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Showing drug card for Succinic acid (DB00139)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-04-16 16:47:27
Primary Accession Number DB00139
Secondary Accession Number
  • NUTR00054
Name Succinic acid
Drug Type
  • Approved
  • Nutraceutical
  • Small Molecule
Description A water-soluble, colorless crystal with an acid taste that is used as a chemical intermediate, in medicine, the manufacture of lacquers, and to make perfume esters. It is also used in foods as a sequestrant, buffer, and a neutralizing agent. (Hawley's Condensed Chemical Dictionary, 12th ed, p1099; McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed, p1851)
Synonyms
  1. 1,2-Ethanedicarboxylic acid
  2. Acid of amber
  3. Amber acid
  4. Asuccin
  5. Bernsteinsaure
  6. Butanedioic acid
  7. Butanedionic acid
  8. Dicarboxylic acid
  9. Dihydrofumaric acid
  10. Ethanedicarboxylic acid
  11. Ethylene succinic acid
  12. Ethylenesuccinic acid
  13. Sal succini
  14. Spirit of amber
  15. Succinate
  16. Succinellite
  17. Succinicum acidum
  18. Succinicun acidum
Brand Names
  1. Katasuccin
  2. Kyselina jantarova
Brand Mixtures
  1. Ubicoenzyme (Beet + Cerium-Oxalate + Citric Acid + Hydrastis Canadensis + Lipoic Acid + Alpha + Nadidum + Oyster Shells + Selenium + Silicon Dioxide + Succinic Acid + Sulfur + Thuja Occidentalis)
Chemical IUPAC Name butanedioic acid
Chemical Formula C4H6O4
Chemical Structure Structure
CAS Registry Number 110-15-6
InChI Identifier InChI=1/C4H6O4/c5-3(6)1-2-4(7)8/h1-2H2,(H,5,6)(H,7,8)/f/h5,7H
InChI Key KDYFGRWQOYBRFD-AOTPWWKUCA
KEGG Drug Not Available
KEGG Compound C00042 Link Image
PubChem Compound 1110 Link Image
PubChem Substance 3344 Link Image
ChEBI ID 15741 Link Image
PharmGKB ID Not Available
HET ID SIN Link Image
GenBank ID Not Available
Drug ID Number [DIN] Not Available
RxList Link Not Available
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Succinate Link Image
FDA Label Not Available
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 118.0880
Monoisotopic Molecular Weight 118.0266
State Solid
Melting Point 185-188 oC
Experimental Water Solubility 83.2 mg/mL at 25 oC [YALKOWSKY,SH & HE,Y (2003)] Source: PhysProp
Predicted Water Solubility 2.11e+02 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity -0.7 Source: PhysProp
Predicted LogP -0.52 Calculated using ALOGPS
Experimental LogS -0.2 [ADME Research, USCD]
Predicted LogS 0.25 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point Not Available
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 1CZE Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES OC(=O)CCC(O)=O
Canonical SMILES OC(=O)CCC(O)=O
Drug Category
  • Anti-Ulcer Agents
  • Dietary supplement
  • Micronutrient
  • Radiation-Protective Agents
ATC Codes Not Available
AHFS Codes
  • 92:02.00*
Indication For nutritional supplementation, also for treating dietary shortage or imbalance
Pharmacology Not Available
Mechanism of Action Succinate is an essential component of the Krebs or citric acid cycle and serves an electron donor in the production of fumaric acid and FADH2. It also has been shown to be a good "natural" antibiotic because of its relative acidic or caustic nature (high concentrations can even cause burns). Succinate supplements have been shown to help reduce the effects of hangovers by activating the degradation of acetaldehyde - a toxic byproduct of alcohol metabolism - into CO2 and H2O through aerobic metabolism. Succinic acid has been shown to stimulate neural system recovery and bolster the immune system. Claims have also been made that it boosts awareness, concentration and reflexes.
Absorption Not Available
Toxicity Oral rat LD50: 2260 mg/kg
Protein Binding Not Available
Biotransformation Not Available
Half Life Not Available
Dosage Forms
Form Route
Liquid Oral
Solution / drops Oral
Patient Information Not Available
Contraindications Not Available
Interactions Not Available
Drug Interactions Not Available
Food Interactions Not Available
Pathways Not Available
General References
  1. Wikipedia Link Image
Organisms Affected
  • Humans and other mammals
Targets
  1. Solute carrier family 13 member 1
  2. Prolyl 4-hydroxylase subunit alpha-1
  3. Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1
  4. Succinate semialdehyde dehydrogenase, mitochondrial
  5. Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial
  6. Succinyl-CoA ligase [GDP-forming] beta-chain, mitochondrial
  7. Solute carrier family 13 member 2
  8. Aspartyl/asparaginyl beta-hydroxylase
  9. Solute carrier family 13 member 3
  10. Oxidoreductase
  11. Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3
  12. Gamma-butyrobetaine dioxygenase
  13. Prolyl 3-hydroxylase 1
  14. Prolyl 3-hydroxylase 2
  15. Prolyl 3-hydroxylase 3
  16. Trimethyllysine dioxygenase, mitochondrial
  17. Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial
  18. Prolyl 4-hydroxylase subunit alpha-2
  19. Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial
  20. Succinyl-CoA ligase [GDP-forming] subunit alpha, mitochondrial
  21. Succinyl-CoA:3-ketoacid-coenzyme A transferase 1, mitochondrial
  22. Succinate-CoA ligase, ADP-forming, beta subunit
  23. Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
  24. Succinate receptor 1
  25. Succinyl-CoA:3-ketoacid-coenzyme A transferase 2, mitochondrial
  26. Succinyl-CoA ligase [ADP-forming] beta-chain, mitochondrial
  27. Mitochondrial dicarboxylate carrier
Drug Target 1 [top]
Target 1 ID 25
Target 1 Name Solute carrier family 13 member 1
Target 1 Synonyms
  1. Na(+)/sulfate cotransporter
  2. Renal sodium/sulfate cotransporter
  3. hNaSi-1
Target 1 Gene Name SLC13A1
Target 1 Protein Sequence >Solute carrier family 13 member 1
MKFFSYILVYRRFLFVVFTVLVLLPLPIVLHTKEAECAYTLFVVATFWLTEALPLSVTAL
LPSLMLPMFGIMPSKKVASAYFKDFHLLLIGVICLATSIEKWNLHKRIALKMVMMVGVNP
AWLTLGFMSSTAFLSMWLSNTSTAAMVMPIAEAVVQQIINAEAEVEATQMTYFNGSTNHG
LEIDESVNGHEINERKEKTKPVPGYNNDTGKISSKVELEKNSGMRTKYRTKKGHVTRKLT
CLCIAYSSTIGGLTTITGTSTNLIFAEYFNTRYPDCRCLNFGSWFTFSFPAALIILLLSW
IWLQWLFLGFNFKEMFKCGKTKTVQQKACAEVIKQEYQKLGPIRYQEIVTLVLFIIMALL
WFSRDPGFVPGWSALFSEYPGFATDSTVALLIGLLFFLIPAKTLTKTTPTGEIVAFDYSP
LITWKEFQSFMPWDIAILVGGGFALADGCEESGLSKWIGNKLSPLGSLPAWLIILISSLM
VTSLTEVASNPATITLFLPILSPLAEAIHVNPLYILIPSTLCTSFAFLLPVANPPNAIVF
SYGHLKVIDMVKAGLGVNIVGVAVVMLGICTWIVPMFDLYTYPSWAPAMSNETMP
Target 1 Number of Residues 604
Target 1 Molecular Weight 66135
Target 1 Theoretical pI 8.19
Target 1 GO Classification
Function
transporter activity
Process
physiological process
cellular physiological process
transport
ion transport
cation transport
monovalent inorganic cation transport
sodium ion transport
Component
cell
membrane
Target 1 General Function Inorganic ion transport and metabolism
Target 1 Specific Function Sodium/sulfate cotransporter that mediates sulfate reabsorption in the kidney
Target 1 Pathways Not Available
Target 1 Reactions Not Available
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • 13-33
  • 41-61
  • 77-97
  • 108-128
  • 131-151
  • 239-259
  • 290-310
  • 348-368
  • 381-401
  • 464-484
  • 491-511
  • 512-532
  • 554-574
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 12620132 Link Image
Target 1 UniProtKB/Swiss-Prot ID Q9BZW2 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name S13A1_HUMAN Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 1 Gene Sequence >1788 bp
ATGAAATTCTTCAGTTACATTCTGGTTTATCGCCGATTTCTCTTCGTGGTTTTCACTGTG
TTGGTTTTACTACCTCTGCCCATCGTCCTCCACACCAAGGAAGCAGAATGTGCCTACACA
CTCTTTGTGGTCGCCACATTTTGGCTCACAGAAGCATTGCCTCTGTCGGTAACAGCTTTG
CTACCTAGTTTAATGTTACCCATGTTTGGGATCATGCCTTCTAAGAAGGTGGCATCTGCT
TATTTCAAGGATTTTCACTTACTGCTAATTGGAGTTATCTGTTTAGCAACATCCATAGAA
AAATGGAATTTGCACAAGAGAATTGCTCTGAAAATGGTGATGATGGTTGGTGTAAATCCT
GCATGGCTGACGCTGGGGTTCATGAGCAGCACTGCCTTTTTGTCTATGTGGCTCAGCAAC
ACCTCGACGGCTGCCATGGTGATGCCCATTGCGGAGGCTGTAGTGCAGCAGATCATCAAT
GCAGAAGCAGAGGTCGAGGCCACTCAGATGACTTACTTCAACGGATCAACCAACCACGGA
CTAGAAATTGATGAAAGTGTTAATGGACATGAAATAAATGAGAGGAAAGAGAAAACAAAA
CCAGTTCCAGGATACAATAATGATACAGGGAAAATTTCAAGCAAGGTGGAGTTGGAAAAG
AACTCAGGCATGAGAACCAAATATCGAACAAAGAAGGGCCACGTGACACGTAAACTTACG
TGTTTGTGCATTGCCTACTCTTCTACCATTGGTGGACTGACAACAATCACTGGTACCTCC
ACCAACTTGATCTTTGCAGAGTATTTCAATACACGCTATCCTGACTGTCGTTGCCTCAAC
TTTGGATCATGGTTTACGTTTTCCTTCCCAGCTGCCCTTATCATTCTACTCTTATCCTGG
ATCTGGCTTCAGTGGCTTTTCCTAGGATTCAATTTTAAGGAGATGTTCAAATGTGGCAAA
ACCAAAACAGTCCAACAAAAAGCTTGTGCTGAGGTGATTAAGCAAGAATACCAAAAGCTT
GGGCCAATAAGGTATCAAGAAATTGTGACCTTGGTCCTCTTCATTATAATGGCTCTGCTA
TGGTTTAGTCGAGACCCCGGATTTGTTCCTGGTTGGTCTGCACTTTTTTCAGAGTACCCT
GGTTTTGCTACAGATTCAACTGTTGCTTTACTTATAGGGCTGCTATTCTTTCTTATCCCA
GCTAAGACACTGACTAAAACTACACCTACAGGAGAAATTGTTGCTTTTGATTACTCTCCA
CTGATTACTTGGAAAGAATTCCAGTCATTCATGCCCTGGGATATAGCCATTCTTGTTGGT
GGAGGGTTTGCCCTGGCAGATGGTTGTGAGGAGTCTGGATTATCTAAGTGGATAGGAAAT
AAATTATCTCCTCTGGGTTCATTACCAGCATGGCTAATAATTCTGATATCTTCTTTGATG
GTGACATCTTTAACTGAGGTAGCCAGCAATCCAGCTACCATTACACTCTTTCTCCCAATA
TTATCTCCATTGGCCGAAGCCATTCATGTGAACCCTCTTTATATTCTGATACCTTCTACT
CTGTGTACTTCATTTGCATTCCTCCTACCAGTAGCAAATCCACCCAATGCTATTGTCTTT
TCATATGGTCATCTGAAAGTCATTGACATGGTTAAAGCTGGACTTGGTGTCAACATTGTT
GGTGTTGCTGTGGTTATGCTTGGCATATGTACTTGGATTGTACCCATGTTTGACCTCTAC
ACTTACCCTTCGTGGGCTCCTGCTATGAGTAATGAGACCATGCCATAA
Target 1 GenBank Gene ID
Target 1 GeneCard ID SLC13A1 Link Image
Target 1 GenAtlas ID SLC13A1 Link Image
Target 1 HGNC ID HGNC:10916 Link Image
Target 1 Chromosome Location 7
Target 1 Locus 7q31-q32
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Lee A, Beck L, Markovich D: The human renal sodium sulfate cotransporter (SLC13A1; hNaSi-1) cDNA and gene: organization, chromosomal localization, and functional characterization. Genomics. 2000 Dec 15;70(3):354-63. [PubMed Link Image]
Target 1 Drug References
  1. Lee A, Beck L, Markovich D: The human renal sodium sulfate cotransporter (SLC13A1; hNaSi-1) cDNA and gene: organization, chromosomal localization, and functional characterization. Genomics. 2000 Dec 15;70(3):354-63. [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]
Drug Target 2 [top]
Target 2 ID 67
Target 2 Name Prolyl 4-hydroxylase subunit alpha-1
Target 2 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 2 Gene Name P4HA1
Target 2 Protein Sequence >Prolyl 4-hydroxylase alpha-1 subunit precursor
MIWYILIIGILLPQSLAHPGFFTSIGQMTDLIHTEKDLVTSLKDYIKAEEDKLEQIKKWA
EKLDRLTSTATKDPEGFVGHPVNAFKLMKRLNTEWSELENLVLKDMSDGFISNLTIQRQY
FPNDEDQVGAAKALLRLQDTYNLDTDTISKGNLPGVKHKSFLTAEDCFELGKVAYTEADY
YHTELWMEQALRQLDEGEISTIDKVSVLDYLSYAVYQQGDLDKALLLTKKLLELDPEHQR
ANGNLKYFEYIMAKEKDVNKSASDDQSDQKTTPKKKGVAVDYLPERQKYEMLCRGEGIKM
TPRRQKKLFCRYHDGNRNPKFILAPAKQEDEWDKPRIIRFHDIISDAEIEIVKDLAKPRL
RRATISNPITGDLETVHYRISKSAWLSGYENPVVSRINMRIQDLTGLDVSTAEELQVANY
GVGGQYEPHFDFARKDEPDAFKELGTGNRIATWLFYMSDVSAGGATVFPEVGASVWPKKG
TAVFWYNLFASGEGDYSTRHAACPVLVGNKWVSNKWLHERGQEFRRPCTLSELE
Target 2 Number of Residues 542
Target 2 Molecular Weight 61050
Target 2 Theoretical pI 5.84
Target 2 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 2 General Function Involved in oxidoreductase activity
Target 2 Specific Function Catalyzes the posttranslational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins
Target 2 Pathways
Name SMPDB Link KEGG Link
Arginine and proline metabolism SMP00020 Link Image map00330 Link Image
Target 2 Reactions
  • procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2
Target 2 Pfam Domain Function
Target 2 Signals
  • 1-17
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 190786 Link Image
Target 2 UniProtKB/Swiss-Prot ID P13674 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name P4HA1_HUMAN Link Image
Target 2 PDB ID 1TJC Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location
  • Endoplasmic reticulum
  • endoplasmic reticulum lumen
Target 2 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 2 GenBank Gene ID
Target 2 GeneCard ID P4HA1 Link Image
Target 2 GenAtlas ID P4HA1 Link Image
Target 2 HGNC ID HGNC:8546 Link Image
Target 2 Chromosome Location 10
Target 2 Locus 10q21.3-q23.1
Target 2 SNPs SNPJam Report Link Image
Target 2 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 2 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 3 [top]
Target 3 ID 97
Target 3 Name Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1
Target 3 Synonyms
  1. EC 1.14.11.4
  2. LH1
  3. Lysyl hydroxylase 1
  4. Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 precursor
Target 3 Gene Name PLOD1
Target 3 Protein Sequence >Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 precursor
MRPLLLLALLGWLLLAEAKGDAKPEDNLLVLTVATKETEGFRRFKRSAQFFNYKIQALGL
GEDWNVEKGTSAGGGQKVRLLKKALEKHADKEDLVILFADSYDVLFASGPRELLKKFRQA
RSQVVFSAEELIYPDRRLETKYPVVSDGKRFLGSGGFIGYAPNLSKLVAEWEGQDSDSDQ
LFYTKIFLDPEKREQINITLDHRCRIFQNLDGALDEVVLKFEMGHVRARNLAYDTLPVLI
HGNGPTKLQLNYLGNYIPRFWTFETGCTVCDEGLRSLKGIGDEALPTVLVGVFIEQPTPF
VSLFFQRLLRLHYPQKHMRLFIHNHEQHHKAQVEEFLAQHGSEYQSVKLVGPEVRMANAD
ARNMGADLCRQDRSCTYYFSVDADVALTEPNSLRLLIQQNKNVIAPLMTRHGRLWSNFWG
ALSADGYYARSEDYVDIVQGRRVGVWNVPYISNIYLIKGSALRGELQSSDLFHHSKLDPD
MAFCANIRQQDVFMFLTNRHTLGHLLSLDSYRTTHLHNDLWEVFSNPEDWKEKYIHQNYT
KALAGKLVETPCPDVYWFPIFTEVACDELVEEMEHFGQWSLGNNKDNRIQGGYENVPTID
IHMNQIGFEREWHKFLLEYIAPMTEKLYPGYYTRAQFDLAFVVRYKPDEQPSLMPHHDAS
TFTINIALNRVGVDYEGGGCRFLRYNCSIRAPRKGWTLMHPGRLTHYHEGLPTTRGTRYI
AVSFVDP
Target 3 Number of Residues 739
Target 3 Molecular Weight 83551
Target 3 Theoretical pI 6.94
Target 3 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 3 General Function Involved in oxidoreductase activity
Target 3 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 3 Pathways
Name SMPDB Link KEGG Link
Lysine degradation SMP00037 Link Image map00310 Link Image
Target 3 Reactions
  • procollagen L-lysine + 2-oxoglutarate + O2 = procollagen 5-hydroxy-L-lysine + succinate + CO2 ALL_REAC (other) R03376
Target 3 Pfam Domain Function
Target 3 Signals
  • 1-18
Target 3 Transmembrane Regions
  • None
Target 3 Essentiality Non-Essential
Target 3 GenBank ID Protein 190074 Link Image
