Tyrosine-protein phosphatase non-receptor type 1

Details

Name
Tyrosine-protein phosphatase non-receptor type 1
Synonyms
  • 3.1.3.48
  • Protein-tyrosine phosphatase 1B
  • PTP-1B
  • PTP1B
Gene Name
PTPN1
Organism
Humans
Amino acid sequence
>lcl|BSEQ0018983|Tyrosine-protein phosphatase non-receptor type 1
MEMEKEFEQIDKSGSWAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLH
QEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLK
CAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWP
DFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKD
PSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWKELSHEDLE
PPPEHIPPPPRPPKRILEPHNGKCREFFPNHQWVKEETQEDKDCPIKEEKGSPLNAAPYG
IESMSQDTEVRSRVVGGSLRGAQAASPAKGEPSLPEKDEDHALSYWKPFLVNMCVATVLT
AGAYLCYRFLFNSNT
Number of residues
435
Molecular Weight
49966.44
Theoretical pI
6.21
GO Classification
Functions
enzyme binding / ephrin receptor binding / poly(A) RNA binding / protein kinase binding / protein tyrosine phosphatase activity / receptor tyrosine kinase binding / zinc ion binding
Processes
actin cytoskeleton reorganization / activation of JUN kinase activity / activation of signaling protein activity involved in unfolded protein response / blood coagulation / cytokine-mediated signaling pathway / endoplasmic reticulum unfolded protein response / insulin receptor signaling pathway / interferon-gamma-mediated signaling pathway / IRE1-mediated unfolded protein response / JAK-STAT cascade involved in growth hormone signaling pathway / negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway / negative regulation of ERK1 and ERK2 cascade / negative regulation of insulin receptor signaling pathway / negative regulation of MAP kinase activity / negative regulation of PERK-mediated unfolded protein response / negative regulation of vascular endothelial growth factor receptor signaling pathway / peptidyl-tyrosine dephosphorylation / peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity / platelet activation / platelet-derived growth factor receptor-beta signaling pathway / positive regulation of IRE1-mediated unfolded protein response / positive regulation of protein tyrosine kinase activity / positive regulation of receptor catabolic process / protein dephosphorylation / regulation of endocytosis / regulation of hepatocyte growth factor receptor signaling pathway / regulation of interferon-gamma-mediated signaling pathway / regulation of intracellular protein transport / regulation of signal transduction / regulation of type I interferon-mediated signaling pathway / type I interferon signaling pathway
Components
cytoplasmic side of endoplasmic reticulum membrane / cytoplasmic vesicle / cytosol / early endosome / endoplasmic reticulum / sorting endosome
General Function
Zinc ion binding
Specific Function
Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of MET.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Endoplasmic reticulum membrane
Gene sequence
>lcl|BSEQ0018984|Tyrosine-protein phosphatase non-receptor type 1 (PTPN1)
ATGGAAGAAGCCCAAAGGAGTTACATTCTTACCCAGGGCCCTTTGCCTAACACATGCGGT
