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Record Information
Version3.6
Creation Date2005-11-16 15:48:42 UTC
Update Date2014-06-13 18:15:54 UTC
HMDB IDHMDB01520
Secondary Accession NumbersNone
Metabolite Identification
Common NameFlavin Mononucleotide
DescriptionFlavin mononucleotide (FMN), or riboflavin-5′-phosphate, is a biomolecule produced from riboflavin (vitamin B2) by the enzyme riboflavin kinase and functions as prosthetic group of various oxidoreductases including NADH dehydrogenase as well as cofactor in biological blue-light photo receptors. During the catalytic cycle, the reversible interconversion of oxidized (FMN), semiquinone (FMNH•) and reduced (FMNH2) forms occurs in the various oxidoreductases. FMN is a stronger oxidizing agent than NAD and is particularly useful because it can take part in both one- and two-electron transfers. Flavin mononucleotide is also used as an orange-red food colour additive. It is the principal form in which riboflavin is found in cells and tissues.
Structure
Thumb
Synonyms
  1. Flanin
  2. Flavine mononucleotide
  3. Flavol
  4. FMN
  5. Riboflavin
  6. Riboflavin 5'-monophosphate
  7. Riboflavin 5'-phosphate
  8. Riboflavin Mononucleotide
  9. Riboflavin monophosphate
  10. Riboflavin phosphate
  11. Riboflavin-5'-phosphate na
  12. Riboflavin-5-phosphate
  13. Riboflavine 5'-monophosphate
  14. Riboflavine 5'-phosphate
  15. Riboflavine dihydrogen phosphate
  16. Riboflavine monophosphate
  17. Riboflavine phosphate
  18. Riboflavine-5'-phosphate
  19. Vitamin B2 phosphate
Chemical FormulaC17H21N4O9P
Average Molecular Weight456.3438
Monoisotopic Molecular Weight456.104614802
IUPAC Name{[(2R,3S,4S)-5-{7,8-dimethyl-2,4-dioxo-2H,3H,4H,10H-benzo[g]pteridin-10-yl}-2,3,4-trihydroxypentyl]oxy}phosphonic acid
Traditional IUPAC Name[(2R,3S,4S)-5-{7,8-dimethyl-2,4-dioxo-3H-benzo[g]pteridin-10-yl}-2,3,4-trihydroxypentyl]oxyphosphonic acid
CAS Registry Number146-17-8
SMILES
CC1=CC2=C(C=C1C)N(C[C@H](O)[C@H](O)[C@H](O)COP(O)(O)=O)C1=NC(=O)NC(=O)C1=N2
InChI Identifier
InChI=1S/C17H21N4O9P/c1-7-3-9-10(4-8(7)2)21(15-13(18-9)16(25)20-17(26)19-15)5-11(22)14(24)12(23)6-30-31(27,28)29/h3-4,11-12,14,22-24H,5-6H2,1-2H3,(H,20,25,26)(H2,27,28,29)/t11-,12+,14-/m0/s1
InChI KeyFVTCRASFADXXNN-SCRDCRAPSA-N
Chemical Taxonomy
KingdomOrganic Compounds
Super ClassAromatic Heteropolycyclic Compounds
ClassPteridines and Derivatives
Sub ClassAlloxazines and Isoalloxazines
Other Descriptors
  • Organic Compounds
  • Pteridines and Derivatives
  • flavin mononucleotide(ChEBI)
Substituents
  • 1,2 Diol
  • Monosaccharide Phosphate
  • Organic Hypophosphite
  • Organic Phosphite
  • Pentose Monosaccharide
  • Phosphoric Acid Ester
  • Pyrazine
  • Pyrimidine
  • Pyrimidone
  • Quinoxaline
  • Saccharide
  • Secondary Alcohol
  • Toluene
Direct ParentFlavins
Ontology
StatusDetected and Quantified
Origin
  • Endogenous
Biofunction
  • Component of Riboflavin metabolism
ApplicationNot Available
Cellular locations
  • Cytoplasm (predicted from logP)
Physical Properties
StateSolid
Experimental Properties
PropertyValueReference
Melting Point290 °CNot Available
Boiling PointNot AvailableNot Available
Water Solubility92 mg/mLNot Available
LogPNot AvailableNot Available
Predicted Properties
PropertyValueSource
water solubility0.67 g/LALOGPS
logP-0.78ALOGPS
logP-1ChemAxon
logS-2.8ALOGPS
pKa (strongest acidic)1.57ChemAxon
pKa (strongest basic)0.68ChemAxon
physiological charge-3ChemAxon
hydrogen acceptor count11ChemAxon
