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Showing drug card for Vitamin C (DB00126)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-04-16 16:47:25
Primary Accession Number DB00126
Secondary Accession Number
  • APRD00084
  • EXPT00568
  • NUTR00001
Name Vitamin C
Drug Type
  • Approved
  • Nutraceutical
  • Small Molecule
Description A six carbon compound related to glucose. It is found naturally in citrus fruits and many vegetables. Ascorbic acid is an essential nutrient in human diets, and necessary to maintain connective tissue and bone. Its biologically active form, vitamin C, functions as a reducing agent and coenzyme in several metabolic pathways. Vitamin C is considered an antioxidant. [PubChem]
Synonyms
  1. AA
  2. Ascorbate
  3. Ascorbic Acid
  4. L-Ascorbate
  5. L-Ascorbic Acid
  6. L-Lyxoascorbic Acid
  7. L-Xyloascorbic Acid
Brand Names
  1. Adenex
  2. Allercorb
  3. Antiscorbic Vitamin
  4. Antiscorbutic Vitamin
  5. Arco-Cee
  6. Ascoltin
  7. Ascor-B.I.D.
  8. Ascorb
  9. Ascorbajen
  10. Ascorbicab
  11. Ascorbicap
  12. Ascorbicin
  13. Ascorbin
  14. Ascorbutina
  15. Ascorin
  16. Ascorteal
  17. Ascorvit
  18. C-Level
  19. C-Long
  20. C-Quin
  21. C-Span
  22. C-Vimin
  23. Cantan
  24. Cantaxin
  25. Catavin C
  26. Ce Lent
  27. Cebicure
  28. Cebid
  29. Cebion
  30. Cebione
  31. Cecon
  32. Cee-Caps Td
  33. Cee-Vite
  34. Cegiolan
  35. Ceglion
  36. Celaskon
  37. Celin
  38. Cemagyl
  39. Cemill
  40. Cenetone
  41. Cenolate
  42. Cereon
  43. Cergona
  44. Cescorbat
  45. Cetamid
  46. Cetane
  47. Cetane-Caps Tc
  48. Cetane-Caps Td
  49. Cetebe
  50. Cetemican
  51. Cevalin
  52. Cevatine
  53. Cevex
  54. Cevi-Bid
  55. Cevimin
  56. Cevital
  57. Cevitamic Acid
  58. Cevitamin
  59. Cevitan
  60. Cevitex
  61. Cewin
  62. Ciamin
  63. Cipca
  64. Citriscorb
  65. Colascor
  66. Concemin
  67. Davitamon C
  68. Duoscorb
  69. Hicee
  70. Hybrin
  71. IDO-C
  72. Kyselina Askorbova
  73. Laroscorbine
  74. Lemascorb
  75. Liqui-Cee
  76. Meri-C
  77. Natrascorb
  78. Planavit C
  79. Proscorbin
  80. Redoxon
  81. Ribena
  82. Roscorbic
  83. Scorbacid
  84. Scorbu-C
  85. Secorbate
  86. Sodascorbate
  87. Testascorbic
  88. Vicelat
  89. Vicin
  90. Vicomin C
  91. Viforcit
  92. Viscorin
  93. Vitace
  94. Vitacee
  95. Vitacimin
  96. Vitacin
  97. Vitamisin
  98. Vitascorbol
  99. Xitix
Brand Mixtures Not Available
Chemical IUPAC Name (2R)-2-[(1S)-1,2-dihydroxyethyl]-4,5-dihydroxyfuran-3-one
Chemical Formula C6H8O6
Chemical Structure Structure
CAS Registry Number 50-81-7
InChI Identifier InChI=1/C6H8O6/c7-1-2(8)5-3(9)4(10)6(11)12-5/h2,5,7-8,10-11H,1H2/t2-,5+/m0/s1
InChI Key TYQCGQRIZGCHNB-JLAZNSOCBA
KEGG Drug D00018 Link Image
KEGG Compound C00072 Link Image
PubChem Compound 5785 Link Image
PubChem Substance 597821 Link Image
ChEBI ID 17208 Link Image
PharmGKB ID PA451898 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 00583960 Link Image
RxList Link http://www.rxlist.com/cgi/generic3/vitamc.htm Link Image
PDRhealth Link http://www.pdrhealth.com/drug_info/nmdrugprofiles/nutsupdrugs/vit_0264.shtml Link Image
Wikipedia Link http://en.wikipedia.org/wiki/Vitamin_C Link Image
FDA Label Not Available
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 176.1241
Monoisotopic Molecular Weight 176.0321
State Solid
Melting Point 191 oC
Experimental Water Solubility 40 g/L Source: PhysProp
Predicted Water Solubility 2.57e+02 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity -0.5 Source: PhysProp
Predicted LogP -1.86 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS 0.16 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point 4.7
Mass Spectrum Not Available
MOL File Show Link Image | Download Link Image
SDF File Show Link Image | Download Link Image
PDB File Show Link Image | Download Link Image
2D Structure
3D Structure
Experimental PDB ID 1F9G Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES OC[C@H](O)[C@H]1OC(O)=C(O)C1=O
Canonical SMILES OCC(O)C1OC(O)=C(O)C1=O
Drug Category
  • Antioxidants
  • Essential Vitamins
  • Free Radical Scavengers
  • Vitamins
  • Vitamins (Vitamin C)
ATC Codes
AHFS Codes
  • 88:04.00
  • 88:12.00
Indication Used to treat vitamin C deficiency, scurvy, delayed wound and bone healing, urine acidification, and in general as an antioxidant. It has also been suggested to be an effective antiviral agent.
Pharmacology Ascorbic Acid (vitamin C) is a water-soluble vitamin indicated for the prevention and treatment of scurvy, as ascorbic acid deficiency results in scurvy. Collagenous structures are primarily affected, and lesions develop in bones and blood vessels. Administration of ascorbic acid completely reverses the symptoms of ascorbic acid deficiency.
Mechanism of Action In humans, an exogenous source of ascorbic acid is required for collagen formation and tissue repair by acting as a cofactor in the posttranslational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins. Ascorbic acid is reversibly oxidized to dehydroascorbic acid in the body. These two forms of the vitamin are believed to be important in oxidation-reduction reactions. The vitamin is involved in tyrosine metabolism, conversion of folic acid to folinic acid, carbohydrate metabolism, synthesis of lipids and proteins, iron metabolism, resistance to infections, and cellular respiration.
Absorption 70% to 90%
Toxicity Not Available
Protein Binding 25%
Biotransformation Hepatic. Ascorbic acid is reversibly oxidised (by removal of the hydrogen from the enediol group of ascorbic acid) to dehydroascorbic acid. The two forms found in body fluids are physiologically active. Some ascorbic acid is metabolized to inactive compounds including ascorbic acid-2-sulfate and oxalic acid.
Half Life 16 days (3.4 hours in people who have excess levels of vitamin C)
Dosage Forms
Form Route
Bar, chewable Oral
Capsule Oral
Capsule, extended release Oral
Granule Oral
Liquid Intravenous
Liquid Oral
Lozenge Oral
Powder Oral
Powder, for solution Oral
Solution Intramuscular
Solution Intravenous
Solution Oral
Solution / drops Oral
Tablet Oral
Tablet, chewable Oral
Tablet, effervescent Oral
Tablet, extended release Oral
Wafer Oral
Patient Information Not Available
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions Not Available
Food Interactions Not Available
Pathways Not Available
General References
  1. Banhegyi G, Mandl J: The hepatic glycogenoreticular system. Pathol Oncol Res. 2001;7(2):107-10. [PubMed Link Image]
  2. Padayatty SJ, Katz A, Wang Y, Eck P, Kwon O, Lee JH, Chen S, Corpe C, Dutta A, Dutta SK, Levine M: Vitamin C as an antioxidant: evaluation of its role in disease prevention. J Am Coll Nutr. 2003 Feb;22(1):18-35. [PubMed Link Image]
  3. Englard S, Seifter S: The biochemical functions of ascorbic acid. Annu Rev Nutr. 1986;6:365-406. [PubMed Link Image]
  4. Proctor P: Similar functions of uric acid and ascorbate in man? Nature. 1970 Nov 28;228(5274):868. [PubMed Link Image]
  5. Meister A: Glutathione-ascorbic acid antioxidant system in animals. J Biol Chem. 1994 Apr 1;269(13):9397-400. [PubMed Link Image]
  6. Drugs.com Link Image
  7. Wikipedia Link Image
  8. RxList Link Image
  9. PDRhealth Link Image
Organisms Affected
  • Humans and other mammals
Targets
  1. Prolyl 4-hydroxylase subunit alpha-1
  2. Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1
  3. Dopamine beta-hydroxylase
  4. Solute carrier family 23 member 1
  5. DNA
  6. Xylose isomerase
  7. Hyaluronate lyase
  8. Phytanoyl-CoA dioxygenase, peroxisomal
  9. Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2
  10. Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3
  11. Gamma-butyrobetaine dioxygenase
  12. Peptidyl-glycine alpha-amidating monooxygenase
  13. Prolyl 3-hydroxylase 1
  14. Hypothetical protein DKFZp686H15154
  15. Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2
  16. Prolyl 3-hydroxylase 2
  17. Prolyl 3-hydroxylase 3
  18. 2-oxoglutarate and iron-dependent oxygenase domain containing 1
  19. Egl nine homolog 2
  20. Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3
  21. Jumonji/ARID domain-containing protein 1D
  22. Egl nine homolog 1
  23. Egl nine homolog 3
  24. Trimethyllysine dioxygenase, mitochondrial
  25. Putative HIF-prolyl hydroxylase PH-4
  26. Myrosinase MA1
  27. Ascorbate peroxidase
Drug Target 1 [top]
Target 1 ID 67
Target 1 Name Prolyl 4-hydroxylase subunit alpha-1
Target 1 Synonyms
  1. 4-PH alpha-1
  2. EC 1.14.11.2
  3. Procollagen-proline,2-oxoglutarate-4-dioxygenase alpha-1 subunit
  4. Prolyl 4-hydroxylase subunit alpha-1 precursor
Target 1 Gene Name P4HA1
Target 1 Protein Sequence >Prolyl 4-hydroxylase alpha-1 subunit precursor
MIWYILIIGILLPQSLAHPGFFTSIGQMTDLIHTEKDLVTSLKDYIKAEEDKLEQIKKWA
EKLDRLTSTATKDPEGFVGHPVNAFKLMKRLNTEWSELENLVLKDMSDGFISNLTIQRQY
FPNDEDQVGAAKALLRLQDTYNLDTDTISKGNLPGVKHKSFLTAEDCFELGKVAYTEADY
YHTELWMEQALRQLDEGEISTIDKVSVLDYLSYAVYQQGDLDKALLLTKKLLELDPEHQR
ANGNLKYFEYIMAKEKDVNKSASDDQSDQKTTPKKKGVAVDYLPERQKYEMLCRGEGIKM
TPRRQKKLFCRYHDGNRNPKFILAPAKQEDEWDKPRIIRFHDIISDAEIEIVKDLAKPRL
RRATISNPITGDLETVHYRISKSAWLSGYENPVVSRINMRIQDLTGLDVSTAEELQVANY
GVGGQYEPHFDFARKDEPDAFKELGTGNRIATWLFYMSDVSAGGATVFPEVGASVWPKKG
TAVFWYNLFASGEGDYSTRHAACPVLVGNKWVSNKWLHERGQEFRRPCTLSELE
Target 1 Number of Residues 542
Target 1 Molecular Weight 61050
Target 1 Theoretical pI 5.84
Target 1 GO Classification
Function
binding
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Process
physiological process
metabolism
macromolecule metabolism
protein metabolism
Component
Not Available
Target 1 General Function Involved in oxidoreductase activity
Target 1 Specific Function Catalyzes the posttranslational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins
Target 1 Pathways
Name SMPDB Link KEGG Link
Arginine and proline metabolism SMP00020 Link Image map00330 Link Image
Target 1 Reactions
  • procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2
Target 1 Pfam Domain Function
Target 1 Signals
  • 1-17
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 190786 Link Image
Target 1 UniProtKB/Swiss-Prot ID P13674 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name P4HA1_HUMAN Link Image
Target 1 PDB ID 1TJC Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location
  • Endoplasmic reticulum
  • endoplasmic reticulum lumen
Target 1 Gene Sequence >1605 bp
ATGATCTGGTATATATTAATTATAGGAATTCTGCTTCCCCAGTCTTTGGCTCATCCAGGC
TTTTTTACTTCAATTGGTCAGATGACTGATTTGATCCATACTGAGAAAGATCTGGTGACT
TCTCTGAAAGATTATATTAAGGCAGAAGAGGACAAGTTAGAACAAATAAAAAAATGGGCA
GAGAAGTTAGATCGGCTAACTAGTACAGCGACAAAAGATCCAGAAGGATTTGTTGGGCAT
CCAGTAAATGCATTCAAATTAATGAAACGTCTGAATACTGAGTGGAGTGAGTTGGAGAAT
CTGGTCCTTAAGGATATGTCAGATGGCTTTATCTCTAACCTAACCATTCAGAGACCAGTA
CTTTCTAATGATGAAGATCAGGTTGGGGCAGCCAAAGCTCTGTTACGTCTCCAGGATACC
TACAATTTGGATACAGATACCATCTCAAAGGGTAATCTTCCAGGAGTGAAACACAAATCT
TTTCTAACGGCTGAGGACTGCTTTGAGTTGGGCAAAGTGGCCTATACAGAAGCAGATTAT
TACCATACGGAACTGTGGATGGAACAAGCCCTAAGGCAACTGGATGAAGGCGAGATTTCT
ACCATAGATAAAGTCTCTGTTCTAGATTATTTGAGCTATGCGGTATATCAGCAGGGAGAC
CTGGATAAGGCACTTTTGCTCACAAAGAAGCTTCTTGAACTAGATCCTGAACATCAGAGA
GCTAATGGTAACTTAAAATATTTTGAGTATATAATGGCTAAAGAAAAAGATGTCAATAAG
TCTGCTTCAGATGACCAATCTGATCAGAAAACTACACCAAAGAAAAAAGGGGTTGCTGTG
GATTACCTGCCAGAGAGACAGAAGTACGAAATGCTGTGCCGTGGGGAGGGTATCAAAATG
ACCCCTCGGAGACAGAAAAAACTCTTTTGCCGCTACCATGATGGAAACCGTAATCCTAAA
TTTATTCTGGCTCCAGCTAAACAGGAGGATGAATGGGACAAGCCTCGTATTATTCGCTTC
CATGATATTATTTCTGATGCAGAAATTGAAATCGTCAAAGACCTAGCAAAACCAAGGCTG
AGCCGAGCTACAGTACATGACCCTGAGACTGGAAAATTGACCACAGCACAGTACAGAGTA
TCTAAGAGTGCCTGGCTCTCTGGCTATGAAAATCCTGTGGTGTCTCGAATTAATATGAGA
ATACAAGATCTAACAGGACTAGATGTTTCCACAGCAGAGGAATTACAGGTAGCAAATTAT
GGAGTTGGAGGACAGTATGAACCCCATTTTGACTTTGCACGGAAAGATGAGCCAGATGCT
TTCAAAGAGCTGGGGACAGGAAATAGAATTGCTACATGGCTGTTTTATATGAGTGATGTG
TCTGCAGGAGGAGCCACTGTTTTTCCTGAAGTTGGAGCTAGTGTTTGGCCCAAAAAAGGA
ACTGCTGTTTTCTGGTATAATCTGTTTGCCAGTGGAGAAGGAGATTATAGTACACGGCAT
GCAGCCTGTCCAGTGCTAGTTGGCAACAAATGGGTATCCAATAAATGGCTCCATGAACGT
GGACAAGAATTTCGAAGACCTTGTACGTTGTCAGAATTGGAATGA
Target 1 GenBank Gene ID
Target 1 GeneCard ID P4HA1 Link Image
Target 1 GenAtlas ID P4HA1 Link Image
Target 1 HGNC ID HGNC:8546 Link Image
Target 1 Chromosome Location 10
Target 1 Locus 10q21.3-q23.1
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Helaakoski T, Vuori K, Myllyla R, Kivirikko KI, Pihlajaniemi T: Molecular cloning of the alpha-subunit of human prolyl 4-hydroxylase: the complete cDNA-derived amino acid sequence and evidence for alternative splicing of RNA transcripts. Proc Natl Acad Sci U S A. 1989 Jun;86(12):4392-6. [PubMed Link Image]
  2. Helaakoski T, Veijola J, Vuori K, Rehn M, Chow LT, Taillon-Miller P, Kivirikko KI, Pihlajaniemi T: Structure and expression of the human gene for the alpha subunit of prolyl 4-hydroxylase. The two alternatively spliced types of mRNA correspond to two homologous exons the sequences of which are expressed in a variety of tissues. J Biol Chem. 1994 Nov 11;269(45):27847-54. [PubMed Link Image]
Target 1 Drug References
  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 Link Image]
  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 Link Image]
Drug Target 2 [top]
Target 2 ID 97
Target 2 Name Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1
Target 2 Synonyms
  1. EC 1.14.11.4
  2. LH1
  3. Lysyl hydroxylase 1
  4. Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 precursor
Target 2 Gene Name PLOD1
Target 2 Protein Sequence >Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 precursor
MRPLLLLALLGWLLLAEAKGDAKPEDNLLVLTVATKETEGFRRFKRSAQFFNYKIQALGL
GEDWNVEKGTSAGGGQKVRLLKKALEKHADKEDLVILFADSYDVLFASGPRELLKKFRQA
RSQVVFSAEELIYPDRRLETKYPVVSDGKRFLGSGGFIGYAPNLSKLVAEWEGQDSDSDQ
LFYTKIFLDPEKREQINITLDHRCRIFQNLDGALDEVVLKFEMGHVRARNLAYDTLPVLI
HGNGPTKLQLNYLGNYIPRFWTFETGCTVCDEGLRSLKGIGDEALPTVLVGVFIEQPTPF
VSLFFQRLLRLHYPQKHMRLFIHNHEQHHKAQVEEFLAQHGSEYQSVKLVGPEVRMANAD
ARNMGADLCRQDRSCTYYFSVDADVALTEPNSLRLLIQQNKNVIAPLMTRHGRLWSNFWG
ALSADGYYARSEDYVDIVQGRRVGVWNVPYISNIYLIKGSALRGELQSSDLFHHSKLDPD
MAFCANIRQQDVFMFLTNRHTLGHLLSLDSYRTTHLHNDLWEVFSNPEDWKEKYIHQNYT
KALAGKLVETPCPDVYWFPIFTEVACDELVEEMEHFGQWSLGNNKDNRIQGGYENVPTID
IHMNQIGFEREWHKFLLEYIAPMTEKLYPGYYTRAQFDLAFVVRYKPDEQPSLMPHHDAS
TFTINIALNRVGVDYEGGGCRFLRYNCSIRAPRKGWTLMHPGRLTHYHEGLPTTRGTRYI
AVSFVDP
Target 2 Number of Residues 739
Target 2 Molecular Weight 83551
Target 2 Theoretical pI 6.94
Target 2 GO Classification
Function
procollagen-lysine 5-dioxygenase activity
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Process
physiological process
metabolism
macromolecule metabolism
protein metabolism
Component
organelle
membrane-bound organelle
intracellular membrane-bound organelle
endoplasmic reticulum
Target 2 General Function Involved in oxidoreductase activity
Target 2 Specific Function Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links
Target 2 Pathways
Name SMPDB Link KEGG Link
Lysine degradation SMP00037 Link Image map00310 Link Image
Target 2 Reactions
  • procollagen L-lysine + 2-oxoglutarate + O2 = procollagen 5-hydroxy-L-lysine + succinate + CO2 ALL_REAC (other) R03376
Target 2 Pfam Domain Function
Target 2 Signals
  • 1-18
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 190074 Link Image
Target 2 UniProtKB/Swiss-Prot ID Q02809 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name PLOD1_HUMAN Link Image
Target 2 PDB ID Not Available
Target 2 Cellular Location
  • Endoplasmic reticulum
  • peripheral
  • rough endoplasmic reticulum
  • rough endoplasmic reticulum membrane
Target 2 Gene Sequence >2184 bp
ATGCGGCCCCTGCTGCTACTGGCCCTGCTGGGCTGGCTGCTGCTGGCCGAAGCGAAGGGC
GACGCCAAGCCGGAGGACAACCTTTTAGTCCTCACGGTGGCCACTAAGGAGACCGAGGGA
TTCCGTCGCTTCAAGCGCTCAGCTCAGTTCTTCAACTACAAGATCCAGGCGCTTGGCCTA
GGGGAGGACTGGAATGTGGAGAAGGGGACGTCGGCAGGTGGAGGGCAGAAGGTCCGGCTG
CTGAAGAAAGCTCTGGAGAAGCACGCAGACAAGGAGGATCTGGTCATTCTCTTCACAGAC
AGCTATGACGTGCTGTTTGCATCGGGGCCCCGGGAGCTCCTGAAGAAGTTCCGGCAGGCC
AGGAGCCAGGTGGTCTTCTCTGCTGAGGAGCTCATCTACCCAGACCGCAGGCTGGAGACC
AAGTATCCGGTGGTGTCCGATGGCAAGAGGTTCCTGGGCTCTGGAGGCTTCATCGGTTAT
GCCCCCAACCTCAGCAAACTGGTGGCCGAGTGGGAGGGCCAGGACAGCGACAGCGATCAG
CTGTTTTACACCAAGATCTTCTTGGACCCGGAGAAGAGGGAGCAGATCAATATCACCCTG
GACCACCGCTGCCGTATCTTCCAGAACCTGGATGGAGCCTTGGATGAGGTCGTGCTCAAG
TTTGAAATGGGCCATGTGAGAGCGAGGAACCTGGCCTATGACACCCTCCCGGTCCTGATC
CATGGCAACGGGCCAACCAAGCTGCAGTTGAACTACCTGGGCAACTACATCCCGCGCTTC
TGGACCTTCGAAACAGGCTGCACCGTGTGTGACGAAGGCTTGCGCAGCCTCAAGGGCATT
GGGGATGAAGCTCTGCCCACGGTCCTGGTCGGCGTGTTCATCGAACAGCCCACGCCGTTT
GTGTCCCTGTTCTTCCAGCGGCTCCTGCGGCTCCACTACCCCCAGAAACACATGCGACTT
TTCATCCACAACCACGAGCAGCACCACAAGGCTCAGGTGGAAGAGTTCCTGGCACAGCAT
GGCAGCGAGTACCAGTCTGTGAAGCTGGTGGGCCCTGAGGTGCGGATGGCGAATGCAGAT
GCCAGGAACATGGGCGCAGACCTGTGCCGGCAGGACCGCAGCTGCACCTACTACTTCAGC
GTGGATGCTGACGTGGCCCTGACCGAGCCCAACAGCCTGCGGCTGCTGATCCAACAGAAC
AAGAATGTCATTGCCCCGCTGATGACCCGGCATGGGAGGCTGTGGTCGAACTTCTGGGGG
GCTCTCAGTGCAGATGGCTACTATGCCCGTTCCGAGGACTACGTGGACATTGTGCAGGGG
CGGCGTGTTGGTGTCTGGAATGTGCCCTATATTTCAAACATCTACTTGATCAAGGGCAGT
GCCCTGCGGGGTGAGCTGCAGTCCTCAGATCTCTTCCACCACAGCAAGCTGGACCCCGAC
ATGGCCTTCTGTGCCAACATCCGGCAGCAGGATGTGTTCATGTTCCTGACCAACCGGCAC
ACCCTTGGCCATCTGCTCTCCCTAGACAGCTACCGCACCACCCACCTGCACAACGACCTC
TGGGAGGTGTTCAGCAACCCCGAGGACTGGAAGGAGAAGTACATCCACCAGAACTACACC
AAAGCCCTGGCAGGGAAGCTGGTGGAGACGCCCTGCCCGGATGTCTATTGGTTCCCCATC
TTCACGGAGGTGGCCTGTGATGAGCTGGTGGAGGAGATGGAGCACTTTGGCCAGTGGTCT
CTGGGCAACAACAAGGACAACCGCATCCAGGGTGGCTACGAGAACGTGCCGACTATTGAC
ATCCACATGAACCAGATCGGCTTTGAGCGGGAGTGGCACAAATTCCTGCTGGAGTACATT
