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Record Information
Version4.0
StatusDetected and Quantified
Creation Date2005-11-16 15:48:42 UTC
Update Date2018-06-19 22:08:11 UTC
HMDB IDHMDB0000538
Secondary Accession Numbers
  • HMDB00538
Metabolite Identification
Common NameAdenosine triphosphate
DescriptionAdenosine triphosphate (ATP) is a nucleotide consisting of a purine base (adenine) attached to the first carbon atom of ribose (a pentose sugar). Three phosphate groups are esterified at the fifth carbon atom of the ribose. ATP is incorporated into nucleic acids by polymerases in the processes of DNA replication and transcription. ATP contributes to cellular energy charge and participates in overall energy balance, maintaining cellular homeostasis. ATP can act as an extracellular signaling molecule via interactions with specific purinergic receptors to mediate a wide variety of processes as diverse as neurotransmission, inflammation, apoptosis, and bone remodelling. Extracellular ATP and its metabolite adenosine have also been shown to exert a variety of effects on nearly every cell type in human skin, and ATP seems to play a direct role in triggering skin inflammatory, regenerative, and fibrotic responses to mechanical injury, an indirect role in melanocyte proliferation and apoptosis, and a complex role in Langerhans cell-directed adaptive immunity. During exercise, intracellular homeostasis depends on the matching of adenosine triphosphate (ATP) supply and ATP demand. Metabolites play a useful role in communicating the extent of ATP demand to the metabolic supply pathways. Effects as different as proliferation or differentiation, chemotaxis, release of cytokines or lysosomal constituents, and generation of reactive oxygen or nitrogen species are elicited upon stimulation of blood cells with extracellular ATP. The increased concentration of adenosine triphosphate (ATP) in erythrocytes from patients with chronic renal failure (CRF) has been observed in many studies but the mechanism leading to these abnormalities still is controversial. (PMID: 15490415 , 15129319 , 14707763 , 14696970 , 11157473 ).
Structure
Thumb
Synonyms
ValueSource
Adenosine 5'-triphosphateChEBI
ADENOSINE-5'-triphosphATEChEBI
AdephosChEBI
AdetolChEBI
AdynolChEBI
AtipiChEBI
AtriphosChEBI
CardenosineChEBI
FosfobionChEBI
GlucobasinChEBI
H4ATPChEBI
MyotriphosChEBI
TriadenylChEBI
TriphosphadenChEBI
Adenosine 5'-triphosphoric acidGenerator
Adenosine triphosphoric acidGenerator
ADENOSINE-5'-triphosphoric acidGenerator
5'-(Tetrahydrogen triphosphate) adenosineHMDB
5'-ATPHMDB
Adenosine 5'-triphosphorateHMDB
AdenylpyrophosphorateHMDB
Adenylpyrophosphoric acidHMDB
ATPHMDB
PhosphobionHMDB
StriadyneHMDB
Triphosphoric acid adenosine esterHMDB
Adenosine triphosphate, chromium saltMeSH
CrATPMeSH
Manganese adenosine triphosphateMeSH
MgATPMeSH
MnATPMeSH
ATP MGCL2MeSH
ATP-MGCL2MeSH
Adenosine triphosphate, magnesium saltMeSH
Adenosine triphosphate, manganese saltMeSH
Magnesium adenosine triphosphateMeSH
Adenosine triphosphate, calcium saltMeSH
AdenylpyrophosphateMeSH
CaATPMeSH
CR(H2O)4 ATPMeSH
Adenosine triphosphate, chromium ammonium saltMeSH
Adenosine triphosphate, magnesium chlorideMeSH
Chromium adenosine triphosphateMeSH
Chemical FormulaC10H16N5O13P3
Average Molecular Weight507.181
Monoisotopic Molecular Weight506.995745159
IUPAC Name({[({[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy](hydroxy)phosphoryl}oxy)phosphonic acid
Traditional Nameadenosine triphosphate
CAS Registry Number56-65-5
SMILES
NC1=NC=NC2=C1N=CN2[C@@H]1O[C@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)[C@@H](O)[C@H]1O
InChI Identifier
InChI=1S/C10H16N5O13P3/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(26-10)1-25-30(21,22)28-31(23,24)27-29(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H,23,24)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChI KeyZKHQWZAMYRWXGA-KQYNXXCUSA-N
Chemical Taxonomy
DescriptionThis compound belongs to the class of organic compounds known as purine ribonucleoside triphosphates. These are purine ribobucleotides with a triphosphate group linked to the ribose moiety.
KingdomOrganic compounds
Super ClassNucleosides, nucleotides, and analogues
ClassPurine nucleotides
Sub ClassPurine ribonucleotides
Direct ParentPurine ribonucleoside triphosphates
Alternative Parents
Substituents
  • Purine ribonucleoside triphosphate
  • Purine ribonucleoside monophosphate
  • Pentose phosphate
  • Pentose-5-phosphate
  • Glycosyl compound
  • N-glycosyl compound
  • 6-aminopurine
  • Monosaccharide phosphate
  • Pentose monosaccharide
  • Imidazopyrimidine
  • Purine
  • Aminopyrimidine
  • Monoalkyl phosphate
  • Monosaccharide
  • N-substituted imidazole
  • Organic phosphoric acid derivative
  • Phosphoric acid ester
  • Imidolactam
  • Alkyl phosphate
  • Pyrimidine
  • Azole
  • Tetrahydrofuran
  • Imidazole
  • Heteroaromatic compound
  • Secondary alcohol
  • 1,2-diol
  • Organoheterocyclic compound
  • Azacycle
  • Oxacycle
  • Organooxygen compound
  • Hydrocarbon derivative
  • Organic nitrogen compound
  • Organic oxide
  • Organopnictogen compound
  • Amine
  • Primary amine
  • Organic oxygen compound
  • Alcohol
  • Organonitrogen compound
  • Aromatic heteropolycyclic compound
Molecular FrameworkAromatic heteropolycyclic compounds
External Descriptors
Ontology
Physiological effect

