1. 5-Phospho-a-D-ribose-1-diphosphate
2. 5-Phospho-alpha-D-ribose 1-diphosphate
3. 5-Phospho-a-D-ribosyl pyrophosphate
4. 5-Phosphoribose 1-pyrophosphate
5. 5-Phosphoribosyl 1-diphosphate
6. 5-Phosphoribosyl a-1-pyrophosphate
7. 5-Phosphoribosyl-1-pyrophosphate
8. 5-Phosphorylribose 1-a-diphosphate
9. 5-Phosphorylribose 1-pyrophosphate
10. 5-Phosphorylribosyl 1-pyrophosphate
11. PP-Ribose-P
12. PRPP
13. Phosphoribosyl pyrophosphate
14. Phosphoribosyl pyrophosphic acid
15. Phosphoribosyl-1-pyrophosphate
16. Phosphoribosyl-pyrophosphate
17. Phosphoribosylpyrophosphorate
18. Phosphoribosylpyrophosphoric acid
19. a-D-5-(dihydrogen phosphate) 1-(trihydrogen pyrophosphate) Ribofuranose
20. a-D-5-Phosphoribosyl 1-pyrophosphate
21. a-D-Ribofuranose 5-phosphate 1-pyrophosphate
22. 5-Phosphorylribose 1-alpha-diphosphate
23. 5-Phospho-alpha-delta-ribose-1-diphosphate
24. 5-Phospho-alpha-delta-ribose 1-diphosphate
25. 5-Phospho-alpha-delta-ribosyl pyrophosphate
26. alpha-delta-5-(dihydrogen phosphate) 1-(trihydrogen pyrophosphate) Ribofuranose
27. alpha-delta-5-Phosphoribosyl 1-pyrophosphate
28. alpha-delta-Ribofuranose 5-phosphate 1-pyrophosphate
29. 5-Phospho-alpha-D-ribose-1-diphosphate
30. 5-Phospho-alpha-D-ribosyl pyrophosphate
31. alpha-D-5-(dihydrogen phosphate) 1-(trihydrogen pyrophosphate) Ribofuranose
32. alpha-D-5-Phosphoribosyl 1-pyrophosphate
33. alpha-D-Ribofuranose 5-phosphate 1-pyrophosphate
34. PRib-PP
35. a-D-Ribofuranose, 5-(dihydrogen phosphate) 1-(trihydrogen diphosphate)
36. alpha-D-Ribofuranose, 5-(dihydrogen phosphate) 1-(trihydrogen diphosphate)
37. 5-phospho-alpha-D-riobse 1-diphosphate

