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Record Information
Version3.6
Creation Date2005-11-16 15:48:42 UTC
Update Date2014-10-29 17:07:09 UTC
HMDB IDHMDB00250
Secondary Accession NumbersNone
Metabolite Identification
Common NamePyrophosphate
DescriptionIn chemistry, the anion, the salts, and the esters of pyrophosphoric acid are called pyrophosphates. The anion is abbreviated PPi and is formed by the hydrolysis of ATP into AMP in cells. This hydrolysis is called pyrophosphorolysis. The pyrophosphate anion has the structure P2O74-, and is an acid anhydride of phosphate. It is unstable in aqueous solution and rapidly hydrolyzes into inorganic phosphate.
Structure
Thumb
Synonyms
  1. (4-)Diphosphoric acid ion
  2. (P2O74-)Diphosphate
  3. Diphosphate
  4. Diphosphoric acid
  5. PPi
  6. Pyrometaphosphate
  7. Pyrophosphate
  8. Pyrophosphate tetraanion
  9. Pyrophosphate(4-) ion
Chemical FormulaO7P2
Average Molecular Weight173.9433
Monoisotopic Molecular Weight173.911925378
IUPAC Name(phosphonatooxy)phosphonate
Traditional Namephosphonatooxyphosphonate
CAS Registry Number14000-31-8
SMILES
[O-]P([O-])(=O)OP([O-])([O-])=O
InChI Identifier
InChI=1S/H4O7P2/c1-8(2,3)7-9(4,5)6/h(H2,1,2,3)(H2,4,5,6)/p-4
InChI KeyXPPKVPWEQAFLFU-UHFFFAOYSA-J
Chemical Taxonomy
KingdomInorganic Compounds
Super ClassHomogeneous Non-metal Compounds
ClassNon-metal Oxoanionic Compounds
Sub ClassNon-metal Pyrophosphates
Other Descriptors
  • phosphorus oxoanion(ChEBI)
Substituents
  • N/A
Direct ParentNon-metal Pyrophosphates
Ontology
StatusDetected and Quantified
Origin
  • Endogenous
Biofunction
  • Component of Alanine and aspartate metabolism
  • Component of Aminoacyl-tRNA biosynthesis
  • Component of Aminophosphonate metabolism
  • Component of Aminosugars metabolism
  • Component of Arginine and proline metabolism
  • Component of Biotin metabolism
  • Component of Fatty acid metabolism
  • Component of Folate biosynthesis
  • Component of Fructose and mannose metabolism
  • Component of Galactose metabolism
  • Component of Glutamate metabolism
  • Component of Glycerophospholipid metabolism
  • Component of Glycine, serine and threonine metabolism
  • Component of Histidine metabolism
  • Component of Lysine biosynthesis
  • Component of Methionine metabolism
  • Component of Nicotinate and nicotinamide metabolism
  • Component of Nitrogen metabolism
  • Component of Nucleotide sugars metabolism
  • Component of Phenylalanine, tyrosine and tryptophan biosynthesis
  • Component of Porphyrin and chlorophyll metabolism
  • Component of Propanoate metabolism
  • Component of Purine metabolism
  • Component of Pyrimidine metabolism
  • Component of Pyruvate metabolism
  • Component of Selenoamino acid metabolism
  • Component of Starch and sucrose metabolism
  • Component of Sulfur metabolism
  • Component of Terpenoid biosynthesis
  • Component of Tryptophan metabolism
  • Component of Valine, leucine and isoleucine biosynthesis
ApplicationNot Available
Cellular locations
  • Cytoplasm
  • Mitochondria
  • Nucleus
  • Endoplasmic reticulum
  • Peroxisome
Physical Properties
StateSolid
Experimental Properties
PropertyValueReference
Melting Point61 °CNot Available
Boiling PointNot AvailableNot Available
Water SolubilityNot AvailableNot Available
LogPNot AvailableNot Available
Predicted Properties
PropertyValueSource
logP-1.4ChemAxon
pKa (Strongest Acidic)1.7ChemAxon
Physiological Charge-3ChemAxon
Hydrogen Acceptor Count6ChemAxon
Hydrogen Donor Count0ChemAxon
Polar Surface Area135.61ChemAxon
Rotatable Bond Count2ChemAxon
Refractivity21.04ChemAxon
Polarizability9.03ChemAxon
Spectra
SpectraGC-MSMS/MS
Biological Properties
Cellular Locations
  • Cytoplasm
  • Mitochondria
  • Nucleus
  • Endoplasmic reticulum
  • Peroxisome
Biofluid Locations
  • Blood
  • Saliva
  • Urine
Tissue Location
  • Epidermis
  • Fibroblasts
  • Intestine
  • Neuron
  • Platelet
  • Prostate
  • Skeletal Muscle
  • Testes
Pathways
NameSMPDB LinkKEGG Link
Transcription/TranslationSMP00019Not Available
Normal Concentrations
BiofluidStatusValueAgeSexConditionReferenceDetails
BloodDetected and Quantified1.8 (0.64-2.96) uMAdult (>18 years old)BothNormal
    • Geigy Scientific ...
details
SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
Normal
details
UrineDetected and Quantified2.56 +/- 1.22 umol/mmol creatinineChildren (1-13 years old)BothNormal
    • Geigy Scientific ...
details
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 IDFDB021918
KNApSAcK IDNot Available
Chemspider ID559142
KEGG Compound IDC00013
BioCyc IDPPI
BiGG ID33511
Wikipedia LinkPyrophosphate
NuGOwiki LinkHMDB00250
Metagene LinkHMDB00250
METLIN ID3306
PubChem Compound644102
PDB IDDPO
ChEBI ID18361
References
Synthesis ReferenceDittmer, Donald C.; Silverstein, V. Opshelor. Production of pyrophosphate from S-n-butyl phosphorothioate. Journal of Organic Chemistry (1961), 26 4706-7.