Health effect:

Disposition

Source:

Biological location:

Process

Naturally occurring process:

Role

Biological role:

Industrial application:

Physical Properties
StateSolid
Experimental Properties
PropertyValueReference
Melting PointNot AvailableNot Available
Boiling PointNot AvailableNot Available
Water Solubility1000 mg/mL; 862 mg/mL (magnesium salt)MERCK INDEX (1996); Human Metabolome Project (salt)
LogPNot AvailableNot Available
Predicted Properties
PropertyValueSource
Water Solubility4.49 g/LALOGPS
logP-0.84ALOGPS
logP-6ChemAxon
logS-2ALOGPS
pKa (Strongest Acidic)0.9ChemAxon
pKa (Strongest Basic)5ChemAxon
Physiological Charge-3ChemAxon
Hydrogen Acceptor Count14ChemAxon
Hydrogen Donor Count7ChemAxon
Polar Surface Area279.13 ŲChemAxon
Rotatable Bond Count8ChemAxon
Refractivity95.81 m³·mol⁻¹ChemAxon
Polarizability38.92 ųChemAxon
Number of Rings3ChemAxon
Bioavailability0ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Spectra
Spectra
Spectrum TypeDescriptionSplash Key
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positivesplash10-004j-9785600000-9d385d54b8bf3d01c79aView in MoNA
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (2 TMS) - 70eV, Positivesplash10-0f7a-2129514000-9059f6c87291f92b0cb5View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientific ) , Negativesplash10-0a4i-0131190000-316dbdca27f38ad8ee57View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientific ) , Negativesplash10-004i-0000900000-f5ffc4694dfd302fd52dView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientific ) , Negativesplash10-0a4i-0000900000-e9a09b9360491c310280View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT , negativesplash10-004i-0000900000-f5ffc4694dfd302fd52dView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT , negativesplash10-0a4i-0000900000-e9a09b9360491c310280View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-000i-0911310000-f883981fb555288ec858View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-000i-0900000000-8ed3fe63c389ec26b73fView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-000i-1900000000-96bc47060403ae952c30View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-0a59-0830290000-0774525fed54afda165aView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-001i-3930000000-a285e09b97437217cb03View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-004i-9300000000-7648d24e56aa73a5feb0View in MoNA
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
2D NMR[1H,13C] 2D NMR SpectrumNot AvailableView in JSpectraViewer
Biological Properties
Cellular Locations
  • Cytoplasm
  • Extracellular
  • Mitochondria
  • Nucleus
  • Endoplasmic reticulum
  • Peroxisome
Biospecimen Locations
  • Blood
  • Cellular Cytoplasm
  • Cerebrospinal Fluid (CSF)
  • Saliva
Tissue Locations
  • Adipose Tissue
  • Bladder
  • Fibroblasts
  • Intestine
  • Kidney
  • Muscle
  • Myelin
  • Nerve Cells
  • Neuron
  • Pancreas
  • Platelet
  • Skeletal Muscle
Pathways
