTAGCTCAAGAAGCTGCC
AACAAGAAATTACAAGGTGAATACACTGAATTAAACGAAAAATTCAACTCTGAAGTCACT
GCTCGTTCAAATGTTGAAAAATCAAAGAAGACCCTCGAAAGTCAATTGGTTGCCGTCAAC
AACGAATTAGATGAAGAGAAGAAGAATCGTGATGCCCTTGAAAAGAAGAAGAAAGCTTTA
GACGCTATGTTAGAGGAAATGAAAGATCAATTAGAATCCACTGGTGGTGAAAAGAAATCA
CTCTATGATCTCAAAGTTAAACAAGAATCAGATATGGAGGCTTTACGTAATCAAATCTCT
GAACTCCAATCAACTATTGCCAAATTAGAAAAGATTAAATCCACTTTAGAAGGTGAAGTT
GCTCGTTTACAAGGTGAATTAGAAGCTGAACAATTAGCCAAATCCAACGTTGAAAAACAA
AAGAAGAAGGTTGAATTAGATTTGGAAGATAAATCTGCTCAATTAGCTGAAGAAACCGCC
GCCAAACAAGCTTTAGATAAATTAAAGAAGAAATTAGAACAAGAATTATCTGAAGTTCAA
ACTCAACTCTCTGAAGCCAACAACAAGAATGTCAACTCTGATTCCACCAACAAACATTTG
GAAACCTCTTTCAATAATCTCAAATTAGAATTGGAAGCTGAACAAAAAGCCAAACAAGCT
CTTGAAAAGAAACGTCTCGGTTTAGAATCTGAATTAAAACATGTCAATGAACAATTGGAA
GAAGAAAAGAAACAAAAAGAATCCAACGAAAAACGTAAAGTTGATTTAGAAAAGGAAGTC
TCTGAACTCAAAGACCAAATTGAAGAAGAAGTTGCCTCCAAGAAAGCTGTCACTGAAGCC
AAGAACAAGAAAGAATCTGAACTCGATGAAATCAAGAGACAATATGCTGATGTTGTTTCA
TCTCGTGATAAATCAGTCGAACAATTAAAGACCTTACAAGCCAAGAATGAAGAATTAAGA
AACACTGCTGAAGAAGCTGAAGGTCAATTAGATCGTGCTGAAAGAAGCAAGAAGAAAGCT
GAATTCGATTTAGAAGAAGCCGTCAAGAATTTGGAAGAAGAAACCGCCAAGAAAGTTAAA
GCTGAAAAAGCCATGAAGAAAGCTGAAACTGACTATCGTTCAACCAAATCTGAATTGGAT
GATGCCAAGAACGTCTCATCTGAACAATACGTTCAAATCAAACGTCTCAATGAAGAACTC
TCTGAATTACGTAGTGTCTTGGAAGAAGCTGATGAACGTTGTAACTCTGCCATCAAAGCA
AAGAAAACCGCTGAATCTGCTTTAGAATCATTGAAAGATGAAATTGATGCTGCCAACAAC
GCCAAAGCTAAAGCTGAAAGAAAATCCAAAGAATTAGAAGTTCGTGTCGCTGAATTAGAA
GAATCATTGGAAGATAAATCTGGTACCGTCAATGTTGAATTCATTCGTAAGAAGGATGCT
GAAATCGATGATTTACGTGCTCGTCTCGACAGAGAAACTGAAAGTCGTATCAAATCTGAT
GAAGATAAGAAGAACACTCGTAAACAATTTGCTGATTTAGAAGCTAAGGTTGAAGAAGCT
CAACGTGAAGTTGTCACCATCGATAGATTAAAGAAGAAACTCGAATCTGATATCATCGAT
TTATCAACTCAATTGGATACTGAAACCAAATCTCGTATCAAGATTGAAAAGAGCAAGAAG
AAACTCGAACAAACTCTCGCTGAAAGAAGAGCCGCTGAAGAAGGTTCATCCAAAGCTGCT
GATGAAGAAATTCGTAAACAAGTCTGGCAAGAGGTTGATGAGTTACGTGCTCAATTAGAT
AGTGAACGTGCTGCTCTCAATGCTTCTGAAAAGAAGATCAAATCTTTGGTCGCCGAAGTC
GATGAAGTCAAGGAACAATTAGAAGATGAAATCCTCGCCAAAGACAAATTAGTCAAAGCC
AAACGTGCCCTCGAAGTTGAATTAGAGGAAGTCAGAGACCAATTAGAAGAGGAAGAAGAT
TCTCGTTCAGAATTAGAAGACAGCAAACGTCGTCTCACTACTGAAGTCGAAGATATCAAG
AAGAAATACGATGCTGAAGTCGAACAAAACACCAAATTAGATGAAGCCAAGAAGAAACTC
ACTGATGATGTTGATACTCTCAAGAAACAATTGGAAGATGAAAAGAAGAAATTGAACGAA
TCTGAACGTGCCAAGAAACGTTTAGAATCTGAAAATGAAGATTTCCTTGCCAAACTTGAT
GCTGAAGTTAAGAATCGTTCACGTGCTGAAAAGGATCGTAAGAAATACGAAAAGGATCTC
AAGGATACCAAATACAAATTAAACGACGAAGCTGCCACCAAGACTCAAACCGAAATTGGT
GCCGCCAAACTCGAAGATCAAATCGATGAATTACGTTCCAAACTTGAACAAGAACAAGCC
AAAGCCACTCAAGCCGATAAGAGTAAGAAGACTTTGGAAGGTGAAATTGACAACTTACGT
GCTCAAATCGAAGATGAAGGTAAGATCAAGATGAGATTAGAAAAAGAAAAACGTGCTCTC
GAAGGTGAATTAGAAGAATTAAGAGAAACCGTTGAAGAAGCTGAAGACTCTAAATCTGAA
GCTGAACAATCCAAACGTTTAGTCGAATTAGAATTAGAAGATGCTCGTCGTAACCTCCAA
AAAGAAATCGATGCCAAAGAAATCGCTGAAGATGCCAAATCTAACCTCCAACGTGAAATC
GTCGAAGCCAAAGGTCGTCTCGAAGAAGAATCCATCGCTCGTACCAACTCTGATCGTTCA
AGAAAGAGACTCGAAGCTGAAATTGATGCCCTCACTGCTCAAGTTGATGCTGAACAAAAA
GCCAAGAATCAACAAATCAAAGAAAACAAGAAGATCGAAACCGAACTCAAAGAATACAGA
AAGAAATTCGGCGAATCAGAAAAGACCAAGACCAAAGAATTCCTCGTTGTCGAAAAACTC
GAAACAGATTACAAGAGAGCCAAGAAAGAAGCTGCTGATGAACAACAACAACGTCTTACT
GTTGAAAACGATCTCCGTAAACACCTCAGTGAAATCTCATTACTCAAAGATGCCATTGAT
AAGTTACAACGTGATCACGATAAGACCAAACGTGAATTGGAAACAGAAACTGCCAGCAAA
ATCGAAATGCAAAGAAAGATGGCCGATTTCTTTGGTGGTTTCAAAGCTTAA

