1. (4-)Diphosphoric acid ion
2. (P2O74-)Diphosphate
3. Diphosphate
4. Pyrometaphosphate
5. Pyrophosphate
6. Pyrophosphate tetraanion
7. Pyrophosphate(4-) ion
8. Pyrophosphic acid
9. Diphosphoric acid
10. PPi

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• Cytoplasm
• endoplasmic reticulum
• mitochondria
• nucleus
• peroxisome

• Blood
• Urine

1. Broll H: [Effect of chloroquine diphosphate on the superhelix structure of DNA and protein synthesis in synovial cells in chronic polyarthritis] Wien Klin Wochenschr. 1983 Dec 23;95(24):877-80. [PubMed ]
2. Golanski J, Pluta J, Baraniak J, Watala C: Limited usefulness of the PFA-100 for the monitoring of ADP receptor antagonists--in vitro experience. Clin Chem Lab Med. 2004 Jan;42(1):25-9. [PubMed ]
3. Mateos-Trigos G, Evans RJ, Heath MF: Effects of P2Y(1) and P2Y(12) receptor antagonists on ADP-induced shape change of equine platelets: comparison with human platelets. Platelets. 2002 Aug-Sep;13(5-6):285-92. [PubMed ]
4. Sirkis SI: [Serum and cerebrospinal fluid enzyme spectra in meningitis and their differential diagnostic value] Zh Nevropatol Psikhiatr Im S S Korsakova. 1982;82(2):193-7. [PubMed ]
5. Barbier O, Torra IP, Sirvent A, Claudel T, Blanquart C, Duran-Sandoval D, Kuipers F, Kosykh V, Fruchart JC, Staels B: FXR induces the UGT2B4 enzyme in hepatocytes: a potential mechanism of negative feedback control of FXR activity. Gastroenterology. 2003 Jun;124(7):1926-40. [PubMed ]
6. March JG, Simonet BM, Grases F: Determination of pyrophosphate in renal calculi and urine by means of an enzymatic method. Clin Chim Acta. 2001 Dec;314(1-2):187-94. [PubMed ]
7. Namiki M, Kitamura M, Nonomura N, Sugao H, Nakamura M, Okuyama A, Utsunomiya M, Itatani H, Matsumoto K, Sonoda T: Direct inhibitory effect of estrogen on the human testis in vitro. Arch Androl. 1988;20(2):131-5. [PubMed ]
8. Kosoglou T, Statkevich P, Johnson-Levonas AO, Paolini JF, Bergman AJ, Alton KB: Ezetimibe: a review of its metabolism, pharmacokinetics and drug interactions. Clin Pharmacokinet. 2005;44(5):467-94. [PubMed ]
9. Pickett DA, Welch DF: Recognition of Staphylococcus saprophyticus in urine cultures by screening colonies for production of phosphatase. J Clin Microbiol. 1985 Mar;21(3):310-3. [PubMed ]
10. Hua HT, Albadawi H, Entabi F, Conrad M, Stoner MC, Meriam BT, Sroufe R, Houser S, Lamuraglia GM, Watkins MT: Polyadenosine diphosphate-ribose polymerase inhibition modulates skeletal muscle injury following ischemia reperfusion. Arch Surg. 2005 Apr;140(4):344-51; discussion 351-2. [PubMed ]
11. Dahlmann N, Ueckermann C: Separation of deoxythymidine-5'-triphosphatase from unspecific hydrolases. A recommended micromethod in the diagnostic evaluation of human carcinoma. Anticancer Res. 1984 Jul-Oct;4(4-5):299-303. [PubMed ]
12. Ebadi M, Sharma SK, Ghafourifar P, Brown-Borg H, El Refaey H: Peroxynitrite in the pathogenesis of Parkinson's disease and the neuroprotective role of metallothioneins. Methods Enzymol. 2005;396:276-98. [PubMed ]
13. Tallaksen CM, Sande A, Bohmer T, Bell H, Karlsen J: Kinetics of thiamin and thiamin phosphate esters in human blood, plasma and urine after 50 mg intravenously or orally. Eur J Clin Pharmacol. 1993;44(1):73-8. [PubMed ]
14. Zhong D, Meins J, Scheidel B, Blume H: [Development of an HPLC method for determination of chloroquine in plasma] Pharmazie. 1993 May;48(5):349-52. [PubMed ]
15. Recio JA, Paez JG, Maskeri B, Loveland M, Velasco JA, Notario V: Both normal and transforming PCPH proteins have guanosine diphosphatase activity but only the oncoprotein cooperates with Ras in activating extracellular signal-regulated kinase ERK1. Cancer Res. 2000 Mar 15;60(6):1720-8. [PubMed ]
16. Puri RN, Colman RF, Colman RW: Modulation of platelet responses by 2-[3-(bromo-2-oxopropylthio)]adenosine-5'-diphosphate involves its binding to as well as covalent modification of an ADP-receptor, aggregin. Arch Biochem Biophys. 1997 Jul 1;343(1):140-5. [PubMed ]
17. Hamagishi Y, Oki T, Tone H, Inui T: A radioimmunoassay for guanosine-5'-diphosphate-3'-diphosphate and adenosine-5'-triphosphate-3'-diphosphate. J Biochem (Tokyo). 1980 Dec;88(6):1785-92. [PubMed ]
18. Lee AY, Youm YH, Kim NH, Yang H, Choi WI: Keratinocytes in the depigmented epidermis of vitiligo are more vulnerable to trauma (suction) than keratinocytes in the normally pigmented epidermis, resulting in their apoptosis. Br J Dermatol. 2004 Nov;151(5):995-1003. [PubMed ]
19. Ito H, Yamamoto H, Kimura Y, Kambe H, Okochi T, Kishimoto S: Affinity chromatography of human plasma gelsolin with polyphosphate compounds on immobilized Cibacron Blue F3GA. J Chromatogr. 1990 Apr 6;526(2):397-406. [PubMed ]
20. Wikipedia

1. Acetyl-coenzyme A synthetase 2-like, mitochondrial precursor
2. Fucose-1-phosphate guanylyltransferase
3. Squalene synthetase
4. Phenylalanyl-tRNA synthetase, mitochondrial precursor
5. Nicotinamide mononucleotide adenylyltransferase 3
6. Nicotinate-nucleotide pyrophosphorylase [carboxylating]
7. Nicotinamide mononucleotide adenylyltransferase 2
8. Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 1
9. Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 2
10. N-acylneuraminate cytidylyltransferase
11. S-adenosylmethionine synthetase isoform type-1
12. Inosine triphosphate pyrophosphatase
13. Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial precursor
14. Adenine phosphoribosyltransferase
15. Hypoxanthine-guanine phosphoribosyltransferase
16. Biotin--protein ligase
17. Phenylalanyl-tRNA synthetase beta chain
18. Ubiquitin-conjugating enzyme E2 A
19. NEDD8-conjugating enzyme Ubc12
20. Ubiquitin/ISG15-conjugating enzyme E2 L6
21. Glycyl-tRNA synthetase
22. Bifunctional aminoacyl-tRNA synthetase [Includes: Glutamyl-tRNA synthetase
23. Long-chain-fatty-acid--CoA ligase 4
24. Tryptophanyl-tRNA synthetase, cytoplasmic
25. Long-chain-fatty-acid--CoA ligase 1
26. Glutaminyl-tRNA synthetase
27. Asparagine synthetase [glutamine-hydrolyzing]
28. Ubiquitin-conjugating enzyme E2 E2
29. Ubiquitin-conjugating enzyme E2 D2
30. DNA ligase 4
31. Arginyl-tRNA synthetase, cytoplasmic
32. Probable leucyl-tRNA synthetase, mitochondrial precursor
33. RNA 3'-terminal phosphate cyclase
34. DNA ligase 3
35. Ubiquitin-conjugating enzyme E2 D3
36. Asparaginyl-tRNA synthetase, cytoplasmic
37. Ubiquitin-activating enzyme E1
38. Tyrosyl-tRNA synthetase, mitochondrial precursor
39. Long-chain-fatty-acid--CoA ligase 6
40. Methionyl-tRNA synthetase, cytoplasmic
41. Alanyl-tRNA synthetase, cytoplasmic
42. Ribose-phosphate pyrophosphokinase I
43. Seryl-tRNA synthetase, mitochondrial precursor
44. Ribose-phosphate pyrophosphokinase II
45. SUMO-conjugating enzyme UBC9
46. Probable histidyl-tRNA synthetase, mitochondrial precursor
47. Ubiquitin-conjugating enzyme E2 J1
48. Long-chain-fatty-acid--CoA ligase 5
49. Histidyl-tRNA synthetase, cytoplasmic
50. Long-chain-fatty-acid--CoA ligase 3
51. Ubiquitin-conjugating enzyme E2 C
52. Ubiquitin-conjugating enzyme E2 N
53. Argininosuccinate synthase
54. Adenylate cyclase type 7
55. Adenylate cyclase type 6
56. Adenylate cyclase type 5
57. Adenylate cyclase type 8
58. Adenylate cyclase type 9
59. Adenylate cyclase type 3
60. Adenylate cyclase type 1
61. Choline-phosphate cytidylyltransferase B
62. DNA-directed RNA polymerase III subunit D
63. DNA-directed RNA polymerase II largest subunit
64. DNA-directed RNA polymerase, mitochondrial precursor
65. DNA-directed RNA polymerase I 135 kDa polypeptide
66. Choline-phosphate cytidylyltransferase A
67. DNA-directed RNA polymerase I-associated factor 53 kDa subunit
68. DNA-directed RNA polymerase III subunit 22.9 kDa polypeptide
69. DNA-directed RNA polymerases III 12.5 kDa polypeptide
70. Adenylate cyclase type 2
71. Geranylgeranyl pyrophosphate synthetase
72. Farnesyl pyrophosphate synthetase
73. DNA polymerase beta
74. DNA polymerase alpha catalytic subunit
75. DNA polymerase lambda
76. DNA polymerase epsilon subunit 4
77. DNA polymerase eta
78. DNA polymerase delta catalytic subunit
79. DNA polymerase zeta catalytic subunit
80. DNA polymerase epsilon, catalytic subunit A
81. DNA polymerase mu
82. DNA polymerase epsilon subunit 3
83. DNA polymerase subunit gamma 1
84. DNA polymerase iota
85. DNA polymerase epsilon subunit 2
86. Guanylate cyclase soluble subunit beta-1
87. Retinal guanylyl cyclase 1 precursor
88. Guanylate cyclase soluble subunit alpha-3
89. Inorganic pyrophosphatase
90. UTP--glucose-1-phosphate uridylyltransferase 2
91. DNA nucleotidylexotransferase
92. Retinal guanylyl cyclase 2 precursor
93. Poly(A) polymerase alpha
94. mRNA-capping enzyme
95. Bifunctional coenzyme A synthase
96. E3 ubiquitin-protein ligase NEDD4-like protein
97. Ubiquitin-protein ligase E3 Mdm2
98. Telomerase reverse transcriptase
99. Novel protein
100. Glutamine-dependent NAD(+) synthetase
101. Acetoacetyl-CoA synthetase
102. Acyl-coenzyme A synthetase ACSM1, mitochondrial precursor
103. Inorganic pyrophosphatase 2, mitochondrial precursor
104. cDNA FLJ77907, highly similar to Homo sapiens aspartyl-tRNA synthetase, mRNA
105. Probable cysteinyl-tRNA synthetase, mitochondrial precursor
106. cDNA FLJ78123, highly similar to Homo sapiens phosphoribosyl pyrophosphate amidotransferase
107. cDNA FLJ75406, highly similar to Homo sapiens guanine monphosphate synthetase
108. Probable glutamyl-tRNA synthetase, mitochondrial precursor
109. cDNA FLJ75173, highly similar to Homo sapiens threonyl-tRNA synthetase, mRNA
110. 2-aminoadipic 6-semialdehyde dehydrogenase
111. Pre-B-cell colony enhancing factor 1
112. ACSS2 protein
113. Guanylate cyclase 1, soluble, alpha 2
114. cDNA FLJ75687, highly similar to Homo sapiens uridine monophosphate synthetase
115. FAD synthetase
116. cDNA FLJ77250, highly similar to Homo sapiens isoleucine-tRNA synthetase
117. Valyl-tRNA synthetase like
118. Signal transduction protein CBL-C
119. HECT domain and RCC1-like domain-containing protein 1
120. Probable E3 ubiquitin-protein ligase HERC2
121. Nuclear respiratory factor 1
122. Probable threonyl-tRNA synthetase 2, cytoplasmic
123. Threonyl-tRNA synthetase, mitochondrial
124. LARS protein (Leucyl-tRNA synthetase, isoform CRA_a) (Leucyl-tRNA synthetase)
125. Uncharacterized protein KARS (Lysyl-tRNA synthetase, isoform CRA_d)
126. Methionyl-tRNA synthetase, mitochondrial
127. Aspartyl-tRNA synthetase, mitochondrial
128. cDNA FLJ75964, highly similar to Homo sapiens prolyl-tRNA synthetase (mitochondrial)(putative) (PARS2), mRNA (Prolyl-tRNA synthetase (Mitochondrial)(Putative))
129. Putative uncharacterized protein DKFZp686F1612 (Cysteinyl-tRNA synthetase, isoform CRA_e)
130. FARSLA protein (Phenylalanine-tRNA synthetase-like, alpha subunit, isoform CRA_b)
131. Probable asparaginyl-tRNA synthetase, mitochondrial
132. SUMO-activating enzyme subunit 2
133. E3 ubiquitin-protein ligase HUWE1
134. E3 ubiquitin-protein ligase Topors
135. STIP1 homology and U-box containing protein 1 (STIP1 homology and U- box containing protein 1, isoform CRA_c)
136. Ubiquitin conjugation factor E4 B
137. Membrane-associated ring finger (C3HC4) 6 (Membrane-associated ring finger (C3HC4) 6, isoform CRA_a)
138. TGIF-interacting ubiquitin ligase 1
139. NEDD4-like E3 ubiquitin-protein ligase WWP2
140. E3 ubiquitin-protein ligase MARCH3
141. NEDD8-conjugating enzyme UBE2F
142. Ubiquitin-conjugating enzyme E2 U
143. Probable E3 ubiquitin-protein ligase MARCH10
144. E3 ubiquitin-protein ligase UBR1
145. E3 ubiquitin-protein ligase MARCH8
146. E3 ubiquitin-protein ligase ZNRF2
147. Tripartite motif-containing protein 32
148. Probable E3 ubiquitin-protein ligase MYCBP2
149. Probable E3 ubiquitin-protein ligase MGRN1
150. E3 ubiquitin-protein ligase UBR2
151. E3 ubiquitin-protein ligase UBR4
152. Autocrine motility factor receptor, isoform 2
153. Ubiquitin-conjugating enzyme E2 S
154. Pre-mRNA-processing factor 19
155. Myosin regulatory light chain interacting protein (Myosin regulatory light chain interacting protein, isoform CRA_a)
156. HNP95 (Ubiquitin-like, containing PHD and RING finger domains, 1, isoform CRA_a) (UHRF1 protein)
157. Putative ubiquitin-conjugating enzyme E2 N-like
158. Midline-1
159. E3 ubiquitin-protein ligase NEDD4
160. CCR4-NOT transcription complex subunit 4
161. cDNA FLJ75810, highly similar to Homo sapiens Parkinson disease (autosomal recessive, juvenile) 2, parkin (PARK2), transcript variant 1, mRNA (Parkinson disease (Autosomal recessive, juvenile) 2, parkin, isoform CRA_c)
162. E3 ubiquitin-protein ligase MARCH2
163. E3 ubiquitin-protein ligase UBR5
164. E3 ubiquitin-protein ligase TRIM33
165. Ubiquitin carrier protein (EC 6.3.2.-)
166. E3 ubiquitin-protein ligase MARCH5
167. Ubiquitin-conjugating enzyme E2 R2
168. E3 ubiquitin-protein ligase MARCH1
169. E3 ubiquitin-protein ligase FANCL
170. Ubiquitin-like modifier-activating enzyme 6
171. Ubiquitin-conjugating enzyme 16 (Ubiquitin-conjugating enzyme E2W (Putative), isoform CRA_c)
172. Galactosyl transferase-associated protein
173. E3 ubiquitin-protein ligase CHFR
174. Ring finger protein 20
175. E3 ubiquitin-protein ligase RAD18
176. Smad-ubiquitin E3 ligase Smurf1-beta (SMAD specific E3 ubiquitin protein ligase 1, isoform CRA_c) (E3 ubiquitin ligase SMURF1) (SMAD specific E3 ubiquitin protein ligase 1)
177. Baculoviral IAP repeat-containing protein 6
178. E3 ubiquitin-protein ligase MARCH4
179. E3 ubiquitin-protein ligase CCNB1IP1
180. cDNA FLJ76639, highly similar to Homo sapiens ring finger protein 1 (RING1), mRNA
181. E3 ubiquitin-protein ligase RNF5
182. Ubiquitin-conjugating enzyme E2 O
183. Praja 1
184. cDNA FLJ75387, highly similar to Homo sapiens ring finger protein 25, mRNA (Ring finger protein 25, isoform CRA_e)
185. RFWD2 protein (Fragment)
186. E3 ubiquitin-protein ligase SMURF2
187. E3 ubiquitin-protein ligase SIAH1
188. E3 ubiquitin-protein ligase SIAH2
189. E3 ubiquitin-protein ligase MARCH7
190. Ubiquitin-conjugating enzyme E2 Z
191. Ubiquitin-like modifier-activating enzyme 7
192. cDNA FLJ77160, highly similar to Homo sapiens ubiquitin-conjugating enzyme E2D 1 (UBC4/5 homolog, yeast) (UBE2D1), mRNA (Ubiquitin- conjugating enzyme E2D 1 (UBC4/5 homolog, yeast), isoform CRA_c)
193. cDNA FLJ76118, highly similar to Homo sapiens ubiquitin-conjugating enzyme E2G 2 (UBC7 homolog, yeast) (UBE2G2), transcript variant 1, mRNA (Ubiquitin-conjugating enzyme E2G 2 (UBC7 homolog, yeast), isoform CRA_a)
194. Ubiquitin carrier protein (EC 6.3.2.-)
195. Ubiquitin-protein ligase E3A
196. E3 ubiquitin-protein ligase RNF128
197. Tripartite motif-containing protein 11
198. BRCA1 associated protein variant (Fragment)
199. E3 ubiquitin-protein ligase synoviolin
200. E3 ubiquitin-protein ligase TRIM63
201. E3 ubiquitin-protein ligase LNX
202. E3 ubiquitin-protein ligase ZNRF1
203. Tripartite motif-containing protein 5
204. CBL protein
205. cDNA FLJ77240, highly similar to Homo sapiens Cas-Br-M (murine) ecotropic retroviral transforming sequence b (CBLB), mRNA (Cas-Br-M (Murine) ecotropic retroviral transforming sequence b, isoform CRA_c)
206. cDNA FLJ75599, highly similar to Homo sapiens hect domain and RLD 3 (HERC3), mRNA (Hect domain and RLD 3)
207. Ubiquitin-protein ligase E3B
208. E3 ubiquitin-protein ligase RNF8
209. cDNA FLJ78055, highly similar to Homo sapiens ubiquitin-activating enzyme E1C (UBA3 homolog, yeast) (UBE1C), transcript variant 1, mRNA (Ubiquitin-activating enzyme E1C) (UBA3 homolog, yeast)
210. E3 ubiquitin-protein ligase LRSAM1
211. Ubiquitin-conjugating enzyme E2 Q2
212. E3 ubiquitin-protein ligase MARCH9
213. Probable E3 ubiquitin-protein ligase TRIP12
214. E3 ubiquitin-protein ligase DZIP3
215. Ubiquitin-protein ligase E3C
216. cDNA FLJ76892, highly similar to Homo sapiens praja 2, RING-H2 motif containing (PJA2), mRNA (Praja 2, RING-H2 motif containing, isoform CRA_a)
217. cDNA FLJ75711, highly similar to Homo sapiens cell division cycle 34 (CDC34), mRNA (Cell division cycle 34, isoform CRA_a)
218. Adenylate cyclase 9 (Adenylate cyclase 9, isoform CRA_a)
219. DNA-directed RNA polymerase III subunit RPC1
220. DNA-directed RNA polymerase I subunit RPA1
221. DNA-directed RNA polymerase subunit
222. DNA-directed RNA polymerases I and III subunit RPAC2
223. cDNA FLJ75210, highly similar to H.sapiens RNA polymerase II 140 kDa subunit (Polymerase (RNA) II (DNA directed) polypeptide B, 140kDa)
224. DNA-directed RNA polymerase (EC 2.7.7.6)
225. DNA-directed RNA polymerase III subunit RPC7-like
226. POLR1C protein (Fragment)
227. cDNA FLJ77390 (Putative uncharacterized protein RP11-311P8.3)
228. TRNA isopentenyltransferase 1 variant (Fragment)
229. Myb-binding protein 1A
230. DNA polymerase theta
231. cDNA FLJ76751, highly similar to Homo sapiens polymerase (DNA directed) sigma (POLS), mRNA (Polymerase (DNA directed) sigma)
232. Poly(A) polymerase beta (Testis specific)
233. cDNA FLJ75300, highly similar to Homo sapiens hMtCCA tRNA- nucleotidyltransferase (TRNA nucleotidyl transferase, CCA-adding, 1, isoform CRA_b)
234. cDNA, FLJ92898, Homo sapiens aminoadipate-semialdehydedehydrogenase-phosphopantetheinyl transferase (AASDHPPT), mRNA (Aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase, isoform CRA_b)
235. cDNA FLJ43223 fis, clone FEBRA2026984, highly similar to Tyrosyl-tRNA synthetase, cytoplasmic (EC 6.1.1.1)
236. cDNA, FLJ94340, Homo sapiens tryptophanyl tRNA synthetase 2 (mitochondrial)(WARS2), nuclear gene encoding mitochondrial protein, mRNA (Tryptophanyl tRNA synthetase 2 (Mitochondrial), isoform CRA_a)
237. Isoleucyl-tRNA synthetase 2, mitochondrial (Isoleucine-tRNA synthetase 2, mitochondrial)
238. Valyl-tRNA synthetase (Valyl-tRNA synthetase, isoform CRA_a)
239. cDNA, FLJ93186, Homo sapiens seryl-tRNA synthetase (SARS), mRNA (Seryl-tRNA synthetase, isoform CRA_e)
240. Arginyl-tRNA synthetase-like, isoform CRA_a
241. cDNA FLJ41040 fis, clone LIVER1000017, highly similar to Bile acyl-CoA synthetase (EC 6.2.1.7)
242. cDNA, FLJ96708, Homo sapiens SUMO-1 activating enzyme subunit 1 (SAE1), mRNA (SUMO-1 activating enzyme subunit 1, isoform CRA_b)
243. cDNA, FLJ94847, Homo sapiens ubiquitin-conjugating enzyme E2E 3 (UBC4/5 homolog, yeast) (UBE2E3), mRNA (Ubiquitin-conjugating enzyme E2E 3 (UBC4/5 homolog, yeast), isoform CRA_a)
244. Ubiquitin-conjugating enzyme E2, J2 (UBC6 homolog, yeast)
245. cDNA FLJ39513 fis, clone PROST2019164, highly similar to E3 ubiquitin ligase IBRDC2 (EC 6.3.2.-)
246. Ring finger protein 138, isoform CRA_a
247. Ubiquitin ligase protein MIB1
248. Ring finger protein 2, isoform CRA_b
249. cDNA, FLJ92287, Homo sapiens ubiquitin-conjugating enzyme E2B (RAD6 homolog) (UBE2B), mRNA (Ubiquitin-conjugating enzyme E2B (RAD6 homolog), isoform CRA_a)
250. cDNA, FLJ95752, Homo sapiens ubiquitin-conjugating enzyme E2E 1 (UBC4/5 homolog, yeast) (UBE2E1), mRNA (Ubiquitin-conjugating enzyme E2E 1 (UBC4/5 homolog, yeast), isoform CRA_a)
251. cDNA, FLJ93536, Homo sapiens ubiquitin-conjugating enzyme E2G 1 (UBC7 homolog, C. elegans) (UBE2G1), mRNA (Ubiquitin-conjugating enzyme E2G 1 (UBC7 homolog, yeast), isoform CRA_e)
252. cDNA, FLJ92022, Homo sapiens ubiquitin-conjugating enzyme E2L 3 (UBE2L3), mRNA (Ubiquitin-conjugating enzyme E2L 3, isoform CRA_a)
253. Itchy homolog E3 ubiquitin protein ligase (Mouse)
254. cDNA FLJ33305 fis, clone BNGH42003529, highly similar to E3 ubiquitin protein ligase TRAF7 (EC 6.3.2.-)
255. Ubiquitin conjugation factor E4 A (HCG2033105, isoform CRA_b)
256. cDNA, FLJ94941, Homo sapiens ligase I, DNA, ATP-dependent (LIG1), mRNA (Ligase I, DNA, ATP-dependent, isoform CRA_a)
257. cDNA FLJ16206 fis, clone CTONG2019590, highly similar to Adenylate cyclase type 4 (EC 4.6.1.1)
258. cDNA, FLJ94990, Homo sapiens CDP-diacylglycerol synthase (phosphatidatecytidylyltransferase) 1 (CDS1), mRNA (CDP-diacylglycerol synthase (Phosphatidate cytidylyltransferase) 1, isoform CRA_a)
259. cDNA, FLJ96552, Homo sapiens CDP-diacylglycerol synthase (phosphatidatecytidylyltransferase) 2 (CDS2), mRNA (CDP-diacylglycerol synthase (Phosphatidate cytidylyltransferase) 2, isoform CRA_a)
260. Nicotinamide nucleotide adenylyltransferase 1 (Nicotinamide nucleotide adenylyltransferase 1, isoform CRA_a) (cDNA, FLJ96727, Homo sapiens nicotinamide nucleotide adenylyltransferase 1(NMNAT1), mRNA)
261. Methionine adenosyltransferase II, beta, isoform CRA_a
262. Polymerase (DNA directed) kappa, isoform CRA_b
263. cDNA, FLJ95510, Homo sapiens poly(A) polymerase gamma (PAPOLG), mRNA (Poly(A) polymerase gamma, isoform CRA_f)
264. cDNA, FLJ93080, highly similar to Homo sapiens UDP-N-acteylglucosamine pyrophosphorylase 1 (UAP1), mRNA (UDP-N-acteylglucosamine pyrophosphorylase 1, isoform CRA_a)
265. cDNA FLJ30970 fis, clone HEART2000444, highly similar to Homo sapiens phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP), mRNA
266. Guanylate cyclase 2C (Heat stable enterotoxin receptor)
267. Guanylate cyclase
268. Guanylate cyclase
269. Phospholysine phosphohistidine inorganic pyrophosphate phosphatase

1. Acetate--CoA ligase 2
2. Acetyl-CoA synthetase 2
3. Acyl- CoA synthetase short-chain family member 1

MAARTLGRGVGRLLGSLRGLSGQPARPPCGVSAPRRAASGPSGSAPAVAAAAAQPGSYPA
LSAQAAREPAAFWGPLARDTLVWDTPYHTVWDCDFSTGKIGWFLGGQLNVSVNCLDQHVR
KSPESVALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVA
AMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLRGGRVVELKKIVDEAVK
HCPTVQHVLVAHRTDNKVHMGDLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGM
PKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLF
ESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPI
NCEAWEWLHRVVGDSRCTLVDTWWQTETGGICIAPRPSEEGAEILPAMAMRPFFGIVPVL
MDEKGSVVEGSNVSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAYRTEG
GYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKD
SAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQELG
DTTTLEDPSIIAEILSVYQKCKDKQAAAK

