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Record Information
Version3.6
Creation Date2005-11-16 15:48:42 UTC
Update Date2013-05-29 22:36:32 UTC
HMDB IDHMDB01532
Secondary Accession NumbersNone
Metabolite Identification
Common NameDeoxyadenosine triphosphate
DescriptionDeoxyadenosine triphosphate (dATP) is a purine nucleoside triphosphate used in cells for DNA synthesis. A nucleoside triphosphate is a molecule type that contains a nucleoside with three phosphates bound to it. dATP contains the sugar deoxyribose, a precursor in DNA synthesis whereby the two existing phosphate groups are cleaved with the remaining deoxyadenosine monophosphate being incorporated into DNA during replication. Due to its enzymatic incorporation into DNA, photoreactive dATP analogs such as N6-[4-azidobenzoyl–(2-aminoethyl)]-2′-deoxyadenosine-5′-triphosphate (AB-dATP) and N6-[4-[3-(trifluoromethyl)-diazirin-3-yl]benzoyl-(2-aminoethyl)]-2′-deoxyadenosine-5′-triphosphate (DB-dATP) have been used for DNA photoaffinity labeling.
Structure
Thumb
Synonyms
  1. 2'-Deoxy-5'-ATP
  2. 2'-Deoxy-ATP
  3. 2'-Deoxyadenosine 5'-triphosphate
  4. 2'-Deoxyadenosine triphosphate
  5. dATP
  6. Deoxy-ATP
  7. Deoxyadenosine 5'-triphosphate
  8. Deoxyadenosine triphosphate
  9. Deoxyadenosine-triphosphate
Chemical FormulaC10H16N5O12P3
Average Molecular Weight491.1816
Monoisotopic Molecular Weight491.000830537
IUPAC Name({[({[(2R,3S,5R)-5-(6-amino-9H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy](hydroxy)phosphoryl}oxy)phosphonic acid
Traditional IUPAC Name({[(2R,3S,5R)-5-(6-aminopurin-9-yl)-3-hydroxyoxolan-2-yl]methoxy(hydroxy)phosphoryl}oxy(hydroxy)phosphoryl)oxyphosphonic acid
CAS Registry Number1927-31-7
SMILES
NC1=NC=NC2=C1N=CN2[C@H]1C[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1
InChI Identifier
InChI=1S/C10H16N5O12P3/c11-9-8-10(13-3-12-9)15(4-14-8)7-1-5(16)6(25-7)2-24-29(20,21)27-30(22,23)26-28(17,18)19/h3-7,16H,1-2H2,(H,20,21)(H,22,23)(H2,11,12,13)(H2,17,18,19)/t5-,6+,7+/m0/s1
InChI KeySUYVUBYJARFZHO-RRKCRQDMSA-N
Chemical Taxonomy
KingdomOrganic Compounds
Super ClassNucleosides, Nucleotides, and Analogues
ClassPurine Nucleotides
Sub ClassPurine Deoxyribonucleotides
Other Descriptors
  • 2'-deoxyadenosine 5'-phosphate(ChEBI)
  • Aromatic Heteropolycyclic Compounds
  • Deoxyribonucleotides(KEGG)
  • Organic Compounds
  • purine 2'-deoxyribonucleoside 5'-triphosphate(ChEBI)
Substituents
  • Aminopyrimidine
  • Imidazole
  • Imidazopyrimidine
  • Organic Hypophosphite
  • Organic Phosphite
  • Organic Pyrophosphate
  • Oxolane
  • Phosphoric Acid Ester
  • Purine
  • Pyrimidine
  • Secondary Alcohol
Direct ParentPurine 2'-deoxyribonucleoside Triphosphates
Ontology
StatusExpected and Not Quantified
Origin
  • Endogenous
Biofunction
  • DNA component
ApplicationNot Available
Cellular locations
  • Mitochondria
  • Nucleus
Physical Properties
StateSolid
Experimental Properties
PropertyValueReference
Melting PointNot AvailableNot Available
Boiling PointNot AvailableNot Available
Water SolubilityNot AvailableNot Available
LogPNot AvailableNot Available
Predicted Properties
PropertyValueSource
water solubility3.83 g/LALOGPS
logP-0.66ALOGPS
logP-5.3ChemAxon
logS-2.1ALOGPS
pKa (strongest acidic)0.9ChemAxon
pKa (strongest basic)5.01ChemAxon
physiological charge-3ChemAxon