1. Luck-Vielmetter D, Schleicher M, Grabatin B, Wippler J, Gerisch G: Replacement of threonine residues by serine and alanine in a phosphorylatable heavy chain fragment of Dictyostelium myosin II. FEBS Lett. 1990 Aug 20;269(1):239-43. [PubMed ]
2. Wagle G, Noegel A, Scheel J, Gerisch G: Phosphorylation of threonine residues on cloned fragments of the Dictyostelium myosin heavy chain. FEBS Lett. 1988 Jan 18;227(1):71-5. [PubMed ]
3. Warrick HM, De Lozanne A, Leinwand LA, Spudich JA: Conserved protein domains in a myosin heavy chain gene from Dictyostelium discoideum. Proc Natl Acad Sci U S A. 1986 Dec;83(24):9433-7. [PubMed ]
4. DeLozanne A, Lewis M, Spudich JA, Leinwand LA: Cloning and characterization of a nonmuscle myosin heavy chain cDNA. Proc Natl Acad Sci U S A. 1985 Oct;82(20):6807-10. [PubMed ]
5. Fisher AJ, Smith CA, Thoden JB, Smith R, Sutoh K, Holden HM, Rayment I: X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4-. Biochemistry. 1995 Jul 18;34(28):8960-72. [PubMed ]
6. Smith CA, Rayment I: X-ray structure of the magnesium(II)-pyrophosphate complex of the truncated head of Dictyostelium discoideum myosin to 2.7 A resolution. Biochemistry. 1995 Jul 18;34(28):8973-81. [PubMed ]
7. Smith CA, Rayment I: X-ray structure of the magnesium(II).ADP.vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 A resolution. Biochemistry. 1996 Apr 30;35(17):5404-17. [PubMed ]
8. Gulick AM, Bauer CB, Thoden JB, Rayment I: X-ray structures of the MgADP, MgATPgammaS, and MgAMPPNP complexes of the Dictyostelium discoideum myosin motor domain. Biochemistry. 1997 Sep 30;36(39):11619-28. [PubMed ]
9. Bauer CB, Kuhlman PA, Bagshaw CR, Rayment I: X-ray crystal structure and solution fluorescence characterization of Mg.2'(3')-O-(N-methylanthraniloyl) nucleotides bound to the Dictyostelium discoideum myosin motor domain. J Mol Biol. 1997 Dec 5;274(3):394-407. [PubMed ]

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. EC 3.1.27.5
2. RNase 1
3. RNase A
4. Ribonuclease pancreatic precursor

MALKSLVLLSLLVLVLLLVRVQPSLGKETAAAKFERQHMDSSTSAASSSNYCNQMMKSRN
LTKDRCKPVNTFVHESLADVQAVCSQKNVACKNGQTNCYQSYSTMSITDCRETGSSKYPN
CAYKTTQANKHIIVACEGNPYVPVHFDASV

• Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates REFERENCE 1 AUTHORS Anfinsen, C.B. and White, F.H., Jr. TITLE The ribonucleases: occurrence, structure, and properties. JOURNAL In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 5, Academic Press, New York, 1961, p. 95-122. REFERENCE 2 [PMID:14247667] AUTHORS BEARD JR, RAZZELL WE. TITLE PURIFICATION OF ALKALINE RIBONUCLEASE II FROM MITOCHONDRIAL AND SOLUBLE FRACTIONS OF LIVER. JOURNAL J. Biol. Chem. 239 (1964) 4186-93. ORGANISM pig [GN:ssc], rat [GN:rno], cow [GN:bta]

• RnaseA (PF00074 )

• 1-26

• None

• Secreted protein

ATGGCTCTGAAGTCCCTGGTCCTGTTGTCGCTGTTGGTCCTGGTGCTGCTGCTGGTGCGG
GTCCAGCCTTCCCTGGGCAAGGAAACTGCAGCAGCCAAGTTTGAGCGGCAGCACATGGAC
TCCAGCACTTCCGCTGCCAGCAGCTCCAACTACTGTAACCAGATGATGAAGAGCCGGAAC
CTGACCAAAGATCGATGCAAGCCAGTGAACACCTTTGTGCACGAGTCCCTGGCTGATGTC
CAGGCCGTGTGCTCCCAGAAAAATGTTGCCTGCAAGAATGGGCAGACCAATTGCTACCAG
AGCTACTCCACCATGAGCATCACCGACTGCCGTGAGACCGGCAGCTCCAAGTACCCCAAC
TGTGCCTACAAGACCACCCAGGCGAATAAACACATCATTGTGGCTTGTGAGGGAAACCCG
TACGTGCCAGTCCACTTTGATGCTTCAGTGTAG