hydrogen donor count6ChemAxon
polar surface area201.58ChemAxon
rotatable bond count7ChemAxon
refractivity107.14ChemAxon
polarizability42.19ChemAxon
Spectra
SpectraLC-MS1D NMR2D NMR
Biological Properties
Cellular Locations
  • Cytoplasm (predicted from logP)
Biofluid Locations
  • Blood
Tissue Location
  • Erythrocyte
  • Eye Lens
  • Muscle
  • Platelet
Pathways
NameSMPDB LinkKEGG Link
Riboflavin MetabolismSMP00070map00740
Normal Concentrations
BiofluidStatusValueAgeSexConditionReferenceDetails
BloodDetected and Quantified0.0084 (0.0035-0.013) uMAdult (>18 years old)FemaleNormal details
BloodDetected and Quantified0.016 +/- 0.009 uMAdolescent (13-18 years old)FemaleNormal details
BloodDetected and Quantified0.0075 (0.004-0.011) uMAdult (>18 years old)BothNormal details
Abnormal Concentrations
BiofluidStatusValueAgeSexConditionReferenceDetails
BloodDetected and Quantified0.013 +/- 0.006 uMChildren (1-13 years old)BothMalnutrition (type kwashiorkor and marasmus) details
BloodDetected and Quantified0.012 +/- 0.006 uMAdolescent (13-18 years old)FemaleAnorexia nervosa details
Associated Disorders and Diseases
Disease References
Anorexia nervosa
  1. Capo-chichi CD, Gueant JL, Lefebvre E, Bennani N, Lorentz E, Vidailhet C, Vidailhet M: Riboflavin and riboflavin-derived cofactors in adolescent girls with anorexia nervosa. Am J Clin Nutr. 1999 Apr;69(4):672-8. Pubmed: 10197568
Associated OMIM IDs
DrugBank IDDB03247
DrugBank Metabolite IDNot Available
Phenol Explorer Compound IDNot Available
Phenol Explorer Metabolite IDNot Available
FoodDB IDFDB001984
KNApSAcK IDC00019686
Chemspider ID559060
KEGG Compound IDC00061
BioCyc IDFMN
BiGG ID33703
Wikipedia LinkFMN
NuGOwiki LinkHMDB01520
Metagene LinkHMDB01520
METLIN ID6295
PubChem Compound643976
PDB IDFMN
ChEBI ID17621
References
Synthesis ReferenceOno, Shigeru; Hirano, Hiroko; Sato, Yoshiyuki. Formation of flavin adenine dinucleotide and flavin mononucleotide by lens homogenate. Experimental Eye Research (1982), 34(2), 297-301.
Material Safety Data Sheet (MSDS)Download (PDF)
General References
  1. Mathew JL, Kabi BC, Rath B: Anti-oxidant vitamins and steroid responsive nephrotic syndrome in Indian children. J Paediatr Child Health. 2002 Oct;38(5):450-37. Pubmed: 12354259
  2. Booth CK, Clark T, Fenn A: Folic acid, riboflavin, thiamine, and vitamin B-6 status of a group of first-time blood donors. Am J Clin Nutr. 1998 Nov;68(5):1075-80. Pubmed: 9808225
  3. Mikalunas V, Fitzgerald K, Rubin H, McCarthy R, Craig RM: Abnormal vitamin levels in patients receiving home total parenteral nutrition. J Clin Gastroenterol. 2001 Nov-Dec;33(5):393-6. Pubmed: 11606856
  4. Baeckert PA, Greene HL, Fritz I, Oelberg DG, Adcock EW: Vitamin concentrations in very low birth weight infants given vitamins intravenously in a lipid emulsion: measurement of vitamins A, D, and E and riboflavin. J Pediatr. 1988 Dec;113(6):1057-65. Pubmed: 3142982
  5. Bamji MS, Bhaskaram P, Jacob CM: Urinary riboflavin excretion and erythrocyte glutathione reductase activity in preschool children suffering from upper respiratory infections and measles. Ann Nutr Metab. 1987;31(3):191-6. Pubmed: 3592624
  6. Ajayi OA: Bioavailability of riboflavin from fortified palm juice. Plant Foods Hum Nutr. 1989 Dec;39(4):375-80. Pubmed: 2631092
  7. Brun TA, Chen J, Campbell TC, Boreham J, Feng Z, Parpia B, Shen TF, Li M: Urinary riboflavin excretion after a load test in rural China as a measure of possible riboflavin deficiency. Eur J Clin Nutr. 1990 Mar;44(3):195-206. Pubmed: 2369885