GCGCCCATGACGGAGAAGCTCTACCCCGGCTACTACACCAGGGCCCAGTTTGACCTGGCC
TTTGTCGTCCGCTACAAGCCTGATGAGCAGCCCTCACTGATGCCACACCATGATGCCTCC
ACCTTCACCATCAACATCGCCCTGAACCGAGTCGGGGTGGATTACGAGGGCGGGGGCTGT
CGGTTCCTGCGCTACAACTGTTCCATCCGAGCCCCAAGGAAGGGCTGGACCCTCATGCAC
CCTGGACGACTCACGCATTACCATGAGGGGCTCCCCACCACCAGGGGCACCCGCTACATC
GCAGTCTCCTTCGTCGATCCCTAA
Target 2 GenBank Gene ID
Target 2 GeneCard ID PLOD1 Link Image
Target 2 GenAtlas ID PLOD1 Link Image
Target 2 HGNC ID HGNC:9081 Link Image
Target 2 Chromosome Location 1
Target 2 Locus 1p36.3-p36.2
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Yeowell HN, Allen JD, Walker LC, Overstreet MA, Murad S, Thai SF: Deletion of cysteine 369 in lysyl hydroxylase 1 eliminates enzyme activity and causes Ehlers-Danlos syndrome type VI. Matrix Biol. 2000 Feb;19(1):37-46. [PubMed Link Image]
  2. Hautala T, Byers MG, Eddy RL, Shows TB, Kivirikko KI, Myllyla R: Cloning of human lysyl hydroxylase: complete cDNA-derived amino acid sequence and assignment of the gene (PLOD) to chromosome 1p36.3----p36.2. Genomics. 1992 May;13(1):62-9. [PubMed Link Image]
  3. Heikkinen J, Hautala T, Kivirikko KI, Myllyla R: Structure and expression of the human lysyl hydroxylase gene (PLOD): introns 9 and 16 contain Alu sequences at the sites of recombination in Ehlers-Danlos syndrome type VI patients. Genomics. 1994 Dec;24(3):464-71. [PubMed Link Image]
  4. Ha VT, Marshall MK, Elsas LJ, Pinnell SR, Yeowell HN: A patient with Ehlers-Danlos syndrome type VI is a compound heterozygote for mutations in the lysyl hydroxylase gene. J Clin Invest. 1994 Apr;93(4):1716-21. [PubMed Link Image]
  5. Pirskanen A, Kaimio AM, Myllyla R, Kivirikko KI: Site-directed mutagenesis of human lysyl hydroxylase expressed in insect cells. Identification of histidine residues and an aspartic acid residue critical for catalytic activity. J Biol Chem. 1996 Apr 19;271(16):9398-402. [PubMed Link Image]
  6. Brinckmann J, Acil Y, Feshchenko S, Katzer E, Brenner R, Kulozik A, Kugler S: Ehlers-Danlos syndrome type VI: lysyl hydroxylase deficiency due to a novel point mutation (W612C). Arch Dermatol Res. 1998 Apr;290(4):181-6. [PubMed Link Image]
Target 2 Drug References
  1. Salavoura K, Valari M, Kolialexi A, Mavrou A, Kitsiou S: A case of Ehlers Danlos syndrome type VI. Genet Couns. 2006;17(3):291-4. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 153
Target 3 Name Dopamine beta-hydroxylase
Target 3 Synonyms
  1. Dopamine beta- monooxygenase
  2. Dopamine beta-hydroxylase precursor
  3. EC 1.14.17.1
Target 3 Gene Name DBH
Target 3 Protein Sequence >Dopamine beta-hydroxylase precursor
MREAAFMYSTAVAIFLVILVAALQGSAPRESPLPYHIPLDPEGSLELSWNVSYTQEAIHF
QLLVRRLKAGVLFGMSDRGELENADLVVLWTDGDTAYFADAWSDQKGQIHLDPQQDYQLL
QVQRTPEGLTLLFKRPFGTCDPKDYLIEDGTVHLVYGILEEPFRSLEAINGSGLQMGLQR
VQLLKPNIPEPELPSDACTMEVQAPNIQIPSQETTYWCYIKELPKGFSRHHIIKYEPIVT
KGNEALVHHMEVFQCAPEMDSVPHFSGPCDSKMKPDRLNYCRHVLAAWALGAKAFYYPEE
AGLAFGGPGSSRYLRLEVHYHNPLVIEGRNDSSGIRLYYTAKLRRFNAGIMELGLVYTPV
MAIPPRETAFILTGYCTDKCTQLALPPSGIHIFASQLHTHLTGRKVVTVLVRDGREWEIV
NQDNHYSPHFQEIRMLKKVVSVHPGDVLITSCTYNTEDRELATVGGFGILEEMCVNYVHY
YPQTQLELCKSAVDAGFLQKYFHLINRFNNEDVCTCPQASVSQQFTSVPWNSFNRDVLKA
LYSFAPISMHCNKSSAVRFQGEWNLQPLPKVISTLEEPTPQCPTSQGRSPAGPTVVSIGG
GKG
Target 3 Number of Residues 613
Target 3 Molecular Weight 67614
Target 3 Theoretical pI 6.31
Target 3 GO Classification
Function
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen
dopamine beta-monooxygenase activity
binding
ion binding
cation binding
transition metal ion binding
copper ion binding
catalytic activity
oxidoreductase activity
monooxygenase activity
Process
amino acid derivative metabolism
biogenic amine metabolism
catecholamine metabolism
physiological process
metabolism
cellular metabolism
amino acid and derivative metabolism
amino acid metabolism
histidine family amino acid metabolism
histidine metabolism
histidine catabolism
Component
Not Available
Target 3 General Function Involved in monooxygenase activity
Target 3 Specific Function Conversion of dopamine to noradrenaline
Target 3 Pathways
Name SMPDB Link KEGG Link
Tyrosine metabolism SMP00006 Link Image map00350 Link Image
Target 3 Reactions
  • 3,4-dihydroxyphenethylamine + ascorbate + O2 = noradrenaline + dehydroascorbate + H2O
Target 3 Pfam Domain Function
Target 3 Signals
  • 1-25
Target 3 Transmembrane Regions
  • 5-27
Target 3 Essentiality Non-Essential
Target 3 GenBank ID Protein 30474 Link Image
Target 3 UniProtKB/Swiss-Prot ID P09172 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name DOPO_HUMAN Link Image
Target 3 PDB ID Not Available
Target 3 Cellular Location
  • Exists both in a soluble form (in chromaffin granules) and as membrane bound (the membrane bound for
Target 3 Gene Sequence >1812 bp
ATGCGGGAGGCAGCCTTCATGTACAGCACAGCAGTGGCCATCTTCCTGGTCATCCTGGTG
GCCGCACTGCAGGGCTCGGCTCCCCGTGAGAGCCCCCTCCCCTATCACATCCCCCTGGAC
CCGGAGGGGTCCCTGGAGCTCTCATGGAATGTCAGCTACACCCAGGAGGCCATCCATTTC
CAGCTCCTGGTGCGGAGGCTCAAGGCTGGCGTCCTGTTTGGGATGTCCGACCGTGGCGAG
CTTGAGAACGCAGATCTCGTGGTGCTCTGGACCGATGGGGACACTGCCTATTTTGCGGAC
GCCTGGAGTGACCAGAAGGGGCAGATCCACCTGGATCCCCAGCAGGACTACCAGCTGCTG
CAGGTGCAGAGGACCCCAGAAGGCCTGACCCTGCTTTTCAAGAGGCCCTTTGGCACCTGC
GACCCCAAGGATTACCTCATTGAAGACGGCACTGTCCACTTGGTCTACGGGATCCTGGAG
GAGCCGTTCCGGTCACTGGAGGCCATCAACGGCTCGGGCCTGCAGATGGGGCTGCAGAGG
GTGCAGCTCCTGAAGCCCAATATCCCCGAACCGGAGTTGCCCTCAGACGCGTGCACCATG
GAGGTCCAAGCTCCCAATATCCAGATCCCCAGCCAGGAGACCACGTACTGGTGCTACATT
AAGGAGCTTCCAAAGGGCTTCTCTCGGCACCACATTATCAAGTACGAGCCCATCGTCACC
AAGGGCAATGAGGCCCTTGTCCACCACATGGAAGTCTTCCAGTGCGCCCCCGAGATGGAC
AGCGTCCCCCACTTCAGCGGGCCCTGCGACTCCAAGATGAAACCCGACCGCCTCAACTAC
TGCCGCCACGTGCTGGCCGCCTGGGCCCTGGGTGCCAAGGCATTTTACTACCCAGAGGAA
GCCGGCCTTGCCTTCGGGGGTCCAGGGTCCTCCAGATATCTCCGCCTGGAAGTTCACTAC
CACAACCCACTGGTGATAGAAGGACGAAACGACTCCTCAGGCATCCGCTTGTACTACACA
GCCAAGCTGCGGCGCTTCAACGCGGGGATCATGGAGCTGGGACTGGTGTACACGCCAGTG
ATGGCCATTCCACCACGGGAGACCGCCTTCATCCTCACTGGCTACTGCACGGACAAGTGC
ACCCAGCTGGCACTGCCTCCCTCCGGGATCCACATCTTCGCCTCTCAGCTCCACACACAC
CTGACTGGGAGAAAGGTGGTCACAGTGCTGGTCCGGGACGGCCGGGAGTGGGAGATCGTG
AACCAGGACAATCACTACAGCCCTCACTTCCAGGAGATCCGCATGTTGAAGAAGGTCGTG
TCGGTCCATCCGGGAGATGTGCTCATCACCTCCTGCACGTACAACACGGAAGACCGGGAG
CTGGCCACAGTGGGGGGCTTCGGGATCCTGGAGGAGATGTGTGTCAACTACGTGCACTAC
TACCCCCAGACGCAGCTGGAGCTCTGCAAGACGGCTGTGGACGCCGGCTTCCTGCAGAAG
TACTTCCACCTCATCAACAGGTTCAACAACGAGGATGTCTGCACCTGCCCTCAGGCGTCC
GTGTCTCAGCAGTTCACCTCTGTTCCCTGGAACTCCTTCAACCGCGACGTACTGAAGGCC
CTGTACAGCTTCGCGCCCATCTCCATGCACTGCAACAAGTCCTCAGCCGTCCGCTTCCAG
GGTGAATGGAACCTGCAGCCCCTGCCCAAGGTCATCTCCACACTGGAAGAGCCCACCCCA
CAGTGCCCCACCAGCCAGGGCCGAAGCCCTGCTGGCCCCACCGTTGTCAGCATTGGTGGG
GGCAAAGGCTGA
Target 3 GenBank Gene ID
Target 3 GeneCard ID DBH Link Image
Target 3 GenAtlas ID DBH Link Image
Target 3 HGNC ID HGNC:2689 Link Image
Target 3 Chromosome Location 9
Target 3 Locus 9q34
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
  2. Halushka MK, Fan JB, Bentley K, Hsie L, Shen N, Weder A, Cooper R, Lipshutz R, Chakravarti A: Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis. Nat Genet. 1999 Jul;22(3):239-47. [PubMed Link Image]
  3. Williams HJ, Bray N, Murphy KC, Cardno AG, Jones LA, Owen MJ: No evidence for allelic association between schizophrenia and a functional variant of the human dopamine beta-hydroxylase gene (DBH). Am J Med Genet. 1999 Oct 15;88(5):557-9. [PubMed Link Image]
  4. Kim CH, Zabetian CP, Cubells JF, Cho S, Biaggioni I, Cohen BM, Robertson D, Kim KS: Mutations in the dopamine beta-hydroxylase gene are associated with human norepinephrine deficiency. Am J Med Genet. 2002 Mar 1;108(2):140-7. [PubMed Link Image]
  5. Kobayashi K, Kurosawa Y, Fujita K, Nagatsu T: Human dopamine beta-hydroxylase gene: two mRNA types having different 3'-terminal regions are produced through alternative polyadenylation. Nucleic Acids Res. 1989 Feb 11;17(3):1089-102. [PubMed Link Image]
  6. Lamouroux A, Vigny A, Faucon Biguet N, Darmon MC, Franck R, Henry JP, Mallet J: The primary structure of human dopamine-beta-hydroxylase: insights into the relationship between the soluble and the membrane-bound forms of the enzyme. EMBO J. 1987 Dec 20;6(13):3931-7. [PubMed Link Image]
  7. Li B, Tsing S, Kosaka AH, Nguyen B, Osen EG, Bach C, Chan H, Barnett J: Expression of human dopamine beta-hydroxylase in Drosophila Schneider 2 cells. Biochem J. 1996 Jan 1;313 ( Pt 1):57-64. [PubMed Link Image]
Target 3 Drug References
  1. Feng J, Shi J, Sirimanne SR, Mounier-Lee CE, May SW: Kinetic and stereochemical studies on novel inactivators of C-terminal amidation. Biochem J. 2000 Sep 1;350 Pt 2:521-30. [PubMed Link Image]
  2. 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 Link Image]
  3. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
  4. Pettingill TM, Strange RW, Blackburn NJ: Carbonmonoxy dopamine beta-hydroxylase. Structural characterization by Fourier transform infrared, fluorescence, and x-ray absorption spectroscopy. J Biol Chem. 1991 Sep 15;266(26):16996-7003. [PubMed Link Image]
  5. Suzuki E, Kurata T, Shibata M, Mori M, Arakawa N: Activities of D- and L-xyloascorbic acid and D- and L-araboascorbic acid as a cofactor for dopamine beta-hydroxylase reaction. J Nutr Sci Vitaminol (Tokyo). 1997 Oct;43(5):491-6. [PubMed Link Image]
Drug Target 4 [top]
Target 4 ID 189
Target 4 Name Solute carrier family 23 member 1
Target 4 Synonyms
  1. Na(+)/L-ascorbic acid transporter 1
  2. Sodium-dependent vitamin C transporter 1
  3. Yolk sac permease-like molecule 3
  4. hSVCT1
Target 4 Gene Name SLC23A1
Target 4 Protein Sequence >Solute carrier family 23 member 1
MRAQEDLEGRTQHETTRDPSTPLPTEPKFDMLYKIEDVPPWYLCILLGFQHYLTCFSGTI
AVPFLLAEALCVGHDQHMVSQLIGTIFTCVGITTLIQTTVGIRLPLFQASAFAFLVPAKA
ILALERWKCPPEEEIYGNWSLPLNTSHIWHPRIREVQGAIMVSSVVEVVIGLLGLPGALL
NYIGPLTVTPTVSLIGLSVFQAAGDRAGSHWGISACSILLIILFSQYLRNLTFLLPVYRW
GKGLTLLRIQIFKMFPIMLAIMTVWLLCYVLTLTDVLPTDPKAYGFQARTDARGDIMAIA
PWIRIPYPCQWGLPTVTAAAVLGMFSATLAGIIESIGDYYACARLAGAPPPPVHAINRGI
FTEGICCIIAGLLGTGNGSTSSSPNIGVLGITKVGSRRVVQYGAAIMLVLGTIGKFTALF
ASLPDPILGGMFCTLFGMITAVGLSNLQFVDMNSSRNLFVLGFSMFFGLTLPNYLESNPG
AINTGILEVDQILIVLLTTEMFVGGCLAFILDNTVPGSPEERGLIQWKAGAHANSDMSSS
LKSYDFPIGMGIVKRITFLKYIPICPVFKGFSSSSKDQIAIPEDTPENTETASVCTKV
Target 4 Number of Residues 607
Target 4 Molecular Weight 64816
Target 4 Theoretical pI 6.58
Target 4 GO Classification
Function
transporter activity
Process
physiological process
cellular physiological process
transport
Component
cell
membrane
Target 4 General Function Nucleotide transport and metabolism
Target 4 Specific Function Sodium/ascorbate cotransporter. Mediates electrogenic uptake of vitamin C, with a stoichiometry of 2 Na(+) for each ascorbate
Target 4 Pathways Not Available
Target 4 Reactions Not Available
Target 4 Pfam Domain Function
Target 4 Signals
  • None
Target 4 Transmembrane Regions
  • 53-73
  • 82-102
  • 104-124
  • 160-180
  • 208-228
  • 251-271
  • 313-333
  • 359-379
  • 403-423
  • 427-447
  • 458-478
  • 491-511
Target 4 Essentiality Non-Essential
Target 4 GenBank ID Protein 3789785 Link Image
Target 4 UniProtKB/Swiss-Prot ID Q9UHI7 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name S23A1_HUMAN Link Image
Target 4 PDB ID Not Available
Target 4 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 4 Gene Sequence >1797 bp
ATGAGGGCCCAGGAGGACCTCGAGGGCCGGACACAGCATGAAACCACCAGGGACCCCTCG
ACCCCGCTACCCACAGAGCCTAAGTTTGACATGTTGTACAAGATCGAGGACGTGCCACCT
TGGTACCTGTGCATCCTGCTAGGGTTCCAGCACATCCATGACTGCTTACGTGGTACCATC
GCCGTGCCCTTCCTGCTGGCTGAGGCGCTGTGTGTGGGCCACAGCCAGACACTCCATTGT
CAGCTCATCGGCACCATCTTCACGTGCGTGGGCATCACCACTCTCATCCAGACCACCGTG
GGCATCCGGCTGCCGCTGTTCCAGGCCAGTGCCTTTGCATTTCTGGTTCCAGCCAAAGCC
ATACTGGCTCTGGAGAGATGGAAATGCCCCCCGGAAGAGGAGATCTACGGTAACTCCAGT
CTGCCCCTGAACACCTCTCATATTTGGCACCCACGGAATCGGGAGGTCCAGGGTGCAATC
ATGGTGTCCAGCGTGGTGGAGGTGGTGATTGGCCTGCTGGGGCTGCCTGGGGCCCTGCTC
AACTCACTTGGGCCTCTCACAGTCACCCCCACTGTCTCCCTCATTGGCCTTTCTGTCTTC
CAAGCTGCTGGCGACCGACCTGGCTCCCACTGGGGCATCTCAGCTTGCTCCATTCTCCTG
ATCATCCTCTTCTCCCAGTACCTGCGCAACCTCACCTTCCTGCTGCCTGTCTACCGCTGG
GGCAAGGGGCTCACTCTCCTCCGCATCCAGATCTTCAAAATGTTTCCTATCATGCTGGCC
ATCATGACCGTGTGGCTGCTCTGCATTGTCCTGACCTTGACAGACGTGCTGCCCACAGAC
CCAAAAGCCATTGGCTTCCAGGCACGAACCGATGCCCGTGGTGACATCATGGCTATTGCA
CCCTGGATCCGCATCCCCTACCCCTGTCAGTGGGGCCTGCCCACGGTGACTGCGGCTGCT
GTCCTGGGAATGTTCAGCGCCACTCTGGCAGGCATCATTGAGTCCATCGGAGATTACTAC
GCCTGTGCCCGCCTGGCTGGTGCACCACCCCCTCCAGTACATGCTATCAACAGGGGCATC
TTCACCGAAGGCATTTGCTGCATCATCGCGGGGCTATTGGGCACGGGCAACGGGTCCACC
TCGTCCAGTCCCAACATTGGCGTCCTGGGAATTACCAAGGTGGGCAGCCGGCGCGTGGTG
CAGTATGGTGCGGCTATCATGCTGGTCCTGGGCACCATCGGCAAGTTCACGGCCCTCTTC
GCCTCGCTCCCTGACCCCATCCTGGGGGGCATGTTCTGCAGTCTCTTTGGCATGATTACA
GCTGTGGGGCTGTCCAACCTGCAATTTGTGGCACTGAACTCCTCTCGCAACCTCTTCGTG
CTGGGATTTTCCATGTTCTTCGGGCTCACGCTGCCCAATTACCTGGAGTCCAACCCTGGC
GCCATCAATACAGGCATTCTTGAAGTGGATCAGATTCTGATTGTGCTGCTGACCACGGAG
ATGTTTGTGGGCGGGTGCCTTGCTTTCATACTTGACAACACAGTGCCAGGGAGCCCAGAG
GAGCGTGGTCTGATACAGTGGAAAGCTGGGGCTCATGCCAACAGTGACATGTCTTCCAGC
CTGAAGAGCTACGATTTCCCATTTGGGATGGGCATAGTAAAAAGAATTACCTTTCTGAAA
TACATTCCTATCTGCCCAGTCTTCAAAGGATTTTCTTCAAGTTCAAAAGATCAGATTGCA
ATTCCAGAAGACACTCCAGAAAATACAGAAACTGCATCTGTGTGCACCAAGGTCTGA
Target 4 GenBank Gene ID
Target 4 GeneCard ID SLC23A1 Link Image
Target 4 GenAtlas ID SLC23A1 Link Image
Target 4 HGNC ID HGNC:10974 Link Image
Target 4 Chromosome Location 5
Target 4 Locus 5q31.2-q31.3
Target 4 SNPs SNPJam Report Link Image
Target 4 General References
  1. Wang H, Dutta B, Huang W, Devoe LD, Leibach FH, Ganapathy V, Prasad PD: Human Na(+)-dependent vitamin C transporter 1 (hSVCT1): primary structure, functional characteristics and evidence for a non-functional splice variant. Biochim Biophys Acta. 1999 Nov 9;1461(1):1-9. [PubMed Link Image]
  2. Daruwala R, Song J, Koh WS, Rumsey SC, Levine M: Cloning and functional characterization of the human sodium-dependent vitamin C transporters hSVCT1 and hSVCT2. FEBS Lett. 1999 Nov 5;460(3):480-4. [PubMed Link Image]
  3. Wang Y, Mackenzie B, Tsukaguchi H, Weremowicz S, Morton CC, Hediger MA: Human vitamin C (L-ascorbic acid) transporter SVCT1. Biochem Biophys Res Commun. 2000 Jan 19;267(2):488-94. [PubMed Link Image]
  4. Liang WJ, Johnson D, Jarvis SM: Vitamin C transport systems of mammalian cells. Mol Membr Biol. 2001 Jan-Mar;18(1):87-95. [PubMed Link Image]
  5. Erichsen HC, Eck P, Levine M, Chanock S: Characterization of the genomic structure of the human vitamin C transporter SVCT1 (SLC23A2). J Nutr. 2001 Oct;131(10):2623-7. [PubMed Link Image]
  6. Faaland CA, Race JE, Ricken G, Warner FJ, Williams WJ, Holtzman EJ: Molecular characterization of two novel transporters from human and mouse kidney and from LLC-PK1 cells reveals a novel conserved family that is homologous to bacterial and Aspergillus nucleobase transporters. Biochim Biophys Acta. 1998 Nov 8;1442(2-3):353-60. [PubMed Link Image]
Target 4 Drug References
  1. Kang JS, Kim HN, Jung da J, Kim JE, Mun GH, Kim YS, Cho D, Shin DH, Hwang YI, Lee WJ: Regulation of UVB-induced IL-8 and MCP-1 production in skin keratinocytes by increasing vitamin C uptake via the redistribution of SVCT-1 from the cytosol to the membrane. J Invest Dermatol. 2007 Mar;127(3):698-706. Epub 2006 Sep 28. [PubMed Link Image]
  2. Johnston L, Laverty G: Vitamin C transport and SVCT1 transporter expression in chick renal proximal tubule cells in culture. Comp Biochem Physiol A Mol Integr Physiol. 2007 Mar;146(3):327-34. Epub 2006 Dec 5. [PubMed Link Image]
  3. Savini I, Rossi A, Pierro C, Avigliano L, Catani MV: SVCT1 and SVCT2: key proteins for vitamin C uptake. Amino Acids. 2007 Jun 1;. [PubMed Link Image]
  4. Perez MJ, Castano B, Gonzalez-Buitrago JM, Marin JJ: Multiple protective effects of melatonin against maternal cholestasis-induced oxidative stress and apoptosis in the rat fetal liver-placenta-maternal liver trio. J Pineal Res. 2007 Sep;43(2):130-9. [PubMed Link Image]
  5. Steiling H, Longet K, Moodycliffe A, Mansourian R, Bertschy E, Smola H, Mauch C, Williamson G: Sodium-dependent vitamin C transporter isoforms in skin: Distribution, kinetics, and effect of UVB-induced oxidative stress. Free Radic Biol Med. 2007 Sep 1;43(5):752-62. Epub 2007 May 10. [PubMed Link Image]
Drug Target 5 [top]
Target 5 ID 874
Target 5 Name DNA
Target 5 Synonyms
  1. Deoxyribonucleic acid
Target 5 Gene Name Not Available
Target 5 Protein Sequence Not Available
Target 5 Number of Residues 0
Target 5 Molecular Weight 7656 (double strand)
Target 5 Theoretical pI Not Available
Target 5 GO Classification
Function
information storage
information transfer
Process
DNA replication and chromosomal cycle
DNA replication
DNA-dependent DNA replication
DNA replication, synthesis of RNA primer
transcription
transcription, DNA dependent
Component
cell
intracellular
nucleus
mitochondria
Target 5 General Function Biological information storage and information transfer
Target 5 Specific Function DNA is the molecule of heredity, as it is responsible for the genetic propagation of most inherited traits. It is a polynucleic acid that carries genetic information on cell growth, division, and function. DNA consists of two long strands of nucleotides twisted into a double helix and held together by hydrogen bonds. The sequence of nucleotides determines hereditary characteristics. Each strand serves as the template for subsequent DNA replication and as a template for mRNA production, leading to protein synthesis via ribosomes.
