| Identification | |||||||||||||||||||||||||||||||||||||
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| Name | Adenosine-5'-Diphosphate | ||||||||||||||||||||||||||||||||||||
| Accession Number | DB03431 (EXPT00436) | ||||||||||||||||||||||||||||||||||||
| Type | small molecule | ||||||||||||||||||||||||||||||||||||
| Groups | experimental | ||||||||||||||||||||||||||||||||||||
| Description | Adenosine 5'-(trihydrogen diphosphate). An adenine nucleotide containing two phosphate groups esterified to the sugar moiety at the 5'-position. [PubChem] |
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| Structure |
Download: MOL | SDF | SMILES | InChI Display: 2D Structure | 3D Structure |
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| Synonyms | Not Available | ||||||||||||||||||||||||||||||||||||
| Brand names | Not Available | ||||||||||||||||||||||||||||||||||||
| Brand name mixtures | Not Available | ||||||||||||||||||||||||||||||||||||
| Categories | Not Available | ||||||||||||||||||||||||||||||||||||
| CAS number | 20398-34-9 | ||||||||||||||||||||||||||||||||||||
| Weight |
Average: 427.2011 Monoisotopic: 427.029414749 |
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| Chemical Formula | C10H15N5O10P2 | ||||||||||||||||||||||||||||||||||||
| InChI Key | InChIKey=XTWYTFMLZFPYCI-FCIPNVEPSA-N | ||||||||||||||||||||||||||||||||||||
| InChI |
InChI=1S/C10H15N5O10P2/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(24-10)1-23-27(21,22)25-26(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7+,10+/m0/s1
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| IUPAC Name |
{[(R)-{[(2S,3R,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl]oxy}phosphonic acid
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| SMILES |
NC1=NC=NC2=C1N=CN2[C@@H]1O[C@@H](CO[P@](O)(=O)OP(O)(O)=O)[C@H](O)[C@H]1O
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| Mass Spec | Not Available | ||||||||||||||||||||||||||||||||||||
| Taxonomy | |||||||||||||||||||||||||||||||||||||
| Kingdom | Not Available | ||||||||||||||||||||||||||||||||||||
| Classes | Not Available | ||||||||||||||||||||||||||||||||||||
| Substructures | Not Available | ||||||||||||||||||||||||||||||||||||
| Pharmacology | |||||||||||||||||||||||||||||||||||||
| Indication | Not Available | ||||||||||||||||||||||||||||||||||||
| Pharmacodynamics | Not Available | ||||||||||||||||||||||||||||||||||||
| Mechanism of action | Not Available | ||||||||||||||||||||||||||||||||||||
| Absorption | Not Available | ||||||||||||||||||||||||||||||||||||
| Volume of distribution | Not Available | ||||||||||||||||||||||||||||||||||||
| Protein binding | Not Available | ||||||||||||||||||||||||||||||||||||
| Metabolism | |||||||||||||||||||||||||||||||||||||
| Route of elimination | Not Available | ||||||||||||||||||||||||||||||||||||
| Half life | Not Available | ||||||||||||||||||||||||||||||||||||
| Clearance | Not Available | ||||||||||||||||||||||||||||||||||||
| Toxicity | Not Available | ||||||||||||||||||||||||||||||||||||
| Affected organisms | Not Available | ||||||||||||||||||||||||||||||||||||
| Pathways | Not Available | ||||||||||||||||||||||||||||||||||||
| Pharmacoeconomics | |||||||||||||||||||||||||||||||||||||
| Manufacturers | Not Available | ||||||||||||||||||||||||||||||||||||
| Packagers | Not Available | ||||||||||||||||||||||||||||||||||||
| Dosage forms | Not Available | ||||||||||||||||||||||||||||||||||||
| Prices | Not Available | ||||||||||||||||||||||||||||||||||||
| Patents | Not Available | ||||||||||||||||||||||||||||||||||||
| Properties | |||||||||||||||||||||||||||||||||||||
| State | solid | ||||||||||||||||||||||||||||||||||||
| Melting point | Not Available | ||||||||||||||||||||||||||||||||||||
| Experimental Properties | Not Available | ||||||||||||||||||||||||||||||||||||
| Predicted Properties |
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| References | |||||||||||||||||||||||||||||||||||||
| Synthesis Reference | Not Available | ||||||||||||||||||||||||||||||||||||
| General Reference | Not Available | ||||||||||||||||||||||||||||||||||||
| External Links |
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| ATC Codes | Not Available | ||||||||||||||||||||||||||||||||||||
| AHFS Codes | Not Available | ||||||||||||||||||||||||||||||||||||
| PDB Entries | |||||||||||||||||||||||||||||||||||||
| FDA label | Not Available | ||||||||||||||||||||||||||||||||||||
| MSDS | Not Available | ||||||||||||||||||||||||||||||||||||
| Interactions | |||||||||||||||||||||||||||||||||||||
| Drug Interactions |