  8. Rao PN, Levine E, Myers MO, Prakash V, Watson J, Stolier A, Kopicko JJ, Kissinger P, Raj SG, Raj MH: Elevation of serum riboflavin carrier protein in breast cancer. Cancer Epidemiol Biomarkers Prev. 1999 Nov;8(11):985-90. Pubmed: 10566553
  9. Zhou X, Huang C, Hong J, Yao S: [Nested case-control study on riboflavin levels in blood and urine and the risk of lung cancer] Wei Sheng Yan Jiu. 2003 Nov;32(6):597-8, 601. Pubmed: 14963913
  10. Thurnham DI, Zheng SF, Munoz N, Crespi M, Grassi A, Hambidge KM, Chai TF: Comparison of riboflavin, vitamin A, and zinc status of Chinese populations at high and low risk for esophageal cancer. Nutr Cancer. 1985;7(3):131-43. Pubmed: 3878498
  11. Bates CJ, Prentice AM, Paul AA, Prentice A, Sutcliffe BA, Whitehead RG: Riboflavin status in infants born in rural Gambia, and the effect of a weaning food supplement. Trans R Soc Trop Med Hyg. 1982;76(2):253-8. Pubmed: 7101408
  12. Edelbroek PM, Linssen AC, Zitman FG, Rooymans HG, de Wolff FA: Analgesic and antidepressive effects of low-dose amitriptyline in relation to its metabolism in patients with chronic pain. Clin Pharmacol Ther. 1986 Feb;39(2):156-62. Pubmed: 3510800
  13. Ahmed F, Khan MR, Akhtaruzzaman M, Karim R, Marks GC, Banu CP, Nahar B, Williams G: Efficacy of twice-weekly multiple micronutrient supplementation for improving the hemoglobin and micronutrient status of anemic adolescent schoolgirls in Bangladesh. Am J Clin Nutr. 2005 Oct;82(4):829-35. Pubmed: 16210713
  14. Buzina R, Grgic Z, Jusic M, Sapunar J, Milanovic N, Brubacher G: Nutritional status and physical working capacity. Hum Nutr Clin Nutr. 1982;36(6):429-38. Pubmed: 7161138
  15. Ortega RM, Quintas ME, Martinez RM, Andres P, Lopez-Sobaler AM, Requejo AM: Riboflavin levels in maternal milk: the influence of vitamin B2 status during the third trimester of pregnancy. J Am Coll Nutr. 1999 Aug;18(4):324-9. Pubmed: 12038475
  16. Lartey A, Manu A, Brown KH, Dewey KG: Predictors of micronutrient status among six- to twelve-month-old breast-fed Ghanaian infants. J Nutr. 2000 Feb;130(2):199-207. Pubmed: 10720170
  17. Blajchman MA, Goldman M, Baeza F: Improving the bacteriological safety of platelet transfusions. Transfus Med Rev. 2004 Jan;18(1):11-24. Pubmed: 14689374
  18. Cikot RJ, Steegers-Theunissen RP, Thomas CM, de Boo TM, Merkus HM, Steegers EA: Longitudinal vitamin and homocysteine levels in normal pregnancy. Br J Nutr. 2001 Jan;85(1):49-58. Pubmed: 11227033
  19. Hardwick CC, Herivel TR, Hernandez SC, Ruane PH, Goodrich RP: Separation, identification and quantification of riboflavin and its photoproducts in blood products using high-performance liquid chromatography with fluorescence detection: a method to support pathogen reduction technology. Photochem Photobiol. 2004 Nov-Dec;80(3):609-15. Pubmed: 15382964
  20. Schorah CJ, Wild J, Hartley R, Sheppard S, Smithells RW: The effect of periconceptional supplementation on blood vitamin concentrations in women at recurrence risk for neural tube defect. Br J Nutr. 1983 Mar;49(2):203-11. Pubmed: 6830748

Enzymes

General function:
Involved in acid phosphatase activity
Specific function:
Not Available
Gene Name:
ACP2
Uniprot ID:
P11117
Molecular weight:
48343.92
Reactions
Flavin Mononucleotide + Water → Riboflavin + Phosphoric aciddetails
General function:
Involved in acid phosphatase activity
Specific function:
Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates. Isoform 3 does not possess phosphatase activity.