Target 5 Pathways
Name SMPDB Link KEGG Link
DNA polymerase map03030 Link Image
RNA polymerase map03020 Link Image
Target 5 Reactions
  • DNA + DNA polymerase + nNTP = 2 DNA + nNDP; DNA + RNA polymerase + NTP = mRNA + nNDP
Target 5 Pfam Domain Function Not Available
Target 5 Signals
  • None
Target 5 Transmembrane Regions
  • None
Target 5 Essentiality Essential
Target 5 GenBank ID Protein Not Available
Target 5 UniProtKB/Swiss-Prot ID Not Available
Target 5 UniProtKB/Swiss-Prot Entry Name Not Available
Target 5 PDB ID 1BNA Link Image
Target 5 PDB File Show
Target 5 3D Structure
Target 5 Cellular Location
  • Nucleus and mitochondria
Target 5 Gene Sequence >Example: Dickerson dodecamer
CGCGAATTCGCG
Target 5 GenBank Gene ID
Target 5 GeneCard ID Not Available
Target 5 GenAtlas ID Not Available
Target 5 HGNC ID Not Available
Target 5 Chromosome Location Not Available
Target 5 Locus All loci
Target 5 SNPs Not Available
Target 5 General References
  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 Link Image]
Target 5 Drug References
  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 Link Image]
  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 Link Image]
  3. Manna P, Sinha M, Sil PC: Protection of arsenic-induced hepatic disorder by arjunolic Acid. Basic Clin Pharmacol Toxicol. 2007 Nov;101(5):333-8. [PubMed Link Image]
  4. Guarnieri S, Loft S, Riso P, Porrini M, Risom L, Poulsen HE, Dragsted LO, Moller P: DNA repair phenotype and dietary antioxidant supplementation. Br J Nutr. 2007 Oct 10;:1-7. [PubMed Link Image]
  5. Singh S, Rana SV: Amelioration of arsenic toxicity by L-Ascorbic acid in laboratory rat. J Environ Biol. 2007 Apr;28(2 Suppl):377-84. [PubMed Link Image]
Drug Target 6 [top]
Target 6 ID 2260
Target 6 Name Xylose isomerase
Target 6 Synonyms
  1. EC 5.3.1.5
Target 6 Gene Name xylA
Target 6 Protein Sequence >Xylose isomerase
MNYQPTPEDRFTFGLWTVGWQGRDPFGDATRRALDPVESVRRLAELGAHGVTFHDDDLIP
FGSSDSEREEHVKRFRQALDDTGMKVPMATTNLFTHPVFKDGGFTANDRDVRRYALRKTI
RNIDLAVELGAETYVAWGGREGAESGGAKDVRDALDRMKEAFDLLGEYVTSQGYDIRFAI
EPKPNEPRGDILLPTVGHALAFIERLERPELYGVNPEVGHEQMAGLNFPHGIAQALWAGK
LFHIDLNGQNGIKYDQDLRFGAGDLRAAFWLVDLLESAGYSGPRHFDFKPPRTEDFDGVW
ASAAGCMRNYLILKERAAAFRADPEVQEALRASRLDELARPTAADGLQALLDDRSAFEEF
DVDAAAARGMAFERLDQLAMDHLLGARG
Target 6 Number of Residues 394
Target 6 Molecular Weight 43228
Target 6 Theoretical pI 4.78
Target 6 GO Classification
Function
catalytic activity
isomerase activity
intramolecular oxidoreductase activity
intramolecular oxidoreductase activity, interconverting aldoses and ketoses
xylose isomerase activity
Process
physiological process
metabolism
macromolecule metabolism
carbohydrate metabolism
Component
Not Available
Target 6 General Function Carbohydrate transport and metabolism
Target 6 Specific Function Involved in D-xylose catabolism
Target 6 Pathways
Name SMPDB Link KEGG Link
Pentose and glucuronate interconversions map00040 Link Image
Target 6 Reactions
  • D-xylose = D-xylulose
Target 6 Pfam Domain Function
Target 6 Signals
  • None
Target 6 Transmembrane Regions
  • None
Target 6 Essentiality Essential
Target 6 GenBank ID Protein 153534 Link Image
Target 6 UniProtKB/Swiss-Prot ID P24300 Link Image
Target 6 UniProtKB/Swiss-Prot Entry Name XYLA_STRRU Link Image
Target 6 PDB ID 1MNZ Link Image
Target 6 PDB File Show
Target 6 3D Structure
Target 6 Cellular Location
  • Cytoplasm
Target 6 Gene Sequence >1167 bp
ATGAACTACCAGCCCACCCCCGAGGACAGGTTCACCTTCGGACTGTGGACCGTCGGCTGG
CAGGGACGGGACCCCTTCGGTGACGCCACGCGGCGCGCCCTCGACCCGGTCGAGTCGGTG
CGGCGGCTGGCCGAGCTGGGCGCCCACGGCGTCACGTTCCACGACGACGACCTCATCCCC
TTCGGCTCCAGCGACAGCGAGCGCGAGGAGCACGTCAAGCGGTTCCGGCAGGCGCTGGAC
GACACCGGCATGAAGGTGCCGATGGCCACCACCAACCTGTTCACCCACCCGGTGTTCAAG
GACGGCGGCTTCACCGCCAACGACCGCGACGTGCGCCGCTACGCCCTGCGCAAGACCATC
CGCAACATCGACCTCGCGGTCGAGCTCGGCGCCGAGACCTATGTGGCCTGGGGCGGCCGC
GAGGGTGCCGAGTCGGGTGGCGCCAAGGACGTGCGGGACGCCCTCGACCGCATGAAGGAG
GCCTTCGACCTGCTCGGCGAGTACGTCACCTCCCAGGGCTACGACATCCGCTTCGCCATC
GAGCCCAAGCCGAACGAGCCGCGCGGCGACATCCTGCTCCCCACCGTCGGCCACGCCCTG
GCGTTCATCGAGCGCCTGGAGCGACCGGAGCTGTACGGCGTGAACCCCGAGGTCGGCCAC
GAGCAGATGGCCGGGCTGAACTTCCCGCACGGCATCGCGCAGGCGCTGTGGGCGGGCAAG
CTGTTCCACATCGACCTCAACGGCCAGAACGGCATCAAGTACGACCAGGACCTCCGCTTC
GGCGCGGGCGACCTGCGGGCCGCGTTCTGGCTGGTGGACCTGCTGGAGTCGGCCGGCTAC
AGCGGCCCGCGGCACTTCGACTTCAAGCCGCCGCGGACCGAGGACTTCGACGGGGTGTGG
GCCTCGGCGGCCGGCTGCATGCGCAACTACCTGATCCTCAAGGAGCGTGCGGCGGCCTTC
CGCGCCGACCCCGAGGTGCAGGAGGCGCTGCGCGCGTCCCGTCTGGACGAGCTGGCCCGG
CCCACGGCGGCCGACGGTCTGCAGGCCCTGCTCGACGACCGGTCCGCCTTCGAGGAGTTC
GACGTCGACGCGGCGGCGGCCCGTGGGATGGCCTTCGAGCGCCTGGACCAGCTGGCGATG
GACCACCTGCTGGGCGCCCGGGGCTGA
Target 6 GenBank Gene ID
Target 6 GeneCard ID Not Available
Target 6 GenAtlas ID Not Available
Target 6 HGNC ID Not Available
Target 6 Chromosome Location Not Available
Target 6 Locus Not Available
Target 6 SNPs SNPJam Report Link Image
Target 6 General References
  1. Wong HC, Ting Y, Lin HC, Reichert F, Myambo K, Watt KW, Toy PL, Drummond RJ: Genetic organization and regulation of the xylose degradation genes in Streptomyces rubiginosus. J Bacteriol. 1991 Nov;173(21):6849-58. [PubMed Link Image]
  2. Whitlow M, Howard AJ, Finzel BC, Poulos TL, Winborne E, Gilliland GL: A metal-mediated hydride shift mechanism for xylose isomerase based on the 1.6 A Streptomyces rubiginosus structures with xylitol and D-xylose. Proteins. 1991;9(3):153-73. [PubMed Link Image]
  3. Carrell HL, Glusker JP, Burger V, Manfre F, Tritsch D, Biellmann JF: X-ray analysis of D-xylose isomerase at 1.9 A: native enzyme in complex with substrate and with a mechanism-designed inactivator. Proc Natl Acad Sci U S A. 1989 Jun;86(12):4440-4. [PubMed Link Image]
Target 6 Drug References
  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 Link Image]
  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 Link Image]
Drug Target 7 [top]
Target 7 ID 2485
Target 7 Name Hyaluronate lyase
Target 7 Synonyms
  1. EC 4.2.2.1
  2. HYase
  3. Hyaluronate lyase precursor
  4. Hyaluronidase
Target 7 Gene Name Not Available
Target 7 Protein Sequence >Hyaluronate lyase precursor
MQTKTKKLIVSLSSLVLSGFLLNHYMTIGAEETTTNTIQQSQKEVQYQQRDTKNLVENGD
FGQTEDGSSPWTGSKAQGWSAWVDQKNSADASTRVIEAKDGAITISSHEKLRAALHRMVP
IEAKKKYKLRFKIKTDNKIGIAKVRIIEESGKDKRLWNSATTSGTKDWQTIEADYSPTLD
VDKIKLELFYETGTGTVSFKDIELVEVADQLSEDSQTDKQLEEKIDLPIGKKHVFSLADY
TYKVENPDVASVKNGILEPLKEGTTNVIVSKDGKEVKKIPLKILASVKDAYTDRLDDWNG
IIAGNQYYDSKNEQMAKLNQELEGKVADSLSSISSQADRTYLWEKFSNYKTSANLTATYR
KLEEMAKQVTNPSSRYYQDETVVRTVRDSMEWMHKHVYNSEKSIVGNWWDYEIGTPRAIN
NTLSLMKEYFSDEEIKKYTDVIEKFVPDPEHFRKTTDNPFKALGGNLVDMGRVKVIAGLL
RKDDQEISSTIRSIEQVFKLVDQGEGFYQDGSYIDHTNVAYTGAYGNVLIDGLSQLLPVI
QKTKNPIDKDKMQTMYHWIDKSFAPLLVNGELMDMSRGRSISRANSEGHVAAVEVLRGIH
RIADMSEGETKQCLQSLVKTIVQSDSYYDVFKNLKTYKDISLMQSLLSDAGVASVPRPSY
LSAFNKMDKTAMYNAEKGFGFGLSLFSSRTLNYEHMNKENKRGWYTSDGMFYLYNGDLSH
YSDGYWPTVNPYKMPGTTETDAKRADSDTGKVLPSAFVGTSKLDDANATATMDFTNWNQT
LTAHKSWFMLKDKIAFLGSNIQNTSTDTAATTIDQRKLESGNPYKVYVNDKEASLTEQEK
DYPETQSVFLESFDSKKNIGYFFFKKSSISMSKALQKGAWKDINEGQSDKEVENEFLTIS
QAHKQNRDSYGYMLIPNVDRATFNQMIKELESSLIENNETLQSVYDAKQGVWGIVKYDDS
VSTISNQFQVLKRGVYTIRKEGDEYKIAYYNPETQESAPDQEVFKKLEQAAQPQVQNSKE
KEKSEEEKNHSDQKNLPQTGEGQSILASLGFLLLGAFYLFRRGKNN
Target 7 Number of Residues 1083
Target 7 Molecular Weight 120772
Target 7 Theoretical pI 5.97
Target 7 GO Classification
Function
carbon-oxygen lyase activity
carbon-oxygen lyase activity, acting on polysaccharides
catalytic activity
lyase activity
Process
Not Available
Component
extracellular region
cell
cell surface
Target 7 General Function Involved in hyaluronidase activity
Target 7 Specific Function Cleaves hyaluronate chains at a beta-D-GalNAc- (1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D- glucosamine
Target 7 Pathways Not Available
Target 7 Reactions
  • Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
Target 7 Pfam Domain Function
Target 7 Signals
  • 1-30
Target 7 Transmembrane Regions
  • None
Target 7 Essentiality Essential
Target 7 GenBank ID Protein 14971788 Link Image
Target 7 UniProtKB/Swiss-Prot ID Q54873 Link Image
Target 7 UniProtKB/Swiss-Prot Entry Name HYSA_STRPN Link Image
Target 7 PDB ID 1OJO Link Image
Target 7 PDB File Show
Target 7 3D Structure
Target 7 Cellular Location
  • Cell wall
  • peptidoglycan-anchor (Potential)
Target 7 Gene Sequence >3201 bp
ATGCAAACAAAAACAAAGAAGCTCATTGTGAGTTTGTCTTCACTTGTTTTATCAGGATTT
TTATTAAACCATTATATGACAATTGGAGCGGAAGAAACGACTACGAATACCATTCAGCAA
AGCCAGAAGGAAGTTCAGTATCAGCAAAGGGATACAAAAAATTTAGTTGAAAATGGTGAT
TTTGGTCAGACGGAGGACGGAAGCAGTCCGTGGACAGGAAGCAAAGCTCAGGGGTGGTCA
GCTTGGGTAGACCAGAAGAATAGTGCAGATGCCTCAACTCGAGTCATTGAGGCTAAGGAT
GGGGCTATCACTATCTCAAGCCATGAGAAATTAAGGGCAGCGCTTCACCGTATGGTTCCT
ATTGAAGCTAAGAAAAAGTATAAACTGCGTTTCAAGATTAAAACAGATAATAAAATCGGG
ATTGCCAAAGTTCGTATCATTGAGGAAAGTGGTAAGGACAAGCGATTGTGGAATTCTGCA
ACGACGTCAGGAACAAAGGACTGGCAGACCATTGAAGCAGACTATAGCCCGACTTTAGAT
GTTGATAAAATCAAGCTGGAGTTATTCTATGAAACAGGAACTGGGACTGTTTCCTTTAAG
GATATTGAGCTGGTAGAGGTAGCAGACCAGCTTTCTGAGGATTCTCAAACAGATAAACAG
CTTGAGGAAAAGATTGATTTACCAATTGGAAAAAAACATGTTTTTTCTCTTGCGGACTAT
ACTTATAAGGTAGAAAATCCTGACGTTGCTTCAGTCAAAAATGGAATTTTAGAACCTCTT
AAGGAAGGGACAACCAATGTCATTGTCAGTAAAGATGGCAAGGAAGTGAAAAAGATTCCT
TTGAAGATTCTGGCCTCTGTTAAGGATGCATACACAGACCGTTTGGATGACTGGAATGGC
ATCATCGCTGGGAATCAATACTATGATTCTAAAAATGAACAGATGGCCAAATTAAACCAG
GAATTGGAAGGAAAGGTAGCTGATAGCCTATCCAGTATTTCAAGTCAGGCGGACCGCACC
TATTTGTGGGAAAAATTTTCAAATTATAAAACGTCTGCAAATCTGACTGCCACTTATCGG
AAATTGGAGGAGATGGCCAAGCAAGTGACCAATCCTTCTTCTCGTTATTATCAAGATGAA
ACTGTCGTTCGAACAGTCAGGGATTCCATGGAATGGATGCATAAACATGTCTACAATAGT
GAAAAGAGCATTGTTGGGAACTGGTGGGATTATGAAATCGGTACACCTCGTGCCATCAAC
AATACCTTGTCTCTGATGAAAGAATACTTCTCTGATGAGGAAATTAAAAAATATACAGAT
GTGATTGAAAAATTTGTACCAGATCCCGAACATTTCCGAAAGACGACTGATAACCCATTC
AAGGCTCTAGGTGGAAACTTAGTTGATATGGGAAGGGTAAAAGTAATAGCTGGTTTACTG
CGTAAGGATGATCAAGAAATTTCTTCTACCATTCGCTCGATTGAGCAAGTGTTCAAGTTG
GTAGACCAAGGTGAAGGTTTTTATCAAGATGGATCCTATATCGACCACACCAATGTTGCC
TATACGGGTGCTTATGGGAATGTTTTGATTGATGGCCTGTCTCAACTGTTGCCAGTCATT
CAAAAGACCAAGAATCCAATCGATAAAGATAAAATGCAAACCATGTACCACTGGATTGAT
AAATCGTTTGCTCCTTTGCTGGTGAATGGAGAGTTGATGGATATGAGTCGTGGACGCTCG
ATCAGTCGTGCAAATAGCGAGGGGCACGTGGCCGCAGTAGAAGTACTAAGAGGGATTCAC
CGAATAGCGGATATGTCTGAAGGAGAAACCAAACAATGTTTGCAGAGTCTTGTGAAGACC
ATTGTTCAATCGGATAGTTATTATGATGTCTTTAAGAATTTGAAGACTTATAAGGATATC
AGTTTGATGCAATCCTTGTTAAGTGATGCAGGAGTCGCAAGTGTTCCAAGACCAAGTTAC
CTATCTGCCTTTAACAAGATGGATAAAACAGCCATGTACAATGCAGAGAAAGGGTTTGGA
TTTGGCTTGTCACTCTTTTCCAGTCGTACCTTGAATTACGAACACATGAACAAGGAAAAT
AAACGTGGTTGGTATACGAGTGATGGGATGTTCTATCTTTACAATGGCGATTTGAGTCAC
TATAGCGATGGCTACTGGCCAACAGTTAATCCATATAAGATGCCTGGTACAACAGAGACG
GATGCTAAGAGAGCGGATAGCGATACAGGTAAAGTTTTACCGTCTGCTTTCGTTGGAACG
AGCAAACTAGATGATGCCAATGCGACAGCAACCATGGATTTCACCAACTGGAATCAAACA
TTGACTGCTCATAAGAGCTGGTTTATGCTAAAGGATAAGATCGCCTTTTTAGGAAGCAAT
ATCCAAAACACTTCAACAGATACTGCTGCAACTACAATTGACCAGAGAAAACTGGAATCA
GGTAATCCATATAAAGTCTATGTCAATGATAAAGAAGCCTCCCTTACAGAACAAGAAAAG
GATTATCCTGAAACCCAAAGTGTCTTTTTAGAATCGTTCGATTCGAAAAAGAATATTGGT
TACTTTTTCTTTAAGAAGAGTTCAATCAGTATGAGTAAGGCTTTGCAAAAGGGAGCCTGG
AAGGATATCAATGAAGGACAGTCAGACAAGGAAGTTGAAAATGAATTTCTTACGATTAGT
CAGGCTCATAAGCAAAATAGAGATTCTTATGGCTATATGCTCATTCCTAACGTGGATCGT
GCCACCTTCAATCAAATGATAAAAGAGTTAGAAAGTAGCCTCATCGAAAATAACGAAACC
CTTCAGTCTGTTTATGATGCTAAACAAGGAGTTTGGGGCATTGTGAAATATGATGATTCT
GTCTCTACTATTTCCAACCAATTCCAAGTTTTGAAACGTGGAGTCTATACCATTCGAAAA
GAAGGGGATGAATATAAGATTGCCTACTATAATCCTGAAACCCAGGAATCAGCTCCAGAT
CAGGAAGTCTTTAAAAAGCTAGAGCAAGCAGCTCAGCCACAAGTACAGAATTCAAAAGAA
AAGGAAAAATCTGAAGAGGAAAAGAACCATTCGGATCAAAAGAATCTCCCTCAGACAGGA
GAAGGTCAGTCAATCTTGGCAAGTCTAGGGTTCTTGCTACTTGGGGCATTTTATCTATTC
CGTAGAGGAAAGAACAACTAA
Target 7 GenBank Gene ID
Target 7 GeneCard ID Not Available
Target 7 GenAtlas ID Not Available
Target 7 HGNC ID Not Available
Target 7 Chromosome Location Not Available
Target 7 Locus Not Available
Target 7 SNPs Not Available
Target 7 General References
  1. Tettelin H, Nelson KE, Paulsen IT, Eisen JA, Read TD, Peterson S, Heidelberg J, DeBoy RT, Haft DH, Dodson RJ, Durkin AS, Gwinn M, Kolonay JF, Nelson WC, Peterson JD, Umayam LA, White O, Salzberg SL, Lewis MR, Radune D, Holtzapple E, Khouri H, Wolf AM, Utterback TR, Hansen CL, McDonald LA, Feldblyum TV, Angiuoli S, Dickinson T, Hickey EK, Holt IE, Loftus BJ, Yang F, Smith HO, Venter JC, Dougherty BA, Morrison DA, Hollingshead SK, Fraser CM: Complete genome sequence of a virulent isolate of Streptococcus pneumoniae. Science. 2001 Jul 20;293(5529):498-506. [PubMed Link Image]
  2. Berry AM, Lock RA, Thomas SM, Rajan DP, Hansman D, Paton JC: Cloning and nucleotide sequence of the Streptococcus pneumoniae hyaluronidase gene and purification of the enzyme from recombinant Escherichia coli. Infect Immun. 1994 Mar;62(3):1101-8. [PubMed Link Image]
  3. Jedrzejas MJ, Chantalat L, Mewbourne RB: Crystallization and preliminary X-ray analysis of Streptococcus pneumoniae hyaluronate lyase. J Struct Biol. 1998 Jan;121(1):73-5. [PubMed Link Image]
Target 7 Drug References
  1. Li S, Taylor KB, Kelly SJ, Jedrzejas MJ: Vitamin C inhibits the enzymatic activity of Streptococcus pneumoniae hyaluronate lyase. J Biol Chem. 2001 May 4;276(18):15125-30. Epub 2001 Jan 12. [PubMed Link Image]
  2. Okorukwu ON, Vercruysse KP: Effects of ascorbic acid and analogs on the activity of testicular hyaluronidase and hyaluronan lyase on hyaluronan. J Enzyme Inhib Med Chem. 2003 Aug;18(4):377-82. [PubMed Link Image]
  3. Botzki A, Rigden DJ, Braun S, Nukui M, Salmen S, Hoechstetter J, Bernhardt G, Dove S, Jedrzejas MJ, Buschauer A: L-Ascorbic acid 6-hexadecanoate, a potent hyaluronidase inhibitor. X-ray structure and molecular modeling of enzyme-inhibitor complexes. J Biol Chem. 2004 Oct 29;279(44):45990-7. Epub 2004 Aug 18. [PubMed Link Image]
  4. 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 Link Image]
  5. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 8 [top]
Target 8 ID 3839
Target 8 Name Phytanoyl-CoA dioxygenase, peroxisomal
Target 8 Synonyms
  1. EC 1.14.11.18
  2. PhyH
  3. Phytanic acid oxidase
  4. Phytanoyl-CoA alpha-hydroxylase
  5. Phytanoyl-CoA dioxygenase, peroxisomal precursor
Target 8 Gene Name PHYH
Target 8 Protein Sequence >Phytanoyl-CoA dioxygenase, peroxisomal
MEQLRAAARLQIVLGHLGRPSAGAVVAHPTSGTISSASFHPQQFQYTLDNNVLTLEQRKF
YEENGFLVIKNLVPDADIQRFRNEFEKICRKEVKPLGLTVMRDVTISKSEYAPSEKMITK
VQDFQEDKELFRYCTLPEILKYVECFTGPNIMAMHTMLINKPPDSGKKTSRHPLHQDLHY
FPFRPSDLIVCAWTAMEHISRNNGCLVVLPGTHKGSLKPHDYPKWEGGVNKMFHGIQDYE
ENKARVHLVMEKGDTVFFHPLLIHGSGQNKTQGFRKAISCHFASADCHYIDVKGTSQENI
EKEVVGIAHKFFGAENSVNLKDIWMFRARLVKGERTNL
Target 8 Number of Residues 343
Target 8 Molecular Weight 38539
Target 8 Theoretical pI 8.65
Target 8 GO Classification Not Available
Target 8 General Function Not Available
Target 8 Specific Function Converts phytanoyl-CoA to 2-hydroxyphytanoyl-CoA
Target 8 Pathways Not Available
Target 8 Reactions
  • phytanoyl-CoA + 2-oxoglutarate + O2 = 2-hydroxyphytanoyl-CoA + succinate + CO2
Target 8 Pfam Domain Function
Target 8 Signals
  • None
Target 8 Transmembrane Regions
  • None
Target 8 Essentiality Non-Essential
Target 8 GenBank ID Protein 2564671 Link Image
Target 8 UniProtKB/Swiss-Prot ID O14832 Link Image
Target 8 UniProtKB/Swiss-Prot Entry Name PAHX_HUMAN Link Image
Target 8 PDB ID Not Available
Target 8 Cellular Location
  • Peroxisome
Target 8 Gene Sequence >1017 bp
ATGGAGCAGCTTCGCGCCGCCGCCCGTCTGCAGATTGTTCTGGGCCACCTCGGCCGCCCC
TCGGCCGGGGCTGTCGTAGCTCATCCCACTTCAGGGACTATTTCCTCTGCCAGTTTCCAT
CCTCAACAATTCCAGTATACTCTGGATAATAATGTTCTAACCCTGGAACAGAGAAAATTT
TATGAAGAAAATGGGTTTCTAGTAATCAAAAATCTTGTACCTGATGCCGATATTCAACGC
TTTCGGAATGAGTTTGAAAAAATCTGCAGAAAGGAGGTGAAACCATTAGGATTAACAGTA
ATGAGAGATGTGACCATTTCGAAATCCGAATATGCTCCAAGTGAGAAGATGATCACGAAG
GTCCAGGATTTCCAGGAAGATAAGGAGCTCTTCAGATACTGCACTCTCCCCGAGATTCTG
AAATATGTGGAGTGCTTCACTGGACCTAATATTATGGCCATGCACACAATGTTGATAAAC
AAACCTCCAGATTCTGGCAAGAAGACGTCCCGTCACCCCCTGCACCAGGACCTGCACTAT
TTCCCCTTCAGGCCCAGCGATCTCATCGTTTGCGCCTGGACGGCGATGGAGCACATCAGC
CGGAACAACGGCTGTCTGGTTGTGCTCCCAGGCACGCACAAGGGCTCCCTGAAGCCCCAC
GATTACCCCAAGTGGGAGGGGGGAGTTAACAAAATGTTCCACGGGATCCAGGACTACGAG
GAAAACAAGGCCCGGGTGCACCTGGTGATGGAGAAGGGCGACACTGTTTTCTTCCATCCT
TTGCTCATCCACGGATCTGGTCAGAATAAAACCCAGGGATTCCGGAAGGCAATTTCCTGC
CATTTCGCCAGTGCCGATTGCCACTACATTGACGTGAAGGGCACCAGTCAAGAAAACATC
GAGAAGGAAGTTGTAGGAATAGCACATAAATTCTTTGGAGCTGAAAATAGCGTGAACTTG
AAGGATATTTGGATGTTTCGAGCTCGACTTGTGAAAGGAGAAAGAACCAATCTTTGA
Target 8 GenBank Gene ID
Target 8 GeneCard ID PHYH Link Image
Target 8 GenAtlas ID PHYH Link Image
Target 8 HGNC ID HGNC:8940 Link Image
Target 8 Chromosome Location 10
Target 8 Locus 10pter-p11.2
Target 8 SNPs SNPJam Report Link Image
Target 8 General References
  1. Chambraud B, Radanyi C, Camonis JH, Rajkowski K, Schumacher M, Baulieu EE: Immunophilins, Refsum disease, and lupus nephritis: the peroxisomal enzyme phytanoyl-COA alpha-hydroxylase is a new FKBP-associated protein. Proc Natl Acad Sci U S A. 1999 Mar 2;96(5):2104-9. [PubMed Link Image]
  2. Lee ZH, Kim H, Ahn KY, Seo KH, Kim JK, Bae CS, Kim KK: Identification of a brain specific protein that associates with a refsum disease gene product, phytanoyl-CoA alpha-hydroxylase. Brain Res Mol Brain Res. 2000 Feb 22;75(2):237-47. [PubMed Link Image]
  3. Jansen GA, Ferdinandusse S, Hogenhout EM, Verhoeven NM, Jakobs C, Wanders RJ: Phytanoyl-CoA hydroxylase deficiency. Enzymological and molecular basis of classical Refsum disease. Adv Exp Med Biol. 1999;466:371-6. [PubMed Link Image]
  4. Jansen GA, Hogenhout EM, Ferdinandusse S, Waterham HR, Ofman R, Jakobs C, Skjeldal OH, Wanders RJ: Human phytanoyl-CoA hydroxylase: resolution of the gene structure and the molecular basis of Refsum's disease. Hum Mol Genet. 2000 May 1;9(8):1195-200. [PubMed Link Image]
  5. Mihalik SJ, Morrell JC, Kim D, Sacksteder KA, Watkins PA, Gould SJ: Identification of PAHX, a Refsum disease gene. Nat Genet. 1997 Oct;17(2):185-9. [PubMed Link Image]
  6. Jansen GA, Ofman R, Ferdinandusse S, Ijlst L, Muijsers AO, Skjeldal OH, Stokke O, Jakobs C, Besley GT, Wraith JE, Wanders RJ: Refsum disease is caused by mutations in the phytanoyl-CoA hydroxylase gene. Nat Genet. 1997 Oct;17(2):190-3. [PubMed Link Image]