Normal Concentrations
BiospecimenStatusValueAgeSexConditionReferenceDetails
BloodDetected and Quantified1077.0 +/- 210.0 uMNewborn (0-30 days old)BothNormal
    • Geigy Scientific ...
details
BloodDetected and Quantified1552.0 +/- 161.0 uMAdult (>18 years old)MaleNormal
    • Geigy Scientific ...
details
BloodDetected and Quantified1390.0 +/- 170.0 uMAdult (>18 years old)BothNormal
    • Geigy Scientific ...
details
BloodDetected and Quantified3152.0 +/- 1698.0 uMAdult (>18 years old)BothNormal details
Cellular CytoplasmDetected and Quantified1540 (1290-1790) uMAdult (>18 years old)BothNormal details
Cerebrospinal Fluid (CSF)Detected and Quantified1.85 +/- 0.03 uMAdult (>18 years old)BothNormal details
SalivaDetected and Quantified0.47 +/- 0.36 uMAdult (>18 years old)BothNormal
    • Zerihun T. Dame, ...
details
SalivaDetected and Quantified0.52 +/- 0.15 uMAdult (>18 years old)Both
Normal
details
SalivaDetected and Quantified0.47 +/- 0.15 uMAdult (>18 years old)Both
Normal
details
SalivaDetected and Quantified0.46 +/- 0.15 uMAdult (>18 years old)Both
Normal
details
Abnormal Concentrations
BiospecimenStatusValueAgeSexConditionReferenceDetails
Cerebrospinal Fluid (CSF)Detected and Quantified0.23 +/- 0.19 uMAdult (>18 years old)BothRachialgia details
Cerebrospinal Fluid (CSF)Detected and Quantified0.80 +/- 0.63 uMAdult (>18 years old)BothSubarachnoid hemorrhage details
Cerebrospinal Fluid (CSF)Detected and Quantified1.08 +/- 0.77 uMAdult (>18 years old)BothEpilepsy details
Cerebrospinal Fluid (CSF)Detected and Quantified0.26 +/- 0.11 uMAdult (>18 years old)Both
Stroke
details
Cerebrospinal Fluid (CSF)Detected and Quantified1.09 +/- 0.76 uMAdult (>18 years old)BothNeuroinfection details
Associated Disorders and Diseases
Disease References
Subarachnoid hemorrhage
  1. Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed:15993662 ]
Epilepsy
  1. Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed:15993662 ]
Neuroinfection
  1. Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed:15993662 ]
Rachialgia
  1. Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed:15993662 ]
Stroke
  1. Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed:15993662 ]
Associated OMIM IDs
DrugBank IDDB00171
Phenol Explorer Compound IDNot Available
FoodDB IDFDB021813
KNApSAcK IDC00001491
Chemspider ID5742
KEGG Compound IDC00002
BioCyc IDATP
BiGG ID33477
Wikipedia LinkAdenosine_triphosphate
METLIN ID5523
PubChem Compound5957
PDB IDATP
ChEBI ID15422
References
Synthesis ReferenceClark, V. M.; Kirby, G. W.; Todd, Alexander. Phosphorylation. XV. Use of phosphoramidic esters in acylation-new preparation of adenosine 5'-pyrophosphate and adenosine 5'-triphosphate. Journal of the Chemical Society (1957), 1497-1501.
Material Safety Data Sheet (MSDS)Not Available
General References
  1. Nakayama Y, Kinoshita A, Tomita M: Dynamic simulation of red blood cell metabolism and its application to the analysis of a pathological condition. Theor Biol Med Model. 2005 May 9;2:18. [PubMed:15882454 ]