Material Safety Data Sheet (MSDS)Download (PDF)
General References
  1. Kosoglou T, Statkevich P, Johnson-Levonas AO, Paolini JF, Bergman AJ, Alton KB: Ezetimibe: a review of its metabolism, pharmacokinetics and drug interactions. Clin Pharmacokinet. 2005;44(5):467-94. Pubmed: 15871634
  2. Sreekumar A, Poisson LM, Rajendiran TM, Khan AP, Cao Q, Yu J, Laxman B, Mehra R, Lonigro RJ, Li Y, Nyati MK, Ahsan A, Kalyana-Sundaram S, Han B, Cao X, Byun J, Omenn GS, Ghosh D, Pennathur S, Alexander DC, Berger A, Shuster JR, Wei JT, Varambally S, Beecher C, Chinnaiyan AM: Metabolomic profiles delineate potential role for sarcosine in prostate cancer progression. Nature. 2009 Feb 12;457(7231):910-4. Pubmed: 19212411
  3. Broll H: [Effect of chloroquine diphosphate on the superhelix structure of DNA and protein synthesis in synovial cells in chronic polyarthritis] Wien Klin Wochenschr. 1983 Dec 23;95(24):877-80. Pubmed: 6670282
  4. Golanski J, Pluta J, Baraniak J, Watala C: Limited usefulness of the PFA-100 for the monitoring of ADP receptor antagonists--in vitro experience. Clin Chem Lab Med. 2004 Jan;42(1):25-9. Pubmed: 15061376
  5. Mateos-Trigos G, Evans RJ, Heath MF: Effects of P2Y(1) and P2Y(12) receptor antagonists on ADP-induced shape change of equine platelets: comparison with human platelets. Platelets. 2002 Aug-Sep;13(5-6):285-92. Pubmed: 12189014
  6. Sirkis SI: [Serum and cerebrospinal fluid enzyme spectra in meningitis and their differential diagnostic value] Zh Nevropatol Psikhiatr Im S S Korsakova. 1982;82(2):193-7. Pubmed: 7072418
  7. Barbier O, Torra IP, Sirvent A, Claudel T, Blanquart C, Duran-Sandoval D, Kuipers F, Kosykh V, Fruchart JC, Staels B: FXR induces the UGT2B4 enzyme in hepatocytes: a potential mechanism of negative feedback control of FXR activity. Gastroenterology. 2003 Jun;124(7):1926-40. Pubmed: 12806625
  8. March JG, Simonet BM, Grases F: Determination of pyrophosphate in renal calculi and urine by means of an enzymatic method. Clin Chim Acta. 2001 Dec;314(1-2):187-94. Pubmed: 11718694
  9. Namiki M, Kitamura M, Nonomura N, Sugao H, Nakamura M, Okuyama A, Utsunomiya M, Itatani H, Matsumoto K, Sonoda T: Direct inhibitory effect of estrogen on the human testis in vitro. Arch Androl. 1988;20(2):131-5. Pubmed: 3395157
  10. Pickett DA, Welch DF: Recognition of Staphylococcus saprophyticus in urine cultures by screening colonies for production of phosphatase. J Clin Microbiol. 1985 Mar;21(3):310-3. Pubmed: 2984240
  11. Hua HT, Albadawi H, Entabi F, Conrad M, Stoner MC, Meriam BT, Sroufe R, Houser S, Lamuraglia GM, Watkins MT: Polyadenosine diphosphate-ribose polymerase inhibition modulates skeletal muscle injury following ischemia reperfusion. Arch Surg. 2005 Apr;140(4):344-51; discussion 351-2. Pubmed: 15837884
  12. Dahlmann N, Ueckermann C: Separation of deoxythymidine-5'-triphosphatase from unspecific hydrolases. A recommended micromethod in the diagnostic evaluation of human carcinoma. Anticancer Res. 1984 Jul-Oct;4(4-5):299-303. Pubmed: 6091528
  13. Ebadi M, Sharma SK, Ghafourifar P, Brown-Borg H, El Refaey H: Peroxynitrite in the pathogenesis of Parkinson's disease and the neuroprotective role of metallothioneins. Methods Enzymol. 2005;396:276-98. Pubmed: 16291239
  14. Tallaksen CM, Sande A, Bohmer T, Bell H, Karlsen J: Kinetics of thiamin and thiamin phosphate esters in human blood, plasma and urine after 50 mg intravenously or orally. Eur J Clin Pharmacol. 1993;44(1):73-8. Pubmed: 8436160
  15. Zhong D, Meins J, Scheidel B, Blume H: [Development of an HPLC method for determination of chloroquine in plasma] Pharmazie. 1993 May;48(5):349-52. Pubmed: 8327563
  16. Recio JA, Paez JG, Maskeri B, Loveland M, Velasco JA, Notario V: Both normal and transforming PCPH proteins have guanosine diphosphatase activity but only the oncoprotein cooperates with Ras in activating extracellular signal-regulated kinase ERK1. Cancer Res. 2000 Mar 15;60(6):1720-8. Pubmed: 10749145