hydrogen acceptor count13ChemAxon
hydrogen donor count6ChemAxon
polar surface area258.9ChemAxon
rotatable bond count8ChemAxon
refractivity94.3ChemAxon
polarizability38.05ChemAxon
Spectra
SpectraMS/MS1D NMR2D NMR
Biological Properties
Cellular Locations
  • Mitochondria
  • Nucleus
Biofluid LocationsNot Available
Tissue Location
  • Erythrocyte
  • Lymphocyte
  • T-Lymphocyte
Pathways
NameSMPDB LinkKEGG Link
Purine MetabolismSMP00050map00230
Normal Concentrations
Not Available
Abnormal Concentrations
Not Available
Associated Disorders and Diseases
Disease ReferencesNone
Associated OMIM IDsNone
DrugBank IDNot Available
DrugBank Metabolite IDNot Available
Phenol Explorer Compound IDNot Available
Phenol Explorer Metabolite IDNot Available
FoodDB IDFDB022674
KNApSAcK IDNot Available
Chemspider ID15194
KEGG Compound IDC00131
BioCyc IDDATP
BiGG ID33969
Wikipedia LinkDeoxyadenosine triphosphate
NuGOwiki LinkHMDB01532
Metagene LinkHMDB01532
METLIN ID6303
PubChem Compound15993
PDB IDDTP
ChEBI ID16284
References
Synthesis ReferenceMunch-Petersen, Agnete. Formation in vitro of deoxyadenosine triphosphate from deoxyadenosine in Ehrlich ascites cells. Biochemical and Biophysical Research Communications (1960), 3 392-6.
Material Safety Data Sheet (MSDS)Download (PDF)
General References
  1. Nespoli L, Porta F, Locatelli F, Aversa F, Carotti A, Lanfranchi A, Gibardi A, Marchesi ME, Abate L, Martelli MF, et al.: Successful lectin-separated bone marrow transplantation in adenosine deaminase deficiency-related severe immunodeficiency. Haematologica. 1990 Nov-Dec;75(6):546-50. Pubmed: 2098297
  2. Hoffbrand AV, Ganeshaguru K, Hooton JW, Tattersall MH: Effect of iron deficiency and desferrioxamine on DNA synthesis in human cells. Br J Haematol. 1976 Aug;33(4):517-26. Pubmed: 1009024
  3. Waddell D, Ullman B: Characterization of a cultured human T-cell line with genetically altered ribonucleotide reductase activity. Model for immunodeficiency. J Biol Chem. 1983 Apr 10;258(7):4226-31. Pubmed: 6339493
  4. Bory C, Boulieu R, Souillet G, Chantin C, Guibaud P, Hershfield MS: Effect of polyethylene glycol-modified adenosine deaminase (PEG-ADA) therapy in two ADA-deficient children: measurement of erythrocyte deoxyadenosine triphosphate as a useful tool. Adv Exp Med Biol. 1991;309A:173-6. Pubmed: 1789201
  5. Dang-Vu AP, Olsen EA, Vollmer RT, Greenberg ML, Hershfield MS: Treatment of cutaneous T cell lymphoma with 2'-deoxycoformycin (pentostatin). J Am Acad Dermatol. 1988 Oct;19(4):692-8. Pubmed: 3263401
  6. Donofrio J, Coleman MS, Hutton JJ, Daoud A, Lampkin B, Dyminski J: Overproduction of adenine deoxynucleosides and deoxynucletides in adenosine deaminase deficiency with severe combined immunodeficiency disease. J Clin Invest. 1978 Oct;62(4):884-7. Pubmed: 308954
  7. Cowan MJ, Shannon KM, Wara DW, Ammann AJ: Rejection of bone marrow transplant and resistance of alloantigen reactive cells to in vivo deoxyadenosine in adenosine deaminase deficiency. Clin Immunol Immunopathol. 1988 Nov;49(2):242-50. Pubmed: 2971490
  8. Grever MR, Siaw MF, Jacob WF, Neidhart JA, Miser JS, Coleman MS, Hutton JJ, Balcerzak SP: The biochemical and clinical consequences of 2'-deoxycoformycin in refractory lymphoproliferative malignancy. Blood. 1981 Mar;57(3):406-17. Pubmed: 6970050