1. Rico M, Santoro J, Gonzalez C, Bruix M, Neira JL, Nieto JL, Herranz J: 3D structure of bovine pancreatic ribonuclease A in aqueous solution: an approach to tertiary structure determination from a small basis of 1H NMR NOE correlations. J Biomol NMR. 1991 Sep;1(3):283-98. [PubMed ]
2. Robertson AD, Purisima EO, Eastman MA, Scheraga HA: Proton NMR assignments and regular backbone structure of bovine pancreatic ribonuclease A in aqueous solution. Biochemistry. 1989 Jul 11;28(14):5930-8. [PubMed ]
3. Rico M, Bruix M, Santoro J, Gonzalez C, Neira JL, Nieto JL, Herranz J: Sequential 1H-NMR assignment and solution structure of bovine pancreatic ribonuclease A. Eur J Biochem. 1989 Aug 15;183(3):623-38. [PubMed ]
4. Carsana A, Confalone E, Palmieri M, Libonati M, Furia A: Structure of the bovine pancreatic ribonuclease gene: the unique intervening sequence in the 5' untranslated region contains a promoter-like element. Nucleic Acids Res. 1988 Jun 24;16(12):5491-502. [PubMed ]
5. Wlodawer A, Svensson LA, Sjolin L, Gilliland GL: Structure of phosphate-free ribonuclease A refined at 1.26 A. Biochemistry. 1988 Apr 19;27(8):2705-17. [PubMed ]
6. McPherson A, Brayer G, Cascio D, Williams R: The mechanism of binding of a polynucleotide chain to pancreatic ribonuclease. Science. 1986 May 9;232(4751):765-8. [PubMed ]
7. Carlisle CH, Palmer RA, Mazumdar SK, Gorinsky BA, Yeates DG: The structure of ribonuclease at 2-5 Angstrom resolution. J Mol Biol. 1974 May 5;85(1):1-18. [PubMed ]
8. Wyckoff HW, Tsernoglou D, Hanson AW, Knox JR, Lee B, Richards FM: The three-dimensional structure of ribonuclease-S. Interpretation of an electron density map at a nominal resolution of 2 A. J Biol Chem. 1970 Jan 25;245(2):305-28. [PubMed ]
9. Shall S, Barnard EA: Heavy atom-labelled derivatives of bovine pancreatic ribonuclease. I. Specific reactions of ribonuclease with N-acetylhomocysteine thiolactone and silver ion. J Mol Biol. 1969 Apr;41(2):237-51. [PubMed ]
10. Wlodawer A, Bott R, Sjolin L: The refined crystal structure of ribonuclease A at 2.0 A resolution. J Biol Chem. 1982 Feb 10;257(3):1325-32. [PubMed ]
11. 7479688 delCardayre SB, Ribo M, Yokel EM, Quirk DJ, Rutter WJ, Raines RT: Engineering ribonuclease A: production, purification and characterization of wild-type enzyme and mutants at Gln11. Protein Eng. 1995 Mar;8(3):261-73.
12. 8587129 Confalone E, Beintema JJ, Sasso MP, Carsana A, Palmieri M, Vento MT, Furia A: Molecular evolution of genes encoding ribonucleases in ruminant species. J Mol Evol. 1995 Dec;41(6):850-8.
13. 9154942 Leonidas DD, Shapiro R, Irons LI, Russo N, Acharya KR: Crystal structures of ribonuclease A complexes with 5'-diphosphoadenosine 3'-phosphate and 5'-diphosphoadenosine 2'-phosphate at 1.7 A resolution. Biochemistry. 1997 May 6;36(18):5578-88.

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. EC 2.7.11.1
2. MAPK-activated protein kinase 2
3. MAPKAP kinase 2
4. MAPKAPK-2
5. MK2

MLSNSQGQSPPVPFPAPAPPPQPPTPALPHPPAQPPPPPPQQFPQFHVKSGLQIKKNAII
DDYKVTSQVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVELHWRASQCPHIVRI
VDVYENLYAGRKCLLIVMECLDGGELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSI
NIAHRDVKPENLLYTSKRPNAILKLTDFGFAKETTSHNSLTTPCYTPYYVAPEVLGPEKY
DKSCDMWSLGVIMYILLCGYPPFYSNHGLAISPGMKTRIRMGQYEFPNPEWSEVSEEVKM
LIRNLLKTEPTQRMTITEFMNHPWIMQSTKVPQTPLHTSRVLKEDKERWEDVKEEMTSAL
ATMRVDYEQIKIKKIEDASNPLLLKRRKKARALEAAALAH

• ATP + a protein = ADP + a phosphoprotein

• Pkinase (PF00069 )

• None

• None

ATGCTGTCCAACTCCCAGGGCCAGAGCCCGCCGGTGCCGTTCCCCGCCCCGGCCCCGCCG
CCGCAGCCCCCCACCCCTGCCCTGCCGCACCCCCCGGCGCAGCCGCCGCCGCCGCCCCCG
CAGCAGTTCCCGCAGTTCCACGTCAAGTCCGGCCTGCAGATCAAGAAGAACGCCATCATC
GATGACTACAAGGTCACCAGCCAGGTCCTGGGGCTGGGCATCAACGGCAAAGTTTTGCAG
ATCTTCAACAAGAGGACCCAGGAGAAATTCGCCCTCAAAATGCTTCAGGACTGCCCCAAG
GCCCGCAGGGAGGTGGAGCTGCACTGGCGGGCCTCCCAGTGCCCGCACATCGTACGGATC
GTGGATGTGTACGAGAATCTGTACGCAGGGAGGAAGTGCCTGCTGATTGTCATGGAATGT
TTGGACGGTGGAGAACTCTTTAGCCGAATCCAGGATCGAGGAGACCAGGCATTCACAGAA
AGAGAAGCATCCGAAATCATGAAGAGCATCGGTGAGGCCATCCAGTATCTGCATTCAATC
AACATTGCCCATCGGGATGTCAAGCCTGAGAATCTCTTATACACCTCCAAAAGGCCCAAC
GCCATCCTGAAACTCACTGACTTTGGCTTTGCCAAGGAAACCACCAGCCACAACTCTTTG
ACCACTCCTTGTTATACACCGTACTATGTGGCTCCAGAAGTGCTGGGTCCAGAGAAGTAT
GACAAGTCCTGTGACATGTGGTCCCTGGGTGTCATCATGTACATCCTGCTGTGTGGGTAT
CCCCCCTTCTACTCCAACCACGGCCTTGCCATCTCTCCGGGCATGAAGACTCGCATCCGA
ATGGGCCAGTATGAATTTCCCAACCCAGAATGGTCAGAAGTATCAGAGGAAGTGAAGATG
CTCATTCGGAATCTGCTGAAAACAGAGCCCACCCAGAGAATGACCATCACCGAGTTTATG
AACCACCCTTGGATCATGCAATCAACAAAGGTCCCTCAAACCCCACTGCACACCAGCCGG
GTCCTGAAGGAGGACAAGGAGCGGTGGGAGGATGTCAAGGGGTGTCTTCATGACAAGAAC
AGCGACCAGGCCACTTGGCTGACCAGGTTGTGA