  17. Puri RN, Colman RF, Colman RW: Modulation of platelet responses by 2-[3-(bromo-2-oxopropylthio)]adenosine-5'-diphosphate involves its binding to as well as covalent modification of an ADP-receptor, aggregin. Arch Biochem Biophys. 1997 Jul 1;343(1):140-5. Pubmed: 9210656
  18. Hamagishi Y, Oki T, Tone H, Inui T: A radioimmunoassay for guanosine-5'-diphosphate-3'-diphosphate and adenosine-5'-triphosphate-3'-diphosphate. J Biochem (Tokyo). 1980 Dec;88(6):1785-92. Pubmed: 6780546
  19. Lee AY, Youm YH, Kim NH, Yang H, Choi WI: Keratinocytes in the depigmented epidermis of vitiligo are more vulnerable to trauma (suction) than keratinocytes in the normally pigmented epidermis, resulting in their apoptosis. Br J Dermatol. 2004 Nov;151(5):995-1003. Pubmed: 15541077
  20. Ito H, Yamamoto H, Kimura Y, Kambe H, Okochi T, Kishimoto S: Affinity chromatography of human plasma gelsolin with polyphosphate compounds on immobilized Cibacron Blue F3GA. J Chromatogr. 1990 Apr 6;526(2):397-406. Pubmed: 2163407

Only showing the first 50 proteins. There are 351 proteins in total.

Enzymes

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 arylesterase activity
Specific function:
Has low activity towards the organophosphate paraxon and aromatic carboxylic acid esters. Rapidly hydrolyzes lactones such as statin prodrugs (e.g. lovastatin). Hydrolyzes aromatic lactones and 5- or 6-member ring lactones with aliphatic substituents but not simple lactones or those with polar substituents.
Gene Name:
PON3
Uniprot ID:
Q15166
Molecular weight:
39607.185
General function:
Involved in fucose-1-phosphate guanylyltransferase acti
Specific function:
Catalyzes the formation of GDP-L-fucose from GTP and L-fucose-1-phosphate. Functions as a salvage pathway to reutilize L-fucose arising from the turnover of glycoproteins and glycolipids.
Gene Name:
FPGT
Uniprot ID:
O14772
Molecular weight:
37630.405
Reactions
Guanosine triphosphate + Fucose 1-phosphate → Pyrophosphate + GDP-L-fucosedetails
General function:
Involved in transferase activity
Specific function:
Not Available
Gene Name:
FDFT1
Uniprot ID:
P37268
Molecular weight:
48114.87
Reactions
Farnesyl pyrophosphate + NAD(P)H → Squalene + Pyrophosphate + NAD(P)(+)details
Farnesyl pyrophosphate → Pyrophosphate + Presqualene diphosphatedetails
Presqualene diphosphate + NADPH + Hydrogen Ion → Pyrophosphate + Squalene + NADPdetails
Farnesyl pyrophosphate + NADPH + Hydrogen Ion → Squalene + Pyrophosphate + NADPdetails
General function:
Involved in nucleotide binding
Specific function:
Not Available
Gene Name:
FARSA
Uniprot ID:
Q9Y285
Molecular weight:
57563.225
Reactions
Adenosine triphosphate + L-Phenylalanine + tRNA(Phe) → Adenosine monophosphate + Pyrophosphate + L-phenylalanyl-tRNA(Phe)details
Adenosine triphosphate + L-Phenylalanine + tRNA(Phe) → Adenosine monophosphate + Pyrophosphate + L-Phenylalanyl-tRNA(Phe)details
General function:
Involved in nucleotide binding
Specific function:
Catalyzes direct attachment of p-Tyr (Tyr) to tRNAPhe. Permits also, with a lower efficiency, the attachment of m-Tyr to tRNAPhe, thereby opening the way for delivery of the misacylated tRNA to the ribosome and incorporation of ROS-damaged amino acid into proteins.
Gene Name:
FARS2
Uniprot ID:
O95363
Molecular weight:
52356.21
Reactions
Adenosine triphosphate + L-Phenylalanine + tRNA(Phe) → Adenosine monophosphate + Pyrophosphate + L-phenylalanyl-tRNA(Phe)details
Adenosine triphosphate + L-Phenylalanine + tRNA(Phe) → Adenosine monophosphate + Pyrophosphate + L-Phenylalanyl-tRNA(Phe)details
General function:
Involved in oxidoreductase activity
Specific function:
Multifunctional enzyme mediating important protective effects. Metabolizes betaine aldehyde to betaine, an important cellular osmolyte and methyl donor. Protects cells from oxidative stress by metabolizing a number of lipid peroxidation-derived aldehydes. Involved in lysine catabolism.
