Showing drug card for Dimethyl sulfoxide (DB01093)

• APRD00925
• EXPT01231

• Approved
• Small Molecule

1. Diemthyl sulfoxide
2. Dimethyl sulfoxide BP
3. Dimethyl sulfur oxide
4. Dimethyl sulphoxide
5. Dimethyl sulpoxide
6. Dimexidum
7. Methyl sulfoxide
8. Methylsulfinylmethane
9. Sulfinylbis-methane
10. Sulfinylbismethane
11. Sulfinyldimethane

1. Decap
2. Deltan
3. Demasorb
4. Demavet
5. Demeso
6. Demsodrox
7. Dermasorb
8. Dimexide
9. Dipirartril-tropico
10. Dolicur
11. Doligur
12. Domoso
13. Dromisol
14. Durasorb
15. Gamasol 90
16. Hyadur
17. Infiltrina
18. Kemsol
19. Rimso 50
20. Sclerosol
21. Somipront
22. Syntexan
23. Topsym

1. Synotic Otic Solution (Dimethyl sulfoxide + Fluocinolone acetonide)

• Show PDF

• Analgesics, Non-Narcotic
• Cryoprotective Agents
• Free Radical Scavengers
• Solvents

• G04BX13
• M02AX03

• 40:36.00
• 92:00.00

1. Wikipedia
2. RxList
3. PDRhealth

• Humans and other mammals

1. Plasminogen activator inhibitor 1
2. Dihydrofolate reductase
3. Transthyretin
4. Aldo-keto reductase family 1 member C3
5. DNA
6. FK506-binding protein 1A
7. Cationic trypsin
8. Triosephosphate isomerase, glycosomal
9. Alcohol dehydrogenase E chain
10. Bacillolysin
11. Peptidyl-prolyl cis-trans isomerase, mitochondrial
12. Beta-galactosidase
13. Oxygen-insensitive NAD(P)H nitroreductase
14. Regulatory protein E2
15. Thermonuclease
16. Gag-Pol polyprotein
17. Dimethyl sulfoxide/trimethylamine N-oxide reductase
18. Triosephosphate isomerase
19. Polynucleotide kinase
20. FK506-binding protein 4

1. Endothelial plasminogen activator inhibitor
2. PAI
3. PAI-1
4. Plasminogen activator inhibitor 1 precursor

MQMSPALTCLVLGLALVFGEGSAVHHPPSYVAHLASDFGVRVFQQVAQASKDRNVVFSPY
GVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAPALRHLYKELMGPWNKDEISTTDAI
FVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAV
DQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPD
GHYYDILELPYHGDTLSMFIAAPYEKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPK
FSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQKVKIEVNESGTVASS
STAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP

• Serpin (PF00079 )

• 1-23

• None

• Secreted protein

ATGCAGATGTCTCCAGCCCTCACCTGCCTAGTCCTGGGCCTGGCCCTTGTCTTTGGTGAA
GGGTCTGCTGTGCACCATCCCCCATCCTACGTGGCCCACCTGGCCTCAGACTTCGGGGTG
AGGGTGTTTCAGCAGGTGGCGCAGGCCTCCAAGGACCGCAACGTGGTTTTCTCACCCTAT
GGGGTGGCCTCGGTGTTGGCCATGCTCCAGCTGACAACAGGAGGAGAAACCCAGCAGCAG
ATTCAAGCAGCTATGGGATTCAAGATTGATGACAAGGGCATGGCCCCCGCCCTCCGGCAT
CTGTACAAGGAGCTCATGGGGCCATGGAACAAGGACGAGATCAGCACCACAGACGCGATC
TTCGTCCAGCGGGATCTGAAGCTGGTCCAGGGCTTCATGCCCCACTTCTTCAGGCTGTTC
CGGAGCACGGTCAAGCAAGTGGACTTTTCAGAGGTGGAGAGAGCCAGATTCATCATCAAT
GACTGGGTGAAGACACACACAAAAGGTATGATCAGCAACTTGCTTGGGAAAGGAGCCGTG
GACCAGCTGACACGGCTGGTGCTGGTGAATGCCCTCTACTTCAACGGCCAGTGGAAGACT
CCCTTCCCCGACTCCAGCACCCACCGCCGCCTCTTCCACAAATCAGACGGCAGCACTGTC
TCTGTGCCCATGATGGCTCAGACCAACAAGTTCAACTATACTGAGTTCACCACGCCCGAT
GGCCATTACTACGACATCCTGGAACTGCCCTACCACGGGGACACCCTCAGCATGTTCATT
GCTGCCCCTTATGAAAAAGAGGTGCCTCTCTCTGCCCTCACCAACATTCTGAGTGCCCAG
CTCATCAGCCACTGGAAAGGCAACATGACCAGGCTGCCCCGCCTCCTGGTTCTGCCCAAG
TTCTCCCTGGAGACTGAAGTCGACCTCAGGAAGCCCCTAGAGAACCTGGGAATGACCGAC
ATGTTCAGACAGTTTCAGGCTGACTTCACGAGTCTTTCAGACCAAGAGCCTCTCCACGTC
GCGCAGGCGCTGCAGAAAGTGAAGATCGAGGTGAACGAGAGTGGCACGGTGGCCTCCTCA
TCCACAGCTGTCATAGTCTCAGCCCGCATGGCCCCCGAGGAGATCATCATGGACAGACCC
TTCCTCTTTGTGGTCCGGCACAACCCCACAGGAACAGTCCTTTTCATGGGCCAAGTGATG
GAACCCTGA

1. Sharp AM, Stein PE, Pannu NS, Carrell RW, Berkenpas MB, Ginsburg D, Lawrence DA, Read RJ: The active conformation of plasminogen activator inhibitor 1, a target for drugs to control fibrinolysis and cell adhesion. Structure. 1999 Feb 15;7(2):111-8. [PubMed ]
2. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed ]
3. Nar H, Bauer M, Stassen JM, Lang D, Gils A, Declerck PJ: Plasminogen activator inhibitor 1. Structure of the native serpin, comparison to its other conformers and implications for serpin inactivation. J Mol Biol. 2000 Mar 31;297(3):683-95. [PubMed ]
4. Liu CX, Li Y, Obermoeller-McCormick LM, Schwartz AL, Bu G: The putative tumor suppressor LRP1B, a novel member of the low density lipoprotein (LDL) receptor family, exhibits both overlapping and distinct properties with the LDL receptor-related protein. J Biol Chem. 2001 Aug 3;276(31):28889-96. Epub 2001 May 30. [PubMed ]
5. 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 ]
6. Mottonen J, Strand A, Symersky J, Sweet RM, Danley DE, Geoghegan KF, Gerard RD, Goldsmith EJ: Structural basis of latency in plasminogen activator inhibitor-1. Nature. 1992 Jan 16;355(6357):270-3. [PubMed ]
7. Pannekoek H, Veerman H, Lambers H, Diergaarde P, Verweij CL, van Zonneveld AJ, van Mourik JA: Endothelial plasminogen activator inhibitor (PAI): a new member of the Serpin gene family. EMBO J. 1986 Oct;5(10):2539-44. [PubMed ]
8. Follo M, Ginsburg D: Structure and expression of the human gene encoding plasminogen activator inhibitor, PAI-1. Gene. 1989 Dec 14;84(2):447-53. [PubMed ]
9. Loskutoff DJ, Linders M, Keijer J, Veerman H, van Heerikhuizen H, Pannekoek H: Structure of the human plasminogen activator inhibitor 1 gene: nonrandom distribution of introns. Biochemistry. 1987 Jun 30;26(13):3763-8. [PubMed ]
10. Andreasen PA, Riccio A, Welinder KG, Douglas R, Sartorio R, Nielsen LS, Oppenheimer C, Blasi F, Dano K: Plasminogen activator inhibitor type-1: reactive center and amino-terminal heterogeneity determined by protein and cDNA sequencing. FEBS Lett. 1986 Dec 15;209(2):213-8. [PubMed ]
11. 3026837 Wun TC, Kretzmer KK: cDNA cloning and expression in E. coli of a plasminogen activator inhibitor (PAI) related to a PAI produced by Hep G2 hepatoma cell. FEBS Lett. 1987 Jan 1;210(1):11-6.
12. 3092219 Ny T, Sawdey M, Lawrence D, Millan JL, Loskutoff DJ: Cloning and sequence of a cDNA coding for the human beta-migrating endothelial-cell-type plasminogen activator inhibitor. Proc Natl Acad Sci U S A. 1986 Sep;83(18):6776-80.
13. 3097076 Ginsburg D, Zeheb R, Yang AY, Rafferty UM, Andreasen PA, Nielsen L, Dano K, Lebo RV, Gelehrter TD: cDNA cloning of human plasminogen activator-inhibitor from endothelial cells. J Clin Invest. 1986 Dec;78(6):1673-80.
14. 3132455 Bosma PJ, van den Berg EA, Kooistra T, Siemieniak DR, Slightom JL: Human plasminogen activator inhibitor-1 gene. Promoter and structural gene nucleotide sequences. J Biol Chem. 1988 Jul 5;263(19):9129-41.
15. 3262512 Strandberg L, Lawrence D, Ny T: The organization of the human-plasminogen-activator-inhibitor-1 gene. Implications on the evolution of the serine-protease inhibitor family. Eur J Biochem. 1988 Oct 1;176(3):609-16.
16. 7522053 Sigurdardottir O, Wiman B: Identification of a PAI-1 binding site in vitronectin. Biochim Biophys Acta. 1994 Sep 21;1208(1):104-10.
17. 7552714 Aertgeerts K, De Bondt HL, De Ranter CJ, Declerck PJ: Mechanisms contributing to the conformational and functional flexibility of plasminogen activator inhibitor-1. Nat Struct Biol. 1995 Oct;2(10):891-7.
18. 9194591 Turkmen B, Schmitt M, Schmalfeldt B, Trommler P, Hell W, Creutzburg S, Graeff H, Magdolen V: Mutational analysis of the genes encoding urokinase-type plasminogen activator (uPA) and its inhibitor PAI-1 in advanced ovarian cancer. Electrophoresis. 1997 May;18(5):686-9.
19. 9634700 Xue Y, Bjorquist P, Inghardt T, Linschoten M, Musil D, Sjolin L, Deinum J: Interfering with the inhibitory mechanism of serpins: crystal structure of a complex formed between cleaved plasminogen activator inhibitor type 1 and a reactive-centre loop peptide. Structure. 1998 May 15;6(5):627-36.

1. Camici GG, Steffel J, Akhmedov A, Schafer N, Baldinger J, Schulz U, Shojaati K, Matter CM, Yang Z, Luscher TF, Tanner FC: Dimethyl sulfoxide inhibits tissue factor expression, thrombus formation, and vascular smooth muscle cell activation: a potential treatment strategy for drug-eluting stents. Circulation. 2006 Oct 3;114(14):1512-21. Epub 2006 Sep 25. [PubMed ]

1. EC 1.5.1.3

VGSLNCIVAVSQNMGIGKNGDLPWPPLRNEFRYFQRMTTTSSVEGKQNLVIMGKKTWFSI
PEKNRPLKGRINLVLSRELKEPPQGAHFLSRSLDDALKLTEQPELANKVDMVWIVGGSSV
YKEAMNHPGHLKLFVTRIMQDFESDTFFPEIDLEKYKLLPEYPGVLSDVQEEKGIKYKFE
VYEKND

• 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+

• DHFR_1 (PF00186 )

• None

• None

ATGGTTGGTTCGCTAAACTGCATCGTCGCTGTGTCCCAGAACATGGGCATCGGCAAGAAC
GGGGACCTGCCCTGGCCACCGCTCAGGAATGAATTCAGATATTTCCAGAGAATGACCACA
ACCTCTTCAGTAGAAGGTAAACAGAATCTGGTGATTATGGGTAAGAAGACCTGGTTCTCC
ATTCCTGAGAAGAATCGACCTTTAAAGGGTAGAATTAATTTAGTTCTCAGCAGAGAACTC
AAGGAACCTCCACAAGGAGCTCATTTTCTTTCCAGAAGTCTAGATGATGCCTTAAAACTT
ACTGAACAACCAGAATTAGCAAATAAAGTAGACATGGTCTGGATAGTTGGTGGCAGTTCT
GTTTATAAGGAAGCCATGAATCACCCAGGCCATCTTAAACTATTTGTGACAAGGATCATG
CAAGACTTTGAAAGTGACACGTTTTTTCCAGAAATTGATTTGGAGAAATATAAACTTCTG
CCAGAATACCCAGGTGTTCTCTCTGATGTCCAGGAGGAGAAAGGCATTAAGTACAAATTT
GAAGTATATGAGAAGAATGATTAA

1. Stockman BJ, Nirmala NR, Wagner G, Delcamp TJ, DeYarman MT, Freisheim JH: Sequence-specific 1H and 15N resonance assignments for human dihydrofolate reductase in solution. Biochemistry. 1992 Jan 14;31(1):218-29. [PubMed ]
2. Davies JF 2nd, Delcamp TJ, Prendergast NJ, Ashford VA, Freisheim JH, Kraut J: Crystal structures of recombinant human dihydrofolate reductase complexed with folate and 5-deazafolate. Biochemistry. 1990 Oct 9;29(40):9467-79. [PubMed ]
3. Oefner C, D'Arcy A, Winkler FK: Crystal structure of human dihydrofolate reductase complexed with folate. Eur J Biochem. 1988 Jun 1;174(2):377-85. [PubMed ]
4. Yang JK, Masters JN, Attardi G: Human dihydrofolate reductase gene organization. Extensive conservation of the G + C-rich 5' non-coding sequence and strong intron size divergence from homologous mammalian genes. J Mol Biol. 1984 Jun 25;176(2):169-87. [PubMed ]
5. Chen MJ, Shimada T, Moulton AD, Cline A, Humphries RK, Maizel J, Nienhuis AW: The functional human dihydrofolate reductase gene. J Biol Chem. 1984 Mar 25;259(6):3933-43. [PubMed ]
6. Masters JN, Attardi G: The nucleotide sequence of the cDNA coding for the human dihydrofolic acid reductase. Gene. 1983 Jan-Feb;21(1-2):59-63. [PubMed ]
7. Cody V, Galitsky N, Luft JR, Pangborn W, Rosowsky A, Blakley RL: Comparison of two independent crystal structures of human dihydrofolate reductase ternary complexes reduced with nicotinamide adenine dinucleotide phosphate and the very tight-binding inhibitor PT523. Biochemistry. 1997 Nov 11;36(45):13897-903. [PubMed ]

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

1. ATTR
2. Prealbumin
3. TBPA
4. TTR
5. Transthyretin precursor

MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDT
WEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDS
GPRRYTIAALLSPYSYSTTAVVTNPKE

• Transthyretin (PF00576 )