Target 3 UniProtKB/Swiss-Prot ID Q02809 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name PLOD1_HUMAN Link Image
Target 3 PDB ID Not Available
Target 3 Cellular Location
  • Endoplasmic reticulum
  • peripheral
  • rough endoplasmic reticulum
  • rough endoplasmic reticulum membrane
Target 3 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 3 GenBank Gene ID
Target 3 GeneCard ID PLOD1 Link Image
Target 3 GenAtlas ID PLOD1 Link Image
Target 3 HGNC ID HGNC:9081 Link Image
Target 3 Chromosome Location 1
Target 3 Locus 1p36.3-p36.2
Target 3 SNPs SNPJam Report Link Image
Target 3 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 3 Drug References
  1. Cudic M, Patel DA, Lauer-Fields JL, Brew K, Fields GB: Development of a convenient peptide-based assay for lysyl hydroxylase. Biopolymers. 2007 Jul 3;. [PubMed Link Image]
Drug Target 4 [top]
Target 4 ID 170
Target 4 Name Succinate semialdehyde dehydrogenase, mitochondrial
Target 4 Synonyms
  1. EC 1.2.1.24
  2. NAD(+)-dependent succinic semialdehyde dehydrogenase
  3. Succinate semialdehyde dehydrogenase, mitochondrial precursor
Target 4 Gene Name ALDH5A1
Target 4 Protein Sequence >Succinate semialdehyde dehydrogenase, mitochondrial precursor
MATCIWLRSCGARRLGSTFPGCRLRPRAGGLVPASGPAPGPAQLRCYAGRLAGLSAALLR
TDSFVGGRWLPAAATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKER
SSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIH
TPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALAL
AELASQAGIPSGVYNVIPCSRKNAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSV
KRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAF
AEAMKKNLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFF
EPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWR
VAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVCYGGL
Target 4 Number of Residues 543
Target 4 Molecular Weight 57215
Target 4 Theoretical pI 8.37
Target 4 GO Classification
Function
oxidoreductase activity, acting on the aldehyde or oxo group of donors
oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
aldehyde dehydrogenase activity
catalytic activity
oxidoreductase activity
Process
physiological process
metabolism
Component
Not Available
Target 4 General Function Energy production and conversion
Target 4 Specific Function Not Available
Target 4 Pathways
Name SMPDB Link KEGG Link
Butanoate metabolism map00650 Link Image
Glutamate metabolism SMP00072 Link Image map00251 Link Image
Target 4 Reactions
  • succinate semialdehyde + NAD+ + H2O = succinate + NADH + 2 H+
Target 4 Pfam Domain Function
Target 4 Signals
  • None
Target 4 Transmembrane Regions
  • None
Target 4 Essentiality Non-Essential
Target 4 GenBank ID Protein 3766467 Link Image
Target 4 UniProtKB/Swiss-Prot ID P51649 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name SSDH_HUMAN Link Image
Target 4 PDB ID Not Available
Target 4 Cellular Location Not Available
Target 4 Gene Sequence >1608 bp
ATGGCGACCTGCATTTGGCTGCGGAGCTGTGGGGCCCGGCGCCTCGGGTCGACGTTTCCA
GGCTGCCGCCTCCGCCCCCGCGCCGGCGGCCTGGTCCCTGCCTCCGGGCCTGCGCCCGGC
CCGGCCCAGCTCCGCTGCTACGCTGGGCGCCTGGCGGGCCTCTCTGCGGCGCTGCTGCGC
ACCGACAGCTTCGTGGGCGGCCGCTGGCTCCCGGCCGCCGCCACCTTCCCCGTGCAAGAC
CCGGCCAGCGGCGCCGCTCTGGGCATGGTAGCCGACTGCGGGGTGCGAGAGGCCCGCGCC
GCCGTGCGCGCTGCCTACGAGGCTTTCTGCCGCTGGAGGGAGGTCTCCGCCAAGGAGAGG
AGTTCATTACTTCGGAAGTGGTACAATTTAATGATACAAAATAAGGATGACCTTGCCAGA
ATAATCACAGCTGAAAGTGGAAAGCCACTGAAGGAGGCACATGGAGAAATTCTCTATTCC
GCCTTTTTCCTAGAGTGGTTCTCTGAGGAAGCCCGCCGTGTTTACGGAGACATTATCCAC
ACCCCGGCAAAGGACAGGCGGGCCCTGGTCCTCAAGCAGCCCATAGGCGTGGCTGCAGTC
ATCACCCCGTGGAATTTCCCCAGTGCCATGATCACCCGGAAGGTGGGGGCCGCCCTGGCA
GCCGGCTGTACTGTCGTGGTGAAGCCTGCCGAAGACACGCCCTTCTCCGCCCTGGCCCTG
GCTGAGCTTGCAAGCCAGGCTGGGATTCCTTCAGGTGTATACAATGTTATTCCCTGTTCT
CGAAAGAATGCCAAGGAAGTAGGGGAGGCAATTTGTACTGATCCTCTGGTGTCCAAAATT
TCCTTTACTGGTTCAACAACTACAGGAAAGATCCTGTTGCACCACGCAGCAAACTCTGTG
AAAAGGGTCTCTATGGAGCTGGGCGGCCTTGCTCCATTTATAGTATTTGACAGTGCCAAC
GTGGACCAGGCTGTAGCAGGGGCCATGGCATCTAAATTTAGGAACACTGGACAGACTTGT
GTTTGCTCAAACCAATTCTTGGTGCAAAGGGGCATCCATGATGCCTTTGTAAAAGCATTC
GCCGAGGCCATGAAGAAGAACCTGCGCGTAGGTAATGGATTTGAGGAAGGAACTACTCAG
GGCCCATTAATTAATGAAAAAGCGGTAGAAAAGGTGGAGAAACAGGTGAATGATGCCGTT
TCTAAAGGTGCCACCGTTGTGACAGGTGGAAAACGACACCAACTTGGAAAAAATTTCTTT
GAGCCTACCCTGCTGTGCAATGTCACCCAGGACATGCTGTGCACTCATGAAGAGACTTTC
GGGCCTCTGGCACCAGTTATCAAGTTCGATACAGAGGAGGAGGCTATAGCAATCGCTAAC
GCAGCTGATGTTGGGTTAGCAGGTTATTTTTACTCTCAAGACCCAGCCCAGATCTGGAGA
GTGGCAGAGCAGCTGGAAGTGGGCATGGTTGGCGTCAACGAAGGATTAATTTCCTCTGTG
GAGTGCCCTTTTGGTGGAGTGAAGCAGTCCGGCCTTGGGCGAGAGGGGTCCAAGTATGGC
ATTGATGAGTATCTGGAACTCAAGTATGTGTGTTACGGGGGCTTGTAG
Target 4 GenBank Gene ID
Target 4 GeneCard ID ALDH5A1 Link Image
Target 4 GenAtlas ID ALDH5A1 Link Image
Target 4 HGNC ID HGNC:408 Link Image
Target 4 Chromosome Location 6
Target 4 Locus 6p22.2-p22.3
Target 4 SNPs SNPJam Report Link Image
Target 4 General References
  1. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  2. Chambliss KL, Caudle DL, Hinson DD, Moomaw CR, Slaughter CA, Jakobs C, Gibson KM: Molecular cloning of the mature NAD(+)-dependent succinic semialdehyde dehydrogenase from rat and human. cDNA isolation, evolutionary homology, and tissue expression. J Biol Chem. 1995 Jan 6;270(1):461-7. [PubMed Link Image]
  3. Trettel F, Malaspina P, Jodice C, Novelletto A, Slaughter CA, Caudle DL, Hinson DD, Chambliss KL, Gibson KM: Human succinic semialdehyde dehydrogenase. Molecular cloning and chromosomal localization. Adv Exp Med Biol. 1997;414:253-60. [PubMed Link Image]
  4. Chambliss KL, Hinson DD, Trettel F, Malaspina P, Novelletto A, Jakobs C, Gibson KM: Two exon-skipping mutations as the molecular basis of succinic semialdehyde dehydrogenase deficiency (4-hydroxybutyric aciduria). Am J Hum Genet. 1998 Aug;63(2):399-408. [PubMed Link Image]
Target 4 Drug References
  1. Yogeeswari P, Sriram D, Vaigundaragavendran J: The GABA shunt: an attractive and potential therapeutic target in the treatment of epileptic disorders. Curr Drug Metab. 2005 Apr;6(2):127-39. [PubMed Link Image]
  2. Chiribau CB, Mihasan M, Ganas P, Igloi GL, Artenie V, Brandsch R: Final steps in the catabolism of nicotine. FEBS J. 2006 Apr;273(7):1528-36. [PubMed Link Image]
  3. Wang C, Zhang HB, Wang LH, Zhang LH: Succinic semialdehyde couples stress response to quorum-sensing signal decay in Agrobacterium tumefaciens. Mol Microbiol. 2006 Oct;62(1):45-56. Epub 2006 Aug 30. [PubMed Link Image]
  4. Ahn SJ, Yang CH, Cooksey DA: Pseudomonas putida 06909 genes expressed during colonization on mycelial surfaces and phenotypic characterization of mutants. J Appl Microbiol. 2007 Jul;103(1):120-32. [PubMed Link Image]
  5. Popov VN, Eprintsev AT, Fedorin DN, Fomenko OIu, Igamberdiev AU: [Role of transamination in the mobilization of respiratory substrates in germinating seeds of castor oil plants] Prikl Biokhim Mikrobiol. 2007 May-Jun;43(3):376-81. [PubMed Link Image]
Drug Target 5 [top]
Target 5 ID 197
Target 5 Name Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial
Target 5 Synonyms
  1. EC 1.3.5.1
  2. Flavoprotein subunit of complex II
  3. Fp
  4. Succinate dehydrogenase flavoprotein subunit, mitochondrial precursor
Target 5 Gene Name SDHA
Target 5 Protein Sequence >Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial precursor
MSGVRGLSRLLSARRLALAKAWPTVLQTGTRGFHFTVDGNKRASAKVSDSISAQYPVVDH
EFDAVVVGAGGAGLRAAFGLSEAGFNTACVTKLFPTRSHTVAAQGGINAALGNMEEDNWR
WHFYDTVKGSDWLGDQDAIHYMTEQAPAAVVELENYGMPFSRTEDGKIYQRAFGGQSLKF
GKGGQAHRCCCVADRTGHSLLHTLYGRSLRYDTSYFVEYFALDLLMENGECRGVIALCIE
DGSIHRIRAKNTVVATGGYGRTYFSCTSAHTSTGDGTAMITRAGLPCQDLEFVQFHPTGI
YGAGCLITEGCRGEGGILINSQGERFMERYAPVAKDLASRDVVSRSMTLEIREGRGCGPE
KDHVYLQLHHLPPEQLATRLPGISETAMIFAGVDVTKEPIPVLPTVHYNMGGIPTNYKGQ
VLRHVNGQDQIVPGLYACGEAACASVHGANRLGANSLLDLVVFGRACALSIEESCRPGDK
VPPIKPNAGEESVMNLDKLRFADGSIRTSELRLSMQKSMQNHAAVFRVGSVLQEGCGKIS
KLYGDLKHLKTFDRGMVWNTDLVETLELQNLMLCALQTIYGAEARKESRGAHAREDYKVR
IDEYDYSKPIQGQQKKPFEEHWRKHTLSYVDVGTGKVTLEYRPVIDKTLNEADCATVPPA
IRSY
Target 5 Number of Residues 675
Target 5 Molecular Weight 72692
Target 5 Theoretical pI 7.41
Target 5 GO Classification
Function
binding
nucleotide binding
purine nucleotide binding
adenyl nucleotide binding
FAD binding
oxidoreductase activity, acting on the CH-CH group of donors
catalytic activity
oxidoreductase activity
Process
energy derivation by oxidation of organic compounds
main pathways of carbohydrate metabolism
tricarboxylic acid cycle
physiological process
metabolism
cellular metabolism
generation of precursor metabolites and energy
electron transport
Component
Not Available
Target 5 General Function Energy production and conversion
Target 5 Specific Function Not Available
Target 5 Pathways
Name SMPDB Link KEGG Link
Citrate cycle (TCA cycle) map00020 Link Image
Oxidative phosphorylation map00190 Link Image
Target 5 Reactions
  • succinate + ubiquinone = fumarate + ubiquinol
Target 5 Pfam Domain Function
Target 5 Signals
  • None
Target 5 Transmembrane Regions
  • None
Target 5 Essentiality Non-Essential
Target 5 GenBank ID Protein 506338 Link Image
Target 5 UniProtKB/Swiss-Prot ID P31040 Link Image
Target 5 UniProtKB/Swiss-Prot Entry Name DHSA_HUMAN Link Image
Target 5 PDB ID Not Available
Target 5 Cellular Location
  • Mitochondrion
  • mitochondrial inner membrane
Target 5 Gene Sequence >1995 bp
ATGTCGGGGGTCCGGGGCCTGTCGCGGCTGCTGAGCGCTCGGCGCCTGGCGCTGGCCAAG
GCGTGGCCAACAGTGTTGCAAACAGGAACCCGAGGTTTTCACTTCACTGTTGATGGGAAC
AAGAGGGCATCTGCTAAAGTTTCAGATTCCATTTCTGCTCAGTATCCAGTAGTGGATCAT
GAATTTGATGCAGTGGTGGTAGGCGCTGGAGGGGCAGGCTTGCGAGCTGCATTTGGCCTT
TCTGAGGCAGGGTTTAATACAGCATGTGTTACCAAGCTGTTTCCTACCAGGTCACACACT
GTTGCAGCACAGGGAGGAATCAATGCTGCTCTGGGGAACATGGAGGAGGACAACTGGAGG
TGGCATTTCTACGACACCGTGAAGGGCTCCGACTGGCTGGGGGACCAGGATGCCATCCAC
TACATGACGGAGCAGGCCCCCGCCGCCGTGGTCGAGCTAGAAAATTATGGCATGCCGTTT
AGCAGAACTGAAGATGGGAAGATTTATCAGCGTGCATTTGGTGGACAGAGCCTCAAGTTT
GGAAAGGGCGGGCAGGCCCATCGGTGCTGCTGTGTGGCTGATCGGACTGGCCACTCGCTA
TTGCACACCTTATATGGACGGTCTCTGCGATATGATACCAGCTATTTTGTGGAGTATTTT
GCCTTGGATCTCCTGATGGAGAACGGGGAGTGCCGTGGTGTCATCGCACTGTGCATAGAG
GACGGGTCCATCCATCGCATAAGAGCAAAGAACACTGTTGTTGCCACAGGAGGCTACGGG
CGCACCTACTTCAGCTGCACGTCTGCCCACACCAGCACTGGCGACGGCACGGCCATGATC
ACCAGGGCAGGCCTTCCTTGCCAGGACCTAGAGTTTGTTCAGTTCCACCCTACAGGCATA
TATGGTGCTGGTTGTCTCATTACGGAAGGATGTCGTGGAGAGGGAGGCATTCTCATTAAC
AGTCAAGGCGAAAGGTTTATGGAGCGATACGCCCCTGTCGCGAAGGACCTGGCGTCTAGA
GATGTGGTGTCTCGGTCCATGACTCTGGAGATCCGAGAAGGAAGAGGCTGTGGCCCTGAG
AAAGATCACGTCTACCTGCAGCTGCACCACCTACCTCCAGAGCAGCTGGCCACGCGCCTG
CCTGGCATTTCAGAGACAGCCATGATCTTCGCTGGCGTGGACGTCACGAAGGAGCCGATC
CCTGTCCTCCCCACCGTGCATTATAACATGGGCGGCATTCCCACCAACTACAAGGGGCAG
GTCCTGAGGCACGTGAATGGCCAGGATCAGATTGTGCCCGGCCTGTACGCCTGTGGGGAG
GCCGCCTGTGCCTCGGTACATGGTGCCAACCGCCTCGGGGCAAACTCGCTCTTGGACCTG
GTTGTCTTTGGTCGGGCATGTGCCCTGAGCATCGAAGAGTCATGCAGGCCTGGAGATAAA
GTCCCTCCAATTAAACCAAACGCTGGGGAAGAATCTGTCATGAATCTTGACAAATTGAGA
TTTGCTGATGGAAGCATAAGAACATCGGAACTGCGACTCAGCATGCAGAAGTCAATGCAA
AATCATGCTGCCGTGTTCCGTGTGGGAAGCGTGTTGCAAGAAGGTTGTGGGAAAATCAGC
AAGCTCTATGGAGACCTAAAGCACCTGAAGACGTTCGACCGGGGAATGGTCTGGAACACG
GACCTGGTGGAGACCCTGGAGCTGCAGAACCTGATGCTGTGTGCGCTGCAGACCATCTAC
GGAGCAGAGGCACGGAAGGAGTCACGGGGCGCGCATGCCAGGGAAGACTACAAGGTGCGG
ATTGATGAGTACGATTACTCCAAGCCCATCCAGGGGCAACAGAAGAAGCCCTTTGAGGAG
CACTGGAGGAAGCACACCCTGTCCTATGTGGACGTTGGCACTGGGAAGGTCACTCTGGAA
TATAGACCCGTGATCGACAAAACTTTGAACGAGGCTGACTGTGCCACCGTCCCGCCAGCC
ATTCGCTCCTACTGA
Target 5 GenBank Gene ID
Target 5 GeneCard ID SDHA Link Image
Target 5 GenAtlas ID SDHA Link Image
Target 5 HGNC ID HGNC:10680 Link Image
Target 5 Chromosome Location 5
Target 5 Locus 5p15
Target 5 SNPs SNPJam Report Link Image
Target 5 General References
  1. Van Coster R, Seneca S, Smet J, Van Hecke R, Gerlo E, Devreese B, Van Beeumen J, Leroy JG, De Meirleir L, Lissens W: Homozygous Gly555Glu mutation in the nuclear-encoded 70 kDa flavoprotein gene causes instability of the respiratory chain complex II. Am J Med Genet A. 2003 Jul 1;120(1):13-8. [PubMed Link Image]
  2. Bourgeron T, Rustin P, Chretien D, Birch-Machin M, Bourgeois M, Viegas-Pequignot E, Munnich A, Rotig A: Mutation of a nuclear succinate dehydrogenase gene results in mitochondrial respiratory chain deficiency. Nat Genet. 1995 Oct;11(2):144-9. [PubMed Link Image]
  3. Hirawake H, Wang H, Kuramochi T, Kojima S, Kita K: Human complex II (succinate-ubiquinone oxidoreductase): cDNA cloning of the flavoprotein (Fp) subunit of liver mitochondria. J Biochem (Tokyo). 1994 Jul;116(1):221-7. [PubMed Link Image]
  4. Morris AA, Farnsworth L, Ackrell BA, Turnbull DM, Birch-Machin MA: The cDNA sequence of the flavoprotein subunit of human heart succinate dehydrogenase. Biochim Biophys Acta. 1994 Mar 29;1185(1):125-8. [PubMed Link Image]
Target 5 Drug References
  1. Takeo S, Kokaze A, Ng CS, Mizuchi D, Watanabe JI, Tanabe K, Kojima S, Kita K: Succinate dehydrogenase in Plasmodium falciparum mitochondria: molecular characterization of the SDHA and SDHB genes for the catalytic subunits, the flavoprotein (Fp) and iron-sulfur (Ip) subunits. Mol Biochem Parasitol. 2000 Apr 15;107(2):191-205. [PubMed Link Image]
  2. Ackrell BA: Cytopathies involving mitochondrial complex II. Mol Aspects Med. 2002 Oct;23(5):369-84. [PubMed Link Image]
  3. Maklashina E, Iverson TM, Sher Y, Kotlyar V, Andrell J, Mirza O, Hudson JM, Armstrong FA, Rothery RA, Weiner JH, Cecchini G: Fumarate reductase and succinate oxidase activity of Escherichia coli complex II homologs are perturbed differently by mutation of the flavin binding domain. J Biol Chem. 2006 Apr 21;281(16):11357-65. Epub 2006 Feb 15. [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 6 [top]
Target 6 ID 391
Target 6 Name Succinyl-CoA ligase [GDP-forming] beta-chain, mitochondrial
Target 6 Synonyms
  1. EC 6.2.1.4
  2. GTP- specific succinyl-CoA synthetase subunit beta
  3. SCS-betaG
  4. Succinyl-CoA ligase beta-chain, mitochondrial precursor
  5. Succinyl-CoA synthetase, betaG chain
Target 6 Gene Name SUCLG2
Target 6 Protein Sequence >Succinyl-CoA ligase [GDP-forming] beta-chain, mitochondrial precursor
MASPVAAQAGKLLRALALRPRFLAAGSQAVQLTSRRWLNLQEYQSKKLMSDNGVRVQRFF
VADTANEALEAAKRLNAKEIVLKAQILAGGRGKGVFNSGLKGGVHLTKDPNVVGQLAKQM