1. Zu YL, Wu F, Gilchrist A, Ai Y, Labadia ME, Huang CK: The primary structure of a human MAP kinase activated protein kinase 2. Biochem Biophys Res Commun. 1994 Apr 29;200(2):1118-24. [PubMed ]
2. Stokoe D, Caudwell B, Cohen PT, Cohen P: The substrate specificity and structure of mitogen-activated protein (MAP) kinase-activated protein kinase-2. Biochem J. 1993 Dec 15;296 ( Pt 3):843-9. [PubMed ]

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. ATASE
2. Amidophosphoribosyltransferase precursor
3. EC 2.4.2.14
4. GPATase
5. Glutamine phosphoribosylpyrophosphate amidotransferase

MLAEIKGLNEECGVFGIWGHEEAPQITYYGLHSLQHRGQEGAGIVATDGEKLTAHKGQGL
ITEVFQNGELSKVKGKGAIGHVRYATAGGGGYENVQPLLFRSQNNGSLALAHNGNLVNAT
QLKQQLENQGSIFQTSSDTEVLAHLIKRSGHFTLKDQIKNSLSMLKGAYAFLIMTETEMI
VALDPNGLRPLSIGMMGDAYVVASETCAFDVVGATYLREVEPGEMLIINDEGMKSERFSM
NINRSICSMEYIYFSRPDSNIDGINVHSARKNLGKMLAQESAVEADVVTGVPDSSISAAI
GYAEATGIPYELGLIKNRYVGRTFIQPSQALREQGVRMKLSAVRGVVEGKRVVMVDDSIV
RGTTSRRIVTMLREAGATEVHVKISSPPIAHPCFYGIDTSTHEELIASSHSVGEIRQEIG
ADTLSFLSVEGLLKGIGRKYDDSNCGQCLACFTGKYPTEIYQDTVLPHVKEAVLTK

• 5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O

• Pribosyltran (PF00156 )
• GATase_2 (PF00310 )

• None

• None

ATGCTTGCTGAAATCAAAGGCTTAAATGAAGAATGCGGCGTTTTTGGGATTTGGGGACAT
GAAGAAGCCCCGCAAATCACGTATTACGGTCTCCACAGCCTTCAGCACCGAGGACAGGAG
GGTGCTGGCATCGTAGCGACTGACGGTGAAAAGCTGACGGCTCACAAAGGCCAAGGTCTG
ATCACTGAAGTATTTCAAAACGGCGAACTCAGCAAAGTAAAGGGAAAAGGCGCTATCGGG
CACGTTCGGTACGCAACGGCTGGAGGCGGCGGATACGAAAATGTTCAGCCGCTCCTCTTC
CGTTCCCAAAACAACGGCAGCCTGGCGCTTGCTCATAACGGAAATCTTGTCAACGCCACT
CAGCTGAAGCAGCAGCTCGAAAATCAAGGGAGCATCTTTCAAACCTCTTCGGATACAGAG
GTTTTGGCTCACCTGATCAAAAGAAGCGGACACTTCACGCTGAAGGATCAAATTAAAAAC
TCGCTTTCTATGCTGAAAGGCGCCTACGCGTTCCTGATCATGACCGAAACAGAAATGATT
GTCGCACTTGATCCAAACGGGCTGAGACCGCTATCCATCGGCATGATGGGCGACGCTTAT
GTGGTCGCATCAGAAACATGCGCATTTGACGTCGTCGGCGCAACGTACCTTCGCGAGGTA
GAGCCGGGAGAAATGCTGATCATTAATGATGAAGGCATGAAATCAGAGCGTTTTTCCATG
AATATCAATCGTTCCATTTGCAGCATGGAGTACATTTATTTCTCCAGACCAGACAGCAAT
ATTGACGGTATTAATGTGCACAGTGCCCGTAAAAACCTTGGGAAAATGCTGGCTCAGGAA
TCCGCAGTTGAAGCTGACGTCGTAACCGGGGTTCCGGATTCCAGTATTTCAGCGGCGATC
GGCTATGCAGAGGCAACAGGCATTCCGTATGAGCTTGGCTTAATCAAAAACCGTTATGTT
GGCAGAACGTTTATTCAGCCGTCCCAGGCTCTGCGTGAGCAAGGCGTCAGAATGAAGCTG
TCTGCGGTGCGCGGGGTTGTAGAAGGCAAACGCGTCGTGATGGTGGATGACTCTATCGTG
CGAGGAACAACTAGCCGCCGGATTGTCACGATGCTAAGAGAGGCGGGTGCGACAGAGGTG
CATGTGAAAATCAGTTCACCGCCGATCGCTCATCCGTGCTTTTACGGCATTGACACTTCC
ACACATGAAGAACTGATCGCGTCTTCGCATTCTGTCGGAGAAATCCGTCAGGAAATCGGA
GCCGATACCCTCTCATTTTTGAGTGTGGAAGGGCTGCTGAAAGGCATCGGCAGAAAATAC
GATGACTCGAATTGCGGACAGTGTCTCGCTTGCTTTACAGGAAAATATCCGACTGAAATT
TACCAGGATACAGTGCTTCCTCACGTAAAAGAAGCAGTATTAACCAAATAA