• Cytoplasm

• Blood

1. Snyder FF, Dyer C, Seegmiller JE, Goldblum RM, Mills GC, Schmalstieg FC: Substrate inhibition of adenosine phosphorylation in adenosine deaminase deficiency and adenosine-mediated inhibition of PP-ribose-P dependent nucleotide synthesis in hypoxanthine phosphoribosyltransferase deficient erythrocytes. J Inherit Metab Dis. 1988;11(2):174-83. [PubMed ]
2. Gordon RB, Keough DT, Emmerson BT: HPRT-deficiency associated with normal PRPP concentration and APRT activity. J Inherit Metab Dis. 1987;10(1):82-8. [PubMed ]
3. Nishida Y, Akaoka I, Nishizawa T, Maruki M, Maruki K: Synthesis and concentration of 5-phosphoribosyl-1-pyrophosphate in erythrocytes from patients with Down's syndrome. Ann Rheum Dis. 1977 Jun;36(3):261-3. [PubMed ]
4. Ghitis J, Schreiber C, Waxman S: Phosphate-induced phosphoribosylpyrophosphate elevations to assess deranged folate and purine nucleotide metabolism. Proc Soc Exp Biol Med. 1987 Oct;186(1):90-5. [PubMed ]
5. Yamaoka T, Yano M, Kondo M, Sasaki H, Hino S, Katashima R, Moritani M, Itakura M: Feedback inhibition of amidophosphoribosyltransferase regulates the rate of cell growth via purine nucleotide, DNA, and protein syntheses. J Biol Chem. 2001 Jun 15;276(24):21285-91. Epub 2001 Apr 4. [PubMed ]
6. Blinov MN, Kamyshentsev MV, Luganova IS, Filanovskaia LI, Filippova VN: [Phosphoribosyl pyrophosphate and its metabolic enzymes in the erythrocytes in certain forms of anemia] Vopr Med Khim. 1976 Jul-Aug;22(4):456-62. [PubMed ]
7. Micheli V, Taddeo A: [Spectrophotometric assay of 5-phosphoribosyl-1-pyrophosphate synthetase (PRPP) in erythrocyte lysate (author's transl)] Quad Sclavo Diagn. 1981 Jun;17(2):209-15. [PubMed ]
8. Sakuma R, Nishina T, Yamanaka H, Kamatani N, Nishioka K, Maeda M, Tsuji A: Phosphoribosylpyrophosphate synthetase in human erythrocytes: assay and kinetic studies using high-performance liquid chromatography. Clin Chim Acta. 1991 Dec 16;203(2-3):143-52. [PubMed ]
9. Zoref-Shani E, Feinstein S, Frishberg Y, Bromberg Y, Sperling O: Kelley-Seegmiller syndrome due to a unique variant of hypoxanthine-guanine phosphoribosyltransferase: reduced affinity for 5-phosphoribosyl-1-pyrophosphate manifested only at low, physiological substrate concentrations. Biochim Biophys Acta. 2000 Feb 21;1500(2):197-203. [PubMed ]
10. Sperling O, Boer P, Brosh S, Elazar E, Szeinberg A, de Vries A: Normal activity of metabolic pathways involved in the formation and utilization of phosphoribosylpyrophosphate in erythrocytes of patients with primary metabolic gout. Nutr Metab. 1975;18(4):217-23. [PubMed ]
11. Gorbach ZV: [Determination of phosphoribosyl pyrophosphate in the erythrocytes] Lab Delo. 1977;(12):724-5. [PubMed ]
12. Marcolongo R, Pompucci G, Micheli V: Familial distribution of increased erythrocyte PP-ribose-P levels. Adv Exp Med Biol. 1977;76A:280-6. [PubMed ]
13. Becker MA, Losman MJ, Itkin P, Simkin PA: Gout with superactive phosphoribosylpyrophosphate synthetase due to increased enzyme catalytic rate. J Lab Clin Med. 1982 Apr;99(4):495-511. [PubMed ]
14. Tax WJ, Veerkamp JH: A simple and sensitive method for estimating the concentration and synthesis of 5-phosphoribosyl 1-pyrophosphate in red blood cells. Clin Chim Acta. 1977 Jul 15;78(2):209-16. [PubMed ]
15. MacDermot KD, Allsop J, Watts RW: The rate of purine synthesis de nova in blood mononuclear cells in vitro from patients with familial hyperuricaemic nephropathy. Clin Sci (Lond). 1984 Aug;67(2):249-58. [PubMed ]
16. Emmerson BT, Gordon RB, Thompson L: Adenine phosphoribosyltransferase deficiency: its inheritance and occurrence in a female with gout and renal disease. Aust N Z J Med. 1975 Oct;5(5):440-6. [PubMed ]
17. Zerez CR, Lachant NA, Tanaka KR: Decreased erythrocyte phosphoribosylpyrophosphate synthetase activity and impaired formation in thalassemia minor: a mechanism for decreased adenine nucleotide content. J Lab Clin Med. 1989 Jul;114(1):43-50. [PubMed ]
18. Rylance HJ, Wallace RC, Nuki G: A method for the determination of 5-phosphoribosyl 1-pyrophosphate concentrations in erythrocytes using high-performance liquid chromatography. Anal Biochem. 1987 Feb 1;160(2):337-41. [PubMed ]
19. Kane MA, Roth E, Raptis G, Schreiber C, Waxman S: Effect of intracellular folate concentration on the modulation of 5-fluorouracil cytotoxicity by the elevation of phosphoribosylpyrophosphate in cultured human KB cells. Cancer Res. 1987 Dec 15;47(24 Pt 1):6444-50. [PubMed ]
20. Lachant NA, Zerez CR, Tanaka KR: Pyrimidine nucleotides impair phosphoribosylpyrophosphate (PRPP) synthetase subunit aggregation by sequestering magnesium. A mechanism for the decreased PRPP synthetase activity in hereditary erythrocyte pyrimidine 5'-nucleotidase deficiency. Biochim Biophys Acta. 1989 Jan 19;994(1):81-8. [PubMed ]
21. Wikipedia