IGYNLATKQTPKEGVKVNKVMVAEALDISRETYLAILMDRSCNGPVLVGSPQGGVDIEEV
AASNPELIFKEQIDIFEGIKDSQAQRMAENLGFVGPLKSQAADQITKLYNLFLKIDATQV
EVNPFGETPEGQVVCFDAKINFDDNAEFRQKDIFAMDDKSENEPIENEAAKYDLKYIGLD
GNIACFVNGAGLAMATCDIIFLNGGKPANFLDLGGGVKEAQVYQAFKLLTADPKVEAILV
NIFGGIVNCAIIANGITKACRELELKVPLVVRLEGTNVQEAQKILNNSGLPITSAIDLED
AAKKAVASVAKK
Target 6 Number of Residues 439
Target 6 Molecular Weight 46511
Target 6 Theoretical pI 6.18
Target 6 GO Classification
Function
catalytic activity
Process
physiological process
metabolism
Component
Not Available
Target 6 General Function Energy production and conversion
Target 6 Specific Function Not Available
Target 6 Pathways
Name SMPDB Link KEGG Link
Citrate cycle (TCA cycle) map00020 Link Image
Propanoate metabolism SMP00016 Link Image map00640 Link Image
Target 6 Reactions
  • GTP + succinate + CoA = GDP + phosphate + succinyl-CoA
Target 6 Pfam Domain Function
Target 6 Signals
  • None
Target 6 Transmembrane Regions
  • None
Target 6 Essentiality Non-Essential
Target 6 GenBank ID Protein 133777003 Link Image
Target 6 UniProtKB/Swiss-Prot ID Q96I99 Link Image
Target 6 UniProtKB/Swiss-Prot Entry Name SUCB2_HUMAN Link Image
Target 6 PDB ID 1EUC Link Image
Target 6 PDB File Show
Target 6 3D Structure
Target 6 Cellular Location
  • Mitochondrion
Target 6 Gene Sequence >1290 bp
CCCGTAGCAGCGCAGGCCGGGAAGCTTCTGCGAGCCCTAGCGCTGCGGCCCCGCTTCCTG
GCGGCCGGGTCCCAGGCAGTTCAATTAACCTCCAGAAGATGGCTGAACCTGCAGGAATAC
CAGAGCAAGAAACTGATGTCTGACAACGGAGTGAGAGTTCAAAGATTCTTTGTAGCAGAC
ACTGCAAATGAAGCTCTCGAGGCTGCTAAGAGACTAAATGCAAAAGAAATTGTTTTAAAA
GCCCAGATCTTAGCTGGAGGAAGAGGAAAAGGTGTCTTCAATAGTGGTTTGAAAGGAGGT
GTTCATTTAACAAAAGACCCTAATGTTGTGGGACAGCTGGCTAAACAGATGATTGGGTAC
AATCTAGCGACAAAACAAACTCCAAAAGAAGGTGTGAAAGTTAACAAGGTGATGGTTGCT
GAAGCCTTGGATATTTCCAGAGAAACCTACCTGGCAATTCTGATGGACCGGTCCTGCAAT
GGCCCCGTGCTGGTGGGCAGCCCCCAGGGGGGCGTCGACATTGAAGAGGTGGCTGCTTCA
AACCCGGAGCTCATTTTTAAGGAGCAAATTGACATTTTTGAAGGAATAAAGGACAGCCAA
GCTCAGCGGATGGCCGAAAATCTAGGCTTCGTTGGGCCTTTGAAAAGCCAGGCTGCAGAT
CAAATTACGAAGCTGTATAATCTCTTCCTGAAAATTGATGCTACTCAGGTGGAAGTGAAT
CCCTTTGGTGAAACTCCAGAAGGACAAGTTGTCTGTTTTGATGCCAAGATAAACTTTGAT
GACAACGCAGAATTCCGACAAAAAGACATATTTGCTATGGACGACAAATCAGAGAATGAG
CCCATTGAAAATGAAGCTGCCAAATATGATCTAAAATACATAGGACTAGATGGGAACATT
GCCTGCTTTGTGAATGGTGCTGGGCTCGCCATGGCTACTTGTGATATCATTTTCCTTAAT
GGTGGGAAGCCAGCCAACTTCTTGGATCTTGGAGGTGGTGTAAAGGAAGCTCAAGTATAT
CAAGCATTCAAATTGCTCACAGCTGATCCTAAGGTTGAAGCCATCCTTGTCAATATATTT
GGTGGTATCGTCAACTGTGCCATCATTGCCAATGGGATCACCAAAGCCTGCCGGGAGCTA
GAACTCAAGGTGCCCCTGGTGGTCCGGCTTGAAGGAACCAACGTCCAAGAGGCCCAGAAG
ATACTCAACAACAGCGGACTCCCCATTACTTCAGCCATTGACCTGGAGGATGCAGCCAAG
AAGGCTGTGGCCAGTGTGGCCAAGAAGTGA
Target 6 GenBank Gene ID
Target 6 GeneCard ID SUCLG2 Link Image
Target 6 GenAtlas ID SUCLG2 Link Image
Target 6 HGNC ID HGNC:11450 Link Image
Target 6 Chromosome Location 3
Target 6 Locus 3p14.1
Target 6 SNPs SNPJam Report Link Image
Target 6 General References
  1. Johnson JD, Mehus JG, Tews K, Milavetz BI, Lambeth DO: Genetic evidence for the expression of ATP- and GTP-specific succinyl-CoA synthetases in multicellular eucaryotes. J Biol Chem. 1998 Oct 16;273(42):27580-6. [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 498
Target 7 Name Solute carrier family 13 member 2
Target 7 Synonyms
  1. Na(+)/dicarboxylate cotransporter 1
  2. NaDC-1
  3. Renal sodium/dicarboxylate cotransporter
Target 7 Gene Name SLC13A2
Target 7 Protein Sequence >Solute carrier family 13 member 2
MATCWQALWAYRSYLIVFFVPILLLPLPILVPSKEAYCAYAIILMALFWCTEALPLAVTA
LFPLILFPMMGIVDASEVAVEYLKDSNLLFFGGLLVAIAVEHWNLHKRIALRVLLIVGVR
PAPLILGFMLVTAFLSMWISNTATSAMMVPIAHAVLDQLHSSQASSNVEEGSNNPTFELQ
EPSPQKEVTKLDNGQALPVTSASSEGRAHLSQKHLHLTQCMSLCVCYSASIGGIATLTGT
APNLVLQGQINSLFPQNGNVVNFASWFSFAFPTMVILLLLAWLWLQILFLGFNFRKNFGI
GEKMQEQQQAAYCVIQTEHRLLGPMTFAEKAISILFVILVLLWFTREPGFFLGWGNLAFP
NAKGESMVSDGTVAIFIGIIMFIIPSKFPGLTQDPENPGKLKAPLGLLDWKTVNQKMPWN
IVLLLGGGYALAKGSERSGLSEWLGNKLTPLQSVPAPAIAIILSLLVATFTECTSNVATT
TIFLPILASMAQAICLHPLYVMLPCTLATSLAFMLPVATPPNAIVFSFGDLKVLDMARAG
FLLNIIGVLIIALAINSWGIPLFSLHSFPSWAQSNTTAQCLPSLANTTTPSP
Target 7 Number of Residues 601
Target 7 Molecular Weight 64411
Target 7 Theoretical pI 7.01
Target 7 GO Classification
Function
transporter activity
Process
physiological process
cellular physiological process
transport
ion transport
cation transport
monovalent inorganic cation transport
sodium ion transport
Component
cell
membrane
Target 7 General Function Inorganic ion transport and metabolism
Target 7 Specific Function Cotransport of sodium ions and dicarboxylates such as succinate and citrate
Target 7 Pathways Not Available
Target 7 Reactions Not Available
Target 7 Pfam Domain Function
Target 7 Signals
  • None
Target 7 Transmembrane Regions
  • 13-33
  • 53-73
  • 86-106
  • 114-134
  • 221-241
  • 274-294
  • 324-344
  • 371-391
  • 450-470
  • 482-502
  • 511-531
  • 545-565
Target 7 Essentiality Non-Essential
Target 7 GenBank ID Protein 1098557 Link Image
Target 7 UniProtKB/Swiss-Prot ID Q13183 Link Image
Target 7 UniProtKB/Swiss-Prot Entry Name S13A2_HUMAN Link Image
Target 7 PDB ID Not Available
Target 7 Cellular Location
  • Membrane
  • multi-pass membrane protein (Potential)
Target 7 Gene Sequence >1779 bp
ATGGCCACCTGCTGGCAGGCCCTGTGGGCCTATCGCTCCTACCTGATCGTGTTCTTCGTG
CCCATTCTCCTGCTGCCTCTGCCCATCCTCGTCCCCAGTAAGGAGGCCTACTGCGCGTAT
GCCATCATCCTCATGGCGCTCTTCTGGTGCACTGAGGCCCTGCCCCTGGCCGTCACTGCC
CTCTTCCCCTTAATCCTGTTCCCTATGATGGGCATCGTGGATGCCTCTGAGGTTGCCGTC
GAGTATCTTAAGGACTCCAACCTCCTGTTCTTCGGGGGGCTGCTGGTGGCCATCGCGGTG
GAACACTGGAACCTGCATAAACGCATCGCCCTCCGTGTCCTCCTCATCGTTGGGGTGCGG
CCTGCCCCGCTAATCCTGGGCTTCATGCTGGTCACGGCCTTCCTGTCCATGTGGATCAGC
AACACGGCCACCTCAGCCATGATGGTGCCCATCGCACATGCCGTCCTGGACCAGCTGCAC
AGCTCGCAAGCCAGCAGCAACGTCGAGGAGGGCAGCAACAACCCCACCTTCGAGCTCCAG
GAACCAAGTCCCCAGAAGGAGGTGACCAAGCTTGATAATGGGCAGGCCCTCCCTGTCACG
TCTGCCTCTTCGGAGGGGAGGGCACATCTCAGCCAGAAGCATCTCCACCTCACCCAGTGC
ATGAGCCTGTGCGTGTGCTACTCCGCCAGCATCGGGGGCATCGCCACGCTGACTGGCACC
GCACCCAACCTGGTGCTGCAAGGCCAGATCAACTCGCTCTTCCCCCAAAACGGCAACGTG
GTGAACTTCGCCTCCTGGTTCAGCTTCGCCTTCCCCACCATGGTCATCTTGCTGCTGCTG
GCCTGGTTGTGGCTGCAGATCCTCTTCCTGGGCTTCAACTTCCGGAAGAACTTTGGCATT
GGGGAAAAGATGCAGGAGCAACAGCAGGCAGCCTACTGCGTCATCCAGACCGAGCACAGG
CTGCTGGGCCCCATGACCTTTGCAGAAAAGGCCATCAGCATCCTATTCGTCATCCTGGTG
CTGCTCTGGTTCACCCGGGAGCCGGGCTTTTTTCTTGGCTGGGGCAATTTGGCTTTTCCC
AATGCCAAGGGGGAGAGCATGGTGTCCGATGGGACAGTGGCCATCTTCATCGGCATAATT
ATGTTCATCATACCCTCCAAGTTCCCAGGGCTGACCCAGGACCCAGAAAACCCAGGGAAG
CTGAAGGCCCCTCTTGGCCTCCTCGACTGGAAGACGGTGAACCAGAAGATGCCGTGGAAT
ATCGTGTTATTGCTGGGTGGTGGCTATGCCCTGGCCAAGGGCAGTGAGCGATCGGGCCTG
TCAGAGTGGCTGGGAAACAAGCTGACCCCACTGCAGAGTGTGCCAGCTCCAGCCATTGCC
ATCATCCTCTCCCTCCTGGTGGCCACCTTCACCGAGTGCACTAGCAACGTGGCCACCACT
ACGATCTTCCTGCCCATCCTAGCCTCCATGGCCCAGGCCATCTGCCTCCACCCTCTCTAC
GTCATGCTCCCCTGCACTCTGGCCACCTCCCTGGCCTTCATGTTGCCTGTGGCCACCCCG
CCCAATGCCATCGTCTTCTCTTTCGGGGACCTCAAAGTGTTGGATATGGCCCGGGCAGGA
TTCCTCCTCAACATCATTGGAGTCCTGATCATCGCACTGGCCATCAACAGCTGGGGCATC
CCCCTCTTCAGCCTGCACTCTTTCCCCTCCTGGGCACAGTCCAACACCACAGCCCAGTGC
CTGCCAAGCCTGGCCAACACCACCACACCAAGCCCCTAG
Target 7 GenBank Gene ID
Target 7 GeneCard ID SLC13A2 Link Image
Target 7 GenAtlas ID SLC13A2 Link Image
Target 7 HGNC ID HGNC:10917 Link Image
Target 7 Chromosome Location 17
Target 7 Locus 17p13.2
Target 7 SNPs SNPJam Report Link Image
Target 7 General References
  1. Pajor AM: Molecular cloning and functional expression of a sodium-dicarboxylate cotransporter from human kidney. Am J Physiol. 1996 Apr;270(4 Pt 2):F642-8. [PubMed Link Image]
Target 7 Drug References
  1. Burckhardt BC, Lorenz J, Kobbe C, Burckhardt G: Substrate specificity of the human renal sodium dicarboxylate cotransporter, hNaDC-3, under voltage-clamp conditions. Am J Physiol Renal Physiol. 2005 Apr;288(4):F792-9. Epub 2004 Nov 23. [PubMed Link Image]
  2. Hall JA, Pajor AM: Functional characterization of a Na(+)-coupled dicarboxylate carrier protein from Staphylococcus aureus. J Bacteriol. 2005 Aug;187(15):5189-94. [PubMed Link Image]
  3. Takahashi R, Ishihara H, Tamura A, Yamaguchi S, Yamada T, Takei D, Katagiri H, Endou H, Oka Y: Cell type-specific activation of metabolism reveals that beta-cell secretion suppresses glucagon release from alpha-cells in rat pancreatic islets. Am J Physiol Endocrinol Metab. 2006 Feb;290(2):E308-16. Epub 2005 Sep 27. [PubMed Link Image]
  4. Hagos Y, Steffgen J, Rizwan AN, Langheit D, Knoll A, Burckhardt G, Burckhardt BC: Functional roles of cationic amino acid residues in the sodium-dicarboxylate cotransporter 3 (NaDC-3) from winter flounder. Am J Physiol Renal Physiol. 2006 Dec;291(6):F1224-31. Epub 2006 May 30. [PubMed Link Image]
Drug Target 8 [top]
Target 8 ID 585
Target 8 Name Aspartyl/asparaginyl beta-hydroxylase
Target 8 Synonyms
  1. ASP beta-hydroxylase
  2. Aspartate beta- hydroxylase
  3. EC 1.14.11.16
  4. Peptide-aspartate beta- dioxygenase
Target 8 Gene Name ASPH
Target 8 Protein Sequence >Aspartyl/asparaginyl beta-hydroxylase
MAQRKNAKSSGNSSSSGSGSGSTSAGSSSPGARRETKHGGHKNGRKGGLSGTSFFTWFMV
IALLGVWTSVAVVWFDLVDYEEVLGKLGIYDADGDGDFDVDDAKVLLGLKERSTSEPAVP
PEEAEPHTEPEEQVPVEAEPQNIEDEAKEQIQSLLHEMVHAEHVEGEDLQQEDGPTGEPQ
QEDDEFLMATDVDDRFETLEPEVSHEETEHSYHVEETVSQDCNQDMEEMMSEQENPDSSE
PVVEDERLHHDTDDVTYQVYEEQAVYEPLENEGIEITEVTAPPEDNPVEDSQVIVEEVSI
FPVEEQQEVPPETNRKTDDPEQKAKVKKKKPKLLNKFDKTIKAELDAAEKLRKRGKIEEA
VNAFKELVRKYPQSPRARYGKAQCEDDLAEKRRSNEVLRGAIETYQEVASLPDVPADLLK
LSLKRRSDRQQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEV
LSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTDDGRFYFHLGDAMQRVGN
KEAYKWYELGHKRGHFASVWQRSLINVNGLKAQPCGPKETGYTQLVKSLERNWKLIRDEG
LAVMDKAKGLFLPEDENLREKGDWSQFTLWQQGRRNENACKGAPKTCTLLEKFPETTGCR
RGQIKYSIMHPGTHVWPHTGPTNCRLRMHLGLVIPKEGCKIRCANETKTWEEGKVLIFDD
SFEHEVWQDASSFRLIFIVDVWHPELTPQQRRSLPAI
Target 8 Number of Residues 769
Target 8 Molecular Weight 85499
Target 8 Theoretical pI 4.67
Target 8 GO Classification
Function
binding
ion binding
cation binding
transition metal ion binding
iron ion 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
peptide-aspartate beta-dioxygenase activity
Process
physiological process
metabolism
macromolecule metabolism
biopolymer metabolism
biopolymer modification
protein modification
peptidyl-amino acid modification
Component
cell
membrane
intrinsic to membrane
intrinsic to organelle membrane
intrinsic to endoplasmic reticulum membrane
integral to endoplasmic reticulum membrane
Target 8 General Function Posttranslational modification, protein turnover, chaperones
Target 8 Specific Function Specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins
Target 8 Pathways Not Available
Target 8 Reactions
  • peptide-L-aspartate + 2-oxoglutarate + O2 = peptide-3-hydroxy-L-aspartate + succinate + CO2
Target 8 Pfam Domain Function
Target 8 Signals
  • None
Target 8 Transmembrane Regions
  • 55-75
Target 8 Essentiality Non-Essential
Target 8 GenBank ID Protein 458032 Link Image
Target 8 UniProtKB/Swiss-Prot ID Q12797 Link Image
Target 8 UniProtKB/Swiss-Prot Entry Name ASPH_HUMAN Link Image
Target 8 PDB ID Not Available
Target 8 Cellular Location
  • Endoplasmic reticulum
  • endoplasmic reticulum membrane
  • single-pass type II membrane protein
Target 8 Gene Sequence >2274 bp
ATGGCCCAGCGTAAGAATGCCAAGAGCAGCGGCAACAGCAGCAGCAGCGGCTCCGGCAGC
GGTAGCACGAGTGCGGGCAGCAGCAGCCCCGGGGCCCGGAGAGAGACAAAGCATGGAGGA
CACAAGAATGGGAGGAAAGGCGGACTCTCAGGAACTTCATTCTTCACGTGGTTTATGGTG
ATTGCATTGCTGGGCGTCTGGACATCTGTAGCTGTCGTTTGGTTTGATCTTGTTGACTAT
GAGGAAGTTCTAGGAAAACTAGGAATCTATGATGCTGATGGTGATGGAGATTTTGATGTG
GATGATGCCAAAGTTTTATTAGGACTTAAAGAGAGATCTACTTCAGAGCCAGCAGTCCCG
CCAGAAGAGGCTGAGCCACACACTGAGCCCGAGGAGCAGGTTCCTGTGGAGGCAGAACCC
CAGAATATCGAAGATGAAGCAAAAGAACAAATTCAGTCCCTTCTCCATGAAATGGTACAC
GCAGAACATGTTGAGGGAGAAGACTTGCAACAAGAAGATGGACCCACAGGAGAACCACAA
CAAGAGGATGATGAGTTTCTTATGGCGACTGATGTAGATGATAGATTTGAGACCCTGGAA
CCTGAAGTATCTCATGAAGAAACCGAGCATAGTTACCACGTGGAAGAGACAGTTTCACAA
GACTGTAATCAGGATATGGAAGAGATGATGTCTGAGCAGGAAAATCCAGATTCCAGTGAA
CCAGTAGTAGAAGATGAAAGATTGCACCATGATACAGATGATGTAACATACCAAGTCTAT
GAGGAACAAGCAGTATATGAACCTCTAGAAAATGAAGGGATAGAAATCACAGAAGTAACT
GCTCCCCCTGAGGATAATCCTGTAGAAGATTCACAGGTAATTGTAGAAGAAGTAAGCATT
TTTCCTGTGGAAGAACAGCAGGAAGTACCACCAGAAACAAATAGAAAAACAGATGATCCA
GAACAAAAAGCAAAAGTTAAGAAAAAGAAGCCTAAACTTTTAAATAAATTTGATAAGACT
ATTAAAGCTGAACTTGATGCTGCAGAAAAACTCCGTAAAAGGGGAAAAATTGAGGAAGCA
GTGAATGCATTTAAAGAACTAGTACGCAAATACCCTCAGAGTCCACGAGCAAGATATGGG
AAGGCGCAGTGTGAGGATGATTTGGCTGAGAAGAGGAGAAGTAATGAGGTGCTACGTGGA
GCCATCGAGACCTACCAAGAGGTGGCCAGCCTACCTGATGTCCCTGCAGACCTGCTGAAG
CTGAGTTTGAAGCGTCGCTCAGACAGGCAACAATTTCTAGGTCATATGAGAGGTTCCCTG
CTTACCCTGCAGAGATTAGTTCAACTATTTCCCAATGATACTTCCTTAAAAAATGACCTT
GGCGTGGGATACCTCTTGATAGGAGATAATGACAATGCAAAGAAAGTTTATGAAGAGGTG
CTGAGTGTGACACCTAATGATGGCTTTGCTAAAGTCCATTATGGCTTCATCCTGAAGGCA
CAGAACAAAATTGCTGAGAGCATCCCATATTTAAAGGAAGGAATAGAATCCGGAGATCCT
GGCACTGATGATGGGAGATTTTATTTCCACCTGGGGGATGCCATGCAGAGGGTTGGGAAC
AAAGAGGCATATAAGTGGTATGAGCTTGGGCACAAGAGAGGACACTTTGCATCTGTCTGG
CAACGCTCACTCATCAATGTGAATGGACTGAAAGCACAGCCTTGTGGCCCAAAAGAAACG
GGCTACACACAGTTAGTAAAGTCTTTAGAAAGAAACTGGAAGTTAATCCGAGATGAAGGC
CTTGCAGTGATGGATAAAGCCAAAGGTCTCTTCCTGCCTGAGGATGAAAACCTGAGGGAA
AAAGGGGACTGGAGCCAGTTCACGCTGTGGCAGCAAGGAAGAAGAAATGAAAATGCCTGC
AAAGGAGCTCCTAAAACCTGTACCTTACTAGAAAAGTTCCCCGAGACAACAGGATGCAGA
AGAGGACAGATCAAATATTCCATCATGCACCCCGGGACTCACGTGTGGCCGCACACAGGG
CCCACAAACTGCAGGCTCCGAATGCACCTGGGCTTGGTGATTCCCAAGGAAGGCTGCAAG
ATTCGATGTGCCAACGAGACCAAGACCTGGGAGGAAGGCAAGGTGCTCATCTTTGATGAC
TCCTTTGAGCACGAGGTATGGCAGGATGCCTCATCTTTCCGGCTGATATTCATCGTGGAT
GTGTGGCATCCGGAACTGACACCACAGCAGAGACGCAGCCTTCCAGCAATTTAG
Target 8 GenBank Gene ID
Target 8 GeneCard ID ASPH Link Image
Target 8 GenAtlas ID ASPH Link Image
Target 8 HGNC ID HGNC:757 Link Image
Target 8 Chromosome Location 8
Target 8 Locus 8q12.1
Target 8 SNPs SNPJam Report Link Image
Target 8 General References
  1. Korioth F, Gieffers C, Frey J: Cloning and characterization of the human gene encoding aspartyl beta-hydroxylase. Gene. 1994 Dec 15;150(2):395-9. [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 673
Target 9 Name Solute carrier family 13 member 3
Target 9 Synonyms