Gene Name:
ALDH7A1
Uniprot ID:
P49419
Molecular weight:
58486.74
Reactions
Aminoadipic acid + Adenosine triphosphate → L-2-Aminoadipate adenylate + Pyrophosphatedetails
General function:
Involved in amidophosphoribosyltransferase activity
Specific function:
Not Available
Gene Name:
PPAT
Uniprot ID:
Q06203
Molecular weight:
57398.52
Reactions
5-Phosphoribosylamine + Pyrophosphate + L-Glutamic acid → L-Glutamine + Phosphoribosyl pyrophosphate + Waterdetails
General function:
Involved in nucleotidyltransferase activity
Specific function:
Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, prefers NAD(+) and NAAD as substrates and degrades NADH, nicotinic acid adenine dinucleotide phosphate (NHD) and nicotinamide guanine dinucleotide (NGD) less effectively. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NAADP(+). Protects against axonal degeneration following mechanical or toxic insults.
Gene Name:
NMNAT1
Uniprot ID:
Q9HAN9
Molecular weight:
31932.22
Reactions
Adenosine triphosphate + beta-nicotinamide D-ribonucleotide → Pyrophosphate + NADdetails
Adenosine triphosphate + beta-nicotinate-D-ribonucleotide → Pyrophosphate + Nicotinic acid adenine dinucleotidedetails
Adenosine triphosphate + nicotinate beta-D-ribonucleotide → Pyrophosphate + Nicotinic acid adenine dinucleotidedetails
General function:
Involved in nucleotidyltransferase activity
Specific function:
Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Can also use GTP and ITP as nucleotide donors. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, can use NAD (+), NADH, NAAD, nicotinic acid adenine dinucleotide phosphate (NHD), nicotinamide guanine dinucleotide (NGD) as substrates. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NAADP(+). Protects against axonal degeneration following injury.
Gene Name:
NMNAT3
Uniprot ID:
Q96T66
Molecular weight:
18255.08
Reactions
Adenosine triphosphate + beta-nicotinamide D-ribonucleotide → Pyrophosphate + NADdetails
Adenosine triphosphate + beta-nicotinate-D-ribonucleotide → Pyrophosphate + Nicotinic acid adenine dinucleotidedetails
Adenosine triphosphate + nicotinate beta-D-ribonucleotide → Pyrophosphate + Nicotinic acid adenine dinucleotidedetails
General function:
Involved in catalytic activity
Specific function:
Involved in the catabolism of quinolinic acid (QA).
Gene Name:
QPRT
Uniprot ID:
Q15274
Molecular weight:
30815.28
Reactions
nicotinate beta-D-ribonucleotide + Pyrophosphate + CO(2) → Quinolinic acid + Phosphoribosyl pyrophosphatedetails
nicotinate beta-D-ribonucleotide + Pyrophosphate + Carbon dioxide → Quinolinic acid + Phosphoribosyl pyrophosphatedetails
General function:
Involved in nucleotidyltransferase activity
Specific function:
Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate but with a lower efficiency. Cannot use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity prefers NAD(+), NADH and NAAD as substrates and degrades nicotinic acid adenine dinucleotide phosphate (NHD) less effectively. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NAADP(+).
Gene Name:
NMNAT2
Uniprot ID:
Q9BZQ4
Molecular weight:
34438.38
Reactions
Adenosine triphosphate + beta-nicotinamide D-ribonucleotide → Pyrophosphate + NADdetails
Adenosine triphosphate + beta-nicotinate-D-ribonucleotide → Pyrophosphate + Nicotinic acid adenine dinucleotidedetails
Adenosine triphosphate + nicotinate beta-D-ribonucleotide → Pyrophosphate + Nicotinic acid adenine dinucleotidedetails
General function:
Involved in ATP binding
Specific function:
Bifunctional 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.
Gene Name:
PAPSS1
Uniprot ID:
O43252
Molecular weight:
70832.725
Reactions
Adenosine triphosphate + Oat gum → Pyrophosphate + Adenosine phosphosulfatedetails
Adenosine triphosphate + Selenocystathionine → Pyrophosphate + Adenylylselenatedetails
General function:
Involved in ATP binding
Specific function:
Bifunctional 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. May have a important role in skeletogenesis during postnatal growth (By similarity).
Gene Name:
PAPSS2
Uniprot ID:
O95340
Molecular weight:
69969.8
Reactions
Adenosine triphosphate + Oat gum → Pyrophosphate + Adenosine phosphosulfatedetails
Adenosine triphosphate + Selenocystathionine → Pyrophosphate + Adenylylselenatedetails
General function:
Involved in lipopolysaccharide biosynthetic process
Specific function:
Catalyzes the activation of N-acetylneuraminic acid (NeuNAc) to cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-NeuNAc), a substrate required for the addition of sialic acid. Has some activity toward NeuNAc, N-glycolylneuraminic acid (Neu5Gc) or 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN).
Gene Name:
CMAS
Uniprot ID:
Q8NFW8
Molecular weight:
48378.835
Reactions
Cytidine triphosphate + N-acylneuraminate → Pyrophosphate + Cytidine monophosphate N-acetylneuraminic aciddetails
Cytidine triphosphate + N-Acetylneuraminic acid → Pyrophosphate + Cytidine monophosphate N-acetylneuraminic aciddetails
Cytidine triphosphate + N-Glycolylneuraminic acid → Pyrophosphate + CMP-N-glycoloylneuraminatedetails
General function:
Involved in methionine adenosyltransferase activity
Specific function:
Catalyzes the formation of S-adenosylmethionine from methionine and ATP.