• 1-20

• None

• Secreted protein

ATGGCTTCTCATCGTCTGCTCCTCCTCTGCCTTGCTGGACTGGTATTTGTGTCTGAGGCT
GGCCCTACGGGCACCGGTGAATCCAAGTGTCCTCTGATGGTCAAAGTTCTAGATGCTGTC
CGAGGCAGTCCTGCCATCAATGTGGCCGTGCATGTGTTCAGAAAGGCTGCTGATGACACC
TGGGAGCCATTTGCCTCTGGGAAAACCAGTGAGTCTGGAGAGCTGCATGGGCTCACAACT
GAGGAGGAATTTGTAGAAGGGATATACAAAGTGGAAATAGACACCAAATCTTACTGGAAG
GCACTTGGCATCTCCCCATTCCATGAGCATGCAGAGGTGGTATTCACAGCCAACGACTCC
GGCCCCCGCCGCTACACCATTGCCGCCCTGCTGAGCCCCTACTCCTATTCCACCACGGCT
GTCGTCACCAATCCCAAGGAATGA

1. Naylor HM, Newcomer ME: The structure of human retinol-binding protein (RBP) with its carrier protein transthyretin reveals an interaction with the carboxy terminus of RBP. Biochemistry. 1999 Mar 2;38(9):2647-53. [PubMed ]
2. Klabunde T, Petrassi HM, Oza VB, Raman P, Kelly JW, Sacchettini JC: Rational design of potent human transthyretin amyloid disease inhibitors. Nat Struct Biol. 2000 Apr;7(4):312-21. [PubMed ]
3. Nakamura M, Hamidi Asl K, Benson MD: A novel variant of transthyretin (Glu89Lys) associated with familial amyloidotic polyneuropathy. Amyloid. 2000 Mar;7(1):46-50. [PubMed ]
4. de Carvalho M, Moreira P, Evangelista T, Ducla-Soares JL, Bento M, Fernandes R, Saraiva MJ: New transthyretin mutation V28M in a Portuguese kindred with amyloid polyneuropathy. Muscle Nerve. 2000 Jul;23(7):1016-21. [PubMed ]
5. 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 ]
6. Blevins G, Macaulay R, Harder S, Fladeland D, Yamashita T, Yazaki M, Hamidi Asl K, Benson MD, Donat JR: Oculoleptomeningeal amyloidosis in a large kindred with a new transthyretin variant Tyr69His. Neurology. 2003 May 27;60(10):1625-30. [PubMed ]
7. Almeida MR, Ferlini A, Forabosco A, Gawinowicz M, Costa PP, Salvi F, Plasmati R, Tassinari CA, Altland K, Saraiva MJ: Two transthyretin variants (TTR Ala-49 and TTR Gln-89) in two Sicilian kindreds with hereditary amyloidosis. Hum Mutat. 1992;1(3):211-5. [PubMed ]
8. Jacobson DR, McFarlin DE, Kane I, Buxbaum JN: Transthyretin Pro55, a variant associated with early-onset, aggressive, diffuse amyloidosis with cardiac and neurologic involvement. Hum Genet. 1992 May;89(3):353-6. [PubMed ]
9. Uemichi T, Murrell JR, Zeldenrust S, Benson MD: A new mutant transthyretin (Arg 10) associated with familial amyloid polyneuropathy. J Med Genet. 1992 Dec;29(12):888-91. [PubMed ]
10. Izumoto S, Younger D, Hays AP, Martone RL, Smith RT, Herbert J: Familial amyloidotic polyneuropathy presenting with carpal tunnel syndrome and a new transthyretin mutation, asparagine 70. Neurology. 1992 Nov;42(11):2094-102. [PubMed ]
11. 1517749 Kametani F, Ikeda S, Yanagisawa N, Ishi T, Hanyu N: Characterization of a transthyretin-related amyloid fibril protein from cerebral amyloid angiopathy in type I familial amyloid polyneuropathy. J Neurol Sci. 1992 Apr;108(2):178-83.
12. 1520326 Murakami T, Atsumi T, Maeda S, Tanase S, Ishikawa K, Mita S, Kumamoto T, Araki S, Ando M: A novel transthyretin mutation at position 30 (Leu for Val) associated with familial amyloidotic polyneuropathy. Biochem Biophys Res Commun. 1992 Aug 31;187(1):397-403.
13. 1520336 Nishi H, Kimura A, Harada H, Hayashi Y, Nakamura M, Sasazuki T: Novel variant transthyretin gene (Ser50 to Ile) in familial cardiac amyloidosis. Biochem Biophys Res Commun. 1992 Aug 31;187(1):460-6.
14. 1544214 Jones LA, Skare JC, Cohen AS, Harding JA, Milunsky A, Skinner M: Familial amyloidotic polyneuropathy: a new transthyretin position 30 mutation (alanine for valine) in a family of German descent. Clin Genet. 1992 Feb;41(2):70-3.
15. 1570831 Saraiva MJ, Almeida Mdo R, Sherman W, Gawinowicz M, Costa P, Costa PP, Goodman DS: A new transthyretin mutation associated with amyloid cardiomyopathy. Am J Hum Genet. 1992 May;50(5):1027-30.
16. 1656975 Saeki Y, Ueno S, Yorifuji S, Sugiyama Y, Ide Y, Matsuzawa Y: New mutant gene (transthyretin Arg 58) in cases with hereditary polyneuropathy detected by non-isotope method of single-strand conformation polymorphism analysis. Biochem Biophys Res Commun. 1991 Oct 15;180(1):380-5.
17. 1666289 Gu JR, Jiang HQ, He LP, Li DZ, Zhou XM, Dai WL, Qian LF, Chen YQ, Schweinfest C, Papas T: Transthyretin (prealbumin) gene in human primary hepatic cancer. Sci China B. 1991 Nov;34(11):1312-8.
18. 1734866 Murakami T, Maeda S, Yi S, Ikegawa S, Kawashima E, Onodera S, Shimada K, Araki S: A novel transthyretin mutation associated with familial amyloidotic polyneuropathy. Biochem Biophys Res Commun. 1992 Jan 31;182(2):520-6.
19. 1877623 Harrison HH, Gordon ED, Nichols WC, Benson MD: Biochemical and clinical characterization of prealbuminCHICAGO: an apparently benign variant of serum prealbumin (transthyretin) discovered with high-resolution two-dimensional electrophoresis. Am J Med Genet. 1991 Jun 15;39(4):442-52.
20. 1932142 Harding J, Skare J, Skinner M: A second transthyretin mutation at position 33 (Leu/Phe) associated with familial amyloidotic polyneuropathy. Biochim Biophys Acta. 1991 Oct 21;1097(3):183-6.
21. 1979335 Moses AC, Rosen HN, Moller DE, Tsuzaki S, Haddow JE, Lawlor J, Liepnieks JJ, Nichols WC, Benson MD: A point mutation in transthyretin increases affinity for thyroxine and produces euthyroid hyperthyroxinemia. J Clin Invest. 1990 Dec;86(6):2025-33.
22. 1997217 Skare JC, Milunsky JM, Milunsky A, Skare IB, Cohen AS, Skinner M: A new transthyretin variant from a patient with familial amyloidotic polyneuropathy has asparagine substituted for histidine at position 90. Clin Genet. 1991 Jan;39(1):6-12.
23. 2015890 Christmanson L, Betsholtz C, Gustavsson A, Johansson B, Sletten K, Westermark P: The transthyretin cDNA sequence is normal in transthyretin-derived senile systemic amyloidosis. FEBS Lett. 1991 Apr 9;281(1-2):177-80.
24. 201845 Blake CC, Oatley SJ: Protein-DNA and protein-hormone interactions in prealbumin: a model of the thyroid hormone nuclear receptor? Nature. 1977 Jul 14;268(5616):115-20.
25. 2046936 Ii S, Minnerath S, Ii K, Dyck PJ, Sommer SS: Two-tiered DNA-based diagnosis of transthyretin amyloidosis reveals two novel point mutations. Neurology. 1991 Jun;41(6):893-8.
26. 2161654 Ueno S, Uemichi T, Yorifuji S, Tarui S: A novel variant of transthyretin (Tyr114 to Cys) deduced from the nucleotide sequences of gene fragments from familial amyloidotic polyneuropathy in Japanese sibling cases. Biochem Biophys Res Commun. 1990 May 31;169(1):143-7.
27. 2363717 Ueno S, Uemichi T, Takahashi N, Soga F, Yorifuji S, Tarui S: Two novel variants of transthyretin identified in Japanese cases with familial amyloidotic polyneuropathy: transthyretin (Glu42 to Gly) and transthyretin (Ser50 to Arg). Biochem Biophys Res Commun. 1990 Jun 29;169(3):1117-21.
28. 2891727 Wallace MR, Dwulet FE, Williams EC, Conneally PM, Benson MD: Identification of a new hereditary amyloidosis prealbumin variant, Tyr-77, and detection of the gene by DNA analysis. J Clin Invest. 1988 Jan;81(1):189-93.
29. 2990465 Wallace MR, Naylor SL, Kluve-Beckerman B, Long GL, McDonald L, Shows TB, Benson MD: Localization of the human prealbumin gene to chromosome 18. Biochem Biophys Res Commun. 1985 Jun 28;129(3):753-8.
30. 2995367 Tsuzuki T, Mita S, Maeda S, Araki S, Shimada K: Structure of the human prealbumin gene. J Biol Chem. 1985 Oct 5;260(22):12224-7.
31. 3022108 Maeda S, Mita S, Araki S, Shimada K: Structure and expression of the mutant prealbumin gene associated with familial amyloidotic polyneuropathy. Mol Biol Med. 1986 Aug;3(4):329-38.
32. 3135807 Cornwell GG 3rd, Sletten K, Johansson B, Westermark P: Evidence that the amyloid fibril protein in senile systemic amyloidosis is derived from normal prealbumin. Biochem Biophys Res Commun. 1988 Jul 29;154(2):648-53.
33. 3675594 Strahler JR, Rosenblum BB, Hanash SM: Identification and characterization of a human transthyretin variant. Biochem Biophys Res Commun. 1987 Oct 14;148(1):471-7.
34. 3722385 Wallace MR, Dwulet FE, Conneally PM, Benson MD: Biochemical and molecular genetic characterization of a new variant prealbumin associated with hereditary amyloidosis. J Clin Invest. 1986 Jul;78(1):6-12.
35. 3818577 Mita S, Maeda S, Shimada K, Araki S: Analyses of prealbumin mRNAs in individuals with familial amyloidotic polyneuropathy. J Biochem (Tokyo). 1986 Nov;100(5):1215-22.
36. 4044580 Soprano DR, Herbert J, Soprano KJ, Schon EA, Goodman DS: Demonstration of transthyretin mRNA in the brain and other extrahepatic tissues in the rat. J Biol Chem. 1985 Sep 25;260(21):11793-8.
37. 4054629 Sasaki H, Yoshioka N, Takagi Y, Sakaki Y: Structure of the chromosomal gene for human serum prealbumin. Gene. 1985;37(1-3):191-7.
38. 4216640 Blake CC, Geisow MJ, Swan ID, Rerat C, Rerat B: Strjcture of human plasma prealbumin at 2-5 A resolution. A preliminary report on the polypeptide chain conformation, quaternary structure and thyroxine binding. J Mol Biol. 1974 Sep 5;88(1):1-12.
39. 4607556 Kanda Y, Goodman DS, Canfield RE, Morgan FJ: The amino acid sequence of human plasma prealbumin. J Biol Chem. 1974 Nov 10;249(21):6796-805.
40. 6093805 Mita S, Maeda S, Shimada K, Araki S: Cloning and sequence analysis of cDNA for human prealbumin. Biochem Biophys Res Commun. 1984 Oct 30;124(2):558-64.
41. 6300852 Pras M, Prelli F, Franklin EC, Frangione B: Primary structure of an amyloid prealbumin variant in familial polyneuropathy of Jewish origin. Proc Natl Acad Sci U S A. 1983 Jan;80(2):539-42.
42. 6487335 Nakazato M, Kangawa K, Minamino N, Tawara S, Matsuo H, Araki S: Revised analysis of amino acid replacement in a prealbumin variant (SKO-III) associated with familial amyloidotic polyneuropathy of Jewish origin. Biochem Biophys Res Commun. 1984 Sep 28;123(3):921-8.
43. 6583672 Dwulet FE, Benson MD: Primary structure of an amyloid prealbumin and its plasma precursor in a heredofamilial polyneuropathy of Swedish origin. Proc Natl Acad Sci U S A. 1984 Feb;81(3):694-8.
44. 6651852 Tawara S, Nakazato M, Kangawa K, Matsuo H, Araki S: Identification of amyloid prealbumin variant in familial amyloidotic polyneuropathy (Japanese type). Biochem Biophys Res Commun. 1983 Nov 15;116(3):880-8.
45. 671542 Blake CC, Geisow MJ, Oatley SJ, Rerat B, Rerat C: Structure of prealbumin: secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 A. J Mol Biol. 1978 May 25;121(3):339-56.
46. 7474944 Gustavsson A, Jahr H, Tobiassen R, Jacobson DR, Sletten K, Westermark P: Amyloid fibril composition and transthyretin gene structure in senile systemic amyloidosis. Lab Invest. 1995 Nov;73(5):703-8.
47. 7599630 Saraiva MJ: Transthyretin mutations in health and disease. Hum Mutat. 1995;5(3):191-6.
48. 7754382 Monaco HL, Rizzi M, Coda A: Structure of a complex of two plasma proteins: transthyretin and retinol-binding protein. Science. 1995 May 19;268(5213):1039-41.
49. 7850982 Booth DR, Tan SY, Hawkins PN, Pepys MB, Frustaci A: A novel variant of transthyretin, 59Thr-->Lys, associated with autosomal dominant cardiac amyloidosis in an Italian family. Circulation. 1995 Feb 15;91(4):962-7.
50. 7910950 Yamamoto K, Hsu SP, Yoshida K, Ikeda S, Nakazato M, Shiomi K, Cheng SY, Furihata K, Ueno I, Yanagisawa N: Familial amyloid polyneuropathy in Taiwan: identification of transthyretin variant (Leu55-->Pro). Muscle Nerve. 1994 Jun;17(6):637-41.
51. 7914929 Uemichi T, Gertz MA, Benson MD: Amyloid polyneuropathy in two German-American families: a new transthyretin variant (Val 107). J Med Genet. 1994 May;31(5):416-7.
52. 7923855 Skare J, Jones LA, Myles N, Kane K, Milunsky A, Cohen A, Skinner M: Two transthyretin mutations (glu42gly, his90asn) in an Italian family with amyloidosis. Clin Genet. 1994 Jun;45(6):281-4.
53. 8019560 Jacobson DR, Buxbaum JN: A double-variant transthyretin allele (Ser 6, Ile 33) in the Israeli patient "SKO" with familial amyloidotic polyneuropathy. Hum Mutat. 1994;3(3):254-60.
54. 8038017 Hesse A, Altland K, Linke RP, Almeida MR, Saraiva MJ, Steinmetz A, Maisch B: Cardiac amyloidosis: a review and report of a new transthyretin (prealbumin) variant. Br Heart J. 1993 Aug;70(2):111-5.
55. 8081397 Jacobson DR, Gertz MA, Buxbaum JN: Transthyretin VAL107, a new variant associated with familial cardiac and neuropathic amyloidosis. Hum Mutat. 1994;3(4):399-401.
56. 8089102 Berni R, Malpeli G, Folli C, Murrell JR, Liepnieks JJ, Benson MD: The Ile-84-->Ser amino acid substitution in transthyretin interferes with the interaction with plasma retinol-binding protein. J Biol Chem. 1994 Sep 23;269(38):23395-8.
57. 8095302 Benson MD 2nd, Turpin JC, Lucotte G, Zeldenrust S, LeChevalier B, Benson MD: A transthyretin variant (alanine 71) associated with familial amyloidotic polyneuropathy in a French family. J Med Genet. 1993 Feb;30(2):120-2.
58. 8133316 Yasuda T, Sobue G, Doyu M, Nakazato M, Shiomi K, Yanagi T, Mitsuma T: Familial amyloidotic polyneuropathy with late-onset and well-preserved autonomic function: a Japanese kindred with novel mutant transthyretin (Ala97 to Gly). J Neurol Sci. 1994 Jan;121(1):97-102.
59. 8257997 Almeida Mdo R, Lopez-Andreu F, Munar-Ques M, Costa PP, Saraiva MJ: Transthyretin ALA 71: a new transthyretin variant in a Spanish family with familial amyloidotic polyneuropathy. Hum Mutat. 1993;2(5):420-1.
60. 8309582 Murakami T, Tachibana S, Endo Y, Kawai R, Hara M, Tanase S, Ando M: Familial carpal tunnel syndrome due to amyloidogenic transthyretin His 114 variant. Neurology. 1994 Feb;44(2):315-8.
61. 8352764 Shiomi K, Nakazato M, Matsukura S, Ohnishi A, Hatanaka H, Tsuji S, Murai Y, Kojima M, Kangawa K, Matsuo H: A basic transthyretin variant (Glu61-->Lys) causes familial amyloidotic polyneuropathy: protein and DNA sequencing and PCR-induced mutation restriction analysis. Biochem Biophys Res Commun. 1993 Aug 16;194(3):1090-6.
62. 8382610 Terry CJ, Damas AM, Oliveira P, Saraiva MJ, Alves IL, Costa PP, Matias PM, Sakaki Y, Blake CC: Structure of Met30 variant of transthyretin and its amyloidogenic implications. EMBO J. 1993 Feb;12(2):735-41.
63. 8428915 Hamilton JA, Steinrauf LK, Braden BC, Liepnieks J, Benson MD, Holmgren G, Sandgren O, Steen L: The x-ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val-30-->Met variant to 1.7-A resolution. J Biol Chem. 1993 Feb 5;268(4):2416-24.
64. 8579098 Vidal R, Garzuly F, Budka H, Lalowski M, Linke RP, Brittig F, Frangione B, Wisniewski T: Meningocerebrovascular amyloidosis associated with a novel transthyretin mis-sense mutation at codon 18 (TTRD 18G) Am J Pathol. 1996 Feb;148(2):361-6.
65. 8990019 Jacobson DR, Pan T, Kyle RA, Buxbaum JN: Transthyretin ILE20, a new variant associated with late-onset cardiac amyloidosis. Hum Mutat. 1997;9(1):83-5.
66. 9789022 Peterson SA, Klabunde T, Lashuel HA, Purkey H, Sacchettini JC, Kelly JW: Inhibiting transthyretin conformational changes that lead to amyloid fibril formation. Proc Natl Acad Sci U S A. 1998 Oct 27;95(22):12956-60.
67. 9818054 Schormann N, Murrell JR, Benson MD: Tertiary structures of amyloidogenic and non-amyloidogenic transthyretin variants: new model for amyloid fibril formation. Amyloid. 1998 Sep;5(3):175-87.