  1. Na(+)/dicarboxylate cotransporter 3
  2. NaDC-3
  3. Sodium-dependent high-affinity dicarboxylate transporter 2
  4. hNaDC3
Target 9 Gene Name SLC13A3
Target 9 Protein Sequence >Solute carrier family 13 member 3
MAALAAAAKKVWSARRLLVLLFTPLALLPVVFALPPKEGRCLFVILLMAVYWCTEALPLS
VTALLPIVLFPFMGILPSNKVCPQYFLDTNFLFLSGLIMASAIEEWNLHRRIALKILMLV
GVQPARLILGMMVTTSFLSMWLSNTASTAMMLPIANAILKSLFGQKEVRKDPSQESEENT
AAVRRNGLHTVPTEMQFLASTEAKDHPGETEVPLDLPADSRKEDEYRRNIWKGFLISIPY
SASIGGTATLTGTAPNLILLGQLKSFFPQCDVVNFGSWFIFAFPLMLLFLLAGWLWISFL
YGGLSFRGWRKNKSEIRTNAEDRARAVIREEYQNLGPIKFAEQAVFILFCMFAILLFTRD
PKFIPGWASLFNPGFLSDAVTGVAIVTILFFFPSQRPSLKWWFDFKAPNTETEPLLTWKK
AQETVPWNIILLLGGGFAMAKGCEESGLSVWIGGQLHPLENVPPALAVLLITVVIAFFTE
FASNTATIIIFLPVLAELAIRLRVHPLYLMIPGTVGCSFAFMLPVSTPPNSIAFASGHLL
VKDMVRTGLLMNLMGVLLLSLAMNTWAQTIFQLGTFPDWADMYSVNVTALPPTLANDTFR
TL
Target 9 Number of Residues 612
Target 9 Molecular Weight 66842
Target 9 Theoretical pI 8.47
Target 9 GO Classification
Function
transporter activity
Process
physiological process
cellular physiological process
transport
ion transport
cation transport
monovalent inorganic cation transport
sodium ion transport
Component
cell
membrane
Target 9 General Function Inorganic ion transport and metabolism
Target 9 Specific Function High-affinity sodium-dicarboxylate cotransporter that accepts a range of substrates with 4-5 carbon atoms. The stoichiometry is probably 3 Na(+) for 1 divalent succinate
Target 9 Pathways Not Available
Target 9 Reactions Not Available
Target 9 Pfam Domain Function
Target 9 Signals
  • None
Target 9 Transmembrane Regions
  • 17-37
  • 56-76
  • 83-103
  • 139-159
  • 230-250
  • 279-299
  • 337-357
  • 373-393
  • 462-482
  • 506-526
  • 547-567
Target 9 Essentiality Non-Essential
Target 9 GenBank ID Protein 8132324 Link Image
Target 9 UniProtKB/Swiss-Prot ID Q8WWT9 Link Image
Target 9 UniProtKB/Swiss-Prot Entry Name S13A3_HUMAN Link Image
Target 9 PDB ID Not Available
Target 9 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 9 Gene Sequence >1809 bp
ATGGCGGCGCTGGCAGCAGCGGCCAAGAAGGTGTGGAGCGCGCGGCGGCTGCTGGTGCTG
CTGTTCACGCCGCTCGCGCTGCTGCCGGTGGTCTTCGCCCTCCCGCCCAAGGAAGGCCGC
TGCTTGTTTGTCATCCTGCTCATGGCGGTGTACTGGTGCACGGAGGCCCTGCCGCTCTCA
GTGACGGCGCTGCTGCCCATCGTCCTCTTCCCCTTCATGGGCATCTTGCCCTCCAACAAG
GTCTGCCCCCAGTACTTCCTCGACACCAACTTCCTCTTCCTCAGTGGGCTGATCATGGCC
AGCGCCATTGAGGAGTGGAACCTGCACCGGCGAATCGCCCTCAAGATCCTGATGCTTGTT
GGAGTCCAGCCGGCCAGGCTCATCCTGGGGATGATGGTGACCACCTCGTTCTTGTCCATG
TGGCTGAGCAACACCGCCTCCACTGCCATGATGCTTCCAATTGCCAATGCCATCCTGAAA
AGTCTCTTTGGCCAGAAGGAGGTTCGAAAGGACCCCAGCCAGGAGAGTGAAGAGAACACA
GCTGCTGTGCGGAGAAACGGCTACACACTGTGCCCACGGAGATGCAGTTTCTCGCCAAGC
ACAGAAGCCAAAGACCACCCTGGGGAGACAGAGGTTCCACTGGATCTGCCGGCTGACTCC
AGGAAGGAGGATGAATATCGTCGGAACATCTGGAAGGGCTTCCTCATCTCCATCCCCTAC
TCAGCCAGTATTGGGGGCACAGCCACACTCACGGGCACAGCCCCTAACCTCATCCTGCTT
GGCCAGCTCAAGAGTTTCTTTCCGCAGTGTGACGTGGTGAATTTCGGCTCCTGGTTCATT
TTCGCCTTCCCTCTTATGCTGTTGTTCCTGTTGGCAGGCTGGCTCTGGATCTCCTTCCTG
TACGGGGGACTGAGCTTCAGGGGCTGGAGGAAGAATAAATCTGAGATAAGAACCAATGCA
GAAGATAGGGCTCGAGCTGTAATTCGGGAAGAATACCAGAACCTGGGGCCCATCAAGTTT
GCCGAACAGGCTGTTTTCATCCTTTTCTGCATGTTTGCCATCCTCCTCTTCACCCGGGAC
CCGAAGTTCATCCCTGGCTGGGCCAGCCTCTTCAATCCTGGGTTTCTTTCTGATGCTGTC
ACCGGCGTGGCTATTGTCACCATCTTGTTCTTCTTCCCGTCCCAAAGGCCCTCTCTCAAG
TGGTGGTTTGACTTCAAAGCTCCCAACACAGAGACAGAGCCCTTGCTGACCTGGAAGAAG
GCCCAGGAGACAGTGCCCTGGAACATCATCCTTCTCCTGGGAGGGGGCTTCGCCATGGCC
AAAGGCTGTGAGGAATCGGGGCTGTCTGTATGGATTGGTGGGCAGCTGCACCCCCTGGAG
AATGTGCCCCCCGCCCTGGCTGTGCTGCTCATCACTGTGGTCATCGCCTTCTTCACTGAG
TTTGCCAGCAACACGGCGACCATCATCATCTTCCTGCCGGTCCTGGCAGAGCTGGCCATC
CGCCTGAGAGTGCACCCCCTGTATCTGATGATTCCGGGCACAGTCGGCTGCTCCTTTGCC
TTCATGCTCCCGGTCTCAACGCCCCCCAACTCCATCGCCTTCGCCTCTGGACACTTGCTG
GTCAAAGACATGGTGCGGACAGGCCTCCTGATGAACCTGATGGGTGTCCTGCTGCTCAGT
TTGGCTATGAATACCTGGGCACAGACCATCTTCCAGCTGGGCACCTTCCCGGACTGGGCT
GATATGTACTCGGTCAATGTCACAGCATTGCCACCCACCTTGGCCAATGACACATTTCGG
ACCCTCTGA
Target 9 GenBank Gene ID
Target 9 GeneCard ID SLC13A3 Link Image
Target 9 GenAtlas ID SLC13A3 Link Image
Target 9 HGNC ID HGNC:14430 Link Image
Target 9 Chromosome Location 20
Target 9 Locus 20q12-q13.1
Target 9 SNPs SNPJam Report Link Image
Target 9 General References
  1. Wang H, Fei YJ, Kekuda R, Yang-Feng TL, Devoe LD, Leibach FH, Prasad PD, Ganapathy V: Structure, function, and genomic organization of human Na(+)-dependent high-affinity dicarboxylate transporter. Am J Physiol Cell Physiol. 2000 May;278(5):C1019-30. [PubMed Link Image]
  2. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
Target 9 Drug References
  1. Burckhardt BC, Lorenz J, Kobbe C, Burckhardt G: Substrate specificity of the human renal sodium dicarboxylate cotransporter, hNaDC-3, under voltage-clamp conditions. Am J Physiol Renal Physiol. 2005 Apr;288(4):F792-9. Epub 2004 Nov 23. [PubMed Link Image]
  2. Oshiro N, Pajor AM: Functional characterization of high-affinity Na(+)/dicarboxylate cotransporter found in Xenopus laevis kidney and heart. Am J Physiol Cell Physiol. 2005 Nov;289(5):C1159-68. Epub 2005 Jun 8. [PubMed Link Image]
  3. Yodoya E, Wada M, Shimada A, Katsukawa H, Okada N, Yamamoto A, Ganapathy V, Fujita T: Functional and molecular identification of sodium-coupled dicarboxylate transporters in rat primary cultured cerebrocortical astrocytes and neurons. J Neurochem. 2006 Apr;97(1):162-73. Epub 2006 Mar 8. [PubMed Link Image]
  4. Hagos Y, Steffgen J, Rizwan AN, Langheit D, Knoll A, Burckhardt G, Burckhardt BC: Functional roles of cationic amino acid residues in the sodium-dicarboxylate cotransporter 3 (NaDC-3) from winter flounder. Am J Physiol Renal Physiol. 2006 Dec;291(6):F1224-31. Epub 2006 May 30. [PubMed Link Image]
  5. Wolff NA, Burckhardt BC, Burckhardt G, Oellerich M, Armstrong VW: Mycophenolic acid (MPA) and its glucuronide metabolites interact with transport systems responsible for excretion of organic anions in the basolateral membrane of the human kidney. Nephrol Dial Transplant. 2007 Sep;22(9):2497-503. Epub 2007 May 25. [PubMed Link Image]
Drug Target 10 [top]
Target 10 ID 1410
Target 10 Name Oxidoreductase
Target 10 Synonyms
  1. 3- hydroxysteroid epimerase
  2. Hydroxysteroid (17-beta
Target 10 Gene Name HSD17B6
Target 10 Protein Sequence >Oxidoreductase
MWLYLAAFVGLYYLLHWYRERQVVSHLQDKYVFITGCDSGFGNLLARQLDARGLRVLAAC
LTEKGAEQLRGQTSDRLETVTLDVTKMESIAAATQWVKEHVGDRGLWGLVNNAGILTPIT
LCEWLNTEDSMNMLKVNLIGVIQVTLSMLPLVRRARGRIVNVSSILGRVAFFVGGYCVSK
YGVEAFSDILRREIQHFGVKISIVEPGYFRTGMTNMTQSLERMKQSWKEAPKHIKETYGQ
QYFDALYNIMKEGLLNCSTNLNLVTDCMEHALTSVHPRTRYSAGWDAKFFFIPLSYLPTS
LADYILTRSWPKPAQAV
Target 10 Number of Residues 322
Target 10 Molecular Weight 35966
Target 10 Theoretical pI 8.91
Target 10 GO Classification
Function
catalytic activity
oxidoreductase activity
Process
physiological process
metabolism
Component
Not Available
Target 10 General Function Lipid transport and metabolism
Target 10 Specific Function Not Available
Target 10 Pathways Not Available
Target 10 Reactions Not Available
Target 10 Pfam Domain Function
Target 10 Signals
  • None
Target 10 Transmembrane Regions
  • None
Target 10 Essentiality Non-Essential
Target 10 GenBank ID Protein 2338748 Link Image
Target 10 UniProtKB/Swiss-Prot ID O14756 Link Image
Target 10 UniProtKB/Swiss-Prot Entry Name O14756_HUMAN Link Image
Target 10 PDB ID Not Available
Target 10 Cellular Location Not Available
Target 10 Gene Sequence >954 bp
ATGTGGCTCTACCTGGCAGCCTTCGTGGGCCTGTACTACCTTCTGCACTGGTACCGGGAG
AGGCAGGTGGTGAGCCACCTCCAAGACAAGTATGTCTTTATCACGGGCTGTGACTCGGGC
TTTGGGAACCTACTGGCCAGACAGCTGGATGCACGAGGCTTGAGAGTGCTGGCTGCGTGT
CTGACGGAGAAGGGGGCCGAGCAGCTGAGGGGCCAGACGTCTGACAGGCTGGAGACGGTG
ACCCTGGATGTTACCAAGATGGAGAGCATCGCTGCAGCTACTCAGTGGGTGAAGGAGCAT
GTGGGGGACAGAGGACTCTGGGGACTGGTGAACAATGCAGGCATTCTTACACCAATTACC
TTATGTGAGTGGCTGAACACTGAGGACTCTATGAATATGCTCAAAGTGAACCTCATTGGT
GTGATCCAGGTGACCTTGAGCATGCTTCCTTTGGTGAGGAGAGCACGGGGAAGAATTGTC
AATGTCTCCAGCATTCTGGGAAGAGTTGCTTTCTTTGTAGGAGGCTACTGTGTCTCCAAG
TATGGAGTGGAAGCCTTTTCAGATATTCTGAGGCGTGAGATTCAACATTTTGGGGTGAAA
ATCAGCATAGTTGAACCTGGCTACTTCAGAACGGGAATGACAAACATGACACAGTCCTTA
GAGCGAATGAAGCAAAGTTGGAAAGAAGCCCCCAAGCATATTAAGGAGACCTATGGACAG
CAGTATTTTGATGCCCTTTACAATATCATGAAGGAAGGGCTGTTGAATTGTAGCACAAAC
CTGAACCTGGTCACTGACTGCATGGAACATGCTCTGACATCGGTGCATCCGCGAACTCGA
TATTCAGCTGGCTGGGATGCTAAATTTTTCTTCATCCCTCTATCTTATTTACCTACATCA
CTGGCAGACTACATTTTGACTAGATCTTGGCCCAAACCAGCCCAGGCAGTCTAA
Target 10 GenBank Gene ID
Target 10 GeneCard ID HSD17B6 Link Image
Target 10 GenAtlas ID HSD17B6 Link Image
Target 10 HGNC ID HGNC:23316 Link Image
Target 10 Chromosome Location 12
Target 10 Locus 12q13
Target 10 SNPs SNPJam Report Link Image
Target 10 General References
  1. Huang XF, Luu-The V: Molecular characterization of a first human 3(alpha-->beta)-hydroxysteroid epimerase. J Biol Chem. 2000 Sep 22;275(38):29452-7. [PubMed Link Image]
  2. Chetyrkin SV, Hu J, Gough WH, Dumaual N, Kedishvili NY: Further characterization of human microsomal 3alpha-hydroxysteroid dehydrogenase. Arch Biochem Biophys. 2001 Feb 1;386(1):1-10. [PubMed Link Image]
  3. 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]
  4. Biswas MG, Russell DW: Expression cloning and characterization of oxidative 17beta- and 3alpha-hydroxysteroid dehydrogenases from rat and human prostate. J Biol Chem. 1997 Jun 20;272(25):15959-66. [PubMed Link Image]
Target 10 Drug References
  1. Goel HC, Gupta D, Gupta S, Garg AP, Bala M: Protection of mitochondrial system by Hippophae rhamnoides L. against radiation-induced oxidative damage in mice. J Pharm Pharmacol. 2005 Jan;57(1):135-43. [PubMed Link Image]
  2. Gupta D, Arora R, Garg AP, Bala M, Goel HC: Modification of radiation damage to mitochondrial system in vivo by Podophyllum hexandrum: mechanistic aspects. Mol Cell Biochem. 2004 Nov;266(1-2):65-77. [PubMed Link Image]
  3. Dudkina NV, Eubel H, Keegstra W, Boekema EJ, Braun HP: Structure of a mitochondrial supercomplex formed by respiratory-chain complexes I and III. Proc Natl Acad Sci U S A. 2005 Mar 1;102(9):3225-9. Epub 2005 Feb 15. [PubMed Link Image]
  4. Huang LS, Sun G, Cobessi D, Wang AC, Shen JT, Tung EY, Anderson VE, Berry EA: 3-nitropropionic acid is a suicide inhibitor of mitochondrial respiration that, upon oxidation by complex II, forms a covalent adduct with a catalytic base arginine in the active site of the enzyme. J Biol Chem. 2006 Mar 3;281(9):5965-72. Epub 2005 Dec 21. [PubMed Link Image]
  5. Bayley JP, van Minderhout I, Weiss MM, Jansen JC, Oomen PH, Menko FH, Pasini B, Ferrando B, Wong N, Alpert LC, Williams R, Blair E, Devilee P, Taschner PE: Mutation analysis of SDHB and SDHC: novel germline mutations in sporadic head and neck paraganglioma and familial paraganglioma and/or pheochromocytoma. BMC Med Genet. 2006 Jan 11;7:1. [PubMed Link Image]
Drug Target 11 [top]
Target 11 ID 3938
Target 11 Name Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3
Target 11 Synonyms
  1. EC 1.14.11.4
  2. LH3
  3. Lysyl hydroxylase 3
  4. Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 precursor
Target 11 Gene Name PLOD3
Target 11 Protein Sequence >Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3
MTSSGPGPRFLLLLPLLLPPAASASDRPRGRDPVNPEKLLVITVATAETEGYLRFLRSAE
FFNYTVRTLGLGEEWRGGDVARTVGGGQKVRWLKKEMEKYADREDMIIMFVDSYDVILAG
SPTELLKKFVQSGSRLLFSAESFCWPEWGLAEQYPEVGTGKRFLNSGGFIGFATTIHQIV
RQWKYKDDDDDQLFYTRLYLDPGLREKLSLNLDHKSRIFQNLNGALDEVVLKFDRNRVRI
RNVAYDTLPIVVHGNGPTKLQLNYLGNYVPNGWTPEGGCGFCNQDRRTLPGGQPPPRVFL
AVFVEQPTPFLPRFLQRLLLLDYPPDRVTLFLHNNEVFHEPHIADSWPQLQDHFSAVKLV
GPEEALSPGEARDMAMDLCRQDPECEFYFSLDADAVLTNLQTLRILIEENRKVIAPMLSR
HGKLWSNFWGALSPDEYYARSEDYVELVQRKRVGVWNVPYISQAYVIRGDTLRMELPQRD
VFSGSDTDPDMAFCKSFRDKGIFLHLSNQHEFGRLLATSRYDTEHLHPDLWQIFDNPVDW
KEQYIHENYSRALEGEGIVEQPCPDVYWFPLLSEQMCDELVAEMEHYGQWSGGRHEDSRL
AGGYENVPTVDIHMKQVGYEDQWLQLLRTYVGPMTESLFPGYHTKARAVMNFVVRYRPDE
QPSLRPHHDSSTFTLNVALNHKGLDYEGGGCRFLRYDCVISSPRKGWALLHPGRLTHYHE
GLPTTWGTRYIMVSFVDP
Target 11 Number of Residues 750
Target 11 Molecular Weight 84786
Target 11 Theoretical pI 5.95
Target 11 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 11 General Function Not Available
Target 11 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 11 Pathways
Name SMPDB Link KEGG Link
Lysine degradation SMP00037 Link Image map00310 Link Image
Target 11 Reactions
  • procollagen L-lysine + 2-oxoglutarate + O2 = procollagen 5-hydroxy-L-lysine + succinate + CO2 ALL_REAC (other) R03376
Target 11 Pfam Domain Function
Target 11 Signals
  • 1-24
Target 11 Transmembrane Regions
  • None
Target 11 Essentiality Non-Essential
Target 11 GenBank ID Protein 3153235 Link Image
Target 11 UniProtKB/Swiss-Prot ID O60568 Link Image
Target 11 UniProtKB/Swiss-Prot Entry Name PLOD3_HUMAN Link Image
Target 11 PDB ID Not Available
Target 11 Cellular Location
  • Endoplasmic reticulum
Target 11 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 11 GenBank Gene ID
Target 11 GeneCard ID PLOD3 Link Image
Target 11 GenAtlas ID PLOD3 Link Image
Target 11 HGNC ID HGNC:9083 Link Image
Target 11 Chromosome Location 7
Target 11 Locus 7q22
Target 11 SNPs SNPJam Report Link Image
Target 11 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 11 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 12 [top]
Target 12 ID 3940
Target 12 Name Gamma-butyrobetaine dioxygenase
Target 12 Synonyms
  1. EC 1.14.11.1
  2. Gamma- BBH
  3. Gamma-butyrobetaine hydroxylase
  4. Gamma-butyrobetaine,2- oxoglutarate dioxygenase
Target 12 Gene Name BBOX1
Target 12 Protein Sequence >Gamma-butyrobetaine dioxygenase
MACTIQKAEALDGAHLMQILWYDEEESLYPAVWLRDNCPCSDCYLDSAKARKLLVEALDV
NIGIKGLIFDRKKVYITWPDEHYSEFQADWLKKRCFSKQARAKLQRELFFPECQYWGSEL
QLPTLDFEDVLRYDEHAYKWLSTLKKVGIVRLTGASDKPGEVSKLGKRMGFLYLTFYGHT
WQVQDKIDANNVAYTTGKLSFHTDYPALHHPPGVQLLHCIKQTVTGGDSEIVDGFNVCQK
LKKNNPQAFQILSSTFVDFTDIGVDYCDFSVQSKHKIIELDDKGQVVRINFNNATRDTIF
DVPVERVQPFYAALKEFVDLMNSKESKFTFKMNPGDVITFDNWRLLHGRRSYEAGTEISR
HLEGAYADWDVVMSRLRILRQRVENGN
Target 12 Number of Residues 393
Target 12 Molecular Weight 44715
Target 12 Theoretical pI 6.73
Target 12 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 12 General Function Not Available