Gene Name:
MAT2A
Uniprot ID:
P31153
Molecular weight:
43660.37
Reactions
Adenosine triphosphate + L-Methionine + Water → Phosphoric acid + Pyrophosphate + S-Adenosylmethioninedetails
Phosphoric acid + Pyrophosphate + S-Adenosylmethionine → Adenosine triphosphate + L-Methionine + Waterdetails
Adenosine triphosphate + Selenomethionine + Water → Phosphoric acid + Pyrophosphate + Se-Adenosylselenomethioninedetails
General function:
Involved in methionine adenosyltransferase activity
Specific function:
Catalyzes the formation of S-adenosylmethionine from methionine and ATP.
Gene Name:
MAT1A
Uniprot ID:
Q00266
Molecular weight:
43647.6
Reactions
Adenosine triphosphate + L-Methionine + Water → Phosphoric acid + Pyrophosphate + S-Adenosylmethioninedetails
Phosphoric acid + Pyrophosphate + S-Adenosylmethionine → Adenosine triphosphate + L-Methionine + Waterdetails
Adenosine triphosphate + Selenomethionine + Water → Phosphoric acid + Pyrophosphate + Se-Adenosylselenomethioninedetails
General function:
Involved in hydrolase activity
Specific function:
Pyrophosphatase that hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) as well as 2'-deoxy-N-6-hydroxylaminopurine triposphate (dHAPTP) and xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions.
Gene Name:
ITPA
Uniprot ID:
Q9BY32
Molecular weight:
16833.23
Reactions
A nucleoside triphosphate + Water → a nucleotide + Pyrophosphatedetails
Guanosine triphosphate + Water → Guanosine monophosphate + Pyrophosphatedetails
Uridine triphosphate + Water → Uridine 5'-monophosphate + Pyrophosphatedetails
Inosine triphosphate + Water → Inosinic acid + Pyrophosphatedetails
dGTP + Water → 2'-Deoxyguanosine 5'-monophosphate + Pyrophosphatedetails
Deoxyuridine triphosphate + Water → dUMP + Pyrophosphatedetails
Xanthosine 5-triphosphate + Water → Xanthylic acid + Pyrophosphatedetails
2'-Deoxyinosine triphosphate + Water → dIMP + Pyrophosphatedetails
6-Mercaptopurine ribonucleoside triphosphate + Water → 6-Thioinosine-5'-monophosphate + Pyrophosphatedetails
General function:
Involved in hydrolase activity
Specific function:
This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Gene Name:
DUT
Uniprot ID:
P33316
Molecular weight:
26562.975
Reactions
Deoxyuridine triphosphate + Water → dUMP + Pyrophosphatedetails
General function:
Involved in adenine phosphoribosyltransferase activity
Specific function:
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Gene Name:
APRT
Uniprot ID:
P07741
Molecular weight:
19607.535
Reactions
Adenosine monophosphate + Pyrophosphate → Adenine + Phosphoribosyl pyrophosphatedetails
Guanosine monophosphate + Pyrophosphate → Guanine + Phosphoribosyl pyrophosphatedetails
AICAR + Pyrophosphate → 5-Aminoimidazole-4-carboxamide + Phosphoribosyl pyrophosphatedetails
General function:
Involved in hypoxanthine phosphoribosyltransferase activity
Specific function:
Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the purine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway.
Gene Name:
HPRT1
Uniprot ID:
P00492
Molecular weight:
24579.155
Reactions
Inosinic acid + Pyrophosphate → Hypoxanthine + Phosphoribosyl pyrophosphatedetails
Guanosine monophosphate + Pyrophosphate → Guanine + Phosphoribosyl pyrophosphatedetails
Adenosine monophosphate + Pyrophosphate → Adenine + Phosphoribosyl pyrophosphatedetails
Xanthylic acid + Pyrophosphate → Xanthine + Phosphoribosyl pyrophosphatedetails
Mercaptopurine + Phosphoribosyl pyrophosphate → 6-Thioinosine-5'-monophosphate + Pyrophosphatedetails
6-Methylmercaptopurine + Phosphoribosyl pyrophosphate → 6-Methylthiopurine 5'-monophosphate ribonucleotide + Pyrophosphatedetails
Thioguanine + Phosphoribosyl pyrophosphate → 6-Thioguanosine monophosphate + Pyrophosphatedetails
General function:
Involved in biotin-[acetyl-CoA-carboxylase] ligase activity
Specific function:
Post-translational modification of specific protein by attachment of biotin. Acts on various carboxylases such as acetyl-CoA-carboxylase, pyruvate carboxylase, propionyl CoA carboxylase, and 3-methylcrotonyl CoA carboxylase.