Target 8 Drug References
  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 Link Image]
  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 Link Image]
Drug Target 9 [top]
Target 9 ID 3935
Target 9 Name Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2
Target 9 Synonyms
  1. EC 1.14.11.4
  2. LH2
  3. Lysyl hydroxylase 2
  4. Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 precursor
Target 9 Gene Name PLOD2
Target 9 Protein Sequence >Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2
MGGCTVKPQLLLLALVLHPWNPCLGADSEKPSSIPTDKLLVITVATKESDGFHRFMQSAK
YFNYTVKVLGQGEEWRGGDGINSIGGGQKVRLMKEVMEHYADQDDLVVMFTECFDVIFAG
GPEEVLKKFQKANHKVVFAADGILWPDKRLADKYPVVHIGKRYLNSGGFIGYAPYVNRIV
QQWNLQDNDDDQLFYTKVYIDPLKREAINITLDHKCKIFQTLNGAVDEVVLKFENGKARA
KNTFYETLPVAINGNGPTKILLNYFGNYVPNSWTQDNGCTLCEFDTVDLSAVDVHPNVSI
GVFIEQPTPFLPRFLDILLTLDYPKEALKLFIHNKEVYHEKDIKVFFDKAKHEIKTIKIV
GPEENLSQAEARNMGMDFCRQDEKCDYYFSVDADVVLTNPRTLKILIEQNRKIIAPLVTR
HGKLWSNFWGALSPDGYYARSEDYVDIVQGNRVGVWNVPYMANVYLIKGKTLRSEMNERN
YFVRDKLDPDMALCRNAREMGVFMYISNRHEFGRLLSTANYNTSHYNNDLWQIFENPVDW
KEKYINRDYSKIFTENIVEQPCPDVFWFPIFSEKACDELVEEMEHYGKWSGGKHHDSRIS
GGYENVPTDDIHMKQVDLENVWLHFIREFIAPVTLKVFAGYYTKGFALLNFVVKYSPERQ
RSLRPHHDASTFTINIALNNVGEDFQGGGCKFLRYNCSIESPRKGWSFMHPGRLTHLHEG
LPVKNGTRYIAVSFIDP
Target 9 Number of Residues 749
Target 9 Molecular Weight 84686
Target 9 Theoretical pI 6.69
Target 9 GO Classification
Function
procollagen-lysine 5-dioxygenase activity
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Process
physiological process
metabolism
macromolecule metabolism
protein metabolism
Component
organelle
membrane-bound organelle
intracellular membrane-bound organelle
endoplasmic reticulum
Target 9 General Function Not Available
Target 9 Specific Function Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links
Target 9 Pathways
Name SMPDB Link KEGG Link
Lysine degradation SMP00037 Link Image map00310 Link Image
Target 9 Reactions
  • procollagen L-lysine + 2-oxoglutarate + O2 = procollagen 5-hydroxy-L-lysine + succinate + CO2 ALL_REAC (other) R03376
Target 9 Pfam Domain Function
Target 9 Signals
  • 1-25
Target 9 Transmembrane Regions
  • None
Target 9 Essentiality Non-Essential
Target 9 GenBank ID Protein 2138314 Link Image
Target 9 UniProtKB/Swiss-Prot ID O00469 Link Image
Target 9 UniProtKB/Swiss-Prot Entry Name PLOD2_HUMAN Link Image
Target 9 PDB ID Not Available
Target 9 Cellular Location
  • Endoplasmic reticulum
Target 9 Gene Sequence >2214 bp
ATGGGGGGATGCACGGTGAAGCCTCAGCTGCTGCTCCTGGCGCTCGTCCTCCACCCCTGG
AATCCCTGTCTGGGTGCGGACTCGGAGAAGCCCTCGAGCATCCCCACAGATAAATTATTA
GTCATAACTGTAGCAACAAAAGAAAGTGATGGATTCCATCGATTTATGCAGTCAGCCAAA
TATTTCAATTATACTGTGAAGGTCCTTGGTCAAGGAGAAGAATGGAGAGGTGGTGATGGA
ATTAATAGTATTGGAGGGGGCCAGAAAGTGAGATTAATGAAAGAAGTCATGGAACACTAT
GCTGATCAAGATGATCTGGTTGTCATGTTTACTGAATGCTTTGATGTCATATTTGCTGGT
GGTCCAGAAGAAGTTCTAAAAAAATTCCAAAAGGCAAACCACAAAGTGGTCTTTGCAGCA
GATGGAATTTTGTGGCCAGATAAAAGACTAGCAGACAAGTATCCTGTTGTGCACATTGGG
AAACGCTATCTGAATTCAGGAGGATTTATTGGCTATGCTCCATATGTCAACCGTATAGTT
CAACAATGGAATCTCCAGGATAATGATGATGATCAGCTCTTTTACACTAAAGTTTACATT
GATCCACTGAAAAGGGAAGCTATTAACATCACATTGGATCACAAATGCAAAATTTTCCAG
ACCTTAAATGGAGCTGTAGATGAAGTTGTTTTAAAATTTGAAAATGGCAAAGCCAGAGCT
AAGAATACATTTTATGAAACATTACCAGTGGCAATTAATGGAAATGGACCCACCAAGATT
CTCCTGAATTATTTTGGAAACTATGTACCCAATTCATGGACACAGGATAATGGCTGCACT
CTTTGTGAATTCGATACAGTCGACTTGTCTGCAGTAGATGTCCATCCAAACGTATCAATA
GGTGTTTTTATTGAGCAACCAACCCCTTTTCTACCTCGGTTTCTGGACATATTGTTGACA
CTGGATTACCCAAAAGAAGCACTTAAACTTTTTATTCATAACAAAGAAGTTTATCATGAA
AAGGACATCAAGGTATTTTTTGATAAAGCTAAGCATGAAATCAAAACTATAAAAATAGTA
GGACCAGAAGAAAATCTAAGTCAAGCGGAAGCCAGAAACATGGGAATGGACTTTTGCCGT
CAGGATGAAAAGTGTGATTATTACTTTAGTGTGGATGCAGATGTTGTTTTGACAAATCCA
AGGACTTTAAAAATTTTGATTGAACAAAACAGAAAGATCATTGCTCCTCTTGTAACTCGT
CATGGAAAGCTGTGGTCCAATTTCTGGGGAGCATTGAGTCCTGATGGATACTATGCACGA
TCTGAAGATTATGTGGATATTGTTCAAGGGAATAGAGTAGGAGTATGGAATGTCCCATAT
ATGGCTAATGTGTACTTAATTAAAGGAAAGACACTCCGATCAGAGATGAATGAAAGGAAC
TATTTTGTTCGTGATAAACTGGATCCTGATATGGCTCTTTGCCGAAATGCTAGAGAAATG
GGTGTATTTATGTACATTTCTAATAGACATGAATTTGGAAGGCTATTATCCACTGCTAAT
TACAATACTTCCCATTATAACAATGACCTCTGGCAGATTTTTGAAAATCCTGTGGACTGG
AAGGAAAAGTATATAAACCGTGATTATTCAAAGATTTTCACTGAAAATATAGTTGAACAG
CCCTGTCCAGATGTCTTTTGGTTCCCCATATTTTCTGAAAAAGCCTGTGATGAATTGGTA
GAAGAAATGGAACATTACGGCAAATGGTCTGGGGGAAAACATCATGATAGCCGTATATCT
GGTGGTTATGAAAATGTCCCAACTGATGATATCCACATGAAGCAAGTTGATCTGGAGAAT
GTATGGCTTGATTTTATCCGGGAGTTCATTGCACCAGTTACACTGAAGGTCTTTGCAGGC
TATTATACGAAGGGATTTGCACTACTGAATTTTGTAGTAAAATACTCCCCTGAACGACAG
CGTTCTCTTCGTCCTCATCATGATGCTTCTACATTTACCATAAACATTGCACTTAATAAC
GTGGGAGAAGACTTTCAGGGAGGTGGTTGCAAATTTCTAAGGTACAATTGCTCTATTGAG
TCACCACGAAAAGGCTGGAGCTTCATGCATCCTGGGAGACTCACACATTTGCATGAAGGA
CTTCCTGTTAAAAATGGAACAAGATACATTGCAGTGTCATTTATAGATCCCTAA
Target 9 GenBank Gene ID
Target 9 GeneCard ID PLOD2 Link Image
Target 9 GenAtlas ID PLOD2 Link Image
Target 9 HGNC ID HGNC:9082 Link Image
Target 9 Chromosome Location 3
Target 9 Locus 3q23-q24
Target 9 SNPs SNPJam Report Link Image
Target 9 General References
  1. Yeowell HN, Walker LC: Tissue specificity of a new splice form of the human lysyl hydroxylase 2 gene. Matrix Biol. 1999 Apr;18(2):179-87. [PubMed Link Image]
  2. van der Slot AJ, Zuurmond AM, Bardoel AF, Wijmenga C, Pruijs HE, Sillence DO, Brinckmann J, Abraham DJ, Black CM, Verzijl N, DeGroot J, Hanemaaijer R, TeKoppele JM, Huizinga TW, Bank RA: Identification of PLOD2 as telopeptide lysyl hydroxylase, an important enzyme in fibrosis. J Biol Chem. 2003 Oct 17;278(42):40967-72. Epub 2003 Jul 24. [PubMed Link Image]
  3. Valtavaara M, Papponen H, Pirttila AM, Hiltunen K, Helander H, Myllyla R: Cloning and characterization of a novel human lysyl hydroxylase isoform highly expressed in pancreas and muscle. J Biol Chem. 1997 Mar 14;272(11):6831-4. [PubMed Link Image]
Target 9 Drug References
  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 Link Image]
  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 Link Image]
Drug Target 10 [top]
Target 10 ID 3938
Target 10 Name Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3
Target 10 Synonyms
  1. EC 1.14.11.4
  2. LH3
  3. Lysyl hydroxylase 3
  4. Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 precursor
Target 10 Gene Name PLOD3
Target 10 Protein Sequence >Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3
MTSSGPGPRFLLLLPLLLPPAASASDRPRGRDPVNPEKLLVITVATAETEGYLRFLRSAE
FFNYTVRTLGLGEEWRGGDVARTVGGGQKVRWLKKEMEKYADREDMIIMFVDSYDVILAG
SPTELLKKFVQSGSRLLFSAESFCWPEWGLAEQYPEVGTGKRFLNSGGFIGFATTIHQIV
RQWKYKDDDDDQLFYTRLYLDPGLREKLSLNLDHKSRIFQNLNGALDEVVLKFDRNRVRI
RNVAYDTLPIVVHGNGPTKLQLNYLGNYVPNGWTPEGGCGFCNQDRRTLPGGQPPPRVFL
AVFVEQPTPFLPRFLQRLLLLDYPPDRVTLFLHNNEVFHEPHIADSWPQLQDHFSAVKLV
GPEEALSPGEARDMAMDLCRQDPECEFYFSLDADAVLTNLQTLRILIEENRKVIAPMLSR
HGKLWSNFWGALSPDEYYARSEDYVELVQRKRVGVWNVPYISQAYVIRGDTLRMELPQRD
VFSGSDTDPDMAFCKSFRDKGIFLHLSNQHEFGRLLATSRYDTEHLHPDLWQIFDNPVDW
KEQYIHENYSRALEGEGIVEQPCPDVYWFPLLSEQMCDELVAEMEHYGQWSGGRHEDSRL
AGGYENVPTVDIHMKQVGYEDQWLQLLRTYVGPMTESLFPGYHTKARAVMNFVVRYRPDE
QPSLRPHHDSSTFTLNVALNHKGLDYEGGGCRFLRYDCVISSPRKGWALLHPGRLTHYHE
GLPTTWGTRYIMVSFVDP
Target 10 Number of Residues 750
Target 10 Molecular Weight 84786
Target 10 Theoretical pI 5.95
Target 10 GO Classification
Function
procollagen-lysine 5-dioxygenase activity
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Process
physiological process
metabolism
macromolecule metabolism
protein metabolism
Component
organelle
membrane-bound organelle
intracellular membrane-bound organelle
endoplasmic reticulum
Target 10 General Function Not Available
Target 10 Specific Function Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links
Target 10 Pathways
Name SMPDB Link KEGG Link
Lysine degradation SMP00037 Link Image map00310 Link Image
Target 10 Reactions
  • procollagen L-lysine + 2-oxoglutarate + O2 = procollagen 5-hydroxy-L-lysine + succinate + CO2 ALL_REAC (other) R03376
Target 10 Pfam Domain Function
Target 10 Signals
  • 1-24
Target 10 Transmembrane Regions
  • None
Target 10 Essentiality Non-Essential
Target 10 GenBank ID Protein 3153235 Link Image
Target 10 UniProtKB/Swiss-Prot ID O60568 Link Image
Target 10 UniProtKB/Swiss-Prot Entry Name PLOD3_HUMAN Link Image
Target 10 PDB ID Not Available
Target 10 Cellular Location
  • Endoplasmic reticulum
Target 10 Gene Sequence >2217 bp
ATGACCTCCTCGGGGCCTGGACCCCGGTTCCTGCTGCTGCTGCCGCTGCTGCTGCCCCCT
GCGGCCTCAGCCTCCGACCGGCCCCGGGGCCGAGACCCGGTCAACCCAGAGAAGCTGCTG
GTGATCACTGTGGCCACAGCTGAAACCGAGGGGTACCTGCGTTTCCTGCGCTCTGCGGAG
TTCTTCAACTACACTGTGCGGACCCTGGGCCTGGGAGAGGAGTGGCGAGGGGGTGATGTG
GCTCGAACAGTTGGTGGAGGACAGAAGGTCCGGTGGTTAAAGAAGGAAATGGAGAAATAC
GCTGACCGGGAGGATATGATCATCATGTTTGTGGATAGCTACGACGTGATTCTGGCCGGC
AGCCCCACAGAGCTGCTGAAGAAGTTCGTCCAGAGTGGCAGCCGCCTGCTCTTCTCTGCA
GAGAGCTTCTGCTGGCCCGAGTGGGGGCTGGCGGAGCAGTACCCTGAGGTGGGCACGGGG
AAGCGCTTCCTCAATTCTGGTGGATTCATCGGTTTTGCCACCACCATCCACCAAATCGTG
CGCCAGTGGAAGTACAAGGATGATGACGACGACCAGCTGTTCTACACACGGCTCTACCTG
GACCCAGGACTGAGGGAGAAACTCAGCCTTAATCTGGATCATAAGTCTCGGATCTTTCAG
AACCTCAACGGGGCTTTAGATGAAGTGGTTTTAAAGTTTGATCGGAACCGTGTGCGTATC
CGGAACGTGGCCTACGACACGCTCCCCATTGTGGTCCATGGAAACGGTCCCACTAAGCTG
CAGCTCAACTACCTGGGAAACTACGTCCCCAATGGCTGGACTCCTGAGGGAGGCTGTGGC
TTCTGCAACCAGGACCGGAGGACACTCCCGGGGGGGCAGCCTCCCCCCCGGGTGTTTCTG
GCCGTGTTTGTGGAACAGCCTACTCCGTTTCTGCCCCGCTTCCTGCAGCGGCTGCTACTC
CTGGACTATCCCCCCGACAGGGTCACCCTTTTCCTGCACAACAACGAGGTCTTCCATGAA
CCCCACATCGCTGACTCCTGGCCGCAGCTCCAGGACCACTTCTCAGCTGTGAAGCTCGTG
GGGCCGGAGGAGGCTCTGAGCCCAGGCGAGGCCAGGGACATGGCCATGGACCTGTGTCGG
CAGGACCCCGAGTGTGAGTTCTACTTCAGCCTGGACGCCGACGCTGTCCTCACCAACCTG
CAGACCCTGCGTATCCTCATTGAGGAGAACAGGAAGGTGATCGCCCCCATGCTGTCCCGC
CACGGCAAGCTGTGGTCCAACTTCTGGGGCGCCCTGAGCCCCGATGAGTACTACGCCCGC
TCCGAGGACTACGTGGAGCTGGTGCAGCGGAAGCGAGTGGGTGTGTGGAATGTACCATAC
ATCTCCCAGGCCTATGTGATCCGGGGTGATACCCTGCGGATGGAGCTGCCCCAGAGGGAT
GTGTTCTCGGGCAGTGACACAGACCCGGACATGGCCTTCTGTAAGAGCTTTCGAGACAAG
GGCATCTTCCTCCATCTGAGCAATCAGCATGAATTTGGCCGGCTCCTGGCCACTTCCAGA
TACGACACGGAGCACCTGCACCCCGACCTCTGGCAGATCTTCGACAACCCCGTCGACTGG
AAGGAGCAGTACATCCACGAGAACTACAGCCGGGCCCTGGAAGGGGAAGGAATCGTGGAG
CAGCCATGCCCGGACGTGTACTGGTTCCCACTGCTGTCAGAACAAATGTGTGATGAGCTG
GTGGCAGAGATGGAGCACTACGGCCAGTGGTCAGGCGGCCGGCATGAGGATTCAAGGCTG
GCTGGAGGCTACGAGAATGTGCCCACCGTGGACATCCACATGAAGCAGGTGGGGTACGAG
GACCAGTGGCTGCAGCTGCTGCGGACGTATGTGGGCCCCATGACCGAGAGCCTGTTTCCC
GGTTACCACACCAAGGCGCGGGCGGTGATGAACTTTGTGGTTCGCTACCGGCCAGACGAG
CAGCCGTCTCTGCGGCCACACCACGACTCATCCACCTTCACCCTCAACGTTGCCCTCAAC
CACAAGGGCCTGGACTATGAGGGAGGTGGCTGCCGCTTCCTGCGCTACGACTGTGTGATC
TCCTCCCCGAGGAAGGGCTGGGCACTCCTGCACCCCGGCCGCCTCACCCACTACCACGAG
GGGCTGCCAACGACCTGGGGCACACGCTACATCATGGTGTCCTTTGTCGACCCCTGA
Target 10 GenBank Gene ID
Target 10 GeneCard ID PLOD3 Link Image
Target 10 GenAtlas ID PLOD3 Link Image
Target 10 HGNC ID HGNC:9083 Link Image
Target 10 Chromosome Location 7
Target 10 Locus 7q22
Target 10 SNPs SNPJam Report Link Image
Target 10 General References
  1. Rautavuoma K, Passoja K, Helaakoski T, Kivirikko KI: Complete exon-intron organization of the gene for human lysyl hydroxylase 3 (LH3). Matrix Biol. 2000 Feb;19(1):73-9. [PubMed Link Image]
  2. 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 Link Image]
  3. Valtavaara M, Szpirer C, Szpirer J, Myllyla R: Primary structure, tissue distribution, and chromosomal localization of a novel isoform of lysyl hydroxylase (lysyl hydroxylase 3) J Biol Chem. 1998 May 22;273(21):12881-6. [PubMed Link Image]
  4. Passoja K, Rautavuoma K, Ala-Kokko L, Kosonen T, Kivirikko KI: Cloning and characterization of a third human lysyl hydroxylase isoform. Proc Natl Acad Sci U S A. 1998 Sep 1;95(18):10482-6. [PubMed Link Image]
Target 10 Drug References
  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 Link Image]
  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 Link Image]
Drug Target 11 [top]
Target 11 ID 3940
Target 11 Name Gamma-butyrobetaine dioxygenase
Target 11 Synonyms
  1. EC 1.14.11.1
  2. Gamma- BBH
  3. Gamma-butyrobetaine hydroxylase
  4. Gamma-butyrobetaine,2- oxoglutarate dioxygenase
Target 11 Gene Name BBOX1
Target 11 Protein Sequence >Gamma-butyrobetaine dioxygenase
MACTIQKAEALDGAHLMQILWYDEEESLYPAVWLRDNCPCSDCYLDSAKARKLLVEALDV
NIGIKGLIFDRKKVYITWPDEHYSEFQADWLKKRCFSKQARAKLQRELFFPECQYWGSEL
QLPTLDFEDVLRYDEHAYKWLSTLKKVGIVRLTGASDKPGEVSKLGKRMGFLYLTFYGHT
WQVQDKIDANNVAYTTGKLSFHTDYPALHHPPGVQLLHCIKQTVTGGDSEIVDGFNVCQK
LKKNNPQAFQILSSTFVDFTDIGVDYCDFSVQSKHKIIELDDKGQVVRINFNNATRDTIF
DVPVERVQPFYAALKEFVDLMNSKESKFTFKMNPGDVITFDNWRLLHGRRSYEAGTEISR
HLEGAYADWDVVMSRLRILRQRVENGN
Target 11 Number of Residues 393
Target 11 Molecular Weight 44715
Target 11 Theoretical pI 6.73
Target 11 GO Classification
Function
catalytic activity
oxidoreductase activity
Process
physiological process
metabolism
cellular metabolism
generation of precursor metabolites and energy
electron transport
Component
Not Available
Target 11 General Function Not Available
Target 11 Specific Function Catalyzes the formation of L-carnitine from gamma- butyrobetaine
Target 11 Pathways
Name SMPDB Link KEGG Link
Lysine degradation SMP00037 Link Image map00310 Link Image
Target 11 Reactions
  • 4-trimethylammoniobutanoate + 2-oxoglutarate + O2 = 3-hydroxy-4-trimethylammoniobutanoate + succinate + CO2
Target 11 Pfam Domain Function
Target 11 Signals
  • None
Target 11 Transmembrane Regions
  • None
Target 11 Essentiality Non-Essential
Target 11 GenBank ID Protein 3746805 Link Image
Target 11 UniProtKB/Swiss-Prot ID O75936 Link Image
Target 11 UniProtKB/Swiss-Prot Entry Name BODG_HUMAN Link Image
Target 11 PDB ID Not Available
Target 11 Cellular Location
  • Cytoplasm
Target 11 Gene Sequence >1164 bp
ATGGCTTGTACCATCCAAAAGGCAGAAGCACTTGACGGGGCTCATTTGATGCAGATCCTC
TGGTATGATGAGGAAGAGTCTCTCTACCCAGCTGTATGGTTGAGAGACAACTGTCCGTGC
TCTGATTGCTACCTGGATTCTGCAAAAGCACGGAAACTTCTAGTGGAAGCTCTTGATGTG
AACATTGGAATTAAAGGCTTGATATTTGACAGAAAAAAGGTGTACATCACATGGCCCGAT
GAGCATTACAGTGAATTCCAGGCTGATTGGCTGAAGAAAAGATGCTTTTCCAAGCAGGCC
AGAGCAAAGCTCCAAAGAGAATTGTTTTTTCCAGAATGCCAATACTGGGGCTCAGAGCTC
CAGCTACCCACTTTGGATTTTGAAGATGTTTTAAGATATGATGAACATGCATACAAGTGG
CTCTCCACCCTCAAGAAAGTAGGCATAGTAAGACTCACCGGAGCATCTGACAAACCAGGA
GAAGTTTCAAAACTTGGGAAAAGGATGGGTTTCCTCTATCTCACATTTTATGGACATACT
TGGCAAGTGCAAGACAAAATCGATGCAAACAATGTGGCTTACACAACTGGGAAGCTAAGC
TTTCACACTGATTATCCAGCCCTCCATCATCCACCTGGGGTTCAGCTTCTTCACTGCATA
AAGCAAACAGTCACAGGGGGTGATTCAGAAATTGTAGATGGGTTTAATGTGTGCCAAAAA
CTAAAGAAAAATAATCCTCAGGCATTCCAGATTTTGTCCTCTACCTTTGTGGACTTTACA
GACATTGGAGTGGATTACTGTGATTTTTCTGTACAATCAAAACATAAAATTATAGAGTTA
GATGATAAAGGCCAAGTGGTTCGCATCAACTTCAATAACGCAACTAGGGACACAATATTT
GATGTACCTGTTGAAAGAGTTCAGCCTTTTTATGCTGCTCTGAAGGAGTTTGTTGACCTC
ATGAACAGCAAAGAATCCAAGTTTACCTTCAAGATGAATCCAGGTGATGTGATTACTTTT
GATAACTGGCGCTTACTTCATGGCCGACGTAGCTATGAAGCAGGAACTGAGATATCCCGC
CATCTAGAAGGAGCTTATGCTGACTGGGATGTGGTCATGTCAAGGCTTCGTATCTTAAGG
CAGAGGGTGGAGAATGGAAACTGA
Target 11 GenBank Gene ID
Target 11 GeneCard ID BBOX1 Link Image
Target 11 GenAtlas ID BBOX1 Link Image
Target 11 HGNC ID HGNC:964 Link Image
Target 11 Chromosome Location 11
Target 11 Locus 11p14.2
Target 11 SNPs SNPJam Report Link Image
Target 11 General References
  1. Vaz FM, van Gool S, Ofman R, Ijlst L, Wanders RJ: Carnitine biosynthesis: identification of the cDNA encoding human gamma-butyrobetaine hydroxylase. Biochem Biophys Res Commun. 1998 Sep 18;250(2):506-10. [PubMed Link Image]
Target 11 Drug References
  1. Vaz FM, van Gool S, Ofman R, IJlst L, Wanders RJ: Carnitine biosynthesis. Purification of gamma-butyrobetaine hydroxylase from rat liver. Adv Exp Med Biol. 1999;466:117-24. [PubMed Link Image]
  2. 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 Link Image]
  3. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
  4. Rebouche CJ: Ascorbic acid and carnitine biosynthesis. Am J Clin Nutr. 1991 Dec;54(6 Suppl):1147S-1152S. [PubMed Link Image]
  5. Dunn WA, Rettura G, Seifter E, Englard S: Carnitine biosynthesis from gamma-butyrobetaine and from exogenous protein-bound 6-N-trimethyl-L-lysine by the perfused guinea pig liver. Effect of ascorbate deficiency on the in situ activity of gamma-butyrobetaine hydroxylase. J Biol Chem. 1984 Sep 10;259(17):10764-70. [PubMed Link Image]
Drug Target 12 [top]
Target 12 ID 3943
Target 12 Name Peptidyl-glycine alpha-amidating monooxygenase
Target 12 Synonyms
  1. EC 1.14.17.3
  2. PAM
  3. PHM)
  4. Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (EC 4.3.2.5
  5. Peptidyl-glycine alpha-amidating monooxygenase precursor
  6. Peptidylamidoglycolate lyase
Target 12 Gene Name PAM
Target 12 Protein Sequence >Peptidyl-glycine alpha-amidating monooxygenase
MAGRVPSLLVLLVFPSSCLAFRSPLSVFKRFKETTRPFSNECLGTTRPVVPIDSSDFALD
IRMPGVTPKQSDTYFCMSMRIPVDEEAFVIDFKPRASMDTVHHMLLFGCNMPSSTGSYWF
CDEGTCTDKANILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNNKD
CSGVSLHLTRLPQPLIAGMYLMMSVDTVIPAGEKVVNSDISCHYKNYPMHVFAYRVHTHH
LGKVVSGYRVRNGQWTLIGRQSPQLPQAFYPVGHPVDVSFGDLLAARCVFTGEGRTEATH
IGGTSSDEMCNLYIMYYMEAKHAVSFMTCTQNVAPDMFRTIPPEANIPIPVKSDMVMMHE
HHKETEYKDKIPLLQQPKREEEEVLDQGDFYSLLSKLLGEREDVVHVHKYNPTEKAESES
DLVAEIANVVQKKDLGRSDAREGAEHERGNAILVRDRIHKFHRLVSTLRPPESRVFSLQQ
PPPGEGTWEPEHTGDFHMEEALDWPGVYLLPGQVSGVALDPKNNLVIFHRGDHVWDGNSF
DSKFVYQQIGLGPIEEDTILVIDPNNAAVLQSSGKNLFYLPHGLSIDKDGNYWVTDVALH
QVFKLDPNNKEGPVLILGRSMQPGSDQNHFCQPTDVAVDPGTGAIYVSDGYCNSRIVQFS
PSGKFITQWGEESSGSSPLPGQFTVPHSLALVPLLGQLCVADRENGRIQCFKTDTKEFVR
EIKHSSFGRNVFAISYIPGLLFAVNGKPHFGDQEPVQGFVMNFSNGEIIDIFKPVRKHFD
MPHDIVASEDGTVYIGDAHTNTVWKFTLTEKLEHRSVKKAGIEVQEIKEAEAVVETKMEN
KPTSSELQKMQEKQKLIKEPGSGVPVVLITTLLVIPVVVLLAIAIFIRWKKSRAFGDSEH
KLETSSGRVLGRFRGKGSGGLNLGNFFASRKGYSRKGFDRLSTEGSDQEKEDDGSESEEE
YSAPLPALAPSSS
Target 12 Number of Residues 989
Target 12 Molecular Weight 108333
Target 12 Theoretical pI 6.39
Target 12 GO Classification
Function
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen
peptidylglycine monooxygenase activity
binding
ion binding
cation binding
transition metal ion binding
copper ion binding
catalytic activity
oxidoreductase activity
monooxygenase activity
Process
physiological process
metabolism
cellular metabolism
peptide metabolism
Component
cell
membrane
Target 12 General Function Not Available