• Gluconeogenesis (map00010 )
• Propanoate Metabolism (map00640 )
• Pyruvate Metabolism (map00620 )

• ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA

• AMP-binding (PF00501 )

• 1-22

CCAAGTGCAAGGTGGTTATCACCTTCAACCAAGGACTCCGGGGTGGGCGCGTGGTGGAGC
TGAAGAAAATAGTGGATGAGGCTGTGAAGCACTGCCCCACCGTGCAGCATGTCCTGGTGG
CTCACAGGACAGACAACAAGGTCCACATGGGGGATCTGGACGTCCCGCTGGAGCAGGAAA
TGGCCAAGGAGGACCCTGTTTGCGCCCCAGAGAGCATGGGCAGTGAGGACATGCTCTTCA
TGCTGTACACCTCAGGGAGCACCGGAATGCCCAAGGGCATCGTCCATACCCAGGCAGGCT
ACCTGCTCTATGCCGCCCTGACTCACAAGCTTGTGTTTGACCACCAGCCAGGTGACATCT
TTGGCTGTGTGGCCGACATCGGTTGGATTACAGGACACAGCTACGTGGTGTATGGGCCTC
TCTGCAATGGTGCCACCAGCGTCCTTTTTGAGAGCACCCCAGTTTATCCCAATGCTGGTC
GGTACTGGGAGACAGTAGAGAGGTTGAAGATCAATCAGTTCTATGGCGCCCCAACGGCTG
TCCGGCTGTTGCTGAAATACGGTGATGCCTGGGTGAAGAAGTATGATCGCTCCTCCCTGC
GGACCCTGGGGTCAGTGGGAGAGCCCATCAACTGTGAGGCCTGGGAGTGGCTTCACAGGG
TGGTGGGGGACAGCAGGTGCACGCTGGTGGACACCTGGTGGCAGACAGAAACAGGTGGCA
TCTGCATCGCACCACGGCCCTCGGAAGAAGGGGCGGAAATCCTCCCTGCCATGGCGATGA
GGCCCTTCTTTGGCATCGTCCCCGTCCTCATGGATGAGAAGGGCAGCGTCGTGGAGGGCA
GCAACGTCTCCGGGGCCCTGTGCATCTCCCAGGCCTGGCCGGGCATGGCCAGGACCATCT
ATGGCGACCACCAGCGATTTGTGGACGCCTACTTCAAGGCCTACCCAGGCTATTACTTCA
CTGGAGACGGGGCTTACCGAACTGAGGGCGGCTATTACCAGATCACAGGGCGGATGGATG
ATGTCATCAACATCAGTGGCCACCGGCTGGGGACCGCAGAGATTGAGGACGCCATCGCCG
ACCACCCTGCAGTACCAGAAAGTGCTGTCATTGGCTACCCCCACGACATCAAAGGAGAAG
CTGCCTTTGCCTTCATTGTGGTGAAAGATAGTGCGGGTGACTCAGATGTGGTGGTGCAGG
AGCTCAAGTCCATGGTGGCCACCAAGATCGCCAAATATGCTGTGCCTGATGAGATCCTGG
TGGTGAAACGTCTTCCAAAAACCAGGTCTGGGAAGGTCATGCGGCGGCTCCTGAGGAAGA
TCATCACTAGTGAGGCCCAGGAGCTGGGAGACACTACCACCTTGGAGGACCCCAGCATCA
TCGCAGAGATCCTGAGTGTCTACCAGAAGTGCAAGGACAAGCAGGCTGCTGCTAAGTGA

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. Nagase T, Nakayama M, Nakajima D, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2001 Apr 27;8(2):85-95. [PubMed ]
3. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed ]

1. GDP-L-fucose pyrophosphorylase
2. GDP-L-fucose diphosphorylase

MAAARDPPEVSLREATQRKLRRFSELRGKLVARGEFWDIVAITAADEKQELAYNQQLSEK
LKRKELPLGVQYHVFVDPAGAKIGNGGSTLCALQCLEKLYGDKWNSFTILLIHSGGYSQR
LPNASALGKIFTALPLGNPIYQMLELKLAMYIDFPLNMNPGILVTCADDIELYSIGEFEF
IRFDKPGFTALAHPSSLTIGTTHGVFVLDPFDDLKHRDLEYRSCHRFLHKPSIEKMYQFN
AVCRPGNFCQQDFAGGDIADLKLDSDYVYTDSLFYMDHKSAKMLLAFYEKIGTLSCEIDA
YGDFLQALGPGATVEYTRNTSNVIKEESELVEMRQRIFHLLKGTSLNVVVLNNSKFYHIG
TTEEYLFYFTSDNSLKSELGLQSITFSIFPDIPECSGKTSCIIQSILDSRCSVAPGSVVE
YSRLGPDVSVGENCIISGSYILTKAALPAHSFVCSLSLKMNRCLKYATMAFGVQDNLKKS
VKTLSDIKLLQFFGVCFLSCLDVWNLKVTEELFSGNKTCLSLWTARIFPVCSSLSDSVIT
SLKMLNAVKNKSAFSLNSYKLLSIEEMLIYKDVEDMITYREQIFLEISLKSSLM

• Fructose and Mannose Metabolism (map00051 )

• GTP + beta-L-fucose 1-phosphate = diphosphate + GDP-L-fucose

• Fucokinase (PF07959 )

• None

• None

ATGGCAGCTGCTAGGGACCCTCCGGAAGTATCGCTGCGAGAAGCCACCCAGCGAAAATTG
CGGAGGTTTTCCGAGCTAAGAGGCAAACTTGTAGCACGTGGAGAATTCTGGGACATAGTT
GCAATAACAGCGGCTGATGAAAAACAGGAACTTGCTTACAACCAACAGCTGTCAGAAAAG
CTGAAAAGAAAGGAGTTACCCCTTGGAGTTCAATATCACGTTTTTGTGGATCCTGCTGGA
GCCAAAATTGGAAATGGAGGATCAACACTTTGTGCCCTTCAATGTTTGGAAAAGCTATAT
GGAGATAAATGGAATTCTTTTACCATCTTATTAATTCACTCTGGTGGCTACAGTCAACGA
CTTCCAAATGCAAGTGCTCTGGGAAAAATTTTCACTGCTTTACCTCTTGGTAACCCCATT
TATCAGATGCTAGAATTAAAGCTAGCCATGTACATTGATTTCCCCTTAAATATGAATCCT
GGAATTCTGGTTACCTGTGCAGATGATATTGAACTTTATAGTATTGGAGAATTTGAGTTT
ATTAGGTTTGACAAACCTGGCTTTACTGCTTTAGCTCATCCTTCTAGTTTGACGATAGGT
ACCACACATGGAGTATTTGTCTTAGATCCTTTTGATGATTTAAAACATAGAGACCTTGAA
TACAGGTCTTGCCATCGTTTCCTTCATAAGCCCAGCATAGAAAAGATGTATCAGTTTAAT
GCTGTGTGTAGACCTGGAAATTTTTGTCAACAGGACTTTGCTGGGGGTGACATTGCCGAT
CTTAAATTAGACTCTGACTATGTCTACACAGATAGCCTATTTTATATGGATCATAAATCA
GCAAAAATGTTACTTGCTTTTTATGAAAAAATAGGCACACTGAGCTGTGAAATAGATGCC
TATGGTGACTTTCTGCAGGCTTTGGGACCTGGAGCAACTGTGGAGTACACCAGAAACACA
TCACATGTCATTAAAGAAGAGTCAGAGTTGGTAGAAATGAGGCAGAGAATATTTCATCTT
CTTAAAGGAACATCACTAAATGTTGTTGTTCTTAATAACTCCAAATTTTATCACATTGGA
ACAACCGAAGAATATTTGTTTTACTTTACCTCAGATAACAGTTTAAAGTCAGAGCTCGGC
TTACAGTCCATAACTTTTAGTATCTTTCCAGATATACCAGAATGCTCTGGCAAAACATCC
TGTATCATTCAAAGCATACTGGATTCAAGATGTTCTGTGGCACCTGGCTCAGTTGTGGAG
TATTCCAGATTGGGGCCTGATGTTTCAGTTGGGGAAAACTGCATTATTAGTGGTTCTTAC
ATCCTAACAAAAGCTGCCCTCCCCGCACATTCTTTTGTATGTTCCTTAAGCTTAAAGATG
AATAGATGCTTAAAGTATGCAACTATGGCATTTGGAGTGCAAGACAACTTGAAAAAGAGT
GTGAAAACATTGTCAGATATAAAGTTACTTCAATTCTTTGGAGTCTGTTTCCTGTCATGC
TTAGATGTTTGGAATCTTAAAGTTACAGAGGAACTGTTCTCTGGTAACAAGACATGTCTG
AGTTTGTGGACTGCACGCATTTTCCCAGTTTGTTCTTCTTTGAGTGACTCAGTTATAACA
TCCCTAAAGATGTTAAATGCTGTTAAGAACAAGTCAGCATTCAGCCTGAATAGCTATAAG
TTGCTGTCCATTGAAGAAATGCTTATCTACAAAGATGTAGAAGATATGATAACTTACAGG
GAACAAATTTTTCTAGAAATCAGTTTAAAAAGCAGTTTGATGTAG

1. Pastuszak I, Ketchum C, Hermanson G, Sjoberg EJ, Drake R, Elbein AD: GDP-L-fucose pyrophosphorylase. Purification, cDNA cloning, and properties of the enzyme. J Biol Chem. 1998 Nov 13;273(46):30165-74. [PubMed ]

1. SQS
2. SS
3. Farnesyl-diphosphate farnesyltransferase
4. FPP:FPP farnesyltransferase

MEFVKCLGHPEEFYNLVRFRIGGKRKVMPKMDQDSLSSSLKTCYKYLNQTSRSFAAVIQA
LDGEMRNAVCIFYLVLRALDTLEDDMTISVEKKVPLLHNFHSFLYQPDWRFMESKEKDRQ
VLEDFPTISLEFRNLAEKYQTVIADICRRMGIGMAEFLDKHVTSEQEWDKYCHYVAGLVG
IGLSRLFSASEFEDPLVGEDTERANSMGLFLQKTNIIRDYLEDQQGGREFWPQEVWSRYV
KKLGDFAKPENIDLAVQCLNELITNALHHIPDVITYLSRLRNQSVFNFCAIPQVMAIATL
AACYNNQQVFKGAVKIRKGQAVTLMMDATNMPAVKAIIYQYMEEIYHRIPDSDPSSSKTR
QIISTIRTQNLPNCQLISRSHYSPIYLSFVMLLAALSWQYLTTLSQVTEDYVQTGEH

• Steroid Biosynthesis (map00100 )
• Squalene Biosynthesis (map00900 )

• 2 farnesyl diphosphate = diphosphate + presqualene diphosphate

• SQS_PSY (PF00494 )

• None

• 284-304 384-404

ATGGAGTTCGTGAAATGCCTTGGCCACCCCGAAGAGTTCTACAACCTGGTGCGCTTCCGG
ATCGGGGGCAAGCGGAAGGTGATGCCCAAGATGGACCAGGACTCGCTCAGCAGCAGCCTG
AAAACTTGCTACAAGTATCTCAATCAGACCAGTCGCAGTTTCGCAGCTGTTATCCAGGCG
CTGGATGGGGAAATGCGCAACGCAGTGTGCATATTTTATCTGGTTCTCCGAGCTCTGGAC
ACACTGGAAGATGACATGACCATCAGTGTGGAAAAGAAGGTCCCGCTGTTACACAACTTT
CACTCTTTCCTTTACCAACCAGACTGGCGGTTCATGGAGAGCAAGGAGAAGGATCGCCAG
GTGCTGGAGGACTTCCCAACGATCTCCCTTGAGTTTAGAAATCTGGCTGAGAAATACCAA
ACAGTGATTGCCGACATTTGCCGGAGAATGGGCATTGGGATGGCAGAGTTTTTGGATAAG
CATGTGACCTCTGAACAGGAGTGGGACAAGTACTGCCACTATGTTGCTGGGCTGGTCGGA
ATTGGCCTTTCCCGTCTTTTCTCAGCCTCAGAGTTTGAAGACCCCTTAGTTGGTGAAGAT
ACAGAACGTGCCAACTCTATGGGCCTGTTTCTGCAGAAAACAAACATCATCCGTGACTAT
CTGGAAGACCAGCAAGGAGGAAGAGAGTTCTGGCCTCAAGAGGTTTGGAGCAGGTATGTT
AAGAAGTTAGGGGATTTTGCTAAGCCGGAGAATATTGACTTGGCCGTGCAGTGCCTGAAT
GAACTTATAACCAATGCACTGCACCACATCCCAGATGTCATCACCTACCTTTCGAGACTC
AGAAACCAGAGTGTGTTTAACTTCTGCGCTATTCCACAGGTGATGGCCATTGCCACTTTG
GCTGCCTGTTATAATAACCAGCAGGTGTTCAAAGGGGCAGTGAAGATTCGGAAAGGGCAA
GCAGTGACCCTGATGATGGATGCCACCAATATGCCAGCTGTCAAAGCCATCATATATCAG
TATATGGAAGAGATTTATCATAGAATCCCCGACTCAGACCCATCTTCTAGCAAAACAAGG
CAGATCATCTCCACCATCCGGACGCAGAATCTTCCCAACTGTCAGCTGATTTCCCGAAGC
CACTACTCCCCCATCTACCTGTCGTTTGTCATGCTTTTGGCTGCCCTGAGCTGGCAGTAC
CTGACCACTCTCTCCCAGGTAACAGAAGACTATGTTCAGACTGGAGAACACTGA

1. Robinson GW, Tsay YH, Kienzle BK, Smith-Monroy CA, Bishop RW: Conservation between human and fungal squalene synthetases: similarities in structure, function, and regulation. Mol Cell Biol. 1993 May;13(5):2706-17. [PubMed ]
2. Jiang G, McKenzie TL, Conrad DG, Shechter I: Transcriptional regulation by lovastatin and 25-hydroxycholesterol in HepG2 cells and molecular cloning and expression of the cDNA for the human hepatic squalene synthase. J Biol Chem. 1993 Jun 15;268(17):12818-24. [PubMed ]
3. Summers C, Karst F, Charles AD: Cloning, expression and characterisation of the cDNA encoding human hepatic squalene synthase, and its relationship to phytoene synthase. Gene. 1993 Dec 22;136(1-2Che):185-92. [PubMed ]
4. Soltis DA, McMahon G, Caplan SL, Dudas DA, Chamberlin HA, Vattay A, Dottavio D, Rucker ML, Engstrom RG, Cornell-Kennon SA, et al.: Expression, purification, and characterization of the human squalene synthase: use of yeast and baculoviral systems. Arch Biochem Biophys. 1995 Feb 1;316(2):713-23. [PubMed ]

1. Phenylalanine--tRNA ligase
2. PheRS

MVGSALRRGAHAYVYLVSKASHISRGHQHQAWGSRPPAAECATQRAPGSVVELLGKSYPQ
DDHSNLTRKVLTRVGRNLHNQQHHPLWLIKERVKEHFYKQYVGRFGTPLFSVYDNLSPVV
TTWQNFDSLLIPADHPSRKKGDNYYLNRTHMLRAHTSAHQWDLLHAGLDAFLVVGDVYRR
DQIDSQHYPIFHQLEAVRLFSKHELFAGIKDGESLQLFEQSSRSAHKQETHTMEAVKLVE
FDLKQTLTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINFHGEWLEVLGCGVMEQQLVN
SAGAQDRIGWAFGLGLERLAMILYDIPDIRLFWCEDERFLKQFCVSNINQKVKFQPLSKY
PAVINDISFWLPSENYAENDFYDLVRTIGGDLVEKVDLIDKFVHPKTHKTSHCYRITYRH
MERTLSQREVRHIHQALQEAAVQLLGVEGRF

• Aminoacyl-tRNA biosynthesis (map00970 )
• Phenylalanine and Tyrosine Metabolism (map00400 )

• ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe)

• FDX-ACB (PF03147 )
• tRNA-synt_2d (PF01409 )

• None

• None

ATGGTGGGCTCAGCTCTCAGGAGAGGTGCCCATGCATATGTCTACCTGGTGAGTAAGGCC
AGTCACATCTCCAGAGGCCATCAGCACCAGGCCTGGGGATCGAGGCCTCCTGCAGCAGAG
TGTGCCACCCAAAGAGCTCCAGGCAGTGTGGTGGAGCTGCTGGGCAAATCCTACCCTCAG
GACGACCACAGCAACCTCACCCGGAAGGTCCTCACCAGAGTTGGCAGGAACCTGCACAAC
CAGCAGCATCACCCTCTGTGGCTGATCAAGGAGAGGGTGAAGGAGCACTTCTACAAGCAG
TATGTGGGCCGCTTTGGGACCCCGTTGTTCTCGGTCTACGACAACCTTTCTCCAGTGGTC
ACGACCTGGCAGAACTTTGACAGCCTGCTCATCCCAGCTGATCACCCCAGCAGGAAGAAG
GGGGACAACTATTACCTGAATCGGACTCACATGCTGAGAGCGCACACGTCTGCACACCAG
TGGGACTTGCTGCACGCGGGACTGGATGCCTTCCTGGTGGTGGGTGATGTCTACAGGCGT
GACCAGATCGACTCCCAGCACTACCCTATTTTCCACCAGCTGGAGGCCGTGCGGCTCTTC
TCCAAGCATGAGTTATTTGCTGGTATAAAGGATGGAGAAAGCCTGCAGCTCTTTGAACAA
AGTTCTCGCTCTGCGCATAAACAAGAGACACACACCATGGAGGCCGTGAAGCTTGTAGAG
TTTGATCTTAAGCAAACGCTTACCAGGCTCATGGCACATCTTTTTGGAGATGAGCTGGAG
ATAAGATGGGTAGACTGCTACTTCCCTTTTACACATCCTTCCTTTGAGATGGAGATCAAC
TTTCATGGAGAATGGCTGGAAGTTCTTGGCTGCGGGGTGATGGAACAACAACTGGTCAAT
TCAGCTGGTGCTCAAGACCGAATCGGCTGGGCTTTTGGCCTAGGATTAGAAAGGCTAGCC
ATGATCCTCTACGACATCCCTGATATCCGTCTCTTCTGGTGTGAGGACGAGCGCTTCCTG
AAGCAGTTCTGTGTATCCAACATTAATCAGAAGGTGAAGTTTCAGCCTCTTAGCAAATAT
CCGGCTGTGATCAATGATATTTCATTCTGGTTGCCCTCTGAGAATTACGCAGAAAATGAT
TTCTATGACTTAGTCCGAACAATTGGAGGAGACCTGGTGGAAAAGGTTGATCTCATAGAC
AAGTTTGTACATCCAAAGACGCACAAGACCAGCCACTGCTACCGCATCACGTACCGCCAC
ATGGAACGGACTCTGTCCCAGAGAGAGGTCAGGCACATCCACCAGGCCTTGCAGGAGGCT
GCAGTCCAGCTGTTGGGTGTGGAGGGCAGGTTCTGA

1. Bullard JM, Cai YC, Demeler B, Spremulli LL: Expression and characterization of a human mitochondrial phenylalanyl-tRNA synthetase. J Mol Biol. 1999 May 14;288(4):567-77. [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 ]

1. NMN adenylyltransferase 3

MKSRIPVVLLACGSFNPITNMHLRMFEVARDHLHQTGMYQVIQGIISPVNDTYGKKDLAA
SHHRVAMARLALQTSDWIRVDPWESEQAQWMETVKVLRHHHSKLLRSPPQMEGPDHGKAL
FSTPAAVPELKLLCGADVLKTFQTPNLWKDAHIQEIVEKFGLVCVGRVGHDPKGYIAESP
ILRMHQHNIHLAKEPVQNEISATYIRRALGQGQSVKYLIPDAVITYIKDHGLYTKGSTWK
GKSTQSTEGKTS

• Nicotinate and Nicotinamide Metabolism (map00760 )

• ATP + nicotinamide ribonucleotide = diphosphate + NAD+

• CTP_transf_2 (PF01467 )

• None

• None

ATGAAGAGCCGAATACCTGTGGTGCTCCTGGCCTGTGGCTCCTTTAACCCCATCACCAAC
ATGCACCTGCGCATGTTTGAGGTGGCCAGAGATCACCTACACCAAACAGGAATGTACCAG
GTCATCCAGGGTATCATCTCTCCTGTCAACGACACCTATGGGAAGAAAGACCTCGCAGCT
TCTCATCACCGAGTGGCCATGGCCCGGCTGGCCCTGCAGACATCCGACTGGATCCGGGTG
GACCCTTGGGAGAGTGAGCAGGCACAGTGGATGGAGACAGTGAAGGTGCTGAGGCATCAT
CACAGCAAACTGCTCAGATCTCCACCCCAGATGGAAGGCCCAGACCATGGCAAGGCACTC
TTCTCGACCCCTGCAGCTGTGCCTGAGCTGAAGCTTCTCTGTGGGGCAGACGTCTTGAAG
ACCTTCCAGACCCCCAACCTCTGGAAGGATGCGCACATCCAGGAAATAGTGGAGAAGTTT
GGCTTGGTGTGCGTGGGCCGAGTAAGTCACGACCCAAAAGGTTACATCGCAGAATCTCCC
ATCCTACGGATGCACCAGCACAACATTCACCTGGCCAAGGAGCCTGTGCAGAATGAGATC
AGTGCCACATACATCAGGCGAGCCTTGGGCCAAGGGCAGAGCGTAAAGTACCTGATTCCC
GATGCTGTCATCACGTACATCAAGGACCATGGCCTCTACACCAAGGGCAGTACCTGGAAA
GGCAAAAGCACCCAGAGCACTGAGGGCAAGACAAGCTAG

1. Quinolinate phosphoribosyltransferase [decarboxylating]
2. QAPRTase
3. QPRTase

MDAEGLALLLPPVTLAALVDSWLREDCPGLNYAALVSGAGPSQAALWAKSPGVLAGQPFF
DAIFTQLNCQVSWFLPEGSKLVPVARVAEVRGPAHCLLLGERVALNTLARCSGIASAAAA
AVEAARGAGWTGHVAGTRKTTPGFRLVEKYGLLVGGAASHRYDLGGLVMVKDNHVVAAGG
VEKAVRAARQAADFALKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKAQF
PSVAVEASGGITLDNLPQFCGPHIDVISMGMLTQAAPALDFSLKLFAKEVAPVPKIH

• Nicotinate and Nicotinamide Metabolism (map00760 )

• nicotinate D-ribonucleotide + diphosphate + CO2 = pyridine-2,3-dicarboxylate + 5-phospho-alpha-D-ribose 1-diphosphate

• QRPTase_C (PF01729 )
• QRPTase_N (PF02749 )

• 1-16

ATGGACGCTGAAGGCCTGGCGCTGCTGCTGCCGCCCGTCACCCTGGCAGCCCTGGTGGAC
AGCTGGCTCCGAGAGGACTGCCCAGGGCTCAACTACGCAGCCTTGGTCAGCGGGGCAGGC
CCCTCGCAGGCGGCGCTGTGGGCCAAATCCCCTGGGGTACTGGCAGGGCAGCCTTTCTTC
GATGCCATATTTACCCAACTCAACTGCCAAGTCTCCTGGTTCCTCCCCGAGGGATCGAAG
CTGGTGCCGGTGGCCAGAGTGGCCGAGGTCCGGGGCCCTGCCCACTGCCTGCTGCTGGGG
GAACGGGTGGCCCTCAACACGCTGGCCCGCTGCAGTGGCATTGCCAGTGCTGCCGCCGCT
GCAGTGGAGGCCGCCAGGGGGGCCGGCTGGACTGGGCACGTGGCAGGCACGAGGAAGACC
ACGCCAGGCTTCCGGCTGGTGGAGAAGTATGGGCTCCTGGTGGGCGGGGCCGCCTCGCAC
CGCTACGACCTGGGAGGGCTGGTGATGTTGAAGGATAACCATGTGGTGCCCCCCGGTGGC
GTGGAGAAGGCGGTGCGGGCGGCCAGACAGGCGGCTGACTTCGCTCTGAAGGTGGAAGTG
GAATGCAGCAGCCTGCAGGAGGTCGTCCAGGCAGCTGAGGCTGGCGCCGACCTTGTCCTG
CTGGACAACTTCAAGCCAGAGGAGCTGCACCCCACGGCCACCGCGCTGAAGGCCCAGTTC
CCGAGTGTGGCTGTGGAAGCCAGTGGGGGCATCACCCTGGACAACCTCCCCCAGTTCTGC
GGGCCGCACATAGACGTCATCTCCATGGGGATGCTGACCCAGGCGGTCCCAGCCCTTGAT
TTCTCCCTCAAGCTGTTTGCCAAAGAGGTGGCTCCAGTGCCCAAAATCCACTAG

1. Fukuoka SI, Nyaruhucha CM, Shibata K: Characterization and functional expression of the cDNA encoding human brain quinolinate phosphoribosyltransferase. Biochim Biophys Acta. 1998 Jan 21;1395(2):192-201. [PubMed ]

1. NMN adenylyltransferase 2

MTETTKTHVILLACGSFNPITKGHIQMFERARDYLHKTGRFIVIGGIVSPVHDSYGKQGL
VSSRHRLIMCQLAVQNSDWIRVDPWECYQDTWQTTCSVLEHHRDLMKRVTGCILSNVNTP
SMTPVIGQPQNETPQPIYQNSNVATKPTAAKILGKVGESLSRICCVRPPVERFTFVDENA
NLGTVMRYEEIELRILLLCGSDLLESFCIPGLWNEADMEVIVGDFGIVVVPRDAADTDRI
MNHSSILRKYKNNIMVVKDDINHPMSVVSSTKSRLALQHGDGHVVDYLSQPVIDYILKSQ
LYINASG

• Nicotinate and Nicotinamide Metabolism (map00760 )

• ATP + nicotinamide ribonucleotide = diphosphate + NAD+

• CTP_transf_2 (PF01467 )

• None

• None

ATGACCGAGACCACCAAGACCCACGTTATCTTGCTCGCCTGCGGCAGCTTCAATCCCATC
ACCAAAGGGCACATTCAGATGTTTGAAAGAGCCAGGGATTATCTGCACAAAACTGGAAGG
TTTATTGTGATTGGCGGGATTGTCTCCCCTGTCCACGACTCCTATGGAAAACAGGGCCTC
GTGTCAAGCCGGCACCGTCTCATCATGTGTCAGCTGGCCGTCCAGAATTCTGATTGGATC
AGGGTGGACCCTTGGGAGTGCTACCAGGACACCTGGCAGACGACCTGCAGCGTGTTGGAA
CACCACCGGGACCTCATGAAGAGGGTGACTGGCTGCATCCTCTCCAATGTCAACACACCT
TCCATGACACCTGTGATCGGACAGCCACAAAACGAGACCCCCCAGCCCATTTACCAGAAC
AGCAACGTGGCCACCAAGCCCACTGCAGCCAAGATCTTGGGGAAGGTGGGAGAAAGCCTC
AGCCGGATCTGCTGTGTCCGCCCGCCGGTGGAGCGTTTCACCTTTGTAGATGAGAATGCC
AATCTGGGCACGGTGATGCGGTATGAAGAGATTGAGCTACGGATCCTGCTGCTGTGTGGT
AGTGACCTGCTGGAGTCCTTCTGCATCCCAGGGCTCTGGAACGAGGCAGATATGGAGGTG
ATTGTTGGTGACTTTGGGATTGTGGTGGTGCCCCGGGATGCAGCCGACACAGACCGAATC
ATGAATCACTCCTCAATACTCCGCAAATACAAAAACAACATCATGGTGGTGAAGGATGAC
ATCAACCATCCCATGTCTGTTGTCAGCTCAACCAAGAGCAGGCTGGCCCTGCAGCATGGG
GACGGCCATGTTGTGGATTACCTGTCCCAGCCGGTCATCGACTACATCCTCAAAAGCCAG
CTGTACATCAATGCCTCCGGCTAG