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| Food Interactions | Not Available | ||||||||||||||||||||||||||||||||||||
| Targets |
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Pharmacological action: unknown
Essential for recycling GMP and indirectly, cGMP Organism class: humanUniProt ID: Q16774 ![]() Gene: GUK1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components:the iron protein (component 2) and a component 1 which is either a molybdenum-iron protein, a vanadium-iron, or an iron-iron protein Organism class: bacterialUniProt ID: P00459 ![]() Gene: nifH1 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 3. Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 Pharmacological action: unknownThis magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction Organism class: humanUniProt ID: O14983 ![]() Gene: ATP2A1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
4. Myosin-11 Pharmacological action: unknownOrganism class: human UniProt ID: P35749 ![]() Gene: MYH11 SNPs: SNPJam Report ![]() References:
5. Inositol-trisphosphate 3-kinase A Pharmacological action: unknownATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate Organism class: humanUniProt ID: P23677 ![]() Gene: ITPKA ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Organism class: human UniProt ID: Q99661 ![]() Gene: KIF2C SNPs: SNPJam Report ![]() References:
7. Aminoglycoside 3'-phosphotransferase Pharmacological action: unknownResistance to kanamycin and structurally-related aminoglycosides, including amikacin Organism class: bacterialUniProt ID: P0A3Y5 ![]() Gene: aphA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Key enzyme in the regulation of glycerol uptake and metabolism Organism class: bacterialUniProt ID: P0A6F3 ![]() Gene: glpK Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L- glutamate 5-phosphate Organism class: bacterialUniProt ID: P0A6C8 ![]() Gene: argB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 10. Thymidine kinase Pharmacological action: unknownATP + thymidine = ADP + thymidine 5'- phosphate Organism class: viralUniProt ID: P24425 ![]() Gene: TK Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 11. Glutamate--cysteine ligase Pharmacological action: unknownATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine Organism class: bacterialUniProt ID: P0A6W9 ![]() Gene: gshA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa Organism class: humanUniProt ID: P06732 ![]() Gene: CKM ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
13. Heat shock protein HSP 90-beta Pharmacological action: unknownMolecular chaperone. Has ATPase activity Organism class: humanUniProt ID: P08238 ![]() Gene: HSP90AB1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
14. S-adenosylmethionine synthetase isoform type-1 Pharmacological action: unknownCatalyzes the formation of S-adenosylmethionine from methionine and ATP Organism class: humanUniProt ID: Q00266 ![]() Gene: MAT1A ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L- glutamate 5-phosphate Organism class: bacterialUniProt ID: Q9HTN2 ![]() Gene: argB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 16. Spliceosome RNA helicase BAT1 Pharmacological action: unknownOrganism class: human UniProt ID: Q13838 ![]() Gene: DDX39B SNPs: SNPJam Report ![]() References:
17. UMP-CMP kinase Pharmacological action: unknownCatalyzes specific phosphoryl transfer from ATP to UMP and CMP Organism class: humanUniProt ID: P30085 ![]() Gene: CMPK ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
18. ATP-binding cassette sub-family A member 6 Pharmacological action: unknownOrganism class: human UniProt ID: Q8N139 ![]() Gene: ABCA6 SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine Organism class: bacterialUniProt ID: P0A1P6 ![]() Gene: glnA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 20. Hypothetical protein MG245 homolog Pharmacological action: unknownOrganism class: bacterial UniProt ID: P75430 ![]() Gene: MPN_348 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 21. Kinesin-like protein KIF11 Pharmacological action: unknownMotor protein required for establishing a bipolar spindle. Blocking of KIF11 prevents centrosome migration and arrest cells in mitosis with monoastral microtubule arrays Organism class: humanUniProt ID: P52732 ![]() Gene: KIF11 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 22. Actin, alpha skeletal muscle Pharmacological action: unknownActins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells Organism class: humanUniProt ID: P68133 ![]() Gene: ACTA1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Organism class: human UniProt ID: P00558 ![]() Gene: PGK1 SNPs: SNPJam Report ![]() References:
24. Pyridoxal kinase Pharmacological action: unknownRequired for synthesis of pyridoxal-5-phosphate from vitamin B6 Organism class: humanUniProt ID: O00764 ![]() Gene: PDXK ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
25. Arsenical pump-driving ATPase Pharmacological action: unknownAnion-transporting ATPase. Catalyzes the extrusion of the oxyanions arsenite, antimonite and arsenate. Maintenance of a low intracellular concentration of oxyanion produces resistance to the toxic agents Organism class: bacterialUniProt ID: P08690 ![]() Gene: arsA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 26. Mast/stem cell growth factor receptor Pharmacological action: unknownThis is the receptor for stem cell factor (mast cell growth factor). It has a tyrosine-protein kinase activity. Binding of the ligands leads to the autophosphorylation of KIT and its association with substrates such as phosphatidylinositol 3-kinase (Pi3K) Organism class: humanUniProt ID: P10721 ![]() Gene: KIT ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 27. ATP-dependent Clp protease ATP-binding subunit clpA Pharmacological action: unknownATP-dependent specificity component of the clpP protease. It directs the protease to specific substrates. The primary function of the clpA-clpP complex appears to be the degradation of unfolded or abnormal proteins Organism class: bacterialUniProt ID: P0ABH9 ![]() Gene: clpA Protein Sequence: FASTA SNPs: SNPJam Report ![]() References: 28. Endoplasmin Pharmacological action: unknownMolecular chaperone that functions in the processing and transport of secreted proteins Organism class: humanUniProt ID: P14625 ![]() Gene: HSP90B1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either cheB or cheY Organism class: bacterialUniProt ID: Q56310 ![]() Gene: cheA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 30. Protein recA Pharmacological action: unknownCan catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with lexA causing its activation and leading to its autocatalytic cleavage Organism class: bacterialUniProt ID: Q59560 ![]() Gene: recA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Organism class: bacterial UniProt ID: O67198 ![]() Gene: ntrC1 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 32. Heat shock cognate 71 kDa protein Pharmacological action: unknownChaperone. Isoform 2 may function as an endogenous inhibitory regulator of HSC70 by competing the co-chaperones Organism class: humanUniProt ID: P11142 ![]() Gene: HSPA8 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
33. Apoptotic protease-activating factor 1 Pharmacological action: unknownOligomeric Apaf-1 mediates the cytochrome c-dependent autocatalytic activation of pro-caspase-9 (Apaf-3), leading to the activation of caspase-3 and apoptosis. This activation requires ATP. Isoform 6 is less effective in inducing apoptosis Organism class: humanUniProt ID: O14727 ![]() Gene: APAF1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 34. Phosphoribosylformylglycinamidine synthase Pharmacological action: unknownATP + 2-N-formyl-1-N-(5-phospho-D- ribosyl)glycinamide + L-glutamine + H(2)O = ADP + phosphate + 2- (formamido)-1-N-(5-phospho-D-ribosyl)acetamidine + L-glutamate Organism class: bacterialUniProt ID: P74881 ![]() Gene: purL Protein Sequence: FASTA SNPs: SNPJam Report ![]() 35. Heat shock protein HSP 90-alpha Pharmacological action: unknownMolecular chaperone. Has ATPase activity Organism class: humanUniProt ID: P07900 ![]() Gene: HSP90AA1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 36. S-adenosylmethionine synthetase Pharmacological action: unknownCatalyzes the formation of S-adenosylmethionine from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme Organism class: bacterialUniProt ID: P0A820 ![]() Gene: metK Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 37. Protein recA Pharmacological action: unknownCan catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with lexA causing its activation and leading to its autocatalytic cleavage (By similarity) Organism class: bacterialUniProt ID: P0A7G9 ![]() Gene: recA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Essential for DNA replication Organism class: viralUniProt ID: P03132 ![]() Gene: REP Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 39. FtsH Pharmacological action: unknownSeems to act as an ATP-dependent zinc metallopeptidase (By similarity) Organism class: bacterialUniProt ID: Q9LCZ4 ![]() Gene: ftsH Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 40. Myosin-14 Pharmacological action: unknownCellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping (By similarity) Organism class: humanUniProt ID: Q7Z406 ![]() Gene: MYH14 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