1. Nicotinate-nucleotide pyrophosphorylase [carboxylating]
2. Adenine phosphoribosyltransferase
3. Hypoxanthine-guanine phosphoribosyltransferase
4. Ribose-phosphate pyrophosphokinase III
5. Ribose-phosphate pyrophosphokinase II
6. cDNA FLJ78123, highly similar to Homo sapiens phosphoribosyl pyrophosphate amidotransferase
7. Ribose-phosphate pyrophosphokinase 1
8. Pre-B-cell colony enhancing factor 1
9. cDNA FLJ75687, highly similar to Homo sapiens uridine monophosphate synthetase
10. cDNA FLJ77390 (Putative uncharacterized protein RP11-311P8.3)

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. 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. Phosphoribosyl pyrophosphate synthetase III
2. PRS-III
3. Phosphoribosyl pyrophosphate synthetase 1-like 1

MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIDESVRGEDVYIVQSGC
GEINDSLMELLIMINACKIASASRVTAVIPCFPYARQDKKDKSRSPISAKLVANMLSIAG
ADHIITMDLHASQIQGFFDIPVDNLYAEPTVLKWIRENIPEWKNCIIVSPDAGGAKRVTS
IADQLNVDFALIHKERKKANEVDCIVLVGDVNDRVAILVDDMADTCVTICLAADKLLSAG
ATRVYAILTHGIFSGPAISRINTACFEAVVVTNTIPQDEKMKHCSKIRVIDISMILAEAI
RRTHNGESVSYLFSHVPL

• Pentose Pathway (map00030 )
• Purine Metabolism (map00230 )

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

• Pribosyltran (PF00156 )

• None

• None

ACGCCGAATATCAAAATCTTCAGCGGCAGCTCCCACCAGGACTTATCCCAGAAAATTGCT
GACCGCCTGGGCCTGGAGCTAGGCAAGGTGGTGACTAAGAAATTCAGCAACCAGGAGACC
TGCGTGGAAATTGATGAGAGTGTGCGTGGAGAGGATGTCTACATCGTTCAGAGTGGTTGT
GGCGAAATCAACGACAGTCTAATGGAGCTTTTGATCATGATTAATGCCTGCAAGATTGCT
TCAGCTAGCCGAGTTACTGCAGTCATCCCATGCTTCCCTTATGCCCGACAGGATAAGAAG
GATAAGAGCCGGTCCCCAATCTCTGCCAAGCTTGTTGCAAATATGCTCTCTATAGCAGGT
GCGGATCATATCATCACCATGGACCTACATGCTTCTCAAATTCAGGGCTTTTTTGATATC
CCAGTAGACAACTTGTATGCAGAGCCAACTGTCCTGAAGTGGATAAGGGAGAATATCCCT
GAGTGGAAGAACTGCATTATTGTCTCGCCAGATGCTGGTGGAGCTAAAAGAGTGACCTCC
ATTGCAGACCAGTTGAATGTGGACTTTGCTTTGATTCATAAAGAACGGAAGAAGGCCAAT
GAAGTGGACTGCATAGTGCTAGTGGGAGATGTGAATGATCGTGTGGCTATCCTTGTAGAT
GACATGGCAGACACTTGTGTTACAATCTGCCTCGCAGCTGACAAACTTCTCTCAGCTGGA
GCAACCAGAGTTTATGCTATCTTGACTCATGGAATCTTTTCTGGCCCAGCCATTTCTCGC
ATCAACACTGCATGCTTTGAAGCAGTGGTAGTCACCAATACCATACCTCAAGATGAGAAG
ATGAAGCATTGCTCCAAAATACGAGTAATTGACATCTCCATGATCCTTGCAGAAGCCATA
AGGAGAACTCATAATGGGGAATCTGTTTCCTACCTGTTCAGCCATGTTCCTTTATAA