Target 12 Specific Function Catalyzes the formation of L-carnitine from gamma- butyrobetaine
Target 12 Pathways
Name SMPDB Link KEGG Link
Lysine degradation SMP00037 Link Image map00310 Link Image
Target 12 Reactions
  • 4-trimethylammoniobutanoate + 2-oxoglutarate + O2 = 3-hydroxy-4-trimethylammoniobutanoate + succinate + CO2
Target 12 Pfam Domain Function
Target 12 Signals
  • None
Target 12 Transmembrane Regions
  • None
Target 12 Essentiality Non-Essential
Target 12 GenBank ID Protein 3746805 Link Image
Target 12 UniProtKB/Swiss-Prot ID O75936 Link Image
Target 12 UniProtKB/Swiss-Prot Entry Name BODG_HUMAN Link Image
Target 12 PDB ID Not Available
Target 12 Cellular Location
  • Cytoplasm
Target 12 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 12 GenBank Gene ID
Target 12 GeneCard ID BBOX1 Link Image
Target 12 GenAtlas ID BBOX1 Link Image
Target 12 HGNC ID HGNC:964 Link Image
Target 12 Chromosome Location 11
Target 12 Locus 11p14.2
Target 12 SNPs SNPJam Report Link Image
Target 12 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 12 Drug References
  1. Yoshisue K, Yamamoto Y, Yoshida K, Saeki M, Minami Y, Esumi Y, Kawaguchi Y: Pharmacokinetics and biological fate of 3-(2,2, 2-trimethylhydrazinium)propionate dihydrate (MET-88), a novel cardioprotective agent, in rats. Drug Metab Dispos. 2000 Jun;28(6):687-94. [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]
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 3949
Target 14 Name Prolyl 3-hydroxylase 2
Target 14 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 14 Gene Name LEPREL1
Target 14 Protein Sequence >Prolyl 3-hydroxylase 2
MRERIWAPPLLLLLPLLLPPPLWGGPPDSPRRELELEPGPLQPFDLLYASGAAAYYSGDY
ERAVRDLEAALRSHRRLREIRTRCARHCAARHPLPPPPPGEGPGAELPLFRSLLGRARCY
RSCETQRLGGPASRHRVSEDVRSDFQRRVPYNYLQRAYIKLNQLEKAVEAAHTFFVANPE
HMEMQQNIENYRATAGVEALQLVDREAKPHMESYNAGVKHYEADDFEMAIRHFEQALREY
FVEDTECRTLCEGPQRFEEYEYLGYKAGLYEAIADHYMQVLVCQHECVRELATRPGRLSP
IENFLPLHYDYLQFAYYRVGEYVKALECAKAYLLCHPDDEDVLDNVDYYESLLDDSIDPA
SIEAREDLTMFVKRHKLESELIKSAAEGLGFSYTEPNYWIRYGGRQDENRVPSGVNVEGA
EVHGFSMGKKLSPKIDRDLREGGPLLYENITFVYNSEQLNGTQRVLLDNVLSEEQCRELH
SVASGIMLVGDGYRGKTSPHTPNEKFEGATVLKALKSGYEGRVPLKSARLFYDISEKARR
IVESYFMLNSTLYFSYTHMVCRTALSGQQDRRNDLSHPIHADNCLLDPEANECWKEPPAY
TFRDYSALLYMNDDFEGGEFIFTEMDAKTVTASIKPKCGRMISFSSGGENPHGVKAVTKG
KRCAVALWFTLDPLYRELERIQADEVIAILDQEQQGKHELNINPKDEL
Target 14 Number of Residues 719
Target 14 Molecular Weight 80985
Target 14 Theoretical pI 5.47
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 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 14 Pathways Not Available
Target 14 Reactions
  • procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-3-hydroxy-L-proline + succinate + CO2
Target 14 Pfam Domain Function
Target 14 Signals
  • 1-24
Target 14 Transmembrane Regions
  • None
Target 14 Essentiality Non-Essential
Target 14 GenBank ID Protein 27526730 Link Image
Target 14 UniProtKB/Swiss-Prot ID Q8IVL5 Link Image
Target 14 UniProtKB/Swiss-Prot Entry Name P3H2_HUMAN Link Image
Target 14 PDB ID Not Available
Target 14 Cellular Location
  • Endoplasmic reticulum
Target 14 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 14 GenBank Gene ID
Target 14 GeneCard ID LEPREL1 Link Image
Target 14 GenAtlas ID LEPREL1 Link Image
Target 14 HGNC ID HGNC:19317 Link Image
Target 14 Chromosome Location 3
Target 14 Locus 3q28
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 3951
Target 15 Name Prolyl 3-hydroxylase 3
Target 15 Synonyms
  1. EC 1.14.11.7
  2. Leprecan-like protein 2
  3. Prolyl 3-hydroxylase 3 precursor
  4. Protein B
Target 15 Gene Name LEPREL2
Target 15 Protein Sequence >Prolyl 3-hydroxylase 3
MLRLLRPLLLLLLLPPPGSPEPPGLTQLSPGAPPQAPDLLYADGLRAYAAGAWAPAVALL
REALRSQAALGRVRLDCGASCAADPGAALPAVLLGAPEPDSGPGPTQGSWERQLLRAALR
RADCLTQCAARRLGPGGAARLRVGSALRDAFRRREPYNYLQRAYYQLKKLDLAAAAAHTF
FVANPMHLQMREDMAKYRRMSGVRPQSFRDLETPPHWAAYDTGLELLGRQEAGLALPRLE
EALQGSLAQMESCRADCEGPEEQQGAEEEEDGAASQGGLYEAIAGHWIQVLQCRQRCVGE
TATRPGRSFPVPDFLPNQLRRLHEAHAQVGNLSQAIENVLSVLLFYPEDEAAKRALNQYQ
AQLGEPRPGLGPREDIQRFILRSLGEKRQLYYAMEHLGTSFKDPDPWTPAALIPEALREK
LREDQEKRPWDHEPVKPKPLTYWKDVLLLEGVTLTQDSRQLNGSERAVLDGLLTPAECGV
LLQLAKDAAGAGARSGYRGRRSPHTPHERFEGLTVLKAAQLARAGTVGSQGAKLLLEVSE
RVRTLTQAYFSPERPLHLSFTHLVCRSAIEGEQEQRMDLSHPVHADNCVLDPDTGECWRE
PPAYTYRDYSGLLYLNDDFQGGDLFFTEPNALTVTARVRPRCGRLVAFSSGVENPHGVWA
VTRGRRCALALWHTWAPEHREQEWIEAKELLQESQEEEEEEEEEMPSKDPSPEPPSRRHQ
RVQDKTGRAPRVREEL
Target 15 Number of Residues 748
Target 15 Molecular Weight 81837
Target 15 Theoretical pI 6.26
Target 15 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 15 General Function Not Available
Target 15 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 15 Pathways Not Available
Target 15 Reactions
  • procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-3-hydroxy-L-proline + succinate + CO2
Target 15 Pfam Domain Function
Target 15 Signals
  • 1-20
Target 15 Transmembrane Regions
  • None
Target 15 Essentiality Non-Essential
Target 15 GenBank ID Protein 1200503 Link Image
Target 15 UniProtKB/Swiss-Prot ID Q8IVL6 Link Image
Target 15 UniProtKB/Swiss-Prot Entry Name P3H3_HUMAN Link Image
Target 15 PDB ID Not Available
Target 15 Cellular Location
  • Endoplasmic reticulum
Target 15 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 15 GenBank Gene ID
Target 15 GeneCard ID LEPREL2 Link Image
Target 15 GenAtlas ID LEPREL2 Link Image
Target 15 HGNC ID HGNC:19318 Link Image
Target 15 Chromosome Location 12
Target 15 Locus 12q13
Target 15 SNPs SNPJam Report Link Image
Target 15 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 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 3964
Target 16 Name Trimethyllysine dioxygenase, mitochondrial
Target 16 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 16 Gene Name TMLHE
Target 16 Protein Sequence >Trimethyllysine dioxygenase, mitochondrial
MWYHRLSHLHSRLQDLLKGGVIYPALPQPNFKSLLPLAVHWHHTASKSLTCAWQQHEDHF
ELKYANTVMRFDYVWLRDHCRSASCYNSKTHQRSLDTASVDLCIKPKTIRLDETTLFFTW
PDGHVTKYDLNWLVKNSYEGQKQKVIQPRILWNAEIYQQAQVPSVDCQSFLETNEGLKKF
LQNFLLYGIAFVENVPPTQEHTEKLAERISLIRETIYGRMWYFTSDFSRGDTAYTKLALD
RHTDTTYFQEPCGIQVFHCLKHEGTGGRTLLVDGFYAAEQVLQKAPEEFELLSKVPLKHE
YIEDVGECHNHMIGIGPVLNIYPWNKELYLIRYNNYDRAVINTVPYDVVHRWYTAHRTLT
IELRRPENEFWVKLKPGRVLFIDNWRVLHGRECFTGYRQLCGCYLTRDDVLNTARLLGLQ
A
Target 16 Number of Residues 428
Target 16 Molecular Weight 49518
Target 16 Theoretical pI 7.79
Target 16 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 16 General Function Secondary metabolites biosynthesis, transport and catabolism
Target 16 Specific Function Converts trimethyllysine (TML) into hydroxytrimethyllysine (HTML)
Target 16 Pathways
Name SMPDB Link KEGG Link
Lysine degradation SMP00037 Link Image map00310 Link Image
Target 16 Reactions
  • N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2 = 3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
Target 16 Pfam Domain Function
Target 16 Signals
  • None
Target 16 Transmembrane Regions
  • None
Target 16 Essentiality Non-Essential
Target 16 GenBank ID Protein 15553435 Link Image
Target 16 UniProtKB/Swiss-Prot ID Q9NVH6 Link Image
Target 16 UniProtKB/Swiss-Prot Entry Name TMLH_HUMAN Link Image
Target 16 PDB ID Not Available
Target 16 Cellular Location
  • Mitochondrion
Target 16 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 16 GenBank Gene ID
Target 16 GeneCard ID TMLHE Link Image
Target 16 GenAtlas ID TMLHE Link Image
Target 16 HGNC ID HGNC:18308 Link Image
Target 16 Chromosome Location X
Target 16 Locus Xq28
Target 16 SNPs SNPJam Report Link Image
Target 16 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 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 3999
Target 17 Name Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial
Target 17 Synonyms
  1. CII-4
  2. CybS
  3. QPs3
  4. Succinate dehydrogenase complex subunit D
  5. Succinate dehydrogenase cytochrome b small subunit, mitochondrial precursor
  6. Succinate-ubiquinone oxidoreductase cytochrome b small subunit
  7. Succinate-ubiquinone reductase membrane anchor subunit
Target 17 Gene Name SDHD
Target 17 Protein Sequence >Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial
MAVLWRLSAVCGALGGRALLLRTPVVRPAHISAFLQDRPIPEWCGVQHIHLSPSHHSGSK
AASLHWTSERVVSVLLLGLLPAAYLNPCSAMDYSLAAALTLHGHWGLGQVVTDYVHGDAL
QKAAKAGLLALSALTFAGLCYFNYHDVGICKAVAMLWKL
Target 17 Number of Residues 161
Target 17 Molecular Weight 17043
Target 17 Theoretical pI 8.75
Target 17 GO Classification
Function
binding
tetrapyrrole binding
heme binding
Process
electron transport
physiological process
metabolism
cellular metabolism
generation of precursor metabolites and energy
energy derivation by oxidation of organic compounds
main pathways of carbohydrate metabolism
tricarboxylic acid cycle
Component
cell
membrane
intrinsic to membrane
integral to membrane
envelope
organelle envelope
mitochondrial envelope
Target 17 General Function Not Available
Target 17 Specific Function Not Available
Target 17 Pathways Not Available
Target 17 Reactions Not Available
Target 17 Pfam Domain Function
Target 17 Signals
  • None
Target 17 Transmembrane Regions
  • 71-91
  • 126-142
Target 17 Essentiality Non-Essential
Target 17 GenBank ID Protein 2351037 Link Image
Target 17 UniProtKB/Swiss-Prot ID O14521 Link Image
Target 17 UniProtKB/Swiss-Prot Entry Name DHSD_HUMAN Link Image
Target 17 PDB ID Not Available
Target 17 Cellular Location
  • Mitochondrion
Target 17 Gene Sequence >480 bp
ATGGCGGTTCTCTGGAGGCTGAGTGCCGTTTGCGGTGCCCTAGGAGGCCGAGCTCTGTTG
CTTCGAACTCCAGTGGTCAGACCTGCTCATATCTCAGCATTTCTTCAGGACCGACCTATC
CCAGAATGGTGTGGAGTGCAGCACATACACTTGTCACCGAGCCACCATTCTGGCTCCAAG
GCTGCATCTCTCCACTGGACTAGCGAGAGGGTTGTCAGTGTTTTGCTCCTGGGTCTGCTT
CCGGCTGCTTATTTGAATCCTTGCTCTGCGATGGACTATTCCCTGGCTGCAGCCCTCACT
CTTCATGGTCACTGGGGCCTTGGACAAGTTGTTACTGACTATGTTCATGGGGATGCCTTG
CAGAAAGCTGCCAAGGCAGGGCTTTTGGCACTTTCAGCTTTAACCTTTGCTGGGCTTTGC
TATTTCAACTATCACGATGTGGGCATCTGCAAAGCTGTTGCCATGCTGTGGAAGCTCTGA
Target 17 GenBank Gene ID
Target 17 GeneCard ID SDHD Link Image
Target 17 GenAtlas ID SDHD Link Image
Target 17 HGNC ID HGNC:10683 Link Image
Target 17 Chromosome Location 11
Target 17 Locus 11q23
Target 17 SNPs SNPJam Report Link Image
Target 17 General References
  1. Baysal BE, Ferrell RE, Willett-Brozick JE, Lawrence EC, Myssiorek D, Bosch A, van der Mey A, Taschner PE, Rubinstein WS, Myers EN, Richard CW 3rd, Cornelisse CJ, Devilee P, Devlin B: Mutations in SDHD, a mitochondrial complex II gene, in hereditary paraganglioma. Science. 2000 Feb 4;287(5454):848-51. [PubMed Link Image]
  2. Gimm O, Armanios M, Dziema H, Neumann HP, Eng C: Somatic and occult germ-line mutations in SDHD, a mitochondrial complex II gene, in nonfamilial pheochromocytoma. Cancer Res. 2000 Dec 15;60(24):6822-5. [PubMed Link Image]
  3. Milunsky JM, Maher TA, Michels VV, Milunsky A: Novel mutations and the emergence of a common mutation in the SDHD gene causing familial paraganglioma. Am J Med Genet. 2001 May 15;100(4):311-4. [PubMed Link Image]
  4. Badenhop RF, Cherian S, Lord RS, Baysal BE, Taschner PE, Schofield PR: Novel mutations in the SDHD gene in pedigrees with familial carotid body paraganglioma and sensorineural hearing loss. Genes Chromosomes Cancer. 2001 Jul;31(3):255-63. [PubMed Link Image]
  5. Taschner PE, Jansen JC, Baysal BE, Bosch A, Rosenberg EH, Brocker-Vriends AH, van Der Mey AG, van Ommen GJ, Cornelisse CJ, Devilee P: Nearly all hereditary paragangliomas in the Netherlands are caused by two founder mutations in the SDHD gene. Genes Chromosomes Cancer. 2001 Jul;31(3):274-81. [PubMed Link Image]
  6. Masuoka J, Brandner S, Paulus W, Soffer D, Vital A, Chimelli L, Jouvet A, Yonekawa Y, Kleihues P, Ohgaki H: Germline SDHD mutation in paraganglioma of the spinal cord. Oncogene. 2001 Aug 16;20(36):5084-6. [PubMed Link Image]
  7. Hirawake H, Taniwaki M, Tamura A, Kojima S, Kita K: Cytochrome b in human complex II (succinate-ubiquinone oxidoreductase): cDNA cloning of the components in liver mitochondria and chromosome assignment of the genes for the large (SDHC) and small (SDHD) subunits to 1q21 and 11q23. Cytogenet Cell Genet. 1997;79(1-2):132-8. [PubMed Link Image]
Target 17 Drug References
  1. Sun F, Huo X, Zhai Y, Wang A, Xu J, Su D, Bartlam M, Rao Z: Crystal structure of mitochondrial respiratory membrane protein complex II. Cell. 2005 Jul 1;121(7):1043-57. [PubMed Link Image]
  2. Bayley JP, Devilee P, Taschner PE: The SDH mutation database: an online resource for succinate dehydrogenase sequence variants involved in pheochromocytoma, paraganglioma and mitochondrial complex II deficiency. BMC Med Genet. 2005 Nov 16;6:39. [PubMed Link Image]
  3. Brink I, Schaefer O, Walz M, Neumann HP: Fluorine-18 DOPA PET imaging of paraganglioma syndrome. Clin Nucl Med. 2006 Jan;31(1):39-41. [PubMed Link Image]
  4. Bayley JP, van Minderhout I, Weiss MM, Jansen JC, Oomen PH, Menko FH, Pasini B, Ferrando B, Wong N, Alpert LC, Williams R, Blair E, Devilee P, Taschner PE: Mutation analysis of SDHB and SDHC: novel germline mutations in sporadic head and neck paraganglioma and familial paraganglioma and/or pheochromocytoma. BMC Med Genet. 2006 Jan 11;7:1. [PubMed Link Image]
  5. Lehtonen HJ, Makinen MJ, Kiuru M, Laiho P, Herva R, van Minderhout I, Hogendoorn PC, Cornelisse C, Devilee P, Launonen V, Aaltonen LA: Increased HIF1 alpha in SDH and FH deficient tumors does not cause microsatellite instability. Int J Cancer. 2007 Sep 15;121(6):1386-9. [PubMed Link Image]
Drug Target 18 [top]
Target 18 ID 4000
Target 18 Name Prolyl 4-hydroxylase subunit alpha-2
Target 18 Synonyms
  1. 4-PH alpha-2
  2. EC 1.14.11.2
  3. Procollagen-proline,2-oxoglutarate-4-dioxygenase alpha-2 subunit
  4. Prolyl 4-hydroxylase subunit alpha-2 precursor
Target 18 Gene Name P4HA2
Target 18 Protein Sequence >Prolyl 4-hydroxylase subunit alpha-2
MKLWVSALLMAWFGVLSCVQAEFFTSIGHMTDLIYAEKELVQSLKEYILVEEAKLSKIKS
WANKMEALTSKSAADAEGYLAHPVNAYKLVKRLNTDWPALEDLVLQDSAAGFIANLSVQR
QFFPTDEDEIGAAKALMRLQDTYRLDPGTISRGELPGTKYQAMLSVDDCFGMGRSAYNEG