1. Sood R, Bonner TI, Makalowska I, Stephan DA, Robbins CM, Connors TD, Morgenbesser SD, Su K, Faruque MU, Pinkett H, Graham C, Baxevanis AD, Klinger KW, Landes GM, Trent JM, Carpten JD: Cloning and characterization of 13 novel transcripts and the human RGS8 gene from the 1q25 region encompassing the hereditary prostate cancer (HPC1) locus. Genomics. 2001 Apr 15;73(2):211-22. [PubMed ]
2. Seki N, Ohira M, Nagase T, Ishikawa K, Miyajima N, Nakajima D, Nomura N, Ohara O: Characterization of cDNA clones in size-fractionated cDNA libraries from human brain. DNA Res. 1997 Oct 31;4(5):345-9. [PubMed ]

1. PAPS synthetase 1
2. PAPSS 1
3. Sulfurylase kinase 1
4. SK1
5. SK 1[Includes: Sulfate adenylyltransferase
6. Sulfate adenylate transferase
7. SAT
8. ATP-sulfurylase
9. Adenylyl-sulfate kinase
10. Adenylylsulfate 3'-phosphotransferase
11. APS kinase
12. Adenosine-5'-phosphosulfate 3'-phosphotransferase
13. 3'- phosphoadenosine-5'-phosphosulfate synthetase]

MEIPGSLCKKVKLSNNAQNWGMQRATNVTYQAHHVSRNKRGQVVGTRGGFRGCTVWLTGL
SGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLF
ADAGLVCITSFISPYTQDRNNARQIHEGASLPFFEVFVDAPLHVCEQRDVKGLYKKARAG
EIKGFTGIDSEYEKPEAPELVLKTDSCDVNDCVQQVVELLQERDIVPVDASYEVKELYVP
ENKLHLAKTDAETLPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGG
VINLSVPIVLTATHEDKERLDGCTAFALMYEGRRVAILRNPEFFEHRKEERCARQWGTTC
KNHPYIKMVMEQGDWLIGGDLQVLDRVYWNDGLDQYRLTPTELKQKFKDMNADAVFAFQL
RNPVHNGHALLMQDTHKQLLERGYRRPVLLLHPLGGWTKDDDVPLMWRMKQHAAVLEEGV
LNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHPETGKDLYEPS
HGAKVLTMAPGLITLEIVPFRVAAYNKKKKRMDYYDSEHHEDFEFISGTRMRKLAREGQK
PPEGFMAPKAWTVLTEYYKSLEKA

• Purine Metabolism (map00230 )
• Selenoamino Acid Metabolism (map00450 )
• Sulfate and Sulfite Metabolism (map00920 )

• ATP + sulfate = diphosphate + adenylylsulfate

• APS_kinase (PF01583 )
• ATP-sulfurylase (PF01747 )

• None

• None

ATGGAGATCCCCGGGAGCTTGTGCAAGAAAGTCAAGCTGAGCAATAACGCGCAGAACTGG
GGAATGCAGAGAGCAACCAATGTCACCTACCAAGCCCATCATGTCAGCAGGAACAAGAGA
GGTCAGGTGGTGGGGACCAGAGGTGGCTTTCGTGGTTGCACAGTTTGGCTAACAGGCTTG
TCTGGAGCGGGAAAGACTACTGTGAGCATGGCCTTGGAGGAGTACCTGGTTTGTCATGGT
ATTCCATGCTACACTCTGGATGGTGACAATATTCGTCAAGGTCTCAATAAAAATCTTGGC
TTTAGTCCTGAAGACAGAGAAGAGAATGTTCGACGCATCGCAGAAGTTGCTAAACTGTTT
GCAGATGCTGGCTTAGTGTGCATCACAAGTTTCATATCACCTTACACTCAGGATCGCAAC
AATGCAAGGCAAATTCATGAAGGTGCAAGTTTACCGTTTTTTGAAGTATTTGTTGATGCT
CCTCTGCATGTTTGTGAACAGAGGGATGTCAAAGGACTCTACAAAAAAGCCCGGGCAGGA
GAAATTAAAGGTTTCACTGGGATCGATTCTGAATATGAAAAGCCAGAGGCCCCTGAGTTG
GTGCTGAAAACAGACTCCTGTGATGTAAATGACTGTGTCCAGCAAGTTGTGGAACTTCTA
CAGGAACGGGATATTGTACCTGTGGATGCATCTTATGAAGTAAAAGAACTATATGTGCCA
GAAAATAAACTTCATTTGGCAAAAACAGATGCGGAAACATTACCAGCACTGAAAATTAAT
AAAGTGGATATGCAGTGGGTGCAGGTTTTGGCAGAAGGTTGGGCAACCCCATTGAATGGC
TTTATGAGAGAGAGGGAGTACTTGCAGTGCCTTCATTTTGATTGTCTTCTGGATGGAGGT
GTCATTAACTTGTCAGTACCTATAGTTCTGACTGCGACTCATGAAGATAAAGAGAGGCTG
GACGGCTGTACAGCATTTGCTCTGATGTATGAGGGCCGCCGTGTGGCCATTCTTCGCAAT
CCAGAGTTTTTTGAGCACAGGAAAGAGGAGCGCTGTGCCAGACAGTGGGGAACGACATGC
AAGAACCACCCCTATATTAAGATGGTGATGGAACAAGGAGATTGGCTGATTGGAGGAGAT
CTTCAAGTCTTGGATCGAGTTTATTGGAATGATGGTCTTGATCAGTATCGTCTTACTCCT
ACTGAGCTAAAGCAGAAATTTAAAGATATGAATGCTGATGCTGTCTTTGCATTTCAACTA
CGCAACCCAGTGCACAATGGACATGCCCTGTTAATGCAGGATACCCATAAGCAACTTCTA
GAGAGGGGCTACCGGCGCCCTGTCCTCCTCCTCCACCCTCTGGGTGCTTGGACAAAGGAT
GACGATGTTCCTTTGATGTGGCGTATGAAGCAGCATGCTGCAGTGTTGGAGGAAGGAGTT
CTGAATCCTGAGACGACAGTGGTGGCCATCTTCCCATCTCCCATGATGTATGCTGGACCA
ACTGAGGTCCAGTGGCATTGCAGAGCACGGATGGTTGCAGGAGCCAACTTTTACATTGTT
GGACGAGACCCTGCTGGCATGCCTCATCCAGAAACAGGGAAGGATCTTTATGAGCCAAGT
CATGGTGCCAAAGTGCTGACGATGGCCCCTGGTTTAATCACTTTGGAAATAGTTCCCTTT
CGAGTTGCAGCTTACAACAAGAAAAAGAAGCGTATGGACTACTATGACTCTGAACACCAT
GAAGACTTTGAATTTATTTCAGGAACACGAATGCGCAAACTTGCTCGAGAAGGCCAGAAA
CCACCTGAAGGTTTCATGGCTCCCAAGGCTTGGACCGTGCTGACAGAATACTACAAATCC
TTGGAGAAAGCTTAG

1. Girard JP, Baekkevold ES, Amalric F: Sulfation in high endothelial venules: cloning and expression of the human PAPS synthetase. FASEB J. 1998 May;12(7):603-12. [PubMed ]
2. Venkatachalam KV, Akita H, Strott CA: Molecular cloning, expression, and characterization of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its functional domains. J Biol Chem. 1998 Jul 24;273(30):19311-20. [PubMed ]
3. Yanagisawa K, Sakakibara Y, Suiko M, Takami Y, Nakayama T, Nakajima H, Takayanagi K, Natori Y, Liu MC: cDNA cloning, expression, and characterization of the human bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase enzyme. Biosci Biotechnol Biochem. 1998 May;62(5):1037-40. [PubMed ]
4. Xu ZH, Otterness DM, Freimuth RR, Carlini EJ, Wood TC, Mitchell S, Moon E, Kim UJ, Xu JP, Siciliano MJ, Weinshilboum RM: Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 (PAPSS1) and PAPSS2: gene cloning, characterization and chromosomal localization. Biochem Biophys Res Commun. 2000 Feb 16;268(2):437-44. [PubMed ]
5. Venkatachalam KV, Fuda H, Koonin EV, Strott CA: Site-selected mutagenesis of a conserved nucleotide binding HXGH motif located in the ATP sulfurylase domain of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase. J Biol Chem. 1999 Jan 29;274(5):2601-4. [PubMed ]

1. PAPS synthetase 2
2. PAPSS 2
3. Sulfurylase kinase 2
4. SK2
5. SK 2[Includes: Sulfate adenylyltransferase
6. Sulfate adenylate transferase
7. SAT
8. ATP-sulfurylase
9. Adenylyl-sulfate kinase
10. Adenylylsulfate 3'-phosphotransferase
11. APS kinase
12. Adenosine-5'-phosphosulfate 3'-phosphotransferase
13. 3'- phosphoadenosine-5'-phosphosulfate synthetase]

MSGIKKQKTENQQKSTNVVYQAHHVSRNKRGQVVGTRGGFRGCTVWLTGLSGAGKTTISF
ALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRIAEVAKLFADAGLVCITS
FISPFAKDRENARKIHESAGLPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDS
DYEKPETPERVLKTNLSTVSDCVHQVVELLQEQNIVPYTIIKDIHELFVPENKLDHVRAE
AETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHFDTLLDDGVINMSIPIVL
PVSAEDKTRLEGCSKFVLAHGGRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVM
ESGDWLVGGDLQVLEKIRWNDGLDQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHAL
LMQDTRRRLLERGYKHPVLLLHPLGGWTKDDDVPLDWRMKQHAAVLEEGVLDPKSTIVAI
FPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMAP
GLTSVEIIPFRVAAYNKAKKAMDFYDPARHNEFDFISGTRMRKLAREGENPPDGFMAPKA
WKVLTDYYRSLEKN

• Purine Metabolism (map00230 )
• Selenoamino Acid Metabolism (map00450 )
• Sulfate and Sulfite Metabolism (map00920 )

• ATP + sulfate = diphosphate + adenylylsulfate

• APS_kinase (PF01583 )
• ATP-sulfurylase (PF01747 )

• None

• None

ATGTCGGGGATCAAGAAGCAAAAGACGGAGAACCAGCAGAAATCCACCAATGTAGTCTAT
CAGGCCCACCATGTGAGCAGGAATAAGAGAGGGCAAGTGGTTGGAACAAGGGGTGGGTTC
CGAGGATGTACCGTGTGGCTAACAGGTCTCTCTGGTGCTGGAAAAACAACGATAAGTTTT
GCCCTGGAGGAGTACCTTGTCTCCCATGCCATCCCTTGTTACTCCCTGGATGGGGACAAT
GTCCGTCATGGCCTTAACAGAAATCTCGGATTCTCTCCTGGGGACAGAGAGGAAAATATC
CGCCGGATTGCTGAGGTGGCTAAGCTGTTTGCTGATGCTGGTCTGGTCTGCATTACCAGC
TTTATTTCTCCATTCGCAAAGGATCGTGAGAATGCCCGCAAAATACATGAATCAGCAGGG
CTGCCATTCTTTGAAATATTTGTAGATGCACCTCTAAATATTTGTGAAAGCAGAGACGTA
AAAGGCCTCTATAAAAGGGCCAGAGCTGGGGAGATTAAAGGATTTACAGGTATTGATTCT
GATTATGAGAAACCTGAAACTCCTGAGCGTGTGCTTAAAACCAATTTGTCCACAGTGAGT
GACTGTGTCCACCAGGTAGTGGAACTTCTGCAAGAGCAGAACATTGTACCCTATACTATA
ATCAAAGATATCCACGAACTCTTTGTGCCGGAAAACAAACTTGACCACGTCCGAGCTGAG
GCTGAAACTCTCCCTTCATTATCAATTACTAAGCTGGATCTCCAGTGGGTCCAGGTTTTG
AGCGAAGGCTGGGCCACTCCCCTCAAAGGTTTCATGCGGGAGAAGGAGTACTTACAGGTT
ATGCACTTTGACACCCTGCTAGATGATGGCGTGATCAACATGAGCATCCCCATTGTACTG
CCCGTCTCTGCAGAGGATAAGACACGGCTGGAAGGGTGCAGCAAGTTTGTCCTGGCACAT
GGTGGACGGAGGGTAGCTATCTTACGAGACGCTGAATTCTATGAACACAGAAAAGAGGAA
CGCTGTTCCCGTGTTTGGGGGACAACATGTACAAAACACCCCCATATCAAAATGGTGATG
GAAAGTGGGGACTGGCTGGTTGGTGGAGACCTTCAGGTGCTGGAGAAAATAAGATGGAAT
GATGGGCTGGACCAATACCGTCTGACACCTCTGGAGCTCAAACAGAAATGTAAAGAAATG
AATGCTGATGCGGTGTTTGCATTCCAGTTGCGCAATCCTGTCCACAATGGCCATGCCCTG
TTGATGCAGGACACCTGCCGCAGGCTCCTAGAGAGGGGCTACAAGCACCCGGTCCTCCTA
CTACACCCTCTGGGCGGCTGGACCAAGGATGACGATGTGCCTCTAGACTGGCGGATGAAG
CAGCACGCGGCTGTGCTCGAGGAAGGGGTCCTGGATCCCAAGTCAACCATTGTTGCCATC
TTTCCGTCTCCCATGTTATATGCTGGCCCCACAGAGGTCCAGTGGCACTGCAGGTCCCGG
ATGATTGCGGGTGCCAATTTCTACATTGTGGGGAGGGACCCTGCAGGAATGCCCCATCCT
GAAACCAAGAAGGATCTGTATGAACCCACTCATGGGGGCAAGGTCTTGAGCATGGCCCCT
GGCCTCACCTCTGTGGAAATCATTCCATTCCGAGTGGCTGCCTACAACAAAGCCAAAAAA
GCCATGGACTTCTATGATCCAGCAAGGCACAATGAGTTTGACTTCATCTCAGGAACTCGA
ATGAGGAAGCTCGCCCGGGAAGGAGAGAATCCCCCAGATGGCTTCATGGCCCCCAAAGCA
TGGAAGGTCCTGACAGATTATTACAGGTCCCTGGAGAAGAACTAA

1. ul Haque MF, King LM, Krakow D, Cantor RM, Rusiniak ME, Swank RT, Superti-Furga A, Haque S, Abbas H, Ahmad W, Ahmad M, Cohn DH: Mutations in orthologous genes in human spondyloepimetaphyseal dysplasia and the brachymorphic mouse. Nat Genet. 1998 Oct;20(2):157-62. [PubMed ]
2. Xu ZH, Otterness DM, Freimuth RR, Carlini EJ, Wood TC, Mitchell S, Moon E, Kim UJ, Xu JP, Siciliano MJ, Weinshilboum RM: Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 (PAPSS1) and PAPSS2: gene cloning, characterization and chromosomal localization. Biochem Biophys Res Commun. 2000 Feb 16;268(2):437-44. [PubMed ]
3. Kurima K, Singh B, Schwartz NB: Genomic organization of the mouse and human genes encoding the ATP sulfurylase/adenosine 5'-phosphosulfate kinase isoform SK2. J Biol Chem. 1999 Nov 19;274(47):33306-12. [PubMed ]
4. Ahmad M, Haque MF, Ahmad W, Abbas H, Haque S, Krakow D, Rimoin DL, Lachman RS, Cohn DH: Distinct, autosomal recessive form of spondyloepimetaphyseal dysplasia segregating in an inbred Pakistani kindred. Am J Med Genet. 1998 Aug 6;78(5):468-73. [PubMed ]

1. CMP-N- acetylneuraminic acid synthetase
2. CMP-NeuNAc synthetase

MDSVEKGAATSVSNPRGRPSRGRPPKLQRNSRGGQGRGVEKPPHLAALILARGGSKGIPL
KNIKHLAGVPLIGWVLRAALDSGAFQSVWVSTDHDEIENVAKQFGAQVHRRSSEVSKDSS
TSLDAIIEFLNYHNEVDIVGNIQATSPCLHPTDLQKVAEMIREEGYDSVFSVVRRHQFRW
SEIQKGVREVTEPLNLNPAKRPRRQDWDGELYENGSFYFAKRHLIEMGYLQGGKMAYYEM
RAEHSVDIDVDIDWPIAEQRVLRYGYFGKEKLKEIKLLVCNIDGCLTNGHIYVSGDQKEI
ISYDVKDAIGISLLKKSGIEVRLISERACSKQTLSSLKLDCKMEVSVSDKLAVVDEWRKE
MGLCWKEVAYLGNEVSDEECLKRVGLSGAPADACSTAQKAVGYICKCNGGRGAIREFAEH
ICLLMEKVNNSCQK

• Aminosugars metabolism (map00530 )

• CTP + N-acylneuraminate = diphosphate + CMP-N-acylneuraminate

• CTP_transf_3 (PF02348 )

• None

• None

ATGGACTCGGTGGAGAAGGGGGCCGCCACCTCCGTCTCCAACCCGCGGGGGCGACCGTCC
CGGGGCCGGCCGCCGAAGCTGCAGCGCAACTCTCGCGGCGGCCAGGGCCGAGGTGTGGAG
AAGCCCCCGCACCTGGCAGCCCTAATTCTGGCCCGGGGAGGCAGCAAAGGCATCCCCCTG
AAGAACATTAAGCACCTGGCGGGGGTCCCGCTCATTGGCTGGGTCCTGCGTGCGGCCCTG
GATTCAGGGGCCTTCCAGAGTGTATGGGTTTCGACAGACCATGATGAAATTGAGAATGTG
GCCAAACAATTTGGTGCACAAGTTCATCGAAGAAGTTCTGAAGTTTCAAAAGACAGCTCT
ACCTCACTAGATGCCATCATAGAATTTCTTAATTATYATAATGAGGKTGACATTGTAGGA
AATATTCAAGCTACTTCTYCATGTTTACATCCTACTGATCTTCAAAAAGTTGCAGAAATG
ATTCGAGAAGAAGGATATGATTCTGKTTTCTCTGTTGTGAGACGCCATCAGTTTCGATGG
AGTGAAATTCAGAAAGGAGTTCGTGAAGTGACCGAACCTCTGAATTTAAATCCAGCTAAA
CGGCCTCGTCGACAAGACTGGGATGGAGAATTATATGAAAATGGCTCATTTTATTTTGCT
AAAAGACATTTGATAGAGATGGGTTACTTGCAGGGTGGAAAAATGGCATACTACGAAATG
CGAGCTGAACATAGTGTGGATATAGATGTGGATATTGATTGGCCTATTGCAGAGCAAAGA
GTATTAAGATATGGCTATTTTGGCAAAGAGAAGCTTAAGGAAATAAAACTTTTGGTTTGC
AATATTGATGGATGTCTCACCAATGGCCACATTTATGTATCAGGAGACCAAAAAGAAATA
ATATCTTATGATGTAAAAGATGCTATTGGGATAAGTTTATTAAAGAAAAGTGGTATTGAG
GTGAGGCTAATCTCAGAAAGGGCCTGTTCAAAGCAGACGCTGTCTTCTTTAAAACTGGAT
TGCAAAATGGAAGTCAGTGTATCAGACAAGCTAGCAGTTGTAGATGAATGGAGAAAAGAA
ATGGGCCTGTGCTGGAAAGAAGTGGCATATCTTGGAAATGAAGTGTCTGATGAAGAGTGC
TTGAAGAGAGTGGGCCTAAGTGGCGCTCCTGCTGATGCCTGTTCCTACGCCCAGAAGGCT
GTTGGATACATTTGCAAATGTAATGGTGGCCGTGGTGCCATCCGAGAATTTGCAGAGCAC
ATTTGCCTACTAATGGAAAAAGTTAATAATTCATGCCAAAAATAG

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

MNGPVDGLCDHSLSEGVFMFTSESVGEGHPDKICDQISDAVLDAHLKQDPNAKVACETVC
KTGMVLLCGEITSMAMVDYQRVVRDTIKHIGYDDSAKGFDFKTCNVLVALEQQSPDIAQC
VHLDRNEEDVGAGDQGLMFGYATDETEECMPLTIILAHKLNARMADLRRSGLLPWLRPDS
KTQVTVQYMQDNGAVIPVRIHTIVISVQHNEDITLEEMRRALKEQVIRAVVPAKYLDEDT
VYHLQPSGRFVIGGPQGDAGVTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARW
VAKSLVKAGLCRRVLVQVSYAIGVAEPLSISIFTYGTSQKTERELLDVVHKNFDLRPGVI
VRDLDLKKPIYQKTACYGHFGRSEFPWEVPRKLVF

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

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

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

• None

• None

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

1. Alvarez L, Corrales F, Martin-Duce A, Mato JM: Characterization of a full-length cDNA encoding human liver S-adenosylmethionine synthetase: tissue-specific gene expression and mRNA levels in hepatopathies. Biochem J. 1993 Jul 15;293 ( Pt 2):481-6. [PubMed ]
2. Horikawa S, Tsukada K: Molecular cloning and nucleotide sequence of cDNA encoding the human liver S-adenosylmethionine synthetase. Biochem Int. 1991 Sep;25(1):81-90. [PubMed ]
3. Ubagai T, Lei KJ, Huang S, Mudd SH, Levy HL, Chou JY: Molecular mechanisms of an inborn error of methionine pathway. Methionine adenosyltransferase deficiency. J Clin Invest. 1995 Oct;96(4):1943-7. [PubMed ]
4. Chamberlin ME, Ubagai T, Mudd SH, Wilson WG, Leonard JV, Chou JY: Demyelination of the brain is associated with methionine adenosyltransferase I/III deficiency. J Clin Invest. 1996 Aug 15;98(4):1021-7. [PubMed ]
5. Chamberlin ME, Ubagai T, Mudd SH, Levy HL, Chou JY: Dominant inheritance of isolated hypermethioninemia is associated with a mutation in the human methionine adenosyltransferase 1A gene. Am J Hum Genet. 1997 Mar;60(3):540-6. [PubMed ]
6. Chamberlin ME, Ubagai T, Mudd SH, Thomas J, Pao VY, Nguyen TK, Levy HL, Greene C, Freehauf C, Chou JY: Methionine adenosyltransferase I/III deficiency: novel mutations and clinical variations. Am J Hum Genet. 2000 Feb;66(2):347-55. [PubMed ]

1. ITPase
2. Inosine triphosphatase
3. Putative oncogene protein hlc14-06-p

MAASLVGKKIVFVTGNAKKLEEVVQILGDKFPCTLVAQKIDLPEYQGEPDEISIQKCQEA
VRQVQGPVLVEDTCLCFNALGGLPGPYIKWFLEKLKPEGLHQLLAGFEDKSAYALCTFAL
STGDPSQPVRLFRGRTSGRIVAPRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNAVSHRFR
ALLELQEYFGSLAA

• Purine Metabolism (map00230 )
• Pyrimidine Metabolism (map00240 )

• A nucleoside triphosphate + H2O = a nucleotide + diphosphate

• Ham1p_like (PF01725 )

• None

• None

ATGGCGGCCTCATTGGTGGGGAAGAAGATCGTGTTTGTAACGGGGAACGCCAAGAAGCTG
GAGGAGGTCGTTCAGATTCTAGGAGATAAGTTTCCACGCACTTTGGTGGCACAGAAAATT
GACCTGCCGGAGTACCAGGGGGAGCCGGATGAGATTTCCATACAGAAATGTCAGGAGGCA
GTTCGCCAGGTACAGGGGCCCGTGCTGGTTGAGGACACTTGTCTGTGCTTCAATGCCCTT
GGAGGGCTCCCCGGCCCCTACATAAAGTGGTTTCTGGAGAAGTTAAAGCCTGAAGGTCTC
CACCAGCTCCTGGCCGGGTTCGAGGACAAGTCAGCCTATGCGCTCTGCACGTTTGCACTC
AGCACCGGGGACCCAAGCCAGCCCGTGCGCCTGTTCAGGGGCCGGACCTCGGGCCGGATC
GTGGCACCCAGAGGCTGCCAGGACTTTGGCTGGGACCCCTGCTTTCAGCCTGATGGATAT
GAGCAGACGTACGCAGAGATGCCTAAGGCGGAGAAGAACGCTGTCTCCCATCGCTTCCGG
GCCCTGCTGGAGCTGCAGGAGTACTTTGGCAGTTTGGCAGCTTGA

1. Lin S, McLennan AG, Ying K, Wang Z, Gu S, Jin H, Wu C, Liu W, Yuan Y, Tang R, Xie Y, Mao Y: Cloning, expression, and characterization of a human inosine triphosphate pyrophosphatase encoded by the itpa gene. J Biol Chem. 2001 Jun 1;276(22):18695-701. Epub 2001 Mar 13. [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. Sumi S, Marinaki AM, Arenas M, Fairbanks L, Shobowale-Bakre M, Rees DC, Thein SL, Ansari A, Sanderson J, De Abreu RA, Simmonds HA, Duley JA: Genetic basis of inosine triphosphate pyrophosphohydrolase deficiency. Hum Genet. 2002 Oct;111(4-5):360-7. Epub 2002 Aug 15. [PubMed ]
4. Cao H, Hegele RA: DNA polymorphisms in ITPA including basis of inosine triphosphatase deficiency. J Hum Genet. 2002;47(11):620-2. [PubMed ]

1. dUTPase
2. dUTP pyrophosphatase

MTPLCPRPALCYHFLTSLLRSAMQNARGTAEGRSRGTLRARPAPRPPAAQHGIPRPLSSA
GRLSQGCRGASTVGAAGWKGELPKAGGSPAPGPETPAISPSKRARPAEVGGMQLRFARLS
EHATAPTRGSARAAGYDLYSAYDYTIPPMEKAVVKTDIQIALPSGCYGRVAPRSGLAAKH
FIDVGAGVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLICERIFYPEIEEVQALDDTE
RGSGGFGSTGKN

• Pyrimidine Metabolism (map00240 )

• dUTP + H2O = dUMP + diphosphate

• dUTPase (PF00692 )

• 1-24

ATGACTCCCCTCTGCCCTCGCCCCGCGCTCTGCTACCATTTCCTTACGTCTCTGCTTCGC
TCAGCGATGCAAAACGCGCGAGGCACGGCAGAGGGCCGAAGCCGCGGTACTCTCCGGGCC
AGGCCCGCCCCTCGGCCGCCGGCCGCGCAGCACGGGATTCCCCGGCCGCTGTCCAGCGCT
GGCCGCCTGAGCCAAGGCTGCCGCGGAGCCAGTACAGTCGGGGCCGCTGGCTGGAAGGGC
GAGCTTCCTAAGGCGGGGGGAAGCCCGGCGCCGGGGCCGGAGACACCCGCCATTTCACCC
AGTAAGCGGGCCCGGCCTGCGGAGGTGGGCGGCATGCAGCTCCGCTTTGCCCGGCTCTCC
GAGCACGCCACGGCCCCCACCCGGGGCTCCGCGCGCGCCGCGGGCTACGACCTGTACAGT
GCCTATGATTACACAATACCACCTATGGAGAAAGCTGTTGTGAAAACGGACATTCAGATA
GCGCTCCCTTCTGGGTGTTATGGAAGAGTGGCTCCACGGTCAGGCTTGGCTGCAAAACAC
TTTATTGATGTAGGAGCTGGTGTCATAGATGAAGATTATAGAGGAAATGTTGGTGTTGTA
CTGTTTAATTTTGGCAAAGAAAAGTTTGAAGTCAAAAAAGGTGATCGAATTGCACAGCTC
ATTTGCGAACGGATTTTTTATCCAGAAATAGAAGAAGTTCAAGCCTTGGATGACACCGAA
AGGGGTTCAGGAGGTTTTGGTTCCACTGGAAAGAATTAA