  9. Simmonds HA, Fairbanks LD, Morris GS, Webster DR, Harley EH: Altered erythrocyte nucleotide patterns are characteristic of inherited disorders of purine or pyrimidine metabolism. Clin Chim Acta. 1988 Feb 15;171(2-3):197-210. Pubmed: 3370820
  10. Hirschhorn R, Roegner V, Rubinstein A, Papageorgiou P: Plasma deoxyadenosine, adenosine, and erythrocyte deoxyATP are elevated at birth in an adenosine deaminase-deficient child. J Clin Invest. 1980 Mar;65(3):768-71. Pubmed: 6965496
  11. Schmalstieg FC, Mills GC, Tsuda H, Goldman AS: Severe combined immunodeficiency in a child with a healthy adenosine deaminase deficient mother. Pediatr Res. 1983 Dec;17(12):935-40. Pubmed: 6606796
  12. Simmonds HA, Webster DR, Perrett D, Reiter S, Levinsky RJ: Formation and degradation of deoxyadenosine nucleotides in inherited adenosine deaminase deficiency. Biosci Rep. 1982 May;2(5):303-14. Pubmed: 6980023
  13. Simmonds HA, Sahota A, Potter CF, Perrett D, Hugh-Jones K, Watson JG: Purine metabolism in adenosine deaminase deficiency. Ciba Found Symp. 1978;(68):255-62. Pubmed: 387357
  14. Hirschhorn R, Roegner-Maniscalco V, Kuritsky L, Rosen FS: Bone marrow transplantation only partially restores purine metabolites to normal in adenosine deaminase-deficient patients. J Clin Invest. 1981 Dec;68(6):1387-93. Pubmed: 7033281
  15. Goday A, Simmonds HA, Webster DR, Levinsky RJ, Watson AR, Hoffbrand AV: Importance of platelet-free preparations for evaluating lymphocyte nucleotide levels in inherited or acquired immunodeficiency syndromes. Clin Sci (Lond). 1983 Dec;65(6):635-43. Pubmed: 6414755
  16. Chen SH, Ochs HD, Scott CR, Giblett ER, Tingle AJ: Adenosine deaminase deficiency: disappearance of adenine deoxynucleotides from a patient's erythrocytes after successful marrow transplantation. J Clin Invest. 1978 Dec;62(6):1386-9. Pubmed: 372236
  17. Gruber HE, Cohen AH, Firestein GS, Redelman D, Bluestein HG: Deoxy-ATP accumulation in adenosine deaminase-inhibited human B and T lymphocytes. Adv Exp Med Biol. 1986;195 Pt A:503-7. Pubmed: 3487921
  18. Bory C, Boulieu R, Souillet G, Chantin C, Rolland MO, Mathieu M, Hershfield M: Comparison of red cell transfusion and polyethylene glycol-modified adenosine deaminase therapy in an adenosine deaminase-deficient child: measurement of erythrocyte deoxyadenosine triphosphate as a useful tool. Pediatr Res. 1990 Aug;28(2):127-30. Pubmed: 2395602
  19. Peters GJ, De Abreu RA, Oosterhof A, Veerkamp JH: Concentration of nucleotides and deoxynucleotides in peripheral and phytohemagglutinin-stimulated mammalian lymphocytes. Effects of adenosine and deoxyadenosine. Biochim Biophys Acta. 1983 Aug 23;759(1-2):7-15. Pubmed: 6603870
  20. Morgan G, Levinsky RJ, Hugh-Jones K, Fairbanks LD, Morris GS, Simmonds HA: Heterogeneity of biochemical, clinical and immunological parameters in severe combined immunodeficiency due to adenosine deaminase deficiency. Clin Exp Immunol. 1987 Dec;70(3):491-9. Pubmed: 3436096
  21. Zofall M, Bartholomew B: Two novel dATP analogs for DNA photoaffinity labeling. Nucleic Acids Res. 2000 Nov 1;28(21):4382-90. Pubmed: 11058139

Enzymes

General function:
Involved in ATP binding
Specific function:
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, N(4)-acetylcytidine, N(4)-benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5-methylcytidine, and N(4)-anisoylcytidine.