1. Ebbole DJ, Zalkin H: Cloning and characterization of a 12-gene cluster from Bacillus subtilis encoding nine enzymes for de novo purine nucleotide synthesis. J Biol Chem. 1987 Jun 15;262(17):8274-87. [PubMed ]
2. Makaroff CA, Paluh JL, Zalkin H: Mutagenesis of ligands to the [4 Fe-4S] center of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase. J Biol Chem. 1986 Aug 25;261(24):11416-23. [PubMed ]
3. Mantsala P, Zalkin H: Glutamine amidotransferase function. Replacement of the active-site cysteine in glutamine phosphoribosylpyrophosphate amidotransferase by site-directed mutagenesis. J Biol Chem. 1984 Nov 25;259(22):14230-6. [PubMed ]
4. Vollmer SJ, Switzer RL, Hermodson MA, Bower SG, Zalkin H: The glutamine-utilizing site of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase. J Biol Chem. 1983 Sep 10;258(17):10582-5. [PubMed ]
5. Makaroff CA, Zalkin H, Switzer RL, Vollmer SJ: Cloning of the Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase gene in Escherichia coli. Nucleotide sequence determination and properties of the plasmid-encoded enzyme. J Biol Chem. 1983 Sep 10;258(17):10586-93. [PubMed ]
6. Smith JL, Zaluzec EJ, Wery JP, Niu L, Switzer RL, Zalkin H, Satow Y: Structure of the allosteric regulatory enzyme of purine biosynthesis. Science. 1994 Jun 3;264(5164):1427-33. [PubMed ]
7. Chen S, Tomchick DR, Wolle D, Hu P, Smith JL, Switzer RL, Zalkin H: Mechanism of the synergistic end-product regulation of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase by nucleotides. Biochemistry. 1997 Sep 2;36(35):10718-26. [PubMed ]
8. Kunst F, Ogasawara N, Moszer I, Albertini AM, Alloni G, Azevedo V, Bertero MG, Bessieres P, Bolotin A, Borchert S, Borriss R, Boursier L, Brans A, Braun M, Brignell SC, Bron S, Brouillet S, Bruschi CV, Caldwell B, Capuano V, Carter NM, Choi SK, Codani JJ, Connerton IF, Danchin A, et al.: The complete genome sequence of the gram-positive bacterium Bacillus subtilis. Nature. 1997 Nov 20;390(6657):249-56. [PubMed ]

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. EC 2.7.1.21

MASYPCHQHASAFDQAARSRGHNNRRTALRPRRQQEATEVRPEQKMPTLLRVYIDGPHGM
GKTTTTQLLVALGSRDDIVYVPEPMTYWRVLGASETIANIYTTQHRLDQGEISAGDAAVV
MTSAQITMGMPYAVTDAVLAPHIGGEAGSSHAPPPALTLIFDRHPIAALLCYPAARYLMG
SMTPQAVLAFVALIPPTLPGTNIVLGALPEDRHIDRLAKRQRPGERLDLAMLAAIRRVYG
LLANTVRYLQCGGSWREDWGQLSGTAVPPQGAEPQSNAGPRPHIGDTLFTLFRAPELLAP
NGDLYNVFAWALDVLAKRLRSMHVFILDYDQSPAGCRDALLQLTSGMVQTHVTTPGSIPT
ICDLARTFAREMGEAN

• ATP + thymidine = ADP + thymidine 5'-phosphate

• Herpes_TK (PF00693 )

• None

• None

TCAGTTAGCCTCCCCCATCTCCCGGGCAAACGTGCGCGCCAGGTCGCAGATCGTCGGTAT
GGAGCCTGGGGTGGTGACGTGGGTCTGGACCATCCCGGAGGTAAGTTGCAGCAGGGCGTC
CCGGCAGCCGGCGGGCGATTGGTCGTAATCCAGGATAAAGACATGCATGGGACGGAGGCG
TTTGGCCAAGACGTCCAAAGCCCAGGCAAACACGTTATACAGGTCGCCGTTGGGGGCCAG
CAACTCGGGGGCCCGAAACAGGGTAAATAACGTGTCCCCGATATGGGGTCGTGGGCCCGC
GTTGCTCTGGGGCTCGGCACCCTGGGGCGGCACGGCCGCCCCCGAAAGCTGTCCCCAATC
CTCCCGCCACGACCCGCCGCCCTGCAGATACCGCACCGTATTGGCAAGCAGCCCATAAAC
GCGGCGAATCGCGGCCAGCATAGCCAGGTCAAGCCGCTCGCCGGGGCGCTGGCGTTTGGC
CAGGCGGTCGATGTGTCTGTCCTCCGGAAGGGCCCCCAACACGATGTTTGTGCCGGGCAA
GGTCGGCGGGATGAGGGCCACGAACGCCAGCACGGCCTGGGGGGTCATGCTGCCCATAAG
GTATCGCGCGGCCGGGTAGCACAGGAGGGCGGCGATGGGATGGCGGTCGAAGATGAGGGT
GAGGGCCGGGGGCGGGGCATGTGAGCTCCCAGCCTCCCCCCCGATATGAGGAGCCAGAAC
GGCGTCGGTCACGGCATAAGGCATGCCCATTGTTATCTGGGCGCTTGTCATTACCACCGC
CGCGTCCCCGGCCGATATCTCACCCTGGTCGAGGCGGTGTTGTGTGGTGTAGATGTTCGC
GATTGTCTCGGAAGCCCCCAACACCCGCCAGTAAGTCATCGGCTCGGGTACGTAGACGAT
ATCGTCGCGCGAACCCAGGGCCACCAGCAGTTGCGTGGTGGTGGTTTTCCCCATCCCGTG
GGGACCGTCTATATAAACCCGCAGTAGCGTGGGCATTTTCTGCTCCAGGCGGACTTCCGT
GGCTTTTTGTTGCCGGCGAGGGCGCAACGCCGTACGTCGGTTGTTATGGCCGCGAGAACG
CGCAGCCTGGTCGAACGCAGACGCGTGTTGATGGCAGGGGTACGAAGCCAT