1. Ladner RD, McNulty DE, Carr SA, Roberts GD, Caradonna SJ: Characterization of distinct nuclear and mitochondrial forms of human deoxyuridine triphosphate nucleotidohydrolase. J Biol Chem. 1996 Mar 29;271(13):7745-51. [PubMed ]
2. McIntosh EM, Ager DD, Gadsden MH, Haynes RH: Human dUTP pyrophosphatase: cDNA sequence and potential biological importance of the enzyme. Proc Natl Acad Sci U S A. 1992 Sep 1;89(17):8020-4. [PubMed ]
3. Strahler JR, Zhu XX, Hora N, Wang YK, Andrews PC, Roseman NA, Neel JV, Turka L, Hanash SM: Maturation stage and proliferation-dependent expression of dUTPase in human T cells. Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):4991-5. [PubMed ]

1. APRT

MADSELQLVEQRIRSFPDFPTPGVVFRDISPVLKDPASFRAAIGLLARHLKATHGGRIDY
IAGLDSRGFLFGPSLAQELGLGCVLIRKRGKLPGPTLWASYSLEYGKAELEIQKDALEPG
QRVVVVDDLLATGGTMNAACELLGRLQAEVLECVSLVELTSLKGREKLAPVPFFSLLQYE

• Purine Metabolism (map00230 )

• AMP + diphosphate = adenine + 5-phospho-alpha-D-ribose 1-diphosphate

• Pribosyltran (PF00156 )

• None

• None

ATGGCCGACTCCGAGCTGCAGCTGGTTGAGCAGCGGATCCGCAGCTTCCCCGACTTCCCC
ACCCCAGGCGTGGTATTCAGGGACATCTCGCCCGTCCTGAAGGACCCCGCCTCCTTCCGC
GCCGCCATCGGCCTCCTGGCGCGACACCTGAAGGCGACCCACGGGGGCCGCATCGACTAC
ATCGCAGGCCTAGACTCCCGAGGCTTCCTCTTTGGCCCCTCCCTGGCCCAGGAGCTTGGA
CTGGGCTGCGTGCTCATCCGAAAGCGGGGGAAGCTGCCAGGCCCCACTCTGTGGGCCTCC
TATTCCCTGGAGTACGGGAAGGCTGAGCTGGAGATTCAGAAAGACGCCCTGGAGCCAGGA
CAGAGGGTGGTCGTCGTGGATGATCTGCTGGCCACTGGTGGAACCATGAACGCTGCCTGT
GAGCTGCTGGGCCGCCTGCAGGCTGAGGTCCTGGAGTGCGTGAGCCTGGTGGAGCTGACC
TCGCTTAAGGGCAGGGAGAAGCTGGCACCTGTACCCTTCTTCTCTCTCCTGCAGTATGAG
TGA

1. Hidaka Y, Tarle SA, O'Toole TE, Kelley WN, Palella TD: Nucleotide sequence of the human APRT gene. Nucleic Acids Res. 1987 Nov 11;15(21):9086. [PubMed ]
2. Broderick TP, Schaff DA, Bertino AM, Dush MK, Tischfield JA, Stambrook PJ: Comparative anatomy of the human APRT gene and enzyme: nucleotide sequence divergence and conservation of a nonrandom CpG dinucleotide arrangement. Proc Natl Acad Sci U S A. 1987 May;84(10):3349-53. [PubMed ]
3. Wilson JM, O'Toole TE, Argos P, Shewach DS, Daddona PE, Kelley WN: Human adenine phosphoribosyltransferase. Complete amino acid sequence of the erythrocyte enzyme. J Biol Chem. 1986 Oct 15;261(29):13677-83. [PubMed ]
4. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed ]
5. Chen J, Sahota A, Laxdal T, Scrine M, Bowman S, Cui C, Stambrook PJ, Tischfield JA: Identification of a single missense mutation in the adenine phosphoribosyltransferase (APRT) gene from five Icelandic patients and a British patient. Am J Hum Genet. 1991 Dec;49(6):1306-11. [PubMed ]
6. Sahota A, Chen J, Boyadjiev SA, Gault MH, Tischfield JA: Missense mutation in the adenine phosphoribosyltransferase gene causing 2,8-dihydroxyadenine urolithiasis. Hum Mol Genet. 1994 May;3(5):817-8. [PubMed ]
7. Hidaka Y, Palella TD, O'Toole TE, Tarle SA, Kelley WN: Human adenine phosphoribosyltransferase. Identification of allelic mutations at the nucleotide level as a cause of complete deficiency of the enzyme. J Clin Invest. 1987 Nov;80(5):1409-15. [PubMed ]
8. Hidaka Y, Tarle SA, Fujimori S, Kamatani N, Kelley WN, Palella TD: Human adenine phosphoribosyltransferase deficiency. Demonstration of a single mutant allele common to the Japanese. J Clin Invest. 1988 Mar;81(3):945-50. [PubMed ]
9. Kamatani N, Hakoda M, Otsuka S, Yoshikawa H, Kashiwazaki S: Only three mutations account for almost all defective alleles causing adenine phosphoribosyltransferase deficiency in Japanese patients. J Clin Invest. 1992 Jul;90(1):130-5. [PubMed ]
10. Deng L, Yang M, Frund S, Wessel T, De Abreu RA, Tischfield JA, Sahota A: 2,8-Dihydroxyadenine urolithiasis in a patient with considerable residual adenine phosphoribosyltransferase activity in cell extracts but with mutations in both copies of APRT. Mol Genet Metab. 2001 Mar;72(3):260-4. [PubMed ]

1. HGPRT
2. HGPRTase

MATRSPGVVISDDEPGYDLDLFCIPNHYAEDLERVFIPHGLIMDRTERLARDVMKEMGGH
HIVALCVLKGGYKFFADLLDYIKALNRNSDRSIPMTVDFIRLKSYCNDQSTGDIKVIGGD
DLSTLTGKNVLIVEDIIDTGKTMQTLLSLVRQYNPKMVKVASLLVKRTPRSVGYKPDFVG
FEIPDKFVVGYALDYNEYFRDLNHVCVISETGKAKYKA

• Purine Metabolism (map00230 )

• IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate

• Pribosyltran (PF00156 )

• None

• None

ATGGCGACCCGCAGCCCTGGCGTCGTGATTAGTGATGATGAACCAGGTTATGACCTTGAT
TTATTTTGCATACCTAATCATTATGCTGAGGATTTGGAAAGGGTGTTTATTCCTCATGGA
CTAATTATGGACAGGACTGAACGTCTTGCTCGAGATGTGATGAAGGAGATGGGAGGCCAT
CACATTGTAGCCCTCTGTGTGCTCAAGGGGGGCTATAAATTCTTTGCTGACCTGCTGGAT
TACATCAAAGCACTGAATAGAAATAGTGATAGATCCATTCCTATGACTGTAGATTTTATC
AGACTGAAGAGCTATTGTAATGACCAGTCAACAGGGGACATAAAAGTAATTGGTGGAGAT
GATCTCTCAACTTTAACTGGAAAGAATGTCTTGATTGTGGAAGATATAATTGACACTGGC
AAAACAATGCAGACTTTGCTTTCCTTGGTCAGGCAGTATAATCCAAAGATGGTCAAGGTC
GCAAGCTTGCTGGTGAAAAGGACCCCACGAAGTGTTGGATATAAGCCAGACTTTGTTGGA
TTTGAAATTCCAGACAAGTTTGTTGTAGGATATGCCCTTGACTATAATGAATACTTCAGG
GATTTGAATCATGTTTGTGTCATTAGTGAAACTGGAAAAGCAAAATACAAAGCCTAA

1. Jolly DJ, Okayama H, Berg P, Esty AC, Filpula D, Bohlen P, Johnson GG, Shively JE, Hunkapillar T, Friedmann T: Isolation and characterization of a full-length expressible cDNA for human hypoxanthine phosphoribosyl transferase. Proc Natl Acad Sci U S A. 1983 Jan;80(2):477-81. [PubMed ]
2. Edwards A, Voss H, Rice P, Civitello A, Stegemann J, Schwager C, Zimmermann J, Erfle H, Caskey CT, Ansorge W: Automated DNA sequencing of the human HPRT locus. Genomics. 1990 Apr;6(4):593-608. [PubMed ]
3. Wilson JM, Tarr GE, Mahoney WC, Kelley WN: Human hypoxanthine-guanine phosphoribosyltransferase. Complete amino acid sequence of the erythrocyte enzyme. J Biol Chem. 1982 Sep 25;257(18):10978-85. [PubMed ]
4. Patel PI, Framson PE, Caskey CT, Chinault AC: Fine structure of the human hypoxanthine phosphoribosyltransferase gene. Mol Cell Biol. 1986 Feb;6(2):393-403. [PubMed ]
5. Eads JC, Scapin G, Xu Y, Grubmeyer C, Sacchettini JC: The crystal structure of human hypoxanthine-guanine phosphoribosyltransferase with bound GMP. Cell. 1994 Jul 29;78(2):325-34. [PubMed ]
6. Shi W, Li CM, Tyler PC, Furneaux RH, Grubmeyer C, Schramm VL, Almo SC: The 2.0 A structure of human hypoxanthine-guanine phosphoribosyltransferase in complex with a transition-state analog inhibitor. Nat Struct Biol. 1999 Jun;6(6):588-93. [PubMed ]
7. Balendiran GK, Molina JA, Xu Y, Torres-Martinez J, Stevens R, Focia PJ, Eakin AE, Sacchettini JC, Craig SP 3rd: Ternary complex structure of human HGPRTase, PRPP, Mg2+, and the inhibitor HPP reveals the involvement of the flexible loop in substrate binding. Protein Sci. 1999 May;8(5):1023-31. [PubMed ]
8. Sculley DG, Dawson PA, Emmerson BT, Gordon RB: A review of the molecular basis of hypoxanthine-guanine phosphoribosyltransferase (HPRT) deficiency. Hum Genet. 1992 Nov;90(3):195-207. [PubMed ]
9. Wilson JM, Kobayashi R, Fox IH, Kelley WN: Human hypoxanthine-guanine phosphoribosyltransferase. J Biol Chem. 1983 May 25;258(10):6458-60. [PubMed ]
10. Wilson JM, Kelley WN: Molecular basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in a patient with the Lesch-Nyhan syndrome. J Clin Invest. 1983 May;71(5):1331-5. [PubMed ]
11. Wilson JM, Tarr GE, Kelley WN: Human hypoxanthine (guanine) phosphoribosyltransferase: an amino acid substitution in a mutant form of the enzyme isolated from a patient with gout. Proc Natl Acad Sci U S A. 1983 Feb;80(3):870-3. [PubMed ]
12. Wilson JM, Kelley WN: Human hypoxanthine-guanine phosphoribosyltransferase. Structural alteration in a dysfunctional enzyme variant (HPRTMunich) isolated from a patient with gout. J Biol Chem. 1984 Jan 10;259(1):27-30. [PubMed ]
13. Cariello NF, Scott JK, Kat AG, Thilly WG, Keohavong P: Resolution of a missense mutant in human genomic DNA by denaturing gradient gel electrophoresis and direct sequencing using in vitro DNA amplification: HPRT Munich. Am J Hum Genet. 1988 May;42(5):726-34. [PubMed ]
14. Davidson BL, Pashmforoush M, Kelley WN, Palella TD: Genetic basis of hypoxanthine guanine phosphoribosyltransferase deficiency in a patient with the Lesch-Nyhan syndrome (HPRTFlint). Gene. 1988 Mar 31;63(2):331-6. [PubMed ]
15. Davidson BL, Palella TD, Kelley WN: Human hypoxanthine-guanine phosphoribosyltransferase: a single nucleotide substitution in cDNA clones isolated from a patient with Lesch-Nyhan syndrome (HPRTMidland). Gene. 1988 Aug 15;68(1):85-91. [PubMed ]
16. Fujimori S, Hidaka Y, Davidson BL, Palella TD, Kelley WN: Identification of a single nucleotide change in a mutant gene for hypoxanthine-guanine phosphoribosyltransferase (HPRT Ann Arbor). Hum Genet. 1988 May;79(1):39-43. [PubMed ]
17. Davidson BL, Chin SJ, Wilson JM, Kelley WN, Palella TD: Hypoxanthine-guanine phosphoribosyltransferase. Genetic evidence for identical mutations in two partially deficient subjects. J Clin Invest. 1988 Dec;82(6):2164-7. [PubMed ]
18. Keough DT, Gordon RB, de Jersey J, Emmerson BT: Biochemical basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in nine families. J Inherit Metab Dis. 1988;11(3):229-38. [PubMed ]
19. Igarashi T, Minami M, Nishida Y: Molecular analysis of hypoxanthine-guanine phosphoribosyltransferase mutations in five unrelated Japanese patients. Acta Paediatr Jpn. 1989 Jun;31(3):303-13. [PubMed ]
20. Davidson BL, Pashmforoush M, Kelley WN, Palella TD: Human hypoxanthine-guanine phosphoribosyltransferase deficiency. The molecular defect in a patient with gout (HPRTAshville). J Biol Chem. 1989 Jan 5;264(1):520-5. [PubMed ]
21. Fujimori S, Davidson BL, Kelley WN, Palella TD: Identification of a single nucleotide change in the hypoxanthine-guanine phosphoribosyltransferase gene (HPRTYale) responsible for Lesch-Nyhan syndrome. J Clin Invest. 1989 Jan;83(1):11-3. [PubMed ]
22. Davidson BL, Tarle SA, Palella TD, Kelley WN: Molecular basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in ten subjects determined by direct sequencing of amplified transcripts. J Clin Invest. 1989 Jul;84(1):342-6. [PubMed ]
23. Gibbs RA, Nguyen PN, McBride LJ, Koepf SM, Caskey CT: Identification of mutations leading to the Lesch-Nyhan syndrome by automated direct DNA sequencing of in vitro amplified cDNA. Proc Natl Acad Sci U S A. 1989 Mar;86(6):1919-23. [PubMed ]
24. Gibbs RA, Nguyen PN, Edwards A, Civitello AB, Caskey CT: Multiplex DNA deletion detection and exon sequencing of the hypoxanthine phosphoribosyltransferase gene in Lesch-Nyhan families. Genomics. 1990 Jun;7(2):235-44. [PubMed ]
25. Skopek TR, Recio L, Simpson D, Dallaire L, Melancon SB, Ogier H, O'Neill JP, Falta MT, Nicklas JA, Albertini RJ: Molecular analyses of a Lesch-Nyhan syndrome mutation (hprtMontreal) by use of T-lymphocyte cultures. Hum Genet. 1990 Jun;85(1):111-6. [PubMed ]
26. Gordon RB, Sculley DG, Dawson PA, Beacham IR, Emmerson BT: Identification of a single nucleotide substitution in the coding sequence of in vitro amplified cDNA from a patient with partial HPRT deficiency (HPRTBRISBANE). J Inherit Metab Dis. 1990;13(5):692-700. [PubMed ]
27. Davidson BL, Tarle SA, Van Antwerp M, Gibbs DA, Watts RW, Kelley WN, Palella TD: Identification of 17 independent mutations responsible for human hypoxanthine-guanine phosphoribosyltransferase (HPRT) deficiency. Am J Hum Genet. 1991 May;48(5):951-8. [PubMed ]
28. Tarle SA, Davidson BL, Wu VC, Zidar FJ, Seegmiller JE, Kelley WN, Palella TD: Determination of the mutations responsible for the Lesch-Nyhan syndrome in 17 subjects. Genomics. 1991 Jun;10(2):499-501. [PubMed ]
29. Sculley DG, Dawson PA, Beacham IR, Emmerson BT, Gordon RB: Hypoxanthine-guanine phosphoribosyltransferase deficiency: analysis of HPRT mutations by direct sequencing and allele-specific amplification. Hum Genet. 1991 Oct;87(6):688-92. [PubMed ]
30. Yamada Y, Goto H, Ogasawara N: Identification of two independent Japanese mutant HPRT genes using the PCR technique. Adv Exp Med Biol. 1991;309B:121-4. [PubMed ]
31. Lightfoot T, Joshi R, Nuki G, Snyder FF: The point mutation of hypoxanthine-guanine phosphoribosyltransferase (HPRTEdinburgh) and detection by allele-specific polymerase chain reaction. Hum Genet. 1992 Mar;88(6):695-6. [PubMed ]
32. Sege-Peterson K, Chambers J, Page T, Jones OW, Nyhan WL: Characterization of mutations in phenotypic variants of hypoxanthine phosphoribosyltransferase deficiency. Hum Mol Genet. 1992 Sep;1(6):427-32. [PubMed ]
33. Burgemeister R, Rotzer E, Gutensohn W, Gehrke M, Schiel W: Identification of a new missense mutation in exon 2 of the human hypoxanthine phosphoribosyltransferase gene (HPRTIsar): a further example of clinical heterogeneity in HPRT deficiencies. Hum Mutat. 1995;5(4):341-4. [PubMed ]
34. Fujimori S, Sakuma R, Yamaoka N, Hakoda M, Yamanaka H, Kamatani N: An asymptomatic germline missense base substitution in the hypoxanthine phosphoribosyltransferase (HPRT) gene that reduces the amount of enzyme in humans. Hum Genet. 1997 Jan;99(1):8-10. [PubMed ]
35. Liu G, Aral B, Zabot MT, Kamoun P, Ceballos-Picot I: The molecular basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in French families; report of two novel mutations. Hum Mutat. 1998;Suppl 1:S88-90. [PubMed ]

1. Biotin apo-protein ligase[Includes: Biotin--[methylmalonyl-CoA-carboxytransferase] ligase
2. Holocarboxylase synthetase
3. HCS
4. Biotin-- [methylcrotonoyl-CoA-carboxylase] ligase

MEDRLHMDNGLVPQKIVSVHLQDSTLKEVKDQVSNKQAQILEPKPEPSLEIKPEQDGMEH
VGRDDPKALGEEPKQRRGSASGSEPAGDSDRGGGPVEHYHLHLSSCHECLELENSTIESV
KFASAENIPDLPYDYSSSLESVADETSPEREGRRVNLTGKAPNILLYVGSDSQEALGRFH
EVRSVLADCVDIDSYILYHLLEDSALRDPWTDNCLLLVIATRESIPEDLYQKFMAYLSQG
GKVLGLSSSFTFGGFQVTSKGALHKTVQNLVFSKADQSEVKLSVLSSGCRYQEGPVRLSP
GRLQGHLENEDKDRMIVHVPFGTRGGEAVLCQVHLELPPSSNIVQTPEDFNLLKSSNFRR
YEVLREILTTLGLSCDMKQVPALTPLYLLSAAEEIRDPLMQWLGKHVDSEGEIKSGQLSL
RFVSSYVSEVEITPSCIPVVTNMEAFSSEHFNLEIYRQNLQTKQLGKVILFAEVTPTTMR
LLDGLMFQTPQEMGLIVIAARQTEGKGRGGNVWLSPVGCALSTLLISIPLRSQLGQRIPF
VQHLMSVAVVEAVRSIPEYQDINLRVKWPNDIYYSDLMKIGGVLVNSTLMGETFYILIGC
GFNVTNSNPTICINDLITEYNKQHKAELKPLRADYLIARVVTVLEKLIKEFQDKGPNSVL
PLYYRYWVHSGQQVHLGSAEGPKVSIVGLDDSGFLQVHQEGGEVVTVHPDGNSFDMLRNL
ILPKRR

• Biotin metabolism (map00780 )

• ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]

• BPL_C (PF02237 )
• BPL_LipA_LipB (PF03099 )

• None

• None

ATGGAAGATAGACTCCACATGGATAATGGACTGGTACCCCAAAAGATTGTGTCGGTGCAC
TTGCAGGACTCCACTCTGAAGGAAGTTAAGGATCAGGTCTCAAACAAGCAAGCCCAGATC
CTAGAGCCGAAGCCTGAACCTTCTCTTGAGATTAAGCCTGAGCAGGACGGTATGGAGCAT
GTTGGCAGAGATGACCCAAAGGCTCTTGGTGAAGAACCCAAACAAAGGAGAGGCAGTGCC
TCTGGGAGTGAGCCTGCTGGGGACAGTGACAGGGGAGGGGGCCCCGTTGAGCATTATCAC
CTCCATCTGTCTAGTTGCCACGAGTGTCTGGAACTTGAGAACAGCACCATTGAGTCAGTC
AAGTTTGCGTCTGCCGAGAACATTCCAGACCTTCCCTACGATTATAGCAGCAGTTTGGAG
AGTGTTGCTGATGAGACCTCCCCCGAAAGAGAAGGGAGGAGAGTCAACCTCACGGGAAAG
GCACCCAACATCCTCCTCTATGTGGGCTCCGACTCCCAGGAAGCCCTCGGCCGGTTCCAC
GAGGTCCGGTCTGTGCTGGCCGACTGTGTGGACATTGACAGTTATATTCTCTACCACCTG
CTGGAGGACAGTGCTCTCAGAGACCCGTGGACGGACAACTGTCTGCTGTTGGTCATTGCT
ACCAGGGAGTCCATTCCCGAAGACCTGTACCAGAAGTTCATGGCCTATCTTTCTCAGGGA
GGGAAGGTGTTGGGCCTGTCTTCATCCTTCACCTTTGGTGGCTTTCAGGTGACAAGCAAG
GGTGCACTGCACAAGACAGTCCAGAACTTGGTTTTCTCCAAGGCTGACCAGAGCGAGGTG
AAGCTCAGCGTCTTGAGCAGTGGCTGCAGGTACCAGGAAGGCCCCGTCCGGCTCAGCCCC
GGCAGGCTCCAGGGCCACCTGGAGAATGAGGACAAGGACAGGATGATTGTGCATGTGCCT
TTTGGAACTCGCGGGGGAGAAGCTGTTCTTTGCCAGGTGCACTTAGAACTACCTCCCAGC
TCCAACATAGTGCAAACTCCAGAAGATTTTAACTTGCTCAAGTCAAGCAATTTTAGAAGA
TACGAAGTCCTTAGAGAGATTCTGACAACCCTTGGCCTCAGCTGTGACATGAAACAAGTT
CCTGCCTTAACTCCTCTTTACTTGCTGTCAGCTGCGGAGGAAATCAGGGATCCTCTTATG
CAGTGGCTTGGGAAACATGTGGACTCCGAGGGAGAAATAAAATCCGGCCAGCTCTCTCTT
AGATTTGTTTCATCCTACGTGTCTGAAGTAGAAATAACCCCATCTTGTATACCTGTGGTG
ACCAACATGGAGGCCTTCTCATCAGAACATTTCAACTTAGAGATCTATCGCCAAAATCTG
CAGACCAAGCAGTTGGGGAAAGTAATTTTGTTTGCCGAAGTGACCCCCACAACGATGCGT
CTCCTGGATGGGCTGATGTTTCAGACACCGCAGGAAATGGGCTTAATAGTGATCGCGGCC
CGGCAGACCGAGGGCAAAGGACGGGGAGGGAATGTGTGGCTGAGCCCTGTGGGATGTGCT
CTTTCTACTCTGCTCATCTCCATTCCACTGAGATCCCAGCTGGGACAGAGGATCCCGTTT
GTCCAGCATCTGATGTCCGTGGCTGTCGTGGAAGCAGTGAGGTCCATTCCCGAGTATCAG
GATATCAACTTACGAGTGAAGTGGCCCAACGATATTTATTACAGTGACCTCATGAAGATC
GGCGGAGTTCTGGTTAACTCAACACTCATGGGAGAAACATTTTATATACTTATTGGCTGT
GGATTTAATGTGACTAACAGTAACCCTACCATCTGCATCAACGACCTCATCACAGAATAC
AATAAACAACACAAGGCAGAACTGAAGCCCTTAAGAGCCGATTATCTCATCGCCAGAGTC
GTGACTGTGCTGGAGAAACTGATCAAAGAGTTTCAGGACAAAGGGCCCAACAGCGTCCTT
CCCCTTTATTACCGATACTGGGTCCACAGTGGTCAGCAAGTCCATCTGGGCAGCGCAGAG
GGACCAAAGGTGTCCATCGTTGGCCTGGACGATTCTGGCTTCCTCCAGGTTCACCAGGAG
GGCGGCGAGGTTGTGACTGTGCACCCGGACGGCAACTCCTTCGACATGCTGAGAAACCTC
ATCCTCCCCAAACGGCGGTAA

1. Suzuki Y, Aoki Y, Ishida Y, Chiba Y, Iwamatsu A, Kishino T, Niikawa N, Matsubara Y, Narisawa K: Isolation and characterization of mutations in the human holocarboxylase synthetase cDNA. Nat Genet. 1994 Oct;8(2):122-8. [PubMed ]
2. Yang X, Aoki Y, Li X, Sakamoto O, Hiratsuka M, Kure S, Taheri S, Christensen E, Inui K, Kubota M, Ohira M, Ohki M, Kudoh J, Kawasaki K, Shibuya K, Shintani A, Asakawa S, Minoshima S, Shimizu N, Narisawa K, Matsubara Y, Suzuki Y: Structure of human holocarboxylase synthetase gene and mutation spectrum of holocarboxylase synthetase deficiency. Hum Genet. 2001 Nov;109(5):526-34. Epub 2001 Oct 5. [PubMed ]
3. Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [PubMed ]
4. Dahmane N, Ghezala GA, Gosset P, Chamoun Z, Dufresne-Zacharia MC, Lopes C, Rabatel N, Gassanova-Maugenre S, Chettouh Z, Abramowski V, Fayet E, Yaspo ML, Korn B, Blouin JL, Lehrach H, Poutska A, Antonarakis SE, Sinet PM, Creau N, Delabar JM: Transcriptional map of the 2.5-Mb CBR-ERG region of chromosome 21 involved in Down syndrome. Genomics. 1998 Feb 15;48(1):12-23. [PubMed ]
5. Aoki Y, Suzuki Y, Sakamoto O, Li X, Takahashi K, Ohtake A, Sakuta R, Ohura T, Miyabayashi S, Narisawa K: Molecular analysis of holocarboxylase synthetase deficiency: a missense mutation and a single base deletion are predominant in Japanese patients. Biochim Biophys Acta. 1995 Dec 12;1272(3):168-74. [PubMed ]
6. Dupuis L, Leon-Del-Rio A, Leclerc D, Campeau E, Sweetman L, Saudubray JM, Herman G, Gibson KM, Gravel RA: Clustering of mutations in the biotin-binding region of holocarboxylase synthetase in biotin-responsive multiple carboxylase deficiency. Hum Mol Genet. 1996 Jul;5(7):1011-6. [PubMed ]
7. Aoki Y, Suzuki Y, Li X, Sakamoto O, Chikaoka H, Takita S, Narisawa K: Characterization of mutant holocarboxylase synthetase (HCS): a Km for biotin was not elevated in a patient with HCS deficiency. Pediatr Res. 1997 Dec;42(6):849-54. [PubMed ]
8. Aoki Y, Li X, Sakamoto O, Hiratsuka M, Akaishi H, Xu L, Briones P, Suormala T, Baumgartner ER, Suzuki Y, Narisawa K: Identification and characterization of mutations in patients with holocarboxylase synthetase deficiency. Hum Genet. 1999 Feb;104(2):143-8. [PubMed ]