DYYHTVLWMEQVLKQLDAGEEATTTKSQVLDYLSYAVFQLGDLHRALELTRRLLSLDPSH
ERAGGNLRYFEQLLEEEREKTLTNQTEAELATPEGIYERPVDYLPERDVYESLCRGEGVK
LTPRRQKRLFCRYHHGNRAPQLLIAPFKEEDEWDSPHIVRYYDVMSDEEIERIKEIAKPK
LARATVRDPKTGVLTVASYRVSKSSWLEEDDDPVVARVNRRMQHITGLTVKTAELLQVAN
YGVGGQYEPHFDFSRNDERDTFKHLGTGNRVATFLNYMSDVEAGGATVFPDLGAAIWPKK
GTAVFWYNLLRSGEGDYRTRHAACPVLVGCKWVSNKWFHERGQEFLRPCGSTEVD
Target 18 Number of Residues 543
Target 18 Molecular Weight 60903
Target 18 Theoretical pI 5.43
Target 18 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 18 General Function Not Available
Target 18 Specific Function Catalyzes the posttranslational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins
Target 18 Pathways
Name SMPDB Link KEGG Link
Arginine and proline metabolism SMP00020 Link Image map00330 Link Image
Target 18 Reactions
  • procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2
Target 18 Pfam Domain Function
Target 18 Signals
  • 1-21
Target 18 Transmembrane Regions
  • None
Target 18 Essentiality Non-Essential
Target 18 GenBank ID Protein 2439985 Link Image
Target 18 UniProtKB/Swiss-Prot ID O15460 Link Image
Target 18 UniProtKB/Swiss-Prot Entry Name P4HA2_HUMAN Link Image
Target 18 PDB ID Not Available
Target 18 Cellular Location
  • Endoplasmic reticulum
Target 18 Gene Sequence >1608 bp
ATGAAACTCTGGGTGTCTGCATTGCTGATGGCCTGGTTTGGTGTCCTGAGCTGTGTGCAG
GCCGAATTCTTCACCTCTATTGGGCACATGACTGACCTGATTTATGCAGAGAAAGAGCTG
GTGCAGTCTCTGAAAGAGTACATCCTTGTGGAGGAAGCCAAGCTTTCCAAGATTAAGAGC
TGGGCCAACAAAATGGAAGCCTTGACTAGCAAGTCAGCTGCTGATGCTGAGGGCTACCTG
GCTCACCCTGTGAATGCCTACAAACTGGTGAAGCGGCTAAACACAGACTGGCCTGCGCTG
GAGGACCTTGTCCTGCAGGACTCAGCTGCAGGTTTTATCGCCAACCTCTCTGTGCAGCGG
CAGTTCTTCCCCACTGATGAGGACGAGATAGGAGCTGCCAAAGCCCTGATGAGACTTCAG
GACACATACAGGCTGGACCCAGGCACAATTTCCAGAGGGGAACTTCCAGGAACCAAGTAC
CAGGCAATGCTGAGTGTGGATGACTGCTTTGGGATGGGCCGCTCGGCCTACAATGAAGGG
GACTATTATCATACGGTGTTGTGGATGGAGCAGGTGCTAAAGCAGCTTGATGCCGGGGAG
GAGGCCACCACAACCAAGTCACAGGTGCTGGACTACCTCAGCTATGCTGTCTTCCAGTTG
GGTGATCTGCACCGTGCCCTGGAGCTCACCCGCCGCCTGCTCTCCCTTGACCCAAGCCAC
GAACGAGCTGGAGGGAATCTGCGGTACTTTGAGCAGTTATTGGAGGAAGAGAGAGAAAAA
ACGTTAACAAATCAGACAGAAGCTGAGCTAGCAACCCCAGAAGGCATCTATGAGAGGCCT
GTGGACTACCTGCCTGAGAGGGATGTTTACGAGAGCCTCTGTCGTGGGGAGGGTGTCAAA
CTGACACCCCGTAGACAGAAGAGGCTTTTCTGTAGGTACCACCATGGCAACAGGGCCCCA
CAGCTGCTCATTGCCCCCTTCAAAGAGGAGGACGAGTGGGACAGCCCGCACATCGTCAGG
TACTACGATGTCATGTCTGATGAGGAAATCGAGAGGATCAAGGAGATCGCAAAACCTAAA
CTTGCACGAGCCACCGTTCGTGATCCCAAGACAGGAGTCCTCACTGTCGCCAGCTACCGG
GTTTCCAAAAGCTCCTGGCTAGAGGAAGATGATGACCCTGTTGTGGCCCGAGTAAATCGT
CGGATGCAGCATATCACAGGGTTAACAGTAAAGACTGCAGAATTGTTACAGGTTGCAAAT
TATGGAGTGGGAGGACAGTATGAACCGCACTTCGACTTCTCTAGGAATGATGAGCGAGAT
ACTTTCAAGCATTTAGGGACGGGGAATCGTGTGGCTACTTTCTTAAACTACATGAGTGAT
GTAGAAGCTGGTGGTGCCACCGTCTTCCCTGATCTGGGGGCTGCAATTTGGCCTAAGAAG
GGTACAGCTGTGTTCTGGTACAACCTCTTGCGGAGCGGGGAAGGTGACTACCGAACAAGA
CATGCTGCCTGCCCTGTGCTTGTGGGCTGCAAGTGGGTCTCCAATAAGTGGTTCCATGAA
CGAGGACAGGAGTTCTTGAGACCTTGTGGATCAACAGAAGTTGACTGA
Target 18 GenBank Gene ID
Target 18 GeneCard ID P4HA2 Link Image
Target 18 GenAtlas ID P4HA2 Link Image
Target 18 HGNC ID HGNC:8547 Link Image
Target 18 Chromosome Location 5
Target 18 Locus 5q31
Target 18 SNPs SNPJam Report Link Image
Target 18 General References
  1. Nokelainen M, Nissi R, Kukkola L, Helaakoski T, Myllyharju J: Characterization of the human and mouse genes for the alpha subunit of type II prolyl 4-hydroxylase. Identification of a previously unknown alternatively spliced exon and its expression in various tissues. Eur J Biochem. 2001 Oct;268(20):5300-9. [PubMed Link Image]
  2. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  3. Annunen P, Helaakoski T, Myllyharju J, Veijola J, Pihlajaniemi T, Kivirikko KI: Cloning of the human prolyl 4-hydroxylase alpha subunit isoform alpha(II) and characterization of the type II enzyme tetramer. The alpha(I) and alpha(II) subunits do not form a mixed alpha(I)alpha(II)beta2 tetramer. J Biol Chem. 1997 Jul 11;272(28):17342-8. [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 4001
Target 19 Name Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial
Target 19 Synonyms
  1. EC 1.3.5.1
  2. Ip
  3. Iron-sulfur subunit of complex II
  4. Succinate dehydrogenase iron-sulfur subunit, mitochondrial precursor
Target 19 Gene Name SDHB
Target 19 Protein Sequence >Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial
MAAVVALSLRRRLPATTLGGACLQASRGAQTAAATAPRIKKFAIYRWDPDKAGDKPHMQT
YEVDLNKCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTN
LNKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQYLQSIEEREKL
DGLYECILCACCSTSCPSYWWNGDKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSL
YRCHTIMNCTRTCPKGLNPGKAIAEIKKMMATYKEKKASV
Target 19 Number of Residues 284
Target 19 Molecular Weight 31630
Target 19 Theoretical pI 8.92
Target 19 GO Classification
Function
catalytic activity
oxidoreductase activity
binding
ion binding
cation binding
transition metal ion binding
iron ion binding
transporter activity
electron transporter activity
Process
energy derivation by oxidation of organic compounds
main pathways of carbohydrate metabolism
tricarboxylic acid cycle
physiological process
metabolism
cellular metabolism
generation of precursor metabolites and energy
electron transport
Component
cell
membrane
Target 19 General Function Energy production and conversion
Target 19 Specific Function Succinate + ubiquinone = fumarate + ubiquinol
Target 19 Pathways
Name SMPDB Link KEGG Link
Oxidative phosphorylation map00020 Link Image
Target 19 Reactions
  • succinate + ubiquinone = fumarate + ubiquinol
Target 19 Pfam Domain Function
Target 19 Signals
  • None
Target 19 Transmembrane Regions
  • None
Target 19 Essentiality Non-Essential
Target 19 GenBank ID Protein 665925 Link Image
Target 19 UniProtKB/Swiss-Prot ID P21912 Link Image
Target 19 UniProtKB/Swiss-Prot Entry Name DHSB_HUMAN Link Image
Target 19 PDB ID Not Available
Target 19 Cellular Location
  • Mitochondrion
Target 19 Gene Sequence >843 bp
ATGGCGGCGGTGGTCGCACTCTCCTTGAGGCGCCGGTTGCCGGCCACAACCCTTGGCGGA
GCCTGCCTGCAGGCCTCCCGAGGAGCCCAGACAGCTGCAGCCACAGCTCCCCGTATCAAG
AAATTTGCCATCTATCGATGGGACCCAGACAAGGCTGGAGACAAACCTCATATGCAGACT
TATAAGGTTGACCTTAATAAATGTGGCCCCATGGTATTGGATGCTTTAATCAAGATTAAG
AATGAAGTTGACTCTACTTTGACCTTCCGAAGATCATGCAGAGAAGGCATCTGTGGCTCT
TGTGCAATGAACATCAATGGAGGCAACACTCTAGCTTGCACCCGAAGGATTGACACCAAC
CTCAATAAGGTCTCAAAAATCTACCCTCTTCCACACATGTATGTGATAAAGGATCTTGTT
CCCGATTTGAGCAACTTCTATGCACAGTACAAATCCATTGAGCCTTATTTGAAGAAGAAG
GATGAATCTCAGGAAGGCAAGCAGCAGTATCTGCAGTCCATAGAAGAGCGTGAGAAACTG
GACGGGCTCTACGAGTGCATTCTCTGTGCCTGCTGTAGCACCAGCTGCCCCAGCTACTGG
TGGAACGGAGACAAATATCTGGGGCCTGCAGTTCTTATGCAGGCCTATCGCTGGATGATT
GACTCCAGAGATGACTTCACAGAGGAGCGCCTGGCCAAGCTGCAGGACCCATTCTCTCTA
TACCGCTGCCACACCATCATGAACTGCACAAGGACCTGTCCTAAGGGTCTGAATCCAGGG
AAAGCTATTGCAGAGATCAAGAAAATGATGGCAACCTATAAGGAGAAGAAAGCTTCAGTT
TAA
Target 19 GenBank Gene ID
Target 19 GeneCard ID SDHB Link Image
Target 19 GenAtlas ID SDHB Link Image
Target 19 HGNC ID HGNC:10681 Link Image
Target 19 Chromosome Location 1
Target 19 Locus 1p36.1-p35
Target 19 SNPs SNPJam Report Link Image
Target 19 General References
  1. Kita K, Oya H, Gennis RB, Ackrell BA, Kasahara M: Human complex II (succinate-ubiquinone oxidoreductase): cDNA cloning of iron sulfur (Ip) subunit of liver mitochondria. Biochem Biophys Res Commun. 1990 Jan 15;166(1):101-8. [PubMed Link Image]
  2. Gould SJ, Subramani S, Scheffler IE: Use of the DNA polymerase chain reaction for homology probing: isolation of partial cDNA or genomic clones encoding the iron-sulfur protein of succinate dehydrogenase from several species. Proc Natl Acad Sci U S A. 1989 Mar;86(6):1934-8. [PubMed Link Image]
  3. Au HC, Ream-Robinson D, Bellew LA, Broomfield PL, Saghbini M, Scheffler IE: Structural organization of the gene encoding the human iron-sulfur subunit of succinate dehydrogenase. Gene. 1995 Jul 4;159(2):249-53. [PubMed Link Image]
Target 19 Drug References
  1. Arikawa Y, Kuroyanagi T, Shimosaka M, Muratsubaki H, Enomoto K, Kodaira R, Okazaki M: Effect of gene disruptions of the TCA cycle on production of succinic acid in Saccharomyces cerevisiae. J Biosci Bioeng. 1999;87(1):28-36. [PubMed Link Image]
  2. Bayley JP, Devilee P, Taschner PE: The SDH mutation database: an online resource for succinate dehydrogenase sequence variants involved in pheochromocytoma, paraganglioma and mitochondrial complex II deficiency. BMC Med Genet. 2005 Nov 16;6:39. [PubMed Link Image]
  3. Bayley JP, van Minderhout I, Weiss MM, Jansen JC, Oomen PH, Menko FH, Pasini B, Ferrando B, Wong N, Alpert LC, Williams R, Blair E, Devilee P, Taschner PE: Mutation analysis of SDHB and SDHC: novel germline mutations in sporadic head and neck paraganglioma and familial paraganglioma and/or pheochromocytoma. BMC Med Genet. 2006 Jan 11;7:1. [PubMed Link Image]
  4. Lehtonen HJ, Makinen MJ, Kiuru M, Laiho P, Herva R, van Minderhout I, Hogendoorn PC, Cornelisse C, Devilee P, Launonen V, Aaltonen LA: Increased HIF1 alpha in SDH and FH deficient tumors does not cause microsatellite instability. Int J Cancer. 2007 Sep 15;121(6):1386-9. [PubMed Link Image]
  5. Szeto SS, Reinke SN, Sykes BD, Lemire BD: Ubiquinone-binding site mutations in the Saccharomyces cerevisiae succinate dehydrogenase generate superoxide and lead to the accumulation of succinate. J Biol Chem. 2007 Sep 14;282(37):27518-26. Epub 2007 Jul 18. [PubMed Link Image]
Drug Target 20 [top]
Target 20 ID 4002
Target 20 Name Succinyl-CoA ligase [GDP-forming] subunit alpha, mitochondrial
Target 20 Synonyms
  1. EC 6.2.1.4
  2. SCS- alpha
  3. Succinyl-CoA ligase subunit alpha, mitochondrial precursor
  4. Succinyl-CoA synthetase subunit alpha
Target 20 Gene Name SUCLG1
Target 20 Protein Sequence >Succinyl-CoA ligase [GDP-forming] subunit alpha, mitochondrial
MVSGSSGLAAARLLSRSFLLPQNGIRHCSYTASRQHLYVDKNTKIICQGFTGKQGTFHSQ
QALEYGTKLVGGTTPGKGGQTHLGLPVFNTVKEAKEQTGATASVIYVPPPFAAAAINEAI
EAEIPLVVCITEGIPQQDMVRVKHKLLRQEKTRLIGPNCPGVINPGECKIGIMPGHIHKK
GRIGIVSRSGTLTYEAVHQTTQVGLGQSLCVGIGGDPFNGTDFIDCLEIFLNDSATEGII
LIGEIGGNAEENAAEFLKQHNSGPNSKPVVSFIAGLTAPPGRRMGHAGAIIAGGKGGAKE
KISALQSAGVVVSMSPAQLGTTIYKEFEKRKML
Target 20 Number of Residues 338
Target 20 Molecular Weight 35048
Target 20 Theoretical pI 9.24
Target 20 GO Classification
Function
catalytic activity
Process
physiological process
metabolism
Component
Not Available
Target 20 General Function Energy production and conversion
Target 20 Specific Function GTP + succinate + CoA = GDP + phosphate + succinyl-CoA
Target 20 Pathways
Name SMPDB Link KEGG Link
Propanoate metabolism map00020 Link Image
Target 20 Reactions
  • GTP + succinate + CoA = GDP + phosphate + succinyl-CoA
Target 20 Pfam Domain Function
Target 20 Signals
  • None
Target 20 Transmembrane Regions
  • None
Target 20 Essentiality Non-Essential
Target 20 GenBank ID Protein 9409794 Link Image
Target 20 UniProtKB/Swiss-Prot ID P53597 Link Image
Target 20 UniProtKB/Swiss-Prot Entry Name SUCA_HUMAN Link Image
Target 20 PDB ID 1EUC Link Image
Target 20 PDB File Show
Target 20 3D Structure
Target 20 Cellular Location
  • Mitochondrion
Target 20 Gene Sequence >1002 bp
ATGGTCTCCGGCAGCAGCGGCCTCGCCGCCGCCCGTCTCCTGTCGCGCAGCTTCCTCCTG
CCGCAGAATGGAATTCGGCATTGTTCCTACACAGCTTCTCGGCAACATCTCTATGTTGAT
AAAAATACAAAGATTATTTGCCAGGGTTTCACTGGCAAACAGGGCACCTTTCACAGCCAG
CAGGCATTGGAATATGGCACCAAACTCGTTGGAGGAACACTCCCAGGGAAAGGAGGCCAG
ACACATCTGGGCTTACCTGTCTTTAATACTGTGAAGGAGGCCAAAGAACAGACAGGAGCA
ACGGCTTCTGTCATTTATGTTCCTCCGCCTTTTGCTGCTGCTGCCATTAATGAAGCTATT
GAGGCAGAAATTCCCTTGGTTGTGTGTATCACTGAAGGAATTCCCCAGCAGGACATGGTA
CGAGTCAAGCACAAACTGCTGCGCCAGGAAAAGACAAGGCTAATTGGGCCCAACTGCCCT
GGAGTCATCAATCCTGGAGAATGTAAAATTGGGATCATGCCTGGCCATATTCACAAAAAA
GGAAGGATTGGCATTGTGTCCAGATCTGGCACCCTGACTTATGAAGCAGTTCACCAAACA
ACGCAAGTTGGATTGGGGCAGTCTTTGTGCGTTGGCATTGGAGGTGATCCTTTTAATGGA
ACAGATTTTATTGACTGCCTCGAAATCTTTTTGAACGATTCTGCCACAGAAGGCATCATA
TTGATTGGTGAAATTGGTGGTAATGCAGAAGAGAATGCTGCAGAATTTTTGAAGCAACAT
AATTCAGGTCCAAATTCCAAGCCTGTAGTGTCCTTCATTGCTGGTTTAACTGCTCCTCCT
GGGAGAAGAATGGGTCATGCCGGGGCAATTATTGCTGGAGGAAAAGGTGGAGCTAAAGAG
AAGATCTCTGCCCTTCAGAGTGCAGGAGTTGTGGTCAGTATGTCTCCTGCACAGCTGGGA
ACCACGATCTACAAGGAATTTGAAAAGAGGAAGATGCTATGA
Target 20 GenBank Gene ID
Target 20 GeneCard ID SUCLG1 Link Image
Target 20 GenAtlas ID SUCLG1 Link Image
Target 20 HGNC ID HGNC:11449 Link Image
Target 20 Chromosome Location 2
Target 20 Locus 2p11.2
Target 20 SNPs SNPJam Report Link Image
Target 20 General References
  1. James M, Man NT, Edwards YH, Morris GE: The molecular basis for cross-reaction of an anti-dystrophin antibody with alpha-actinin. Biochim Biophys Acta. 1997 Apr 12;1360(2):169-76. [PubMed Link Image]
Target 20 Drug References
  1. Ostergaard E, Christensen E, Kristensen E, Mogensen B, Duno M, Shoubridge EA, Wibrand F: Deficiency of the alpha subunit of succinate-coenzyme A ligase causes fatal infantile lactic acidosis with mitochondrial DNA depletion. Am J Hum Genet. 2007 Aug;81(2):383-7. Epub 2007 Jun 4. [PubMed Link Image]
Drug Target 21 [top]
Target 21 ID 4003
Target 21 Name Succinyl-CoA:3-ketoacid-coenzyme A transferase 1, mitochondrial
Target 21 Synonyms
  1. EC 2.8.3.5
  2. Scot-S
  3. Somatic-type succinyl CoA:3-oxoacid CoA- transferase
  4. Succinyl-CoA:3-ketoacid-coenzyme A transferase 1, mitochondrial precursor
Target 21 Gene Name OXCT1
Target 21 Protein Sequence >Succinyl-CoA:3-ketoacid-coenzyme A transferase 1, mitochondrial
MAALKLLSSGLRLCASARGSGATWYKGCVCSFSTSAHRHTKFYTDPVEAVKDIPDGATVL
VGGFGLCGIPENLIDALLKTGVKGLTAVSNNAGVDNFGLGLLLRSKQIKRMVSSYVGENA
EFERQYLSGELEVELTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGGSPIKYNKDGSV
AIASKPREVREFNGQHFILEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMCKAAET
TVVEVEEIVDIGAFAPEDIHIPQIYVHRLIKGEKYEKRIERLSIRKEGDGEAKSAKPGDD
VRERIIKRAALEFEDGMYANLGIGIPLLASNFISPNITVHLQSENGVLGLGPYPRQHEAD
ADLINAGKETVTILPGASFFSSDESFAMIRGGHVDLTMLGAMQVSKYGDLANWMIPGKMV
KGMGGAMDLVSSAKTKVVVTMEHSAKGNAHKIMEKCTLPLTGKQCVNRIITEKAVFDVDK
KKGLTLIELWEGLTVDDVQKSTGCDFAVSPKLMPMQQIAN
Target 21 Number of Residues 528
Target 21 Molecular Weight 56158
Target 21 Theoretical pI 7.52