1. Lehigh Shirey EA, Jelaso Langerveld A, Mihalko D, Ide CF: Polychlorinated biphenyl exposure delays metamorphosis and alters thyroid hormone system gene expression in developing Xenopus laevis. Environ Res. 2006 Oct;102(2):205-14. Epub 2006 May 23. [PubMed ]

1. 17-beta-HSD 5
2. 17-beta-hydroxysteroid dehydrogenase type 5
3. 3-alpha- hydroxysteroid dehydrogenase type 2
4. 3-alpha-HSD type 2
5. 3-alpha-HSD type II, brain
6. Chlordecone reductase homolog HAKRb
7. DD-3
8. DD3
9. Dihydrodiol dehydrogenase 3
10. Dihydrodiol dehydrogenase type I
11. EC 1.-.-.-
12. EC 1.1.1.188
13. EC 1.1.1.213
14. EC 1.1.1.62
15. EC 1.3.1.20
16. Estradiol 17-beta-dehydrogenase
17. HA1753
18. PGFS
19. Prostaglandin F synthase
20. Trans-1,2- dihydrobenzene-1,2-diol dehydrogenase

MDSKQQCVKLNDGHFMPVLGFGTYAPPEVPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQ
VGLAIRSKIADGSVKREDIFYTSKLWSTFHRPELVRPALENSLKKAQLDYVDLYLIHSPM
SLKPGEELSPTDENGKVIFDIVDLCTTWEAMEKCKDAGLAKSIGVSNFNRRQLEMILNKP
GLKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRDKRWVDPNSPVLLEDPV
LCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLD
RNLHYFNSDSFASHPNYPYSDEY

• estradiol-17beta + NAD(P)+ = estrone + NAD(P)H + H+

• Aldo_ket_red (PF00248 )

• None

• None

• Cytoplasm

ATGGATTCCAAACAGCAGTGTGTAAAGCTAAATGATGGCCACTTCATGCCTGTATTGGGA
TTTGGCACCTATGCACCTCCAGAGGTTCCGAGAAGTAAAGCTTTGGAGGTCACAAAATTA
GCAATAGAAGCTGGGTTCCGCCATATAGATTCTGCTCATTTATACAATAATGAGGAGCAG
GTTGGACTGGCCATCCGAAGCAAGATTGCAGATGGCAGTGTTGAGAGAGAAGACATATTC
TACACTTCAAAGCTTTGGTCCACTTTTCATCGACCAGAGTTGGTCCGACCAGCCTTGGAA
AACTCACTGAAGAAAGCTCAATTGGACTATGTTGACCTCTATCTTATTCATTCTCCAATG
TCTCTAAAGCCAGGTGAGGAACTTTCACCAACAGATGAAAATGGAAAAGTAATATTTGAC
ATAGTGGATCTCTGTACCACCTGGGAGGCCATGGAGAAGTGTAAGGATGCAGGATTGGCC
AAGTCCATTGGGGTATCAAACTTCAACCGCAGGCAGCTGGAGATCATCCTCAACAAGCCA
GGACTCAAGTACAAGCCTGTCTGCAACCAGGTAGAATGTCATCCGTATTTCAACCGGAGT
AAATTGCTAGATTTCTGCAAGTCGAAAGATATTGTTCTGGTTGCCTATAGTGCTCTGGGA
TCTCAACGAGACAAACGATGGGTGGACCCGAACTCCCCGGTCCTCTTGGAGGACCCAGTC
CTTTGTGCCTTGGCAAAAAAGCACAAGCGAACCCCAGCCCTGATTGCCCTGCGCTACCAG
CTGCAGCGTGGGGTTGTGGTCCTGGCCAAGAGCTACAATGAGCAGCGCATCAGACAGAAC
GTGCAGGTTTTTGAGTTCCAGTTGACTGCAGAGGACATGAAAGCCATAGATGGCCTAGAC
AGAAATCTCCACTATTTTAACAGTGATAGTTTTGCTAGCCACCCTAATTATCCATATTCA
GATGAATATTAA

1. Griffin LD, Mellon SH: Selective serotonin reuptake inhibitors directly alter activity of neurosteroidogenic enzymes. Proc Natl Acad Sci U S A. 1999 Nov 9;96(23):13512-7. [PubMed ]
2. Suzuki-Yamamoto T, Nishizawa M, Fukui M, Okuda-Ashitaka E, Nakajima T, Ito S, Watanabe K: cDNA cloning, expression and characterization of human prostaglandin F synthase. FEBS Lett. 1999 Dec 3;462(3):335-40. [PubMed ]
3. Nishizawa M, Nakajima T, Yasuda K, Kanzaki H, Sasaguri Y, Watanabe K, Ito S: Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes. Genes Cells. 2000 Feb;5(2):111-25. [PubMed ]
4. Penning TM, Burczynski ME, Jez JM, Lin HK, Ma H, Moore M, Ratnam K, Palackal N: Structure-function aspects and inhibitor design of type 5 17beta-hydroxysteroid dehydrogenase (AKR1C3). Mol Cell Endocrinol. 2001 Jan 22;171(1-2):137-49. [PubMed ]
5. Khanna M, Qin KN, Cheng KC: Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular cloning of multiple cDNAs encoding structurally related proteins in humans. J Steroid Biochem Mol Biol. 1995 Jun;53(1-6):41-6. [PubMed ]
6. Khanna M, Qin KN, Wang RW, Cheng KC: Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 alpha-hydroxysteroid dehydrogenases. J Biol Chem. 1995 Aug 25;270(34):20162-8. [PubMed ]
7. Nagase T, Miyajima N, Tanaka A, Sazuka T, Seki N, Sato S, Tabata S, Ishikawa K, Kawarabayasi Y, Kotani H, et al.: Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1995;2(1):37-43. [PubMed ]
8. Qin KN, New MI, Cheng KC: Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase. J Steroid Biochem Mol Biol. 1993 Dec;46(6):673-9. [PubMed ]
9. Lin HK, Jez JM, Schlegel BP, Peehl DM, Pachter JA, Penning TM: Expression and characterization of recombinant type 2 3 alpha-hydroxysteroid dehydrogenase (HSD) from human prostate: demonstration of bifunctional 3 alpha/17 beta-HSD activity and cellular distribution. Mol Endocrinol. 1997 Dec;11(13):1971-84. [PubMed ]
10. Dufort I, Rheault P, Huang XF, Soucy P, Luu-The V: Characteristics of a highly labile human type 5 17beta-hydroxysteroid dehydrogenase. Endocrinology. 1999 Feb;140(2):568-74. [PubMed ]

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

1. Deoxyribonucleic acid

• DNA + DNA polymerase + nNTP = 2 DNA + nNDP; DNA + RNA polymerase + NTP = mRNA + nNDP

• None

• None

• Nucleus and mitochondria

CGCGAATTCGCG

1. Nadeau D, Marchand C: Change in the kinetics of sulphacetamide tissue distribution in Walker tumor-bearing rats. Drug Metab Dispos. 1975 Nov-Dec;3(6):565-76. [PubMed ]

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]
3. Kholod N, Boniver J, Delvenne P: A New Dimethyl Sulfoxide-Based Method for Gene Promoter Methylation Detection. J Mol Diagn. 2007 Oct 4;. [PubMed ]

1. 12 kDa FKBP
2. EC 5.2.1.8
3. FKBP-12
4. Immunophilin FKBP12
5. PPIase
6. Peptidyl-prolyl cis-trans isomerase
7. Rotamase

MGVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGW
EEGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFDVELLKLE

• peptidylproline (omega=180) = peptidylproline (omega=0)

• FKBP_C (PF00254 )

• None

• None

• Cytoplasm

ATGGGAGTGCAGGTGGAAACCATCTCCCCCGGAGACGGGCGCACCTTCCCGAAGCGCGGC
CAGACCTGCGTGGTGCACTACACCGGGATGCTTGAAGATGGAAAGAAATTCGATTCCTCC
CGGGACAGGAACAAGCCCTTTAAGTTTATGCTGGGCAAGCAGGAGGTGATCCGAGGCTGG
GAAGAAGGGGTTGCCCAGATGAGTGTGGGTCAGAGAGCCAAACTGACCATCTCCCCAGAC
TATGCCTACGGTGCCACTGGGCACCCGGGCATCATCCCACCACACGCCACTCTCGTCTTC
GATGTGGAGCTTCTAAAACTGGAATGA

1. Jayaraman T, Brillantes AM, Timerman AP, Fleischer S, Erdjument-Bromage H, Tempst P, Marks AR: FK506 binding protein associated with the calcium release channel (ryanodine receptor). J Biol Chem. 1992 May 15;267(14):9474-7. [PubMed ]

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

1. Beta-trypsin
2. Cationic trypsin precursor
3. EC 3.4.21.4

FIFLALLGAAVAFPVDDDDKIVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAH
CYKSGIQVRLGEDNINVVEGNEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRV
ASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKSAYPGQITSNM
FCAGYLEGGKDSCQGDSGGPVVCSGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQTI
ASN

• Preferential cleavage: Arg!, Lys! INHIBITOR Tos-Lys-CH2Cl; Tos-Arg-CH2Cl

• Trypsin (PF00089 )

• 1-14

• None

• Secreted protein
• extracellular space

CTTCATCTTTCTGGCTCTCTTGGGAGCCGCTGTTGCTTTCCCCGTGGACGATGATGACAA
GATCGTGGGCGGCTACACCTGTGGGGCAAATACTGTCCCCTACCAAGTGTCCCTGAACTC
TGGCTACCACTTCTGCGGGGGCTCCCTCATCAACAGCCAGTGGGTGGTGTCTGCGGCTCA
CTGCTACAAGTCCGGAATCCAAGTGCGTCTGGGAGAAGACAACATTAATGTCGTTGAGGG
CAATGAGCAATTCATCAGCGCATCCAAGAGTATCGTCCATCCCAGCTACAACTCAAACAC
CTTAAACAACGACATCATGCTGATTAAACTGAAATCAGCTGCCAGTCTCAACAGCCGAGT
AGCCTCTATCTCTCTGCCAACATCCTGTGCCTCTGCTGGCACCCAGTGTCTCATCTCTGG
CTGGGGCAACACCAAAAGCAGTGGCACCAGCTACCCTGATGTCCTGAAGTGTCTGAAGGC
TCCCATCCTATCAGACAGCTCTTGCAAAAGTGCCTACCCAGGCCAGATCACCAGCAACAT
GTTCTGTGCGGGCTACCTGGAGGGCGGAAAGGACTCCTGCCAGGGTGACTCCGGTGGCCC
TGTGGTCTGCAGTGGAAAGCTCCAGGGCATTGTCTCCTGGGGCTCTGGCTGCGCTCAGAA
AAACAAGCCTGGTGTCTACACCAAGGTCTGCAACTACGTGAGCTGGATTAAGCAGACCAT
CGCCTCCAACTAA

1. Titani K, Ericsson LH, Neurath H, Walsh KA: Amino acid sequence of dogfish trypsin. Biochemistry. 1975 Apr 8;14(7):1358-66. [PubMed ]
2. Hartley BS: Homologies in serine proteinases. Philos Trans R Soc Lond B Biol Sci. 1970 Feb 12;257(813):77-87. [PubMed ]
3. Bode W, Schwager P: The refined crystal structure of bovine beta-trypsin at 1.8 A resolution. II. Crystallographic refinement, calcium binding site, benzamidine binding site and active site at pH 7.0. J Mol Biol. 1975 Nov 15;98(4):693-717. [PubMed ]
4. Kossiakoff AA, Chambers JL, Kay LM, Stroud RM: Structure of bovine trypsinogen at 1.9 A resolution. Biochemistry. 1977 Feb 22;16(4):654-64. [PubMed ]
5. Kauffman DL: The disulphide bridges of trypsin. J Mol Biol. 1965 Jul;12(3):929-32. [PubMed ]
6. Mikes O, Holeysovsky V, Tomasek V, Sorm F: Covalent structure of bovine trypsinogen. The position of the remaining amides. Biochem Biophys Res Commun. 1966 Aug 12;24(3):346-52. [PubMed ]