1. Taira M, Iizasa T, Shimada H, Kudoh J, Shimizu N, Tatibana M: A human testis-specific mRNA for phosphoribosylpyrophosphate synthetase that initiates from a non-AUG codon. J Biol Chem. 1990 Sep 25;265(27):16491-7. [PubMed ]

1. Phosphoribosyl pyrophosphate synthetase II
2. PRS-II
3. PPRibP

MPNIVLFSGSSHQDLSQRVADRLGLELGKVVTKKFSNQETSVEIGESVRGEDVYIIQSGC
GEINDNLMELLIMINACKIASSSRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAG
ADHIITMDLHASQIQGFFDIPVDNLYAEPAVLQWIRENIAEWKNCIIVSPDAGGAKRVTS
IADRLNVEFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAG
ATKVYAILTHGIFSGPAISRINNAAFEAVVVTNTIPQEDKMKHCTKIQVIDISMILAEAI
RRTHNGESVSYLFSHVPL

• Pentose Pathway (map00030 )
• Purine Metabolism (map00230 )

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

• Pribosyltran (PF00156 )

• None

• None

ATGCCCAACATCGTGCTGTTCAGCGGCAGCTCGCATCAGGACCTATCCCAGCGCGTGGCC
GACCGCCTGGGCCTGGAGCTGGGCAAGGTGGTCACGAAGAAGTTCAGCAACCAGGAGACC
AGCGTGGAGATTGGTGAAAGCGTGAGAGGGGAAGATGTCTACATCATCCAGAGCGGCTGC
GGGGAAATTAACGACAACCTGATGGAACTCCTCATCATGATCAATGCCTGCAAGATTGCG
TCATCATCCAGAGTAACTGCCGTGATCCCGTGTTTCCCATACGCCCGACAAGATAAAAAG
GACAAGAGTCGTGCCCCAATTTCTGCAAAACTTGTGGCCAATATGCTGTCGGTGGCTGGG
GCGGATCACATCATCACCATGGACCTGCATGCTTCTCAGATACAGGGATTCTTTGATATT
CCTGTGGATAATTTGTATGCGGAGCCCGCAGTCCTGCAGTGGATTCGGGAAAACATTGCC
GAGTGGAAGAACTGTATCATTGTTTCACCTGACGCAGGGGGAGCCAAAAGGGTTACATCA
ATTGCAGACAGGTTGAATGTGGAATTTGCTTTGATCCACAAAGAGAGGAAGAAGGCGAAT
GAAGTGGACCGGATGGTCCTGGTGGGCGACGTGAAGGACCGTGTGGCCATCCTCGTGGAT
GACATGGCTGACACTTGCGGCACCATCTGCCATGCTGCGGACAAGCTGCTGTCAGCTGGA
GCCACCAAAGTGTATGCTATCCTTACCCATGGGATCTTCTCTGGACCAGCTATTTCCAGA
ATAAATAATGCCGCCTTTGAGGCTGTTGTCGTCACAAACACAATTCCGCAAGAGGACAAA
ATGAAACACTGCACCAAGATTCAGGTCATTGACATTTCCATGATCTTGGCCGAAGCAATC
CGAAGGACACACAATGGGGAATCCGTGTCCTACCTGTTCAGCCATGTCCCGCTATAA