1. McGeoch DJ, Dalrymple MA, Davison AJ, Dolan A, Frame MC, McNab D, Perry LJ, Scott JE, Taylor P: The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1. J Gen Virol. 1988 Jul;69 ( Pt 7):1531-74. [PubMed ]
2. McKnight SL: The nucleotide sequence and transcript map of the herpes simplex virus thymidine kinase gene. Nucleic Acids Res. 1980 Dec 20;8(24):5949-64. [PubMed ]
3. Brown DG, Visse R, Sandhu G, Davies A, Rizkallah PJ, Melitz C, Summers WC, Sanderson MR: Crystal structures of the thymidine kinase from herpes simplex virus type-1 in complex with deoxythymidine and ganciclovir. Nat Struct Biol. 1995 Oct;2(10):876-81. [PubMed ]
4. Wild K, Bohner T, Aubry A, Folkers G, Schulz GE: The three-dimensional structure of thymidine kinase from herpes simplex virus type 1. FEBS Lett. 1995 Jul 17;368(2):289-92. [PubMed ]
5. Wild K, Bohner T, Folkers G, Schulz GE: The structures of thymidine kinase from herpes simplex virus type 1 in complex with substrates and a substrate analogue. Protein Sci. 1997 Oct;6(10):2097-106. [PubMed ]
6. Champness JN, Bennett MS, Wien F, Visse R, Summers WC, Herdewijn P, de Clerq E, Ostrowski T, Jarvest RL, Sanderson MR: Exploring the active site of herpes simplex virus type-1 thymidine kinase by X-ray crystallography of complexes with aciclovir and other ligands. Proteins. 1998 Aug 15;32(3):350-61. [PubMed ]
7. Bennett MS, Wien F, Champness JN, Batuwangala T, Rutherford T, Summers WC, Sun H, Wright G, Sanderson MR: Structure to 1.9 A resolution of a complex with herpes simplex virus type-1 thymidine kinase of a novel, non-substrate inhibitor: X-ray crystallographic comparison with binding of aciclovir. FEBS Lett. 1999 Jan 25;443(2):121-5. [PubMed ]

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

MEVLFEAKVGDITLKLAQGDITQYPAKAIVNAANKRLEHGGGVAYAIAKACAGDAGLYTE
ISKKAMREQFGRDYIDHGEVVVTPAMNLEERGIKYVFHTVGPICSGMWSEELKEKLYKAF
LGPLEKAEEMGVESIAFPAVSAGIYGCDLEKVVETFLEAVKNFKGSAVKEVALVIYDRKS
AEVALKVFERSL

• A1pp (PF01661 )

• None

• None

ATGGAACGGCGTACTTTAATCATGGAGGTGCTTTTTGAGGCCAAGGTTGGGGACATCACT
CTGAAGCTCGCTCAGGGGGACATCACCCAATACCCGGCAAAGGCAATTGTCAACGCGGCC
AACAAGAGGCTGGAGCACGGCGGAGGGGTGGCTTATGCCATCGCAAAAGCGTGTGCAGGA
GATGCCGGGCTCTACACGGAAATCAGCAAAAAGGCCATGAGAGAGCAGTTTGGAAGAGAC
TACATCGACCACGGCGAGGTCGTTGTTACACCGGCCATGAACCTCGAGGAGAGGGGAATA
AAGTACGTTTTCCACACCGTGGGGCCGATATGCAGCGGCATGTGGAGCGAAGAACTGAAA
GAGAAGCTTTACAAGGCTTTTCTTGGCCCGCTGGAGAAGGCGGAGGAGATGGGCGTCGAA
TCCATAGCCTTCCCTGCTGTGAGCGCTGGGATATACGGCTGTGATCTGGAAAAGGTTGTT
GAGACGTTCCTCGAAGCTGTGAAGAACTTCAAGGGTTCGGCTGTCAAGGAAGTCGCGCTT
GTAATCTACGACAGAAAGTCTGCGGAGGTGGCGCTGAAGGTCTTTGAGAGGAGTCTTTGA

1. Klenk HP, Clayton RA, Tomb JF, White O, Nelson KE, Ketchum KA, Dodson RJ, Gwinn M, Hickey EK, Peterson JD, Richardson DL, Kerlavage AR, Graham DE, Kyrpides NC, Fleischmann RD, Quackenbush J, Lee NH, Sutton GG, Gill S, Kirkness EF, Dougherty BA, McKenney K, Adams MD, Loftus B, Peterson S, Reich CI, McNeil LK, Badger JH, Glodek A, Zhou L, Overbeek R, Gocayne JD, Weidman JF, McDonald L, Utterback T, Cotton MD, Spriggs T, Artiach P, Kaine BP, Sykes SM, Sadow PW, D'Andrea KP, Bowman C, Fujii C, Garland SA, Mason TM, Olsen GJ, Fraser CM, Smith HO, Woese CR, Venter JC: The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus. Nature. 1997 Nov 27;390(6658):364-70. [PubMed ]