Gene Name:
ACP1
Uniprot ID:
P24666
Molecular weight:
18042.315
Reactions
Flavin Mononucleotide + Water → Riboflavin + Phosphoric aciddetails
General function:
Involved in hydrolase activity
Specific function:
Involved in osteopontin/bone sialoprotein dephosphorylation. Its expression seems to increase in certain pathological states such as Gaucher and Hodgkin diseases, the hairy cell, the B-cell, and the T-cell leukemias.
Gene Name:
ACP5
Uniprot ID:
P13686
Molecular weight:
36598.47
Reactions
Flavin Mononucleotide + Water → Riboflavin + Phosphoric aciddetails
General function:
Involved in acid phosphatase activity
Specific function:
A non-specific tyrosine phosphatase that dephosphorylates a diverse number of substrates under acidic conditions (pH 4-6) including alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated proteins. Has lipid phosphatase activity and inactivates lysophosphatidic acid in seminal plasma. Isoform 2: the cellular form also has ecto-5'-nucleotidase activity in dorsal root ganglion (DRG) neurons. Generates adenosine from AMP which acts as a pain suppressor. Acts as a tumor suppressor of prostate cancer through dephosphorylation of ERBB2 and deactivation of MAPK-mediated signaling.
Gene Name:
ACPP
Uniprot ID:
P15309
Molecular weight:
44565.715
Reactions
Flavin Mononucleotide + Water → Riboflavin + Phosphoric aciddetails
General function:
Involved in catalytic activity
Specific function:
Involved primarily in ATP hydrolysis at the plasma membrane. Plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. In vitro, has a broad specificity, hydrolyzing other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling. Appears to modulate insulin sensitivity.
Gene Name:
ENPP1
Uniprot ID:
P22413
Molecular weight:
104923.58
Reactions
FAD + Water → Adenosine monophosphate + Flavin Mononucleotidedetails
General function:
Involved in iron ion binding
Specific function:
Catalyzes a dehydrogenation to introduce C5-6 double bond into lathosterol.
Gene Name:
SC5DL
Uniprot ID:
O75845
Molecular weight:
35300.55
General function:
Involved in oxidoreductase activity
Specific function:
This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5.
Gene Name:
POR
Uniprot ID:
P16435
Molecular weight:
77047.575
References
  1. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. Pubmed: 10592235
General function:
Involved in catalytic activity
Specific function:
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Gene Name:
DHODH
Uniprot ID:
Q02127
Molecular weight:
42866.93
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed: 17139284
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed: 17016423
  3. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. Pubmed: 10592235
General function:
Involved in NADH dehydrogenase (ubiquinone) activity
Specific function:
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Gene Name:
NDUFV1
Uniprot ID:
P49821
Molecular weight:
49867.66
General function:
Involved in catalytic activity
Specific function:
Cleaves a variety of phosphodiester and phosphosulfate bonds including deoxynucleotides, nucleotide sugars, and NAD (By similarity).
Gene Name:
ENPP3
Uniprot ID:
O14638
Molecular weight:
100123.54
Reactions
FAD + Water → Adenosine monophosphate + Flavin Mononucleotidedetails
General function:
Involved in oxidoreductase activity
Specific function:
Involved in the reductive regeneration of cob(I)alamin cofactor required for the maintenance of methionine synthase in a functional state.
Gene Name:
MTRR
Uniprot ID:
Q9UBK8
Molecular weight:
77672.995
General function:
Involved in pyridoxamine-phosphate oxidase activity
Specific function:
Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Gene Name:
PNPO
Uniprot ID:
Q9NVS9
Molecular weight:
29987.79
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed: 17139284
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed: 17016423
  3. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. Pubmed: 10592235
General function:
Involved in catalytic activity
Specific function:
Broad specificity oxidoreductase that catalyzes the NADPH-dependent reduction of a variety of flavins, such as riboflavin, FAD or FMN, biliverdins, methemoglobin and PQQ (pyrroloquinoline quinone). Contributes to heme catabolism and metabolizes linear tetrapyrroles. Can also reduce the complexed Fe(3+) iron to Fe(2+) in the presence of FMN and NADPH. In the liver, converts biliverdin to bilirubin.