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

1. EC 5.3.1.1
2. TIM
3. Triose- phosphate isomerase

MSKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCVVASTFVHLAMTKERLSHPKF
VIAAQNAIAKSGAFTGEVSLPILKDFGVNWIVLGHSERRAYYGETNEIVADKVAAAVASG
FMVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWAKVVIAYEPVWAIGTGKVATP
QQAQEAHALIRSWVSSKIGADVAGELRILYGGSVNGKNARTLYQQRDVNGFLVGGASLKP
EFVDIIKATQ

• D-glyceraldehyde 3-phosphate = glycerone phosphate

• TIM (PF00121 )

• None

• None

• Glycosome

ATGTCCAAGCCACAACCCATCGCAGCAGCCAACTGGAAGTGCAACGGCTCCCAACAGTCT
TTGTCGGAGCTTATTGATCTGTTTAACTCCACAAGCATCAACCACGACGTGCAATGCGTA
GTGGCCTCCACCTTTGTTCACCTTGCCATGACGAAGGAGCGTCTTTCACACCCCAAATTT
GTGATTGCGGCGCAGAACGCCATTGCAAAGAGCGGTGCCTTCACCGGCGAAGTCTCCCTG
CCCATCCTCAAAGATTTCGGTGTCAACTGGATTGTTCTGGGTCACTCCGAGCGCCGCGCA
TACTATGGTGAGACAAACGAGATTGTTGCGGACAAGGTTGCCGCCGCCGTTGCTTCTGGT
TTCATGGTTATTGCTTGCATCGGCGAAACGCTGCAGGAGCGTGAATCAGGTCGCACCGCT
GTTGTTGTGCTCACACAGATCGCTGCTATTGCTAAGAAACTGAAGAAGGCTGACTGGGCC
AAAGTTGTCATCGCCTACGAACCCGTTTGGGCCATTGGTACCGGCAAGGTGGCGACACCA
CAGCAAGCGCAGGAAGCCCACGCACTCATCCGCAGCTGGGTGAGCAGCAAGATTGGAGCA
GATGTCGCGGGAGAGCTCCGCATTCTTTACGGCGGTTCTGTTAATGGAAAGAATGCGCGC
ACTCTTTACCAACAGCGAGACGTCAACGGCTTCCTTGTTGGTGGTGCCTCACTTAAGCCA
GAATTTGTGGACATCATCAAAGCCACTCAGTGA

1. Wierenga RK, Noble ME, Davenport RC: Comparison of the refined crystal structures of liganded and unliganded chicken, yeast and trypanosomal triosephosphate isomerase. J Mol Biol. 1992 Apr 20;224(4):1115-26. [PubMed ]
2. Wierenga RK, Noble ME, Vriend G, Nauche S, Hol WG: Refined 1.83 A structure of trypanosomal triosephosphate isomerase crystallized in the presence of 2.4 M-ammonium sulphate. A comparison with the structure of the trypanosomal triosephosphate isomerase-glycerol-3-phosphate complex. J Mol Biol. 1991 Aug 20;220(4):995-1015. [PubMed ]
3. Swinkels BW, Gibson WC, Osinga KA, Kramer R, Veeneman GH, van Boom JH, Borst P: Characterization of the gene for the microbody (glycosomal) triosephosphate isomerase of Trypanosoma brucei. EMBO J. 1986 Jun;5(6):1291-8. [PubMed ]
4. Wierenga RK, Kalk KH, Hol WG: Structure determination of the glycosomal triosephosphate isomerase from Trypanosoma brucei brucei at 2.4 A resolution. J Mol Biol. 1987 Nov 5;198(1):109-21. [PubMed ]
5. Borst P: How proteins get into microbodies (peroxisomes, glyoxysomes, glycosomes). Biochim Biophys Acta. 1986 May 5;866(4):179-203. [PubMed ]
6. Borchert TV, Pratt K, Zeelen JP, Callens M, Noble ME, Opperdoes FR, Michels PA, Wierenga RK: Overexpression of trypanosomal triosephosphate isomerase in Escherichia coli and characterisation of a dimer-interface mutant. Eur J Biochem. 1993 Feb 1;211(3):703-10. [PubMed ]
7. Borchert TV, Kishan KV, Zeelen JP, Schliebs W, Thanki N, Abagyan R, Jaenicke R, Wierenga RK: Three new crystal structures of point mutation variants of monoTIM: conformational flexibility of loop-1, loop-4 and loop-8. Structure. 1995 Jul 15;3(7):669-79. [PubMed ]

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

1. EC 1.1.1.1

MSTAGKVIKCKAAVLWEEKKPFSIEEVEVAPPKAHEVRIKMVATGICRSDDHVVSGTLVT
PLPVIAGHEAAGIVESIGEGVTTVRPGDKVIPLFTPQCGKCRVCKHPEGNFCLKNDLSMP
RGTMQDGTSRFTCRGKPIHHFLGTSTFSQYTVVDEISVAKIDAASPLEKVCLIGCGFSTG
YGSAVKVAKVTQGSTCAVFGLGGVGLSVIMGCKAAGAARIIGVDINKDKFAKAKEVGATE
CVNPQDYKKPIQEVLTEMSNGGVDFSFEVIGRLDTMVTALSCCQEAYGVSVIVGVPPDSQ
NLSMNPMLLLSGRTWKGAIFGGFKSKDSVPKLVADFMAKKFALDPLITHVLPFEKINEGF
DLLRSGESIRTILTF

• an alcohol + NAD+ = an aldehyde or ketone + NADH + H+

• ADH_zinc_N (PF00107 )
• ADH_N (PF08240 )

• None

• None

• Cytoplasm

ATGAGCACAGCAGGAAAAGTAATAAAATGCAAAGCGGCTGTGCTGTGGGAGGAAAAGAAA
CCATTTTCCATCGAGGAGGTGGAGGTTGCACCCCCGAAGGCCCATGAAGTCCGTATAAAG
ATGGTGGCCACAGGAATTTGTCGCTCAGATGACCACGTGGTTAGTGGAACCCTTGTCACA
CCTCTTCCTGTGATCGCAGGCCATGAGGCAGCGGGCATTGTGGAGAGCATTGGAGAAGGC
GTCACTACAGTAAGACCAGGTGATAAAGTCATCCCACTCTTTACTCCCCAGTGTGGAAAA
TGCAGGGTTTGTAAGCACCCTGAAGGCAACTTCTGCTTGAAAAATGATCTGAGCATGCCT
CGGGGAACCATGCAGGATGGTACCAGCAGGTTCACCTGCAGAGGGAAGCCCATCCACCAC
TTCCTTGGCACCAGCACCTTCTCCCAGTACACCGTGGTGGACGAGATCTCAGTGGCCAAG
ATCGATGCGGCCTCACCGCTGGAGAAAGTCTGTCTCATTGGCTGTGGATTTTCTACTGGT
TATGGGTCTGCAGTCAAGGTTGCCAAGGTCACCCAGGGCTCCACCTGTGCCGTGTTTGGC
CTTGGAGGAGTGGGCCTGTCTGTTATCATGGGCTGTAAAGCAGCCGGAGCGGCCAGGATC
ATTGGGGTGGACATCAACAAAGACAAGTTTGCAAAGGCCAAAGAAGTGGGTGCCACTGAG
TGTGTCAACCCTCAGGACTACAAGAAACCCATCCAGGAGGTGCTGACAGAAATGAGCAAT
GGAGGTGTGGATTTTTCCTTTGAAGTCATTGGTCGGCTCGACACTATGGTGACTGCCTTG
TCATGCTGTCAAGAAGCATATGGTGTGAGCGTCATTGTGGGAGTACCTCCTGATTCCCAA
AATCTCTCTATGAATCCTATGTTGCTACTGAGTGGACGTACCTGGAAAGGAGCTATTTTT
GGCGGTTTTAAGAGTAAAGATTCTGTCCCCAAACTTGTGGCCGATTTTATGGCTAAAAAG
TTTGCACTGGATCCTTTAATCACCCATGTTTTACCTTTTGAAAAAATAAATGAAGGATTT
GACCTGCTTCGCTCTGGAGAGAGTATCCGTACCATCCTGACGTTTTGA

1. Park DH, Plapp BV: Isoenzymes of horse liver alcohol dehydrogenase active on ethanol and steroids. cDNA cloning, expression, and comparison of active sites. J Biol Chem. 1991 Jul 15;266(20):13296-302. [PubMed ]
2. Eklund H, Nordstrom B, Zeppezauer E, Soderlund G, Ohlsson I, Boiwe T, Soderberg BO, Tapia O, Branden CI, Akeson A: Three-dimensional structure of horse liver alcohol dehydrogenase at 2-4 A resolution. J Mol Biol. 1976 Mar 25;102(1):27-59. [PubMed ]
3. Jornvall H: Horse liver alcohol dehydrogenase. On the primary structures of the isoenzymes. Eur J Biochem. 1970 Sep;16(1):41-9. [PubMed ]
4. Eklund H, Samama JP, Jones TA: Crystallographic investigations of nicotinamide adenine dinucleotide binding to horse liver alcohol dehydrogenase. Biochemistry. 1984 Dec 4;23(25):5982-96. [PubMed ]

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

1. Bacillolysin precursor
2. EC 3.4.24.28
3. Neutral protease

MKRKMKMKLVRFGLAAGLAAQVFFLPYNALASTEHVTWNQQFQTPQFISGDLLKVNGTSP
EELVYQYVEKNENKFKFHENAKDTLQLKEKKNDNLGFTFMRFQQTYKGIPVFGAVVTAHV
KDGTLTALSGTLIPNLDTKGSLKSGKKLSEKQARDIAEKDLVANVTKEVPEYEQGKDTEF
VVYVNGDEASLAYVVNLNFLTPEPGNWLYIIDAVDGKILNKFNQLDAAKPGDVKSITGTS
TVGVGRGVLGDQKNINTTYSTYYYLQDNTRGNGIFTYDAKYRTTLPGSLWADADNQFFAS
YDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAIRSSVHYSQGYNNAFWNGSQMVYGDG
DGQTFIPLSGGIDVVAHELTHAVTDYTAGLIYQNESGAINEAISDIFGTLVEFYANKNPD
WEIGEDVYTPGISGDSLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLIS
QGGTHYGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTSQEVAS
VKQAFDAVGVK

• Similar, but not identical, to that of thermolysin

• Peptidase_M4 (PF01447 )
• Peptidase_M4_C (PF02868 )
• PepSY (PF03413 )
• FTP (PF07504 )

• 1-31

• None

• Secreted protein

ATGAAAAGGAAAATGAAAATGAAATTAGTACGTTTTGGTCTTGCAGCAGGACTAGCGGCC
CAAGTATTTTTTTTACCTTACAATGCGCTGGCTTCAACGGAACACGTTACATGGAACCAA
CAATTTCAAACCCCTCAATTCATCTCCGGTGATCTGCTGAAAGTGAATGGCACATCCCCA
GAAGAACTCGTCTATCAATATGTTGAAAAAAACGAAAACAAGTTTAAATTTCATGAAAAC
GCTAAGGATACTCTACAATTGAAAGAAAAGAAAAATGATAACCTTGGTTTTACGTTTATG
CGCTTCCAACAAACGTATAAAGGGATTCCTGTGTTTGGAGCAGTAGTAACTGCGCACGTG
AAAGATGGCACGCTGACGGCGCTATCAGGGACACTGATTCCGAATTTGGACACGAAAGGA
TCCTTAAAAAGCGGGAAGAAATTGAGTGAGAAACAAGCGCGTGACATTGCTGAAAAAGAT
TTAGTGGCAAATGTAACAAAGGAAGTACCGGAATATGAACAGGGAAAAGACACCGAGTTT
GTTGTTTATGTCAATGGGGACGAGGCTTCTTTAGCGTACGTTGTCAATTTAAACTTTTTA
ACTCCTGAACCAGGAAACTGGCTGTATATCATTGATGCCGTAGACGGAAAAATTTTAAAT
AAATTTAACCAACTTGACGCCGCAAAACCAGGTGATGTGAAGTCGATAACAGGAACATCA
ACTGTCGGAGTGGGAAGAGGAGTACTTGGTGATCAAAAAAATATTAATACAACCTACTCT
ACGTACTACTATTTACAAGATAATACGCGTGGAAATGGGATTTTCACGTATGATGCGAAA
TACCGTACGACATTGCCGGGAAGCTTATGGGCAGATGCAGATAACCAATTTTTTGCGAGC
TATGATGCTCCAGCGGTTGATGCTCATTATTACGCTGGTGTGACATATGACTACTATAAA
AATGTTCATAACCGTCTCAGTTACGACGGAAATAATGCAGCTATTAGATCATCCGTTCAT
TATAGCCAAGGCTATAATAACGCATTTTGGAACGGTTCGCAAATGGTGTATGGCGATGGT
GATGGTCAAACATTTATTCCACTTTCTGGTGGTATTGATGTGGTCGCACATGAGTTAACG
CATGCGGTAACCGATTATACAGCCGGACTCATTTATCAAAACGAATCTGGTGCAATTAAT
GAGGCAATATCTGATATTTTTGGAACGTTAGTCGAATTTTACGCTAACAAAAATCCAGAT
TGGGAAATTGGAGAGGATGTGTATACACCTGGTATTTCAGGGGATTCGCTCCGTTCGATG
TCCGATCCGGCAAAGTATGGTGATCCAGATCACTATTCAAAGCGCTATACAGGCACGCAA
GATAATGGCGGGGTTCATATCAATAGCGGAATTATCAACAAAGCCGCTTATTTGATTAGC
CAAGGCGGTACGCATTACGGTGTGAGTGTTGTCGGAATCGGACGCGATAAATTGGGGAAA
ATTTTCTATCGTGCATTAACGCAATATTTAACACCAACGTCCAACTTTAGCCAACTTCGT
GCTGCCGCTGTTCAATCAGCCACTGACTTGTACGGTTCGACAAGCCAGGAAGTCGCTTCT
GTGAAGCAGGCCTTTGATGCGGTAGGGGTGAAATAA

1. Nishiya Y, Imanaka T: Cloning and nucleotide sequences of the Bacillus stearothermophilus neutral protease gene and its transcriptional activator gene. J Bacteriol. 1990 Sep;172(9):4861-9. [PubMed ]
2. Kubo M, Imanaka T: Cloning and nucleotide sequence of the highly thermostable neutral protease gene from Bacillus stearothermophilus. J Gen Microbiol. 1988 Jul;134(7):1883-92. [PubMed ]

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]
3. Mortensen AM, Novak RF: Enhanced proteolysis and changes in membrane-associated calpain following phenylhydrazine insult to human red cells. Toxicol Appl Pharmacol. 1991 Sep 15;110(3):435-49. [PubMed ]