  2. Gottlieb C, Svanborg K, Eneroth P, Bygdeman M: Effect of prostaglandins on human sperm function in vitro and seminal adenosine triphosphate content. Fertil Steril. 1988 Feb;49(2):322-7. [PubMed:3338588 ]
  3. Mahmoud AM, Comhaire FH, Vermeulen L, Andreou E: Comparison of the resazurin test, adenosine triphosphate in semen, and various sperm parameters. Hum Reprod. 1994 Sep;9(9):1688-93. [PubMed:7836519 ]
  4. Kadmon M, Klunemann C, Bohme M, Ishikawa T, Gorgas K, Otto G, Herfarth C, Keppler D: Inhibition by cyclosporin A of adenosine triphosphate-dependent transport from the hepatocyte into bile. Gastroenterology. 1993 May;104(5):1507-14. [PubMed:7683296 ]
  5. Sun Y, MaLossi J, Jacobs SC, Chai TC: Effect of doxazosin on stretch-activated adenosine triphosphate release in bladder urothelial cells from patients with benign prostatic hyperplasia. Urology. 2002 Aug;60(2):351-6. [PubMed:12137852 ]
  6. Ryan LM, Rachow JW, McCarty BA, McCarty DJ: Adenosine triphosphate levels in human plasma. J Rheumatol. 1996 Feb;23(2):214-9. [PubMed:8882021 ]
  7. Yoshida M, Miyamae K, Iwashita H, Otani M, Inadome A: Management of detrusor dysfunction in the elderly: changes in acetylcholine and adenosine triphosphate release during aging. Urology. 2004 Mar;63(3 Suppl 1):17-23. [PubMed:15013648 ]
  8. Bar-Meir M, Elpeleg ON, Saada A: Effect of various agents on adenosine triphosphate synthesis in mitochondrial complex I deficiency. J Pediatr. 2001 Dec;139(6):868-70. [PubMed:11743516 ]
  9. Mannucci L, Pastore A, Rizzo C, Piemonte F, Rizzoni G, Emma F: Impaired activity of the gamma-glutamyl cycle in nephropathic cystinosis fibroblasts. Pediatr Res. 2006 Feb;59(2):332-5. [PubMed:16439602 ]
  10. Livingston JH, Brown JK, Harkness RA, McCreanor GM: Cerebrospinal fluid nucleotide metabolites following non-convulsive status epilepticus. Dev Med Child Neurol. 1989 Apr;31(2):168-73. [PubMed:2737369 ]
  11. Rutkowski B, Swierczynski J, Slominska E, Szolkiewicz M, Smolenski RT, Marlewski M, Butto B, Rutkowski P: Disturbances of purine nucleotide metabolism in uremia. Semin Nephrol. 2004 Sep;24(5):479-83. [PubMed:15490415 ]
  12. Holzer AM, Granstein RD: Role of extracellular adenosine triphosphate in human skin. J Cutan Med Surg. 2004 Mar-Apr;8(2):90-6. Epub 2004 May 3. [PubMed:15129319 ]
  13. Myburgh KH: Can any metabolites partially alleviate fatigue manifestations at the cross-bridge? Med Sci Sports Exerc. 2004 Jan;36(1):20-7. [PubMed:14707763 ]
  14. Gartland A, Buckley KA, Hipskind RA, Bowler WB, Gallagher JA: P2 receptors in bone--modulation of osteoclast formation and activity via P2X7 activation. Crit Rev Eukaryot Gene Expr. 2003;13(2-4):237-42. [PubMed:14696970 ]
  15. Di Virgilio F, Chiozzi P, Ferrari D, Falzoni S, Sanz JM, Morelli A, Torboli M, Bolognesi G, Baricordi OR: Nucleotide receptors: an emerging family of regulatory molecules in blood cells. Blood. 2001 Feb 1;97(3):587-600. [PubMed:11157473 ]