41. Activator of Pharmacological action: unknownRequired for the activation of (R)-2-hydroxyglutaryl-CoA dehydratase. This protein is extremely sensitive towards oxygen Organism class: bacterialUniProt ID: P11568 ![]() Gene: hgdC Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 42. Heat shock 70 kDa protein 1 Pharmacological action: unknownIn cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage Organism class: humanUniProt ID: P08107 ![]() Gene: HSPA1A ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 43. Galactokinase Pharmacological action: unknownMajor enzyme for galactose metabolism Organism class: humanUniProt ID: P51570 ![]() Gene: GALK1 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Catalyzes the conversion of dTMP to dTDP Organism class: humanUniProt ID: P23919 ![]() Gene: DTYMK ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione Organism class: bacterialUniProt ID: P04425 ![]() Gene: gshB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin-mononucleotide (FMN) Organism class: humanUniProt ID: Q969G6 ![]() Gene: RFK ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Involved in the repair of mismatches in DNA Organism class: humanUniProt ID: P54278 ![]() Gene: PMS2 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 48. Mono-ADP-ribosyltransferase C3 Pharmacological action: unknownADP-ribosylates eukaryotic Rho and Rac proteins on an asparagine residue Organism class: viralUniProt ID: P15879 ![]() Gene: C3 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 49. ATP-dependent Clp protease ATP-binding subunit clpX Pharmacological action: unknownATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of clpP (By similarity) Organism class: bacterialUniProt ID: O25926 ![]() Gene: clpX Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 50. Serine/threonine-protein kinase 6 Pharmacological action: unknownMay play a role in cell cycle regulation during anaphase and/or telophase, in relation to the function of the centrosome/spindle pole region during chromosome segregation. Maybe involved in microtubule formation and/or stabilization. May play a key role during tumor development and progression Organism class: humanUniProt ID: O14965 ![]() Gene: AURKA ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 51. Phosphoenolpyruvate carboxykinase [ATP] Pharmacological action: unknownATP + oxaloacetate = ADP + phosphoenolpyruvate + CO(2) Organism class: bacterialUniProt ID: P22259 ![]() Gene: pckA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A Organism class: bacterialUniProt ID: P0A6I9 ![]() Gene: coaE Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Non-receptor protein-tyrosine kinase implicated in signaling pathways involved in cell motility, proliferation and apoptosis. Activated by tyrosine-phosphorylation in response to either integrin clustering induced by cell adhesion or antibody cross-linking, or via G-protein coupled receptor (GPCR) occupancy by ligands such as bombesin or lysophosphatidic acid, or via LDL receptor occupancy. Plays a potential role in oncogenic transformations resulting in increased kinase activity Organism class: humanUniProt ID: Q05397 ![]() Gene: PTK2 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 54. Thymidine kinase Pharmacological action: unknownIn latent infection, may allow the virus to be reactivated and to grow in cells lacking a high concentration of phosphorylated nucleic acid precursors, such as nerve cells that do not replicate their genome Organism class: viralUniProt ID: P03176 ![]() Gene: TK Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 55. ATP-binding cassette sub-family E member 1 Pharmacological action: unknownOrganism class: human UniProt ID: P61221 ![]() Gene: ABCE1 SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