CACTTTTGGGAGATGGTGTGGGAGCAGAAAAGCAGGGGTGTCGTCATGCTCAACAGAGTG
ATGGAGAAAGGTTCGTTAAAATGCGCACAATACTGGCCACAAAAAGAAGAAAAAGAGATG
ATCTTTGAAGACACAAATTTGAAATTAACATTGATCTCTGAAGATATCAAGTCATATTAT
ACAGTGCGACAGCTAGAATTGGAAAACCTTACAACCCAAGAAACTCGAGAGATCTTACAT
TTCCACTATACCACATGGCCTGACTTTGGAGTCCCTGAATCACCAGCCTCATTCTTGAAC
TTTCTTTTCAAAGTCCGAGAGTCAGGGTCACTCAGCCCGGAGCACGGGCCCGTTGTGGTG
CACTGCAGTGCAGGCATCGGCAGGTCTGGAACCTTCTGTCTGGCTGATACCTGCCTCTTG
CTGATGGACAAGAGGAAAGACCCTTCTTCCGTTGATATCAAGAAAGTGCTGTTAGAAATG
AGGAAGTTTCGGATGGGGCTGATCCAGACAGCCGACCAGCTGCGCTTCTCCTACCTGGCT
GTGATCGAAGGTGCCAAATTCATCATGGGGGACTCTTCCGTGCAGGATCAGTGGAAGGAG
CTTTCCCACGAGGACCTGGAGCCCCCACCCGAGCATATCCCCCCACCTCCCCGGCCACCC
AAACGAATCCTGGAGCCACACAATGGGAAATGCAGGGAGTTCTTCCCAAATCACCAGTGG
GTGAAGGAAGAGACCCAGGAGGATAAAGACTGCCCCATCAAGGAAGAAAAAGGAAGCCCC
TTAAATGCCGCACCCTACGGCATCGAAAGCATGAGTCAAGACACTGAAGTTAGAAGTCGG
GTCGTGGGGGGAAGTCTTCGAGGTGCCCAGGCTGCCTCCCCAGCCAAAGGGGAGCCGTCA
CTGCCCGAGAAGGACGAGGACCATGCACTGAGTTACTGGAAGCCCTTCCTGGTCAACATG
TGCGTGGCTACGGTCCTCACGGCCGGCGCTTACCTCTGCTACAGGTTCCTGTTCAACAGC
AACACATAG
Chromosome Location
20
Locus
20q13.1-q13.2
External Identifiers
ResourceLink
UniProtKB IDP18031
UniProtKB Entry NamePTN1_HUMAN
GenBank Protein ID190742
GenBank Gene IDM31724
GenAtlas IDPTPN1
HGNC IDHGNC:9642
General References
  1. Chernoff J, Schievella AR, Jost CA, Erikson RL, Neel BG: Cloning of a cDNA for a major human protein-tyrosine-phosphatase. Proc Natl Acad Sci U S A. 1990 Apr;87(7):2735-9. [PubMed:2157211]
  2. Brown-Shimer S, Johnson KA, Lawrence JB, Johnson C, Bruskin A, Green NR, Hill DE: Molecular cloning and chromosome mapping of the human gene encoding protein phosphotyrosyl phosphatase 1B. Proc Natl Acad Sci U S A. 1990 Jul;87(13):5148-52. [PubMed:2164224]
  3. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed:11780052]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334]
  5. Charbonneau H, Tonks NK, Kumar S, Diltz CD, Harrylock M, Cool DE, Krebs EG, Fischer EH, Walsh KA: Human placenta protein-tyrosine-phosphatase: amino acid sequence and relationship to a family of receptor-like proteins. Proc Natl Acad Sci U S A. 1989 Jul;86(14):5252-6. [PubMed:2546149]
  6. Flint AJ, Gebbink MF, Franza BR Jr, Hill DE, Tonks NK: Multi-site phosphorylation of the protein tyrosine phosphatase, PTP1B: identification of cell cycle regulated and phorbol ester stimulated sites of phosphorylation. EMBO J. 1993 May;12(5):1937-46. [PubMed:8491187]
  7. Frangioni JV, Beahm PH, Shifrin V, Jost CA, Neel BG: The nontransmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence. Cell. 1992 Feb 7;68(3):545-60. [PubMed:1739967]
  8. Liu F, Chernoff J: Protein tyrosine phosphatase 1B interacts with and is tyrosine phosphorylated by the epidermal growth factor receptor. Biochem J. 1997 Oct 1;327 ( Pt 1):139-45. [PubMed:9355745]
  9. Moeslein FM, Myers MP, Landreth GE: The CLK family kinases, CLK1 and CLK2, phosphorylate and activate the tyrosine phosphatase, PTP-1B. J Biol Chem. 1999 Sep 17;274(38):26697-704. [PubMed:10480872]