1. Cyclophilin F
2. EC 5.2.1.8
3. PPIase
4. Peptidyl-prolyl cis-trans isomerase, mitochondrial precursor
5. Rotamase

MLALRCGSRWLGLLSVPRSVPLRLPAARACSKGSGDPSSSSSSGNPLVYLDVDANGKPLG
RVVLELKADVVPKTAENFRALCTGEKGFGYKGSTFHRVIPSFMCQAGDFTNHNGTGGKSI
YGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDV
VKKIESFGSKSGRTSKKIVITDCGQLS

• peptidylproline (omega=180) = peptidylproline (omega=0)

• Pro_isomerase (PF00160 )

• None

• None

• Mitochondrion
• mitochondrial matrix

ATGCTGGCGCTGCGCTGCGGCTCCCGCTGGCTCGGCCTGCTCTCCGTCCCGCGCTCCGTG
CCGCTGCGCCTCCCCGCGGCCCGCGCCTGCAGCAAGGGCTCCGGCGACCCGTCCTCTTCC
TCCTCCTCCGGGAACCCGCTCGTGTACCTGGACGTGGACGCCAACGGGAAGCCGCTCGGC
CGCGTGGTGCTGGAGCTGAAGGCAGATGTCGTCCCAAAGACAGCTGAGAACTTCAGAGCC
CTGTGCACTGGTGAGAAGGGCTTCGGCTACAAAGGCTCCACCTTCCACAGGGTGATCCCT
TCCTTCATGTGCCAGGCGGGCGACTTCACCAACCACAATGGCACAGGCGGGAAGTCCATC
TACGGAAGCCGCTTTCCTGACGAGAACTTTACACTGAAGCACGTGGGGCCAGGTGTCCTG
TCCATGGCTAATGCTGGTCCTAACACCAACGGCTCCCAGTTCTTCATCTGCACCATAAAG
ACAGACTGGTTGGATGGCAAGCATGTTGTGTTCGGTCACGTCAAAGAGGGCATGGACGTC
GTGAAGAAAATAGAATCTTTCGGCTCTAAGAGTGGGAGGACATCCAAGAAGATTGTCATC
ACAGACTGTGGCCAGTTGAGCTAA

1. Bergsma DJ, Eder C, Gross M, Kersten H, Sylvester D, Appelbaum E, Cusimano D, Livi GP, McLaughlin MM, Kasyan K, et al.: The cyclophilin multigene family of peptidyl-prolyl isomerases. Characterization of three separate human isoforms. J Biol Chem. 1991 Dec 5;266(34):23204-14. [PubMed ]

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

1. EC 3.2.1.23
2. Lactase

MTMITDSLAVVLQRRDWENPGVTQLNRLAAHPPFASWRNSEEARTDRPSQQLRSLNGEWR
FAWFPAPEAVPESWLECDLPEADTVVVPSNWQMHGYDAPIYTNVTYPITVNPPFVPTENP
TGCYSLTFNVDESWLQEGQTRIIFDGVNSAFHLWCNGRWVGYGQDSRLPSEFDLSAFLRA
GENRLAVMVLRWSDGSYLEDQDMWRMSGIFRDVSLLHKPTTQISDFHVATRFNDDFSRAV
LEAEVQMCGELRDYLRVTVSLWQGETQVASGTAPFGGEIIDERGGYADRVTLRLNVENPK
LWSAEIPNLYRAVVELHTADGTLIEAEACDVGFREVRIENGLLLLNGKPLLIRGVNRHEH
HPLHGQVMDEQTMVQDILLMKQNNFNAVRCSHYPNHPLWYTLCDRYGLYVVDEANIETHG
MVPMNRLTDDPRWLPAMSERVTRMVQRDRNHPSVIIWSLGNESGHGANHDALYRWIKSVD
PSRPVQYEGGGADTTATDIICPMYARVDEDQPFPAVPKWSIKKWLSLPGETRPLILCEYA
HAMGNSLGGFAKYWQAFRQYPRLQGGFVWDWVDQSLIKYDENGNPWSAYGGDFGDTPNDR
QFCMNGLVFADRTPHPALTEAKHQQQFFQFRLSGQTIEVTSEYLFRHSDNELLHWMVALD
GKPLASGEVPLDVAPQGKQLIELPELPQPESAGQLWLTVRVVQPNATAWSEAGHISAWQQ
WRLAENLSVTLPAASHAIPHLTTSEMDFCIELGNKRWQFNRQSGFLSQMWIGDKKQLLTP
LRDQFTRAPLDNDIGVSEATRIDPNAWVERWKAAGHYQAEAALLQCTADTLADAVLITTA
HAWQHQGKTLFISRKTYRIDGSGQMAITVDVEVASDTPHPARIGLNCQLAQVAERVNWLG
LGPQENYPDRLTAACFDRWDLPLSDMYTPYVFPSENGLRCGTRELNYGPHQWRGDFQFNI
SRYSQQQLMETSHRHLLHAEEGTWLNIDGFHMGIGGDDSWSPSVSAEFQLSAGRYHYQLV
WCQK

• Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides ALL_REAC (other) R01105 R01678 R01679 R03355 R03616 R04633 R04783 R05112 R05994(G) R06010(G) R06098(G) R06099(G) R06111(G) R06144(G) R06202(G) R07807(G)

• Glyco_hydro_2 (PF00703 )
• Glyco_hydro_2_C (PF02836 )
• Glyco_hydro_2_N (PF02837 )
• Bgal_small_N (PF02929 )

• None

• None

• Cytoplasmic

ATGACCATGATTACGGATTCACTGGCCGTCGTTTTACAACGTCGTGACTGGGAAAACCCT
GGCGTTACCCAACTTAATCGCCTTGCAGCACATCCCCCTTTCGCCAGCTGGCGTAATAGC
GAAGAGGCCCGCACCGATCGCCCTTCCCAACAGTTGCGCAGCCTGAATGGCGAATGGCGC
TTTGCCTGGTTTCCGGCACCAGAAGCGGTGCCGGAAAGCTGGCTGGAGTGCGATCTTCCT
GAGGCCGATACTGTCGTCGTCCCCTCAAACTGGCAGATGCACGGTTACGATGCGCCCATC
TACACCAACGTAACCTATCCCATTACGGTCAATCCGCCGTTTGTTCCCACGGAGAATCCG
ACGGGTTGTTACTCGCTCACATTTAATGTTGATGAAAGCTGGCTACAGGAAGGCCAGACG
CGAATTATTTTTGATGGCGTTAACTCGGCGTTTCATCTGTGGTGCAACGGGCGCTGGGTC
GGTTACGGCCAGGACAGTCGTTTGCCGTCTGAATTTGACCTGAGCGCATTTTTACGCGCC
GGAGAAAACCGCCTCGCGGTGATGGTGCTGCGTTGGAGTGACGGCAGTTATCTGGAAGAT
CAGGATATGTGGCGGATGAGCGGCATTTTCCGTGACGTCTCGTTGCTGCATAAACCGACT
ACACAAATCAGCGATTTCCATGTTGCCACTCGCTTTAATGATGATTTCAGCCGCGCTGTA
CTGGAGGCTGAAGTTCAGATGTGCGGCGAGTTGCGTGACTACCTACGGGTAACAGTTTCT
TTATGGCAGGGTGAAACGCAGGTCGCCAGCGGCACCGCGCCTTTCGGCGGTGAAATTATC
GATGAGCGTGGTGGTTATGCCGATCGCGTCACACTACGTCTGAACGTCGAAAACCCGAAA
CTGTGGAGCGCCGAAATCCCGAATCTCTATCGTGCGGTGGTTGAACTGCACACCGCCGAC
GGCACGCTGATTGAAGCAGAAGCCTGCGATGTCGGTTTCCGCGAGGTGCGGATTGAAAAT
GGTCTGCTGCTGCTGAACGGCAAGCCGTTGCTGATTCGAGGCGTTAACCGTCACGAGCAT
CATCCTCTGCATGGTCAGGTCATGGATGAGCAGACGATGGTGCAGGATATCCTGCTGATG
AAGCAGAACAACTTTAACGCCGTGCGCTGTTCGCATTATCCGAACCATCCGCTGTGGTAC
ACGCTGTGCGACCGCTACGGCCTGTATGTGGTGGATGAAGCCAATATTGAAACCCACGGC
ATGGTGCCAATGAATCGTCTGACCGATGATCCGCGCTGGCTACCGGCGATGAGCGAACGC
GTAACGCGAATGGTGCAGCGCGATCGTAATCACCCGAGTGTGATCATCTGGTCGCTGGGG
AATGAATCAGGCCACGGCGCTAATCACGACGCGCTGTATCGCTGGATCAAATCTGTCGAT
CCTTCCCGCCCGGTGCAGTATGAAGGCGGCGGAGCCGACACCACGGCCACCGATATTATT
TGCCCGATGTACGCGCGCGTGGATGAAGACCAGCCCTTCCCGGCTGTGCCGAAATGGTCC
ATCAAAAAATGGCTTTCGCTACCTGGAGAGACGCGCCCGCTGATCCTTTGCGAATACGCC
CACGCGATGGGTAACAGTCTTGGCGGTTTCGCTAAATACTGGCAGGCGTTTCGTCAGTAT
CCCCGTTTACAGGGCGGCTTCGTCTGGGACTGGGTGGATCAGTCGCTGATTAAATATGAT
GAAAACGGCAACCCGTGGTCGGCTTACGGCGGTGATTTTGGCGATACGCCGAACGATCGC
CAGTTCTGTATGAACGGTCTGGTCTTTGCCGACCGCACGCCGCATCCAGCGCTGACGGAA
GCAAAACACCAGCAGCAGTTTTTCCAGTTCCGTTTATCCGGGCAAACCATCGAAGTGACC
AGCGAATACCTGTTCCGTCATAGCGATAACGAGCTCCTGCACTGGATGGTGGCGCTGGAT
GGTAAGCCGCTGGCAAGCGGTGAAGTGCCTCTGGATGTCGCTCCACAAGGTAAACAGTTG
ATTGAACTGCCTGAACTACCGCAGCCGGAGAGCGCCGGGCAACTCTGGCTCACAGTACGC
GTAGTGCAACCGAACGCGACCGCATGGTCAGAAGCCGGGCACATCAGCGCCTGGCAGCAG
TGGCGTCTGGCGGAAAACCTCAGTGTGACGCTCCCCGCCGCGTCCCACGCCATCCCGCAT
CTGACCACCAGCGAAATGGATTTTTGCATCGAGCTGGGTAATAAGCGTTGGCAATTTAAC
CGCCAGTCAGGCTTTCTTTCACAGATGTGGATTGGCGATAAAAAACAACTGCTGACGCCG
CTGCGCGATCAGTTCACCCGTGCACCGCTGGATAACGACATTGGCGTAAGTGAAGCGACC
CGCATTGACCCTAACGCCTGGGTCGAACGCTGGAAGGCGGCGGGCCATTACCAGGCCGAA
GCAGCGTTGTTGCAGTGCACGGCAGATACACTTGCTGATGCGGTGCTGATTACGACCGCT
CACGCGTGGCAGCATCAGGGGAAAACCTTATTTATCAGCCGGAAAACCTACCGGATTGAT
GGTAGTGGTCAAATGGCGATTACCGTTGATGTTGAAGTGGCGAGCGATACACCGCATCCG
GCGCGGATTGGCCTGAACTGCCAGCTGGCGCAGGTAGCAGAGCGGGTAAACTGGCTCGGA
TTAGGGCCGCAAGAAAACTATCCCGACCGCCTTACTGCCGCCTGTTTTGACCGCTGGGAT
CTGCCATTGTCAGACATGTATACCCCGTACGTCTTCCCGAGCGAAAACGGTCTGCGCTGC
GGGACGCGCGAATTGAATTATGGCCCACACCAGTGGCGCGGCGACTTCCAGTTCAACATC
AGCCGCTACAGTCAACAGCAACTGATGGAAACCAGCCATCGCCATCTGCTGCACGCGGAA
GAAGGCACATGGCTGAATATCGACGGTTTCCATATGGGGATTGGTGGCGACGACTCCTGG
AGCCCGTCAGTATCGGCGGAATTCCAGCTGAGCGCCGGTCGCTACCATTACCAGTTGGTC
TGGTGTCAAAAATAA

1. Juers DH, Heightman TD, Vasella A, McCarter JD, Mackenzie L, Withers SG, Matthews BW: A structural view of the action of Escherichia coli (lacZ) beta-galactosidase. Biochemistry. 2001 Dec 11;40(49):14781-94. [PubMed ]
2. Gebler JC, Aebersold R, Withers SG: Glu-537, not Glu-461, is the nucleophile in the active site of (lac Z) beta-galactosidase from Escherichia coli. J Biol Chem. 1992 Jun 5;267(16):11126-30. [PubMed ]
3. Calos MP, Miller JH: Molecular consequences of deletion formation mediated by the transposon Tn9. Nature. 1980 May 1;285(5759):38-41. [PubMed ]
4. Kalnins A, Otto K, Ruther U, Muller-Hill B: Sequence of the lacZ gene of Escherichia coli. EMBO J. 1983;2(4):593-7. [PubMed ]
5. Fowler AV, Smith PJ: The active site regions of lacZ and ebg beta-galactosidases are homologous. J Biol Chem. 1983 Sep 10;258(17):10204-7. [PubMed ]
6. Herrchen M, Legler G: Identification of an essential carboxylate group at the active site of lacZ beta-galactosidase from Escherichia coli. Eur J Biochem. 1984 Feb 1;138(3):527-31. [PubMed ]
7. Buchel DE, Gronenborn B, Muller-Hill B: Sequence of the lactose permease gene. Nature. 1980 Feb 7;283(5747):541-5. [PubMed ]
8. Jacobson RH, Zhang XJ, DuBose RF, Matthews BW: Three-dimensional structure of beta-galactosidase from E. coli. Nature. 1994 Jun 30;369(6483):761-6. [PubMed ]
9. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-74. [PubMed ]
10. Fowler AV, Zabin I: Amino acid sequence of beta-galactosidase. XI. Peptide ordering procedures and the complete sequence. J Biol Chem. 1978 Aug 10;253(15):5521-5. [PubMed ]

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

1. Dihydropteridine reductase
2. EC 1.-.-.-
3. EC 1.5.1.34
4. FMN-dependent nitroreductase

MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVASTEEGKARV
AKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQEDADGRFATPEAKAANDKG
RKFFADMHRKDLHDDAEWMAKQVYLNVGNFLLGVAALGLDAVPIEGFDAAILDAEFGLKE
KGYTSLVVVPVGHHSVEDFNATLPKSRLPQNITLTEV

• a 5,6,7,8-tetrahydropteridine + NAD(P)+ = a 6,7-dihydropteridine + NAD(P)H + H+

• Nitroreductase (PF00881 )