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. EC 2.7.13.3

MMEEYLGVFVDETKEYLQNLNDTLLELEKNPEDMELINEAFRALHTLKGMAGTMGFSSMA
KLCHTLENILDKARNSEIKITSDLLDKIFAGVDMITRMVDKIVSEGSDDIGENIDVFSDT
IKSFASSGKEKPSEIKNETETKGEEEHKGESTSNEEVVVLPEEVAHVLQEARNKGFKTFY
IKVILKEGTQLKSARIYLVFHKLEELKCEVVRTIPSVEEIEEEKFENEVELFVISPVDLE
KLSEALSSIADIERVIIKEVTAVTEESGAEKRTEKEEKTEKTEEKAERKKVISQTVRVDI
EKLDNLMDLMGELVIARSRILETLKKYNIKELDESLSHLSRITLDLQNVVMKIRMVPISF
VFNRFPRMVRDLAKKMNKEVNFIMRGEDTELDRTFVEEIGEPLLHLLRNAIDHGIEPKEE
RIAKGKPPIGTLILSARHEGNNVVIEVEDDGRGIDKEKIIRKAIEKGLIDESKAATLSDQ
EILNFLFVPGFSTKEKVSEVSGRGVGMDVVKNVVESLNGSISIESEKDKGTKVTIRLPLT
LAIIQALLVKVNNLVYAIPIANIDTILSISKEDIQRVQDRDVIVIRGEVIPVYRLWEVLQ
IEHKEELEEMEAVIVRVGNRKYGIVVDDLLGQDDIVIKSLGKVFSEVKEFSGAAILGDGS
IALIINVSGIV

• ATP + protein L-histidine = ADP + protein N-phospho-L-histidine

• CheW (PF01584 )
• Hpt (PF01627 )
• HATPase_c (PF02518 )
• H-kinase_dim (PF02895 )
• P2 (PF07194 )

• None

• None

• Cytoplasm (Potential)

ATGATGGAAGAATATCTCGGAGTGTTTGTCGATGAGACAAAAGAATACCTTCAAAATCTG
AACGATACCCTCCTCGAATTGGAGAAAAATCCCGAAGATATGGAACTCATAAACGAAGCG
TTCAGGGCTCTTCATACCCTGAAAGGAATGGCAGGTACAATGGGGTTTTCCAGTATGGCG
AAGCTCTGCCATACCTTAGAAAACATCCTCGATAAAGCCAGAAACAGCGAGATAAAGATA
ACTTCCGATCTCCTCGATAAGATCTTCGCGGGGGTCGATATGATAACCAGAATGGTTGAT
AAGATCGTCTCCGAGGGAAGTGACGACATCGGAGAAAACATAGACGTGTTCTCCGACACC
ATAAAAAGCTTTGCATCATCGGGAAAAGAGAAGCCTTCAGAAATCAAAAATGAAACGGAA
ACAAAGGGTGAGGAAGAACACAAAGGAGAATCAACAAGCAATGAAGAAGTCGTAGTTCTT
CCTGAAGAAGTTGCCCACGTTCTTCAGGAAGCGAGAAACAAGGGTTTCAAAACGTTTTAT
ATTAAAGTGATTCTCAAAGAAGGAACGCAGTTGAAATCCGCCAGGATTTACCTCGTTTTC
CACAAGCTTGAAGAACTGAAGTGTGAAGTTGTGAGAACGATTCCTTCGGTTGAAGAGATA
GAAGAAGAGAAATTCGAAAACGAAGTGGAACTCTTCGTAATCTCCCCTGTGGATCTGGAG
AAACTCTCTGAAGCTCTGTCAAGCATCGCCGATATAGAGAGGGTAATAATAAAAGAAGTA
ACCGCCGTCACCGAAGAATCAGGGGCTGAGAAAAGAACCGAGAAAGAAGAGAAAACTGAA
AAAACTGAGGAAAAGGCCGAAAGAAAAAAGGTTATTTCGCAAACAGTCAGGGTAGATATA
GAGAAACTGGGCAATTTGATGGATTTGATGGGAGAACTGGTCATCGCAAGGAGCAGAATA
CTGGAAACGCTCAAGAAATACAACATAAAAGAACTGGATGAGAGTTTGTCTCATCTCAGC
AGGATCACCTTAGACCTTCAGAATGTTGTGATGAAGATCAGAATGGTTCCCATCTCCTTT
GTTTTCAACAGATTCCCTCGAATGGTGAGAGACCTTGCCAAAAAGATGAACAAAGAAGTG
AATTTCATCATGAGAGGAGAAGACACAGAGCTCGACAGAACGTTCGTTGAAGAAATTGGC
GAACCCCTGCTCCATCTCCTGAGAAACGCCATCGACCACGGTATAGAACCCAAAGAAGAA
CGAATAGCCAAAGGAAAACCCCCCATTGGAACACTCATTCTCTCGGCACGTCACGAGGGA
AACAACGTGGTAATAGAAGTCGAAGATGACGGAAGGGGTATAGACAAGGAAAAGATCATC
AGAAAAGCCATAGAAAAGGGACTCATAGATGAATCAAAGGCCGCTACCCTTTCTGATCAG
GAGATTCTGAACTTCCTCTTCGTTCCGGGATTCTCCACAAAGGAAAAAGTCTCAGAAGTC
TCCGGAAGAGGCGTGGGAATGGATGTCGTGAAAAATGTGGTGGAATCTTTGAATGGTAGC
ATAAGCATAGAAAGCGAGAAAGATAAAGGAACAAAAGTTACGATAAGACTACCGCTCACT
CTGGCCATCATTCAGGCGCTCCTCGTCAAAGTCAACAATCTCGTCTACGCGATTCCGATA
GCGAACATAGACACAATACTCAGCATTTCAAAAGAGGATATTCAAAGAGTTCAGGACAGA
GATGTGATAGTCATAAGAGGAGAAGTGATACCCGTTTACCGTCTGTGGGAAGTGCTTCAA
ATAGAGCACAAAGAAGAACTGGAGGAGATGGAAGCGGTTATTGTGAGGGTAGGAAACAGG
AAGTACGGTATCGTCGTAGACGATCTTCTCGGTCAGGACGATATCGTGATAAAATCTCTT
GGAAAGGTGTTCTCTGAGGTGAAGGAATTCAGCGGAGCAGCTATTCTCGGTGATGGTAGT
ATAGCGCTGATAATCAACGTCTCCGGCATTGTATAA