  10. Ravichandran LV, Chen H, Li Y, Quon MJ: Phosphorylation of PTP1B at Ser(50) by Akt impairs its ability to dephosphorylate the insulin receptor. Mol Endocrinol. 2001 Oct;15(10):1768-80. [PubMed:11579209]
  11. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed:15592455]
  12. Sangwan V, Paliouras GN, Abella JV, Dube N, Monast A, Tremblay ML, Park M: Regulation of the Met receptor-tyrosine kinase by the protein-tyrosine phosphatase 1B and T-cell phosphatase. J Biol Chem. 2008 Dec 5;283(49):34374-83. doi: 10.1074/jbc.M805916200. Epub 2008 Sep 26. [PubMed:18819921]
  13. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. doi: 10.1016/j.molcel.2008.07.007. [PubMed:18691976]
  14. Nievergall E, Janes PW, Stegmayer C, Vail ME, Haj FG, Teng SW, Neel BG, Bastiaens PI, Lackmann M: PTP1B regulates Eph receptor function and trafficking. J Cell Biol. 2010 Dec 13;191(6):1189-203. doi: 10.1083/jcb.201005035. Epub 2010 Dec 6. [PubMed:21135139]
  15. Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal. 2010 Jan 12;3(104):ra3. doi: 10.1126/scisignal.2000475. [PubMed:20068231]
  16. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [PubMed:21269460]
  17. Krishnan N, Fu C, Pappin DJ, Tonks NK: H2S-Induced sulfhydration of the phosphatase PTP1B and its role in the endoplasmic reticulum stress response. Sci Signal. 2011 Dec 13;4(203):ra86. doi: 10.1126/scisignal.2002329. [PubMed:22169477]
  18. Rigbolt KT, Prokhorova TA, Akimov V, Henningsen J, Johansen PT, Kratchmarova I, Kassem M, Mann M, Olsen JV, Blagoev B: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Sci Signal. 2011 Mar 15;4(164):rs3. doi: 10.1126/scisignal.2001570. [PubMed:21406692]
  19. Barford D, Flint AJ, Tonks NK: Crystal structure of human protein tyrosine phosphatase 1B. Science. 1994 Mar 11;263(5152):1397-404. [PubMed:8128219]
  20. Puius YA, Zhao Y, Sullivan M, Lawrence DS, Almo SC, Zhang ZY: Identification of a second aryl phosphate-binding site in protein-tyrosine phosphatase 1B: a paradigm for inhibitor design. Proc Natl Acad Sci U S A. 1997 Dec 9;94(25):13420-5. [PubMed:9391040]
  21. Pannifer AD, Flint AJ, Tonks NK, Barford D: Visualization of the cysteinyl-phosphate intermediate of a protein-tyrosine phosphatase by x-ray crystallography. J Biol Chem. 1998 Apr 24;273(17):10454-62. [PubMed:9553104]
  22. Groves MR, Yao ZJ, Roller PP, Burke TR Jr, Barford D: Structural basis for inhibition of the protein tyrosine phosphatase 1B by phosphotyrosine peptide mimetics. Biochemistry. 1998 Dec 22;37(51):17773-83. [PubMed:9922143]
  23. Salmeen A, Andersen JN, Myers MP, Meng TC, Hinks JA, Tonks NK, Barford D: Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate. Nature. 2003 Jun 12;423(6941):769-73. [PubMed:12802338]
  24. van Montfort RL, Congreve M, Tisi D, Carr R, Jhoti H: Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B. Nature. 2003 Jun 12;423(6941):773-7. [PubMed:12802339]
  25. Ukkola O, Rankinen T, Lakka T, Leon AS, Skinner JS, Wilmore JH, Rao DC, Kesaniemi YA, Bouchard C: Protein tyrosine phosphatase 1B variant associated with fat distribution and insulin metabolism. Obes Res. 2005 May;13(5):829-34. [PubMed:15919835]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01133Tiludronic acidapproved, investigational, vet_approvedunknowninhibitorDetails