• None

• None

ATGGATATCATTTCTGTCGCCTTAAAGCGTCATTCCACTAAGGCATTTGATGCCAGCAAA
AAACTTACCCCGGAACAGGCCGAGCAGATCAAAACGCTACTGCAATACAGCCCATCCAGC
ACCAACTCCCAGCCGTGGCATTTTATTGTTGCCAGCACGGAAGAAGGTAAAGCGCGTGTT
GCCAAATCCGCTGCCGGTAATTACGTGTTCAACGAGCGTAAAATGCTTGATGCCTCGCAC
GTCGTGGTGTTCTGTGCAAAAACCGCGATGGACGATGTCTGGCTGAAGCTGGTTGTTGAC
CAGGAAGATGCCGATGGCCGCTTTGCCACGCCGGAAGCGAAAGCCGCGAACGATAAAGGT
CGCAAGTTCTTCGCTGATATGCACCGTAAAGATCTGCATGATGATGCAGAGTGGATGGCA
AAACAGGTTTATCTCAACGTCGGTAACTTCCTGCTCGGCGTGGCGGCTCTGGGTCTGGAC
GCGGTACCCATCGAAGGTTTTGACGCCGCCATCCTCGATGCAGAATTTGGTCTGAAAGAG
AAAGGCTACACCAGTCTGGTGGTTGTTCCGGTAGGTCATCACAGCGTTGAAGATTTTAAC
GCTACGCTGCCGAAATCTCGTCTGCCGCAAAACATCACCTTAACCGAAGTGTAA

1. Parkinson GN, Skelly JV, Neidle S: Crystal structure of FMN-dependent nitroreductase from Escherichia coli B: a prodrug-activating enzyme. J Med Chem. 2000 Oct 5;43(20):3624-31. [PubMed ]
2. Anlezark GM, Melton RG, Sherwood RF, Coles B, Friedlos F, Knox RJ: The bioactivation of 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB1954)--I. Purification and properties of a nitroreductase enzyme from Escherichia coli--a potential enzyme for antibody-directed enzyme prodrug therapy (ADEPT). Biochem Pharmacol. 1992 Dec 15;44(12):2289-95. [PubMed ]
3. Vasudevan SG, Shaw DC, Armarego WL: Dihydropteridine reductase from Escherichia coli. Biochem J. 1988 Oct 15;255(2):581-8. [PubMed ]
4. Michael NP, Brehm JK, Anlezark GM, Minton NP: Physical characterisation of the Escherichia coli B gene encoding nitroreductase and its over-expression in Escherichia coli K12. FEMS Microbiol Lett. 1994 Dec 1;124(2):195-202. [PubMed ]
5. Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. [PubMed ]
6. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-74. [PubMed ]
7. Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [PubMed ]

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

MEAIAKRLDACQDQLLELYEENSIDIHKHIMHWKCIRLESVLLHKAKQMGLSHIGLQVVP
PLTVSETKGHNAIEMQMHLESLAKTQYGVEPWTLQDTSYEMWLTPPKRCFKKQGNTVEVK
FDGCEDNVMEYVVWTHIYLQDNDSWVKVTSSVDAKGIYYTCGQFKTYYVNFNKEAQKYGS
TNHWEVCYGSTVICSPASVSSTVREVSIAEPTTYTPAQTTAPTVSACTTEDGVSAPPRKR
ARGPSTNNTLCVANIRSVDSTINNIVTDNYNKHQRRNNCHSAATPIVQLQGDSNCLKCFR
YRLNDKYKHLFELASSTWHWASPEAPHKNAIVTLTYSSEEQRQQFLNSVKIPPTIRHKVG
FMSLHLL

• PPV_E2_N (PF00508 )
• PPV_E2_C (PF00511 )

• None

• None

• Nucleus

ATGGAAGCAATAGCCAAGCGTTTAGATGCGTGCCAGGATCAGTTGTTAGAACTTTATGAA
GAAAACAGTATTGATATACACAAACACATTATGCATTGGAAATGCATACGATTGGAAAGT
GTATTACTACACAAAGCAAAACAAATGGGCCTGAGCCACATCGGGTTACAAGTAGTACCA
CCATTAACTGTGTCAGAGACTAAAGGACATAATGCTATTGAAATGCAAATGCATTTAGAA
TCCTTAGCAAAAACTCAGTATGGTGTGGAACCTTGGACATTACAGGACACCAGTTATGAA
ATGTGGCTAACACCACCCAAACGGTGCTTTAAAAAACAGGGAAATACTGTGGAGGTAAAA
TTTGATGGCTGTGAAGACAATGTAATGGAGTATGTGGTATGGACACATATATACCTGCAG
GACAACGACTCATGGGTAAAAGTAACTAGTTCCGTAGATGCCAAGGGCATATATTATACA
TGTGGACAATTTAAAACATATTATGTAAATTTTAATAAAGAGGCACAAAAGTATGGTAGT
ACCAATCATTGGGAAGTATGTTATGGCAGCACAGTTATATGTTCTCCTGCATCTGTATCT
AGCACTGTACGAGAAGTATCCATTGCTGAACCTACTACATACACCCCCGCACAGACCACC
GCCCCTACAGTGTCCGCCTGCACCACGGAAGACGGCGTGTCGGCGCCGCCTAGGAAGCGA
GCACGTGGACCGTCCACTAACAACACCCTGTGTGTGGCCAACATCAGATCCGTGGACAGT
ACAATCAACAACATCGTCACTGACAATTACAACAAGCACCAAAGAAGGAACAACTGTCAC
AGTGCAGCTACGCCTATAGTGCAACTGCAAGGTGATTCCAATTGTTTAAAATGTTTTAGA
TATAGACTGAATGACAAATATAAACATTTGTTTGAATTAGCATCTTCAACGTGGCATTGG
GCCTCACCTGAGGCACCACATAAAAATGCAATTGTAACATTAACATATAGCAGTGAGGAA
CAACGTCAGCAATTTTTAAACAGTGTAAAAATACCACCCACCATTAGGCATAAGGTGGGG
TTTATGTCATTACATTTATTGTAA

1. Dartmann K, Schwarz E, Gissmann L, zur Hausen H: The nucleotide sequence and genome organization of human papilloma virus type 11. Virology. 1986 May;151(1):124-30. [PubMed ]

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

1. EC 3.1.31.1
2. Micrococcal nuclease
3. Staphylococcal nuclease
4. TNase
5. Thermonuclease precursor

MLVMTEYLLSAGICMAIVSILLIGMAISNVSKGQYAKRFFFFATSCLVLTLVVVSSLSSS
ANASQTDNGVNRSGSEDPTVYSATSTKKLHKEPATLIKAIDGDTVKLMYKGQPMTFRLLL
VDTPETKHPKKGVEKYGPEASAFTKKMVENAKKIEVEFDKGQRTDKYGRGLAYIYADGKM
VNEALVRQGLAKVAYVYKPNNTHEQHLRKSEAQAKKEKLNIWSEDNADSGQ

• Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products

• SNase (PF00565 )

• 1-26

• None

• Nuclease A:Secreted protein. Nuclease B:Membrane

GTGTTAGTTATGACAGAATACTTATTAAGTGCTGGCATATGTATGGCAATTGTTTCAATA
TTACTTATAGGGATGGCTATCAGTAATGTTTCGAAAGGGCAATACGCAAAGAGGTTTTTC
TTTTTCGCTACTAGTTGCTTAGTGTTAACTTTAGTTGTAGTTTCAAGTCTAAGTAGCTCA
GCAAATGCATCACAAACAGATAACGGCGTAAATAGAAGTGGTTCTGAAGATCCAACAGTA
TATAGTGCAACTTCAACTAAAAAATTACATAAAGAACCTGCGACTTTAATTAAAGCGATT
GATGGTGATACGGTTAAATTAATGTACAAAGGTCAACCAATGACATTCAGACTATTATTG
GTTGATACACCTGAAACAAAGCATCCTAAAAAAGGTGTAGAGAAATATGGTCCTGAAGCA
AGTGCATTTACGAAAAAAATGGTAGAAAATGCAAAGAAAATTGAAGTCGAGTTTGACAAA
GGTCAAAGAACTGATAAATATGGACGTGGCTTAGCGTATATTTATGCTGATGGAAAAATG
GTAAACGAAGCTTTAGTTCGTCAAGGCTTGGCTAAAGTTGCTTATGTTTACAAACCTAAC
AATACACATGAACAACATTTAAGAAAAAGTGAAGCACAAGCGAAAAAAGAGAAATTAAAT
ATTTGGAGCGAAGACAACGCTGATTCAGGTCAATAA

1. Wang JF, Mooberry ES, Walkenhorst WF, Markley JL: Solution studies of staphylococcal nuclease H124L. 1. Backbone 1H and 15N resonances and secondary structure of the unligated enzyme as identified by three-dimensional NMR spectroscopy. Biochemistry. 1992 Jan 28;31(3):911-20. [PubMed ]
2. Hynes TR, Fox RO: The crystal structure of staphylococcal nuclease refined at 1.7 A resolution. Proteins. 1991;10(2):92-105. [PubMed ]
3. Cotton FA, Hazen EE Jr, Legg MJ: Staphylococcal nuclease: proposed mechanism of action based on structure of enzyme-thymidine 3',5'-bisphosphate-calcium ion complex at 1.5-A resolution. Proc Natl Acad Sci U S A. 1979 Jun;76(6):2551-5. [PubMed ]
4. Miller JR, Kovacevic S, Veal LE: Secretion and processing of staphylococcal nuclease by Bacillus subtilis. J Bacteriol. 1987 Aug;169(8):3508-14. [PubMed ]
5. Kovacevic S, Veal LE, Hsiung HM, Miller JR: Secretion of staphylococcal nuclease by Bacillus subtilis. J Bacteriol. 1985 May;162(2):521-8. [PubMed ]
6. Cone JL, Cusumano CL, Taniuchi H, Anfinsen CB: Staphylococcal nuclease (Foggi strain). II. The amino acid sequence. J Biol Chem. 1971 May 25;246(10):3103-10. [PubMed ]
7. Bohnert JL, Taniuchi H: The examination of the presence of amide groups in glutamic acid and aspartic acid residues of staphylococcal nuclease (Foggi strain). J Biol Chem. 1972 Jul 25;247(14):4557-60. [PubMed ]
8. Shortle D: A genetic system for analysis of staphylococcal nuclease. Gene. 1983 May-Jun;22(2-3):181-9. [PubMed ]
9. Shortle D, Abeygunawardana C: NMR analysis of the residual structure in the denatured state of an unusual mutant of staphylococcal nuclease. Structure. 1993 Oct 15;1(2):121-34. [PubMed ]
10. Davis A, Moore IB, Parker DS, Taniuchi H: Nuclease B. A possible precursor of nuclease A, an extracellular nuclease of Staphylococcus aureus. J Biol Chem. 1977 Sep 25;252(18):6544-53. [PubMed ]

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]
3. Pramanik SK, Bag J: Expression of muscle-specific proteins is necessary to regulate translation of the mRNA for a 40-kDa housekeeping polypeptide in rat L6 cells. Eur J Biochem. 1989 Jul 1;182(3):687-98. [PubMed ]
4. Chakrabarti S, Kassis AI, Slayter HS, Bump EA, Sahu SK, Makrigiorgos GM: Continuous detection of radiation or metal generated hydroxyl radicals within core chromatin particles. Int J Radiat Biol. 1998 Jan;73(1):53-63. [PubMed ]

1. CA
2. Capsid protein p24
3. EC 2.7.7.49
4. EC 2.7.7.7
5. EC 3.1.26.4
6. EC 3.4.23.16
7. IN]
8. Integrase
9. MA
10. NC
11. Nucleocapsid protein p7
12. PR
13. Pr160Gag-Pol[Contains: Matrix protein p17
14. Protease
15. Retropepsin
16. Reverse transcriptase/ribonuclease H
17. Spacer peptide p2
18. TF
19. Transframe peptide
20. p15
21. p51 RT
22. p6*
23. p6-pol
24. p66 RT

MGARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQI
LGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEIKDTKEALDKIEEEQNKSKKKAQQAAA
DTGHSSQVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGAT
PQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTT
STLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRF
YKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKA
RVLAEAMSQVTNTATIMMQRGNFRNQRKMVKCFNCGKEGHTARNCRAPRKKGCWKCGKEG
HQMKDCTERQANFLREDLAFLQGKAREFSSEQTRANSPTISSEQTRANSPTRRELQVWGR
DNNSPSEAGADRQGTVSFNFPQITLWQRPLVTIKIGGQLKEALLDTGADDTVLEEMSLPG
RWKPKMIGGIGGFIKVRQYDQILIEICGHKAIGTVLVGPTPVNIIGRNLLTQIGCTLNFP
ISPIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEKEGKISKIGPENPYNTPVF
AIKKKDSTKWRKLVDFRELNKRTQDFWEVQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLD
EDFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFKKQNPDIVIY
QYMDDLYVGSDLEIGQHRTKIEELRQHLLRWGLTTPDKKHQKEPPFLWMGYELHPDKWTV
QPIVLPEKDSWTVNDIQKLVGKLNWASQIYPGIKVRQLCKLLRGTKALTEVIPLTEEAEL
ELAENREILKEPVHGVYYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTGKYARMRGAH
TNDVKQLTEAVQKITTESIVIWGKTPKFKLPIQKETWETWWTEYWQATWIPEWEFVNTPP
LVKLWYQLEKEPIVGAETFYVDGAANRETKLGKAGYVTNKGRQKVVPLTNTTNQKTELQA
IYLALQDSGLEVNIVTDSQYALGIIQAQPDKSESELVNQIIEQLIKKEKVYLAWVPAHKG
IGGNEQVDKLVSAGIRKILFLDGIDKAQDEHEKYHSNWRAMASDFNLPPVVAKEIVASCD
KCQLKGEAMHGQVDCSPGIWQLDCTHLEGKVILVAVHVASGYIEAEVIPAETGQETAYFL
LKLAGRWPVKTIHTDNGSNFTSATVKAACWWAGIKQEFGIPYNPQSQGVVESMNKELKKI
IGQVRDQAEHLKTAVQMAVFIHNFKRKGGIGGYSAGERIVDIIATDIQTKELQKQITKIQ
NFRVYYRDSRNPLWKGPAKLLWKGEGAVVIQDNSDIKVVPRRKAKIIRDYGKQMAGDDCV
ASRQDED

• Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro

• RnaseH (PF00075 )
• RVP (PF00077 )
• RVT_1 (PF00078 )
• zf-CCHC (PF00098 )
• Gag_p17 (PF00540 )
• Integrase (PF00552 )
• Gag_p24 (PF00607 )
• rve (PF00665 )
• Integrase_Zn (PF02022 )
• RVT_connect (PF06815 )
• RVT_thumb (PF06817 )

• None

• None

• Nucleus. Cytoplasm (By similarity). Note=Following virus entry, the nuclear localization signal (NLS