Target 12 Specific Function Bifunctional enzyme that catalyzes 2 sequencial steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity
Target 12 Pathways Not Available
Target 12 Reactions
  • peptidylamidoglycolate = peptidyl amide + glyoxylate
Target 12 Pfam Domain Function
Target 12 Signals
  • 1-20
Target 12 Transmembrane Regions
  • 864-887
Target 12 Essentiality Non-Essential
Target 12 GenBank ID Protein 189595 Link Image
Target 12 UniProtKB/Swiss-Prot ID P19021 Link Image
Target 12 UniProtKB/Swiss-Prot Entry Name AMD_HUMAN Link Image
Target 12 PDB ID 1SDW Link Image
Target 12 PDB File Show
Target 12 3D Structure
Target 12 Cellular Location
  • Membrane
Target 12 Gene Sequence >2925 bp
ATGGCTGGCCGCGTCCCTAGCCTGCTAGTTCTCCTTGTTTTTCCAAGCAGCTGTTTGGCT
TTCCGAAGCCCACTTTCTGTCTTTAAGAGGTTTAAAGAAACTACCAGACCATTTTCCAAT
GAATGTCTTGGTACCACCAGACCCGTAGTTCCTATTGATTCATCAGATTTTGCATTGGAT
ATTCGCATGCCTGGGGTTACACCTAAACAGTCCGATACATACTTCTGCATGTCTATGCGA
ATACCAGTGGATGAGGAAGCCTTCGTGATTGACTTCAAGCCTCGAGCCAGCATGGATACT
GTCCATCACATGTTACTTTTTGGATGCAATATGCCTTCATCCACTGGAAGTTACTGGTTT
TGTGATGAAGGAACCTGTACAGATAAAGCCAATATTCTGTATGCCTGGGCGAGAAATGCT
CCCCCTACCCGGCTCCCCAAAGGTGTTGGATTCAGAGTTGGAGGAGAGACTGGAAGTAAA
TACTTTGTACTACAGGTACACTATGGGGATATTAGTGCTTTTAGAGATAATAACAAGGAC
TGTTCTGGTGTGTCCTTACACCTCACACGTCTGCCACAGCCTTTAATTGCTGGCATGTAC
CTTATGATGTCTGTTGACACTGTTATCCCAGCAGGAGAAAAAGTGGTGAATTCTGACATT
TCATGCCATTATAAAAATTATCCAATGCATGTCTTTGCCTATAGAGTTCACACTCACCAT
TTAGGTAAGGTAGTAAGTGGATACAGAGTAAGAAATGGACAGTGGACACTGATTGGACGG
CAGAGCCCTCAGCTGCCACAGGCTTTCTACCCTGTGGGGCATCCAGTTGATGTAAGTTTT
GGTGACCTACTGGCTGCAAGATGTGTATTCACTGGTGAAGGAAGGACAGAAGCCACACAC
ATTGGTGGCACGTCTAGTGATGAAATGTGCAACTTATACATTATGTATTACATGGAAGCC
AAGCATGCAGTTTCTTTCATGACCTGTACCCAGAATGTAGCTCCAGATATGTTCAGAACC
ATACCACCAGAGGCCAACATTCCAATTCCCGTGAAGTCTGATATGGTTATGATGCATGAA
CATCATAAAGAAACAGAATATAAAGATAAGATTCCTTTACTACAGCAGCCAAAACGAGAA
GAAGAAGAAGTGTTAGACCAGGGTGATTTCTATTCACTACTTTCCAAGCTGCTAGGAGAA
AGGGAAGATGTTGTTCATGTGCACAAATATAATCCTACAGAAAAGGCAGAATCAGAGTCA
GACCTGGTAGCTGAGATTGCAAATGTAGTCCAAAAAAAGGATCTTGGTCGATCTGATGCC
AGAGAGGGTGCAGAACATGAGAGGGGTAATGCTATTCTTGTCAGAGACAGAATTCACAAA
TTCCACAGACTAGTATCTACCTTGAGGCCACCAGAGAGCAGAGTTTTCTCATTACAGCAG
CCCCCACCTGGTGAAGGCACCTGGGAACCAGAACACACAGGAGATTTCCACATGGAAGAG
GCACTGGATTGGCCTGGAGTATACTTGTTACCAGGCCAGGTTTCTGGGGTGGCTCTAGAC
CCTAAGAATAACCTGGTGATTTTCCACAGAGGTGACCATGTCTGGGATGGAAACTCGTTT
GACAGCAAGTTTGTTTACCAGCAAATAGGACTCGGACCAATTGAAGAAGACACTATTCTT
GTCATAGATCCAAATAATGCTGCAGTACTCCAGTCCAGTGAAAAAAATCTGTTTTACTTG
CCACATGGCTTGAGTATAGATAAAGATGGGAATTATTGGGTCACAGACGTGGCTCTCCAT
CAGGTGTTCAAACTGGATCCAAACAATAAAGAAGGCCCTGTATTAATCCTGGGAAGGAGC
ATGCAACCAGGCAGTGACCAGAATCACTTCTGTCAACCCACTGATGTGGCTGTGGATCCA
GGCACTGGAGCCATTTATGTATCAGATGGTTACTGCAACAGCAGGATTGTGCAGTTTTCA
CCAAGTGGAAAGTTCATCACACAGTGGGGAGAAGAGTCTTCAGGGAGCAGTCCTCTGCCA
GGCCAGTTCACTGTTCCTCACAGCTTGGCTCTTGTGCCTCTTTTGGGCCAATTATGTGTG
GCAGACCGGGAAAATGGTCGGATCCAGTGTTTTAAAACTGACACCAAAGAATTTGTGAGA
GAGATTAAGCATTCATCATTTGGAAGAAATGTATTTGCAATTTCATATATACCAGGCTTG
CTCTTTGCAGTGAATGGGAAGCCTCATTTTGGGGACCAAGAACCTGTACAAGGATTTGTG
ATGAACTTTTCCAATGGGGAAATTATAGACATCTTCAAGCCAGTGCGCAAGCACTTTGAT
ATGCCTCATGATATTGTTGCATCTGAAGATGGGACCGTGTACATTGGAGATGCTCATACC
AACACCGTGTGGAAGTTCACCTTGACTGAGAAATTGGAACATCGATCAGTTAAAAAGGCT
GGCATTGAGGTCCAGGAAATCAAAGAAGCCGAGGCAGTTGTTGAAACCAAAATGGAGAAC
AAACCCACCTCCTCAGAATTGCAGAAGATGCAAGAGAAACAGAAGCTGATCAAAGAGCCA
GGCTCGGGAGTGCCTGTTGTTCTCATTACAACCCTTCTGGTTATTCCGGTGGTTGTCCTG
CTGGCCATTGCCATATTTATTCGGTGGAAAAAATCAAGGGCCTTTGGAGCAGATTCTGAA
CACAAACTCGAGACGAGTTCAGGAAGAGTACTGGGAAGATTTAGAGGAAAGGGAAGTGGA
GGCTTAAACCTTGGTAATTTCTTTGCAAGCCGTAAGGGCTACAGTCGAAAAGGGTTTGAC
CGGCTTAGCACTGAGGGCAGTGACCAAGAGAAAGAGGATGATGGAAGTGAATCAGAAGAG
GAGTATTCAGCACCTCTGCCTGCGCTCGCACCTTCCTCCTCCTGA
Target 12 GenBank Gene ID
Target 12 GeneCard ID PAM Link Image
Target 12 GenAtlas ID PAM Link Image
Target 12 HGNC ID HGNC:8596 Link Image
Target 12 Chromosome Location 5
Target 12 Locus 5q14-q21
Target 12 SNPs SNPJam Report Link Image
Target 12 General References
  1. Glauder J, Ragg H, Rauch J, Engels JW: Human peptidylglycine alpha-amidating monooxygenase: cDNA, cloning and functional expression of a truncated form in COS cells. Biochem Biophys Res Commun. 1990 Jun 15;169(2):551-8. [PubMed Link Image]
  2. Tateishi K, Arakawa F, Misumi Y, Treston AM, Vos M, Matsuoka Y: Isolation and functional expression of human pancreatic peptidylglycine alpha-amidating monooxygenase. Biochem Biophys Res Commun. 1994 Nov 30;205(1):282-90. [PubMed Link Image]
  3. Yun HY, Keutmann HT, Eipper BA: Alternative splicing governs sulfation of tyrosine or oligosaccharide on peptidylglycine alpha-amidating monooxygenase. J Biol Chem. 1994 Apr 8;269(14):10946-55. [PubMed Link Image]
  4. Husten EJ, Tausk FA, Keutmann HT, Eipper BA: Use of endoproteases to identify catalytic domains, linker regions, and functional interactions in soluble peptidylglycine alpha-amidating monooxygenase. J Biol Chem. 1993 May 5;268(13):9709-17. [PubMed Link Image]
Target 12 Drug References
  1. Floryszak-Wieczorek J, Milczarek G, Arasimowicz M, Ciszewski A: Do nitric oxide donors mimic endogenous NO-related response in plants? Planta. 2006 Nov;224(6):1363-72. Epub 2006 Jun 14. [PubMed Link Image]
  2. Crespo A, Marti MA, Roitberg AE, Amzel LM, Estrin DA: The catalytic mechanism of peptidylglycine alpha-hydroxylating monooxygenase investigated by computer simulation. J Am Chem Soc. 2006 Oct 4;128(39):12817-28. [PubMed Link Image]
  3. Romero I, Teresa Sanchez-Ballesta M, Maldonado R, Isabel Escribano M, Merodio C: Anthocyanin, antioxidant activity and stress-induced gene expression in high CO(2)-treated table grapes stored at low temperature. J Plant Physiol. 2007 Jun 12;. [PubMed Link Image]
Drug Target 13 [top]
Target 13 ID 3945
Target 13 Name Prolyl 3-hydroxylase 1
Target 13 Synonyms
  1. EC 1.14.11.7
  2. Growth suppressor 1
  3. Leprecan-1
  4. Leucine- and proline- enriched proteoglycan 1
  5. Prolyl 3-hydroxylase 1 precursor
Target 13 Gene Name LEPRE1
Target 13 Protein Sequence >Prolyl 3-hydroxylase 1
MAVRALKLLTTLLAVVAAASQAEVESEAGWGMVTPDLLFAEGTAAYARGDWPGVVLSMER
ALRSRAALRALRLRCRTQCAADFPWELDPDWSPSPAQASGAAALRDLSFFGGLLRRAACL
RRCLGPPAAHSLSEEMELEFRKRSPYNYLQVAYFKINKLEKAVAAAHTFFVGNPEHMEMQ
QNLDYYQTMSGVKEADFKDLETQPHMQEFRLGVRLYSEEQPQEAVPHLEAALQEYFVAYE
ECRALCEGPYDYDGYNYLEYNADLFQAITDHYIQVLNCKQNCVTELASHPSREKPFEDFL
PSHYNYLQFAYYNIGNYTQAVECAKTYLLFFPNDEVMNQNLAYYAAMLGEEHTRSIGPRE
SAKEYRQRSLLEKELLFFAYDVFGIPFVDPDSWTPEEVIPKRLQEKQKSERETAVRISQE
IGNLMKEIETLVEEKTKESLDVSRLTREGGPLLYEGISLTMNSKLLNGSQRVVMDGVISD
HECQELQRLTNVAATSGDGYRGQTSPHTPNEKFYGVTVFKALKLGQEGKVPLQSAHLYYN
VTEKVRRIMESYFRLDTPLYFSYSHLVCRTAIEEVQAERKDDSHPVHVDNCILNAETLVC
VKEPPAYTFRDYSAILYLNGDFDGGNFYFTELDAKTVTAEVQPQCGRAVGFSSGTENPHG
VKAVTRGQRCAIALWFTLDPRHSERDRVQADDLVKMLFSPEEMDLSQEQPLDAQQGPPEP
AQESLSGSESKPKDEL
Target 13 Number of Residues 748
Target 13 Molecular Weight 83395
Target 13 Theoretical pI 4.79
Target 13 GO Classification
Function
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Process
physiological process
metabolism
macromolecule metabolism
protein metabolism
Component
Not Available
Target 13 General Function Not Available
Target 13 Specific Function Basement membrane-associated chondroitin sulfate proteoglycan (CSPG). Has prolyl 3-hydroxylase activity catalyzing the posttranslational formation of 3-hydroxyproline in -Xaa-Pro- Gly- sequences in collagens, especially types IV and V. May be involved in the secretory pathway of cells. Has growth suppressive activity in fibroblasts
Target 13 Pathways Not Available
Target 13 Reactions
  • procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-3-hydroxy-L-proline + succinate + CO2
Target 13 Pfam Domain Function
Target 13 Signals
  • 1-22
Target 13 Transmembrane Regions
  • None
Target 13 Essentiality Non-Essential
Target 13 GenBank ID Protein 11127636 Link Image
Target 13 UniProtKB/Swiss-Prot ID Q32P28 Link Image
Target 13 UniProtKB/Swiss-Prot Entry Name P3H1_HUMAN Link Image
Target 13 PDB ID Not Available
Target 13 Cellular Location
  • Endoplasmic reticulum
Target 13 Gene Sequence >2211 bp
ATGGCGGTACGCGCGTTGAAGCTGCTGACCACACTGCTGGCTGTCGTGGCCGCTGCCTCC
CAAGCCGAGGTCGAGTCCGAGGCAGGATGGGGCATGGTGACGCCTGATCTGCTCTTCGCC
GAGGGGACCGCAGCCTACGCGCGCGGGGACTGGCCCGGGGTGGTCCTGAGCATGGAACGG
GCGCTGCGCTCCCGGGCAGCCCTCCGCGCCCTTCGCCTGCGCTGCCGCACCCAGTGTGCC
GCCGACTTCCCGTGGGAGCTGGACCCCGACTGGTCCCCCAGCCCGGCCCAGGCCTCGGGC
GCCGGCGCCCTGCGCGACCTGAGCTTCTTCGGGGGCCTTCTGCGTCGCGCTGCCTGCCTG
CGCCGCTGCCTCGGGCCGCCGGCCGCCCACTCGCTCAGCGAAGAGATGGAGCTGGAGTTC
CGCAAGCGGAGCCCCTACAACTACCTGCAGGTCGCCTACTTCAAGATCAACAAGTTGGAG
AAAGCTGTTGCTGCAGCACACACCTTCTTCGTGGGCAATCCTGAGCACATGGAAATGCAG
CAGAACCTAGACTATTACCAAACCATGTCTGGAGTGAAGGAGGCCGACTTCAAGGATCTT
GAGACTCAACCCCATATGCAAGAATTTCGACTGGGAGTGCGACTCTACTCAGAGGAACAG
CCACAGGAAGCTGTGCCCCACCTAGAGGCGGCGCTGCAAGAATACTTTGTGGCCTATGAG
GAGTGCCGTGCCCTCTGCGAAGGGCCCTATGACTACGATGGCTACAACTACCTTGAGTAC
AACGCTGACCTCTTCCAGGCCATCACAGATCATTACATCCAGGTCCTCAACTGTAAGCAG
AACTGTGTCACGGAGCTTGCTTCCCACCCAAGTCGAGAGAAGCCCTTTGAAGACTTCCTC
CCATCGCATTATAATTATCTGCAGTTTGCCTACTATAACATTGGGAATTATACACAAGCT
GGTGAATGTGCCAAGACCTATCTTCTCTTCTTCCCCAATGACGAGGTGATGAACCAAAAT
TTGGCCTATTATGCAGCTATGCTTGGAGAAGAACACACCAGATCCATCGGCCCCCGTGAG
AGTGCCAAGGAGTACCGACAGCGAAGCCTACTGGAAAAAGAACTGCTTTTCTTCGCTTAT
GATGTTTTTGGAATTCCCTTTGTGGATCCGGATTCATGGACTCCAGAAGAAGTGATTCCC
AAGAGATTGCAAGAGAAACAGAAGTCAGAACGGGAAACAGCCGTACGCATCTCCCAGGAG
ATTGGGAACCTTATGAAGGAAATCGAGACCCTTGTGGAAGAGAAGACCAAGGAGTCACTG
GATGTGAGCAGACTGACCCGGGAAGGTGGCCCCCTGCTGTATGAAGGCATCAGTCTCACC
ATGAACTCCAAACTCCTGAATGGTTACCAGCGGGTGGTGATGGACGGCGTAATCTCTGAC
CACGAGTGTCAGGAGCTGCAGAGACTGACCAATGTGGCAGCAACCTCAGGAGATGGCTAC
CGGGGTCAGACCTCCCCACATACTCCCAATGAAAAGTTCTATGGTGTCACTGTCTTCAAA
GCCCTCAAGCTGGGGCAAGAAGGCAAAGTTCCTCTGCAGAGTGCCCACCTGTACTACAAC
GTGACGGAGAAAGTGCGGCGCATCATGGAGTCCTACTTCCGCCTGGATACGCCCCTCTAC
TTTTCCTACTCTCATCTGGTGTGCCGCACTGCCATCGAAGAGGTCCAGGCAGAGAGGAAG
GATGATAGTCATCCAGTCCACGTGGACAACTGCATCCTGAATGCCGAGACCCTCGTGTGT
GTCAAAGAGCCCCCAGCCTACACCTTCCGCGACTACAGCGCCATCCTTTACCTAAATGGG
GACTTCGATGGCGGAAACTTTTATTTCACTGAACTGGATGCCAAGACCGTGACGGCAGAG
GTGCAGCCTCAGTGTGGAAGAGCCGTGGGATTCTCTTCAGGCACTGAAAACCCACATGGA
GTGAAGGCTGTCACCAGGGGGCAGCGCTGTGCCATCGCCCTGTGGTTCACCCTGGACCCT
CGACACAGCGAGCGGGACAGGGTGCAGGCAGATGACCTGGTGAAGATGCTCTTCAGCCCA
GAAGAGATGGACCTCTCCCAGGAGCAGCCCCTGGATGCCCAGCAGGGCCCCCCCGAACCT
GCACAAGAGTCTCTCTCAGGCAGTGAATCGAAGCCCAAGGATGAGCTATGA
Target 13 GenBank Gene ID
Target 13 GeneCard ID LEPRE1 Link Image
Target 13 GenAtlas ID LEPRE1 Link Image
Target 13 HGNC ID HGNC:19316 Link Image
Target 13 Chromosome Location 1
Target 13 Locus 1p34.1
Target 13 SNPs SNPJam Report Link Image
Target 13 General References
  1. Kaul SC, Sugihara T, Yoshida A, Nomura H, Wadhwa R: Gros1, a potential growth suppressor on chromosome 1: its identity to basement membrane-associated proteoglycan, leprecan. Oncogene. 2000 Jul 27;19(32):3576-83. [PubMed Link Image]
Target 13 Drug References
  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 Link Image]
  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 Link Image]
Drug Target 14 [top]
Target 14 ID 3946
Target 14 Name Hypothetical protein DKFZp686H15154
Target 14 Synonyms Not Available
Target 14 Gene Name DKFZp686H15154
Target 14 Protein Sequence >Hypothetical protein DKFZp686H15154
MATVGAPRHFCRCACFCTDNLYVARYGLHVRFRGEQQLRRDYGPILRSRGCVSAKDFQQL
LAELEQEVERRQRLGQESAARKALIASSYHPARPEVYDSLQDAALAPEFLAVTEYSVSPD
ADLKGLLQRLETVSEEKRIYRVPVFTAPFCQALLEELEHFEQSDMPKGRPNTMNNYGVLL
HELGLDEPLMTPLRERFLQPLMALLYPDCGGGRLDSHRAFVVKYAPGQDLELGCHYDNAE
LTLSVALGKVFTGGALYFGGLFQAPTALTEPLEVEHVVGQGVLHRGGQLHGARPLGTGER
WNLVVWLRASAVRNSLCPMCCREPDLVDDEGFGDGFTREEPATVDVCALT
Target 14 Number of Residues 355
Target 14 Molecular Weight 38970
Target 14 Theoretical pI 5.44
Target 14 GO Classification
Function
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Process
physiological process
metabolism
macromolecule metabolism
protein metabolism
Component
Not Available
Target 14 General Function Not Available
Target 14 Specific Function Not Available
Target 14 Pathways Not Available
Target 14 Reactions Not Available
Target 14 Pfam Domain Function
Target 14 Signals
  • None
Target 14 Transmembrane Regions
  • None
Target 14 Essentiality Non-Essential
Target 14 GenBank ID Protein 34364724 Link Image
Target 14 UniProtKB/Swiss-Prot ID Q6N063 Link Image
Target 14 UniProtKB/Swiss-Prot Entry Name Q6N063_HUMAN Link Image
Target 14 PDB ID Not Available
Target 14 Cellular Location Not Available
Target 14 Gene Sequence >1053 bp
ATGGCGACGGTGGGGGCTCCGCGGCACTTCTGCCGCTGCGCCTGCTTCTGCACCGATAAC
TTGTACGTGGCGCGCTATGGGCTGCACGTGCGCTTCCGAGGCGAGCAGCAGCTGCGCCGG
GACTACGGCCCGATCCTGCGCAGCCGAGGCTGTGTTAGCGCCAAGGACTTCCAGCAGCTG
TTAGCAGAGCTTGAGCAGGAGGTGGAGCGGCGGCAGCGGCTGGGGCAGGAGTCAGCAGCT
AGGAAAGCCCTCATCGCGAGTTCCTACCACCCGGCACGGCCTGAGGTCTACGACTCACTG
CAGGATGCAGCTCTGGCCCCCGAGTTCCTGGCCGTGACTGAGTACAGCGTGTCCCCAGAC
GCAGACCTCAAGGGCCTTCTCCAGCGGCTGGAGACAGTATCGGAGGAGAAGCGCATCTAC
CGGGTGCCTGTTTTCACAGCGCCCTTCTGCCAGGCCCTGCTGGAAGAGCTGGAGCACTTC
GAGCAATCGGACATGCCTAAGGGGAGGCCCAACACCATGAACAACTACGGGGTGCTGCTG
CACGAGCTCGGGCTGGACGAGCCGCTGATGACACCACTGCGGGAGCGCTTCCTGCAGCCG
CTGATGGCCCTGCTGTACCCTGACTGTGGCGGGGGCCGGCTCGACAGCCACCGGGCCTTT
GTGGTCAAATACGCACCGGGCCAGGACCTGGAGCTGGGCTGCCACTATGATAATGCCGAG
CTCACCCTCAGTGTGGCCTTGGGCAAGGTCTTCACAGGGGGCGCCCTGTATTTTGGGGGC
CTCTTCCAGGCACCCACAGCCCTGACGGAGCCCCTGGAGGTGGAGCACGTGGTGGGCCAG
GGTGTCCTCCACCGTGGCGGCCAGCTGCATGGAGCCCGGCCCTTGGGCACTGGTGAGCGT
TGGAACCTTGTCGTCTGGCTCCGAGCCTCTGCTGTGCGCAACAGCCTCTGTCCCATGTGC
TGCCGTGAGCCCGACCTGGTGGACGATGAGGGCTTCGGTGATGGCTTCACCCGAGAGGAG
CCCGCCACGGTGGATGTATGTGCGCTCACCTGA
Target 14 GenBank Gene ID
Target 14 GeneCard ID OGFOD2 Link Image
Target 14 GenAtlas ID OGFOD2 Link Image
Target 14 HGNC ID HGNC:25823 Link Image
Target 14 Chromosome Location Not Available
Target 14 Locus Not Available
Target 14 SNPs SNPJam Report Link Image
Target 14 General References Not Available
Target 14 Drug References
  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 Link Image]
  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 Link Image]
Drug Target 15 [top]
Target 15 ID 3948
Target 15 Name Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2
Target 15 Synonyms
  1. Alkylated DNA repair protein alkB homolog 2
  2. EC 1.14.11.-
  3. Oxy DC1
Target 15 Gene Name ALKBH2
Target 15 Protein Sequence >Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2
MDRFLVKGAQGGLLRKQEEQEPTGEEPAVLGGDKESTRKRPRREAPGNGGHSAGPSWRHI
RAEGLDCSYTVLFGKAEADEIFQELEKEVEYFTGALARVQVFGKWHSVPRKQATYGDAGL
TYTFSGLTLSPKPWIPVLERIRDHVSGVTGQTFNFVLINRYKDGCDHIGEHRDDERELAP
GSPIASVSFGACRDFVFRHKDSRGKSPSRRVAVVRLPLAHGSLLMMNHPTNTHWYHSLPV
RKKVLAPRVNLTFRKILLTKK
Target 15 Number of Residues 265
Target 15 Molecular Weight 29323
Target 15 Theoretical pI 10.22
Target 15 GO Classification Not Available
Target 15 General Function Replication, recombination and repair
Target 15 Specific Function Dioxygenase that repairs alkylated DNA and RNA containing 1-methyladenine and 3-methylcytosine by oxidative demethylation. Has strong preference for double-stranded DNA. Has low efficiency with single-stranded substrates. Requires molecular oxygen, alpha-ketoglutarate and iron
Target 15 Pathways Not Available
Target 15 Reactions Not Available
Target 15 Pfam Domain Function
Target 15 Signals
  • None
Target 15 Transmembrane Regions
  • None
Target 15 Essentiality Non-Essential
Target 15 GenBank ID Protein 53988530 Link Image
Target 15 UniProtKB/Swiss-Prot ID Q6NS38 Link Image
Target 15 UniProtKB/Swiss-Prot Entry Name ALKB2_HUMAN Link Image
Target 15 PDB ID Not Available
Target 15 Cellular Location
  • Nucleus
Target 15 Gene Sequence >786 bp
ATGGACAGATTCCTGGTGAAAGGGGCTCAAGGGGGCCTTTTGAGGAAGCAGGAGGAGCAA
GAGCCAACTGGAGAAGAGCCAGCTGTGTTGGGAGGAGACAAAGAAAGCACAAGGAAGAGG
CCCAGGGGAGAGGCCCCAGGGAATGGAGGCCACTCAGCAGGCCCTAGCTGGCGGCACATT
CGGGCTGAGGGCCTGGACTGCAGTTACACAGTCCTGTTTGGCAAAGCTGAGGCAGATGAG
ATTTTCCAAGAGTTGGAGAAAGAAGTAGAATATTTTACAGGAGCACTGGCCAGAGTCCAG
GTATTCGGGAAGTGGCACAGTGTGCCCAGGAAGCAAGCAACGTATGGCGACGCTGGGCTG
ACCTACACATTTTCAGGCCTCACGCTGTCTCCAAAGCCCTGGATCCCAGTTCTAGAGCGC
ATCCGGGATCACGTCTCTGGGGTGACTGGACAGACCTTCAACTTTGTGCTCATCAACAGG
TATAAAGATGGCTGTGACCACATCGGGGAGCACCGAGATGATGAAAGAGAACTGGCCCCT
GGGAGCCCCATTGCCTCTGTCTCCTTCGGTGCCTGCAGAGACTTTGTCTTCCGGCATAAG
GATTCCCGTGGGAAAAGCCCCTCCAGGAGGGTGGCGGTGGTCAGGCTGCCGCTGGCCCAC
GGGAGCTTACTAATGATGAACCACCCGACCAACACGCACTGGTACCACAGTCTTCCCGTG
AGAAAGAAGGTTCTGGCTCCACGGGTGAATCTGACTTTTCGTAAAATTTTGCTTACTAAA
AAATAA
Target 15 GenBank Gene ID
Target 15 GeneCard ID ALKBH2 Link Image
Target 15 GenAtlas ID ALKBH2 Link Image
Target 15 HGNC ID HGNC:32487 Link Image
Target 15 Chromosome Location 12
Target 15 Locus 12q24.11
Target 15 SNPs SNPJam Report Link Image
Target 15 General References Not Available
Target 15 Drug References
  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 Link Image]
  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 Link Image]
Drug Target 16 [top]
Target 16 ID 3949
Target 16 Name Prolyl 3-hydroxylase 2
Target 16 Synonyms
  1. EC 1.14.11.7
  2. Leprecan-like protein 1
  3. Myxoid liposarcoma-associated protein 4
  4. Prolyl 3-hydroxylase 2 precursor
Target 16 Gene Name LEPREL1
Target 16 Protein Sequence >Prolyl 3-hydroxylase 2
MRERIWAPPLLLLLPLLLPPPLWGGPPDSPRRELELEPGPLQPFDLLYASGAAAYYSGDY
ERAVRDLEAALRSHRRLREIRTRCARHCAARHPLPPPPPGEGPGAELPLFRSLLGRARCY
RSCETQRLGGPASRHRVSEDVRSDFQRRVPYNYLQRAYIKLNQLEKAVEAAHTFFVANPE
HMEMQQNIENYRATAGVEALQLVDREAKPHMESYNAGVKHYEADDFEMAIRHFEQALREY
FVEDTECRTLCEGPQRFEEYEYLGYKAGLYEAIADHYMQVLVCQHECVRELATRPGRLSP
IENFLPLHYDYLQFAYYRVGEYVKALECAKAYLLCHPDDEDVLDNVDYYESLLDDSIDPA
SIEAREDLTMFVKRHKLESELIKSAAEGLGFSYTEPNYWIRYGGRQDENRVPSGVNVEGA
EVHGFSMGKKLSPKIDRDLREGGPLLYENITFVYNSEQLNGTQRVLLDNVLSEEQCRELH
SVASGIMLVGDGYRGKTSPHTPNEKFEGATVLKALKSGYEGRVPLKSARLFYDISEKARR
IVESYFMLNSTLYFSYTHMVCRTALSGQQDRRNDLSHPIHADNCLLDPEANECWKEPPAY
TFRDYSALLYMNDDFEGGEFIFTEMDAKTVTASIKPKCGRMISFSSGGENPHGVKAVTKG
KRCAVALWFTLDPLYRELERIQADEVIAILDQEQQGKHELNINPKDEL
Target 16 Number of Residues 719
Target 16 Molecular Weight 80985
Target 16 Theoretical pI 5.47
Target 16 GO Classification
Function
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Process