Only showing the first 10 proteins. There are 1040 proteins in total.

Enzymes

General function:
Involved in ATP binding
Specific function:
Catalyzes specific phosphoryl transfer from ATP to UMP and CMP.
Gene Name:
CMPK1
Uniprot ID:
P30085
Molecular weight:
20180.12
Reactions
Adenosine triphosphate + (d)CMP → ADP + (d)CDPdetails
Adenosine triphosphate + Uridine 5'-monophosphate → ADP + Uridine 5'-diphosphatedetails
Adenosine triphosphate + Cytidine monophosphate → ADP + CDPdetails
Adenosine triphosphate + dCMP → ADP + dCDPdetails
General function:
Involved in ATP binding
Specific function:
Required for the phosphorylation of the deoxyribonucleosides deoxycytidine (dC), deoxyguanosine (dG) and deoxyadenosine (dA). Has broad substrate specificity, and does not display selectivity based on the chirality of the substrate. It is also an essential enzyme for the phosphorylation of numerous nucleoside analogs widely employed as antiviral and chemotherapeutic agents.
Gene Name:
DCK
Uniprot ID:
P27707
Molecular weight:
30518.315
Reactions
Adenosine triphosphate + Adenosine → ADP + Adenosine monophosphatedetails
Adenosine triphosphate + Deoxycytidine → ADP + dCMPdetails
General function:
Involved in ATP citrate synthase activity
Specific function:
ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Has a central role in de novo lipid synthesis. In nervous tissue it may be involved in the biosynthesis of acetylcholine.
Gene Name:
ACLY
Uniprot ID:
P53396
Molecular weight:
120838.27
Reactions
ADP + Phosphoric acid + Acetyl-CoA + Oxalacetic acid → Adenosine triphosphate + Citric acid + Coenzyme Adetails
Adenosine triphosphate + Citric acid + Coenzyme A → ADP + Phosphoric acid + Acetyl-CoA + Oxalacetic aciddetails
General function:
Involved in acetyl-CoA carboxylase activity
Specific function:
ACC-beta may be involved in the provision of malonyl-CoA or in the regulation of fatty acid oxidation, rather than fatty acid biosynthesis. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.
Gene Name:
ACACB
Uniprot ID:
O00763
Molecular weight:
276538.575
Reactions
Adenosine triphosphate + Acetyl-CoA + Carbonic acid → ADP + Phosphoric acid + Malonyl-CoAdetails
Adenosine triphosphate + biotin-[carboxyl-carrier-protein] + CO(2) → ADP + Phosphoric acid + carboxy-biotin-[carboxyl-carrier-protein]details
Adenosine triphosphate + Holo-[carboxylase] + Carbonic acid → ADP + Phosphoric acid + Carboxybiotin-carboxyl-carrier proteindetails
General function:
Involved in catalytic activity
Specific function:
Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second. Catalyzes in a tissue specific manner, the initial reactions of glucose (liver, kidney) and lipid (adipose tissue, liver, brain) synthesis from pyruvate.
Gene Name:
PC
Uniprot ID:
P11498
Molecular weight:
129632.565
Reactions
Adenosine triphosphate + Pyruvic acid + Carbonic acid → ADP + Phosphoric acid + Oxalacetic aciddetails
General function:
Involved in acetate-CoA ligase activity
Specific function:
Activates acetate so that it can be used for lipid synthesis or for energy generation.
Gene Name:
ACSS2
Uniprot ID:
Q9NR19
Molecular weight:
78579.11
Reactions
Adenosine triphosphate + Acetic acid + Coenzyme A → Adenosine monophosphate + Pyrophosphate + Acetyl-CoAdetails