This is a non-secretory ribonuclease. It is a pyrimidine specific nuclease with a slight preference for U. Cytotoxin and helminthotoxin. Selectively chemotactic for dendritic cells. Possesses a wide variety of biological activities Organism class: humanUniProt ID: P10153 ![]() Gene: RNASE2 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 57. MAP kinase-activated protein kinase 2 Pharmacological action: unknownIts physiological substrate seems to be the small heat shock protein (HSP27/HSP25). In vitro can phosphorylate glycogen synthase at 'Ser-7' and tyrosine hydroxylase (on 'Ser-19' and 'Ser-40'). This kinase phosphorylates Ser in the peptide sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue. Mediates both ERK and p38 MAPK/MAPK14 dependent neutrophil responses. Participates in TNF alpha-stimulated exocytosis of secretory vesicles in neutrophils. Plays a role in phagocytosis-induced respiratory burst activity Organism class: humanUniProt ID: P49137 ![]() Gene: MAPKAPK2 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 58. Transitional endoplasmic reticulum ATPase Pharmacological action: unknownOrganism class: human UniProt ID: P55072 ![]() Gene: VCP SNPs: SNPJam Report ![]() References:
59. Amidophosphoribosyltransferase Pharmacological action: unknown5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H(2)O Organism class: bacterialUniProt ID: P00497 ![]() Gene: purF Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 60. Multidrug resistance ABC transporter ATP-binding and permease protein Pharmacological action: unknownEfflux transporter for a variety of amphiphilic cationic compounds, including antibiotics (By similarity) Organism class: bacterialUniProt ID: Q9CHL8 ![]() Gene: lmrA Protein Sequence: FASTA SNPs: SNPJam Report ![]() 61. Hexokinase-1 Pharmacological action: unknownATP + D-hexose = ADP + D-hexose 6-phosphate Organism class: humanUniProt ID: P19367 ![]() Gene: HK1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 62. Chromosomal replication initiator protein dnaA Pharmacological action: unknownPlays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box):5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids (By similarity) Organism class: bacterialUniProt ID: O66659 ![]() Gene: dnaA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 63. [3-methyl-2-oxobutanoate dehydrogenase [lipoamide]] kinase, mitochondrial Pharmacological action: unknownOrganism class: human UniProt ID: O14874 ![]() Gene: BCKDK SNPs: SNPJam Report ![]() References:
64. Preprotein translocase subunit secA Pharmacological action: unknownInvolved in protein export. Interacts with the secY/secE subunits. SecA has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane Organism class: bacterialUniProt ID: P28366 ![]() Gene: secA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 65. FolC bifunctional protein [Includes: Folylpolyglutamate synthase Pharmacological action: unknownConversion of folates to polyglutamate derivatives Organism class: bacterialUniProt ID: P08192 ![]() Gene: folC Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 66. Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 Pharmacological action: unknownBifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS:activated sulfate donor used by sulfotransferase). In mammals, PAPS is the sole source of sulfate; APS appears to be only an intermediate in the sulfate- activation pathway. Also involved in the biosynthesis of sulfated L-selectin ligands in endothelial cells Organism class: humanUniProt ID: O43252 ![]() Gene: PAPSS1 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
67. Holliday junction ATP-dependent DNA helicase ruvB Pharmacological action: unknownThe ruvA-ruvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is an helicase that mediates the Holliday junction migration by localized denaturation and reannealing Organism class: bacterialUniProt ID: Q56313 ![]() Gene: ruvB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 68. Alpha-aminoadipate--lysW ligase lysX Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q5SH23 ![]() Gene: lysX SNPs: SNPJam Report ![]() References:
69. UDP-N-acetylmuramoylalanine--D-glutamate ligase Pharmacological action: unknownCell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA) Organism class: bacterialUniProt ID: P14900 ![]() Gene: murD Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 70. Phosphoribosylglycinamide formyltransferase 2 Pharmacological action: unknownCatalyzes two reactions:the first one is the production of beta-formyl glycinamide ribonucleotide (GAR) from formate, ATP and beta GAR; the second, a side reaction, is the production of acetyl phosphate and ADP from acetate and ATP Organism class: bacterialUniProt ID: P33221 ![]() Gene: purT Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 71. Plasmid segregation protein parM Pharmacological action: unknownInvolved in the control of plasmid partition. Required for the accurate segregation of the plasmid Organism class: bacterialUniProt ID: P11904 ![]() Gene: parM Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 