1. Phenylalanine-- tRNA ligase beta chain
2. PheRS

MPTVSVKRDLLFQALGRTYTDEEFDELCFEFGLELDEITSEKEIISKEQGNVKAAGASDV
VLYKIDVPANRYDLLCLEGLVRGLQVFKERIKAPVYKRVMPDGKIQKLIITEETAKIRPF
AVAAVLRNIKFTKDRYDSFIELQEKLHQNICRKRALVAIGTHDLDTLSGPFTYTAKRPSD
IKFKPLNKTKEYTACELMNIYKTDNHLKHYLHIIENKPLYPVIYDSNGVVLSMPPIINGD
HSRITVNTRNIFIECTGTDFTKAKIVLDIIVTMFSEYCENQFTVEAAEVVFPNGKSHTFP
ELAYRKEMVRADLINKKVGIRETPENLAKLLTRMYLKSEVIGDGNQIEIEIPPTRADIIH
ACDIVEDAAIAYGYNNIQMTLPKTYTIANQFPLNKLTELLRHDMAAAGFTEALTFALCSQ
EDIADKLGVDISATKAVHISNPKTAEFQVARTTLLPGLLKTIAANRKMPLPLKLFEISDI
VIKDSNTDVGAKNYRHLCAVYYNKNPGFEIIHGLLDRIMQLLDVPPGEDKGGYVIKASEG
PAFFPGRCAEIFARGQSVGKLGVLHPDVITKFELTMPCSSLEINIGPFL

• Aminoacyl-tRNA biosynthesis (map00970 )
• Phenylalanine and Tyrosine Metabolism (map00400 )

• ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe)

• B3_4 (PF03483 )
• B5 (PF03484 )

• None

• None

ATGCCGACTGTCAGCGTGAAGCGTGATCTGCTCTTCCAAGCCCTGGGCCGCACCTACACT
GACGAAGAATTTGATGAACTATGTTTTGAATTTGGTCTGGAGCTTGATGAAATTACATCT
GAGAAGGAAATAATAAGTAAAGAACAAGGTAATGTAAAGGCAGCAGGAGCCTCTGATGTT
GTTCTTTACAAAATTGACGTCCCTGCCAATAGATATGATCTCCTGTGTCTGGAAGGATTG
GTTCGAGGACTTCAGGTCTTCAAAGAAAGGATAAAGGCTCCAGTGTATAAACGGGTAATG
CCTGATGGAAAAATCCAGAAATTGATTATCACAGAAGAGACAGCTAAGATACGTCCTTTT
GCGGTAGCAGCAGTTCTCCGTAATATAAAGTTTACTAAAGATCGATATGACAGCTTCATT
GAACTTCAGGAGAAATTACATCAGAATATTTGCAGGAAAAGAGCACTGGTTGCCATTGGT
ACCCATGATTTGGACACTTTGTCGGGCCCATTTACTTATACTGCAAAGCGTCCTTCAGAT
ATCAAATTCAAGCCTCTAAATAAGACCAAGGAGTATACAGCCTGTGAACTGATGAACATA
TACAAGACTGACAATCACCTGAAACATTATTTACATATCATTGAAAACAAACCCCTGTAT
CCAGTTATCTATGATAGCAATGGTGTCGTCCTTTCAATGCCTCCCATCATCAATGGGGAT
CATTCCAGAATAACAGTAAATACTAGAAATATTTTTATTGAATGCACGGGAACTGACTTT
ACTAAGGCAAAAATAGTTCTTGATATTATTGTCACCATGTTCAGTGAATATTGTGAGAAT
CAATTTACGGTCGAAGCTGCTGAAGTGGTTTTTCCTAATGGAAAATCACATACCTTTCCA
GAATTAGCTTACCGAAAGGAGATGGTGAGAGCTGACCTAATTAACAAAAAAGTTGGAATC
AGAGAAACTCCAGAAAATCTTGCCAAACTTCTGACCAGGATGTATTTAAAATCAGAAGTC
ATAGGTGATGGGAATCAGATTGAGATTGAAATCCCTCCAACCAGAGCTGACATTATCCAT
GCATGTGATATTGTAGAAGATGCAGCTATTGCTTATGGATATAACAACATTCAGATGACT
CTCCCGAAAACTTACACCATAGCTAATCAATTTCCTCTTAATAAGCTCACTGAACTTCTC
CGACATGACATGGCAGCCGCTGGCTTCACTGAAGCACTTACCTTTGCCCTGTGCTCCCAA
GAAGATATTGCTGATAAACTAGGTGTGGATATCTCTGCAACAAAGGCAGTCCACATAAGT
AATCCTAAAACAGCTGAATTTCAGGTGGCACGCACTACCCTTCTTCCTGGCCTCCTGAAG
ACCATAGCAGCAAATCGTAAGATGCCCCTTCCACTGAAACTGTTTGAAATCTCTGACATT
GTAATAAAAGATTCTAATACAGATGTAGGTGCAAAAAACTACAGACATCTCTGTGCTGTT
TATTACAACAAGAATCCTGGGTTTGAGATCATTCATGGGCTGCTGGACAGAATTATGCAG
TTGCTCGATGTGCCTCCTGGTGAAGACAAGGGGGGATATGTGATCAAAGCATCAGAAGGG
CCTGCTTTCTTCCCCGGGCGATGTGCAGAGATCTTTGCCAGGGTTCAAAGCGTCGGGAAG
CTTGGGGTCCTTCATCCTGACGTTATCACCAAATTTGAGCTGACCATGCCCTGCTCCTCC
CTAGAAATCAATATTGGACCCTTTTTGTGA

1. Rodova M, Ankilova V, Safro MG: Human phenylalanyl-tRNA synthetase: cloning, characterization of the deduced amino acid sequences in terms of the structural domains and coordinately regulated expression of the alpha and beta subunits in chronic myeloid leukemia cells. Biochem Biophys Res Commun. 1999 Feb 24;255(3):765-73. [PubMed ]
2. Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed ]

1. Ubiquitin-protein ligase A
2. Ubiquitin carrier protein A
3. HR6A
4. hHR6A

MSTPARRRLMRDFKRLQEDPPAGVSGAPSENNIMVWNAVIFGPEGTPFEDGTFKLTIEFT
EEYPNKPPTVRFVSKMFHPNVYADGSICLDILQNRWSPTYDVSSILTSIQSLLDEPNPNS
PANSQAAQLYQENKREYEKRVSAIVEQSWRDC

• Ubiquitin mediated proteolysis (map04120 )

• ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine

• UQ_con (PF00179 )

• None

• None

ATGTCCACCCCGGCTCGGCGGCGCCTCATGCGGGACTTCAAGAGGTTGCAGGAGGATCCT
CCAGCCGGAGTCAGCGGGGCTCCGTCCGAGAACAACATAATGGTGTGGAACGCGGTCATT
TTCGGGCCTGAAGGGACCCCGTTTGGGGATGGAACATTTAAACTTACAATAGAATTCACT
GAAGAATATCCAAATAAACCACCTACAGTTAGATTTGTCTCTAAGATGTTCCATCCAAAT
GTCTATGCAGATGGTAGTATATGTCTGGACATACTTCAGAACCGTTGGAGTCCAACCTAT
GATGTGTCTTCCATTCTAACATCCATACAGTCTCTGTTGGATGAACCCAATCCCAATAGT
CCAGCAAACAGCCAGGCTGCTCAGCTGTACCAGGAGAACAAACGGGAATATGAAAAGCGT
GTTTCTGCAATAGTAGAACAAAGCTGGCGTGATTGTTGA

1. Koken MH, Reynolds P, Jaspers-Dekker I, Prakash L, Prakash S, Bootsma D, Hoeijmakers JH: Structural and functional conservation of two human homologs of the yeast DNA repair gene RAD6. Proc Natl Acad Sci U S A. 1991 Oct 15;88(20):8865-9. [PubMed ]

1. Ubiquitin-conjugating enzyme E2 M
2. NEDD8 protein ligase
3. NEDD8 carrier protein

MIKLFSLKQQKKEEESAGGTKGSSKKASAAQLRIQKDINELNLPKTCDISFSDPDDLLNF
KLVICPDEGFYKSGKFVFSFKVGQGYPHDPPKVKCETMVYHPNIDLEGNVCLNILREDWK
PVLTINSIIYGLQYLFLEPNPEDPLNKEAAEVLQNNRRLFEQNVQRSMRGGYIGSTYFER
CLK

• UQ_con (PF00179 )

• None

• None

ATGATCAAGCTGTTCTCGCTGAAGCAGCAGAAGAAGGAGGAGGAGTCGGCGGGCGGCACC
AAGGGCAGCAGCAAGAAGGCGTCGGCGGCGCAGCTGCGGATCCAGAAGGACATAAACGAG
CTGAACCTGCCCAAGACGTGTGATATCAGCTTCTCAGATCCAGACGACCTCCTCAACTTC
AAGCTGGTCATCTGTCCTGATGAGGGCTTCTACAAGAGTGGGAAGTTTGTGTTCAGTTTT
AAGGTGGGCCAGGGTTACCCGCATGATCCCCCCAAGGTGAAGTGTGAGACAATGGTCTAT
CACCCCAACATTGACCTCGAGGGCAACGTCTGCCTCAACATCCTCAGAGAGGACTGGAAG
CCAGTCCTTACGATAAACTCCATAATTTATGGCCTGCAGTATCTCTTCTTGGAGCCCAAC
CCCGAGGACCCACTGAACAAGGAGGCCGCAGAGGTCCTGCAGAACAACCGGCGGCTGTTT
GAGCAGAACGTGCAGCGCTCCATGCGGGGTGGCTACATCGGCTCCACCTACTTTGAGCGC
TGCCTGAAATAG

1. Osaka F, Kawasaki H, Aida N, Saeki M, Chiba T, Kawashima S, Tanaka K, Kato S: A new NEDD8-ligating system for cullin-4A. Genes Dev. 1998 Aug 1;12(15):2263-8. [PubMed ]
2. Gong L, Yeh ET: Identification of the activating and conjugating enzymes of the NEDD8 conjugation pathway. J Biol Chem. 1999 Apr 23;274(17):12036-42. [PubMed ]
3. Wada H, Yeh ET, Kamitani T: A dominant-negative UBC12 mutant sequesters NEDD8 and inhibits NEDD8 conjugation in vivo. J Biol Chem. 2000 Jun 2;275(22):17008-15. [PubMed ]

1. Ubiquitin- protein ligase L6
2. Ubiquitin carrier protein L6
3. UbcH8
4. Retinoic acid-induced gene B protein
5. RIG-B

MASMRVVKELEDLQKKPPPYLRNLSSDDANVLVWHALLLPDQPPYHLKAFNLRISFPPEY
PFKPPMIKFTTKIYHPNVDENGQICLPIISSENWKPCTKTCQVLEALNVLVNRPNIREPL
RMDLADLLTQNPELFRKNAEEFTLRFGVDRPS

• Ubiquitin mediated proteolysis (map04120 )

• ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine

• UQ_con (PF00179 )

• None

• None

ATGGCGAGCATGCGAGTGGTGAAGGAGCTGGAGGATCTTCAGAAGAAGCCTCCCCCATAC
CTGCGGAACCTGTCCAGCGATGATGCCAATGTCCTGGTGTGGCACGCTCTCCTCCTACCC
GACCAACCTCCCTACCACCTGAAAGCCTTCAACCTGCGCATCAGCTTCCCGCCGGAGTAT
CCGTTCAAGCCTCCCATGATCAAATTCACAACCAAGATCTACCACCCCAACGTGGACGAG
AACGGACAGATTTGCCTGCCCATCATCAGCAGTGAGAACTGGAAGCCTTGCACCAAGACT
TGCCAAGTCCTGGAGGCCCTCAATGTGCTGGTGAATAGACCGAATATCAGGGAGCCCCTG
CGGATGGACCTCGCTGACCTGCTGACACAGAATCCGGAGCTGTTCAGAAAGAATGCCGAA
GAGTTCACCCTCCGATTCGGAGTGGACCGGCCCTCCTAA

1. Kumar S, Kao WH, Howley PM: Physical interaction between specific E2 and Hect E3 enzymes determines functional cooperativity. J Biol Chem. 1997 May 23;272(21):13548-54. [PubMed ]
2. Ardley HC, Rose SA, Tan N, Leek JP, Markham AF, Robinson PA: Genomic organization of the human ubiquitin-conjugating enzyme gene, UBE2L6 on chromosome 11q12. Cytogenet Cell Genet. 2000;89(1-2):137-40. [PubMed ]

1. Glycine--tRNA ligase
2. GlyRS

MPSPRPVLLRGARAALLLLLPPRLLARPSLLLRRSLSAASCAPISLPAAASRSSMDGAGA
EEVLAPLRLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVLEAKELALQPKDDIVD
RAKMEDTLKRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEEQILEIDC
TMLTPEPVLKTSGHVDKFADFMVKDVKNGECFRADHLLKAHLQKLMSDKKCSVEKKSEME
SVLAQLDNYGQQELADLFVNYNVKSPITGNDLSPPVSFNLMFKTFIGPGGNMPGYLRPET
AQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPSEK
DHPKFQNVADLHLYLYSAKAQVSGQSARKMRLGDAVEQGVINNTVLGYFIGRIYLYLTKV
GISPDKLRFRQHMENEMAHYACDCWDAESKTSYGWIEIVGCADRSCYDLSCHARATKVPL
VAEKPLKEPKTVNVVQFEPSKGAIGKAYKKDAKLVMEYLAICDECYITEMEMLLNEKGEF
TIETEGKTFQLTKDMINVKRFQKTLYVEEVVPNVIEPSFGLGRIMYTVFEHTFHVREGDE
QRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHGVSHKVDDSSGSIGRRYAR
TDEIGVAFGVTIDFDTVNKTPHTATLRDRDSMRQIRAEISELPSIVQDLANGNITWADVE
ARYPLFEGQETGKKETIEE

• Aminoacyl-tRNA biosynthesis (map00970 )
• Glycine, Serine and Threonine Metabolism (map00260 )

• ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly)

• HGTP_anticodon (PF03129 )
• tRNA-synt_2b (PF00587 )
• WHEP-TRS (PF00458 )

• 1-26

ATGCCCTCTCCGCGTCCAGTGCTGCTTAGAGGTGCTCGCGCCGCTCTGCTGCTGCTGCTG
CCGCCCCGGCTCTTAGCCCGACCCTCGCTCCTGCTCCGCCGGTCCCTCAGCGCGGCCTCC
TGCGCCCCGATCTCCTTGCCCGCCGCCGCCTCCCGGAGCAGCATGGACGGCGCGGGGGCT
GAGGAGGTGCTGGCACCTCTGAGGCTAGCAGTGCGCCAGCAGGGAGATCTTGTGCGAAAA
CTCAAAGAAGATAAAGCACCCCAAGTAGACGTAGACAAAGCAGTGGCTGAGCTCAAAGCC
CGCAAGAGGGTTCTGGAAGCAAAGGAGCTGGCGTTACAGCCCAAAGATGATATTGTAGAC
CGAGCAAAAATGGAAGATACCCTGAAGAGGAGGTTTTTCTATGATCAAGCTTTTGCTATT
TATGGAGGTGTTAGTGGTCTGTATGACTTTGGGCCAGTTGGCTGTGCTTTGAAGAACAAT
ATTATTCAGACCTGGAGGCAGCACTTTATCCAAGAGGAACAGATCCTGGAGATCGATTGC
ACCATGCTCACCCCTGAGCCAGTTTTAAAGACCTCTGGCCATGTAGACAAATTTGCTGAC
TTCATGGTGAAAGACGTAAAAAATGGAGAATGTTTTCGTGCTGACCATCTATTAAAAGCT
CATTTACAGAAATTGATGTCTGATAAGAAGTGTTCTGTCGAAAAGAAATCAGAAATGGAA
AGTGTTTTGGCCCAGCTTGATAACTATGGACAGCAAGAACTTGCGGATCTTTTTGTGAAC
TATAATGTAAAATCTCCCATTACTGGAAATGATCTATCCCCTCCAGTGTCTTTTAACTTA
ATGTTCAAGACTTTCATTGGGCCTGGAGGAAACATGCCTGGGTACTTGAGACCAGAAACT
GCACAGGGGATTTTCTTGAATTTCAAACGACTTTTGGAGTTCAACCAAGGAAAGTTGCCT
TTTGCTGCTGCCCAGATTGGAAATTCTTTTAGAAATGAGATCTCCCCTCGATCTGGACTG
ATCAGAGTCAGAGAATTCACAATGGCAGAAATTGAGCACTTTGTAGATCCCAGTGAGAAA
GACCACCCCAAGTTCCAGAATGTGGCAGACCTTCACCTTTATTTGTATTCAGCAAAAGCC
CAGGTCAGCGGACAGTCCGCTCGGAAAATGCGCCTGGGAGATGCTGTTGAACAGGGTGTG
ATTAATAACACAGTATTAGGCTATTTCATTGGCCGCATCTACCTCTACCTCACGAAGGTT
GGAATATCTCCAGATAAACTCCGCTTCCGGCAGCACATGGAGAATGAGATGGCCCATTAT
GCCTGTGACTGTTGGGATGCAGAATCCAAAACATCCTACGGTTGGATTGAGATTGTTGGA
TGTGCTGATCGTTCCTGTTATGACCTCTCCTGTCATGCACGAGCCACCAAAGTCCCACTT
GTAGCTGAGAAACCTCTGAAAGAACCCAAAACAGTCAATGTTGTTCAGTTTGAACCCAGT
AAGGGAGCAATTGGTAAGGCATATAAGAAGGATGCAAAACTGGTGATGGAGTATCTTGCC
ATTTGTGATGAGTGCTACATTACAGAAATGGAGATGCTGCTGAATGAGAAAGGGGAATTC
ACAATTGAAACTGAAGGGAAAACATTTCAGTTAACAAAAGACATGATCAATGTGAAGAGA
TTCCAGAAAACACTATATGTGGAAGAAGTTGTTCCGAATGTAATTGAACCTTCCTTCGGC
CTGGGTAGGATCATGTATACGGTATTTGAACATACATTCCATGTACGAGAAGGAGATGAA
CAGAGAACATTCTTCAGTTTCCCTGCTGTAGTTGCTCCATTCAAATGTTCCGTCCTCCCA
CTGAGCCAAAACCAGGAGTTCATGCCATTTGTCAAGGAATTATCGGAAGCCCTGACCAGG
CATGGAGTATCTCACAAAGTAGACGATTCCTCTGGGTCAATCGGAAGGCGCTATGCCAGG
ACTGATGAGATTGGCGTGGCTTTTGGTGTCACCATTGACTTTGACACAGTGAACAAGACC
CCCCACACTGCAACTCTGAGGGACCGTGACTCAATGCGGCAGATAAGAGCAGAGATCTCT
GAGCTGCCCAGCATAGTCCAAGACCTAGCCAATGGCAACATCACATGGGCTGATGTGGAG
GCCAGGTATCCTCTGTTTGAAGGGCAAGAGACTGGTAAAAAAGAGACAATCGAGGAATGA

1. Shiba K, Schimmel P, Motegi H, Noda T: Human glycyl-tRNA synthetase. Wide divergence of primary structure from bacterial counterpart and species-specific aminoacylation. J Biol Chem. 1994 Nov 25;269(47):30049-55. [PubMed ]
2. Williams J, Osvath S, Khong TF, Pearse M, Power D: Cloning, sequencing and bacterial expression of human glycine tRNA synthetase. Nucleic Acids Res. 1995 Apr 25;23(8):1307-10. [PubMed ]
3. Ge Q, Trieu EP, Targoff IN: Primary structure and functional expression of human Glycyl-tRNA synthetase, an autoantigen in myositis. J Biol Chem. 1994 Nov 18;269(46):28790-7. [PubMed ]

1. Glutamate--tRNA ligase
2. Prolyl-tRNA synthetase
3. Proline--tRNA ligase]

MEHTEIDHWLEFSATKLSSCDSFTSTINELNHCLSLRTYLVGNSLSLADLCVWATLKGNA
AWQEQLKQKKAPVHVKRWFGFLEAQQAFQSVGTKWDVSTTKARVAPEKKQDVGKFVELPG
AEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVI
LEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRIESKHR
KNPIEKNLQMWEEMKKGSQFGHSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYN
VYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTV
LSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKI
WAFNKKVIDPVAPRYVALLKKEVIPVNVPEAQEEMKEVAKHPKNPEVGLKPVWYSPKVFI
EGADAETFSEGEMVTFINWGNLNITKIHKNADGKIISLDAKFNLENKDYKKTTKVTWLAE
TTHALPIPVICVTYEHLITKPVLGKDEDFKQYVNKNSKHEELMLGDPCLKDLKKGDIIQL
QRRGFFICDQPYEPVSPYSCKEAPCVLIYIPDGHTKEMPTSGSKEKTKVEATKNETSAPF
KERPTPSLNNNCTTSEDSLVLYNRVAVQGDVVRELKAKKAPKEDVDAAVKQLLSLKAEYK
EKTGQEYKPGNPPAEIGQNISSNSSASILESKSLYDEVAAQGEVVRKLKAEKSPKAKINE
AVECLLSLKAQYKEKTGKEYIPGQPPLSQSSDSSPTRNSEPAGLETPEAKVLFDKVASQG
EVVRKLKTEKAPKDQVDIAVQELLQLKAQYKSLIGVEYKPVSATGAEDKDKKKKEKENKS
EKQNKPQKQNDGQRKDPSKNQGGGLSSSGAGEGQGPKKQTRLGLEAKKEENLADWYSQVI
TKSEMIEYHDISGCYILRPWAYAIWEAIKDFFDAEIKKLGVENCYFPMFVSQSALEKEKT
HVADFAPEVAWVTRSGKTELAEPIAIRPTSETVMYPAYAKWVQSHRDLPIKLNQWCNVVR
WEFKHPQPFLRTREFLWQEGHSAFATMEEAAEEVLQILDLYAQVYEELLAIPVVKGRKTE
KEKFAGGDYTTTIEAFISASGRAIQGGTSHHLGQNFSKMFEIVFEDPKIPGEKQFAYQNS
WGLTTRTIGVMTMVHGDNMGLVLPPRVACVQVVIIPCGITNALSEEDKEALIAKCNDYRR
RLLSVNIRVRADLRDNYSPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTV
AENEAETKLQAILEDIQVTLFTRASEDLKTHMVVANTMEDFQKILDSGKIVQIPFCGEID
CEDWIKKTTARDQDLEPGAPSMGAKSLCIPFKPLCELQPGAKCVCGKNPAKYYTLFGRSY

• Aminoacyl-tRNA biosynthesis (map00970 )
• Glutamate Metabolism (map00251 )
• Porphyrin Metabolism (map00860 )

• ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)

• HGTP_anticodon (PF03129 )
• ProRS-C_1 (PF09180 )
• tRNA-synt_1c (PF00749 )
• tRNA-synt_1c_C (PF03950 )
• tRNA-synt_2b (PF00587 )
• WHEP-TRS (PF00458 )

• None

• None

ATGGAACATACTGAGATTGATCACTGGTTGGAGTTCAGTGCTACAAAATTATCTTCATGT
GATTCCTTTACTTCTACAATTAATGAACTCAATCATTGCCTGTCTCTGAGAACATACTTA
GTTGGAAACTCCTTGAGTTTAGCAGATTTATGTGTTTGGGCCACCCTAAAAGGAAATGCT
GCCTGGCAAGAACAGTTGAAACAGAAGAAAGCTCCAGTTCATGTAAAACGTTGGTTTGGC
TTTCTTGAAGCCCAGCAGGCCTTCCAGTCAGTAGGTACCAAGTGGGATGTTTCAACAACC
AAAGCTCGAGTGGCACCTGAGAAAAAGCAAGATGTTGGGAAATTTGTTGAGCTTCCAGGT
GCGGAGATGGGAAAGGTTACCGTCAGATTTCCTCCAGAGGCCAGTGGTTACTTACACATT
GGGCATGCAAAAGCTGCTCTTCTGAACCAGCACTACCAGGTTAACTTTAAAGGGAAACTG
ATCATGAGATTTGATGACACAAATCCTGAAAAAGAAAAGGAAGATTTTGAGAAGGTTATC
TTGGAAGATGTTGCAATGTTGCATATCAAACCAGATCAATTTACTTATACTTCGGATCAT
TTTGAAACTATAATGAAGTATGCAGAGAAGCTAATTCAAGAAGGGAAGGCTTATGTGGAT
GATACTCCTGCTGAACAGATGAAAGCAGAACGTGAGCAGAGGATAGAATCTAAACATAGA
AAAAACCCTATTGAGAAGAATCTACAAATGTGGGAAGAAATGAAAAAAGGGAGCCAGTTT
GGTCACTCCTGTTGTTTGCGAGCAAAAATTGACATGAGTAGTAACAATGGATGCATGAGA
GATCCAACCCTTTATCGCTGCAAAATTCAACCACATCCAAGAACTGGAAATAAATACAAT
GTTTATCCAACATATGATTTTGCCTGCCCCATAGTTGACAGCATCGAAGGTGTTACACAT
GCCCTGAGAACAACAGAATACCATGACAGAGATGAGCAGTTTTACTGGATTATTGAAGCT
TTAGGCATAAGAAAACCATATATTTGGGAATATAGTCGGCTAAATCTCAACAACACAGTG
CTATCCAAAAGAAAACTCACATGGTTTGTCAATGAAGGACTAGTAGATGGATGGGATGAC
CCAAGATTTCCTACGGTTCGTGGTGTACTGAGAAGAGGGATGACAGTTGAAGGACTGAAA
CAGTTTATTGCTGCTCAGGGCTCCTCACGTTCAGTCGTGAACATGGAGTGGGACAAAATC
TGGGCGTTTAACAAAAAGGTTATTGACCCAGTGGCTCCACGATATGTTGCATTACTGAAG
AAAGAAGTGATCCCAGTGAATGTACCTGAAGCTCAGGAGGAGATGAAAGAAGTAGCCAAA
CACCCAAAGAATCCTGAGGTTGGCTTGAAGCCTGTGTGGTATAGTCCCAAAGTTTTCATT
GAAGGTGCTGATGCAGAGACTTTTTCGGAGGGTGAGATGGTTACATTTATAAATTGGGGC
AACCTCAACATTACAAAAATACACAAAAATGCAGATGGAAAAATCATATCTCTTGATGCA
AAGTTTAATTTGGAAAACAAAGACTACAAGAAAACCACTAAGGTCACTTGGCTTGCAGAG
ACTACACATGCTCTTCCTATTCCAGTAATCTGTGTCACTTATGAGCACTTGATCACAAAG
CCAGTGCTAGGAAAAGACGAGGACTTTAAGCAGTATGTCAACAAGAACAGTAAGCATGAA
GAGCTAATGCTAGGGGATCCCTGCCTTAAGGATTTGAAAAAAGGAGATATTATACAACTC
CAGAGAAGAGGATTCTTCATATGTGATCAACCTTATGAACCTGTTAGCCCATATAGTTGC
AAGGAAGCCCCGTGTGTTTTGATATACATTCCTGATGGGCACACAAAGGAAATGCCAACA
TCAGGGTCAAAGGAAAAGACCAAAGTAGAAGCCACAAAAAATGAGACCTCTGCTCCTTTT
AAGGAAAGACCAACACCTTCTCTGAATAATAATTGTACTACATCTGAGGATTCCTTGGTC
CTTTACAATAGAGTGGCTGTTCAAGGAGATGTGGTTCGTGAATTAAAAGCCAAGAAAGCA
CCAAAGGAAGATGTAGATGCAGCTGTAAAACAGCTTTTGTCTTTGAAAGCTGAATATAAG
GAGAAAACTGGCCAGGAATATAAACCTGGAAACCCTCCTGCTGAAATAGGACAGAATATT
TCTTCTAATTCCTCAGCAAGTATTCTGGAAAGTAAATCTCTGTATGATGAAGTTGCTGCA
CAAGGGGAGGTGGTTCGTAAGCTAAAAGCTGAAAAATCCCCTAAGGCTAAAATAAATGAA
GCTGTAGAATGCTTACTGTCCCTGAAGGCTCAGTATAAAGAAAAAACTGGGAAGGAGTAC
ATACCTGGTCAGCCCCCATTATCTCAAAGTTCGGATTCAAGCCCAACCAGAAATTCTGAA
CCTGCTGGTTTAGAAACACCAGAAGCGAAAGTACTTTTTGACAAAGTAGCTTCTCAAGGG
GAAGTAGTTCGGAAACTTAAAACTGAAAAAGCCCCTAAGGATCAAGTAGATATAGCTGTT
CAAGAACTCCTTCAGCTAAAGGCACAGTACAAGTCTTTGATAGGAGTAGAGTATAAGCCT
GTGTCGGCCACTGGAGCTGAGGACAAAGATAAGAAGAAGAAAGAAAAAGAAAATAAATCT
GAAAAGCAGAATAAGCCTCAGAAACAAAATGATGGCCAAAGGAAAGACCCTTCTAAAAAC
CAAGGAGGTGGGCTCTCATCAAGTGGAGCAGGAGAAGGGCAGGGGCCTAAGAAACAGACC
AGGTTGGGTCTTGAGGCAAAAAAAGAAGAAAATCTTGCTGATTGGTATTCTCAGGTCATC
ACAAAGTCAGAAATGATTGAATACCATGACATAAGTGGCTGTTATATTCTTCGTCCCTGG
GCCTATGCCATTTGGGAAGCCATCAAGGACTTTTTTGATGCTGAGATCAAGAAACTTGGT
GTTGAAAACTGCTACTTCCCCATGTTTGTGTCTCAAAGTGCATTAGAGAAAGAGAAGACT
CATGTTGCTGACTTTGCCCCAGAGGTTGCTTGGGTTACAAGATCTGGCAAAACCGAGCTG
GCAGAACCAATTGCCATTCGTCCTACTAGTGAAACAGTAATGTATCCTGCATATGCAAAA
TGGGTACAATCACACAGAGACCTGCCCATCAAGCTCAATCAGTGGTGCAATGTGGTGCGT
TGGGAATTCAAGCATCCTCAGCCTTTCCTACGTACTCGTGAATTTCTTTGGCAGGAAGGG
CACAGTGCTTTTGCTACCATGGAAGAGGCAGCGGAAGAGGTCTTGCAGATACTTGACTTA
TATGCTCAGGTATATGAAGAACTCCTGGCAATTCCTGTTGTTAAAGGAAGAAAGACGGAA
AAGGAAAAATTTGCAGGAGGAGACTATACAACTACAATAGAAGCATTTATATCTGCTAGT
GGAAGAGCTATCCAGGGAGGAACATCACATCATTTAGGGCAGAATTTTTCCAAAATGTTT
GAAATCGTTTTTGAAGATCCAAAGATACCAGGAGAGAAGCAATTTGCCTATCAAAACTCC
TGGGGCCTGACAACTCGAACTATTGGTGTTATGACCATGGTTCATGGGGACAACATGGGT
TTAGTATTACCACCCCGTGTAGCATGTGTTCAGGTGGTGATTATTCCTTGTGGCATTACC
AATGCACTTTCTGAAGAAGACAAAGAAGCGCTGATTGCAAAATGCAATGATTATCGAAGG
CGATTACTCAGTGTTAACATCCGCGTTAGAGCTGATTTACGAGATAATTATTCTCCAGGT
TGGAAATTCAATCACTGGGAGCTCAAGGGAGTTCCCATTAGACTTGAAGTTGGGCCACGT
GATATGAAGAGCTGTCAGTTTGTAGCCGTCAGACGAGATACTGGAGAAAAGCTGACAGTT
GCTGAAAATGAGGCAGAGACTAAACTTCAAGCTATTTTGGAAGACATCCAGGTCACCCTT
TTCACAAGGGCTTCTGAAGACCTTAAGACTCATATGGTTGTGGCTAATACAATGGAAGAC
TTTCAGAAGATACTAGATTCTGGAAAGATTGTTCAGATTCCATTCTGTGGGGAAATTGAC
TGTGAGGACTGGATCAAAAAGACCACTGCCAGGGATCAAGATCTTGAACCTGGTGCTCCA
TCCATGGGAGCTAAAAGCCTTTGCATCCCCTTCAAACCACTCTGTGAACTGCAGCCTGGA
GCCAAATGTGTCTGTGGCAAGAACCCTGCCAAGTACTACACCTTATTTGGTCGCAGCTAC
TGA