1. Nelson KE, Clayton RA, Gill SR, Gwinn ML, Dodson RJ, Haft DH, Hickey EK, Peterson JD, Nelson WC, Ketchum KA, McDonald L, Utterback TR, Malek JA, Linher KD, Garrett MM, Stewart AM, Cotton MD, Pratt MS, Phillips CA, Richardson D, Heidelberg J, Sutton GG, Fleischmann RD, Eisen JA, White O, Salzberg SL, Smith HO, Venter JC, Fraser CM: Evidence for lateral gene transfer between Archaea and bacteria from genome sequence of Thermotoga maritima. Nature. 1999 May 27;399(6734):323-9. [PubMed ]
2. Swanson RV, Sanna MG, Simon MI: Thermostable chemotaxis proteins from the hyperthermophilic bacterium Thermotoga maritima. J Bacteriol. 1996 Jan;178(2):484-9. [PubMed ]
3. Bilwes AM, Alex LA, Crane BR, Simon MI: Structure of CheA, a signal-transducing histidine kinase. Cell. 1999 Jan 8;96(1):131-41. [PubMed ]

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase
2. 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase
3. EC 2.7.6.3
4. HPPK
5. PPPK

MTVAYIAIGSNLASPLEQVNAALKALGDIPESHILTVSSFYRTPPLGPQDQPDYLNAAVA
LETSLAPEELLNHTQRIELQQGRVRKAERWGPRTLDLDIMLFGNEVINTERLTVPHYDMK
NRGFMLWPLFEIAPELVFPDGEMLRQILHTRAFDKLNKW

• ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine = AMP + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate

• HPPK (PF01288 )

• None

• None

ATGACAGTGGCGTATATTGCCATAGGCAGCAATCTGGCCTCTCCGCTGGAGCAGGTCAAT
GCTGCCCTGAAAGCATTAGGCGATATCCCTGAAAGCCACATTCTTACCGTTTCTTCGTTT
TACCGCACCCCACCGCTGGGCCCGCAAGATCAACCCGATTACTTAAACGCAGCCGTGGCG
CTGGAAACCTCTCTTGCACCTGAAGAGCTACTCAATCACACACAGCGTATTGAATTGCAG
CAAGGTCGCGTCCGCAAAGCTGAACGCTGGGGACCACGCACGCTGGATCTCGACATCATG
CTGTTTGGTAATGAAGTGATAAATACTGAACGCCTGACCGTTCCGCACTACGATATGAAG
AATCGTGGATTTATGCTGTGGCCGCTGTTTGAAATCGCGCCGGAGTTGGTGTTTCCTGAT
GGGGAGATGTTGCGTCAAATCTTACATACAAGAGCATTTGACAAATTAAACAAATGGTAA

1. Xiao B, Shi G, Chen X, Yan H, Ji X: Crystal structure of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, a potential target for the development of novel antimicrobial agents. Structure. 1999 May;7(5):489-96. [PubMed ]
2. Stammers DK, Achari A, Somers DO, Bryant PK, Rosemond J, Scott DL, Champness JN: 2.0 A X-ray structure of the ternary complex of 7,8-dihydro-6-hydroxymethylpterinpyrophosphokinase from Escherichia coli with ATP and a substrate analogue. FEBS Lett. 1999 Jul 30;456(1):49-53. [PubMed ]
3. Talarico TL, Ray PH, Dev IK, Merrill BM, Dallas WS: Cloning, sequence analysis, and overexpression of Escherichia coli folK, the gene coding for 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase. J Bacteriol. 1992 Sep;174(18):5971-7. [PubMed ]
4. Talarico TL, Dev IK, Dallas WS, Ferone R, Ray PH: Purification and partial characterization of 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase and 7,8-dihydropteroate synthase from Escherichia coli MC4100. J Bacteriol. 1991 Nov;173(21):7029-32. [PubMed ]
5. Liu JD, Parkinson JS: Genetics and sequence analysis of the pcnB locus, an Escherichia coli gene involved in plasmid copy number control. J Bacteriol. 1989 Mar;171(3):1254-61. [PubMed ]
6. Fujita N, Mori H, Yura T, Ishihama A: Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region. Nucleic Acids Res. 1994 May 11;22(9):1637-9. [PubMed ]
7. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-74. [PubMed ]

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. EC 2.7.4.6
2. NDK
3. NDP kinase

MSTNKVNKERTFLAVKPDGVARGLVGEIIARYEKKGFVLVGLKQLVPTKDLAESHYAEHK
ERPFFGGLVSFITSGPVVAMVFEGKGVVASARLMIGVTNPLASAPGSIRGDFGVDVGRNI
IHGSDSVESANREIALWFKPEELLTEVKPNPNLYE

• ATP + nucleoside diphosphate = ADP + nucleoside triphosphate

• NDK (PF00334 )

• None

• None

• Cytoplasm

ATGTCCACAAATAAAGTAAACAAAGAAAGAACTTTCCTTGCTGTTAAACCAGACGGTGTT
GCTCGTGGTTTAGTTGGTGAAATCATCGCCAGATACGAAAAGAAAGGTTTCGTTTTAGTT
GGTTTAAAACAATTAGTTCCAACCAAAGACTTAGCTGAATCTCACTATGCTGAACACAAA
GAAAGACCATTCTTCGGTGGTTTAGTCTCATTCATTACCTCTGGTCCAGTCGTTGCTATG
GTCTTCGAAGGTAAAGGTGTTGTTGCCTCTGCCCGTTTAATGATCGGTGTTACCAACCCA
TTAGCCTCAGCCCCAGGTTCAATTCGTGGTGATTTCGGTGTTGATGTTGGTAGAAACATC
ATCCACGGTTCTGATTCAGTTGAATCTGCCAACAGAGAAATTGCTTTATGGTTCAAACCA
GAAGAATTATTAACTGAAGTTAAACCAAACCCAAATTTATACGAATAA