72. Glycogen synthase kinase-3 beta Pharmacological action: unknownParticipates in the Wnt signaling pathway. Implicated in the hormonal control of several regulatory proteins including glycogen synthase, MYB and the transcription factor JUN. Phosphorylates JUN at sites proximal to its DNA-binding domain, thereby reducing its affinity for DNA Organism class: humanUniProt ID: P49841 ![]() Gene: GSK3B ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides or purine ribonucleosides. Can use ATP or GTP as a phosphate donor. Can also phosphorylate cytidine and uridine nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4- thiouridine, 5-bromouridine, 4-N-acetylcytidine, 4-N- benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5- methylcytidine, and 4-N-anisoylcytidine Organism class: humanUniProt ID: Q9BZX2 ![]() Gene: UCK2 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 74. NTPase P4 Pharmacological action: unknownOrganism class: viral UniProt ID: Q94M05 ![]() Protein Sequence: FASTA Gene Sequence: FASTA 75. Serine/threonine-protein kinase SRPK2 Pharmacological action: unknownPhosphorylates RS domain-containing proteins, such as SFRS1 and SFRS2 on serine residues. Role in spliceosome assembly and in mediating the trafficking of splicing factors. Appears to mediate HBV core protein phosphorylation which is a prerequisite for pregenomic RNA encapsidation into viral capsids Organism class: humanUniProt ID: P78362 ![]() Gene: SRPK2 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
76. 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase Pharmacological action: unknownATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8- dihydropteridine = AMP + (2-amino-4-hydroxy-7,8-dihydropteridin-6- yl)methyl diphosphate Organism class: bacterialUniProt ID: P26281 ![]() Gene: folK Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 77. D-alanine--D-alanine ligase B Pharmacological action: unknownCell wall formation (By similarity) Organism class: bacterialUniProt ID: Q83MF7 ![]() Gene: ddlB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 78. Protein recA Pharmacological action: unknownCan catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with lexA causing its activation and leading to its autocatalytic cleavage Organism class: bacterialUniProt ID: P62219 ![]() Gene: recA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 79. DNA polymerase III subunit tau Pharmacological action: unknownThe gamma chain seems to interact with the delta subunit to transfer the beta subunit on the DNA Organism class: bacterialUniProt ID: P06710 ![]() Gene: dnaX Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
ATP + (R)-pantothenate = ADP + (R)-4'- phosphopantothenate Organism class: bacterialUniProt ID: P0A6I3 ![]() Gene: coaA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 81. Large T antigen Pharmacological action: unknownInitiates DNA unwinding and replication via elaborate interactions with the viral origin of replication. Binds two adjacent sites in the SV40 origin Organism class: viralUniProt ID: P03070 ![]() Protein Sequence: FASTA Gene Sequence: FASTA 82. 3-hydroxy-3-methylglutaryl-coenzyme A reductase Pharmacological action: unknownThis transmembrane glycoprotein is involved in the control of cholesterol biosynthesis. It is the rate-limiting enzyme of sterol biosynthesis Organism class: humanUniProt ID: P04035 ![]() Gene: HMGCR ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Microtubule-dependent motor required for normal distribution of mitochondria and lysosomes (By similarity) Organism class: humanUniProt ID: P33176 ![]() Gene: KIF5B Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Organism class: human UniProt ID: P48637 ![]() Gene: GSS ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Organism class: bacterial UniProt ID: P83820 ![]() Protein Sequence: FASTA 86. Glutamate dehydrogenase 1, mitochondrial Pharmacological action: unknownMay be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate Organism class: humanUniProt ID: P00367 ![]() Gene: GLUD1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 87. Shikimate kinase Pharmacological action: unknownCatalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate Organism class: bacterialUniProt ID: P0A4Z2 ![]() Gene: aroK Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 88. Adenylate kinase Pharmacological action: unknownCatalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. This small ubiquitous enzyme involved in the energy metabolism and nucleotide synthesis, is essential for maintenance and cell growth Organism class: bacterialUniProt ID: P69441 ![]() Gene: adk Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 89. Phosphopantetheine adenylyltransferase Pharmacological action: unknownReversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate (By similarity) Organism class: bacterialUniProt ID: O34797 ![]() Gene: coaD Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