1. Fett R, Knippers R: The primary structure of human glutaminyl-tRNA synthetase. A highly conserved core, amino acid repeat regions, and homologies with translation elongation factors. J Biol Chem. 1991 Jan 25;266(3):1448-55. [PubMed ]
2. Thommes P, Fett R, Schray B, Kunze N, Knippers R: The core region of human glutaminyl-tRNA synthetase homologies with the Escherichia coli and yeast enzymes. Nucleic Acids Res. 1988 Jun 24;16(12):5391-406. [PubMed ]
3. Cerini C, Kerjan P, Astier M, Gratecos D, Mirande M, Semeriva M: A component of the multisynthetase complex is a multifunctional aminoacyl-tRNA synthetase. EMBO J. 1991 Dec;10(13):4267-77. [PubMed ]
4. Kaiser E, Eberhard D, Knippers R: Exons encoding the highly conserved part of human glutaminyl-tRNA synthetase. J Mol Evol. 1992 Jan;34(1):45-53. [PubMed ]
5. Jeong EJ, Hwang GS, Kim KH, Kim MJ, Kim S, Kim KS: Structural analysis of multifunctional peptide motifs in human bifunctional tRNA synthetase: identification of RNA-binding residues and functional implications for tandem repeats. Biochemistry. 2000 Dec 26;39(51):15775-82. [PubMed ]

1. Long-chain acyl-CoA synthetase 4
2. LACS 4

MKLKLNVLTIILLPVHLLITIYSALIFIPWYFLTNAKKKNAMAKRIKAKPTSDKPGSPYR
SVTHFDSLAVIDIPGADTLDKLFDHAVSKFGKKDSLGTREILSEENEMQPNGKVFKKLIL
GNYKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTL
YATLGKEAVVHGLNESEASYLITSVELLESKLKTALLDISCVKHIIYVDNKAINKAEYPE
GFEIHSMQSVEELGSNPENLGIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMT
GQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIKKGSK
GDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYDAPLC
NLLLFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEV
TDYTTGRVGAPLICCEIKLKDWQEGGYTINDKPNPRGEIVIGGQNISMGYFKNEEKTAED
YSVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLIDN
ICAFAKSDQSYVISFVVPNQKRLTLLAQQKGVEGTWVDICNNPAMEAEILKEIREAANAM
KLERFEIPIKVRLSPEPWTPETGLVTDAFKLKRKELRNHYLKDIERMYGGK

• Fatty Acid Metabolism (map00071 )

• ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA

• AMP-binding (PF00501 )

• 1-23

ATGGCAAAGAGAATAAAAGCTAAGCCCACTTCAGACAAACCTGGAAGTCCATATCGCTCT
GTCACACACTTCGACTCACTAGCTGTAATAGACATCCCTGGAGCAGATACTCTGGATAAA
TTATTTGACCATGCTGTATCCAAGTTTGGGAAGAAGGACAGCCTTGGGACCAGGGAAATC
CTAAGTGAAGAAAATGAAATGCAGCCAAATGGAAAAGTTTTTAAGAAGTTAATTCTTGGG
AATTATAAATGGATGAACTATCTTGAAGTGAATCGCAGAGTGAATAACTTTGGTAGTGGA
CTCACTGCACTGGGACTAAAACCAAAGAACACCATTGCCATCTTCTGTGAGACCAGGGCC
GAATGGATGATTGCAGCACAGACCTGCTTTAAGTACAACTTTCCTCTTGTGACTTTATAT
GCCACACTTGGCAAAGAAGCAGTAGTTCATGGGCTAAATGAATCTGAGGCTTCCTATCTG
ATTACCAGTGTTGAACTTCTGGAAAGTAAACTTAAGACTGCATTGTTAGATATCAGTTGT
GTTAAACATATCATTTATGTGGACAATAAGGCTATCAATAAAGCAGAGTACCCTGAAGGA
TTTGAGATTCACAGCATGCAATCAGTAGAAGAGTTGGGATCTAACCCAGAAAACTTGGGC
ATTCCTCCAAGTAGACCAACGCCTTCAGACATGGCCATTGTTATGTATACTAGTGGTTCT
ACTGGCCGACCTAAGGGAGTGATGATGCATCATAGCAATTTGATAGCTGGAATGACAGGC
CAGTGTGAAAGAATACCTGGACTGGGACCGAAGGACACATATATTGGCTACTTGCCTTTG
GCTCATGTGCTAGAACTGACAGCAGAGATATCTTGCTTTACCTATGGCTGCAGGATTGGA
TATTCTTCTCCGCTTACACTCTCTGACCAGTCCAGCAAAATTAAAAAAGGAAGCAAAGGA
GACTGTACTGTACTGAAGCCCACACTTATGGCTGCTGTTCCGGAAATCATGGATAGAATT
TATAAGAATGTTATGAGCAAAGTCCAAGAGATGAATTATATTCAGAAAACTCTGTTCAAG
ATAGGGTATGATTACAAATTGGAACAGATCAAAAAGGGATATGATGCACCTCTTTGCAAT
CTGTTACTGTTTAAAAAGGTCAAGGCCCTGCTGGGAGGGAATGTCCGCATGATGCTGTCT
GGAGGGGCCCCGCTATCTCCTCAGACACACCGATTCATGAATGTCTGCTTCTGCTGCCCA
ATTGGCCAGGGTTATGGACTGACAGAATCATGTGGTGCTGGGACAGTTACTGAAGTAACT
GACTATACTACTGGCAGAGTTGGAGCACCTCTTATTTGCTGTGAAATTAAGCTAAAAGAC
TGGCAAGAAGGCGGTTATACAATTAATGACAAGCCAAACCCCAGAGGTGAAATCGTAATT
GGTGGACAGAACATCTCCATGGGATATTTTAAAAATGAAGAGAAAACAGCAGAAGATTAT
TCTGTGGATGAAAATGGACAAAGGTGGTTTTGCACTGGTGATATTGGAGAATTCCATCCC
GATGGATGTTTACAGATTATAGATCGTAAGAAAGATCTAGTGAAGTTACAAGCAGGAGAG
TATGTATCTCTTGGGAAAGTAGAAGCTGCACTGAAGAATTGTCCACTTATTGACAACATC
TGTGCTTTTGCCAAAAGTGATCAGTCCTATGTGATCAGTTTTGTGGTTCCTAACCAGAAA
AGGTTGACACTTTTGGCACAACAGAAAGGGGTAGAAGGAACTTGGGTTGATATCTGCAAT
AATCCTGCTATGGAAGCTGAAATACTGAAAGAAATTCGAGAAGCTGCAAATGCCATGAAA
TTGGAGCGATTTGAAATTCCAATCAAGGTTCGATTAAGCCCAGAGCCATGGACCCCTGAA
ACTGGTTTGGTAACTGATGCTTTCAAACTGAAAAGGAAGGAGCTGAGGAACCATTACCTC
AAAGACATTGAACGAATGTATGGGGGCAAATAA

1. Cao Y, Traer E, Zimmerman GA, McIntyre TM, Prescott SM: Cloning, expression, and chromosomal localization of human long-chain fatty acid-CoA ligase 4 (FACL4). Genomics. 1998 Apr 15;49(2):327-30. [PubMed ]
2. Piccini M, Vitelli F, Bruttini M, Pober BR, Jonsson JJ, Villanova M, Zollo M, Borsani G, Ballabio A, Renieri A: FACL4, a new gene encoding long-chain acyl-CoA synthetase 4, is deleted in a family with Alport syndrome, elliptocytosis, and mental retardation. Genomics. 1998 Feb 1;47(3):350-8. [PubMed ]
3. Meloni I, Muscettola M, Raynaud M, Longo I, Bruttini M, Moizard MP, Gomot M, Chelly J, des Portes V, Fryns JP, Ropers HH, Magi B, Bellan C, Volpi N, Yntema HG, Lewis SE, Schaffer JE, Renieri A: FACL4, encoding fatty acid-CoA ligase 4, is mutated in nonspecific X-linked mental retardation. Nat Genet. 2002 Apr;30(4):436-40. Epub 2002 Mar 11. [PubMed ]

1. Tryptophan-- tRNA ligase
2. TrpRS
3. IFP53
4. hWRS

MPNSEPASLLELFNSIATQGELVRSLKAGNASKDEIDSAVKMLVSLKMSYKAAAGEDYKA
DCPPGNPAPTSNHGPDATEAEEDFVDPWTVQTSSAKGIDYDKLIVRFGSSKIDKELINRI
ERATGQRPHHFLRRGIFFSHRDMNQVLDAYENKKPFYLYTGRGPSSEAMHVGHLIPFIFT
KWLQDVFNVPLVIQMTDDEKYLWKDLTLDQAYSYAVENAKDIIACGFDINKTFIFSDLDY
MGMSSGFYKNVVKIQKHVTFNQVKGIFGFTDSDCIGKISFPAIQAAPSFSNSFPQIFRDR
TDIQCLIPCAIDQDPYFRMTRDVAPRIGYPKPALLHSTFFPALQGAQTKMSASDPNSSIF
LTDTAKQIKTKVNKHAFSGGRDTIEEHRQFGGNCDVDVSFMYLTFFLEDDDKLEQIRKDY
TSGAMLTGELKKALIEVLQPLIAEHQARRKEVTDEIVKEFMTPRKLSFDFQ

• Aminoacyl-tRNA biosynthesis (map00970 )
• Tryptophan Metabolism (map00380 )

• ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp)

• tRNA-synt_1b (PF00579 )
• WHEP-TRS (PF00458 )

• None

• None

ATGCCCAACAGTGAGCCCGCATCTCTGCTGGAGCTGTTCAACAGCATCGCCACACAAGGG
GAGCTCGTAAGGTCCCTCAAAGCGGGAAATGCGTCAAAGGATGAAATTGATTCTGCAGTA
AAGATGTTGGTGTCATTAAAAATGAGCTACAAAGCTGCCGCGGGGGAGGATTACAAGGCT
GACTGTCCTCCAGGGAACCCAGCACCTACCAGTAATCATGGCCCAGATGCCACAGAAGCT
GAAGAGGATTTTGTGGACCCATGGACAGTACAGACAAGCAGTGCAAAAGGCATAGACTAC
GATAAGCTCATTGTTCGGTTTGGAAGTAGTAAAATTGACAAAGAGCTAATAAACCGAATA
GAGAGAGCCACCGGCCAAAGACCACACCACTTCCTGCGCAGAGGCATCTTCTTCTCACAC
AGAGATATGAATCAGGTTCTTGATGCCTATGAAAATAAGAAGCCATTTTATCTGTACACG
GGCCGGGGCCCCTCTTCTGAAGCAATGCATGTAGGTCACCTCATTCCATTTATTTTCACA
AAGTGGCTCCAGGATGTATTTAACGTGCCCTTGGTGATCCAGATGACGGATGACGAGAAG
TATCTGTGGAAGGACCTGACCCTGGACCAGGCCTATAGCTATGCTGTGGAGAATGCCAAG
GACATCATCGCCTGTGGCTTTGACATCAACAAGACTTTCATATTCTCTGACCTGGACTAC
ATGGGGATGAGCTCAGGTTTCTACAAAAATGTGGTGAAGATTCAAAAGCATGTTACCTTC
AACCAAGTGAAAGGCATTTTCGGCTTCACTGACAGCGACTGCATTGGGAAGATCAGTTTT
CCTGCCATCCAGGCTGCTCCCTCCTTCAGCAACTCATTCCCACAGATCTTCCGAGACAGG
ACGGATATCCAGTGCCTTATCCCATGTGCCATTGACCAGGATCCTTACTTTAGAATGACA
AGGGACGTCGCCCCCAGGATCGGCTATCCTAAACCAGCCCTGTTGCACTCCACCTTCTTC
CCAGCCCTGCAGGGCGCCCAGACCAAAATGAGTGCCAGCGACCCCAACTCCTCCATCTTC
CTCACCGACACGGCCAAGCAGATCAAAACCAAGGTCAATAAGCATGCGTTTTCTGGAGGG
AGAGACACCATCGAGGAGCACAGGCAGTTTGGGGGCAACTGTGATGTGGACGTGTCTTTC
ATGTACCTGACCTTCTTCCTCGAGGACGACGACAAGCTCGAGCAGATCAGGAAGGATTAC
ACCAGCGGAGCCATGCTCACCGGTGAGCTCAAGAAGGCACTCATAGAGGTTCTGCAGCCC
TTGATCGCAGAGCACCAGGCCCGGCGCAAGGAGGTCACGGATGAGATAGTGAAAGAGTTC
ATGACTCCCCGGAAGCTGTCCTTCGACTTTCAGTAG

1. Rubin BY, Anderson SL, Xing L, Powell RJ, Tate WP: Interferon induces tryptophanyl-tRNA synthetase expression in human fibroblasts. J Biol Chem. 1991 Dec 25;266(36):24245-8. [PubMed ]
2. Fleckner J, Rasmussen HH, Justesen J: Human interferon gamma potently induces the synthesis of a 55-kDa protein (gamma 2) highly homologous to rabbit peptide chain release factor and bovine tryptophanyl-tRNA synthetase. Proc Natl Acad Sci U S A. 1991 Dec 15;88(24):11520-4. [PubMed ]
3. Frolova LYu, Sudomoina MA, Grigorieva AYu, Zinovieva OL, Kisselev LL: Cloning and nucleotide sequence of the structural gene encoding for human tryptophanyl-tRNA synthetase. Gene. 1991 Dec 30;109(2):291-6. [PubMed ]
4. Buwitt U, Flohr T, Bottger EC: Molecular cloning and characterization of an interferon induced human cDNA with sequence homology to a mammalian peptide chain release factor. EMBO J. 1992 Feb;11(2):489-96. [PubMed ]
5. Sokolova IV, Narovlianskii AN, Amchenkova AM, Turpaev KT: [Alternative splicing of 5'-terminal exons of the human tryptophanyl-tRNA synthetase gene] Mol Biol (Mosk). 1996 Mar-Apr;30(2):319-29. [PubMed ]
6. Frolova LY, Grigorieva AY, Sudomoina MA, Kisselev LL: The human gene encoding tryptophanyl-tRNA synthetase: interferon-response elements and exon-intron organization. Gene. 1993 Jun 30;128(2):237-45. [PubMed ]
7. Rasmussen HH, van Damme J, Puype M, Gesser B, Celis JE, Vandekerckhove J: Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. Electrophoresis. 1992 Dec;13(12):960-9. [PubMed ]
8. Bange FC, Flohr T, Buwitt U, Bottger EC: An interferon-induced protein with release factor activity is a tryptophanyl-tRNA synthetase. FEBS Lett. 1992 Mar 30;300(2):162-6. [PubMed ]

1. Long-chain acyl-CoA synthetase 1
2. LACS 1
3. Palmitoyl-CoA ligase 1
4. Long-chain fatty acid CoA ligase 2
5. Long-chain acyl-CoA synthetase 2
6. LACS 2
7. Acyl-CoA synthetase 1
8. ACS1
9. Palmitoyl-CoA ligase 2

MQAHELFRYFRMPELVDFRQYVRTLPTNTLMGFGAFAALTTFWYATRPKPLKPPCDLSMQ
SVEVAGSGGARRSALLDSDEPLVYFYDDVTTLYEGFQRGIQVSNNGPCLGSRKPDQPYEW
LSYKQVAELSECIGSALIQKGFKTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDT
LGNEAITYIVNKAELSLVFVDKPEKAKLLLEGVENKLIPGLKIIVVMDAYGSELVERGQR
CGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAF
VKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQP
TVFPVVPRLLNRMFDRIFGQANTTLKRWLLDFASKRKEAELRSGIIRNNSLWDRLIFHKV
QSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHV
GAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGD
IGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAI
VVPDVETLCSWAQKRGFEGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKGITLHP
ELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYSTIKV

• Fatty Acid Metabolism (map00071 )

• ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA

• AMP-binding (PF00501 )

• None

• 25-45

ATGCAAGCCCATGAGCTGTTCCGGTATTTTCGAATGCCAGAGCTGGTTGACTTCCGACAG
TACGTGCGTACTCTTCCGACCAACACGCTTATGGGCTTCGGAGCTTTTGCAGCACTCACC
ACCTTCTGGTACGCCACGAGACCCAAACCCCTGAAGCCGCCATGCGACCTCTCCATGCAG
TCAGTGGAAGTGGCGGGTAGTGGTGGTGCACGAAGATCCGCACTACTTGACAGCGACGAG
CCCTTGGTGTATTTCTATGATGATGTCACAACATTATACGAAGGTTTCCAGAGGGGAATA
CAGGTGTCAAATAATGGCCCTTGTTTAGGCTCTCGGAAACCAGACCAACCCTATGAATGG
CTTTCATATAAACAGGTTGCAGAATTGTCGGAGTGCATAGGCTCAGCACTGATCCAGAAG
GGCTTCAAGACTGCCCCAGATCAGTTCATTGGCATCTTTGCTCAAAATAGACCTGAGTGG
GTGATTATTGAACAAGGATGCTTTGCTTATTCGATGGTGATCGTTCCACTTTATGATACC
CTTGGAAATGAAGCCATCACGTACATAGTCAACAAAGCTGAACTCTCTCTGGTTTTTGTT
GACAAGCCAGAGAAGGCCAAACTCTTATTAGAGGGTGTAGAAAATAAGTTAATACCAGGC
CTTAAAATCATAGTTGTCATGGATGCCTACGGCAGTGAACTGGTGGAACGAGGCCAGAGG
TGTGGGGTGGAAGTCACCAGCATGAAGGCGATGGAGGACCTGGGAAGAGCCAACAGACGG
AAGCCCAAGCCTCCAGCACCTGAAGATCTTGCAGTAATTTGTTTCACAAGTGGAACTACA
GGCAACCCCAAAGGAGCAATGGTCACTCACCGAAACATAGTGAGCGATTGTTCAGCTTTT
GTGAAAGCAACAGAGAATACAGTCAATCCTTGCCCAGATGATACTTTGATATCTTTCTTG
CCTCTCGCCCATATGTTTGAGAGAGTTGTAGAGTGTGTAATGCTGTGTCATGGAGCTAAA
ATCGGATTTTTCCAAGGAGATATCAGGCTGCTCATGGATGACCTCAAGGTGCTTCAACCC
ACTGTCTTCCCCGTGGTTCCAAGACTGCTGAACCGGATGTTTGACCGAATTTTCGGACAA
GCAAACACCACGCTGAAGCGATGGCTCTTGGACTTTGCCTCCAAGAGGAAAGAAGCAGAG
CTTCGCAGCGGCATCATCAGAAACAACAGCCTGTGGGACCGGCTGATCTTCCACAAAGTA
CAGTCGAGCCTGGGCGGAAGAGTCCGGCTGATGGTGACAGGAGCCGCCCCGGTGTCTGCC
ACTGTGCTGACGTTCCTCAGAGCAGCCCTGGGCTGTCAGTTTTATGAAGGATACGGACAG
ACAGAGTGCACTGCCGGGTGCTGCCTAACCATGCCTGGAGACTGGACCGCAGGCCATGTT
GGGGCCCCGATGCCGTGCAATTTGATAAAACTTGTTGATGTGGAAGAAATGAATTACATG
GCTGCCGAGGGCGAGGGCGAGGTGTGTGTGAAAGGGCCAAATGTATTTCAGGGCTACTTG
AAGGACCCAGCGAAAACAGCAGAAGCTTTGGACAAAGACGGCTGGTTACACACAGGGGAC
ATTGGAAAATGGTTACCAAATGGCACCTTGAAAATTATCGACCGGAAAAAGCACATATTT
AAGCTGGCACAAGGAGAATACATAGCCCCTGAAAAGATTGAAAATATCTACATGCGAAGT
GAGCCTGTTGCTCAGGTGTTTGTCCACGGAGAAAGCCTGCAGGCATTTCTCATTGCAATT
GTGGTACCAGATGTTGAGACATTATGTTCCTGGGCCCAAAAGAGAGGATTTGAAGGGTCG
TTTGAGGAACTGTGCAGAAATAAGGATGTCAAAAAAGCTATCCTCGAAGATATGGTGAGA
CTTGGGAAGGATTCTGGTCTGAAACCATTTGAACAGGTCAAAGGCATCACATTGCACCCT
GAATTATTTTCTATCGACAATGGCCTTCTGACTCCAACAATGAAGGCGAAAAGGCCAGAG
CTGCGGAACTATTTCAGGTCGCAGATAGATGACCTCTATTCCACTATCAAGGTTTAG

1. Abe T, Fujino T, Fukuyama R, Minoshima S, Shimizu N, Toh H, Suzuki H, Yamamoto T: Human long-chain acyl-CoA synthetase: structure and chromosomal location. J Biochem (Tokyo). 1992 Jan;111(1):123-8. [PubMed ]
2. Ghosh B, Barbosa E, Singh I: Molecular cloning and sequencing of human palmitoyl-CoA ligase and its tissue specific expression. Mol Cell Biochem. 1995 Oct 4;151(1):77-81. [PubMed ]
3. Malhotra KT, Malhotra K, Lubin BH, Kuypers FA: Identification and molecular characterization of acyl-CoA synthetase in human erythrocytes and erythroid precursors. Biochem J. 1999 Nov 15;344 Pt 1:135-43. [PubMed ]

1. Glutamine--tRNA ligase
2. GlnRS

MAALDSLSLFTSLGLSEQKARETLKNSALSAQLREAATQAQQTLGSTIDKATGILLYGLA
SRLRDTRRLSFLVSYIASKKIHTEPQLSAALEYVRSHPLDPIDTVDFERECGVGVIVTPE
QIEEAVEAAINRHRPQLLVERYHFNMGLLMGEARAVLKWADGKMIKNEVDMQVLHLLGPK
LEADLEKKFKVAKARLEETDRRTAKDVVENGETADQTLSLMEQLRGEALKFHKPGENYKT
PGYVVTPHTMNLLKQHLEITGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFL
RFDDTNPEKEEAKFFTAICDMVAWLGYTPYKVTYASDYFDQLYAWAVELIRRGLAYVCHQ
RGEELKGHNTLPSPWRDRPMEESLLLFEAMRKGKFSEGEATLRMKLVMEDGKMDPVAYRV
KYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYCPV
QWEYGRLNLHYAVVSKRKILQLVATGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVG
VTVAQTTMEPHLLEACVRDVLNDTAPRAMAVLESLRVIITNFPAAKSLDIQVPNFPADET
KGFHQVPFAPIVFIERTDFKEEPEPGFKRLAWGQPVGLRHTGYVIELQHVVKGPSGCVES
LEVTCRRADAGEKPKAFIHWVSQPLMCEVRLYERLFQHKNPEDPTEVPGGFLSDLNLASL
HVVDAALVDCSVALAKPFDKFQFERLGYFSVDPDSHQGKLVFNRTVTLKEDPGKV

• Aminoacyl-tRNA biosynthesis (map00970 )
• Glutamate Metabolism (map00251 )

• ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln)

• tRNA-synt_1c (PF00749 )
• tRNA-synt_1c_C (PF03950 )
• tRNA_synt_1c_R1 (PF04558 )
• tRNA_synt_1c_R2 (PF04557 )