Gene Name:
HLCS
Uniprot ID:
P50747
Molecular weight:
80759.345
Reactions
Adenosine triphosphate + Biotin + apo-[methylmalonyl-CoA:pyruvate carboxytransferase] → Adenosine monophosphate + Pyrophosphate + [methylmalonyl-CoA:pyruvate carboxytransferase]details
Adenosine triphosphate + Biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)] → Adenosine monophosphate + Pyrophosphate + [propionyl-CoA:carbon-dioxide ligase (ADP-forming)]details
Adenosine triphosphate + Biotin + apo-[3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)] → Adenosine monophosphate + Pyrophosphate + [3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)]details
Adenosine triphosphate + Biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] → Adenosine monophosphate + Pyrophosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]details
Adenosine triphosphate + Biotin → Pyrophosphate + Biotinyl-5'-AMPdetails
General function:
Involved in RNA binding
Specific function:
Not Available
Gene Name:
FARSB
Uniprot ID:
Q9NSD9
Molecular weight:
66114.93
Reactions
Adenosine triphosphate + L-Phenylalanine + tRNA(Phe) → Adenosine monophosphate + Pyrophosphate + L-phenylalanyl-tRNA(Phe)details
Adenosine triphosphate + L-Phenylalanine + tRNA(Phe) → Adenosine monophosphate + Pyrophosphate + L-Phenylalanyl-tRNA(Phe)details
General function:
Involved in acid-amino acid ligase activity
Specific function:
Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In association with the E3 enzyme BRE1 (RNF20 and/or RNF40), it plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B at 'Lys-120' to form H2BK120ub1. H2BK120ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. In vitro catalyzes 'Lys-11', as well as 'Lys-48'-linked polyubiquitination. Required for postreplication repair of UV-damaged DNA.
Gene Name:
UBE2A
Uniprot ID:
P49459
Molecular weight:
17315.265
Reactions
Adenosine triphosphate + ubiquitin + protein lysine → Adenosine monophosphate + Pyrophosphate + protein N-ubiquityllysinedetails
General function:
Involved in ATP binding
Specific function:
Accepts the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX1, but not RBX2, suggests that the RBX1-UBE2M complex neddylates specific target proteins, such as CUL1, CUL2, CUL3 and CUL4. Involved in cell proliferation.
Gene Name:
UBE2M
Uniprot ID:
P61081
Molecular weight:
20899.8
Reactions
Adenosine triphosphate + NEDD8 + protein lysine → Adenosine monophosphate + Pyrophosphate + protein N-NEDD8yllysinedetails
General function:
Involved in acid-amino acid ligase activity
Specific function:
Catalyzes the covalent attachment of ubiquitin or ISG15 to other proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Promotes ubiquitination and subsequent proteasomal degradation of FLT3.
Gene Name:
UBE2L6
Uniprot ID:
O14933
Molecular weight:
17768.52
Reactions
Adenosine triphosphate + ubiquitin + protein lysine → Adenosine monophosphate + Pyrophosphate + protein N-ubiquityllysinedetails
General function:
Involved in nucleotide binding
Specific function:
Catalyzes the attachment of glycine to tRNA(Gly). Is also able produce diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs.
Gene Name:
GARS
Uniprot ID:
P41250
Molecular weight:
83164.83
Reactions
Adenosine triphosphate + Glycine + tRNA(Gly) → Adenosine monophosphate + Pyrophosphate + glycyl-tRNA(Gly)details
Adenosine triphosphate + Glycine + tRNA(Gly) → Adenosine monophosphate + Pyrophosphate + Glycyl-tRNA(Gly)details
General function:
Involved in nucleotide binding
Specific function:
Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the multisynthetase complex and assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation.
Gene Name:
EPRS
Uniprot ID:
P07814
Molecular weight:
170589.705
Reactions
Adenosine triphosphate + L-Glutamic acid + tRNA(Glu) → Adenosine monophosphate + Pyrophosphate + L-glutamyl-tRNA(Glu)details
Adenosine triphosphate + L-Proline + tRNA(Pro) → Adenosine monophosphate + Pyrophosphate + L-prolyl-tRNA(Pro)details
Adenosine triphosphate + L-Proline + tRNA(Pro) → Adenosine monophosphate + Pyrophosphate + L-Prolyl-tRNA(Pro)details
tRNA(Glu) + L-Glutamic acid + Adenosine triphosphate → L-Glutamyl-tRNA(Glu) + Pyrophosphate + Adenosine monophosphatedetails
General function:
Involved in catalytic activity
Specific function:
Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses arachidonate and eicosapentaenoate as substrates.
Gene Name:
ACSL4
Uniprot ID:
O60488
Molecular weight:
74435.495
Reactions
Adenosine triphosphate + a long-chain fatty acid + Coenzyme A → Adenosine monophosphate + Pyrophosphate + an acyl-CoAdetails
Adenosine triphosphate + Palmitic acid + Coenzyme A → Adenosine monophosphate + hexadecanoyl-CoA + Pyrophosphatedetails
General function:
Involved in acid-amino acid ligase activity
Specific function:
Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and auto-ubiquitination of STUB1, TRAF6 and TRIM63/MURF1. Ubiquitinates STUB1-associated HSP90AB1 in vitro. Lacks inherent specificity for any particular lysine residue of ubiquitin. Essential for viral activation of IRF3. Mediates polyubiquitination of CYP3A4.