ATP + 7,8-diaminononanoate + CO(2) = ADP + phosphate + dethiobiotin Organism class: bacterialUniProt ID: P13000 ![]() Gene: bioD Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single stranded and double stranded RNA Organism class: humanUniProt ID: P07998 ![]() Gene: RNASE1 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
92. ATP-dependent hsl protease ATP-binding subunit hslU Pharmacological action: unknownChaperone subunit of a proteasome-like degradation complex Organism class: bacterialUniProt ID: P43773 ![]() Gene: hslU Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Synthesizes alpha-1,4-glucan chains using ADP-glucose Organism class: bacterialUniProt ID: P0A3F3 ![]() Gene: glgA1 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Required for the phosphorylation of several deoxyribonucleosides and certain nucleoside analogs widely employed as antiviral and chemotherapeutic agents Organism class: humanUniProt ID: P27707 ![]() Gene: DCK Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 95. Putative partitioning protein Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q72H90 ![]() Gene: TT_C1605 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate Organism class: bacterialUniProt ID: P10880 ![]() Gene: aroL Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 97. Riboflavin kinase/FMN adenylyltransferase Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q9WZW1 ![]() Gene: TM_0857 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Acts as a 5'-hydroxyl kinase, a 3'-phosphatase and a 2',3'-cyclic phosphodiesterase. Catalyzes the transfer of the terminal phosphate of ATP to the 5'-hydroxyl termini of ribo- and deoxyribonucleotides. In the presence of ADP the enzyme also catalyzes an exchange reaction. In the exchange reaction, an excess ADP causes the enzyme to transfer the 5' terminal phosphate from phosphorylated DNA to ADP. These activities modify the ends of nicked tRNA generated by a bacterial response to infection and facilitate repair by T4 RNA ligase Organism class: viralUniProt ID: P06855 ![]() Gene: pseT Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 99. Nucleoside diphosphate kinase A Pharmacological action: unknownMajor role in the synthesis of nucleoside triphosphates other than ATP Organism class: humanUniProt ID: P15531 ![]() Gene: NME1 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
100. 2-keto-3-deoxy-gluconate kinase Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q746L7 ![]() Gene: TT_P0036 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 101. Kinesin-like protein KIFC1 Pharmacological action: unknownOrganism class: human UniProt ID: Q9BW19 ![]() Gene: KIFC1 SNPs: SNPJam Report ![]() References:
102. D-alanine--D-alanine ligase Pharmacological action: unknownCell wall formation (By similarity) Organism class: bacterialUniProt ID: Q48745 ![]() Gene: ddl Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 103. Antigen peptide transporter 1 Pharmacological action: unknownInvolved in the transport of antigens from the cytoplasm to the endoplasmic reticulum for association with MHC class I molecules. Also acts as a molecular scaffold for the final stage of MHC class I folding, namely the binding of peptide. Nascent MHC class I molecules associate with TAP via tapasin. Inhibited by the covalent attachment of herpes simplex virus ICP47 protein, which blocks the peptide-binding site of TAP. Inhibited by human cytomegalovirus US6 glycoprotein, which binds to the lumenal side of the TAP complex and inhibits peptide translocation by specifically blocking ATP-binding to TAP1 and prevents the conformational rearrangement of TAP induced by peptide binding. Inhibited by human adenovirus E3-19K glycoprotein, which binds the TAP complex and acts as a tapasin inhibitor, preventing MHC class I/TAP association. Expression of TAP1 is down-regulated by human Epstein-Barr virus vIL-10 protein, thereby affecting the transport of peptides into the endoplasmic reticulum and subsequent peptide loading by MHC class I molecules Organism class: humanUniProt ID: Q03518 ![]() Gene: TAP1 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 104. Thymidine kinase Pharmacological action: unknownATP + thymidine = ADP + thymidine 5'- phosphate Organism class: bacterialUniProt ID: Q97F65 ![]() Gene: tdk Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 105. TrwB Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q04230 ![]() Gene: trwB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Organism class: bacterial UniProt ID: Q9WXM9 ![]() Gene: TM_0021 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 107. Cystic fibrosis transmembrane conductance regulator Pharmacological action: unknownInvolved in the transport of chloride ions. May regulate bicarbonate secretion and salvage in epithelial cells by regulating the SLC4A7 transporter Organism class: humanUniProt ID: P13569 ![]() Gene: CFTR ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
108. Phosphoribosylaminoimidazole carboxylase ATPase subunit Pharmacological action: unknownPossesses an ATPase activity that is dependent on the presence of AIR (aminoimidazole ribonucleotide). The association of purK and purE produces an enzyme complex capable of converting AIR to CAIR efficiently under physiological condition Organism class: bacterialUniProt ID: P09029 ![]() Gene: purK Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 109. Replication factor C subunit 5 Pharmacological action: unknownOrganism class: human UniProt ID: P40937 ![]() Gene: RFC5 SNPs: SNPJam Report ![]() References:
110. Preprotein translocase secA 1 subunit Pharmacological action: unknownInvolved in protein export. Interacts with the secY/secE subunits. SecA has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane (By similarity) Organism class: bacterialUniProt ID: P0A5Y8 ![]() Gene: secA1 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 111. T-complex protein 1 subunit gamma Pharmacological action: unknownOrganism class: human UniProt ID: P49368 ![]() Gene: CCT3 SNPs: SNPJam Report ![]() References:
112. Myosin-Id Pharmacological action: unknownOrganism class: human UniProt ID: O94832 ![]() Gene: MYO1D SNPs: SNPJam Report ![]() References:
113. Kinesin-like protein KIF1A Pharmacological action: unknownMotor for anterograde axonal transport of synaptic vesicle precursors (By similarity) Organism class: humanUniProt ID: Q12756 ![]() Gene: KIF1A Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
114. Trimethylamine dehydrogenase Pharmacological action: unknownTrimethylamine + H(2)O + electron-transferring flavoprotein = dimethylamine + formaldehyde + reduced electron- transferring flavoprotein Organism class: bacterialUniProt ID: P16099 ![]() Gene: tmd Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 115. Ribokinase Pharmacological action: unknownATP + D-ribose = ADP + D-ribose 5-phosphate Organism class: bacterialUniProt ID: P0A9J6 ![]() Gene: rbsK Protein Sequence: FASTA SNPs: SNPJam Report ![]() References: 116. Transient receptor potential cation channel subfamily M member 7 Pharmacological action: unknownOrganism class: human UniProt ID: Q96QT4 ![]() Gene: TRPM7 SNPs: SNPJam Report ![]() References:
117. UPF0079 ATP-binding protein HI0065 Pharmacological action: unknownOrganism class: bacterial UniProt ID: P44492 ![]() Gene: HI_0065 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Molecular chaperone. Has ATPase activity Organism class: bacterialUniProt ID: P0A6Z3 ![]() Gene: htpG Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 119. Kinesin-like protein KIF3B Pharmacological action: unknownOrganism class: human UniProt ID: O15066 ![]() Gene: KIF3B SNPs: SNPJam Report ![]() References:
120. [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 2, mitochondrial Pharmacological action: unknownInhibits the mitochondrial pyruvate dehydrogenase complex by phosphorylation of the E1 alpha subunit, thus contributing to the regulation of glucose metabolism Organism class: humanUniProt ID: Q15119 ![]() Gene: PDK2 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
121. Cag-alfa Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q7BK04 ![]() Gene: cag-alfa Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() |
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1. Nucleoside diphosphate kinase A Major role in the synthesis of nucleoside triphosphates other than ATP UniProt ID: P15531![]() Gene: NME1 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() Required for the phosphorylation of several deoxyribonucleosides and certain nucleoside analogs widely employed as antiviral and chemotherapeutic agents UniProt ID: P27707![]() Gene: DCK Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() |
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