Gene Name:
UCK1
Uniprot ID:
Q9HA47
Molecular weight:
22760.43
Reactions
Deoxyadenosine triphosphate + Cytidine → dADP + Cytidine monophosphatedetails
Deoxyadenosine triphosphate + Uridine → dADP + Uridine 5'-monophosphatedetails
General function:
Involved in nucleoside diphosphate kinase activity
Specific function:
Major role in the synthesis of nucleoside triphosphates other than ATP (By similarity).
Gene Name:
NME4
Uniprot ID:
O00746
Molecular weight:
20658.45
Reactions
Adenosine triphosphate + dADP → ADP + Deoxyadenosine triphosphatedetails
General function:
Involved in nucleoside diphosphate kinase activity
Specific function:
Major role in the synthesis of nucleoside triphosphates other than ATP. Possesses nucleoside-diphosphate kinase, serine/threonine-specific protein kinase, geranyl and farnesyl pyrophosphate kinase, histidine protein kinase and 3'-5' exonuclease activities. Involved in cell proliferation, differentiation and development, signal transduction, G protein-coupled receptor endocytosis, and gene expression. Required for neural development including neural patterning and cell fate determination.
Gene Name:
NME1
Uniprot ID:
P15531
Molecular weight:
17148.635
Reactions
Adenosine triphosphate + dADP → ADP + Deoxyadenosine triphosphatedetails
General function:
Involved in nucleoside diphosphate kinase activity
Specific function:
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Gene Name:
NME7
Uniprot ID:
Q9Y5B8
Molecular weight:
42491.365
Reactions
Adenosine triphosphate + dADP → ADP + Deoxyadenosine triphosphatedetails
General function:
Involved in nucleoside diphosphate kinase activity
Specific function:
Major role in the synthesis of nucleoside triphosphates other than ATP. Negatively regulates Rho activity by interacting with AKAP13/LBC. Acts as a transcriptional activator of the MYC gene; binds DNA non-specifically (PubMed:8392752). Exhibits histidine protein kinase activity.
Gene Name:
NME2
Uniprot ID:
P22392
Molecular weight:
30136.92
Reactions
Adenosine triphosphate + dADP → ADP + Deoxyadenosine triphosphatedetails
General function:
Involved in nucleoside diphosphate kinase activity
Specific function:
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Probably has a role in normal hematopoiesis by inhibition of granulocyte differentiation and induction of apoptosis.
Gene Name:
NME3
Uniprot ID:
Q13232
Molecular weight:
19014.85
Reactions
Adenosine triphosphate + dADP → ADP + Deoxyadenosine triphosphatedetails
General function:
Involved in nucleoside diphosphate kinase activity
Specific function:
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Inhibitor of p53-induced apoptosis.
Gene Name:
NME6
Uniprot ID:
O75414
Molecular weight:
22002.965
Reactions
Adenosine triphosphate + dADP → ADP + Deoxyadenosine triphosphatedetails
General function:
Involved in ATP binding
Specific function:
Catalyzes the initial step in utilization of glucose by the beta-cell and liver at physiological glucose concentration. Glucokinase has a high Km for glucose, and so it is effective only when glucose is abundant. The role of GCK is to provide G6P for the synthesis of glycogen. Pancreatic glucokinase plays an important role in modulating insulin secretion. Hepatic glucokinase helps to facilitate the uptake and conversion of glucose by acting as an insulin-sensitive determinant of hepatic glucose usage.
Gene Name:
GCK
Uniprot ID:
P35557
Molecular weight:
52191.07
General function:
Involved in ATP binding
Specific function:
Not Available
Gene Name:
HK3
Uniprot ID:
P52790
Molecular weight:
99024.56
General function:
Involved in ATP binding
Specific function:
Not Available
Gene Name:
HK2
Uniprot ID:
P52789
Molecular weight:
102379.06
General function:
Involved in magnesium ion binding
Specific function:
Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation. Plays a general role in caspase independent cell death of tumor cells. The ratio betwween the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival.
Gene Name:
PKM
Uniprot ID:
P14618
Molecular weight:
65930.14
Reactions
Deoxyadenosine triphosphate + Pyruvic acid → dADP + Phosphoenolpyruvic aciddetails
General function:
Involved in magnesium ion binding
Specific function:
Plays a key role in glycolysis (By similarity).
Gene Name:
PKLR
Uniprot ID:
P30613
Molecular weight:
61829.575
Reactions
Deoxyadenosine triphosphate + Pyruvic acid → dADP + Phosphoenolpyruvic aciddetails
General function:
Involved in DNA binding
Specific function:
Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases.