• None

• None

ATGGCGGCTCTAGACTCCCTGTCGCTCTTCACTAGCCTCGGCCTGAGCGAGCAGAAGGCC
CGCGAGACGCTCAAGAACTCGGCTCTGAGCGCGCAGCTGCGCGAGGCCGCTACTCAGGCT
CAGCAGACCCTGGGTTCCACCATTGACAAAGCTACCGGGATCCTGTTATATGGCTTGGCC
TCCCGACTCAGGGATACCCGGCGTCTCTCCTTCCTTGTAAGCTACATAGCCAGTAAGAAG
ATCCACACTGAGCCCCAGCTAAGCGCTGCCCTTGAGTATGTGCGGAGTCACCCCTTGGAC
CCCATCGACACTGTGGACTTCGAGCGGGAATGTGGCGTGGGTGTCATTGTGACCCCAGAG
CAGATTGAGGAGGCTGTGGAGGCTGCTATTAACAGGCACCGGCCCCAGCTCCTGGTGGAA
CGTTACCATTTCAACATGGGGCTGCTGATGGGAGAGGCTCGGGCTGTGCTGAAGTGGGCA
GATGGCAAAATGATCAAGAATGAAGTGGACATGCAGGTCCTCCACCTTCTGGGCCCCAAG
TTGGAGGCTGATCTGGAGAAGAAGTTCAAGGTGGCAAAAGCTCGGCTAGAAGAAACAGAC
CGGAGGACGGCAAAGGATGTGGTGGAGAATGGCGAGACTGCTGACCAGACCCTGTCTCTG
ATGGAGCAGCTCCGGGGGGAGGCCCTTAAGTTCCACAAGCCTGGTGAGAACTACAAGACC
CCAGGCTATGTGGTCACTCCACACACCATGAATCTACTAAAGCAGCACCTGGAGATTACT
GGTGGGCAGGTACGTACCCGGTTCCCGCCAGAACCCAATGGAATCCTGCATATTGGACAT
GCCAAAGCCATCAATTTCAACTTTGGCTATGCCAAGGCCAACAATGGCATCTGTTTTCTG
CGTTTTGATGACACCAACCCTGAGAAGGAGGAAGCAAAGTTCTTCACGGCCATCTGTGAC
ATGGTAGCCTGGCTAGGCTACACACCTTACAAAGTCACATATGCGTCTGACTATTTTGAC
CAGCTATATGCGTGGGCTGTGGAGCTCATCCGCAGGGGTCTGGCTTATGTGTGCCACCAG
CGAGGAGAGGAGCTCAAAGGCCATAATACTCTGCCTTCACCCTGGAGAGACCGTCCCATG
GAGGAGTCACTGCTGCTCTTTGAGGCAATGCGCAAGGGCAAGTTTTCAGAGGGCGAGGCC
ACACTACGGATGAAGCTGGTGATGGAGGATGGCAAGATGGACCCTGTAGCCTATCGAGTC
AAGTATACACCACACCACCGCACAGGGGACAAATGGTGCATCTATCCCACCTACGACTAC
ACACACTGCCTCTGTGACTCCATCGAGCACATCACTCACTCACTCTGCACCAAGGAATTC
CAGGCCCGACGCTCTTCCTACTTCTGGCTTTGCAATGCACTGGACGTCTATTGCCCTGTG
CAGTGGGAGTATGGCCGCCTCAACCTGCACTATGCTGTTGTCTCTAAGAGGAAGATCCTC
CAGCTTGTAGCAACTGGTGCTGTGCGGGACTGGGATGACCCACGGCTCTTTACACTCACG
GCCCTGCGACGGCGGGGCTTCCCACCTGAGGCCATCAACAACTTCTGTGCCCGGGTGGGA
GTGACTGTGGCACAAACCACAATGGAGCCACATCTTCTAGAAGCCTGTGTGCGTGATGTG
CTGAATGACACAGCCCCACGAGCCATGGCTGTGCTGGAGTCACTACGGGTCATCATCACC
AACTTTCCTGCTGCCAAGTCCTTGGACATCCAGGTGCCCAACTTCCCAGCTGATGAGACC
AAAGGCTTCCATCAGGTTCCCTTTGCACCCATTGTCTTCATTGAGAGGACTGACTTCAAG
GAGGAGCCAGAGCCAGGATTTAAGCGCCTGGCTTGGGGCCAGCCTGTGGGCCTGAGGCAT
ACAGGCTACGTCATTGAGCTGCAGCATGTTGTCAAGGGCCCCAGTGGTTGTGTAGAGAGT
CTGGAGGTGACCTGCAGACGGGCAGATGCTGGAGAGAAGCCAAAGGCCTTTATTCACTGG
GTGTCACAGCCTTTGATGTGTGAGGTTCGCCTCTATGAGCGACTATTCCAGCACAAGAAC
CCTGAAGATCCTACTGAGGTGCCTGGTGGATTTTTAAGTGACCTGAACCTGGCATCACTA
CACGTGGTGGATGCAGCATTAGTGGACTGCTCTGTGGCCCTGGCAAAACCCTTCGACAAG
TTCCAGTTTGAGCGTCTTGGATATTTCTCCGTGGATCCAGACAGCCATCAGGGAAAGCTT
GTCTTTAACCGAACTGTCACACTGAAGGAAGACCCAGGAAAGGTGTGA

1. Lamour V, Quevillon S, Diriong S, N'Guyen VC, Lipinski M, Mirande M: Evolution of the Glx-tRNA synthetase family: the glutaminyl enzyme as a case of horizontal gene transfer. Proc Natl Acad Sci U S A. 1994 Aug 30;91(18):8670-4. [PubMed ]

1. Glutamine- dependent asparagine synthetase
2. Cell cycle control protein TS11

MCGIWALFGSDDCLSVQCLSAMKIAHRGPDAFRFENVNGYTNCCFGFHRLAVVDPLFGMQ
PIRVKKYPYLWLCYNGEIYNHKKMQQHFEFEYQTKVDGEIILHLYDKGGIEQTICMLDGV
FAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEAKGLVTLKHSATPFLKVEPF
LPGHYEVLDLKPNGKVASVEMVKYHHCRDVPLHALYDNVEKLFPGFEIETVKNNLRILFN
NAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEAQVQYPLQTFAIGMEDSPDLLAAR
KVADHIGSEHYEVLFNSEEGIQALDEVIFSLETYDITTVRASVGMYLISKYIRKNTDSVV
IFSGEGSDELTQGYIYFHKAPSPEKAEEESERLLRELYLFDVLRADRTTAAHGLELRVPF
LDHRFSSYYLSLPPEMRIPKNGIEKHLLRETFEDSNLIPKEILWRPKEAFSDGITSVKNS
WFKILQEYVEHQVDDAMMANAAQKFPFNTPKTKEGYYYRQVFERHYPGRADWLSHYWMPK
WINATDPSARTLTHYKSAVKA

• Nitrogen Metabolism (map00910 )

• ATP + L-aspartate + L-glutamine = AMP + diphosphate + L-asparagine + L-glutamate

• Asn_synthase (PF00733 )
• GATase_2 (PF00310 )

• None

• None

ATGTGTGGCATTTGGGCGCTGTTTGGCAGTGATGATTGCCTTTCTGTTCAGTGTCTGAGT
GCTATGAAGATTGCACACAGAGGTCCAGATGCATTCCGTTTTGAGAATGTCAATGGATAC
ACCAACTGCTGCTTTGGATTTCACCGGTTGGCGGTAGTTGACCCGCTGTTTGGAATGCAG
CCAATTCGAGTGAAGAAATATCCGTATTTGTGGCTCTGTTACAATGGTGAAATCTACAAC
CATAAGAAGATGCAACAGCATTTTGAATTTGAATACCAGACCAAAGTGGATGGTGAGATA
ATCCTTCATCTTTATGACAAAGGAGGAATTGAGCAAACAATTTGTATGTTGGATGGTGTG
TTTGCATTTGTTTTACTGGATACTGCCAATAAGAAAGTGTTCCTGGGTAGAGATACATAT
GGAGTCAGACCTTTGTTTAAAGCAATGACAGAAGATGGATTTTTGGCTGTATGTTCAGAA
GCTAAAGGTCTTGTTACATTGAAGCACTCCGCGACTCCCTTTTTAAAAGTGGAGCCTTTT
CTTCCTGGACACTATGAAGTTTTGGATTTAAAGCCAAATGGCAAAGTTGCATCCGTGGAA
ATGGTTAAATATCATCACTGTCGGGATGTACCCCTGCACGCCCTCTATGACAATGTGGAG
AAACTCTTTCCAGGTTTTGAGATAGAAACTGTGAAGAACAACCTCAGGATCCTTTTTAAT
AATGCTGTAAAGAAACGTTTGATGACAGACAGAAGGATTGGCTGCCTTTTATCAGGGGGC
TTGGACTCCAGCTTGGTTGCTGCCACTCTGTTGAAGCAGCTGAAAGAAGCCCAAGTACAG
TATCCTCTCCAGACATTTGCAATTGGCATGGAAGACAGCCCCGATTTACTGGCTGCTAGA
AAGGTGGCAGATCATATTGGAAGTGAACATTATGAAGTCCTTTTTAACTCTGAGGAAGGC
ATTCAGGCTCTGGATGAAGTCATATTTTCCTTGGAAACTTATGACATTACAACAGTTCGT
GCTTCAGTAGGTATGTATTTAATTTCCAAGTATATTCGGAAGAACACAGATAGCGTGGTG
ATCTTCTCTGGAGAAGGATCAGATGAACTTACGCAGGGTTACATATATTTTCACAAGGCT
CCTTCTCCTGAAAAAGCCGAGGAGGAGAGTGAGAGGCTTCTGAGGGAACTCTATTTGTTT
GATGTTCTCCGCGCAGATCGAACTACTGCTGCCCATGGTCTTGAACTGAGAGTCCCATTT
CTAGATCATCGATTTTTTTCCTATTACTTGTCTCTGCCACCAGAAATGAGAATTCCAAAG
AATGGGATAGAAAAACATCTCCTGAGAGAGACGTTTGAGGATTCCAATCTGATACCCAAA
GAGATTCTCTGGCGACCAAAAGAAGCCTTCAGTGATGGAATAACTTCAGTTAAGAATTCC
TGGTTTAAGATTTTACAGGAATACGTTGAACATCAGGTTGATGATGCAATGATGGCAAAT
GCAGCCCAGAAATTTCCCTTCAATACTCCTAAAACCAAAGAAGGATATTACTACCGTCAA
GTCTTTGAACGCCATTACCCAGGCCGGGCTGACTGGCTGAGCCATTACTGGATGCCCAAG
TGGATCAATGCCACTGACCCTTCTGCCCGCACGCTGACCCACTACAAGTCAGCTGTCAAA
GCTTAG

1. Andrulis IL, Chen J, Ray PN: Isolation of human cDNAs for asparagine synthetase and expression in Jensen rat sarcoma cells. Mol Cell Biol. 1987 Jul;7(7):2435-43. [PubMed ]
2. Zhang YP, Lambert MA, Cairney AE, Wills D, Ray PN, Andrulis IL: Molecular structure of the human asparagine synthetase gene. Genomics. 1989 Apr;4(3):259-65. [PubMed ]
3. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed ]
4. Greco A, Ittmann M, Basilico C: Molecular cloning of a gene that is necessary for G1 progression in mammalian cells. Proc Natl Acad Sci U S A. 1987 Mar;84(6):1565-9. [PubMed ]
5. Greco A, Gong SS, Ittmann M, Basilico C: Organization and expression of the cell cycle gene, ts11, that encodes asparagine synthetase. Mol Cell Biol. 1989 Jun;9(6):2350-9. [PubMed ]
6. Van Heeke G, Schuster SM: Expression of human asparagine synthetase in Escherichia coli. J Biol Chem. 1989 Apr 5;264(10):5503-9. [PubMed ]
7. Van Heeke G, Schuster SM: The N-terminal cysteine of human asparagine synthetase is essential for glutamine-dependent activity. J Biol Chem. 1989 Nov 25;264(33):19475-7. [PubMed ]

1. Ubiquitin-protein ligase E2
2. Ubiquitin carrier protein E2
3. UbcH8

MSTEAQRVDDSPSTSGGSSDGDQRESVQQEPEREQVQPKKKEGKISSKTAAKLSTSAKRI
QKELAEITLDPPPNCSAGPKGDNIYEWRSTILGPPGSVYEGGVFFLDITFSPDYPFKPPK
VTFRTRIYHCNINSQGVICLDILKDNWSPALTISKVLLSICSLLTDCNPADPLVGSIATQ
YMTNRAEHDRMARQWTKRYAT

• Ubiquitin mediated proteolysis (map04120 )

• ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine

• UQ_con (PF00179 )

• None

• None

ATGTCCACTGAGGCACAAAGAGTTGATGACAGTCCAAGCACTAGTGGAGGAAGTTCCGAT
GGAGATCAACGTGAAAGTGTTCAGCAAGAACCAGAAAGAGAACAAGTTCAGCCCAAGAAA
AAGGAGGGAAAAATATCCAGCAAAACCGCTGCTAAATTGTCAACTAGTGCTAAAAGAATT
CAGAAGGAACTTGCAGAAATCACATTGGACCCTCCTCCCAACTGTAGTGCTGGACCCAAA
GGAGACAACATTTATGAATGGAGGTCAACTATATTGGGACCCCCAGGATCTGTCTATGAA
GGAGGGGTGTTCTTTCTTGACATTACCTTTTCACCAGACTATCCGTTTAAACCCCCTAAG
GTTACCTTCCGAACAAGAATCTATCACTGTAATATTAACAGCCAAGGTGTGATCTGTCTG
GACATCTTAAAGGACAACTGGAGTCCGGCTTTAACTATTTCTAAAGTTCTCCTCTCCATC
TGCTCACTTCTTACAGATTGCAACCCTGCTGACCCTCTGGTGGGCAGCATCGCCACACAG
TACATGACCAACAGAGCAGAGCATGACCGGATGGCCAGACAGTGGACCAAGCGGTACGCC
ACATAG

1. Ubiquitin-protein ligase D2
2. Ubiquitin carrier protein D2
3. Ubiquitin-conjugating enzyme E2-17 kDa 2
4. E2(17KB 2

MALKRIHKELNDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDY
PFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLV
PEIARIYKTDREKYNRIAREWTQKYAM

• Ubiquitin mediated proteolysis (map04120 )

• ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine

• UQ_con (PF00179 )

• None

• None

ATGGCTCTGAAGAGAATCCACAAGGAATTGAATGATCTGGCACGGGACCCTCCAGCACAG
TGTTCAGCAGGTCCTGTTGGAGATGATATGTTCCATTGGCAAGCTACAATAATGGGGCCA
AATGACAGTCCCTATCAGGGTGGAGTATTTTTCTTGACAATTCATTTCCCAACAGATTAC
CCCTTCAAACCACCTAAGGTTGCATTTACAACAAGAATTTATCATCCAAATATTAACAGT
AATGGCAGCATTTGTCTTGATATTCTACGATCACAGTGGTCTCCAGCACTAACTATTTCA
AAAGTACTCTTGTCCATCTGTTCTCTGTTGTGTGATCCCAATCCAGATGATCCTTTAGTG
CCTGAGATTGCTCGGATCTACAAAACAGATAGAGAAAAGTACAACAGAATAGCTCGGGAA
TGGACTCAGAAGTATGCGATGTAA

1. Jensen JP, Bates PW, Yang M, Vierstra RD, Weissman AM: Identification of a family of closely related human ubiquitin conjugating enzymes. J Biol Chem. 1995 Dec 22;270(51):30408-14. [PubMed ]
2. Rolfe M, Beer-Romero P, Glass S, Eckstein J, Berdo I, Theodoras A, Pagano M, Draetta G: Reconstitution of p53-ubiquitinylation reactions from purified components: the role of human ubiquitin-conjugating enzyme UBC4 and E6-associated protein (E6AP). Proc Natl Acad Sci U S A. 1995 Apr 11;92(8):3264-8. [PubMed ]
3. Strack P, Caligiuri M, Pelletier M, Boisclair M, Theodoras A, Beer-Romero P, Glass S, Parsons T, Copeland RA, Auger KR, Benfield P, Brizuela L, Rolfe M: SCF(beta-TRCP) and phosphorylation dependent ubiquitinationof I kappa B alpha catalyzed by Ubc3 and Ubc4. Oncogene. 2000 Jul 20;19(31):3529-36. [PubMed ]

1. DNA ligase IV
2. Polydeoxyribonucleotide synthase [ATP] 4

MAASQTSQTVASHVPFADLCSTLERIQKSKGRAEKIRHFREFLDSWRKFHDALHKNHKDV
TDSFYPAMRLILPQLERERMAYGIKETMLAKLYIELLNLPRDGKDALKLLNYRTPTGTHG
DAGDFAMIAYFVLKPRCLQKGSLTIQQVNDLLDSIASNNSAKRKDLIKKSLLQLITQSSA
LEQKWLIRMIIKDLKLGVSQQTIFSVFHNDAAELHNVTTDLEKVCRQLHDPSVGLSDISI
TLFSAFKPMLAAIADIEHIEKDMKHQSFYIETKLDGERMQMHKDGDVYKYFSRNGYNYTD
QFGASPTEGSLTPFIHNAFKADIQICILDGEMMAYNPNTQTFMQKGTKFDIKRMVEDSDL
QTCYCVFDVLMVNNKKLGHETLRKRYEILSSIFTPIPGRIEIVQKTQAHTKNEVIDALNE
AIDKREEGIMVKQPLSIYKPDKRGEGWLKIKPEYVSGLMDELDILIVGGYWGKGSRGGMM
SHFLCAVAEKPPPGEKPSVFHTLSRVGSGCTMKELYDLGLKLAKYWKPFHRKAPPSSILC
GTEKPEVYIEPCNSVIVQIKAAEIVPSDMYKTGCTLRFPRIEKIRDDKEWHECMTLDDLE
QLRGKASGKLASKHLYIGGDDEPQEKKRKAAPKMKKVIGIIEHLKAPNLTNVNKISNIFE
DVEFCVMSGTDSQPKPDLENRIAEFGGYIVQNPGPDTYCVIAGSENIRVKNIILSNKHDV
VKPAWLLECFKTKSFVPWQPRFMIHMCPSTKEHFAREYDCYGDSYFIDTDLNQLKEVFSG
IKNSNEQTPEEMASLIADLEYRYSWDCSPLSMFRRHTVYLDSYAVINDLSTKNEGTRLAI
KALELRFHGAKVVSCLAEGVSHVIIGEDHSRVADFKAFRRTFKRKFKILKESWVTDSIDK
CELQEENQYLI

• ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m = AMP + diphosphate + (deoxyribonucleotide)n+m

• BRCT (PF00533 )
• DNA_ligase_A_C (PF04679 )
• DNA_ligase_A_M (PF01068 )
• DNA_ligase_A_N (PF04675 )

• None

• None

ATGAGACTAATTCTTCCTCAGCTAGAAAGAGAGAGAATGGCCTATGGAATTAAAGAAACT
ATGCTTGCTAAGCTTTATATTGAGTTGCTTAATTTACCTAGAGATGGAAAAGATGCCCTC
AAACTTTTAAACTACAGAACACCCACTGGAACTCATGGAGATGCTGGAGACTTTGCAATG
ATTGCATATTTTGTGTTGAAGCCAAGATGTTTACAGAAAGGAAGTTTAACCATACAGCAA
GTAAACGACCTTTTAGACTCAATTGCCAGCAATAATTCTGCTAAAAGAAAAGACCTAATA
AAAAAGAGCCTTCTTCAACTTATAACTCAGAGTTCAGCACTTGAGCAAAAGTGGCTTATA
CGGATGATCATAAAGGATTTAAAGCTTGGTGTTAGTCAGCAAACTATCTTTTCTGTTTTT
CATAATGATGCTGCTGAGTTGCATAATGTCACTACAGATCTGGAAAAAGTCTGTAGGCAA
CTGCATGATCCTTCTGTAGGACTCAGTGATATTTCTATCACTTTATTTTCTGCATCAAAA
CCAATGCTAGCTGCTATTGCAGATATTGAGCACATTGAGAAGGATATGAAACATCAGAGT
TTCTACATAGAAACCAAGCTAGATGGTGAACGTATGCAAATGCACAAAGATGGAGATGTA
TATAAATACTTCTCTCGAAATGGATATAACTACACTGATCAGTTTGGTGCTTCTCCTACT
GAAGGTTCTCTTACCCCATTCATTCATAATGCATTCAAAGCAGATATACAAATCTGTATT
CTTGATGGTGAGATGATGGCCTATAATCCTAATACACAAACTTTCATGCAAAAGGGAACT
AAGTTTGATATTAAAAGAATGGTAGAGGATTCTGATCTGCAAACTTGTTATTGTGTTTTT
GATGTATTGATGGTTAATAATAAAAAGCTAGGGCATGAGACTCTGAGAAAGAGGTATGAG
ATTCTTAGTAGTATTTTTACACCAATTCCAGGTAGAATAGAAATAGTGCAGAAAACACAA
GCTCATACTAAGAATGAAGTAATTGATGCATTGAATGAAGCAATAGATAAAAGAGAAGAG
GGAATTATGGTAAAACAACCTCTATCCATCTACAAGCCAGACAAAAGAGGTGAAGGGTGG
TTAAAAATTAAACCAGAGTATGTCAGTGGACTAATGGATGAATTGGACATTTTAATTGTT
GGAGGATATTGGGGTAAAGGATCACGGGGTGGAATGATGTCTCATTTTCTGTGTGCAGTA
GCAGAGAAGCCCCCTCCTGGTGAGAAGCCATCTGTGTTTCATACTCTCTCTCGTGTTGGG
TCTGGCTGCACCATGAAAGAACTGTATGATCTGGGTTTGAAATTGGCCAAGTATTGGAAG
CCTTTTCATAGAAAAGCTCCACCAAGCAGCATTTTATGTGGAACAGAGAAGCCAGAAGTA
TACATTGAACCTTGTAATTCTGTCATTGTTCAGATTAAAGCAGCAGAGATCGTACCCAGT
GATATGTATAAAACTGGCTGCACCTTGCGTTTTCCACGAATTGAAAAGATAAGAGATGAC
AAGGAGTGGCATGAGTGCATGACCCTGGACGACCTAGAACAACTTAGGGGGAAGGCATCT
GGTAAGCTCGCATCTAAACACCTTTATATAGGTGGTGATGATGAACCACAAGAAAAAAAG
CGGAAAGCTGCCCCAAAGATGAAGAAAGTTATTGGAATTATTGAGCACTTAAAAGCACCT
AACCTTACTAACGTTAACAAAATTTCTAATATATTTGAAGATGTAGAGTTTTGTGTTATG
AGTGGAACAGATAGCCAGCCAAAGCCTGACCTGGAGAACAGAATTGCAGAATTTGGTGGT
TATATAGTACAAAATCCAGGCCCAGACACGTACTGTGTAATTGCAGGGTCTGAGAACATC
AGAGTGAAAAACATAATTTTGTCAAATAAACATGATGTTGTCAAGCCTGCATGGCTTTTA
GAATGTTTTAAGACCAAAAGCTTTGTACCATGGCAGCCTCGCTTTATGATTCATATGTGC
CCATCAACCAAAGAACATTTTGCCCGTGAATATGATTGCTATGGTGATAGTTATTTCATT
GATACAGACTTGAACCAACTGAAGGAAGTATTCTCAGGAATTAAAAATTCTAACGAGCAG
ACTCCTGAAGAAATGGCTTCTCTGATTGCTGATTTAGAATATCGGTATTCCTGGGATTGC
TCTCCTCTCAGTATGTTTCGACGCCACACCGTTTATTTGGACTCGTATGCTGTTATTAAT
GACCTGAGTACCAAAAATGAGGGGACAAGGTTAGCTATTAAAGCCTTGGAGCTTCGGTTT
CATGGAGCAAAAGTAGTTTCTTGTTTAGCTGAGGGAGTGTCTCATGTAATAATTGGGGAA
GATCATAGTCGTGTTGCAGATTTTAAAGCTTTTAGAAGAACTTTTAAGAGAAAGTTTAAA
ATCCTAAAAGAAAGTTGGGTAACTGATTCAATAGACAAGTGTGAATTACAAGAAGAAAAC
CAGTATTTGATTTAA

1. Wei YF, Robins P, Carter K, Caldecott K, Pappin DJ, Yu GL, Wang RP, Shell BK, Nash RA, Schar P, et al.: Molecular cloning and expression of human cDNAs encoding a novel DNA ligase IV and DNA ligase III, an enzyme active in DNA repair and recombination. Mol Cell Biol. 1995 Jun;15(6):3206-16. [PubMed ]
2. Robins P, Lindahl T: DNA ligase IV from HeLa cell nuclei. J Biol Chem. 1996 Sep 27;271(39):24257-61. [PubMed ]
3. Grawunder U, Zimmer D, Fugmann S, Schwarz K, Lieber MR: DNA ligase IV is essential for V(D)J recombination and DNA double-strand break repair in human precursor lymphocytes. Mol Cell. 1998 Oct;2(4):477-84. [PubMed ]
4. Calsou P, Delteil C, Frit P, Drouet J, Salles B: Coordinated assembly of Ku and p460 subunits of the DNA-dependent protein kinase on DNA ends is necessary for XRCC4-ligase IV recruitment. J Mol Biol. 2003 Feb 7;326(1):93-103. [PubMed ]
5. Riballo E, Critchlow SE, Teo SH, Doherty AJ, Priestley A, Broughton B, Kysela B, Beamish H, Plowman N, Arlett CF, Lehmann AR, Jackson SP, Jeggo PA: Identification of a defect in DNA ligase IV in a radiosensitive leukaemia patient. Curr Biol. 1999 Jul 1;9(13):699-702. [PubMed ]
6. Riballo E, Doherty AJ, Dai Y, Stiff T, Oettinger MA, Jeggo PA, Kysela B: Cellular and biochemical impact of a mutation in DNA ligase IV conferring clinical radiosensitivity. J Biol Chem. 2001 Aug 17;276(33):31124-32. Epub 2001 May 10. [PubMed ]
7. O'Driscoll M, Cerosaletti KM, Girard PM, Dai Y, Stumm M, Kysela B, Hirsch B, Gennery A, Palmer SE, Seidel J, Gatti RA, Varon R, Oettinger MA, Neitzel H, Jeggo PA, Concannon P: DNA ligase IV mutations identified in patients exhibiting developmental delay and immunodeficiency. Mol Cell. 2001 Dec;8(6):1175-85. [PubMed ]

1. Arginine--tRNA ligase
2. ArgRS

MDVLVSECSARLLQQEEEIKSLTAEIDRLKNCGCLGASPNLEQLQEENLKLKYRLNILRK
SLQAERNKPTKNMINIISRLQEVFGHAIKAAYPDLENPPLLVTPSQQAKFGDYQCNSAMG
ISQMLKTKEQKVNPREIAENITKHLPDNECIEKVEIAGPGFINVHLRKDFVSEQLTSLLV
NGVQLPALGENKKVIVDFSSPNIAKEMHVGHLRSTIIGESISRLFEFAGYDVLRLNHVGD
WGTQFGMLIAHLQDKFPDYLTVSPPIGDLQVFYKESKKRFDTEEEFKKRAYQCVVLLQGK
NPDITKAWKLICDVSRQELNKIYDALDVSLIERGESFYQDRMNDIVKEFEDRGFVQVDDG
RKIVFVPGCSIPLTIVKSDGGYTYDTSDLAAIKQRLFEEKADMIIYVVDNGQSVHFQTIF
AAAQMIGWYDPKVTRVFHAGFGVVLGEDKKKFKTRSGETVRLMDLLGEGLKRSMDKLKEK
ERDKVLTAEELNAAQTSVAYGCIKYADLSHNRLNDYIFSFDKMLDDRGNTAAYLLYAFTR
IRSIARLANIDEEMLQKAARETKILLDHEKEWKLGRCILRFPEILQKILDDLFLHTLCDY
IYELATAFTEFYDSCYCVEKDRQTGKILKVNMWRMLLCEAVAAVMAKGFDILGIKPVQRM