physiological process
metabolism
macromolecule metabolism
protein metabolism
Component
Not Available
Target 16 General Function Not Available
Target 16 Specific Function Has prolyl 3-hydroxylase activity catalyzing the posttranslational formation of 3-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens, especially types IV and V
Target 16 Pathways Not Available
Target 16 Reactions
  • procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-3-hydroxy-L-proline + succinate + CO2
Target 16 Pfam Domain Function
Target 16 Signals
  • 1-24
Target 16 Transmembrane Regions
  • None
Target 16 Essentiality Non-Essential
Target 16 GenBank ID Protein 27526730 Link Image
Target 16 UniProtKB/Swiss-Prot ID Q8IVL5 Link Image
Target 16 UniProtKB/Swiss-Prot Entry Name P3H2_HUMAN Link Image
Target 16 PDB ID Not Available
Target 16 Cellular Location
  • Endoplasmic reticulum
Target 16 Gene Sequence >2127 bp
ATGCGGGAGCGCATCTGGGCGCCGCCGCTGCTGCTGCTGCTGCCGCTGCTACTGCCGCCG
CCACTGTGGGGCGGCCCCCCGGACAGCCCACGCCGGGAGCTGGAGCTGGAGCCCGGGCCT
CTGCAGCCCTTCGACCTGCTCTACGCCAGCGGCGCGGCCGCCTACTACAGCGGAGACTAC
GAGCGAGCGGTGCGCGACTTGGAAGCGGCGCTGCGCAGCCACCGGCGCCTGCGGGAAATC
CGCACGCGCTGTGCCCGCCACTGCGCGGCGCGCCACCCGCTCCCGCCCCCGCCCCCCGGC
GAGGGCCCCGGCGCTGAGCTGCCCCTTTTCCGCTCCTTGTTGGGGCGGGCGCGCTGTTAT
CGCAGCTGTGAGACCCAGCGCCTCGGGGGCCCCGCATCCCGCCACCGCGTCAGCGAGGAT
GTGCGCAGCGACTTCCAGCGCAGAGTGCCCTACAACTACCTGCAGCGGGCCTACATCAAG
CTTAACCAGCTCGAAAAAGCAGTGGAAGCAGCTCACACATTTTTCGTGGCTAACCCTGAG
CACATGGAAATGCAGCAGAACATTGAGAATTACAGGGCGACAGCTGGTGTTGAAGCATTG
CAGTTGGTAGACAGAGAAGCCAAGCCACACATGGAGAGTTACAATGCAGGAGTTAAACAT
TATGAGGCTGATGACTTTGAGATGGCTATCAGGCATTTCGAACAAGCCTTAAGAGAATAT
TTCGTTGAAGATACAGAATGCCGGACCCTATGTGAGGGGCCTCAGAGATTTGAAGAATAT
GAGTATTTAGGGTATAAGGCTGGTCTGTATGAAGCTATTGCAGATCACTACATGCAGGTG
CTTGTTTGTCAGCATGAATGTGTGAGGGAACTTGCCACCCGCCCTGGCCGCCTCTCTCCC
ATCGAGAATTTTCTTCCTCTGCACTATGATTACCTACAGTTTGCCTACTATCGAGTTGGT
GAGTATGTGAAAGCCCTGGAGTGTGCCAAAGCCTATCTTCTATGCCATCCAGATGATGAG
GATGTCCTAGACAATGTGGATTACTATGAGAGTCTGCTGGATGATAGCATTGACCCGGCA
TCCATTGAGGCCAGAGAGGATTTAACAATGTTTGTGAAACGTCATAAGCTGGAGTCTGAG
CTGATAAAATCAGCTGCAGAAGGTCTGGGGTTTTCATACACTGAACCGAATTATTGGATC
AGATATGGAGGACGACAGGATGAGAATCGGGTCCCTTCAGGAGTGAACGTAGAGGGAGCA
GAAGTTCATGGATTCTCAATGGGAAAAAAGCTATCACCCAAGATAGATCGAGACCTAAGA
GAAGGTGGTCCTCTACTCTATGAGAACATCACATTCGTCTACAACTCGGAGCAGCTGAAC
GGGACTCAGCGGGTTCTCCTGGATAACGTCCTGTCGGAAGAACAGTGCCGGGAGCTCCAC
AGCGTGGCCAGTGGAATCATGCTTGTTGGTGATGGATACAGAGGAAAAACTTCACCCCAT
ACACCCAATGAAAAGTTTGAAGGTGCAACTGTCCTGAAAGCACTCAAATCTGGTTATGAA
GGTCGAGTCCCACTGAAGAGCGCTCGTCTGTTTTATGACATCAGCGAAAAGGCTCGAAGG
ATTGTAGAATCTTATTTTATGCTGAACTCAACTCTGTATTTTTCCTATACACACATGGTC
TGCCGAACAGCCCTGTCTGGTCAGCAGGATAGAAGAAATGACCTCAGTCATCCCATCCAT
GCTGACAACTGTTTGTTGGATCCAGAGGCCAACGAATGCTGGAAGGAGCCTCCTGCTTAC
ACATTTCGAGACTATAGTGCTCTCCTATATATGAATGATGACTTTGAAGGAGGAGAATTC
ATATTCACAGAGATGGATGCTAAGACTGTGACTGCCTCTATAAAACCAAAATGTGGGCGC
ATGATCAGCTTCTCATCTGGAGGAGAGAACCCTCATGGGGTGAAGGCAGTCACCAAGGGA
AAGAGGTGTGCTGTGGCTCTGTGGTTCACCTTGGACCCACTTTATAGAGAATTGGAGCGA
ATACAGGCTGATGAAGTGATTGCAATTCTGGATCAAGAACAGCAAGGGAAGCATGAACTG
AATATCAACCCTAAAGATGAGCTATAA
Target 16 GenBank Gene ID
Target 16 GeneCard ID LEPREL1 Link Image
Target 16 GenAtlas ID LEPREL1 Link Image
Target 16 HGNC ID HGNC:19317 Link Image
Target 16 Chromosome Location 3
Target 16 Locus 3q28
Target 16 SNPs SNPJam Report Link Image
Target 16 General References Not Available
Target 16 Drug References
  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 Link Image]
  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 Link Image]
Drug Target 17 [top]
Target 17 ID 3951
Target 17 Name Prolyl 3-hydroxylase 3
Target 17 Synonyms
  1. EC 1.14.11.7
  2. Leprecan-like protein 2
  3. Prolyl 3-hydroxylase 3 precursor
  4. Protein B
Target 17 Gene Name LEPREL2
Target 17 Protein Sequence >Prolyl 3-hydroxylase 3
MLRLLRPLLLLLLLPPPGSPEPPGLTQLSPGAPPQAPDLLYADGLRAYAAGAWAPAVALL
REALRSQAALGRVRLDCGASCAADPGAALPAVLLGAPEPDSGPGPTQGSWERQLLRAALR
RADCLTQCAARRLGPGGAARLRVGSALRDAFRRREPYNYLQRAYYQLKKLDLAAAAAHTF
FVANPMHLQMREDMAKYRRMSGVRPQSFRDLETPPHWAAYDTGLELLGRQEAGLALPRLE
EALQGSLAQMESCRADCEGPEEQQGAEEEEDGAASQGGLYEAIAGHWIQVLQCRQRCVGE
TATRPGRSFPVPDFLPNQLRRLHEAHAQVGNLSQAIENVLSVLLFYPEDEAAKRALNQYQ
AQLGEPRPGLGPREDIQRFILRSLGEKRQLYYAMEHLGTSFKDPDPWTPAALIPEALREK
LREDQEKRPWDHEPVKPKPLTYWKDVLLLEGVTLTQDSRQLNGSERAVLDGLLTPAECGV
LLQLAKDAAGAGARSGYRGRRSPHTPHERFEGLTVLKAAQLARAGTVGSQGAKLLLEVSE
RVRTLTQAYFSPERPLHLSFTHLVCRSAIEGEQEQRMDLSHPVHADNCVLDPDTGECWRE
PPAYTYRDYSGLLYLNDDFQGGDLFFTEPNALTVTARVRPRCGRLVAFSSGVENPHGVWA
VTRGRRCALALWHTWAPEHREQEWIEAKELLQESQEEEEEEEEEMPSKDPSPEPPSRRHQ
RVQDKTGRAPRVREEL
Target 17 Number of Residues 748
Target 17 Molecular Weight 81837
Target 17 Theoretical pI 6.26
Target 17 GO Classification
Function
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Process
physiological process
metabolism
macromolecule metabolism
protein metabolism
Component
Not Available
Target 17 General Function Not Available
Target 17 Specific Function Has prolyl 3-hydroxylase activity catalyzing the posttranslational formation of 3-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens, especially types IV and V
Target 17 Pathways Not Available
Target 17 Reactions
  • procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-3-hydroxy-L-proline + succinate + CO2
Target 17 Pfam Domain Function
Target 17 Signals
  • 1-20
Target 17 Transmembrane Regions
  • None
Target 17 Essentiality Non-Essential
Target 17 GenBank ID Protein 1200503 Link Image
Target 17 UniProtKB/Swiss-Prot ID Q8IVL6 Link Image
Target 17 UniProtKB/Swiss-Prot Entry Name P3H3_HUMAN Link Image
Target 17 PDB ID Not Available
Target 17 Cellular Location
  • Endoplasmic reticulum
Target 17 Gene Sequence >2211 bp
ATGCTCCGGCTCCTCCGGCCGCTGCTGCTACTGCTGCTGCTGCCTCCCCCGGGGTCCCCT
GAGCCCCCCGGCCTGACCCAGCTGTCCCCGGGGGCGCCCCCGCAGGCCCCCGACTTGCTC
TACGCTGACGGGCTGCGCGCCTACGCGGCCGGGGCTTGGGCGCCGGCCGTGGCGCTGCTG
CGGGAGGCGCTGCGGAGCCAGGCGGCGCTGGGCCGGGTGCGGCTGGATTGCGGGGCGAGC
TGCGCGGCCGATCCGGGCGCCGCGCTCCCCGCCGTGCTTCTCGGGGCCCCGGAGCCCGAC
TCCGGGCCGGGACCCACGCAGGGGTCCTGGGAGCGACAGCTTCTCCGTGCAGCGCTCCGC
CGCGCAGACTGCCTGACCCAGTGCGCAGCACGGAGGCTGGGCCCCGGGGGCGCGGCGCGG
CTTCGCGTGGGGAGCGCGCTCCGGGACGCCTTCCGCCGTCGGGAGCCCTACAACTACCTG
CAGAGGGCCTATTACCAGTTGAAGAAGCTGGATCTGGCAGCTGCGGCAGCACACACCTTC
TTTGTAGCAAACCCCATGCACCTGCAGATGCGGGAGGACATGGCTAAGTACAGACGAATG
TCGGGAGTTCGGCCCCAGAGCTTCCGGGACCTGGAGACGCCCCCACACTGGGCAGCCTAT
GACACTGGCCTGGAGCTACTGGGGCGCCAGGAGGCAGGACTGGCACTGCCCAGGCTAGAG
GAGGCTCTTCAGGGGAGCCTGGCCCAGATGGAGAGCTGCCGTGCTGACTGTGAGGGGCCT
GAGGAGCAGCAGGGGGCTGAAGAAGAGGAGGATGGGGCTGCGAGCCAGGGGGGCCTCTAT
GAGGCCATTGCAGGACACTGGATTCAGGTCCTGCAGTGCCGGCAACGCTGTGTGGGGGAA
ACAGCCACACGCCCTGGTCGCAGCTTCCCTGTCCCAGACTTCCTTCCCAACCAGCTGAGG
CGGCTACATGAGGCCCATGCTCAGGTGGGCAATCTGTCCCAGGCTATAGAAAATGTCCTG
AGTGTCCTGCTCTTCTACCCGGAGGATGAGGCTGCCAAGAGGGCTCTGAACCAGTACCAG
GCCCAGCTGGGAGAGCCGAGACCTGGCCTCGGACCCAGAGAGGACATCCAGCGCTTCATC
CTCCGATCCCTGGGGGAGAAGAGGCAGCTCTACTATGCCATGGAGCACCTGGGGACCAGC
TTCAAGGATCCTGACCCCTGGACCCCTGCAGCTCTCATCCCTGAGGCACTTAGAGAAAAG
CTCAGAGAGGATCAAGAGAAGAGGCCTTGGGACCATGAGCCCGTGAAGCCAAAGCCCTTG
ACCTACTGGAAGGATGTCCTTCTCCTGGAGGGTGTGACCTTGACCCAGGATTCCAGGCAG
CTGAATGGGTCGGAGCGGGCGGTGTTGGATGGGCTGCTCACCCCAGCCGAGTGTGGGGTG
CTGCTGCAGCTGGCTAAGGATGCAGCTGGGGCTGGAGCCAGGTCTGGCTATCGTGGTCGC
CGCTCCCCTCACACCCCCCATGAACGCTTCGAGGGGCTCACGGTGCTTAAGGCTGCGCAG
CTGGCCCGGGCTGGGACAGTGGGCAGTCAGGGTGCTAAGCTGCTTCTGGAGGTGAGCGAG
CGGGTGCGGACCTTGACCCAGGCCTACTTCTCCCCGGAACGGCCCCTGCATCTGTCCTTC
ACCCACCTGGTGTGCCGCAGCGCCATAGAAGGAGAGCAAGAGCAGCGCATGGACCTGAGT
CACCCAGTGCACGCAGACAACTGCGTCCTGGACCCTGACACGGGAGAGTGCTGGCGGGAG
CCCCCAGCCTACACCTATCGGGACTACAGCGGACTCCTCTACCTCAACGATGACTTCCAG
GGTGGGGACCTGTTCTTCACGGAGCCCAACGCCCTCACTGTCACGGCTCGGGTGCGTCCT
CGCTGTGGGCGCCTTGTGGCCTTCAGCTCCGGTGTCGAGAATCCCCATGGGGTGTGGGCC
GTGACTCGGGGACGGCGCTGTGCCCTGGCACTGTGGCACACGTGGGCACCTGAGCACAGG
GAGCAGGAGTGGATAGAAGCCAAAGAACTGCTGCAGGAGTCACAGGAGGAGGAGGAAGAG
GAAGAGGAAGAAATGCCCAGCAAAGACCCTTCCCCAGAGCCCCCTAGCCGCAGGCACCAG
AGGGTCCAAGACAAGACTGGAAGGGCACCTCGGGTTCGGGAGGAGCTGTGA
Target 17 GenBank Gene ID
Target 17 GeneCard ID LEPREL2 Link Image
Target 17 GenAtlas ID LEPREL2 Link Image
Target 17 HGNC ID HGNC:19318 Link Image
Target 17 Chromosome Location 12
Target 17 Locus 12q13
Target 17 SNPs SNPJam Report Link Image
Target 17 General References
  1. Ansari-Lari MA, Muzny DM, Lu J, Lu F, Lilley CE, Spanos S, Malley T, Gibbs RA: A gene-rich cluster between the CD4 and triosephosphate isomerase genes at human chromosome 12p13. Genome Res. 1996 Apr;6(4):314-26. [PubMed Link Image]
  2. Ansari-Lari MA, Shen Y, Muzny DM, Lee W, Gibbs RA: Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination. Genome Res. 1997 Mar;7(3):268-80. [PubMed Link Image]
Target 17 Drug References
  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 Link Image]
  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 Link Image]
Drug Target 18 [top]
Target 18 ID 3953
Target 18 Name 2-oxoglutarate and iron-dependent oxygenase domain containing 1
Target 18 Synonyms Not Available
Target 18 Gene Name OGFOD1
Target 18 Protein Sequence >2-oxoglutarate and iron-dependent oxygenase domain containing 1
MNGKRPAEPGPARVGKKGKKEVMAEFSDAVTEETLKKQVAEAWSRRTPFSHEVIVMDMDP
FLHCVIPNFIQSQDFLEGLQKELMNLDFHEKYNDLYKFQQSDDLKKRREPHISTLRKILF
EDFRSWLSDISKIDLESTIDMSCAKYEFTDALLCHDDELEGRRIAFILYLVPPWDRSMGG
TLDLYSIDEHFQPKQIVKSLIPSWNKLVFFEVSPVSFHQVSEVLSEEKSRLSISGWFHGP
SLTRPPNYFEPPIPRSPHIPQDHEILYDWINPTYLDMDYQVQIQEEFEESSEILLKEFLK
PEKFTKVCEALEHGHVEWSSRGPPNKRFYEKAEESKLPEILKECMKLFRSEALFLLLSNF
TGLKLHFLAPSEEDEMNDKKEAETTDITEEGTSHSPPEPENNQMAISNNSQQSNEQTDPE
PEENETKKESSVPMCQGELRHWKTGHYTLIHDHSKAEFALDLILYCGCEGWEPEYGGFTS
YIAKGEDEELLTVNPESNSLALVYRDRETLKFVKHINHRSLEQKKTFPNRTGFWDFSFIY
YE
Target 18 Number of Residues 551
Target 18 Molecular Weight 63247
Target 18 Theoretical pI 4.77
Target 18 GO Classification
Function
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Process
physiological process
metabolism
macromolecule metabolism
protein metabolism
Component
Not Available
Target 18 General Function Not Available
Target 18 Specific Function Not Available
Target 18 Pathways Not Available
Target 18 Reactions Not Available
Target 18 Pfam Domain Function
Target 18 Signals
  • None
Target 18 Transmembrane Regions
  • None
Target 18 Essentiality Non-Essential
Target 18 GenBank ID Protein 21410525 Link Image
Target 18 UniProtKB/Swiss-Prot ID Q8N543 Link Image
Target 18 UniProtKB/Swiss-Prot Entry Name Q8N543_HUMAN Link Image
Target 18 PDB ID Not Available
Target 18 Cellular Location Not Available
Target 18 Gene Sequence >1629 bp
ATGAATGGGAAGCGGCCAGCGGAGCCCGGCCCAGCCCGGGTGGGAAAAAAGGGAAAGAAG
GAGGTGATGGCGGAGTTTTCGGACGCTGTTACGGAAGAAACCTTGAAAAAGCAGGTGGCT
GAGGCCTGGAGCCGCAGGACGCCGTTCAGTCACGAAGTCATTGTCATGGACATGGACCCT
TTTCTTCACTGTGTGATCCCAAACTTCATCCAAAGCCAAGACTTCTTAGAAGGGCTTCAG
AAGGAACTGATGAACTTGGACTTCCATGAGAAGTATAATGATTTATATAAGTTCCAGCAG
TCTGATGATTTGAAGAAGAGAAGAGAGCCTCACATCTCCACTTTAAGGAAAATTCTGTTT
GAAGATTTCCGGTCCTGGCTTTCTGATATTTCTAAAATTGACCTGGAATCAACCATTGAC
ATGTCCTGTGCTAAATATGAATTCACTGATGCCCTGCTGTGCCATGATGATGAGCTGGAA
GGGCGCCGGATTGCCTTCATCCTGTACCTGGTTCCTCCCTGGGACAGGAGCATGGGTGGT
ACCCTGGACCTGTACAGCATTGATGAACACTTTCAGCCGAAGCAGATTGTCAAGTCTCTT
ATCCCTTCGTGGAACAAACTGGTTTTCTTTGAAGTATCTCCTGTGTCCTTTCACCAGGTG
TCTGAAGTGCTGTCTGAAGAAAAGTCACGTTTGTCTATAAGTGGCTGGTTTCATGGTCCA
TCATTGACTCGGCCTCCCAACTACTTTGAACCCCCCATACCTCGGAGCCCTCACATCCCA
CAAGATCATGAGATTTTGTATGATTGGATCAACCCTACTTATCTGGACATGGATTACCAA
GTTCAAATTCAAGAAGAGTTTGAAGAAAGTTCTGAAATTCTCCTGAAGGAGTTTCTTAAG
CCTGAGAAATTCACGAAAGTCTGTGAGGCCTTGGAGCATGGACATGTGGAATGGAGCAGC
CGAGGTCCCCCTAACAAAAGGTTTTATGAGAAAGCTGAGGAGAGTAAGCTTCCTGAGATA
TTGAAGGAGTGCATGAAGTTATTTCGCTCTGAGGCACTATTCTTGCTGCTCTCCAACTTC
ACAGGCCTGAAGCTTCATTTCTTGGCCCCTTCGGAAGAAGATGAGATGAATGATAAAAAA
GAGGCAGAAACCACTGATATCACTGAAGAAGGGACTAGCCATAGTCCTCCTGAGCCAGAG
AATAATCAGATGGCCATCAGCAACAACAGCCAACAGAGCAATGAGCAGACAGACCCAGAG
CCAGAGGAAAATGAAACAAAGAAAGAATCAAGTGTTCCCATGTGCCAAGGGGAACTGAGG
CATTGGAAGACCGGTCACTACACTTTAATTCATGACCATAGCAAGGCTGAATTTGCCCTA
GACTTAATTCTGTACTGTGGCTGTGAAGGCTGGGAGCCAGAATATGGCGGTTTTACTTCT
TACATTGCCAAAGGTGAAGATGAAGAGCTGCTAACAGTGAATCCAGAAAGCAATTCTTTG
GCATTGGTCTACAGAGACAGAGAGACTCTGAAATTTGTCAAGCATATTAACCACCGAAGC
CTGGAACAAAAGAAAACCTTCCCAAACAGAACAGGTTTCTGGGACTTTTCATTCATCTAT
TATGAATGA
Target 18 GenBank Gene ID
Target 18 GeneCard ID OGFOD1 Link Image
Target 18 GenAtlas ID OGFOD1 Link Image
Target 18 HGNC ID HGNC:25585 Link Image
Target 18 Chromosome Location 16
Target 18 Locus 16q13
Target 18 SNPs SNPJam Report Link Image
Target 18 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Target 18 Drug References
  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 Link Image]
  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 Link Image]
Drug Target 19 [top]
Target 19 ID 3954
Target 19 Name Egl nine homolog 2
Target 19 Synonyms
  1. EC 1.14.11.-
  2. Estrogen-induced tag 6
  3. HIF-PH1
  4. HIF-prolyl hydroxylase 1
  5. HPH-3
  6. Hypoxia-inducible factor prolyl hydroxylase 1
  7. PHD1
  8. Prolyl hydroxylase domain-containing protein 1
Target 19 Gene Name EGLN2
Target 19 Protein Sequence >Egl nine homolog 2
MDSPCQPQPLSQALPQLPGSSSEPLEPEPGRARMGVESYLPCPLLPSYHCPGVPSEASAG
SGTPRATATSTTASPLRDGFGGQDGGELRPLQSEGAAALVTKGCQRLAAQGARPEAPKRK
WAEDGGDAPSPSKRPWARQENQEAEREGGMSCSCSSGSGEASAGLMEEALPSAPERLALD
YIVPCMRYYGICVKDSFLGAALGGRVLAEVEALKRGGRLRDGQLVSQRAIPPRSIRGDQI
AWVEGHEPGCRSIGALMAHVDAVIRHCAGRLGSYVINGRTKAMVACYPGNGLGYVRHVDN
PHGDGRCITCIYYLNQNWDVKVHGGLLQIFPEGRPVVANIEPLFDRLLIFWSDRRNPHEV
KPAYATRYAITVWYFDAKERAAAKDKYQLASGQKGVQVPVSQPPTPT
Target 19 Number of Residues 413
Target 19 Molecular Weight 43651
Target 19 Theoretical pI 7.97
Target 19 GO Classification
Function
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Process
physiological process
metabolism
macromolecule metabolism
protein metabolism
Component
Not Available
Target 19 General Function Posttranslational modification, protein turnover, chaperones
Target 19 Specific Function Catalyzes the posttranslational formation of 4- hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates HIF-1 alpha at 'Pro-402' and 'Pro-564', and HIF-2 alpha. Functions as a cellular oxygen sensor and, under normoxic conditions, targets HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. May play a role in cell growth regulation
Target 19 Pathways Not Available
Target 19 Reactions Not Available
Target 19 Pfam Domain Function
Target 19 Signals
  • None
Target 19 Transmembrane Regions
  • None
Target 19 Essentiality Non-Essential
Target 19 GenBank ID Protein 14547148 Link Image
Target 19 UniProtKB/Swiss-Prot ID Q96KS0 Link Image
Target 19 UniProtKB/Swiss-Prot Entry Name EGLN2_HUMAN Link Image
Target 19 PDB ID Not Available
Target 19 Cellular Location
  • Cytoplasm
Target 19 Gene Sequence >1224 bp
ATGGACAGCCCGTGCCAGCCGCAGCCCCTAAGTCAGGCTCTCCCTCAGTTACCAGGGTCT
TCGTCAGAGCCCTTGGAGCCTGAGCCTGGCCGGGCCAGGATGGGAGTGGAGAGTTACCTG
CCCTGTCCCCTGCTCCCCTCCTACCACTGTCCAGGAGTGCCTAGTGAGGCCTCGGCAGGG
AGTGGGACCCCCAGAGCCACAGCCACCTCTACCACTGCCAGCCCTCTTCGGGACGGTTTT
GGCGGGCAGGATGGTGGTGAGCTGCGGCCGCTGCAGAGTGAAGGCGCTGCAGCGCTGGTC
ACCAAGGGGTGCCAGCGATTGGCAGCCCAGGGCGCACGGCCTGAGGCCCCCAAACGGAAA
TGGGCCGAGGATGGTGGGGATGCCCCTTCACCCAGCAAACGGCCCTGGGCCAGGCAAGAG
AACCAGGAGGCAGAGCGGGAGGGTGGCATGAGCTGCAGCTGCAGCAGTGGCAGTGGTGAG
GCCAGTGCTGGGCTGATGGAGGAGGCGCTGCCCTCTGCGCCCGAGCGCCTGGCCCTGGAC
TATATCGTGCCCTGCATGCGGTACTACGGCATCTGCGTCAAGGACAGCTTCCTGGGGGCA
GCACTGGGCGGTCGCGTGCTGGCCGAGGTGGAGGCCCTCAAACGGGGTGGGCGCCTGCGA
GACGGGCAGCTAGTGAGCCAGAGGGCGATCCCGCCGCGCAGCATCCGTGGGGACCAGATT
GCCTGGGTGGAAGGCCATGAACCAGGCTGTCGAAGCATTGGTGCCCTCATGGCCCATGTG
GACGCCGTCATCCGCCACTGCGCAGGGCGGCTGGGCAGCTATGTCATCAACGGGCGCACC
AAGGCCATGGTGGCGTGTTACCCAGGCAACGGGCTCGGGTACGTAAGGCACGTTGACAAT
CCCCACGGCGATGGGCGCTGCATCACCTGTATCTATTACCTGAATCAGAACTGGGACGTT
AAGGTGCATGGCGGCCTGCTGCAGATCTTCCCTGAGGGCCGGCCCGTGGTAGCCAACATC
GAGCCACTCTTTGACCGGTTGCTCATTTTCTGGTCTGACCGGCGGAACCCCCACGAGGTG
AAGCCAGCCTATGCCACCAGGTACGCCATCACTGTCTGGTATTTTGATGCCAAGGAGCGG
GCAGCAGCCAAAGACAAGTATCAGCTAGCATCAGGACAGAAAGGTGTCCAAGTACCTGTA
TCACAGCCGCCTACGCCCACCTAG
Target 19 GenBank Gene ID
Target 19 GeneCard ID EGLN2 Link Image
Target 19 GenAtlas ID EGLN2 Link Image
Target 19 HGNC ID HGNC:14660 Link Image
Target 19 Chromosome Location 19
Target 19 Locus 19q13.2
Target 19 SNPs SNPJam Report Link Image
Target 19 General References
  1. Taylor MS: Characterization and comparative analysis of the EGLN gene family. Gene. 2001 Sep 5;275(1):125-32. [PubMed Link Image]
  2. Semenza GL: HIF-1, O(2), and the 3 PHDs: how animal cells signal hypoxia to the nucleus. Cell. 2001 Oct 5;107(1):1-3. [PubMed Link Image]
  3. Epstein AC, Gleadle JM, McNeill LA, Hewitson KS, O'Rourke J, Mole DR, Mukherji M, Metzen E, Wilson MI, Dhanda A, Tian YM, Masson N, Hamilton DL, Jaakkola P, Barstead R, Hodgkin J, Maxwell PH, Pugh CW, Schofield CJ, Ratcliffe PJ: C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell. 2001 Oct 5;107(1):43-54. [PubMed Link Image]
  4. Seth P, Krop I, Porter D, Polyak K: Novel estrogen and tamoxifen induced genes identified by SAGE (Serial Analysis of Gene Expression). Oncogene. 2002 Jan 24;21(5):836-43. [PubMed Link Image]
  5. McNeill LA, Hewitson KS, Gleadle JM, Horsfall LE, Oldham NJ, Maxwell PH, Pugh CW, Ratcliffe PJ, Schofield CJ: The use of dioxygen by HIF prolyl hydroxylase (PHD1). Bioorg Med Chem Lett. 2002 Jun 17;12(12):1547-50. [PubMed Link Image]
  6. Oehme F, Ellinghaus P, Kolkhof P, Smith TJ, Ramakrishnan S, Hutter J, Schramm M, Flamme I: Overexpression of PH-4, a novel putative proline 4-hydroxylase, modulates activity of hypoxia-inducible transcription factors. Biochem Biophys Res Commun. 2002 Aug 16;296(2):343-9. [PubMed Link Image]
Target 19 Drug References
  1. Nytko KJ, Spielmann P, Camenisch G, Wenger RH, Stiehl DP: Regulated function of the prolyl-4-hydroxylase domain (PHD) oxygen sensor proteins. Antioxid Redox Signal. 2007 Sep;9(9):1329-38. [PubMed Link Image]
  2. Bruegge K, Jelkmann W, Metzen E: Hydroxylation of hypoxia-inducible transcription factors and chemical compounds targeting the HIF-alpha hydroxylases. Curr Med Chem. 2007;14(17):1853-62. [PubMed Link Image]
Drug Target 20 [top]
Target 20 ID 3956
Target 20 Name Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3