Gene Name:
UBE2D1
Uniprot ID:
P51668
Molecular weight:
16601.86
Reactions
Adenosine triphosphate + ubiquitin + protein lysine → Adenosine monophosphate + Pyrophosphate + protein N-ubiquityllysinedetails
General function:
Involved in nucleotide binding
Specific function:
Isoform 1, isoform 2 and T1-TrpRS have aminoacylation activity while T2-TrpRS lacks it. Isoform 2, T1-TrpRS and T2-TrpRS possess angiostatic activity whereas isoform 1 lacks it. T2-TrpRS inhibits fluid shear stress-activated responses of endothelial cells. Regulates ERK, Akt, and eNOS activation pathways that are associated with angiogenesis, cytoskeletal reorganization and shear stress-responsive gene expression.
Gene Name:
WARS
Uniprot ID:
P23381
Molecular weight:
53164.91
Reactions
Adenosine triphosphate + L-Tryptophan + tRNA(Trp) → Adenosine monophosphate + Pyrophosphate + L-tryptophyl-tRNA(Trp)details
Adenosine triphosphate + L-Tryptophan + tRNA(Trp) → Adenosine monophosphate + Pyrophosphate + L-Tryptophanyl-tRNA(Trp)details
General function:
Involved in catalytic activity
Specific function:
Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitoleate, oleate and linoleate.
Gene Name:
ACSL1
Uniprot ID:
P33121
Molecular weight:
77942.685
Reactions
Adenosine triphosphate + a long-chain fatty acid + Coenzyme A → Adenosine monophosphate + Pyrophosphate + an acyl-CoAdetails
Adenosine triphosphate + Palmitic acid + Coenzyme A → Adenosine monophosphate + hexadecanoyl-CoA + Pyrophosphatedetails
General function:
Involved in acid-amino acid ligase activity
Specific function:
Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. May be involved in degradation of muscle-specific proteins. Mediates polyubiquitination of CYP3A4.
Gene Name:
UBE2G1
Uniprot ID:
P62253
Molecular weight:
19509.035
Reactions
Adenosine triphosphate + ubiquitin + protein lysine → Adenosine monophosphate + Pyrophosphate + protein N-ubiquityllysinedetails
General function:
Involved in nucleotide binding
Specific function:
Not Available
Gene Name:
QARS
Uniprot ID:
P47897
Molecular weight:
87797.97
Reactions
Adenosine triphosphate + L-Glutamine + tRNA(Gln) → Adenosine monophosphate + Pyrophosphate + L-glutaminyl-tRNA(Gln)details
Adenosine triphosphate + L-Glutamine + tRNA(Gln) → Adenosine monophosphate + Pyrophosphate + Glutaminyl-tRNAdetails
General function:
Involved in nucleotide binding
Specific function:
Not Available
Gene Name:
TARS
Uniprot ID:
P26639
Molecular weight:
83434.5
Reactions
Adenosine triphosphate + L-Threonine + tRNA(Thr) → Adenosine monophosphate + Pyrophosphate + L-threonyl-tRNA(Thr)details
Adenosine triphosphate + L-Threonine + tRNA(Thr) → Adenosine monophosphate + Pyrophosphate + L-Threonyl-tRNA(Thr)details
General function:
Involved in asparagine synthase (glutamine-hydrolyzing) activity
Specific function:
Not Available
Gene Name:
ASNS
Uniprot ID:
P08243
Molecular weight:
62167.855
Reactions
Adenosine triphosphate + L-Aspartic acid + L-Glutamine + Water → Adenosine monophosphate + Pyrophosphate + L-Asparagine + L-Glutamic aciddetails
General function:
Involved in acid-amino acid ligase activity
Specific function:
Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination.
Gene Name:
UBE2E2
Uniprot ID:
Q96LR5
Molecular weight:
22254.87
Reactions
Adenosine triphosphate + ubiquitin + protein lysine → Adenosine monophosphate + Pyrophosphate + protein N-ubiquityllysinedetails
General function:
Involved in acid-amino acid ligase activity
Specific function:
Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and autoubiquitination of STUB1 and TRAF6. Involved in the signal-induced conjugation and subsequent degradation of NFKBIA, FBXW2-mediated GCM1 ubiquitination and degradation, MDM2-dependent degradation of p53/TP53 and the activation of MAVS in the mitochondria by DDX58/RIG-I in response to viral infection. Essential for viral activation of IRF3.
Gene Name:
UBE2D2
Uniprot ID:
P62837
Molecular weight:
16735.06
Reactions
Adenosine triphosphate + ubiquitin + protein lysine → Adenosine monophosphate + Pyrophosphate + protein N-ubiquityllysinedetails
General function:
Involved in DNA ligase (ATP) activity
Specific function:
Efficiently joins single-strand breaks in a double-stranded polydeoxynucleotide in an ATP-dependent reaction. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends.
Gene Name:
LIG4
Uniprot ID:
P49917
Molecular weight:
103969.85
Reactions
Adenosine triphosphate + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) → Adenosine monophosphate + Pyrophosphate + (deoxyribonucleotide)(n+m)details
General function:
Involved in nucleotide binding
Specific function:
Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis. Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1.
Gene Name:
RARS
Uniprot ID:
P54136
Molecular weight:
75378.295
Reactions
Adenosine triphosphate + L-Arginine + tRNA(Arg) → Adenosine monophosphate + Pyrophosphate + L-arginyl-tRNA(Arg)details
Adenosine triphosphate + L-Arginine + tRNA(Arg) → Adenosine monophosphate + Pyrophosphate + L-Arginyl-tRNA(Arg)details
General function:
Involved in catalytic activity
Specific function:
Involved in the de novo synthesis of guanine nucleotides which are not only essential for DNA and RNA synthesis, but also provide GTP, which is involved in a number of cellular processes important for cell division.