Target 21 GO Classification
Function
catalytic activity
transferase activity
transferase activity, transferring sulfur-containing groups
CoA-transferase activity
Process
physiological process
metabolism
Component
Not Available
Target 21 General Function Lipid transport and metabolism
Target 21 Specific Function Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate
Target 21 Pathways
Name SMPDB Link KEGG Link
Butanoate metabolism map00072 Link Image
Target 21 Reactions
  • succinyl-CoA + a 3-oxo acid = succinate + a 3-oxoacyl-CoA
Target 21 Pfam Domain Function
Target 21 Signals
  • None
Target 21 Transmembrane Regions
  • None
Target 21 Essentiality Non-Essential
Target 21 GenBank ID Protein 1519052 Link Image
Target 21 UniProtKB/Swiss-Prot ID P55809 Link Image
Target 21 UniProtKB/Swiss-Prot Entry Name SCOT_HUMAN Link Image
Target 21 PDB ID 1OOY Link Image
Target 21 PDB File Show
Target 21 3D Structure
Target 21 Cellular Location
  • Mitochondrion
Target 21 Gene Sequence >1563 bp
ATGGCGGCTCTCAAACTCCTCTCCTCCGGGCTTCGGCTCTGCGCCTCTGCCCGCGGATCT
GGGGCAACCTGGTACAAGGGATGTGTTTGTTCCTTTTCCACCAGTGCTCATCGCCATACC
AAGTTTTATACAGATCCAGTAGAAGCTGTAAAAGACATCCCTGATGGTGCCACGGTTTTG
GTTGGTGGTTTTGGGCTATGTGGAATTCCAGAGAATCTTATAGATGCTTTACTGAAAACT
GGAGTAAAAGGACTAACTGCAGTCAGCAACAATGCAGGGGTTGACAATTTTGGTTTGGGG
CTTTTGCTTCGGTCGAAGCAGATAAAACGCATGGTCTCTTCATATGTGGGAGAAAATGCA
GAATTTGAACGACAGTACTTATCTGGTGAATTAGAAGTGGAGCTGACACCACAGGGCACA
CTTGCAGAGAGGATCCGTGCAGGCGGGGCTGGAGTTCCTGCATTTTACACCCCAACAGGG
TATGGGACCCTGGTACAAGAAGGAGGATCGCCCATCAAATACAACAAAGATGGCAGTGTT
GCCATTGCCAGTAAGCCAAGAGAGGTGAGGGAGTTCAATGGTCAGCACTTTATTTTGGAG
GAAGCAATTACAGGGGATTTTGCTTTGGTGAAAGCCTGGAAGGCGGACCGAGCAGGAAAC
GTGATTTTCAGGAAAAGTGCAAGGAATTTCAACTTGCCAATGTGCAAAGCTGCAGAAACC
ACAGTGGTAGAGGTTGAAGAAATTGTGGATATTGGAGCATTTGCTCCAGAAGACATCCAT
ATTCCTCAGATTTATGTACATCGCCTTATAAAGGGAGAAAAATATGAGAAAAGAATTGAG
CGTTTATCAATCCGGAAAGAGGGAGATGGGGAAGCCAAATCTGCTAAACCTGGAGATGAC
GTAAGGGAACGAATCATCAAGAGGGCCGCTCTTGAGTTTGAGGATGGCATGTATGCTAAT
TTGGGCATAGGAATCCCTCTCCTGGCCAGCAATTTTATCAGCCCAAATATAACTGTTCAT
CTTCAAAGTGAAAATGGAGTTCTGGGTTTGGGTCCATATCCACGACAACATGAAGCTGAT
GCAGATCTCATCAATGCAGGCAAGGAAACAGTTACTATTCTTCCAGGAGCCTCTTTTTTC
TCCAGCGATGAATCATTTGCAATGATTAGAGGTGGACACGTCGATCTGACAATGCTAGGA
GCGATGCAGGTTTCCAAATATGGTGACCTGGCTAACTGGATGATACCTGGGAAGATGGTG
AAAGGAATGGGAGGTGCTATGGATTTAGTGTCCAGTGCGAAAACCAAAGTGGTGGTCACC
ATGGAGCATTCTGCAAAGGGAAATGCACATAAAATCATGGAGAAATGTACATTACCATTG
ACTGGAAAGCAATGTGTCAACCGCATTATTACTGAAAAGGCTGTGTTTGATGTGGACAAG
AAGAAAGGGTTGACTCTGATTGAGCTCTGGGAAGGCCTGACAGTGGATGACGTACAAAAG
AGTACTGGGTGTGATTTTGCAGTTTCACCAAAACTCATGCCAATGCAGCAGATCGCAAAT
TGA
Target 21 GenBank Gene ID
Target 21 GeneCard ID OXCT1 Link Image
Target 21 GenAtlas ID OXCT1 Link Image
Target 21 HGNC ID HGNC:8527 Link Image
Target 21 Chromosome Location 5
Target 21 Locus 5p13.1
Target 21 SNPs SNPJam Report Link Image
Target 21 General References
  1. Fukao T, Mitchell GA, Song XQ, Nakamura H, Kassovska-Bratinova S, Orii KE, Wraith JE, Besley G, Wanders RJ, Niezen-Koning KE, Berry GT, Palmieri M, Kondo N: Succinyl-CoA:3-ketoacid CoA transferase (SCOT): cloning of the human SCOT gene, tertiary structural modeling of the human SCOT monomer, and characterization of three pathogenic mutations. Genomics. 2000 Sep 1;68(2):144-51. [PubMed Link Image]
  2. Kassovska-Bratinova S, Fukao T, Song XQ, Duncan AM, Chen HS, Robert MF, Perez-Cerda C, Ugarte M, Chartrand C, Vobecky S, Kondo N, Mitchell GA: Succinyl CoA: 3-oxoacid CoA transferase (SCOT): human cDNA cloning, human chromosomal mapping to 5p13, and mutation detection in a SCOT-deficient patient. Am J Hum Genet. 1996 Sep;59(3):519-28. [PubMed Link Image]
  3. Song XQ, Fukao T, Watanabe H, Shintaku H, Hirayama K, Kassovska-Bratinova S, Kondo N, Mitchell GA: Succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency: two pathogenic mutations, V133E and C456F, in Japanese siblings. Hum Mutat. 1998;12(2):83-8. [PubMed Link Image]
Target 21 Drug References
  1. Coros AM, Swenson L, Wolodko WT, Fraser ME: Structure of the CoA transferase from pig heart to 1.7 A resolution. Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1717-25. Epub 2004 Sep 23. [PubMed Link Image]
Drug Target 22 [top]
Target 22 ID 4005
Target 22 Name Succinate-CoA ligase, ADP-forming, beta subunit
Target 22 Synonyms Not Available
Target 22 Gene Name SUCLA2
Target 22 Protein Sequence >Succinate-CoA ligase, ADP-forming, beta subunit
MAASMFYGRLVAVATLRNHRPRTAQQQQRNLSLHEYMSMELLQEAGVSVPKGYVAKSPDE
AYAIAKKLGSKDVVIKAQVLAGGRGKGTFESGLKGGVKIVFSPEEAKAVSSQMIGKKLFT
KQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGPVLIGSSHGGVNIEDVAAESPEA
IIKEPIDIEEGIKKEQALQLAQKMGFPPNIVESAAENMVKLYSLFLKYDATMIEINPMVE
DSDGAVLCMDAKINFDSNSAYRQKKIFDLQDWTQEDERDKDAAKANLNYIGLDGNIGCLV
NGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEAFKLITSDKKVLAILVNIFGGIM
RCDVIAQGIVMAVKDLEIKIPVVVRLQGTRVDDAKALIADSGLKILACDDLDEAARMVVK
LSEIVTLAKQAHVDVKFQLPI
Target 22 Number of Residues 448
Target 22 Molecular Weight 48040
Target 22 Theoretical pI 7.09
Target 22 GO Classification
Function
catalytic activity
Process
physiological process
metabolism
Component
Not Available
Target 22 General Function Energy production and conversion
Target 22 Specific Function Not Available
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 55957259 Link Image
Target 22 UniProtKB/Swiss-Prot ID Q5T9Q6 Link Image
Target 22 UniProtKB/Swiss-Prot Entry Name Q5T9Q6_HUMAN Link Image
Target 22 PDB ID Not Available
Target 22 Cellular Location Not Available
Target 22 Gene Sequence >1326 bp
ATGGCGGCCTCCATGTTCTACGGCAGGCTAGTGGCCGTGGCCACCCTTCGGAACCACCGG
CCTCGGACGGCCCAGCAACAGCAAAGGAATCTCTCACTACATGAATACATGAGTATGGAA
TTATTGCAAGAAGCTGGTGTCTCCGTTCCCAAAGGATATGTGGCAAAGTCACCAGATGAA
GCTTATGCAATTGCCAAAAAATTAGGTTCAAAAGATGTCGTGATAAAGGCACAGGTTTTA
GCTGGTGGTAGAGGAAAAGGAACATTTGAAAGTGGCCTCAAAGGAGGAGTGAAGATAGTT
TTCTCTCCAGAAGAAGCAAAAGCTGTTTCTTCACAAATGATTGGGAAAAAATTGTTTACC
AAGCAAACGGGAGAAAAGGGCAGAATATGCAATCAAGTATTGGTCTGTGAGCGAAAATAT
CCCAGGAGAGAATACTACTTTGCAATAACAATGGAAAGGTCATTTCAAGGTCCTGTATTA
ATAGGAAGTTCACATGGTGGTGTCAACATTGAAGATGTTGCTGCTGAGTCTCCTGAAGCA
ATAATTAAAGAACCTATTGATATTGAAGAAGGCATCAAAAAGGAACAAGCTCTCCAGCTT
GCACAGAAGATGGGATTTCCACCTAATATTGTGGAATCAGCAGCAGAAAACATGGTCAAG
CTTTACAGCCTTTTTCTGAAATACGATGCAACCATGATAGAAATAAATCCAATGGTGGAA
GATTCAGATGGAGCTGTATTGTGTATGGATGCAAAGATCAATTTTGACTCTAATTCAGCC
TATCGCCAAAAGAAAATCTTTGATCTACAGGACTGGACCCAGGAAGATGAAAGGGACAAA
GATGCTGCTAAGGCAAATCTCAACTACATTGGCCTCGATGGAAATATAGGCTGCCTAGTA
AATGGTGCTGGTTTGGCTATGGCCACAATGGATATAATAAAACTTCATGGAGGGACTCCA
GCCAACTTCCTTGATGTTGGTGGTGGTGCTACAGTCCATCAAGTAACAGAAGCATTTAAG
CTTATCACTTCAGATAAAAAGGTACTGGCTATTCTGGTCAACATTTTTGGAGGAATCATG
CGCTGTGATGTTATTGCACAGGGTATAGTCATGGCAGTAAAAGACTTGGAAATTAAAATA
CCTGTTGTGGTACGGTTACAAGGTACACGAGTCGATGATGCTAAGGCACTGATAGCGGAC
AGTGGACTTAAAATACTTGCTTGTGATGACTTGGATGAAGCTGCTAGAATGGTTGTAAAG
CTCTCTGAAATAGTGACCTTAGCGAAGCAAGCACATGTGGATGTGAAATTTCAGTTGCCA
ATATGA
Target 22 GenBank Gene ID
Target 22 GeneCard ID SUCLA2 Link Image
Target 22 GenAtlas ID SUCLA2 Link Image
Target 22 HGNC ID HGNC:11448 Link Image
Target 22 Chromosome Location 13
Target 22 Locus 13q12.2-q13.3
Target 22 SNPs SNPJam Report Link Image
Target 22 General References Not Available
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 4006
Target 23 Name Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
Target 23 Synonyms
  1. CYBL
  2. Integral membrane protein CII-3
  3. QPs-1
  4. QPs1
  5. Succinate dehydrogenase complex subunit C
  6. Succinate dehydrogenase cytochrome b560 subunit, mitochondrial precursor
  7. Succinate-ubiquinone oxidoreductase cytochrome B large subunit
Target 23 Gene Name SDHC
Target 23 Protein Sequence >Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
MAALLLRHVGRHCLRAHFSPQLCIRNAVPLGTTAKEEMERFWNKNIGSNRPLSPHITIYS
WSLPMAMSICHRGTGIALSAGVSLFGMSALLLPGNFESYLELVKSLCLGPALIHTAKFAL
VFPLMYHTWNGIRHLMWDLGKGLKIPQLYQSGVVVLVLTVLSSMGLAAM
Target 23 Number of Residues 171
Target 23 Molecular Weight 18611
Target 23 Theoretical pI 10.12
Target 23 GO Classification
Function
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on the CH-CH group of donors
succinate dehydrogenase activity
Process
electron transport
physiological process
metabolism
cellular metabolism
generation of precursor metabolites and energy
energy derivation by oxidation of organic compounds
main pathways of carbohydrate metabolism
tricarboxylic acid cycle
Component
cell
membrane
Target 23 General Function Energy production and conversion
Target 23 Specific Function Mono-heme cytochrome b. May act as a mediator of low potential couples in an electron flow through cardiac complex II. Is involved in system II of the mitochondrial electron transport chain which is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q)
Target 23 Pathways Not Available
Target 23 Reactions Not Available
Target 23 Pfam Domain Function
Target 23 Signals
  • None
Target 23 Transmembrane Regions
  • 71-93
  • 105-127
  • 147-168
Target 23 Essentiality Non-Essential
Target 23 GenBank ID Protein 1814226 Link Image
Target 23 UniProtKB/Swiss-Prot ID Q99643 Link Image
Target 23 UniProtKB/Swiss-Prot Entry Name C560_HUMAN Link Image
Target 23 PDB ID Not Available
Target 23 Cellular Location
  • Mitochondrion
Target 23 Gene Sequence >510 bp
ATGGCTGCGCTGTTGCTGAGACACGTTGGTCGTCATTGCCTCCGAGCCCACTTTAGCCCT
CAGCTCTGTATCAGAAATGCTGTTCCTTTGGGAACCACGGCCAAAGAAGAGATGGAGCGG
TTCTGGAATAAGAATATAGGTTCAAACCGTCCTCTGTCTCCCCACATTACTATCTACAGT
TGGTCTCTTCCCATGGCGATGTCCATCTGCCACCGTGGCACTGGTATTGCTTTGAGTGCA
GGGGTCTCTCTTTTTGGCATGTCGGCCCTGTTACTCCCTGGGAACTTTGAGTCTTATTTG
GAACTTGTGAAGTCCCTGTGTCTGGGGCCAGCACTGATCCACACAGCTAAGTTTGCACTT
GTCTTCCCTCTCATGTATCATACCTGGAATGGGATCCGACACTTGATGTGGGACCTAGGA
AAAGGCCTGAAGATTCCCCAGCTATACCAGTCTGGAGTGGTTGTCCTGGTTCTTACTGTG
TTGTCCTCTATGGGGCTGGCAGCCATGTGA
Target 23 GenBank Gene ID
Target 23 GeneCard ID SDHC Link Image
Target 23 GenAtlas ID SDHC Link Image
Target 23 HGNC ID HGNC:10682 Link Image
Target 23 Chromosome Location 1
Target 23 Locus 1q23.3
Target 23 SNPs SNPJam Report Link Image
Target 23 General References
  1. Niemann S, Muller U: Mutations in SDHC cause autosomal dominant paraganglioma, type 3. Nat Genet. 2000 Nov;26(3):268-70. [PubMed Link Image]
  2. Hirawake H, Taniwaki M, Tamura A, Kojima S, Kita K: Cytochrome b in human complex II (succinate-ubiquinone oxidoreductase): cDNA cloning of the components in liver mitochondria and chromosome assignment of the genes for the large (SDHC) and small (SDHD) subunits to 1q21 and 11q23. Cytogenet Cell Genet. 1997;79(1-2):132-8. [PubMed Link Image]
  3. Elbehti-Green A, Au HC, Mascarello JT, Ream-Robinson D, Scheffler IE: Characterization of the human SDHC gene encoding of the integral membrane proteins of succinate-quinone oxidoreductase in mitochondria. Gene. 1998 Jun 15;213(1-2):133-40. [PubMed Link Image]
Target 23 Drug References
  1. Leibowitz G, Khaldi MZ, Shauer A, Parnes M, Oprescu AI, Cerasi E, Jonas JC, Kaiser N: Mitochondrial regulation of insulin production in rat pancreatic islets. Diabetologia. 2005 Aug;48(8):1549-59. Epub 2005 Jun 29. [PubMed Link Image]
  2. Kubo Y, Takagi H, Nakamori S: Effect of gene disruption of succinate dehydrogenase on succinate production in a sake yeast strain. J Biosci Bioeng. 2000;90(6):619-24. [PubMed Link Image]
  3. Bayley JP, Devilee P, Taschner PE: The SDH mutation database: an online resource for succinate dehydrogenase sequence variants involved in pheochromocytoma, paraganglioma and mitochondrial complex II deficiency. BMC Med Genet. 2005 Nov 16;6:39. [PubMed Link Image]
  4. Bayley JP, van Minderhout I, Weiss MM, Jansen JC, Oomen PH, Menko FH, Pasini B, Ferrando B, Wong N, Alpert LC, Williams R, Blair E, Devilee P, Taschner PE: Mutation analysis of SDHB and SDHC: novel germline mutations in sporadic head and neck paraganglioma and familial paraganglioma and/or pheochromocytoma. BMC Med Genet. 2006 Jan 11;7:1. [PubMed Link Image]
  5. Szeto SS, Reinke SN, Sykes BD, Lemire BD: Ubiquinone-binding site mutations in the Saccharomyces cerevisiae succinate dehydrogenase generate superoxide and lead to the accumulation of succinate. J Biol Chem. 2007 Sep 14;282(37):27518-26. Epub 2007 Jul 18. [PubMed Link Image]
Drug Target 24 [top]
Target 24 ID 4007
Target 24 Name Succinate receptor 1
Target 24 Synonyms
  1. G-protein coupled receptor 91
  2. P2Y purinoceptor 1-like
Target 24 Gene Name SUCNR1
Target 24 Protein Sequence >Succinate receptor 1
MAWNATCKNWLAAEAALEKYYLSIFYGIEFVVGVLGNTIVVYGYIFSLKNWNSSNIYLFN
LSVSDLAFLCTLPMLIRSYANGNWIYGDVLCISNRYVLHANLYTSILFLTFISIDRYLII
KYPFREHLLQKKEFAILISLAIWVLVTLELLPILPLINPVITDNGTTCNDFASSGDPNYN
LIYSMCLTLLGFLIPLFVMCFFYYKIALFLKQRNRQVATALPLEKPLNLVIMAVVIFSVL
FTPYHVMRNVRIASRLGSWKQYQCTQVVINSFYIVTRPLAFLNSVINPVFYFLLGDHFRD
MLMNQLRHNFKSLTSFSRWAHELLLSFREK
Target 24 Number of Residues 335
Target 24 Molecular Weight 38284
Target 24 Theoretical pI 9.18
Target 24 GO Classification
Function
nucleotide receptor activity, G-protein coupled
purinergic nucleotide receptor activity, G-protein coupled
signal transducer activity
receptor activity
transmembrane receptor activity
G-protein coupled receptor activity
rhodopsin-like receptor activity
Process
cellular process
cell communication
signal transduction
cell surface receptor linked signal transduction
G-protein coupled receptor protein signaling pathway
Component
cell
membrane
intrinsic to membrane
integral to membrane
Target 24 General Function Not Available
Target 24 Specific Function Receptor for succinate
Target 24 Pathways Not Available
Target 24 Reactions Not Available
Target 24 Pfam Domain Function
Target 24 Signals
  • None
Target 24 Transmembrane Regions
  • 28-48
  • 56-76
  • 100-120
  • 134-154
  • 182-202
  • 227-247
  • 278-298
Target 24 Essentiality Non-Essential
Target 24 GenBank ID Protein 13517983 Link Image
Target 24 UniProtKB/Swiss-Prot ID Q9BXA5 Link Image
Target 24 UniProtKB/Swiss-Prot Entry Name SUCR1_HUMAN Link Image
Target 24 PDB ID Not Available
Target 24 Cellular Location
  • Membrane
Target 24 Gene Sequence >993 bp