1. Iizasa T, Taira M, Shimada H, Ishijima S, Tatibana M: Molecular cloning and sequencing of human cDNA for phosphoribosyl pyrophosphate synthetase subunit II. FEBS Lett. 1989 Feb 13;244(1):47-50. [PubMed ]
2. Iizasa T, Taira M, Shimada H, Tatibana M: Deduced amino acid sequence from human phosphoribosylpyrophosphate synthetase subunit II cDNA. Adv Exp Med Biol. 1989;253A:519-23. [PubMed ]
3. Ishizuka T, Iizasa T, Taira M, Ishijima S, Sonoda T, Shimada H, Nagatake N, Tatibana M: Promoter regions of the human X-linked housekeeping genes PRPS1 and PRPS2 encoding phosphoribosylpyrophosphate synthetase subunit I and II isoforms. Biochim Biophys Acta. 1992 Mar 24;1130(2):139-48. [PubMed ]

1. PPAT, mRNA
2. Phosphoribosyl pyrophosphate amidotransferase, isoform CRA_b

MELEELGIREECGVFGCIASGEWPTQLDVPHVITLGLVGLQHRGQESAGIVTSDGSSVPT
FKSHKGMGLVNHVFTEDNLKKLYVSNLGIGHTRYATTGKCELENCQPFVVETLHGKIAVA
HNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTPPQEQDDTPDWVARIKNLMKEA
PTAYSLLIMHRDVIYAVRDPYGNRPLCIGRLIPVSDINDKEKKTSETEGWVVSSESCSFL
SIGARYYREVLPGEIVEISRHNVQTLDIISRSEGNPVAFCIFEYVYFARPDSMFEDQMVY
TVRYRCGQQLAIEAPVDADLVSTVPESATPAALAYAGKCGLPYVEVLCKNRYVGRTFIQP
NMRLRQLGVAKKFGVLSDNFKGKRIVLVDDSIVRGNTISPIIKLLKESGAKEVHIRVASP
PIKYPCFMGINIPTKEELIANKPEFDHLAEYLGANSVVYLSVEGLVSSVQEGIKFKKQKE
KKHDIMIQENGNGLECFEKSGHCTACLTGKYPVELEW

• None

• None

1. Phosphoribosyl pyrophosphate synthetase I
2. PRS-I
3. PPRibP

MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIGESVRGEDVYIVQSGC
GEINDNLMELLIMINACKIASASRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAG
ADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIRENISEWRNCTIVSPDAGGAKRVTS
IADRLNVDFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAG
ATRVYAILTHGIFSGPAISRINNACFEAVVVTNTIPQEDKMKHCSKIQVIDISMILAEAI
RRTHNGESVSYLFSHVPL

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

• Pribosyltran (PF00156 )

• None

• None

1. Pre-B-cell colony enhancing factor 1, isoform CRA_a
2. cDNA FLJ76475, highly similar to Homo sapiens pre-B-cell colony enhancing factor 1
3. PBEF1, transcript variant 1, mRNA

MNPAAEAEFNILLATDSYKVTHYKQYPPNTSKVYSYFECREKKTENSKLRKVKYEETVFY
GLQYILNKYLKGKVVTKEKIQEAKDVYKEHFQDDVFNEKGWNYILEKYDGHLPIEIKAVP
EGFVIPRGNVLFTVENTDPECYWLTNWIETILVQSWYPITVATNSREQKKILAKYLLETS
GNLDGLEYKLHDFGYRGVSSQETAGIGASAHLVNFKGTDTVAGLALIKKYYGTKDPVPGY
SVPAAEHSTITAWGKDHEKDAFEHIVTQFSSVPVSVVSDSYDIYNACEKIWGEDLRHLIV
SRSTQAPLIIRPDSGNPLDTVLKVLEILGKKFPVTENSKGYKLLPPYLRVIQGDGVDINT
LQEIVEGMKQKMWSIENIAFGSGGGLLQKLTRDLLNCSFKCSYVVTNGLGINVFKDPVAD
PNKRSKKGRLSLHRTPAGNFVTLEEGKGDLEEYGQDLLHTVFKNGKVTKSYSFDEIRKNA
QLNIELEAAHH

• NAPRTase (PF04095 )

• None

• None

1. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed ]

1. orotate phosphoribosyl transferase and orotidine-5'- decarboxylase
2. UMPS, mRNA
3. Uridine monophosphate synthetase
4. Orotate phosphoribosyl transferase and orotidine-5'-decarboxylase, isoform CRA_b