Gene Name:
POLB
Uniprot ID:
P06746
Molecular weight:
38177.34
General function:
Involved in nucleotide binding
Specific function:
Plays an essential role in the initiation of DNA replication. During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit POLA1/p180, a regulatory subunit POLA2/p70 and two primase subunits PRIM1/p49 and PRIM2/p58) is recruited to DNA at the replicative forks via direct interactions with MCM10 and WDHD1. The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands. These primers are initially extended by the polymerase alpha catalytic subunit and subsequently transferred to polymerase delta and polymerase epsilon for processive synthesis on the lagging and leading strand, respectively. The reason this transfer occurs is because the polymerase alpha has limited processivity and lacks intrinsic 3' exonuclease activity for proofreading error, and therefore is not well suited for replicating long complexes.
Gene Name:
POLA1
Uniprot ID:
P09884
Molecular weight:
165911.405
Reactions
Deoxyadenosine triphosphate + DNA → Pyrophosphate + DNAdetails
General function:
Involved in protein binding
Specific function:
Required for optimal DNA polymerase delta activity
Gene Name:
POLD3
Uniprot ID:
Q15054
Molecular weight:
51400.0
General function:
Involved in DNA binding
Specific function:
Repair polymerase. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Has both DNA polymerase and terminal transferase activities. Has a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.
Gene Name:
POLL
Uniprot ID:
Q9UGP5
Molecular weight:
63481.66
General function:
Involved in sequence-specific DNA binding
Specific function:
May play a role in allowing polymerase epsilon to carry out its replication and/or repair function.
Gene Name:
POLE4
Uniprot ID:
Q9NR33
Molecular weight:
12208.63
Reactions
Deoxyadenosine triphosphate + DNA → Pyrophosphate + DNAdetails
General function:
Involved in damaged DNA binding
Specific function:
DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Plays an important role in the repair of UV-induced pyrimidine dimers. Depending on the context, it inserts the correct base, but causes frequent base transitions and transversions. May play a role in hypermutation at immunoglobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity. Targets POLI to replication foci.
Gene Name:
POLH
Uniprot ID:
Q9Y253
Molecular weight:
78412.77
General function:
Involved in nucleotide binding
Specific function:
Possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single stranded DNA in the 3'- to 5'-direction. Required with its accessory proteins (proliferating cell nuclear antigen (PCNA) and replication factor C (RFC) or activator 1) for leading strand synthesis. Also involved in completing Okazaki fragments initiated by the DNA polymerase alpha/primase complex.
Gene Name:
POLD1
Uniprot ID:
P28340
Molecular weight:
123629.95
Reactions
Deoxyadenosine triphosphate + DNA → Pyrophosphate + DNAdetails
General function:
Involved in nucleotide binding
Specific function:
Interacts with MAD2L2 to form the error prone DNA polymerase zeta involved in translesion DNA synthesis.
Gene Name:
REV3L
Uniprot ID:
O60673
Molecular weight:
352772.565
General function:
Involved in nucleotide binding
Specific function:
Participates in DNA repair and in chromosomal DNA replication.
Gene Name:
POLE
Uniprot ID:
Q07864
Molecular weight:
261515.525
Reactions
Deoxyadenosine triphosphate + DNA → Pyrophosphate + DNAdetails
General function:
Involved in DNA binding
Specific function:
Gap-filling polymerase involved in repair of DNA double-strand breaks by non-homologous end joining (NHEJ). Participates in immunoglobulin (Ig) light chain gene rearrangement in V(D)J recombination.
Gene Name:
POLM
Uniprot ID:
Q9NP87
Molecular weight:
54815.075
General function:
Involved in damaged DNA binding
Specific function:
DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Depending on the context, it inserts the correct base, but causes frequent base transitions, transversions and frameshifts. Lacks 3'-5' proofreading exonuclease activity. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity.
Gene Name:
POLK
Uniprot ID:
Q9UBT6
Molecular weight:
98807.815
General function:
Involved in sequence-specific DNA binding
Specific function:
Forms a complex with DNA polymerase epsilon subunit CHRAC1 and binds naked DNA, which is then incorporated into chromatin, aided by the nucleosome-remodeling activity of ISWI/SNF2H and ACF1.