Gene Name:
GMPS
Uniprot ID:
P49915
Molecular weight:
76714.79
Reactions
Adenosine triphosphate + Xanthylic acid + L-Glutamine + Water → Adenosine monophosphate + Pyrophosphate + Guanosine monophosphate + L-Glutamic aciddetails
Adenosine triphosphate + Xanthylic acid + Ammonia → Adenosine monophosphate + Pyrophosphate + Guanosine monophosphatedetails
6-Thioxanthine 5'-monophosphate + Adenosine triphosphate + L-Glutamine + Water → 6-Thioguanosine monophosphate + Adenosine monophosphate + Pyrophosphate + L-Glutamic aciddetails
General function:
Involved in acid-amino acid ligase activity
Specific function:
Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. Participates in the regulation of transepithelial sodium transport in renal cells. May be involved in cell growth arrest.
Gene Name:
UBE2E3
Uniprot ID:
Q969T4
Molecular weight:
22912.32
Reactions
Adenosine triphosphate + ubiquitin + protein lysine → Adenosine monophosphate + Pyrophosphate + protein N-ubiquityllysinedetails
General function:
Involved in ATP binding
Specific function:
Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In association with the E3 enzyme BRE1 (RNF20 and/or RNF40), it plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B at 'Lys-120' to form H2BK120ub1. H2BK120ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. In vitro catalyzes 'Lys-11'-, as well as 'Lys-48'- and 'Lys-63'-linked polyubiquitination. Required for postreplication repair of UV-damaged DNA. Associates to the E3 ligase RAD18 to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on 'Lys-164'. May be involved in neurite outgrowth.
Gene Name:
UBE2B
Uniprot ID:
P63146
Molecular weight:
17312.205
Reactions
Adenosine triphosphate + ubiquitin + protein lysine → Adenosine monophosphate + Pyrophosphate + protein N-ubiquityllysinedetails
General function:
Involved in nucleotide binding
Specific function:
Not Available
Gene Name:
LARS2
Uniprot ID:
Q15031
Molecular weight:
101975.43
Reactions
Adenosine triphosphate + L-Leucine + tRNA(Leu) → Adenosine monophosphate + Pyrophosphate + L-leucyl-tRNA(Leu)details
Adenosine triphosphate + L-Leucine + tRNA(Leu) → Adenosine monophosphate + Pyrophosphate + L-Leucyl-tRNAdetails
General function:
Involved in acid-amino acid ligase activity
Specific function:
Catalyzes the covalent attachment of ubiquitin to other proteins. Seems to function in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum (ERAD) (By similarity).
Gene Name:
UBE2J2
Uniprot ID:
Q8N2K1
Molecular weight:
28898.06
Reactions
Adenosine triphosphate + ubiquitin + protein lysine → Adenosine monophosphate + Pyrophosphate + protein N-ubiquityllysinedetails
General function:
Involved in acid-amino acid ligase activity
Specific function:
Ubiquitin-conjugating enzyme E2 that specifically acts with HECT-type and RBR family E3 ubiquitin-protein ligases. Does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine: in contrast, it has activity with the RBR family E3 enzymes, such as PARK2 and ARIH1, that function like function like RING-HECT hybrids. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'-linked polyubiquitination. Involved in the selective degradation of short-lived and abnormal proteins. Down-regulated during the S-phase it is involved in progression through the cell cycle. Regulates nuclear hormone receptors transcriptional activity. May play a role in myelopoiesis.
Gene Name:
UBE2L3
Uniprot ID:
P68036
Molecular weight:
24003.385
Reactions
Adenosine triphosphate + ubiquitin + protein lysine → Adenosine monophosphate + Pyrophosphate + protein N-ubiquityllysinedetails
General function:
Involved in ligase activity, forming phosphoric ester bonds
Specific function:
Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing.
Gene Name:
RTCA
Uniprot ID:
O00442
Molecular weight:
40709.05
Reactions
Adenosine triphosphate + RNA 3'-terminal-phosphate → Adenosine monophosphate + Pyrophosphate + RNA terminal-2',3'-cyclic-phosphatedetails
General function:
Involved in nucleotide binding
Specific function:
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr) (By similarity).
Gene Name:
YARS
Uniprot ID:
P54577
Molecular weight:
59143.025
Reactions
Adenosine triphosphate + L-Tyrosine + tRNA(Tyr) → Adenosine monophosphate + Pyrophosphate + L-tyrosyl-tRNA(Tyr)details
Adenosine triphosphate + L-Tyrosine + tRNA(Tyr) → Adenosine monophosphate + Pyrophosphate + L-Tyrosyl-tRNA(Tyr)details
General function:
Involved in DNA ligase (ATP) activity
Specific function:
Interacts with DNA-repair protein XRCC1 and can correct defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents.
Gene Name:
LIG3
Uniprot ID:
P49916
Molecular weight:
106017.03
Reactions
Adenosine triphosphate + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) → Adenosine monophosphate + Pyrophosphate + (deoxyribonucleotide)(n+m)details

Only showing the first 50 proteins. There are 351 proteins in total.