MAVARAALGPLVTGLYDVQAFKFGDFVLKSGLSSPIYIDLRGIVSRPRLLSQVADILFQT
AQNAGISFDTVCGVPYTALPLATVICSTNQIPMLIRRKETKDYGTKRLVEGTINPGETCL
IIEDVVTSGSSVLETVEVLQKEGLKVTDAIVLLDREQGGKDKLQAHGIRLHSVCTLSKML
EILEQQKKVDAETVGRVKRFIQENVFVAANHNGSPLSIKEAPKELSFGARAELPRIHPVA
SKLLRLMQKKETNLCLSADVSLARELLQLADALGPSICMLKTHVDILNDFTLDVMKELIT
LAKCHEFLIFEDRKFADIGNTVKKQYEGGIFKIASWADLVNAHVVPGSGVVKGLQEVGLP
LHRGCLLIAEMSSTGSLATGDYTRAAVRMAEEHSEFVVGFISGSRVSMKPEFLHLTPGVQ
LEAGGDNLGQQYNSPQEVIGKRGSDIIIVGRGIISAADRLEAAEMYRKAAWEAYLSRLGV

• None

• None

MATELQCPDSMPCHNQQVNSASTPSPEQLRPGDLILDHAGGNRASRAKVILLTGYAHSSL
PAELDSGACGGSSLNSEGNSGSGDSSSYDAPAGNSFLEDCELSRQIGAQLKLLPMNDQIR
ELQTIIRDKTASRGDFMFSADRLIRLVVEEGLNQLPYKECMVTTPTGYKYEGVKFEKGNC
GVSIMRSGEAMEQGLRDCCRSIRIGKILIQSDEETQRAKVYYAKFPPDIYRRKVLLMYPI
LSTGNTVIEAVKVLIEHGVQPSVIILLSLFSTPHGAKSIIQEFPEITILTTEVHPVAPTH
FGQKYFGTD

• None

• None

ATGGCCACGGAGTTACAGTGTCCGGACTCCATGCCCTGTCACAACCAGCAAGTAAACTCT
GCCTCAACCCCAAGTCCCGAGCAGCTGCGACCTGGCGATCTGATCCTGGACCACGCAGGG
GGAAACAGAGCCTCCAGGGCCAAGGTGATTCTCCTCACGGGGTACGCCCATTCTAGCCTG
CCGGCCGAGCTGGACTCTGGGGCCTGCGGCGGCTCCAGCCTCAACTCAGAGGGCAACAGT
GGTAGTGGTGACAGTAGCAGCTATGACGCACCAGCTGGCAACTCCTTCCTAGAGGACTGC
GAACTCTCCCGGCAGATCGGGGCGCAGCTTAAGCTGCTGCCTATGAATGATCAGATACGG
GAGCTACAGACCATCATCCGGGACAAGACAGCCAGTAGAGGTGACTTCATGTTTTCTGCG
GATCGTTTGATCAGACTTGTTGTGGAAGAGGGATTGAATCAGCTGCCATATAAAGAATGC
ATGGTGACCACTCCAACAGGGTACAAGTATGAAGGAGTGAAATTTGAGAAGGGAAATTGT
GGGGTCAGCATAATGAGAAGCGGTGAGGCAATGGAACAAGGTTTACGAGACTGCTGTCGA
TCCATACGAATTGGAAAGATCCTGATTCAGAGTGATGAGGAGACACAAAGAGCCAAAGTA
TATTATGCCAAATTCCCCCCAGACATTTACCGGAGAAAAGTCCTTCTGATGTATCCAATT
CTCAGCACTGGAAATACTGTAATTGAAGCTGTAAAGGTTCTTATAGAACATGGAGTTCAA
CCCAGTGTTATCATCCTACTCAGTCTGTTCTCCACTCCTCATGGTGCCAAATCAATCATT
CAGGAGTTTCCAGAGATCACAATTTTAACTACTGAAGTTCATCCTGTTGCACCTACACAT
TTTGGACAGAAATACTTTGGAACAGACTAA