ATGGGTGCGAGAGCGTCAGTATTAAGCGGGGGAGAATTAGATCGATGGGAAAAAATTCGG
TTAAGGCCAGGGGGAAAGAAAAAATATAAATTAAAACATATAGTATGGGCAAGCAGGGAG
CTAGAACGATTCGCAGTTAATCCTGGCCTGTTAGAAACATCAGAAGGCTGTAGACAAATA
CTGGGACAGCTACAACCATCCCTTCAGACAGGATCAGAAGAACTTAGATCATTATATAAT
ACAGTAGCAACCCTCTATTGTGTGCATCAAAGGATAGAGATAAAAGACACCAAGGAAGCT
TTAGACAAGATAGAGGAAGAGCAAAACAAAAGTAAGAAAAAAGCACAGCAAGCAGCAGCT
GACACAGGACACAGCAGTCAGGTCAGCCAAAATTACCCTATAGTGCAGAACATCCAGGGG
CAAATGGTACATCAGGCCATATCACCTAGAACTTTAAATGCATGGGTAAAAGTAGTAGAA
GAGAAGGCTTTCAGCCCAGAAGTAATACCCATGTTTTCAGCATTATCAGAAGGAGCCACC
CCACAAGATTTAAACACCATGCTAAACACAGTGGGGGGACATCAAGCAGCCATGCAAATG
TTAAAAGAGACCATCAATGAGGAAGCTGCAGAATGGGATAGAGTACATCCAGTGCATGCA
GGGCCTATTGCACCAGGCCAGATGAGAGAACCAAGGGGAAGTGACATAGCAGGAACTACT
AGTACCCTTCAGGAACAAATAGGATGGATGACAAATAATCCACCTATCCCAGTAGGAGAA
ATTTATAAAAGATGGATAATCCTGGGATTAAATAAAATAGTAAGAATGTATAGCCCTACC
AGCATTCTGGACATAAGACAAGGACCAAAAGAACCTTTTAGAGACTATGTAGACCGGTTC
TATAAAACTCTAAGAGCCGAGCAAGCTTCACAGGAGGTAAAAAATTGGATGACAGAAACC
TTGTTGGTCCAAAATGCGAACCCAGATTGTAAGACTATTTTAAAAGCATTGGGACCAGCG
GCTACACTAGAAGAAATGATGACAGCATGTCAGGGAGTAGGAGGACCCGGCCATAAGGCA
AGAGTTTTGGCTGAAGCAATGAGCCAAGTAACAAATACAGCTACCATAATGATGCAGAGA
GGCAATTTTAGGAACCAAAGAAAGATGGTTAAGTGTTTCAATTGTGGCAAAGAAGGGCAC
ACAGCCAGAAATTGCAGGGCCCCTAGGAAAAAGGGCTGTTGGAAATGTGGAAAGGAAGGA
CACCAAATGAAAGATTGTACTGAGAGACAGGCTAATTTTTTAGGGAAGATCTGGCCTTCC
TACAAGGGAAGGCCAGGGAATTTTCTTCAGAGCAGACCAGAGCCAACAGCCCCACCATTT
CTTCAGAGCAGACCAGAGCCAACAGCCCCACCAGAAGAGAGCTTCAGGTCTGGGGTAGAG
ACAACAACTCCCCCTCAGAAGCAGGAGCCGATAGACAAGGAACTGTATCCTTTAACTTCC
CTCAGATCACTCTTTGGCAACGACCCCTCGTCACAATAA

1. Sarafianos SG, Das K, Clark AD Jr, Ding J, Boyer PL, Hughes SH, Arnold E: Lamivudine (3TC) resistance in HIV-1 reverse transcriptase involves steric hindrance with beta-branched amino acids. Proc Natl Acad Sci U S A. 1999 Aug 31;96(18):10027-32. [PubMed ]
2. Sluis-Cremer N, Arion D, Kaushik N, Lim H, Parniak MA: Mutational analysis of Lys65 of HIV-1 reverse transcriptase. Biochem J. 2000 May 15;348 Pt 1:77-82. [PubMed ]
3. Sarafianos SG, Clark AD Jr, Das K, Tuske S, Birktoft JJ, Ilankumaran P, Ramesha AR, Sayer JM, Jerina DM, Boyer PL, Hughes SH, Arnold E: Structures of HIV-1 reverse transcriptase with pre- and post-translocation AZTMP-terminated DNA. EMBO J. 2002 Dec 2;21(23):6614-24. [PubMed ]
4. Tachedjian G, Aronson HE, de los Santos M, Seehra J, McCoy JM, Goff SP: Role of residues in the tryptophan repeat motif for HIV-1 reverse transcriptase dimerization. J Mol Biol. 2003 Feb 14;326(2):381-96. [PubMed ]
5. Koval'skii DB, Kanibolotskii DS, Dubina VN, Korneliuk AI: [Conformational changes in HIV-1 proteinase: effect of protonation of the active center on conformation of HIV-1 proteinase in water] Ukr Biokhim Zh. 2002 Nov-Dec;74(6):135-8. [PubMed ]
6. Kohlstaedt LA, Wang J, Friedman JM, Rice PA, Steitz TA: Crystal structure at 3.5 A resolution of HIV-1 reverse transcriptase complexed with an inhibitor. Science. 1992 Jun 26;256(5065):1783-90. [PubMed ]
7. Davies JF 2nd, Hostomska Z, Hostomsky Z, Jordan SR, Matthews DA: Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase. Science. 1991 Apr 5;252(5002):88-95. [PubMed ]
8. Wohrl BM, Volkmann S, Moelling K: Mutations of a conserved residue within HIV-1 ribonuclease H affect its exo- and endonuclease activities. J Mol Biol. 1991 Aug 5;220(3):801-18. [PubMed ]
9. Jupp RA, Phylip LH, Mills JS, Le Grice SF, Kay J: Mutating P2 and P1 residues at cleavage junctions in the HIV-1 pol polyprotein. Effects on hydrolysis by HIV-1 proteinase. FEBS Lett. 1991 Jun 3;283(2):180-4. [PubMed ]
10. Erickson J, Neidhart DJ, VanDrie J, Kempf DJ, Wang XC, Norbeck DW, Plattner JJ, Rittenhouse JW, Turon M, Wideburg N, et al.: Design, activity, and 2.8 A crystal structure of a C2 symmetric inhibitor complexed to HIV-1 protease. Science. 1990 Aug 3;249(4968):527-33. [PubMed ]
11. 2476069 Mizrahi V, Lazarus GM, Miles LM, Meyers CA, Debouck C: Recombinant HIV-1 reverse transcriptase: purification, primary structure, and polymerase/ribonuclease H activities. Arch Biochem Biophys. 1989 Sep;273(2):347-58.
12. 2537531 Weber IT, Miller M, Jaskolski M, Leis J, Skalka AM, Wlodawer A: Molecular modeling of the HIV-1 protease and its substrate binding site. Science. 1989 Feb 17;243(4893):928-31.
13. 2578615 Ratner L, Haseltine W, Patarca R, Livak KJ, Starcich B, Josephs SF, Doran ER, Rafalski JA, Whitehorn EA, Baumeister K, et al.: Complete nucleotide sequence of the AIDS virus, HTLV-III. Nature. 1985 Jan 24-30;313(6000):277-84.
14. 2982104 Muesing MA, Smith DH, Cabradilla CD, Benton CV, Lasky LA, Capon DJ: Nucleic acid structure and expression of the human AIDS/lymphadenopathy retrovirus. Nature. 1985 Feb 7-13;313(6002):450-8.
15. 7532306 Rodgers DW, Gamblin SJ, Harris BA, Ray S, Culp JS, Hellmig B, Woolf DJ, Debouck C, Harrison SC: The structure of unliganded reverse transcriptase from the human immunodeficiency virus type 1. Proc Natl Acad Sci U S A. 1995 Feb 14;92(4):1222-6.
16. 7542140 Ding J, Das K, Tantillo C, Zhang W, Clark AD Jr, Jessen S, Lu X, Hsiou Y, Jacobo-Molina A, Andries K, et al.: Structure of HIV-1 reverse transcriptase in a complex with the non-nucleoside inhibitor alpha-APA R 95845 at 2.8 A resolution. Structure. 1995 Apr 15;3(4):365-79.
17. 7545077 Ding J, Das K, Moereels H, Koymans L, Andries K, Janssen PA, Hughes SH, Arnold E: Structure of HIV-1 RT/TIBO R 86183 complex reveals similarity in the binding of diverse nonnucleoside inhibitors. Nat Struct Biol. 1995 May;2(5):407-15.
18. 7552753 Eijkelenboom AP, Lutzke RA, Boelens R, Plasterk RH, Kaptein R, Hard K: The DNA-binding domain of HIV-1 integrase has an SH3-like fold. Nat Struct Biol. 1995 Sep;2(9):807-10.
19. 7613867 Priestle JP, Fassler A, Rosel J, Tintelnot-Blomley M, Strop P, Grutter MG: Comparative analysis of the X-ray structures of HIV-1 and HIV-2 proteases in complex with CGP 53820, a novel pseudosymmetric inhibitor. Structure. 1995 Apr 15;3(4):381-9.
20. 7687065 Jacobo-Molina A, Ding J, Nanni RG, Clark AD Jr, Lu X, Tantillo C, Williams RL, Kamer G, Ferris AL, Clark P, et al.: Crystal structure of human immunodeficiency virus type 1 reverse transcriptase complexed with double-stranded DNA at 3.0 A resolution shows bent DNA. Proc Natl Acad Sci U S A. 1993 Jul 1;90(13):6320-4.
21. 8805568 Hsiou Y, Ding J, Das K, Clark AD Jr, Hughes SH, Arnold E: Structure of unliganded HIV-1 reverse transcriptase at 2.7 A resolution: implications of conformational changes for polymerization and inhibition mechanisms. Structure. 1996 Jul 15;4(7):853-60.
22. 9111014 Palaniappan C, Wisniewski M, Jacques PS, Le Grice SF, Fay PJ, Bambara RA: Mutations within the primer grip region of HIV-1 reverse transcriptase result in loss of RNase H function. J Biol Chem. 1997 Apr 25;272(17):11157-64.
23. 9450540 Hong L, Zhang XJ, Foundling S, Hartsuck JA, Tang J: Structure of a G48H mutant of HIV-1 protease explains how glycine-48 replacements produce mutants resistant to inhibitor drugs. FEBS Lett. 1997 Dec 22;420(1):11-6.
24. 9533880 Gao HQ, Boyer PL, Arnold E, Hughes SH: Effects of mutations in the polymerase domain on the polymerase, RNase H and strand transfer activities of human immunodeficiency virus type 1 reverse transcriptase. J Mol Biol. 1998 Apr 3;277(3):559-72.
25. 9813120 Hsiou Y, Das K, Ding J, Clark AD Jr, Kleim JP, Rosner M, Winkler I, Riess G, Hughes SH, Arnold E: Structures of Tyr188Leu mutant and wild-type HIV-1 reverse transcriptase complexed with the non-nucleoside inhibitor HBY 097: inhibitor flexibility is a useful design feature for reducing drug resistance. J Mol Biol. 1998 Nov 27;284(2):313-23.
26. 9831551 Huang H, Chopra R, Verdine GL, Harrison SC: Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance. Science. 1998 Nov 27;282(5394):1669-75.
27. 9878383 Turner BG, Summers MF: Structural biology of HIV. J Mol Biol. 1999 Jan 8;285(1):1-32.

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

1. DMSO reductase
2. DMSOR
3. Dimethyl sulfoxide/trimethylamine N-oxide reductase precursor
4. EC 1.7.2.3

MTKFSGNELRAELYRRAFLSYSVAPGALGMFGRSLLAKGARAEALANGTVMSGSHWGVFT
ATVENGRATAFTPWEKDPHPTPMLEGVLDSIYSPTRIKYPMVRREFLEKGVNADRSTRGN
GDFVRVSWDQALDLVAAEVKRVEETYGPQGVFGGSYGWKSPGRLHNCTTLLRRMLTLAGG
YVNGAGDYSTGAAQVIMPHVVGTLEVYEQQTAWPVLAENTEVMVFWAADPIKTSQIGWVI
PEHGAYPGLEALKAKGTKVIVIDPVRTKTVEFFGADHVTPKPQTDVAIMLGMAHTLVAED
LYDKDFIANYTSGFDKFLPYLMGETDSTPKTAEWASDISGVPAETIKELARLFISKRTML
AAGWSMQRMHHGEQAHWMLVTLASMLGQIGLPGGGFGLSYHYSGGGTPSTSGPALSGITD
GGAATKGPEWLAASGASVIPVARVVDMLENPGAEFDFNGTRSKFPDVKMAYWVGGNPFVH
HQDRNRMVKAWEKLETFIVHDFQWTPTARHADIVLPATTSYERNDIETIGDYSNTGILAM
KKIVEPLYEARSDYDIFAAVAERLGKGKEFTEGKDEMGWIKSFYDDAAKQGKAGGVEMPA
FDAFWAEGIVEFPVTDGADFVRYASFREDPLLNPLGTPTGLIEIYSKNIEKMGYDDCPAH
PTWMEPLERLDGPGAKYPLHIAASHPFNRLHSQLNGTVLREGYAVQGHEPCLMHPDDAAA
RGIADGDVVRVHNDRGQILTGVKVTDAVMKGVIQIYEGGWYDPSDVTEPGTLDKYGDVNV
LSADIGTSKLAQGNCGQTVLAEVEKYTGPAVTLTGFVAPKAAE

• Molybdopterin (PF00384 )
• Molydop_binding (PF01568 )