Target 20 Synonyms
  1. Alkylated DNA repair protein alkB homolog 3
  2. DEPC-1
  3. EC 1.14.11.-
  4. Prostate cancer antigen 1
Target 20 Gene Name ALKBH3
Target 20 Protein Sequence >Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3
MEEKRRRARVQGAWAAPVKSQAIAQPATTAKSHLHQKPGQTWKNKEHHLSDREFVFKEPQ
QVVRRAPEPRVIDREGVYEISLSPTGVSRVCLYPGFVDVKEADWILEQLCQDVPWKQRTG
IREDITYQQPRLTAWYGELPYTYSRITMEPNPHWHPVLRTLKNRIEENTGHTFNSLLCNL
YRNEKDSVDWHSDDEPSLGRCPIIASLSFGATRTFEMRKKPPPEENGDYTYVERVKIPLD
HGTLLIMEGATQADWQHRVPKEYHSREPRVNLTFRTVYPDPRGAPW
Target 20 Number of Residues 290
Target 20 Molecular Weight 33375
Target 20 Theoretical pI 8.58
Target 20 GO Classification Not Available
Target 20 General Function Replication, recombination and repair
Target 20 Specific Function Dioxygenase that repairs alkylated DNA containing 1- methyladenine and 3-methylcytosine by oxidative demethylation. Has a strong preference for single-stranded DNA. May also act on RNA. Requires molecular oxygen, alpha-ketoglutarate and iron
Target 20 Pathways Not Available
Target 20 Reactions Not Available
Target 20 Pfam Domain Function Not Available
Target 20 Signals
  • None
Target 20 Transmembrane Regions
  • None
Target 20 Essentiality Non-Essential
Target 20 GenBank ID Protein 16326129 Link Image
Target 20 UniProtKB/Swiss-Prot ID Q96Q83 Link Image
Target 20 UniProtKB/Swiss-Prot Entry Name ALKB3_HUMAN Link Image
Target 20 PDB ID Not Available
Target 20 Cellular Location
  • Cytoplasm
Target 20 Gene Sequence >861 bp
ATGGAGGAAAAAAGACGGCGAGCCCGAGTTCAGGGAGCCTGGGCTGCCCCTGTTAAAAGC
CAGGCCATTGCTCAGCCAGCTACCACTGCTAAGAGCCATCTCCACCAGAAGCCTGGCCAG
ACCTGGAAGAACAAAGAGCATCATCTCTCTGACAGAGAGTTTGTGTTCAAAGAACCTCAG
CAGGTAGTACGTAGAGCTCCTGAGCCACGAGTGATTGACAGAGAGGGTGTGTATGAAATC
AGCCTGTCACCCACAGGTGTATCTAGGGTCTGTTTGTATCCTGGCTTTGTTGACGTGAAA
GAAGCTGACTGGATATTGGAACAGCTTTGTCAAGATGTTCCCTGGAAACAGAGGACCGGC
ATCAGAGAGGATATAACTTATCAGCAACCAAGACTTACAGCATGGTATGGAGAACTTCCT
TACACTTATTCAAGAATCACTATGGAACCAAATCCTCACTGGCACCCTGTGCTGCGCACA
CTAAAGAACCGCATTGAAGAGAACACTGGCCACACCTTCAACTCCTTACTCTGCAATCTT
TATCGCAATGAGAAGGACAGCGTGGACTGGCACAGTGATGATGAACCCTCACTAGGGAGG
TGCCCCATTATTGCTTCACTAAGTTTTGGTGCCACACGCACATTTGAGATGAGAAAGAAG
CCACCACCAGAAGAGAATGGAGACTACACATATGTGGAAAGAGTGAAGATACCCTTGGAT
CATGGGACCTTGTTAATCATGGAAGGAGCGACACAAGCTGACTGGCAGCATCGAGTGCCC
AAAGAATACCACTCTAGAGAACCGAGAGTGAACCTGACCTTTCGGACAGTCTATCCAGAC
CCTCGAGGGGCACCCTGGTGA
Target 20 GenBank Gene ID
Target 20 GeneCard ID ALKBH3 Link Image
Target 20 GenAtlas ID ALKBH3 Link Image
Target 20 HGNC ID HGNC:30141 Link Image
Target 20 Chromosome Location 11
Target 20 Locus 11p11.2
Target 20 SNPs SNPJam Report Link Image
Target 20 General References Not Available
Target 20 Drug References
  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 Link Image]
  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 Link Image]
Drug Target 21 [top]
Target 21 ID 3958
Target 21 Name Jumonji/ARID domain-containing protein 1D
Target 21 Synonyms
  1. H-Y
  2. Histocompatibility Y antigen
  3. Protein SmcY
Target 21 Gene Name JARID1D
Target 21 Protein Sequence >Jumonji/ARID domain-containing protein 1D
MEPGCDEFLPPPECPVFEPSWAEFQDPLGYIAKIRPIAEKSGICKIRPPADWQPPFAVEV
DNFRFTPRVQRLNELEAQTRVKLNYLDQIAKFWEIQGSSLKIPNVERKILDLYSLSKIVI
EEGGYEAICKDRRWARVAQRLHYPPGKNIGSLLRSHYERIIYPYEMFQSGANHVQCNTHP
FDNEVKDKEYKPHSIPLRQSVQPSKFSSYSRRAKRLQPDPEPTEEDIEKHPELKKLQIYG
PGPKMMGLGLMAKDKDKTVHKKVTCPPTVTVKDEQSGGGNVSSTLLKQHLSLEPCTKTTM
QLRKNHSSAQFIDSYICQVCSRGDEDDKLLFCDGCDDNYHIFCLLPPLPEIPRGIWRCPK
CILAECKQPPEAFGFEQATQEYSLQSFGEMADSFKSDYFNMPVHMVPTELVEKEFWRLVS
SIEEDVTVEYGADIHSKEFGSGFPVSNSKQNLSPEEKEYATSGWNLNVMPVLDQSVLCHI
NADISGMKVPWLYVGMVFSAFCWHIEDHWSYSINYLHWGEPKTWYGVPSLAAEHLEEVMK
MLTPELFDSQPDLLHQLVTLMNPNTLMSHGVPVVRTNQCAGEFVITFPRAYHSGFNQGYN
FAEAVNFCTADWLPAGRQCIEHYRRLRRYCVFSHEELICKMAAFPETLDLNLAVAVHKEM
FIMVQEERRLRKALLEKGVTEAEREAFELLPDDERQCIKCKTTCFLSALACYDCPDGLVC
LSHINDLCKCSSSRQYLRYRYTLDELPTMLHKLKIRAESFDTWANKVRVALEVEDGRKRS
FEELRALESEARERRFPNSELLQRLKNCLSEVEACIAQVLGLVSGQVARMDTPQLTLTEL
RVLLEQMGSLPCAMHQIGDVKDVLEQVEAYQAEAREALATLPSSPGLLRSLLERGQQLGV
EVPEAHQLQQQVEQAQWLDEVKQALAPSAHRGSLVIMQGLLVMGAKIASSPSVDKARAEL
QELLTIAERWEEKAHFCLEARQKHPPATLEAIIRETENIPVHLPNIQALKEALTKAQAWI
ADVDEIQNGDHYPCLDDLEGLVAVGRDLPVGLEELRQLELQVLTAHSWREKASKTFLKKN
SCYTLLEVLCPCADAGSDSTKRSRWMEKALGLYQCDTELLGLSAQDLRDPGSVIVAFKEG
EQKEKEGILQLRRTNSAKPSPLAPSLMASSPTSICVCGQVPAGVGVLQCDLCQDWFHGQC
VSVPHLLTSPKPSLTSSPLLAWWEWDTKFLCPLCMRSRRPRLETILALLVALQRLPVRLP
EGEALQCLTERAIGWQDRARKALASEDVTALLRQLAELRQQLQAKPRPEEASVYTSATAC
DPIREGSGNNISKVQGLLENGDSVTSPENMAPGKGSDLELLSSLLPQLTGPVLELPEAIR
APLEELMMEGDLLEVTLDENHSIWQLLQAGQPPDLDRIRTLLELEKFEHQGSRTRSRALE
RRRRRQKVDQGRNVENLVQQELQSKRARSSGIMSQVGREEEHYQEKADRENMFLTPSTDH
SPFLKGNQNSLQHKDSGSSAACPSLMPLLQLSYSDEQQL
Target 21 Number of Residues 1564
Target 21 Molecular Weight 174075
Target 21 Theoretical pI 5.66
Target 21 GO Classification
Function
ion binding
cation binding
transition metal ion binding
zinc ion binding
protein binding
binding
nucleic acid binding
DNA binding
Process
regulation of biological process
regulation of physiological process
regulation of metabolism
regulation of cellular metabolism
regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
regulation of transcription
regulation of transcription, DNA-dependent
Component
organelle
membrane-bound organelle
intracellular membrane-bound organelle
nucleus
cell
intracellular
Target 21 General Function Not Available
Target 21 Specific Function May play a role in spermatogenesis
Target 21 Pathways Not Available
Target 21 Reactions Not Available
Target 21 Pfam Domain Function
Target 21 Signals
  • None
Target 21 Transmembrane Regions
  • None
Target 21 Essentiality Non-Essential
Target 21 GenBank ID Protein 1661016 Link Image
Target 21 UniProtKB/Swiss-Prot ID Q9BY66 Link Image
Target 21 UniProtKB/Swiss-Prot Entry Name JAD1D_HUMAN Link Image
Target 21 PDB ID Not Available
Target 21 Cellular Location
  • Cytoplasmic
Target 21 Gene Sequence >4620 bp
ATGGAACCGGGGTGTGACGAGTTCCTGCCGCCACCGGAGTGCCCGGTTTTTGAGCCTAGC
TGGGCTGAATTCCAAGACCCGCTTGGCTACATTGCGAAAATAAGGCCCATAGCAGAGAAG
TCTGGCATCTGCAAAATCCGCCCACCCGCGGATTGGCAGCCTCCTTTTGCAGTAGAAGTT
GACAATTTCAGATTTACTCCTCGCGTCCAAAGGCTAAATGAACTGGAGGCCCAAACTAGA
GTGAAATTGAACTATTTGGATCAGATTGCAAAATTCTGGGAAATTCAAGGCTCCTCTTTA
AAGATTCCCAATGTGGAGCGGAAGATCTTGGACCTCTACAGCCTTAGTAAGATTGTGATT
GAGGAAGGTGGCTATGAAGCCATCTGCAAGGATCGTCGGTGGGCTCGAGTTGCCCAGCGT
CTCCACTACCCACCAGGCAAAAACATTGGCTCCCTGCTACGATCACATTACGAACGCATT
ATTTACCCCTATGAAATGTTTCAGTCTGGAGCCAACCATGTGCAATGTAACACACACCCG
TTTGACAATGAGGTAAAAGATAAGGAATACAAGCCCCACAGCATCCCCCTTAGACAGTCT
GTGCAGCCTTCAAAGTTCAGCAGCTACAGTCGACGGGCAAAAAGGCTACAGCCTGATCCA
GAGCCTACAGAGGAGGACATTGAGAAGCATCCAGAGCTAAAGAAGTTACAGATATATGGG
CCAGGTCCCAAAATGATGGGCTTGGGCCTTATGGCTAAGGATAAGGATAAGACTGTGCAT
AAGAAAGTCACATGCCCCCCAACTGTTACGGTGAAGGATGAGCAAAGTGGAGGTGGGAAC
GTGTCATCAACATTGCTCAAGCAGCACTTGAGCCTAGAGCCCTGCACTAAGACAACCATG
CAACTTCGAAAGAATCACAGCAGTGCCCAGTTTATTGACTCATATATTTGCCAAGTATGC
TCCCGTGGGGATGAAGATAATAAGCTTCTTTTCTGTGATGGCTGTGATGACAATTACCAC
ATCTTCTGCTTGTTACCACCCCTTCCTGAAATCCCCAGAGGCATCTGGAGGTGCCCAAAA
TGTATCTTGGCGGAGTGTAAACAGCCTCCTGAAGCTTTTGGATTTGAACAGGCTACCCAG
GAGTACAGTTTGCAGAGTTTTGGTGAAATGGCTGATTCCTTCAAGTCCGACTACTTCAAC
ATGCCTGTACATATGGTGCCTACAGAACTTGTAGAGAAGGAATTCTGGAGGCTGGTGAGC
AGCATTGAGGAAGACGTGACAGTTGAATATGGAGCTGATATTCATTCCAAAGAATTTGGC
AGTGGCTTTCCTGTCAGCAATAGCAAACAAAACTTATCTCCTGAGGAGAAGGAGTATGCG
ACCAGTGGTTGGAACCTGAATGTGATGCCAGTGCTAGATCAGTCTGTTCTCTGTCACATC
AATGCAGACATCTCAGGCATGAAGGTGCCCTGGCTGTACGTGGGCATGGTTTTCTCAGCA
TTTTGTTGGCATATTGAGGATCACTGGAGTTACTCTATTAACTATCTGCATTGGGGTGAG
CCGAAGACCTGGTATGGTGTACCCTCCCTGGCAGCAGAGCATTTGGAGGAGGTGATGAAG
ATGCTGACACCTGAGCTGTTTGATAGCCAGCCTGATCTCCTACACCAGCTTGTCACTCTC
ATGAATCCCAACACTTTGATGTCCCATGGTGTGCCAGTTGTCCGCACAAACCAGTGTGCA
GGGGAGTTTGTCATCACTTTTCCTCGTGCTTACCACAGTGGTTTTAACCAAGGCTACAAT
TTTGCTGAAGCTGTCAACTTTTGTACTGCTGACTGGCTACCTGCTGGACGCCAGTGCATT
GAACACTACCGCCGGCTCCGGCGCTATTGTGTCTTCTCCCACGAGGAGCTCATCTGCAAG
ATGGCTGCCTTCCCAGAGACGTTGGATCTCAATCTAGCAGTAGCTGTGCACAAGGAGATG
TTCATTATGGTTCAGGAGGAGCGACGTCTACGAAAGGCCCTTTTGGAGAAGGGCGTCACG
GAGGCTGAGCGAGAGGCTTTTGAGCTGCTCCCAGATGATGAACGCCAGTGCATCAAGTGC
AAGACCACGTGCTTCTTGTCAGCCCTGGCCTGCTACGACTGCCCAGATGGCCTTGTATGC
CTTTCCCACATCAATGACCTCTGCAAGTGCTCTAGTAGCCGACAGTACCTCCGGTATCGG
TACACCTTGGATGAGCTCCCCACCATGCTGCATAAACTGAAGATTCGGGCTGAGTCTTTT
GACACCTGGGCCAACAAAGTGCGAGTGGCCTTGGAGGTGGAGGATGGCCGTAAACGCAGC
TTTGAAGAGCTAAGGGCACTGGAGTCTGAGGCTCGTGAGAGGAGGTTTCCTAATAGTGAG
CTGCTTCAGCGACTGAAGAACTGCCTGAGTGAGGTGGAGGCTTGTATTGCTCAAGTCCTG
GGGCTGGTCAGTGGTCAGGTGGCCAGGATGGACACTCCACAGCTGACTTTGACTGAACTC
CGGGTCCTTCTTGAGCAGATGGGCAGCCTGCCCTGCGCCATGCATCAGATTGGGGATGTC
AAGGATGTCCTGGAACAGGTGGAGGCCTATCAAGCTGAGGCTCGTGAGGCTCTGGCCACA
CTGCCCTCTAGTCCAGGGCTATTGCGGTCCCTGTTGGAGAGGGGGCAGCAGCTGGGTGTA
GAGGTGCCTGAAGCCCATCAGCTTCAGCAGCAGGTGGAGCAGGCGCAATGGCTAGATGAA
GTGAAGCAGGCCCTGGCCCCTTCTGCTCACAGGGGCTCTCTGGTCATCATGCAGGGGCTT
TTGGTTATGGGTGCCAAGATAGCCTCCAGCCCTTCTGTGGACAAGGCCCGGGCTGAGCTG
CAAGAACTACTGACCATTGCAGAGCGCTGGGAAGAAAAGGCTCATTTCTGCCTGGAGGCC
AGGCAGAAGCATCCACCAGCCACATTGGAAGCCATAATTCGTGAGACAGAAAACATCCCT
GTTCACCTGCCTAACATCCAGGCTCTCAAAGAAGCTCTGACTAAGGCACAAGCTTGGATT
GCTGATGTGGATGAGATCCAAAATGGTGACCACTACCCCTGTCTAGATGACTTGGAGGGC
CTGGTGGCTGTGGGCCGGGACCTGCCTGTGGGGCTGGAAGAGCTGAGACAGCTAGAGCTG
CAGGTATTGACAGCACATTCCTGGAGAGAGAAGGCCTCCAAGACCTTTCTCAAGAAGAAT
TCTTGCTACACACTGCTTGAGGTGCTTTGCCCGTGTGCAGACGCTGGCTCAGACAGCACC
AAGCGTAGCCGGTGGATGGAGAAGGCGCTGGGGTTGTACCAGTGTGACACAGAGCTGCTG
GGGCTGTCTGCACAGGACCTCAGAGACCCAGGCTCTGTGATTGTGGCCTTCAAGGAAGGG
GAACAGAAGGAGAAGGAGGGTATCCTGCAGCTGCGTCGCACCAACTCAGCCAAGCCCAGT
CCACTGGCACCATCCCTCATGGCCTCTTCTCCAACTTCTATCTGTGTGTGTGGGCAGGTG
CCAGCTGGGGTGGGACTTCTGCAGTGTGACCTGTGTCAGGACTGGTTCCATGGGCAGTGT
GTGTCAGTGCCCCATCTCCTCACCTCTCCAAAGCCCAGTCTCACTTCATCTCCACTGCTA
GCCTGGTGGGAATGGGACACAAAATTCCTGTGTCCACTGTGTATGCGCTCACGACGGCCA
CGCCTAGAGACAATCCTAGCCTTGCTGGTTGCCCTGCAGAGGCTGCCCGTGCGGCTGCCT
GAGGGTGAGGCCCTTCAGTGTCTCACAGAGAGGGCCATTGGCTGGCAAGACCGTGCCAGA
AAGGCTCTGGCCTTTGAAGATGTGACTGCTCTGTTGCGACAGCTGGCTGAGCTTCGCCAA
CAGCTACAGGCCAAACCCAGACCAGAGGAGGCCTCAGTCTACACTTCAGCCACTGCCTGT
GACCCTATCAGAGAAGGCAGTGGCAACAATATTTCTAAGGTCCAAGGGCTGCTGGAGAAT
GGAGACAGTGTGACCAGTCCTGAGAACATGGCTCCAGGAAAGGGCTCTGACCTGGAGCTA
CTGTCCTCGCTGTTGCCGCAGTTGACTGGCCCTGTGTTGGAGCTGCCTGAGGCAATCCGG
GCTCCCCTGGAGGAGCTCATGATGGAAGGGGGCCTGCTTGAGGTGACCCTGGATGAGAAC
CACAGCATCTGGCAGCTGCTGCAGGCTGGACAGCCTCCAGACCTGGACAGAATTCGCACA
CTTCTGGAGCTGGAAAAATTTGAACATCAAGGGAGTCGGACAAGGAGCCGGGCTCTGGAG
AGGCGACGGCGGCGGCAGAAGGTGGATCAGGGTAGAAACGTTGAGAATCTTGTTCAACAG
GAGCTTCAGTCAAAAAGGGCTCGGAGCTCAGGGATTATGTCTCAGGTGGGCCGAGAAGAA
GAACATTATCAGGAGAAAGCAGACCGTGAAAATATGTTCCTGACACCTTCCACAGACCAC
AGCCCTTTCTTGAAAGGAAACCAAAATAGCTTACAACACAAGGATTCAGGCTCTTCAGCT
GCTTGTCCTTCTTTAATGCCTTTGCTACAACTCTCCTACTCTGATGAGCAACAGTTGTGA
Target 21 GenBank Gene ID
Target 21 GeneCard ID JARID1D Link Image
Target 21 GenAtlas ID JARID1D Link Image
Target 21 HGNC ID HGNC:11115 Link Image
Target 21 Chromosome Location Not Available
Target 21 Locus Yq11|Yq11
Target 21 SNPs SNPJam Report Link Image
Target 21 General References
  1. Shen P, Wang F, Underhill PA, Franco C, Yang WH, Roxas A, Sung R, Lin AA, Hyman RW, Vollrath D, Davis RW, Cavalli-Sforza LL, Oefner PJ: Population genetic implications from sequence variation in four Y chromosome genes. Proc Natl Acad Sci U S A. 2000 Jun 20;97(13):7354-9. [PubMed Link Image]
  2. Kent-First MG, Maffitt M, Muallem A, Brisco P, Shultz J, Ekenberg S, Agulnik AI, Agulnik I, Shramm D, Bavister B, Abdul-Mawgood A, VandeBerg J: Gene sequence and evolutionary conservation of human SMCY. Nat Genet. 1996 Oct;14(2):128-9. [PubMed Link Image]
  3. Nagase T, Seki N, Ishikawa K, Ohira M, Kawarabayasi Y, Ohara O, Tanaka A, Kotani H, Miyajima N, Nomura N: Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain. DNA Res. 1996 Oct 31;3(5):321-9, 341-54. [PubMed Link Image]
  4. Agulnik AI, Bishop CE, Lerner JL, Agulnik SI, Solovyev VV: Analysis of mutation rates in the SMCY/SMCX genes shows that mammalian evolution is male driven. Mamm Genome. 1997 Feb;8(2):134-8. [PubMed Link Image]
Target 21 Drug References
  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 Link Image]
  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 Link Image]
Drug Target 22 [top]
Target 22 ID 3960
Target 22 Name Egl nine homolog 1
Target 22 Synonyms
  1. EC 1.14.11.-
  2. HIF-PH2
  3. HIF-prolyl hydroxylase 2
  4. HPH-2
  5. Hypoxia-inducible factor prolyl hydroxylase 2
  6. PHD2
  7. Prolyl hydroxylase domain-containing protein 2
  8. SM-20
Target 22 Gene Name EGLN1
Target 22 Protein Sequence >Egl nine homolog 1
MANDSGGPGGPSPSERDRQYCELCGKMENLLRCSRCRSSFYCCKEHQRQDWKKHKLVCQG
SEGALGHGVGPHQHSGPAPPAAVPPPRAGAREPRKAAARRDNASGDAAKGKVKAKPPADP
AAAASPCRAAAGGQGSAVAAEAEPGKEEPPARSSLFQEKANLYPPSNTPGDALSPGGGLR
PNGQTKPLPALKLALEYIVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTDGQL
VSQKSDSSKDIRGDKITWIEGKEPGCETIGLLMSSMDDLIRHCNGKLGSYKINGRTKAMV
ACYPGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDAKVSGGILRIFPEGKAQFADIEPKF
DRLLFFWSDRRNPHEVQPAYATRYAITVWYFDADERARAKVKYLTGEKGVRVELNKPSDS
VGKDVF
Target 22 Number of Residues 433
Target 22 Molecular Weight 46021
Target 22 Theoretical pI 8.66
Target 22 GO Classification
Function
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Process
physiological process
metabolism
macromolecule metabolism
protein metabolism
Component
Not Available
Target 22 General Function Posttranslational modification, protein turnover, chaperones
Target 22 Specific Function Catalyzes the posttranslational formation of 4- hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates HIF-1 alpha at 'Pro-402' and 'Pro-564', and HIF-2 alpha. Functions as a cellular oxygen sensor and, under normoxic conditions, targets HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex
Target 22 Pathways Not Available
Target 22 Reactions Not Available
Target 22 Pfam Domain Function
Target 22 Signals
  • None
Target 22 Transmembrane Regions
  • None
Target 22 Essentiality Non-Essential
Target 22 GenBank ID Protein 11345052 Link Image
Target 22 UniProtKB/Swiss-Prot ID Q9GZT9 Link Image
Target 22 UniProtKB/Swiss-Prot Entry Name EGLN1_HUMAN Link Image
Target 22 PDB ID Not Available
Target 22 Cellular Location Not Available
Target 22 Gene Sequence >1281 bp
ATGGCCAATGACAGCGGCGGGCCCGGCGGGCCGAGCCCGAGCGAGCGAGACCGGCAGTAC
TGCGAGCTGTGCGGGAAGATGGAGAACCTGCTGCGCTGCAGCCGCTGCCGCAGCTCCTTC
TACTGCTGCAAGGAGCACCAGCGTCAGGACTGGAAGAAGCACAAGCTCGTGTGCCAGGGC
AGCGAGGGCGCCCTCGGCCACGGAGTGGGCCCACACCAGCATTCCGGCCCCGCGCCGCCG
GCTGCAGTGCCGCCGCCCAGGGCCGGGGCCCGGGAGCCCAGGAAGGCAGCGGCGCGCCGG
GACAACGCCTCCGGGGACGCGGCCAAGGGAAAAGTAAAGGCCAAGCCCCCGGCCGACCCA
GCGGCGGCCGCGTCGCCGTGTCGTGCGGCCGCCGGCGGCCAGGGCTCGGCGGTGGCTGCC
GAAGCCGAGCCCGGCAAGGAGGAGCCGCCGGCCCGCTCATCGCTGTTCCAGGAGAAGGCG
AACCTGTACCCCCCAAGCAACACGCCCGGGGATGCGCTGAGCCCCGGCGGCGGCCTGCGG
CCCAACGGGCAGACGAAGCCCCTGCCGGCGCTGAAGCTGGCGCTCGAGTACATCGTGCCG
TGCATGAACAAGCACGGCATCTGTGTGGTGGACGACTTCCTCGGCAAGGAGACCGGACAG
CAGATCGGCGACGAGGTGCGCGCCCTGCACGACACCGGGAAGTTCACGGACGGGCAGCTG
GTCAGCCAGAAGAGTGACTCGTCCAAGGACATCCGAGGCGATAAGATCACCTGGATCGAG
GGCAAGGAGCCCGGCTGCGAAACCATTGGGCTGCTCATGAGCAGCATGGACGACCTGATA
CGCCACTGTAACGGGAAGCTGGGCAGCTACAAAATCAATGGCCGGACGAAAGCCATGGTT
GCTTGTTATCCGGGCAATGGAACGGGTTATGTACGTCATGTTGATAATCCAAATGGAGAT
GGAAGATGTGTGACATGTATATATTATCTTAATAAAGACTGGGATGCCAAGGTAAGTGGA
GGTATACTTCGAATTTTTCCAGAAGGCAAAGCCCAGTTTGCTGACATTGAACCCAAATTT
GATAGACTGCTGTTTTTCTGGTCTGACCGTCGCAACCCTCATGAAGTACAACCAGCATAT
GCTACAAGGTACGCAATAACTGTTTGGTATTTTGATGCAGATGAGAGAGCACGAGCTAAA
GTAAAATATCTAACAGGTGAAAAAGGTGTGAGGGTTGAACTCAATAAACCTTCAGATTCG
GTCGGTAAAGACGTCTTCTAG
Target 22 GenBank Gene ID
Target 22 GeneCard ID EGLN1 Link Image
Target 22 GenAtlas ID EGLN1 Link Image
Target 22 HGNC ID HGNC:1232 Link Image
Target 22 Chromosome Location 1
Target 22 Locus 1q42.1
Target 22 SNPs SNPJam Report Link Image
Target 22 General References
  1. Dupuy D, Aubert I, Duperat VG, Petit J, Taine L, Stef M, Bloch B, Arveiler B: Mapping, characterization, and expression analysis of the SM-20 human homologue, c1orf12, and identification of a novel related gene, SCAND2. Genomics. 2000 Nov 1;69(3):348-54. [PubMed Link Image]
  2. Taylor MS: Characterization and comparative analysis of the EGLN gene family. Gene. 2001 Sep 5;275(1):125-32. [PubMed Link Image]
  3. Semenza GL: HIF-1, O(2), and the 3 PHDs: how animal cells signal hypoxia to the nucleus. Cell. 2001 Oct 5;107(1):1-3. [PubMed Link Image]
  4. Epstein AC, Gleadle JM, McNeill LA, Hewitson KS, O'Rourke J, Mole DR, Mukherji M, Metzen E, Wilson MI, Dhanda A, Tian YM, Masson N, Hamilton DL, Jaakkola P, Barstead R, Hodgkin J, Maxwell PH, Pugh CW, Schofield CJ, Ratcliffe PJ: C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell. 2001 Oct 5;107(1):43-54. [PubMed Link Image]
  5. Oehme F, Ellinghaus P, Kolkhof P, Smith TJ, Ramakrishnan S, Hutter J, Schramm M, Flamme I: Overexpression of PH-4, a novel putative proline 4-hydroxylase, modulates activity of hypoxia-inducible transcription factors. Biochem Biophys Res Commun. 2002 Aug 16;296(2):343-9. [PubMed Link Image]
  6. Ivan M, Haberberger T, Gervasi DC, Michelson KS, Gunzler V, Kondo K, Yang H, Sorokina I, Conaway RC, Conaway JW, Kaelin WG Jr: Biochemical purification and pharmacological inhibition of a mammalian prolyl hydroxylase acting on hypoxia-inducible factor. Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13459-64. Epub 2002 Sep 26. [PubMed Link Image]
  7. Cioffi CL, Liu XQ, Kosinski PA, Garay M, Bowen BR: Differential regulation of HIF-1 alpha prolyl-4-hydroxylase genes by hypoxia in human cardiovascular cells. Biochem Biophys Res Commun. 2003 Apr 11;303(3):947-53. [PubMed Link Image]
Target 22 Drug References
  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 Link Image]
  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 Link Image]
Drug Target 23 [top]
Target 23 ID 3962
Target 23 Name Egl nine homolog 3
Target 23 Synonyms
  1. EC 1.14.11.-
  2. HIF-PH3
  3. HIF-prolyl hydroxylase 3
  4. HPH-1
  5. Hypoxia-inducible factor prolyl hydroxylase 3
  6. PHD3
  7. Prolyl hydroxylase domain-containing protein 3
Target 23 Gene Name EGLN3
Target 23 Protein Sequence >Egl nine homolog 3