Adenosine triphosphate + Acetic acid → Pyrophosphate + Acetyl adenylatedetails
Adenosine triphosphate + Propionic acid → Pyrophosphate + Propinol adenylatedetails
General function:
Involved in acetate-CoA ligase activity
Specific function:
Important for maintaining normal body temperature during fasting and for energy homeostasis. Essential for energy expenditure under ketogenic conditions (By similarity). Converts acetate to acetyl-CoA so that it can be used for oxidation through the tricarboxylic cycle to produce ATP and CO(2).
Gene Name:
ACSS1
Uniprot ID:
Q9NUB1
Molecular weight:
74625.88
Reactions
Adenosine triphosphate + Acetic acid + Coenzyme A → Adenosine monophosphate + Pyrophosphate + Acetyl-CoAdetails
Adenosine triphosphate + Acetic acid → Pyrophosphate + Acetyl adenylatedetails
Adenosine triphosphate + Propionic acid → Pyrophosphate + Propinol adenylatedetails
General function:
Involved in acetyl-CoA carboxylase activity
Specific function:
Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.
Gene Name:
ACACA
Uniprot ID:
Q13085
Molecular weight:
269997.01
Reactions
Adenosine triphosphate + Acetyl-CoA + Carbonic acid → ADP + Phosphoric acid + Malonyl-CoAdetails
Adenosine triphosphate + biotin-[carboxyl-carrier-protein] + CO(2) → ADP + Phosphoric acid + carboxy-biotin-[carboxyl-carrier-protein]details
Adenosine triphosphate + Holo-[carboxylase] + Carbonic acid → ADP + Phosphoric acid + Carboxybiotin-carboxyl-carrier proteindetails
General function:
Involved in thymidylate kinase activity
Specific function:
Catalyzes the conversion of dTMP to dTDP.
Gene Name:
DTYMK
Uniprot ID:
P23919
Molecular weight:
23819.105
Reactions
Adenosine triphosphate + 5-Thymidylic acid → ADP + dTDPdetails
Adenosine triphosphate + dUMP → ADP + dUDPdetails
General function:
Involved in hydrolase activity
Specific function:
In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Could also be implicated in the prevention of platelet aggregation by hydrolyzing platelet-activating ADP to AMP. Hydrolyzes ATP and ADP equally well.
Gene Name:
ENTPD1
Uniprot ID:
P49961
Molecular weight:
58706.0
Reactions
Adenosine triphosphate + Water → Adenosine monophosphate + Phosphoric aciddetails
Adenosine triphosphate + Water → ADP + Phosphoric aciddetails

Transporters

General function:
Involved in ATP binding
Specific function:
Involved in the export of copper out of the cells, such as the efflux of hepatic copper into the bile.
Gene Name:
ATP7B
Uniprot ID:
P35670
Molecular weight:
157261.34
General function:
Involved in ATP binding
Specific function:
May supply copper to copper-requiring proteins within the secretory pathway, when localized in the trans-Golgi network. Under conditions of elevated extracellular copper, it relocalized to the plasma membrane where it functions in the efflux of copper from cells.
Gene Name:
ATP7A
Uniprot ID:
Q04656
Molecular weight:
163372.275
General function:
Involved in ATP binding
Specific function:
Involved 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
Gene Name:
TAP1
Uniprot ID:
Q03518
Molecular weight:
87216.9

Only showing the first 10 proteins. There are 1040 proteins in total.