• 1-42

• None

• Periplasm

ATGACGAAGTTTTCCGGAAACGAGCTGCGCGCAGAGCTTTACCGCCGCGCTTTCCTCAGC
TACTCGGTTGCACCGGGCGCGCTGGGCATGTTCGGCCGGTCGCTTCTGGCCAAGGGCGCC
CGCGCCGAGGCGCTGGCCAATGGCACGGTGATGTCGGGCAGCCACTGGGGCGTCTTTACC
GCGACGGTCGAAAACGGCCGCGCCACCGCCTTCACCCCCTGGGAAAAAGACCCGCATCCG
ACGCCGATGCTGGAAGGCGTGCTGGACTCGATCTATTCGCCGACGCGGATCAAATATCCG
ATGGTGCGGCGCGAATTCCTCGAAAAAGGCGTGAATGCTGATCGCTCCACCCGCGGCAAC
GGCGATTTTGTCCGCGTCAGCTGGGATCAGGCGCTCGATCTGGTCGCGGCCGAGGTCAAA
CGGGTCGAAGAGACCTACGGCCCCCAGGGCGTCTTTGGCGGCTCCTATGGCTGGAAAAGC
CCCGGGCGGCTGCACAATTGCACCACGCTTCTGCGCCGGATGCTGACGCTGGCGGGCGGC
TATGTGAACGGCGCGGGCGATTATTCGACCGGCGCGGCGCAGGTGATCATGCCGCATGTG
GTCGGCACGCTGGAAGTCTATGAACAGCAGACCGCCTGGCCGGTGCTGGCGGAAAACACC
GAAGTCATGGTGTTCTGGGCCGCCGATCCGATCAAGACATCACAAATCGGCTGGGTGATC
CCCGAACATGGCGCCTATCCGGGGCTTGAGGCGCTCAAGGCCAAGGGCACCAAGGTCATC
GTCATCGATCCGGTCCGCACCAAGACGGTCGAATTCTTCGGCGCGGATCACGTCACGCCG
AAACCGCAGACCGATGTGGCGATCATGCTGGGCATGGCGCATACGCTGGTGGCCGAAGAC
CTGTATGATAAGGACTTCATCGCCAACTACACCTCGGGCTTCGACAAGTTCCTGCCCTAT
CTGATGGGCGAGACCGACAGCACGCCGAAGACCGCCGAATGGGCGTCGGATATCAGCGGC
GTTCCGGCCGAGACGATCAAGGAACTGGCGCGGCTGTTCATCTCGAAACGCACGATGCTG
GCGGCGGGCTGGTCGATGCAGCGGATGCATCACGGCGAGCAGGCGCATTGGATGCTGGTG
ACGCTGGCCTCGATGCTGGGTCAGATCGGGCTGCCGGGCGGCGGCTTCGGGCTGTCCTAT
CACTATTCGGGCGGTGGCACGCCCTCGACGAGCGGTCCGGCGCTTTCGGGCATCACCGAT
GGCGGGGCGGCAACGAAGGGGCCGGAATGGCTGGCGGCGAGCGGCGCTTCGGTGATCCCG
GTGGCGCGCGTGGTCGACATGCTGGAAAACCCCGGCGCCGAATTCGACTTCAACGGTACG
CGGTCGAAATTCCCGGATGTGAAGATGGCCTATTGGGTTGGCGGAAACCCCTTCGTTCAC
CATCAGGACCGCAACCGCATGGTCAAGGCCTGGGAAAAACTGGAAACCTTCATCGTGCAT
GACTTCCAGTGGACGCCCACGGCGCGGCATGCCGACATCGTGCTGCCCGCGACGACCAGC
TATGAACGCAACGACATCGAGACGATCGGCGATTATTCGAACACCGGCATCCTGGCGATG
AAGAAGATCGTCGAGCCGCTTTACGAAGCCCGCAGCGATTACGACATCTTCGCCGCGGTC
GCCGAACGGCTGGGCAAGGGCAAGGAGTTCACCGAAGGCAAGGACGAGATGGGCTGGATC
AAGTCCTTCTACGACGATGCCGCCAAGCAGGGAAAGGCGGGGGGCGTCGAGATGCCCGCC
TTCGACGCCTTCTGGGCGGAAGGGATCGTGGAATTCCCGGTCACCGACGGCGCGGACTTC
GTGCGCTATGCCAGCTTCCGGGAAGATCCGCTGCTCAACCCGCTGGGCACGCCGACCGGC
CTGATCGAGATCTACTCGAAGAACATCGAGAAGATGGGCTATGACGACTGCCCGGCGCAT
CCGACCTGGATGGAACCGCTTGAACGGCTCGACGGGCCGGGGGCGAAATATCCGCTGCAC
ATCGCGGCGTCGCACCCGTTCAACCGGCTGCACTCGCAGCTCAACGGCACGGTGCTGCGC
GAAGGCTATGCGGTGCAGGGGCACGAGCCCTGCCTGATGCACCCCGACGACGCCGCCGCG
CGCGGCATCGCCGATGGCGACGTGGTGCGGGTGCACAATGATCGCGGTCAGATCCTGACC
GGGGTCAAGGTGACCGATGCGGTGATGAAGGGGGTAATCCAGATCTACGAAGGGGGCTGG
TATGATCCCTCGGACGTGACCGAGCCGGGGACGCTCGACAAATACGGCGACGTTAACGTG
CTGTCGGCCGATATCGGCACGTCGAAACTGGCGCAGGGCAACTGTGGTCAGACCGTGCTG
GCCGAGGTCGAGAAATACACCGGCCCCGCCGTCACCCTGACCGGCTTTGTGGCCCCGAAG
GCGGCGGAATAA

1. Stewart LJ, Bailey S, Bennett B, Charnock JM, Garner CD, McAlpine AS: Dimethylsulfoxide reductase: an enzyme capable of catalysis with either molybdenum or tungsten at the active site. J Mol Biol. 2000 Jun 9;299(3):593-600. [PubMed ]
2. Bray RC, Adams B, Smith AT, Bennett B, Bailey S: Reversible dissociation of thiolate ligands from molybdenum in an enzyme of the dimethyl sulfoxide reductase family. Biochemistry. 2000 Sep 19;39(37):11258-69. [PubMed ]
3. Shaw AL, Hanson GR, McEwan AG: Cloning and sequence analysis of the dimethylsulfoxide reductase structural gene from Rhodobacter capsulatus. Biochim Biophys Acta. 1996 Sep 30;1276(3):176-80. [PubMed ]
4. Knablein J, Mann K, Ehlert S, Fonstein M, Huber R, Schneider F: Isolation, cloning, sequence analysis and localization of the operon encoding dimethyl sulfoxide/trimethylamine N-oxide reductase from Rhodobacter capsulatus. J Mol Biol. 1996 Oct 18;263(1):40-52. [PubMed ]
5. Schneider F, Lowe J, Huber R, Schindelin H, Kisker C, Knablein J: Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 A resolution. J Mol Biol. 1996 Oct 18;263(1):53-69. [PubMed ]

1. EC 5.3.1.1
2. TIM
3. Triose-phosphate isomerase

APSRKFFVGGNWKMNGRKKNLGELITTLNAAKVPADTEVVCAPPTAYIDFARQKLDPKIA
VAAQNCYKVTNGAFTGEISPGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALSEG
LGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWSKVVLAYEPVWAIGTGKTATPQQ
AQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPEF
VDIINAKQ

• TIM (PF00121 )

• None

• None

1. Corran PH, Waley SG: The amino acid sequence of rabbit muscle triose phosphate isomerase. Biochem J. 1975 Feb;145(2):335-44. [PubMed ]
2. Hartman FC: Haloacetol phosphates. Characterization of the active site of rabbit muscle triose phosphate isomerase. Biochemistry. 1971 Jan 5;10(1):146-54. [PubMed ]
3. Putney SD, Herlihy WC, Schimmel P: A new troponin T and cDNA clones for 13 different muscle proteins, found by shotgun sequencing. Nature. 1983 Apr 21;302(5910):718-21. [PubMed ]
4. Sun AQ, Yuksel KU, Gracy RW: Terminal marking of triosephosphate isomerase: consequences of deamidation. Arch Biochem Biophys. 1995 Oct 1;322(2):361-8. [PubMed ]

1. EC 2.7.1.78
2. PNK
3. Polynucleotide 5'-hydroxy- kinase

MKKIILTIGCPGSGKSTWAREFIAKNPGFYNINRDDYRQSIMAHEERDEYKYTKKKEGIV
TGMQFDTAKSILYGGDSVKGVIISDTNLNPERRLAWETFAKEYGWKVEHKVFDVPWTELV
KRNSKRGTKAVPIDVLRSMYKSMREYLGLPVYNGTPGKPKAVIFDVDGTLAKMNGRGPYD
LEKCDTDVINPMVVELSKMYALMGYQIVVVSGRESGTKEDPTKYYRMTRKWVEDIAGVPL
VMQCQREQGDTRKDDVVKEEIFWKHIAPHFDVKLAIDDRTQVVEMWRRIGVECWQVASGD
F

• None

• None

ATGAAAAAGATTATTTTGACTATTGGCTGTCCTGGTTCTGGTAAGAGTACTTGGGCTCGT
GAATTTATTGCTAAGAATCCCGGGTTTTATAATATCAATCGTGATGACTATCGCCAATCT
ATTATGGCGCATGAAGAACGCGATGAGTACAAGTATACCAAAAAGAAAGAAGGTATCGTA
ACTGGTATGCAGTTTGATACAGCTAAAAGTATTCTGTACGGTGGCGATTCTGTTAAGGGA
GTAATCATTTCAGATACTAACCTGAATCCTGAACGTCGCCTAGCATGGGAAACTTTTGCC
AAAGAATACGGCTGGAAAGTTGAACATAAAGTGTTTGATGTTCCTTGGACTGAATTGGTT
AAACGTAACTCAAAACGCGGAACTAAAGCAGTACCAATTGATGTTTTACGTTCAATGTAT
AAAAGCATGCGAGAGTATCTCGGTCTTCCAGTATATAATGGGACTCCTGGTAAACCAAAA
GCAGTTATTTTTGATGTTGATGGTACACTAGCTAAAATGAATGGTCGTGGTCCTTATGAC
CTTGAAAAATGCGATACCGATGTTATCAATCCTATGGTTGTTGAACTGTCTAAGATGTAT
GCTCTTATGGGTTATCAAATCGTAGTCGTTTCAGGTCGTGAAAGTGGAACTAAAGAAGAC
CCAACGAAATATTATCGTATGACCCGTAAATGGGTTGAGGACATTGCTGGCGTTCCATTA
GTTATGCAATGTCAGCGCGAACAAGGCGATACCCGTAAAGACGATGTAGTTAAAGAAGAA
ATTTTCTGGAAACACATTGCACCGCATTTTGACGTGAAATTAGCTATTGATGACCGAACT
CAAGTAGTTGAAATGTGGCGTCGTATCGGTGTTGAATGCTGGCAAGTCGCTTCGGGAGAT
TTTTAA

1. Galburt EA, Pelletier J, Wilson G, Stoddard BL: Structure of a tRNA repair enzyme and molecular biology workhorse: T4 polynucleotide kinase. Structure. 2002 Sep;10(9):1249-60. [PubMed ]
2. Miller ES, Kutter E, Mosig G, Arisaka F, Kunisawa T, Ruger W: Bacteriophage T4 genome. Microbiol Mol Biol Rev. 2003 Mar;67(1):86-156, table of contents. [PubMed ]
3. Midgley CA, Murray NE: T4 polynucleotide kinase; cloning of the gene (pseT) and amplification of its product. EMBO J. 1985 Oct;4(10):2695-703. [PubMed ]

1. 52 kDa FK506-binding protein
2. EC 5.2.1.8
3. FKBP52 protein
4. FKBP59
5. HBI
6. HSP-binding immunophilin
7. PPIase
8. Peptidyl-prolyl cis-trans isomerase
9. Rotamase
10. p59 protein

MTAEEMKATESGAQSAPLPMEGVDISPKQDEGVLKVIKREGTGTEMPMIGDRVFVHYTGW
LLDGTKFDSSLDRKDKFSFDLGKGEVIKAWDIAIATMKVGEVCHITCKPEYAYGSAGSPP
KIPPNATLVFEVELFEFKGEDLTEEEDGGIIRRIQTRGEGYAKPNEGAIVEVALEGYYKD
KLFDQRELRFEIGEGENLDLPYGLERAIQRMEKGEHSIVYLKPSYAFGSVGKEKFQIPPN
AELKYELHLKSFEKAKESWEMNSEEKLEQSTIVKERGTVYFKEGKYKQALLQYKKIVSWL
EYESSFSNEEAQKAQALRLASHLNLAMCHLKLQAFSAAIESCNKALELDSNNEKGLFRRG
EAHLAVNDFELARADFQKVLQLYPNNKAAKTQLAVCQQRIRRQLAREKKLYANMFERLAE
EENKAKAEASSGDHPTDTEMKEEQKSNTAGSQSQVETEA

• FKBP_C (PF00254 )
• TPR_1 (PF00515 )

• None

• None

• Cytoplasm. Nucleus

ATGACAGCCGAGGAGATGAAGGCGACCGAGAGCGGGGCGCAGTCGGCGCCGCTGCCCATG
GAGGGAGTGGACATCAGCCCCAAACAGGACGAAGGCGTGCTGAAGGTCATCAAGAGAGAG
GGCACAGGTACAGAGATGCCCATGATTGGGGACCGAGTCTTTGTCCACTACACTGGCTGG
CTATTAGATGGCACAAAGTTTGACTCCAGTCTGGATCGCAAGGACAAATTCTCCTTTGAC
CTGGGAAAAGGGGAGGTCATCAAGGCTTGGGACATTGCCATAGCCACCATGAAGGTGGGG
GAGGTGTGCCACATCACCTGCAAACCAGAATATGCCTACGGTTCAGCAGGCAGTCCTCCA
AAGATTCCCCCCAATGCCACGCTTGTATTTGAGGTGGAGTTGTTTGAGTTTAAGGGAGAA
GATCTGACGGAAGAGGAAGATGGCGGAATCATTCGCAGAATACAGACTCGCGGTGAAGGC
TATGCTAAGCCCAATGAGGGTGCTATCGTGGAGGTTGCACTGGAAGGGTACTACAAGGAC
AAGCTCTTTGACCAGCGGGAGCTCCGCTTTGAGATTGGCGAGGGGGAGAACCTGGATCTG
CCTTATGGTCTGGAGAGGGCCATTCAGCGCATGGAGAAAGGAGAACATTCCATCGTGTAC
CTCAAGCCCAGCTATGCTTTTGGCAGTGTTGGGAAGGAAAAGTTCCAAATCCCACCAAAT
GCTGAGCTGAAATATGAATTACACCTCAAGAGTTTTGAAAAGGCCAAGGAGTCTTGGGAG
ATGAATTCAGAAGAGAAGCTGGAACAGAGCACCATAGTGAAAGAGCGGGGCACTGTGTAC
TTCAAGGAAGGTAAATACAAGCAAGCTTTACTACAGTATAAGAAGATCGTGTCTTGGCTG
GAATATGAGTCTAGTTTTTCCAATGAGGAAGCACAGAAAGCACAGGCCCTTCGACTGGCC
TCTCACCTCAACCTGGCCATGTGTCATCTGAAACTACAGGCCTTCTCTGCTGCCATTGAA
AGCTGTAACAAGGCCCTAGAACTGGACAGCAACAACGAGAAGGGCCTCTTCCGCCGGGGA
GAGGCCCACCTGGCCGTGAATGACTTTGAACTGGCACGGGCTGATTTCCAGAAGGTCCTG
CAGCTCTACCCCAACAACAAAGCCGCCAAGACCCAGCTGGCTGTGTGCCAGCAGCGGATC
CGAAGGCAGCTTGCCCGGGAGAAGAAGCTCTATGCCAATATGTTTGAGAGGCTGGCTGAG
GAGGAGAACAAGGCCAAGGCAGAGGCTTCCTCAGGAGACCATCCCACTGACACAGAGATG
AAGGAGGAGCAGAAGAGCAACACGGCAGGGAGCCAGTCTCAGGTGGAGACAGAAGCATAG

1. Peattie DA, Harding MW, Fleming MA, DeCenzo MT, Lippke JA, Livingston DJ, Benasutti M: Expression and characterization of human FKBP52, an immunophilin that associates with the 90-kDa heat shock protein and is a component of steroid receptor complexes. Proc Natl Acad Sci U S A. 1992 Nov 15;89(22):10974-8. [PubMed ]
2. Yem AW, Tomasselli AG, Heinrikson RL, Zurcher-Neely H, Ruff VA, Johnson RA, Deibel MR Jr: The Hsp56 component of steroid receptor complexes binds to immobilized FK506 and shows homology to FKBP-12 and FKBP-13. J Biol Chem. 1992 Feb 15;267(5):2868-71. [PubMed ]
3. Tai PK, Albers MW, Chang H, Faber LE, Schreiber SL: Association of a 59-kilodalton immunophilin with the glucocorticoid receptor complex. Science. 1992 May 29;256(5061):1315-8. [PubMed ]
4. Sanchez ER, Faber LE, Henzel WJ, Pratt WB: The 56-59-kilodalton protein identified in untransformed steroid receptor complexes is a unique protein that exists in cytosol in a complex with both the 70- and 90-kilodalton heat shock proteins. Biochemistry. 1990 May 29;29(21):5145-52. [PubMed ]