DB017343-(Oxalyl-Amino)-Naphthalene-2-Carboxylic AcidexperimentalunknownDetails
DB01820Compound 12, N-Acetyl-4-[(Carboxycarbonyl)(2-Carboxyphenyl)Amino]-N-Pentyl-1-NapthylalaniamideexperimentalunknownDetails
DB020145-(2-Fluoro-5-{(1E)-3-[3-hydroxy-2-(methoxycarbonyl)phenoxy]-1-propen-1-yl}phenyl)-1,2-oxazole-3-carboxylic acidexperimentalunknownDetails
DB020722-(Oxalyl-Amino)-4,7-Dihydro-5h-Thieno[2,3-C]Thiopyran-3-Carboxylic AcidexperimentalunknownDetails
DB022593-(3,5-Dibromo-4-Hydroxy-Benzoyl)-2-Ethyl-Benzofuran-6-Sulfonic Acid (4-Sulfamoyl-Phenyl)-AmideexperimentalunknownDetails
DB02420[[4-(Aminomethyl)Phenyl]Amino]Oxo-Acetic Acid,experimentalunknownDetails
DB024362-{4-[(2s)-2-[({[(1s)-1-Carboxy-2-Phenylethyl]Amino}Carbonyl)Amino]-3-Oxo-3-(Pentylamino)Propyl]Phenoxy}Malonic AcidexperimentalunknownDetails
DB02620Sp7343-Sp7964experimentalunknownDetails
DB026222-(Oxalyl-Amino)-Benzoic AcidexperimentalunknownDetails
DB02651{[2-(1h-1,2,3-Benzotriazol-1-Yl)-2-(3,4-Difluorophenyl)Propane-1,3-Diyl]Bis[4,1-Phenylene(Difluoromethylene)]}Bis(Phosphonic Acid)experimentalunknownDetails
DB02662Novo Nordisk a/S CompoundexperimentalunknownDetails
DB02784N-[4-(2-{2-[3-(2-Bromo-Acetylamino)-Propionylamino]-3-Hydroxy-Propionylamino}-Ethyl)-Phenyl]-Oxalamic AcidexperimentalunknownDetails
DB028277-(1,1-Dioxo-1h-Benzo[D]Isothiazol-3-Yloxymethyl)-2-(Oxalyl-Amino)-4,7-Dihydro-5h-Thieno[2,3-C]Pyran-3-Carboxylic AcidexperimentalunknownDetails
DB02977PNU177836experimentalunknownDetails
DB02615Compound 19experimentalunknownDetails
DB031022-(Oxalyl-Amino)-4,7-Dihydro-5h-Thieno[2,3-C]Pyran-3-Carboxylic AcidexperimentalunknownDetails
DB03154{[7-(Difluoro-Phosphono-Methyl)-Naphthalen-2-Yl]-Difluoro-Methyl}-Phosphonic AcidexperimentalunknownDetails
DB033113-(3,5-Dibromo-4-Hydroxy-Benzoyl)-2-Ethyl-Benzofuran-6-Sulfonic Acid [4-(Thiazol-2-Ylsulfamoyl)-Phenyl]-AmideexperimentalunknownDetails
DB034834-Benzoylamino-4-{1-{1-Carbamoyl-2-[4-(Difluoro-Phosphono-Methyl)-Phenyl]-Ethylcarbamoyl}-2-[4-(Difluoro-Phosphono-Methyl)-Phenyl]-Ethylcarbamoyl}-Butyric AcidexperimentalunknownDetails
DB03557N-{1-[5-(1-Carbamoyl-2-Mercapto-Ethylcarbamoyl)-Pentylcarbamoyl]-2-[4-(Difluoro-Phosphono-Methyl)-Phenyl]-Ethyl}-3-{2-[4-(Difluoro-Phosphono-Methyl)-Phenyl]-Acetylamino}-Succinamic AcidexperimentalunknownDetails
DB03661Cysteinesulfonic AcidexperimentalunknownDetails
DB036702-(Oxalyl-Amino)-4,5,6,7-Tetrahydro-Thieno[2,3-C]Pyridine-3-Carboxylic AcidexperimentalunknownDetails
DB037144-Carbamoyl-4-{[6-(Difluoro-Phosphono-Methyl)-Naphthalene-2-Carbonyl]-Amino}-Butyric AcidexperimentalunknownDetails
DB03982Compound 5, 2-(Naphthalen-1-Yl-Oxalyl-Amino)-BenzoicacidexperimentalunknownDetails
DB040016-(Oxalyl-Amino)-1h-Indole-5-Carboxylic AcidexperimentalunknownDetails
DB040882-[{4-[(2S)-2-{[(Allyloxy)carbonyl]amino}-3-({4-[3-hydroxy-2-(methoxycarbonyl)phenoxy]butyl}amino)-3-oxopropyl]phenyl}(carboxycarbonyl)amino]benzoic acidexperimentalunknownDetails