ATGGCATGGAATGCAACTTGCAAAAACTGGCTGGCAGCAGAGGCTGCCCTGGAAAAGTAC
TACCTTTCCATTTTTTATGGGATTGAGTTCGTTGTGGGAGTCCTTGGAAATACCATTGTT
GTTTACGGCTACATCTTCTCTCTGAAGAACTGGAACAGCAGTAATATTTATCTCTTTAAC
CTCTCTGTCTCTGACTTAGCTTTTCTGTGCACCCTCCCCATGCTGATAAGGAGTTATGCC
AATGGAAACTGGATATATGGAGACGTGCTCTGCATAAGCAACCGATATGTGCTTCATGCC
AACCTCTATACCAGCATTCTCTTTCTCACTTTTATCAGCATAGATCGATACTTGATAATT
AAGTATCCTTTCCGAGAACACCTTCTGCAAAAGAAAGAGTTTGCTATTTTAATCTCCTTG
GCCATTTGGGTTTTAGTAACCTTAGAGTTACTACCCATACTTCCCCTTATAAATCCTGTT
ATAACTGACAATGGCACCACCTGTAATGATTTTGCAAGTTCTGGAGACCCCAACTACAAC
CTCATTTACAGCATGTGTCTAACACTGTTGGGGTTCCTTATTCCTCTTTTTGTGATGTGT
TTCTTTTATTACAAGATTGCTCTCTTCCTAAAGCAGAGGAATAGGCAGGTTGCTACTGCT
CTGCCCCTTGAAAAGCCTCTCAACTTGGTCATCATGGCAGTGGTAATCTTCTCTGTGCTT
TTTACACCCTATCACGTCATGCGGAATGTGAGGATCGCTTCACGCCTGGGGAGTTGGAAG
CAGTATCAGTGCACTCAGGTCGTCATCAACTCCTTTTACATTGTGACACGGCCTTTGGCC
TTTCTGAACAGTGTCATCAACCCTGTCTTCTATTTTCTTTTGGGAGATCACTTCAGGGAC
ATGCTGATGAATCAACTGAGACACAACTTCAAATCCCTTACATCCTTTAGCAGATGGGCT
CATGAACTCCTACTTTCATTCAGAGAAAAGTGA
Target 24 GenBank Gene ID
Target 24 GeneCard ID SUCNR1 Link Image
Target 24 GenAtlas ID SUCNR1 Link Image
Target 24 HGNC ID HGNC:4542 Link Image
Target 24 Chromosome Location 3
Target 24 Locus 3q24-q25.1
Target 24 SNPs SNPJam Report Link Image
Target 24 General References
  1. Wittenberger T, Schaller HC, Hellebrand S: An expressed sequence tag (EST) data mining strategy succeeding in the discovery of new G-protein coupled receptors. J Mol Biol. 2001 Mar 30;307(3):799-813. [PubMed Link Image]
Target 24 Drug References
  1. Macaulay IC, Tijssen MR, Thijssen-Timmer DC, Gusnanto A, Steward M, Burns P, Langford CF, Ellis PD, Dudbridge F, Zwaginga JJ, Watkins NA, van der Schoot CE, Ouwehand WH: Comparative gene expression profiling of in vitro differentiated megakaryocytes and erythroblasts identifies novel activatory and inhibitory platelet membrane proteins. Blood. 2007 Apr 15;109(8):3260-9. Epub 2006 Dec 27. [PubMed Link Image]
Drug Target 25 [top]
Target 25 ID 4008
Target 25 Name Succinyl-CoA:3-ketoacid-coenzyme A transferase 2, mitochondrial
Target 25 Synonyms
  1. EC 2.8.3.5
  2. SCOT-t
  3. Succinyl-CoA:3-ketoacid-coenzyme A transferase 2, mitochondrial precursor
  4. Testis-specific succinyl CoA:3-oxoacid CoA- transferase
Target 25 Gene Name OXCT2
Target 25 Protein Sequence >Succinyl-CoA:3-ketoacid-coenzyme A transferase 2, mitochondrial
MAALRLLASVLGRGVPAGGSGLALSQGCARCFATSPRLRAKFYADPVEMVKDISDGATVM
IGGFGLCGIPENLIAALLRTRVKDLQVVSSNVGVEDFGLGLLLAARQVRRIVCSYVGENT
LCESQYLAGELELELTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGGAPIRYTPDGHL
ALMSQPREVREFNGDHFLLERAIRADFALVKGWKADRAGNVVFRRSARNFNVPMCKAADV
TAVEVEEIVEVGAFPPEDIHVPNIYVDRVIKGQKYEKRIERLTILKEEDGDAGKEEDART
RIIRRAALEFEDGMYANLGIGIPLLASNFISPSMTVHLHSENGILGLGPFPTEDEVDADL
INAGKQTVTVLPGGCFFASDDSFAMIRGGHIQLTMLGAMQVSKYGDLANWMIPGKKVKGM
GGAMDLVSSQKTRVVVTMQHCTKDNTPKIMEKCTMPLTGKRCVDRIITEKAVFDVHRKKE
LTLRELWEGLTVDDIKKSTGCAFAVSPNLRPMQQVAP
Target 25 Number of Residues 525
Target 25 Molecular Weight 56141
Target 25 Theoretical pI 7.15
Target 25 GO Classification
Function
catalytic activity
transferase activity
transferase activity, transferring sulfur-containing groups
CoA-transferase activity
Process
physiological process
metabolism
Component
Not Available
Target 25 General Function Lipid transport and metabolism
Target 25 Specific Function Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate
Target 25 Pathways
Name SMPDB Link KEGG Link
Butanoate metabolism map00072 Link Image
Target 25 Reactions
  • succinyl-CoA + a 3-oxo acid = succinate + a 3-oxoacyl-CoA
Target 25 Pfam Domain Function
Target 25 Signals
  • None
Target 25 Transmembrane Regions
  • None
Target 25 Essentiality Non-Essential
Target 25 GenBank ID Protein 13548673 Link Image
Target 25 UniProtKB/Swiss-Prot ID Q9BYC2 Link Image
Target 25 UniProtKB/Swiss-Prot Entry Name SCOT2_HUMAN Link Image
Target 25 PDB ID Not Available
Target 25 Cellular Location
  • Mitochondrion
Target 25 Gene Sequence >1554 bp
ATGGCGGCGCTGCGGCTCCTGGCGTCAGTGCTCGGGCGCGGGGTCCCCGCCGGCGGCTCA
GGGCTCGCGCTGTCCCAGGGCTGCGCCCGCTGCTTTGCCACCAGTCCCCGGCTCCGTGCC
AAGTTCTACGCGGACCCGGTGGAGATGGTGAAGGACATCTCTGACGGGGCGACCGTCATG
ATCGGGGGCTTCGGGCTCTGCGGGATCCCCGAGAACCTGATCGCCGCGCTGCTCAGGACC
CGCGTGAAAGACCTGCAGGTGGTCAGCAGCAACGTGGGCGTGGAGGACTTCGGCCTGGGC
CTCCTGCTGGCCGCCAGGCAGGTCCGTCGCATCGTCTGTTCCTACGTGGGCGAGAACACC
CTGTGCGAGAGCCAGTACCTGGCAGGAGAGCTGGAGCTGGAGCTCACGCCCCAGGGCACC
CTGGCCGAGCGCATCCGCGCGGGGGGCGCCGGGGTGCCCGCCTTCTACACCCCCACGGGC
TACGGGACCCTGGTCCAGGAAGGGGGCGCCCCCATCCGCTACACCCCGGACGGCCACCTG
GCGCTCATGAGCCAGCCCCGAGAGGTGAGGGAGTTCAACGGCGACCACTTCCTTTTGGAG
CGCGCCATCCGGGCAGACTTCGCCCTGGTGAAAGGGTGGAAGGCCGACCGGGCAGGAAAC
GTGGTCTTCAGGAGAAGCGCCCGCAATTTCAACGTGCCCATGTGCAAAGCTGCAGACGTC
ACGGCGGTGGAGGTGGAAGAGATCGTGGAGGTGGGGGCTTTCCCCCCAGAAGACATCCAC
GTTCCTAACATTTATGTAGATCGCGTGATAAAGGGGCAGAAATACGAGAAACGAATTGAG
CGCTTAACGATCCTGAAAGAGGAAGATGGAGACGCTGGAAAGGAAGAGGACGCCAGGACG
CGCATCATCAGACGCGCAGCTCTGGAATTTGAGGACGGCATGTACGCCAATCTGGGCATA
GGCATCCCCCTGCTGGCCAGCAACTTCATCAGTCCCAGCATGACTGTCCATCTTCACAGT
GAGAACGGGATCCTGGGCCTGGGCCCGTTTCCCATGGAAGATGAGGTGGATGCCGACCTC
ATCAATGCAGGCAAGCAGACGGTCACGGTGCTTCCCGGGGGCTGCTTCTTCGCCAGCGAC
GACTCCTTCGCCATGATCCGAGGGGGACACATCCAACTAACCATGCTTGGAGCCATGCAG
GTTTCCAAATACGGCGACCTGGCGAACTGGATGATCCCTGGCAAGAAGGTGAAAGGCATG
GGCGGTGCCATGGACTTGGTGTCCAGTCAGAAGACCAGAGTGGTGGTCACCATGCAGCAC
TGCACAAAGGACAACACCCCCAAGATCATGGAGAAATGCACCATGCCGCTGACCGGGAAG
CGGTGCGTGGACCGCATCATCACCGAGAAGGCCGTGTTTGACGTGCACAGGAAGAAAGAG
CTGACGCTGAGGGAGCTCTGGGAGGGCCTGACGGTGGACGACATCAAAAAGAGCACGGGG
TGTGCCTTTGCTGTGTCCCCGAACCTCAGGCCCATGCAGCAGGTGGCACCCTGA
Target 25 GenBank Gene ID
Target 25 GeneCard ID OXCT2 Link Image
Target 25 GenAtlas ID OXCT2 Link Image
Target 25 HGNC ID HGNC:18606 Link Image
Target 25 Chromosome Location 1
Target 25 Locus 1p34
Target 25 SNPs SNPJam Report Link Image
Target 25 General References Not Available
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 4009
Target 26 Name Succinyl-CoA ligase [ADP-forming] beta-chain, mitochondrial
Target 26 Synonyms
  1. ATP- specific succinyl-CoA synthetase subunit beta
  2. EC 6.2.1.5
  3. Renal carcinoma antigen NY-REN-39
  4. SCS-betaA
  5. Succinyl-CoA ligase beta-chain, mitochondrial precursor
  6. Succinyl-CoA synthetase, betaA chain
Target 26 Gene Name SUCLA2
Target 26 Protein Sequence >Succinyl-CoA ligase [ADP-forming] beta-chain, mitochondrial
MAASMFYGRLVAVATLRNHRPRTAQRAAAQVLGSSGLFNNHGLQVQQQQQRNLSLHEYMS
MELLQEAGVSVPKGYVAKSPDEAYAIAKKLGSKDVVIKAQVLAGGRGKGTFESGLKGGVK
IVFSPEEAKAVSSQMIGKKLFTKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGP
VLIGSSHGGVNIEDVAAESPEAIIKEPIDIEEGIKKEQALQLAQKMGFPPNIVESAAENM
VKLYSLFLKYDATMIEINPMVEDSDGAVLCMDAKINFDSNSAYRQKKIFDLQDWTQEDER
DKDAAKANLNYIGLDGNIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEA
FKLITSDKKVLAILVNIFGGIMRCDVIAQGIVMAVKDLEIKIPVVVRLQGTRVDDAKALI
ADSGLKILACDDLDEAARMVVKLSEIVTLAKQAHVDVKFQLPI
Target 26 Number of Residues 470
Target 26 Molecular Weight 50318
Target 26 Theoretical pI 7.50
Target 26 GO Classification
Function
catalytic activity
Process
physiological process
metabolism
Component
Not Available
Target 26 General Function Energy production and conversion
Target 26 Specific Function ATP + succinate + CoA = ADP + phosphate + succinyl-CoA
Target 26 Pathways
Name SMPDB Link KEGG Link
Reductive carboxylate cycle (CO2 fixation) map00020 Link Image
Target 26 Reactions
  • ATP + succinate + CoA = ADP + phosphate + succinyl-CoA
Target 26 Pfam Domain Function
Target 26 Signals
  • None
Target 26 Transmembrane Regions
  • None
Target 26 Essentiality Non-Essential
Target 26 GenBank ID Protein 7328935 Link Image
Target 26 UniProtKB/Swiss-Prot ID Q9P2R7 Link Image
Target 26 UniProtKB/Swiss-Prot Entry Name SUCB1_HUMAN Link Image
Target 26 PDB ID Not Available
Target 26 Cellular Location
  • Mitochondrion
Target 26 Gene Sequence >1392 bp
ATGGCGGCCTCCATGTTCTACGGCAGGCTAGTGGCCGTGGCCACCCTTCGGAACCACCGG
CCTCGGACGGCCCAGCGGGCTGCTGCTCAGGTTCTGGGAAGTTCTGGATTGTTTAATAAC
CATGGACTCCAAGTACAGCAGCAACAGCAAAGGAATCTCTCACTACATGAATACATGAGT
ATGGAATTATTGCAAGAAGCTGGTGTCTCCGTTCCCAAAGGATATGTGGCAAAGTCACCA
GATGAAGCTTATGCAATTGCCAAAAAATTAGGTTCAAAAGATGTCGTGATAAAGGCACAG
GTTTTAGCTGGTGGTAGAGGAAAAGGAACATTTGAAAGTGGCCTCAAAGGAGGAGTGAAG
ATAGTTTTCTCTCCAGAAGAAGCAAAAGCTGTTTCTTCACAAATGATTGGGAAAAAATTG
TTTACCAAGCAAACGGGAGAAAAGGGCAGAATATGCAATCAAGTATTGGTCTGTGAGCGA
AAATATCCCAGGAGAGAATACTACTTTGCAATAACAATGGAAAGGTCATTTCAAGGTCCT
GTATTAATAGGAAGTTCACATGGTGGTGTCAACATTGAAGATGTTGCTGCTGAGTCTCCT
GAAGCAATAATTAAAGAACCTATTGATATTGAAGAAGGCATCAAAAAGGAACAAGCTCTC
CAGCTTGCACAGAAGATGGGATTTCCACCTAATATTGTGGAATCAGCAGCAGAAAACATG
GTCAAGCTTTACAGCCTTTTTCTGAAATACGATGCAACCATGATAGAAATAAATCCAATG
GTGGAAGATTCAGATGGAGCTGTATTGTGTATGGATGCAAAGATCAATTTTGACTCTAAT
TCAGCCTATCGCCAAAAGAAAATCTTTGATCTACAGGACTGGACCCAGGAAGATGAAAGG
GACAAAGATGCTGCTAAGGCAAATCTCAACTACATTGGCCTCGATGGAAATATAGGCTGC
CTAGTAAATGGTGCTGGTTTGGCTATGGCCACAATGGATATAATAAAACTTCATGGAGGG
ACTCCAGCCAACTTCCTTGATGTTGGTGGTGGTGCTACAGTCCATCAAGTAACAGAAGCA
TTTAAGCTTATCACTTCAGATAAAAAGGTACTGGCTATTCTGGTCAACATTTTTGGAGGA
ATCATGCGCTGTGATGTTATTGCACAGGGTATAGTCATGGCAGTAAAAGACTTGGAAATT
AAAATACCTGTTGTGGTACGGTTACAAGGTACACGAGTCGATGATGCTAAGGCACTGATA
GCGGACAGTGGACTTAAAATACTTGCTTGTGATGACTTGGATGAAGCTGCTAGAATGGTT
GTAAAGCTCTCTGAAATAGTGACCTTAGCGAAGCAAGCACATGTGGATGTGAAATTTCAG
TTGCCAATATGA
Target 26 GenBank Gene ID
Target 26 GeneCard ID SUCLA2 Link Image
Target 26 GenAtlas ID SUCLA2 Link Image
Target 26 HGNC ID HGNC:11448 Link Image
Target 26 Chromosome Location 13
Target 26 Locus 13q12.2-q13.3
Target 26 SNPs SNPJam Report Link Image
Target 26 General References
  1. Scanlan MJ, Gordan JD, Williamson B, Stockert E, Bander NH, Jongeneel V, Gure AO, Jager D, Jager E, Knuth A, Chen YT, Old LJ: Antigens recognized by autologous antibody in patients with renal-cell carcinoma. Int J Cancer. 1999 Nov 12;83(4):456-64. [PubMed Link Image]
  2. Furuyama K, Sassa S: Interaction between succinyl CoA synthetase and the heme-biosynthetic enzyme ALAS-E is disrupted in sideroblastic anemia. J Clin Invest. 2000 Mar;105(6):757-64. [PubMed Link Image]
  3. Johnson JD, Mehus JG, Tews K, Milavetz BI, Lambeth DO: Genetic evidence for the expression of ATP- and GTP-specific succinyl-CoA synthetases in multicellular eucaryotes. J Biol Chem. 1998 Oct 16;273(42):27580-6. [PubMed Link Image]
Target 26 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 27 [top]
Target 27 ID 4010
Target 27 Name Mitochondrial dicarboxylate carrier
Target 27 Synonyms
  1. Solute carrier family 25 member 10
Target 27 Gene Name SLC25A10
Target 27 Protein Sequence >Mitochondrial dicarboxylate carrier
MAAEARVSRWYFGGLASCGAACCTHPLDLLKVHLQTQQEVKLRMTGMALRVVRTDGILAL
YSGLSASLCRQMTYSLTRFAIYETVRDRVAKGSQGPLPFHEKVLLGSVSGLAGGFVGTPA
DLVNVRMQNDVKLPQGQRRNYAHALDGLYRVAREEGLRRLFSGATMASSRGALVTVGQLS
CYDQAKQLVLSTGYLSDNIFTHFVASFIAGGCATFLCQPLDVLKTRLMNSKGEYQGVFHC
AVETAKLGPLAFYKGLVPAGIRLIPHTVLTFVFLEQLRKNFGIKVPS
Target 27 Number of Residues 291
Target 27 Molecular Weight 31283
Target 27 Theoretical pI 9.91
Target 27 GO Classification
Function
binding
Process
physiological process
cellular physiological process
transport
intracellular transport
mitochondrial transport
Component
cell
membrane
organelle
membrane-bound organelle
intracellular membrane-bound organelle
mitochondrion
Target 27 General Function Not Available
Target 27 Specific Function Involved in translocation of malonate, malate and succinate in exchange for phosphate, sulfate, sulfite or thiosulfate across mitochondrial inner membrane
Target 27 Pathways Not Available
Target 27 Reactions Not Available
Target 27 Pfam Domain Function
Target 27 Signals
  • None
Target 27 Transmembrane Regions
  • 10-30
  • 103-123
  • 203-223
  • 255-275
Target 27 Essentiality Non-Essential
Target 27 GenBank ID Protein 6224534 Link Image
Target 27 UniProtKB/Swiss-Prot ID Q9UBX3 Link Image
Target 27 UniProtKB/Swiss-Prot Entry Name DIC_HUMAN Link Image
Target 27 PDB ID Not Available
Target 27 Cellular Location
  • Mitochondrion
Target 27 Gene Sequence >864 bp
ATGGCAGCCGAGGCGCGCGTGTCGCGCTGGTACTTCGGGGGGCTGGCCTCCTGCGGGGCC
GCCTGCTGCACGCACCCGCTGGACCTGCTCAAGGTGCATCTGCAGACGCAGCAGGAGGTG
AAGCTGCGCATGACGGGCATGGCGCTGCGGGTGGTGCGTACCGACGGCATCCTGGCACTC
TACAGCGGCCTGAGCGCCTCGCTGTGCAGACAGATGACCTACTCCCTGACTCGGTTCGCC
ATCTACGAGACTGTGCGGGACCGCGTGGCCAAGGGCAGCCAGGGGCCTCTCCCCTTCCAC
GAGAAGGTGTTGCTGGGCTCCGTCAGCGGTTTAGCTGGAGGCTTCGTGGGGACGCCCGCA
GACTTGGTCAACGTCAGGATGCAGAACGACGTGAAGCTGCCCCAGGGTCAGCGGCGCAAC
TACGCCCATGCGCTGGATGGCCTGTACCGCGTAGCTCGTGAAGAGGGTCTCAGGAGACTG
TTCTCGGGTGCAACCATGGCATCCAGCCGAGGGGCCTTAGTCACTGTGGGCCAGCTGTCC
TGCTACGACCAGGCCAAGCAGCGGGTCCTTAGCACCGGGTACCTCTCTGACAACATCTTC
ACTCACTTTGTCGCCAGCTTTATTGCAGGTGGATGTGCCACGTTCCTGTGCCAGCCCCTG
GATGTGCTGAAGACTCGCCTGATGAACTCCAAGGGGGAGTATCAGGGCGTTTTCCACTGC
GCCGTGGAGACAGCGAAGCTCGGGCCTCTGGCCTTTTACAAGGGCCTCGTCCCAGCTGGC
ATCCGCCTCATCCCCCACACCGTGCTCACTTTTGTGTTTCTGGAACAGCTACGCAAAAAC
TTTGGCATCAAAGTGCCATCCTGA
Target 27 GenBank Gene ID
Target 27 GeneCard ID SLC25A10 Link Image
Target 27 GenAtlas ID SLC25A10 Link Image
Target 27 HGNC ID HGNC:10980 Link Image
Target 27 Chromosome Location 17
Target 27 Locus 17q25.3
Target 27 SNPs SNPJam Report Link Image
Target 27 General References
  1. Fiermonte G, Dolce V, Arrigoni R, Runswick MJ, Walker JE, Palmieri F: Organization and sequence of the gene for the human mitochondrial dicarboxylate carrier: evolution of the carrier family. Biochem J. 1999 Dec 15;344 Pt 3:953-60. [PubMed Link Image]
Target 27 Drug References
  1. Mizuarai S, Miki S, Araki H, Takahashi K, Kotani H: Identification of dicarboxylate carrier Slc25a10 as malate transporter in de novo fatty acid synthesis. J Biol Chem. 2005 Sep 16;280(37):32434-41. Epub 2005 Jul 15. [PubMed Link Image]
  2. Ventura FV, Ruiter J, Ijlst L, de Almeida IT, Wanders RJ: Differential inhibitory effect of long-chain acyl-CoA esters on succinate and glutamate transport into rat liver mitochondria and its possible implications for long-chain fatty acid oxidation defects. Mol Genet Metab. 2005 Nov;86(3):344-52. Epub 2005 Sep 19. [PubMed Link Image]

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.