Gene Name:
POLE3
Uniprot ID:
Q9NRF9
Molecular weight:
16859.4
Reactions
Deoxyadenosine triphosphate + DNA → Pyrophosphate + DNAdetails
General function:
Involved in DNA binding
Specific function:
Involved in the replication of mitochondrial DNA. Associates with mitochondrial DNA.
Gene Name:
POLG
Uniprot ID:
P54098
Molecular weight:
139561.06
General function:
Involved in damaged DNA binding
Specific function:
Error-prone DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Favors Hoogsteen base-pairing in the active site. Inserts the correct base with high-fidelity opposite an adenosine template. Exhibits low fidelity and efficiency opposite a thymidine template, where it will preferentially insert guanosine. May play a role in hypermutation of immunogobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but may not have lyase activity.
Gene Name:
POLI
Uniprot ID:
Q9UNA4
Molecular weight:
83005.335
General function:
Involved in DNA binding
Specific function:
Participates in DNA repair and in chromosomal DNA replication.
Gene Name:
POLE2
Uniprot ID:
P56282
Molecular weight:
56417.05
Reactions
Deoxyadenosine triphosphate + DNA → Pyrophosphate + DNAdetails
General function:
Involved in protein binding
Specific function:
Oligomeric 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
Gene Name:
APAF1
Uniprot ID:
O14727
Molecular weight:
141838.8
General function:
Involved in ATP binding
Specific function:
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, N(4)-acetylcytidine, N(4)-benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5-methylcytidine, and N(4)-anisoylcytidine.
Gene Name:
UCK2
Uniprot ID:
Q9BZX2
Molecular weight:
29298.92
Reactions
Deoxyadenosine triphosphate + Cytidine → dADP + Cytidine monophosphatedetails
Deoxyadenosine triphosphate + Uridine → dADP + Uridine 5'-monophosphatedetails
General function:
Involved in ATP binding
Specific function:
May contribute to UTP accumulation needed for blast transformation and proliferation.
Gene Name:
UCKL1
Uniprot ID:
Q9NWZ5
Molecular weight:
59465.77
Reactions
Deoxyadenosine triphosphate + Cytidine → dADP + Cytidine monophosphatedetails
Deoxyadenosine triphosphate + Uridine → dADP + Uridine 5'-monophosphatedetails
General function:
Involved in binding
Specific function:
May activate or repress transcription via interactions with sequence specific DNA-binding proteins. Repression may be mediated at least in part by histone deacetylase activity (HDAC activity)
Gene Name:
MYBBP1A
Uniprot ID:
Q9BQG0
Molecular weight:
148853.2
General function:
Involved in DNA binding
Specific function:
Has a DNA polymerase activity on nicked double-stranded DNA and on a singly primed DNA template. The enzyme activity is resistant to aphidicolin, and inhibited by dideoxynucleotides. Exhibites a single-stranded DNA-dependent ATPase activity. Could be involved in the repair of interstrand cross-links.
Gene Name:
POLQ
Uniprot ID:
O75417
Molecular weight:
289616.715
General function:
Not Available
Specific function:
The function of the small subunit is not yet clear.
Gene Name:
POLD2
Uniprot ID:
P49005
Molecular weight:
51289.0
Reactions
Deoxyadenosine triphosphate + DNA → Pyrophosphate + DNAdetails
General function:
Not Available
Specific function:
Does not seem to have NDK kinase activity. Confers protection from cell death by Bax and alters the cellular levels of several antioxidant enzymes including Gpx5. May play a role in spermiogenesis by increasing the ability of late-stage spermatids to eliminate reactive oxygen species (By similarity).
Gene Name:
NME5
Uniprot ID:
P56597
Molecular weight:
Not Available
Reactions
Adenosine triphosphate + dADP → ADP + Deoxyadenosine triphosphatedetails
General function:
Not Available
Specific function:
DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication.
Gene Name:
PRIM1
Uniprot ID:
P49642
Molecular weight:
Not Available
Reactions
Deoxyadenosine triphosphate + DNA → Pyrophosphate + DNAdetails
General function:
Not Available
Specific function:
DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication.
Gene Name:
PRIM2
Uniprot ID:
P49643
Molecular weight:
Not Available
Reactions
Deoxyadenosine triphosphate + DNA → Pyrophosphate + DNAdetails