DB041423-(3,5-Dibromo-4-Hydroxy-Benzoyl)-2-Ethyl-Benzofuran-6-Sulfonic Acid DimethylamideexperimentalunknownDetails
DB04204[(4-{4-[4-(Difluoro-Phosphono-Methyl)-Phenyl]-Butyl}-Phenyl)-Difluoro-Methyl]-Phosphonic AcidexperimentalunknownDetails
DB04285{4-[(2s,4e)-2-(1,3-Benzothiazol-2-Yl)-2-(1h-1,2,3-Benzotriazol-1-Yl)-5-Phenylpent-4-Enyl]Phenyl}(Difluoro)Methylphosphonic AcidexperimentalunknownDetails
DB045252-(Carboxymethoxy)-5-[(2s)-2-({(2s)-2-[(3-Carboxypropanoyl)Amino] -3-Phenylpropanoyl}Amino)-3-Oxo-3-(Pentylamino)Propyl]Benzoic AcidexperimentalunknownDetails
DB048001-METHYL-3-PHENYL-1H-PYRAZOL-5-YLSULFAMIC ACIDexperimentalunknownDetails
DB05506ISIS 113715investigationalunknownDetails
DB06333TrodusquemineinvestigationalunknownDetails
DB06521ErtiprotafibinvestigationalunknownDetails
DB068294-BROMO-3-(CARBOXYMETHOXY)-5-[3-(CYCLOHEXYLAMINO)PHENYL]THIOPHENE-2-CARBOXYLIC ACIDexperimentalunknownDetails
DB06887[(3S)-3-(Methylcarbamoyl)-2-{[(2-methyl-2-propanyl)oxy]carbonyl}-1,2,3,4-tetrahydro-7-isoquinolinyl]sulfamic acidexperimentalunknownDetails
DB071304-BROMO-3-(CARBOXYMETHOXY)-5-PHENYLTHIOPHENE-2-CARBOXYLIC ACIDexperimentalunknownDetails
DB071345-(4-CHLORO-5-PHENYL-3-THIENYL)-1,2,5-THIADIAZOLIDIN-3-ONE 1,1-DIOXIDEexperimentalunknownDetails
DB071974-BROMO-3-(CARBOXYMETHOXY)-5-(4-HYDROXYPHENYL)THIOPHENE-2-CARBOXYLIC ACIDexperimentalunknownDetails
DB07263[{2-bromo-4-[(2R)-3-oxo-2,3-diphenylpropyl]phenyl}(difluoro)methyl]phosphonic acidexperimentalunknownDetails
DB072895-[3-(BENZYLAMINO)PHENYL]-4-BROMO-3-(CARBOXYMETHOXY)THIOPHENE-2-CARBOXYLIC ACIDexperimentalunknownDetails
DB072952-[(7-HYDROXY-NAPHTHALEN-1-YL)-OXALYL-AMINO]-BENZOIC ACIDexperimentalunknownDetails
DB072983-(CARBOXYMETHOXY)THIENO[2,3-B]PYRIDINE-2-CARBOXYLIC ACIDexperimentalunknownDetails
DB074804-PHOSPHONOOXY-PHENYL-METHYL-[4-PHOSPHONOOXY]BENZENexperimentalunknownDetails
DB07651N-ACETYL-L-PHENYLALANYL-4-[DIFLUORO(PHOSPHONO)METHYL]-L-PHENYLALANINAMIDEexperimentalunknownDetails
DB07719[(3R)-3-(Methylcarbamoyl)-2-{[(2-methyl-2-propanyl)oxy]carbonyl}-1,2,3,4-tetrahydro-7-isoquinolinyl]sulfamic acidexperimentalunknownDetails
DB077305-(3-HYDROXYPHENYL)ISOTHIAZOL-3(2H)-ONE 1,1-DIOXIDEexperimentalunknownDetails
DB080015-(3-{3-[3-HYDROXY-2-(METHOXYCARBONYL)PHENOXY]PROPENYL}PHENYL)-4-(HYDROXYMETHYL)ISOXAZOLE-3-CARBOXYLIC ACIDexperimentalunknownDetails
DB08003ISOTHIAZOLIDINONE ANALOGexperimentalunknownDetails
DB081474-[3-(dibenzylamino)phenyl]-2,4-dioxobutanoic acidexperimentalunknownDetails
DB08371PARA-(BENZOYL)-PHENYLALANINEexperimentalunknownDetails
DB083976-(DIFLUORO-PHOSPHONO-METHYL)-NAPHTHALENE-2-CARBOXYLIC ACIDexperimentalunknownDetails
DB08549(3R)-METHYLCARBAMOYL-7-SULFOAMINO-3,4-DIHYDRO-1H-ISOQUINOLINE-2-CARBOXYLIC ACID BENZYL ESTERexperimentalunknownDetails
DB085915-(4-METHOXYBIPHENYL-3-YL)-1,2,5-THIADIAZOLIDIN-3-ONE 1,1-DIOXIDEexperimentalunknownDetails
DB085931,2,5-THIADIAZOLIDIN-3-ONE-1,1-DIOXIDEexperimentalunknownDetails
DB08783(4-{(2S)-2-[(tert-butoxycarbonyl)amino]-3-methoxy-3-oxopropyl}phenyl)methaneseleninic acidexperimentalunknownDetails