MPLGHIMRLDLEKIALEYIVPCLHEVGFCYLDNFLGEVVGDCVLERVKQLHCTGALRDGQ
LAGPRAGVSKRHLRGDQITWIGGNEEGCEAISFLLSLIDRLVLYCGSRLGKYYVKERSKA
MVACYPGNGTGYVRHVDNPNGDGRCITCIYYLNKNWDAKLHGGILRIFPEGKSFIADVEP
IFDRLLFFWSDRRNPHEVQPSYATRYAMTVWYFDAEERAEAKKKFRNLTRKTESALTED
Target 23 Number of Residues 242
Target 23 Molecular Weight 27262
Target 23 Theoretical pI 7.70
Target 23 GO Classification
Function
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Process
physiological process
metabolism
macromolecule metabolism
protein metabolism
Component
Not Available
Target 23 General Function Posttranslational modification, protein turnover, chaperones
Target 23 Specific Function Catalyzes the posttranslational formation of 4- hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates HIF-1 alpha at 'Pro-564', and HIF-2 alpha. Functions as a cellular oxygen sensor and, under normoxic conditions, targets HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. May play a role in cell growth regulation in muscle cells and in apoptosis in neuronal tissue. Promotes cell death through a caspase-dependent mechanism
Target 23 Pathways Not Available
Target 23 Reactions Not Available
Target 23 Pfam Domain Function
Target 23 Signals
  • None
Target 23 Transmembrane Regions
  • None
Target 23 Essentiality Non-Essential
Target 23 GenBank ID Protein 14547150 Link Image
Target 23 UniProtKB/Swiss-Prot ID Q9H6Z9 Link Image
Target 23 UniProtKB/Swiss-Prot Entry Name EGLN3_HUMAN Link Image
Target 23 PDB ID Not Available
Target 23 Cellular Location
  • Cytoplasm
Target 23 Gene Sequence >720 bp
ATGCCCCTGGGACACATCATGAGGCTGGACCTGGAGAAAATTGCCCTGGAGTACATCGTG
CCCTGTCTGCACGAGGTGGGCTTCTGCTACCTGGACAACTTCCTGGGCGAGGTGGTGGGC
GACTGCGTCCTGGAGCGCGTCAAGCAGCTGCACTGCACCGGGGCCCTGCGGGACGGCCAG
CTGGCGGGGCCGCGCGCCGGCGTCTCCAAGCGACACCTGCGGGGCGACCAGATCACGTGG
ATCGGGGGCAACGAGGAGGGCTGCGAGGCCATCAGCTTCCTCCTGTCCCTCATCGACAGG
CTGGTCCTCTACTGCGGGAGCCGGCTGGGCAAATACTACGTCAAGGAGAGGTCTAAGGCA
ATGGTGGCTTGCTATCCGGGAAATGGAACAGGTTATGTTCGCCACGTGGACAACCCCAAC
GGTGATGGTCGCTGCATCACCTGCATCTACTATCTGAACAAGAATTGGGATGCCAAGCTA
CATGGTGGGATCCTGCGGATATTTCCAGAGGGGAAATCATTCATAGCAGATGTGGAGCCC
ATTTTTGACAGACTCCTGTTCTTCTGGTCAGATCGTAGGAACCCACACGAAGTGCAGCCC
TCTTACGCAACCAGATATGCTATGACTGTCTGGTACTTTGATGCTGAAGAAAGGGCAGAA
GCCAAAAAGAAATTCAGGAATTTAACTAGGAAAACTGAATCTGCCCTCACTGAAGACTGA
Target 23 GenBank Gene ID
Target 23 GeneCard ID EGLN3 Link Image
Target 23 GenAtlas ID EGLN3 Link Image
Target 23 HGNC ID HGNC:14661 Link Image
Target 23 Chromosome Location 14
Target 23 Locus 14q13.1
Target 23 SNPs SNPJam Report Link Image
Target 23 General References
  1. Taylor MS: Characterization and comparative analysis of the EGLN gene family. Gene. 2001 Sep 5;275(1):125-32. [PubMed Link Image]
  2. Semenza GL: HIF-1, O(2), and the 3 PHDs: how animal cells signal hypoxia to the nucleus. Cell. 2001 Oct 5;107(1):1-3. [PubMed Link Image]
  3. Epstein AC, Gleadle JM, McNeill LA, Hewitson KS, O'Rourke J, Mole DR, Mukherji M, Metzen E, Wilson MI, Dhanda A, Tian YM, Masson N, Hamilton DL, Jaakkola P, Barstead R, Hodgkin J, Maxwell PH, Pugh CW, Schofield CJ, Ratcliffe PJ: C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell. 2001 Oct 5;107(1):43-54. [PubMed Link Image]
  4. Bruick RK, McKnight SL: A conserved family of prolyl-4-hydroxylases that modify HIF. Science. 2001 Nov 9;294(5545):1337-40. Epub 2001 Oct 11. [PubMed Link Image]
  5. Oehme F, Ellinghaus P, Kolkhof P, Smith TJ, Ramakrishnan S, Hutter J, Schramm M, Flamme I: Overexpression of PH-4, a novel putative proline 4-hydroxylase, modulates activity of hypoxia-inducible transcription factors. Biochem Biophys Res Commun. 2002 Aug 16;296(2):343-9. [PubMed Link Image]
  6. Cioffi CL, Liu XQ, Kosinski PA, Garay M, Bowen BR: Differential regulation of HIF-1 alpha prolyl-4-hydroxylase genes by hypoxia in human cardiovascular cells. Biochem Biophys Res Commun. 2003 Apr 11;303(3):947-53. [PubMed Link Image]
Target 23 Drug References
  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 Link Image]
  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 Link Image]
Drug Target 24 [top]
Target 24 ID 3964
Target 24 Name Trimethyllysine dioxygenase, mitochondrial
Target 24 Synonyms
  1. EC 1.14.11.8
  2. Epsilon-trimethyllysine 2-oxoglutarate dioxygenase
  3. TML dioxygenase
  4. TML hydroxylase
  5. TML-alpha- ketoglutarate dioxygenase
  6. TMLD
  7. Trimethyllysine dioxygenase, mitochondrial precursor
Target 24 Gene Name TMLHE
Target 24 Protein Sequence >Trimethyllysine dioxygenase, mitochondrial
MWYHRLSHLHSRLQDLLKGGVIYPALPQPNFKSLLPLAVHWHHTASKSLTCAWQQHEDHF
ELKYANTVMRFDYVWLRDHCRSASCYNSKTHQRSLDTASVDLCIKPKTIRLDETTLFFTW
PDGHVTKYDLNWLVKNSYEGQKQKVIQPRILWNAEIYQQAQVPSVDCQSFLETNEGLKKF
LQNFLLYGIAFVENVPPTQEHTEKLAERISLIRETIYGRMWYFTSDFSRGDTAYTKLALD
RHTDTTYFQEPCGIQVFHCLKHEGTGGRTLLVDGFYAAEQVLQKAPEEFELLSKVPLKHE
YIEDVGECHNHMIGIGPVLNIYPWNKELYLIRYNNYDRAVINTVPYDVVHRWYTAHRTLT
IELRRPENEFWVKLKPGRVLFIDNWRVLHGRECFTGYRQLCGCYLTRDDVLNTARLLGLQ
A
Target 24 Number of Residues 428
Target 24 Molecular Weight 49518
Target 24 Theoretical pI 7.79
Target 24 GO Classification
Function
catalytic activity
oxidoreductase activity
Process
physiological process
metabolism
cellular metabolism
generation of precursor metabolites and energy
electron transport
Component
Not Available
Target 24 General Function Secondary metabolites biosynthesis, transport and catabolism
Target 24 Specific Function Converts trimethyllysine (TML) into hydroxytrimethyllysine (HTML)
Target 24 Pathways
Name SMPDB Link KEGG Link
Lysine degradation SMP00037 Link Image map00310 Link Image
Target 24 Reactions
  • N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2 = 3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
Target 24 Pfam Domain Function
Target 24 Signals
  • None
Target 24 Transmembrane Regions
  • None
Target 24 Essentiality Non-Essential
Target 24 GenBank ID Protein 15553435 Link Image
Target 24 UniProtKB/Swiss-Prot ID Q9NVH6 Link Image
Target 24 UniProtKB/Swiss-Prot Entry Name TMLH_HUMAN Link Image
Target 24 PDB ID Not Available
Target 24 Cellular Location
  • Mitochondrion
Target 24 Gene Sequence >1266 bp
ATGTGGTACCACAGATTGTCCCACCTACACAGCAGGCTTCAGGACTTGCTGAAGGGAGGA
GTCATATATCCGGCCCTTCCACAGCCCAACTTCAAAAGCTTACTTCCTTTAGCTGTCCAT
TGGCACCATACAGCCTCCAAGTCTCTGACTTGTGCTTGGCAGCAACATGAAGATCATTTT
GAGCTGAAATATGCTAATACCGTGATGCGCTTTGATTACGTCTGGCTTCGAGACCACTGC
CGCTCAGCATCGTGCTACAACTCTAAGACTCACCAGCGCAGCCTGGATACTGCCAGTGTG
GATTTATGTATCAAGCCAAAGACCATTCGTCTGGATGAGACCACACTCTTTTTCACTTGG
CCAGATGGTCATGTGACTAAATATGATTTGAATTGGCTGGTGAAAAACAGCTATGAAGGG
CAGAAACAAAAAGTCATCCAGCCTAGAATACTATGGAATGCTGAAATCTACCAGCAAGCC
CAAGTTCCATCGGTAGATTGCCAGAGCTTCTTAGAAACCAACGAGGGACTGAAGAAGTTT
CTGCAAAACTTTCTGCTCTATGGAATTGCATTCGTAGAAAATGTCCCTCCCACTCAAGAG
CACACAGAGAAGTTGGCAGAAAGGATCAGCTTAATCAGAGAAACCATTTATGGGAGGATG
TGGTATTTCACTTCAGACTTCTCCAGAGGTGACACTGCGTACACCAAGCTAGCTCTGGAT
CGGCACACTGACACTACCTATTTTCAAGAGCCCTGTGGCATTCAAGTGTTTCATTGTCTT
AAACATGAAGGAACTGGTGGCAGGACACTGCTAGTAGATGGATTCTATGCAGCAGAACAG
GTACTTCAAAAGGCACCTGAGGAATTTGAACTCCTCAGTAAAGTGCCATTGAAGCATGAA
TATATTGAAGATGTTGGAGAATGTCACAACCACATGATTGGGATTGGGCCAGTCTTAAAT
ATCTACCCATGGAATAAAGAGCTGTATTTGATCAGGTACAACAACTATGACCGGGCTGTC
ATCAATACCGTTCCTTATGATGTCGTCCATCGCTGGTATACAGCACACCGGACTCTAACG
ATAGAGTTGAGGAGACCTGAGAATGAGTTTTGGGTCAAACTAAAGCCTGGCAGGGTCCTA
TTTATAGACAACTGGCGTGTCCTACATGGCAGGGAATGCTTCACTGGCTACCGCCAACTG
TGTGGCTGCTATTTAACAAGAGATGATGTATTAAACACTGCTCGCCTCTTGGGGCTTCAG
GCTTAA
Target 24 GenBank Gene ID
Target 24 GeneCard ID TMLHE Link Image
Target 24 GenAtlas ID TMLHE Link Image
Target 24 HGNC ID HGNC:18308 Link Image
Target 24 Chromosome Location X
Target 24 Locus Xq28
Target 24 SNPs SNPJam Report Link Image
Target 24 General References
  1. Vaz FM, Ofman R, Westinga K, Back JW, Wanders RJ: Molecular and Biochemical Characterization of Rat epsilon -N-Trimethyllysine Hydroxylase, the First Enzyme of Carnitine Biosynthesis. J Biol Chem. 2001 Sep 7;276(36):33512-7. Epub 2001 Jun 28. [PubMed Link Image]
Target 24 Drug References
  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 Link Image]
  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 Link Image]
Drug Target 25 [top]
Target 25 ID 3966
Target 25 Name Putative HIF-prolyl hydroxylase PH-4
Target 25 Synonyms
  1. EC 1.14.11.-
  2. Hypoxia-inducible factor prolyl 4-hydroxylase
Target 25 Gene Name PH4
Target 25 Protein Sequence >Putative HIF-prolyl hydroxylase PH-4
MAAAAVTGQRPETAAAEEASRPQWAPPDHCQAQAAAGLGDGEDAPVRPLCKPRGICSRAY
FLVLMVFVHLYLGNVLALLLFVHYSNGDESSDPGPQHRAQGPGPEPTLGPLTRLEGIKVG
HERKVQLVTDRDHFIRTLSLKPLLFEIPGFLTDEECRLIIHLAQMKGLQRSQILPTEEYE
EAMSTMQVSQLDLFRLLDQNRDGHLQLREVLAQTRLGNGWWMTPESIQEMYAAIKADPDG
DGVLSLQEFSNMDLRDFHKYMRSHKAESSELVRNSHHTWLYQGEGAHHIMRAIRQRVLRL
TRLSPEIVELSEPLQVVRYGEGGHYHAHVDSGPVYPETICSHTKLVANESVPFETSCRYM
TVLFYLNNVTGGGETVFPVADNRTYDEMSLIQDDVDLRDTRRHCDKGNLRVKPQQGTAVF
WYNYLPDGQGWVGDVDDYSLHGGCLVTRGTKWIANNWINVDPSRARQALFQQEMARLARE
GGTDSQPEWALDRAYRDARVEL
Target 25 Number of Residues 510
Target 25 Molecular Weight 56662
Target 25 Theoretical pI 5.99
Target 25 GO Classification
Function
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
binding
ion binding
cation binding
calcium ion binding
Process
physiological process
metabolism
macromolecule metabolism
protein metabolism
Component
Not Available
Target 25 General Function Not Available
Target 25 Specific Function May catalyze the posttranslational formation of 4- hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. May function as a cellular oxygen sensor and, under normoxic conditions, may target HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex
Target 25 Pathways Not Available
Target 25 Reactions Not Available
Target 25 Pfam Domain Function
Target 25 Signals
  • None
Target 25 Transmembrane Regions
  • None
Target 25 Essentiality Non-Essential
Target 25 GenBank ID Protein 28566186 Link Image
Target 25 UniProtKB/Swiss-Prot ID Q9NXG6 Link Image
Target 25 UniProtKB/Swiss-Prot Entry Name EGLX_HUMAN Link Image
Target 25 PDB ID Not Available
Target 25 Cellular Location
  • Endoplasmic reticulum
Target 25 Gene Sequence >1509 bp
ATGGCGGCAGCGGCGGTGACAGGCCAGCGGCCTGAGACCGCGGCGGCCGAGGAGGCCTCG
AGGCCGCAGTGGGCGCCGCCAGACCACTGCCAGGCTCAGGCGGCGGCCGGGCTGGGCGAC
GGCGAGGACGCACCGGTGCGTCCGCTGTGCAAGCCCCGCGGCATCTGCTCGCGCGCCTAC
TTCCTGGTGCTGATGGTGTTCGTGCACCTGTACCTGGGTAACGTGCTGGCGCTGCTGCTC
TTCGTGCACTACAGCAACGGCGACGAAAGCAGCGATCCCGGGCCCCAACACCGTGCCCAG
GGCCCCGGGCCCGAGCCCACCTTAGGTCCCCTCACCCGGCTGGAGGGCATCAAGGTGGGG
CACGAGCGTAAGGTCCAGCTGGTCACCGACAGGGATCACTTCATCCGAACCCTCAGCCTC
AAGCCGCTGCTCTTCGAAATCCCCGGCTTCCTGACTGATGAAGAGTGTCGGCTCATCATC
CATCTGGCGCAGATGAAGGGGTTACAGCGCAGCCAGATCCTGCCTACTGAAGAGTATGAA
GAGGCAATGAGCACTATGCAGGTCAGCCAGCTGGACCTCTTCCGGCTGCTGGACCAGAAC
CGTGATGGGCACCTTCAGCTCCGTGAGGTTCTGGCCCAGACTCGCCTGGGAAATGGATGG
TGGATGACTCCAGAGAGCATTCAGGAGATGTACGCCGCGATCAAGGCTGACCCTGATGCT
GACGGAGTGCTGAGTCTGCAGGAGTTCTCCAACATGGACCTTCGGGACTTCCACAAGTAC
ATGAGGAGCCACAAGGCAGAGTCCAGTGAGCTGGTGCGGAACAGCCACCATACCTGGCTC
TACCAGGGTGAGGGTGCCCACCACATCATGCGTGCCATCCGCCAGAGGGTGCTGCGCCTC
ACTCGCCTGTCGCCTGAGATCGTGGAGCTCAGCGAGCCGCTGCAGGTTGTTCGATATGGT
GAGGGGGGCCACTACCATGCCCACGTGGACAGTGGGCCTGTGTACCCAGAGACCATCTGC
TCCCATACCAAGCTGGTAGCCAACGAGTCTGTACCCTTCGAGACCTCCTGCCGCTACATG
ACAGTGCTGTTTTATTTGAACAACGTCACTGGTGGGGGCGAGACTGTTTTCCCTGTAGCA
GATAACAGAACCTACGATGAAATGAGTCTGATTCAGGATGACGTGGACCTCCGTGACACA
CGGAGGCACTGTGACAAGGGAAACCTGCGTGTCAAGCCCCAACAGGGCACAGCAGTCTTC
TGGTACAACTACCTGCCTGATGGGCAAGGTTGGGTGGGTGACGTAGACGACTACTCGCTG
CACGGGGGCTGCCTGGTCACGCGCGGCACCAAGTGGATTGCCAACAACTGGATTAATGTG
GACCCCAGCCGAGCGCGGCAAGCGCTGTTCCAACAGGAGATGGCCCGCCTTGCCCGAGAA
GGGGGCACCGACTCACAGCCCGAGTGGGCTCTGGACCGGGCCTACCGCGATGCGCGCGTG
GAACTCTGA
Target 25 GenBank Gene ID
Target 25 GeneCard ID Not Available
Target 25 GenAtlas ID Not Available
Target 25 HGNC ID Not Available
Target 25 Chromosome Location Not Available
Target 25 Locus Not Available
Target 25 SNPs SNPJam Report Link Image
Target 25 General References
  1. Oehme F, Ellinghaus P, Kolkhof P, Smith TJ, Ramakrishnan S, Hutter J, Schramm M, Flamme I: Overexpression of PH-4, a novel putative proline 4-hydroxylase, modulates activity of hypoxia-inducible transcription factors. Biochem Biophys Res Commun. 2002 Aug 16;296(2):343-9. [PubMed Link Image]
Target 25 Drug References
  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 Link Image]
  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 Link Image]
Drug Target 26 [top]
Target 26 ID 4656
Target 26 Name Myrosinase MA1
Target 26 Synonyms
  1. EC 3.2.1.147
  2. Sinigrinase
  3. Thioglucosidase
Target 26 Gene Name Not Available
Target 26 Protein Sequence >Myrosinase MA1
DEEITCQENLPFTCGNTDALNSSSFSSDFIFGVASSAYQIEGTIGRGLNIWDGFTHRYPN
KSGPDHGNGDTTCDSFSYWQKDIDVLDELNATGYRFSIAWSRIIPRGKRSRGVNEKGIDY
YHGLISGLIKKGITPFVTLFHWDLPQTLQDEYEGFLDPQIIDDFKDYADLCFEEFGDSVK
YWLTINQLYSVPTRGYGSALDAPGRCSPTVDPSCYAGNSSTEPYIVAHHQLLAHAKVVDL
YRKNYTHQGGKIGPTMITRWFLPYNDTDRHSIAATERMKEFFLGWFMGPLTNGTYPQIMI
DTVGERLPSFSPEESNLVKGSYDFLGLNYYFTQYAQPSPNPVNSTNHTAMMDAGAKLTYI
NASGHYIGPLFEKDKADSTDNIYYYPKGIYSVMDYFKNKYYNPLIYVTENGISTPGDENR
NQSMLDYTRIDYLCSHLCFLNKVIKEKDVNVKGYLAWALGDNYEFNKGFTVRFGLSYIDW
NNVTDRDLKKSGQWYQSFISP
Target 26 Number of Residues 509
Target 26 Molecular Weight 57023
Target 26 Theoretical pI 5.08
Target 26 GO Classification
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on glycosyl bonds
hydrolase activity, hydrolyzing O-glycosyl compounds
Process
physiological process
metabolism
macromolecule metabolism
carbohydrate metabolism
Component
Not Available
Target 26 General Function Involved in hydrolase activity, hydrolyzing O-glycosyl compounds
Target 26 Specific Function Degradation of glucosinolates (glucose residue linked by a thioglucoside bound to an amino acid derivative) to glucose, sulfate and any of the products:thiocyanates, isothiocyanates, nitriles, epithionitriles or oxazolidine-2-thiones
Target 26 Pathways Not Available
Target 26 Reactions Not Available
Target 26 Pfam Domain Function
Target 26 Signals
  • None
Target 26 Transmembrane Regions
  • None
Target 26 Essentiality Essential
Target 26 GenBank ID Protein Not Available
Target 26 UniProtKB/Swiss-Prot ID P29736 Link Image
Target 26 UniProtKB/Swiss-Prot Entry Name MYRA_SINAL Link Image
Target 26 PDB ID 1E71 Link Image
Target 26 PDB File Show
Target 26 3D Structure
Target 26 Cellular Location
  • Vacuole
Target 26 Gene Sequence Not Available
Target 26 GenBank Gene ID
Target 26 GeneCard ID Not Available
Target 26 GenAtlas ID Not Available
Target 26 HGNC ID Not Available
Target 26 Chromosome Location Not Available
Target 26 Locus Not Available
Target 26 SNPs Not Available
Target 26 General References
  1. Xue JP, Lenman M, Falk A, Rask L: The glucosinolate-degrading enzyme myrosinase in Brassicaceae is encoded by a gene family. Plant Mol Biol. 1992 Jan;18(2):387-98. [PubMed Link Image]
  2. Burmeister WP, Cottaz S, Driguez H, Iori R, Palmieri S, Henrissat B: The crystal structures of Sinapis alba myrosinase and a covalent glycosyl-enzyme intermediate provide insights into the substrate recognition and active-site machinery of an S-glycosidase. Structure. 1997 May 15;5(5):663-75. [PubMed Link Image]
Target 26 Drug References Not Available
Drug Target 27 [top]
Target 27 ID 4911
Target 27 Name Ascorbate peroxidase
Target 27 Synonyms
  1. Cytosolic ascorbate peroxidase 1
  2. EC 1.11.1.11
Target 27 Gene Name apx1
Target 27 Protein Sequence >Ascorbate peroxidase
MGKSYPTVSADYQKAVEKAKKKLRGFIAEKRCAPLMLRLAWHSAGTFDKGTKTGGPFGTI
KHPAELAHSANNGLDIAVRLLEPLKAEFPILSYADFYQLAGVVAVEVTGGPEVPFHPGRE
DKPEPPPEGRLPDATKGSDHLRDVFGKAMGLTDQDIVALSGGHTIGAAHKERSGFEGPWT
SNPLIFDNSYFTELLSGEKEGLLQLPSDKALLSDPVFRPLVDKYAADEDAFFADYAEAHQ
KLSELGFADA
Target 27 Number of Residues 254
Target 27 Molecular Weight 27052
Target 27 Theoretical pI 5.60
Target 27 GO Classification
Function
antioxidant activity
peroxidase activity
Process
physiological process
metabolism
cellular metabolism
oxygen and reactive oxygen species metabolism
response to oxidative stress
Component
Not Available
Target 27 General Function Involved in peroxidase activity
Target 27 Specific Function Not Available
Target 27 Pathways Not Available
Target 27 Reactions Not Available
Target 27 Pfam Domain Function
Target 27 Signals
  • None
Target 27 Transmembrane Regions
  • None
Target 27 Essentiality Essential
Target 27 GenBank ID Protein Not Available
Target 27 UniProtKB/Swiss-Prot ID Q43758 Link Image
Target 27 UniProtKB/Swiss-Prot Entry Name Q43758_SOYBN Link Image
Target 27 PDB ID 1V0H Link Image
Target 27 PDB File Show
Target 27 3D Structure
Target 27 Cellular Location Not Available
Target 27 Gene Sequence >753 bp
ATGGGAAAGTCTTACCCAACTGTGAGTGCTGATTACCAGAAGGCCGTTGAGAAGGCGAAG
AAGAAGCTCAGAGGCTTCATCGCTGAGAAGAGATGCGCTCCTCTAATGCTCCGTTTGGCA
TGGCACTCTGCTGGAACCTTTGACAAGGGCACGAAGACCGGTGGACCCTTCGGAACCATC
AAGCACCCTGCCGAACTGGCTCACAGCGCTAACAACGGTCTTGACATCGCTGTTAGGCTT
TTGGAGCCACTCAAGGCGGAGTTCCCTATTTTGAGCTACGCCGATTTCTACCAGTTGGCT
GGCGTTGTTGCCGTTGAGGTCACGGGTGGACCTGAAGTTCCATTCCACCCTGGAAGAGAG
GACAAGCCTGAGCCACCACCAGAGGGTCGCTTGCCCGATGCCACTAAGGGTTCTGACCAT
TTGAGAGATGTGTTTGGCAAAGCTATGGGGCTTACTGACCAAGATATCGTTGCTCTATCT
GGGGGTCACACTATTGGAGCTGCACACAAGGAGCGTTCTGGATTTGAGGGTCCCTGGACC
TCTAATCCTCTTATTTTCGACAACTCATACTTCACGGAGTTGTTGAGTGGTGAGAAGGAA
GGTCTCCTTCAGCTACCTTCTGACAAGGCTCTTTTGTCTGACCCTGTATTCCGCCCTCTC
GTTGATAAATATGCAGCGGACGAAGATGCCTTCTTTGCTGATTACGCTGAGGCTCACCAA
AAGCTTTCCGAGCTTGGGTTTGCTGATGCCTAA
Target 27 GenBank Gene ID
Target 27 GeneCard ID Not Available
Target 27 GenAtlas ID Not Available
Target 27 HGNC ID Not Available
Target 27 Chromosome Location Not Available
Target 27 Locus Not Available
Target 27 SNPs SNPJam Report Link Image
Target 27 General References
  1. Chatfield M, Dalton DA: Ascorbate peroxidase from soybean root nodules. Plant Physiol. 1993 Oct;103(2):661-2. [PubMed Link Image]
Target 27 Drug References Not Available

This project is supported by Genome Alberta & Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government. This project is also supported in part by GenomeQuest, Inc., an enterprise genomic information company serving the life science community.