• Aminoacyl-tRNA biosynthesis (map00970 )
• Arginine and Proline Metabolism (map00330 )

• ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)

• Arg_tRNA_synt_N (PF03485 )
• DALR_1 (PF05746 )
• tRNA-synt_1d (PF00750 )

• None

• None

ATGGACGTACTGGTGTCTGAGTGCTCCGCGCGGCTGCTGCAGCAGGAAGAAGAGATTAAA
TCTCTGACTGCTGAAATTGACCGGTTGAAAAACTGTGGCTGTTTAGGAGCTTCTTCAAAT
TTGGAGCAGTTACAAGAAGAAAATTTAAAATTAAAGTATCGACTGAATATTCTTCGAAAG
AGTCTTCAGGCAGAAAGGAACAAACCAACTAAAAATATGATTAACATTATTAGCCGCCTA
CAAGAGGTCTTTGGTCATGCAATTAAGGCTGCATATCCAGATTTGGAAAATCCTCCTCTG
CTAGTGACACCAAGTCAGCAGGCCAAGTTTGGGGACTATCAGTGTAATAGTGCTATGGGT
ATTTCTCAGATGCTTAAAACCAAGGAACCGGAAGTTAATCCAGGGGAATTTGCTGAAAAC
ATTACCAAACACCTCCCGGCCATGGATGTTTTGAAAAGAGTTGAATTTGCTGGCCCTGGC
TTTATTAATGGCCACTTAAGAAAGGATTTTGTATCAGAACAATTGACCAGTCTTCTAGTG
AATGGAGTTCAACTACCTGCTCTGGGAGAGAATAAAAAGGTTATAGTTGACTTTTCCTCC
CCTAATATAGCTAAAGAGATGCATGTAGGCCACCTGAGGTCAACTATCATAGGAGAGAGT
ATAAGCCGCCTCTTTGAATTTGCAGGGTATGACGTGCTCAGGTTAAATCATGTAGGAGAC
TGGGGGACCCAGTTTGGCATGCTCATCGCTCACCTGCAAGACAAATTTCCAGATTATCTA
ACAGTTTCACCTCCTATTGGGGATCTTCAGGTCTTTTATAAGGAATCTAAGAAGAGGTTT
GATACTGAGGAGGAATTTAAGAAGCGAGCATATCAGTGTGTAGTTCTGCTCCAGGGTAAA
AACCCAGATATTACAAAAGCTTATCTGCTGATGTCTGATGTCTCCCGCCAAGAGTTAAAT
AAAATCTATGATGCATTGGACGTCTCTTTAATAGAGAGAGGGGAATCCTTCTATCAAGAT
AGGATGAATGATATTGTAAAGGAATTTGAAGATAGAGGATTTGTGCAGGTGGATGATGGC
AGAAAGATTGTATTTGTCCCAGGGTGTTCCATACCATTAACCATAGTAAAATCAGATGGA
GGTTATACCTATGATACATCTGACCTGGCTGCTATTAAACAAAGACTATTTGAGGAAAAA
GCAGATATGATTATCTATGTTGTGGACAATGGACAATCTGTGCACTTCCAGACAATATTT
GCTGCTGCTCAAATGATTGGTTGGTATGACCCTAAAGTAACTCGAGTCTTCCATGCTGGA
TTTGGTGTGGTGCTAGGGGAAGACAAGAAAAAGTTTAAAACACGTTCGGGTGAAACAGTG
CGCCTCATGGATCTTCTGGGAGAAGGACTAAAACGATCCATGGACAAGTTGAAGGAAAAA
GAAAGAGACAAGGTCTTAACTGCAGAGGAATTGAATGCTGCTCAGACATCCGTTGCATAT
GGCTGCATCAAATATGCTGACCTTTCCCATAACCGGTTGAATGACTACATCTTCTCCTTT
GACAAAATGCTAGATGACAGAGGAAATACAGCTGCTTACTTGTTGTATGCCTTCACTAGA
ATCAGGTCTATTGCACGTCTGGCCAATATTGATGAAGAAATGCTCCAAAAAGCTGCTCGA
GAAACCAAGATTCTTTTGGTTCATGAGAAGGAATGGAAACTAGGCCGGTGCATTTTACGG
TTCCCTGAGATTCTGCAAAAGATTTTAGATGACTTATTTCTCCACACTCTCTGTGATTAT
ATATATGAGCTGGCAACTGCTTTCACAGAGTTCTATGATAGCTGCTACTGTGTGGAGAAA
GATAGACAGACTGGGAAAATATTGAAGGTGAACATGTGGCGTATCTTGTGTGAAACAGTA
GCTGCTGTCATGGCCAAGGGGTTTGATACCCTGGGGATAAAACCTGGCCCAAGGGTGTAA

1. Girjes AA, Hobson K, Chen P, Lavin MF: Cloning and characterization of cDNA encoding a human arginyl-tRNA synthetase. Gene. 1995 Oct 27;164(2):347-50. [PubMed ]
2. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed ]

1. Leucine--tRNA ligase
2. LeuRS

MASVWQRLGFYASLLKRQLNGGPDVIKWERRVIPGCTRSIYSATGKWTKEYTLQTRKDVE
KWWHQRIKEQASKISEADKSKPKFYVLSMFPYPSGKLHMGHVRVYTISDTIARFQKMRGM
QVINPMGWDAFGLPAENAAVERNLHPQSWTQSNIKHMRKQLDRLGLCFSWDREITTCLPD
YYKWTQYLFIKLYEAGLAYQKEALVNWDPVDQTVLANEQVDEHGCSWRSGAKVEQKYLRQ
WFIKTTAYAKAMQDALADLPEWYGIKGMQAHWIGDCVGCHLDFTLKVHGQATGEKLTAYT
ATPEAIYGTSHVAISPSHRLLHGHSSLKEALRMALVPGKDCLTPVMAVNMLTQQEVPVVI
LAKADLEGSLDSKIGIPSTSSEDTILAQTLGLAYSEVIETLPDGTERLSSSAEFTGMTRQ
DAFLALTQKARGKRVGGDVTSDKLKDWLISRQRYWGTPIPIVHCPVCGPTPVPLEDLPVT
LPNIASFTGKGGPPLAMASEWVNCSCPRCKGAAKRETDTMDTFVDSAWYYFRYTDPHNPH
SPFNTAVADYWMPVDLYIGGKEHAVMHLFYARFFSHFCHDQKMVKHREPFHKLLAQGLIK
GQTFRLPSGQYLQREEVDLTGSVPVHAKTKEKLEVTWEKMSKSKHNGVDPEEVVEQYGID
TIRLYILFAAPPEKDILWDVKTDALPGVLRWQQRLWTLTTRFIEARASGKSPQPQLLSNK
EKAEARKLWEYKNSVISQVTTHFTEDFSLNSAISQLMGLSNALSQASQSVILHSPEFEDA
LCALMVMAAPLAPHVTSEIWAGLALVPRKLCAHYTWDASVLLQAWPAVDPEFLQQPEVVQ
MAVLINNKACGKIPVPQQVARDQDKVHEFVLQSELGVRLLQGRSIKKSFLSPRTALINFL
VQD

• Aminoacyl-tRNA biosynthesis (map00970 )

• ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu)

• Anticodon_1 (PF08264 )
• tRNA-synt_1 (PF00133 )
• tRNA-synt_1g (PF09334 )

• None

• None

AGAATGGCTTCTGTTTGGCAGAGATTGGGTTTTTATGCCTCTCTTCTGAAAAGACAGCTA
AATGGTGGGCCAGATGTCATCAAGTGGGAAAGGAGAGTAATTCCCGGATGTACCAGAAGC
ATCTACAGTGCCACGGGAAAGTGGACAAAAGAGTATACATTGCAGACAAGAAAGGATGTT
GAGAAATGGTGGCATCAACGAATAAAAGAACAGGCCTCCAAAATTTCAGAAGCTGATAAA
TCGAAGCCAAAATTTTACGTGCTTTCCATGTTCCCTTATCCTTCTGGTAAGCTGCACATG
GGCCATGTGCGTGTCTACACCATCAGCGACACCATAGCACGGTTCCAGAAGATGAGAGGG
ATGCAGGTCATCAACCCCATGGGATGGGATGCTTTTGGATTGCCTGCTGAAAATGCCGCA
GTCGAGAGGAATCTACATCCACAAAGTTGGACACAAAGTAATATTAAACACATGAGGAAA
CAGCTTGATCGTCTGGGCCTGTGTTTCAGCTGGGATAGGGAAATAACTACGTGTTTGCCA
GATTACTACAAGTGGACTCAGTATCTCTTTATTAAACTGTATGAGGCTGGGCTGGCCTAT
CAAAAGGAGGCCCTGGTTAACTGGGACCCAGTGGATCAAACAGTGCTTGCCAATGAGCAG
GTGGATGAACATGGCTGTTCATGGCGTTCTGGAGCAAAGGTGGAACAGAAGTACCTCAGA
CAATGGTTTATTAAGACAACCGCTTATGCAAAGGCCATGCAGGACGCGTTGGCAGACCTT
CCAGAATGGTATGGAATAAAAGGCATGCAAGCCCACTGGATTGGGGACTGTGTGGGCTGC
CACCTGGACTTCACATTAAAGGTTCATGGGCAAGCCACGGGCGAAAAGCTGACTGCCTAT
ACGGCCACCCCTGAAGCCATTTATGGCACCTCCCACGTGGCCATCTCGCCCAGCCACAGA
CTCCTACATGGGCACAGCTCTCTGAAGGAAGCCTTGAGGATGGCCCTTGTCCCTGGCAAA
GATTGCCTCACGCCTGTAATGGCTGTGAACATGCTTACCCAGCAGGAGGTCCCTGTCGTT
ATTTTGGCCAAAGCTGACTTGGAAGGCTCTCTGGATTCAAAAATAGGAATTCCCAGTACT
AGCTCAGAGGACACCATCTTAGCCCAAACCCTGGGCCTGGCCTACTCTGAAGTCATTGAA
ACTTTGCCAGATGGCACAGAGAGACTGAGCAGCTCTGCTGAGTTCACAGGTATGACCCGG
CAGGATGCTTTTCTAGCCCTGACTCAGAAAGCCCGGGGGAAGAGAGTGGGTGGAGACGTG
ACAAGTGATAAACTGAAAGACTGGCTGATTTCACGGCAGCGGTACTGGGGCACACCAATC
CCCATTGTCCACTGCCCAGTCTGTGGCCCCACACCTGTGCCCCTGGAGGACTTGCCTGTG
ACCCTGCCCAACATCGCGTCTTTCACTGGCAAGGGAGGCCCCCCACTGGCCATGGCTTCA
GAGTGGGTGAACTGCTCCTGCCCAAGGTGCAAGGGAGCAGCCAAGAGAGAGACAGACACG
ATGGATACCTTTGTTGATTCTGCTTGGTACTACTTCAGATACACTGACCCTCATAATCCA
CACAGCCCTTTTAACACAGCAGTGGCCGATTACTGGATGCCTGTGGATTTGTACATTGGA
GGGAAAGAACATGCCGTCATGCACTTGTTCTATGCAAGATTCTTTAGTCATTTTTGCCAT
GATCAAAAAATGGTTAAACATAGGGAGCCTTTTCATAAGCTGCTGGCCCAAGGCCTTATC
AAGGGGCAGACATTCCGCCTACCATCTGGACAGTATCTACAGAGAGAGGAAGTGGATCTC
ACAGGTTCCGTTCCTGTTCATGCAAAAACGAAAGAGAAGTTAGAGGTGACGTGGGAGAAG
ATGAGTAAGTCCAAACACAACGGGGTGGACCCAGAGGAAGTTGTGGAGCAGTATGGGATC
GACACGATTCGGCTCTACATCCTTTTTGCTGCCCCTCCTGAGAAGGATATCTTGTGGGAT
GTGAAAACTGATGCTCTCCCTGGGGTGCTGAGATGGCAACAACGACTGTGGACCTTGACA
ACTCGGTTTATTGAGGCCAGGGCTTCTGGGAAGTCTCCCCAGCCTCAGCTGCTGAGTAAC
AAGGAGAAAGCTGAGGCCAGGAAGCTCTGGGAGTACAAGAACTCCGTCATCTCTCAGGTG
ACCACCCATTTCACAGAGGACTTCTCACTGAATTCTGCAATTTCTCAGCTGATGGGACTC
AGCAATGCCCTCTCGCAAGCCTCTCAGAGCGTCATTCTCCACAGCCCCGAGTTTGAGGAT
GCTTTGTGTGCCCTGATGGTAATGGCTGCTCCACTGGCCCCTCATGTAACCTCAGAGATC
TGGGCAGGCCTGGCGCTGGTGCCGAGGAAGCTCTGTGCCCACTACACTTGGGATGCCAGT
GTGCTGCTCCAGGCATGGCCTGCTGTGGACCCGGAGTTCCTGCAGCAGCCTGAGGTTGTC
CAGATGGCAGTTCTGATCAACAATAAAGCTTGTGGCAAAATTCCTGTGCCCCAACAAGTT
GCCCGGGACCAGGACAAAGTCCACGAATTTGTTCTTCAAAGCGAGCTGGGTGTCAGGCTT
TTGCAAGGACGAAGCATCAAGAAGTCCTTCCTTTCCCCGAGAACTGCCCTCATCAACTTC
CTGGTGCAAGATTGA

1. Nomura N, Miyajima N, Sazuka T, Tanaka A, Kawarabayasi Y, Sato S, Nagase T, Seki N, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1. DNA Res. 1994;1(1):27-35. [PubMed ]

1. RNA-3'-phosphate cyclase
2. RNA cyclase

MAGPRVEVDGSIMEGGGQILRVSTALSCLLGLPLRVQKIRAGRSTPGLRPQHLSGLEMIR
DLCDGQLEGAEIGSTEITFTPEKIKGGIHTADTKTAGSVCLLMQVSMPCVLFAASPSELH
LKGGTNAEMAPQIDYTVMVFKPIVEKFGFIFNCDIKTRGYYPKGGGEVIVRMSPVKQLNP
INLTERGCVTKIYGRAFVAGVLPFKVAKDMAAAAVRCIRKEIRDLYVNIQPVQEPKDQAF
GNGNGIIIIAETSTGCLFAGSSLGKRGVNADKVGIEAAEMLLANLRHGGTVDEYLQDQLI
VFMALANGVSRIKTGPVTLHTQTAIHFAEQIAKAKFIVKKSEDEEDAAKDTYIIECQGIG
MTNPNL

• ATP + RNA 3'-terminal-phosphate = AMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate

• RTC (PF01137 )
• RTC_insert (PF05189 )

• None

• None

ATGGCGGGGCCGCGGGTGGAGGTCGATGGCAGCATCATGGAAGGGGGCGGCCAGATCCTG
AGAGTCTCTACGGCCTTGAGCTGTCTCCTAGGCCTCCCCTTGCGGGTGCAGAAGATCCGA
GCCGGCCGGAGCACGCCAGGCCTGAGGCCTCAACATTTATCTGGACTGGAAATGATTCGA
GATTTGTGTGATGGGCAACTGGAGGGGGCAGAAATTGGCTCAACAGAAATAACCTTTACA
CCAGAGAAGATCAAAGGTGGAATCCACACAGCAGATACCAAGACAGCAGGGAGTGTGTGC
CTCTTGATGCAGGTCTCAATGCCGTGTGTTCTCTTTGCTGCTTCTCCATCAGAACTTCAT
TTGAAAGGTGGAACTAATGCTGAAATGGCACCACAGATCGATTATACAGTGATGGTCTTC
AAGCCAATTGTTGAAAAATTTGGTTTCATATTTAATTGTGACATTAAAACAAGGGGATAT
TACCCAAAAGGGGGTGGTGAAGTGATTGTTCGAATGTCACCAGTTAAACAATTGAACCCT
ATAAATTTAACTGAGCGTGGCTGTGTGACTAAGATATATGGAAGAGCTTTCGTTGCTGGT
GTTTTGCCATTTAAAGTAGCAAAAGATATGGCAGCGGCAGCAGTTAGATGCATCAGAAAG
GAGATCCGGGATTTGTATGTTAACATCCAGCCTGTTCAAGAACCTAAAGACCAAGCATTT
GGCAATGGAAATGGAATAATAATTATTGCTGAGACCTCCACTGGCTGTTTGTTTGCTGGA
TCATCGCTTGGTAAACGAGGTGTAAATGCAGACAAAGTTGGAATTGAAGCTGCCGAAATG
CTATTAGCAAATCTTAGACATGGTGGTACTGTGGATGAGTATCTGCAAGACCAGCTGATT
GTTTTCATGGCATTAGCCAATGGAGTTTCCAGAATAAAAACAGGACCAGTTACACTCCAT
ACGCAAACCGCGATACATTTTGCTGAACAAATAGCAAAGGCTAAATTTATTGTGAAGAAA
TCAGAAGATGAAGAAGACGCCGCTAAAGATACTTATATTATTGAATGCCAAGGAATTGGG
ATGACAAATCCAAATCTATAG

1. Genschik P, Billy E, Swianiewicz M, Filipowicz W: The human RNA 3'-terminal phosphate cyclase is a member of a new family of proteins conserved in Eucarya, Bacteria and Archaea. EMBO J. 1997 May 15;16(10):2955-67. [PubMed ]
2. Filipowicz W, Vicente O: RNA 3'-terminal phosphate cyclase from HeLa cells. Methods Enzymol. 1990;181:499-510. [PubMed ]

1. DNA ligase III
2. Polydeoxyribonucleotide synthase [ATP] 3

MAEQRFCVDYAKRGTAGCKKCKEKIVKGVCRIGKVVPNPFSESGGDMKEWYHIKCMFEKL
ERARATTKKIEDLTELEGWEELEDNEKEQITQHIADLSSKAAGTPKKKAVVQAKLTTTGQ
VTSPVKGASFVTSTNPRKFSGFSAKPNNSGEAPSSPTPKRSLSSSKCDPRHKDCLLREFR
KLCAMVADNPSYNTKTQIIQDFLRKGSAGDGFHGDVYLTVKLLLPGVIKTVYNLNDKQIV
KLFSRIFNCNPDDMARDLEQGDVSETIRVFFEQSKSFPPAAKSLLTIQEVDEFLLRLSKL
TKEDEQQQALQDIASRCTANDLKCIIRLIKHDLKMNSGAKHVLDALDPNAYEAFKASRNL
QDVVERVLHNAQEVEKEPGQRRALSVQASLMTPVQPMLAEACKSVEYAMKKCPNGMFSEI
KYDGERVQVHKNGDHFSYFSRSLKPVLPHKVAHFKDYIPQAFPGGHSMILDSEVLLIDNK
TGKPLPFGTLGVHKKAAFQDANVCLFVFDCIYFNDVSLMDRPLCERRKFLHDNMVEIPNR
IMFSEMKRVTKALDLADMITRVIQEGLEGLVLKDVKGTYEPGKRHWLKVKKDYLNEGAMA
DTADLVVLGAFYGQGSKGGMMSIFLMGCYDPGSQKWCTVTKCAGGHDDATLARLQNELDM
VKISKDPSKIPSWLKVNKIYYPDFIVPDPKKAAVWEITGAEFSKSEAHTADGISIRFPRC
TRIRDDKDWKSATNLPQLKELYQLSKEKADFTVVAGDEGSSTTGGSSEENKGPSGSAVSR
KAPSKPSASTKKAEGKLSNSNSKDGNMQTAKPSAMKVGEKLATKSSPVKVGEKRKAADET
LCQTKVLLDIFTGVRLYLPPSTPDFSRLRRYFVAFDGDLVQEFDMTSATHVLGSRDKNPA
AQQVSPEWIWACIRKRRLVAPC

• ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m = AMP + diphosphate + (deoxyribonucleotide)n+m

• DNA_ligase_A_C (PF04679 )
• DNA_ligase_A_M (PF01068 )
• DNA_ligase_A_N (PF04675 )
• zf-PARP (PF00645 )

• None

• None

ATGGCTGAGCAACGGTTCTGTGTGGACTATGCCAAGCGTGGCACAGCTGGCTGCAAAAAA
TGCAAGGAAAAGATTGTGAAGGGCGTATGCCGAATTGGCAAAGTGGTGCCCAATCCCTTC
TCAGAGTCTGGGGGTGATATGAAAGAGTGGTACCACATTAAATGCATGTTTGAGAAACTA
GAGCGGGCCCGGGCCACCACAAAAAAAATCGAGGACCTCACAGAGCTGGAAGGCTGGGAA
GAGCTGGAAGATAATGAGAAGGAACAGATAACCCAGCACATTGCAGATCTGTCTTCTAAG
GCAGCAGGTACACCAAAGAAGAAAGCTGTTGTCCAGGCTAAGTTGACAACCACTGGCCAG
GTGACTTCTCCAGTGAAAGGCGCCTCATTTGTCACCAGTACCAATCCCCGGAAATTTTCT
GGCTTTTCAGCCAAGCCCAACAACTCTGGGGAAGCCCCCTCGAGCCCCACCCCTAAGAGA
AGTCTGTCTTCAAGCAAATGTGACCCCAGGCATAAGGACTGTCTGCTACGGGAGTTTCGA
AAGTTATGCGCCATGGTGGCCGATAATCCTAGCTACAACACGAAGACCCAGATCATCCAG
GACTTCCTTCGGAAAGGCTCAGCAGGAGATGGTTTCCACGGTGATGTGTACCTAACAGTG
AAGCTGCTGCTGCCAGGAGTCATTAAGACTGTTTACAACTTGAACGATAAGCAGATTGTG
AAGCTTTTCAGTCGCATTTTTAACTGCAACCCAGATGATATGGCACGGGACCTAGAGCAG
GGTGACGTGTCAGAGACAATCAGAGTCTTCTTTGAGCAGAGCAAGTCTTTCCCCCCAGCT
GCCAAGAGCCTCCTTACCATCCAGGAAGTGGATGAGTTCCTTCTGCGGCTGTCCAAGCTC
ACCAAGGAGGATGAGCAGCAACAGGCCCTACAGGACATTGCCTCCAGGTGTACAGCCAAT
GACCTTAAATGCATCATCAGGTTGATCAAACATGATCTGAAGATGAACTCAGGTGCAAAA
CATGTGTTAGACGCCCTTGACCCCAATGCCTATGAAGCCTTCAAAGCCTCGCGCAACCTG
CAGGATGTGGTGGAGCGGGTCCTTCACAACGCGCAGGAGGTGGAGAAGGAGCCGGGCCAG
AGACGAGCTCTGAGCGTCCAGGCCTCGCTGATGACACCTGTGCAGCCCATGTTGGCGGAG
GCCTGCAAGTCCGTTGAGTATGCAATGAAGAAATGTCCCAATGGCATGTTCTCTGAGATC
AAGTACGATGGAGAGCGAGTCCAGGTGCATAAGAATGGAGACCACTTCAGCTACTTCAGC
CGCAGTCTCAAGCCCGTCCTTCCTCACAAGGTGGCCCACTTTAAGGACTACATTCCCCAG
GCTTTTCCTGGGGGCCACAGCATGATCTTGGATTCTGAAGTGCTTCTGATTGACAACAAG
ACAGGCAAACCACTGCCCTTTGGGACTCTGGGAGTACACAAGAAAGCAGCCTTCCAGGAT
GCTAATGTCTGCCTGTTTGTTTTTGATTGTATCTACTTTAATGATGTCAGCTTGATGGAC
AGACCTCTGTGTGAGCGGCGGAAGTTTCTTCATGACAACATGGTTGAAATTCCAAACCGG
ATCATGTTCTCAGAAATGAAGCGAGTCACAAAAGCTTTGGACTTGGCTGACATGATAACC
CGGGTGATCCAGGAGGGATTGGAGGGGCTGGTGCTGAAGGATGTGAAGGGTACATATGAG
CCTGGGAAGCGGCACTGGCTGAAAGTGAAGAAAGACTATTTGAACGAGGGGGCCATGGCC
GACACAGCTGACCTGGTGGTCCTTGGAGCCTTCTATGGGCAAGGGAGCAAAGGCGGCATG
ATGTCAATCTTCCTCATGGGCTGCTACGACCCTGGCAGCCAGAAGTGGTGCACAGTCACC
AAGTGTGCAGGAGGCCATGATGATGCCACGCTTGCCCGCCTGCAGAATGAACTAGACATG
GTGAAGATCAGCAAGGACCCCAGCAAAATACCCAGCTGGTTGAAGGTCAACAAGATCTAC
TATCCTGACTTCATCGTCCCAGACCCAAAGAAAGCTGCCGTGTGGGAGATCACAGGGGCT
GAATTCTCCAAATCGGAGGCTCATACAGCTGACGGGATCTCCATCCGATTCCCTCGCTGC
ACCCGAATCCGAGATGATAAGGACTGGAAATCTGCCACTAACCTTCCCCAACTCAAGGAA
CTGTACCAGTTGTCCAAGGAGAAGGCAGACTTCACTGTAGTGGCTGGAGATGAGGGGAGC
TCCACTACAGGGGGTAGCAGTGAAGAGAATAAGGGTCCCTCAGGGTCTGCTGTGTCCCGC
AAGGCCCCCAGCAAGCCCTCAGCCAGTACCAAGAAAGCAGAAGGGAAGCTGAGTAACTCC
AACAGCAAAGATGGCAACATGCAGACTGCAAAGCCTTCCGCTATGAAGGTGGGGGAGAAG
CTGGCCACAAAGTCTTCTCCAGTGAAAGTAGGGGAGAAGCGGAAAGCTGCTGATGAGACG
CTGTGCCAAACAAAGGTATTGCTGGACATCTTCACTGGGGTGCGGCTTTACTTGCCACCC
TCCACACCAGACTTCAGCCGTCTCAGACGCTACTTTGTGGCATTCGACGGGGACCTGGTA
CAGGAATTTGATATGACTTCAGCCACGCACGTGCTGGGTAGCAGGGACAAGAACCCTGCG
GCCCAGCAGGTCTCCCCAGAGTGGATTTGGGCATGTATCCGGAAACGGAGACTGGTAGCT
CCCTGCTAG

1. Wei YF, Robins P, Carter K, Caldecott K, Pappin DJ, Yu GL, Wang RP, Shell BK, Nash RA, Schar P, et al.: Molecular cloning and expression of human cDNAs encoding a novel DNA ligase IV and DNA ligase III, an enzyme active in DNA repair and recombination. Mol Cell Biol. 1995 Jun;15(6):3206-16. [PubMed ]
2. Chen J, Tomkinson AE, Ramos W, Mackey ZB, Danehower S, Walter CA, Schultz RA, Besterman JM, Husain I: Mammalian DNA ligase III: molecular cloning, chromosomal localization, and expression in spermatocytes undergoing meiotic recombination. Mol Cell Biol. 1995 Oct;15(10):5412-22. [PubMed ]

1. Ubiquitin-protein ligase D3
2. Ubiquitin carrier protein D3
3. Ubiquitin-conjugating enzyme E2-17 kDa 3
4. E2(17KB 3

MALKRINKELSDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDY
PFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLV
PEIARIYKTDRDKYNRISREWTQKYAM

• Ubiquitin mediated proteolysis (map04120 )

• ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine

• UQ_con (PF00179 )

• None

• None