Gene Name:
BLVRB
Uniprot ID:
P30043
Molecular weight:
22119.215
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed: 17139284
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed: 17016423
General function:
Involved in electron carrier activity
Specific function:
Involved in pyrimidine base degradation. Catalyzes the reduction of uracil and thymine. Also involved the degradation of the chemotherapeutic drug 5-fluorouracil.
Gene Name:
DPYD
Uniprot ID:
Q12882
Molecular weight:
111400.32
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed: 17139284
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed: 17016423
  3. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. Pubmed: 10592235
General function:
Involved in FMN binding
Specific function:
Has 2-hydroxyacid oxidase activity. Most active on the 2-carbon substrate glycolate, but is also active on 2-hydroxy fatty acids, with high activity towards 2-hydroxy palmitate and 2-hydroxy octanoate.
Gene Name:
HAO1
Uniprot ID:
Q9UJM8
Molecular weight:
40923.945
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed: 17139284
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed: 17016423
  3. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. Pubmed: 10592235
General function:
Involved in FMN binding
Specific function:
Catalyzes the oxidation of L-alpha-hydroxy acids as well as, more slowly, that of L-alpha-amino acids.
Gene Name:
HAO2
Uniprot ID:
Q9NYQ3
Molecular weight:
38838.35
References
  1. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. Pubmed: 10592235
General function:
Involved in oxidoreductase activity
Specific function:
Not Available
Gene Name:
SARDH
Uniprot ID:
Q9UL12
Molecular weight:
101035.985
General function:
Involved in oxidoreductase activity
Specific function:
Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such COX2.
Gene Name:
NOS2
Uniprot ID:
P35228
Molecular weight:
131116.3
General function:
Involved in oxidoreductase activity
Specific function:
Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter. Probably has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such SRR.
Gene Name:
NOS1
Uniprot ID:
P29475
Molecular weight:
160969.095
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed: 17139284
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed: 17016423
  3. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. Pubmed: 10592235
General function:
Involved in oxidoreductase activity
Specific function:
Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. NO mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets. Isoform eNOS13C: Lacks eNOS activity, dominant-negative form that may down-regulate eNOS activity by forming heterodimers with isoform 1.
Gene Name:
NOS3
Uniprot ID:
P29474
Molecular weight:
133273.59
General function:
Involved in riboflavin kinase activity
Specific function:
Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin-mononucleotide (FMN).
Gene Name:
RFK
Uniprot ID:
Q969G6
Molecular weight:
17623.08
Reactions
Adenosine triphosphate + Riboflavin → ADP + Flavin Mononucleotidedetails
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed: 17139284
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed: 17016423
  3. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. Pubmed: 10592235
General function:
Involved in protein serine/threonine kinase activity
Specific function:
Serine/threonine kinase that may play a role in mediating the growth-factor and stress induced activation of the transcription factor CREB. Essential role in the control of RELA transcriptional activity in response to TNF. Phosphorylates 'Ser- 10' of histone H3 in response to mitogenics, stress stimuli and epidemal growth-factor (EGF) and result in the transcriptional activation of several immediate early genes, including proto- oncogenes FOS and JUN. Mediates the mitogen- and stress-induced phosphorylation of high mobility group protein 14 (HMG-14)
Gene Name:
RPS6KA4
Uniprot ID:
O75676
Molecular weight:
85605.0
References
  1. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. Pubmed: 10592235
General function:
Involved in protein serine/threonine kinase activity
Specific function:
Protein kinase that plays an important role in cellular stress response. Activates certain potassium, sodium, and chloride channels, suggesting an involvement in the regulation of processes such as cell survival, neuronal excitability and renal sodium excretion. Sustained high levels and activity may contribute to conditions such as hypertension and diabetic nephropathy. Mediates cell survival signals, phosphorylates and negatively regulates pro-apoptotic FOXO3A. Phosphorylates NEDD4L, which leads to its inactivation and to the subsequent activation of various channels and transporters such as ENaC, KCNA3/Kv1.3 or EAAT1. Isoform 2 exhibited a greater effect on cell plasma membrane expression of ENaC and Na(+) transport than isoform 1
Gene Name:
SGK1
Uniprot ID:
O00141
Molecular weight:
48942.0
References
  1. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. Pubmed: 10592235
General function:
Involved in catalytic activity
Specific function:
Necessary for the biosynthesis of coenzyme A. Catalyzes the decarboxylation of 4-phosphopantothenoylcysteine to form 4'-phosphopantotheine.
Gene Name:
PPCDC
Uniprot ID:
Q96CD2
Molecular weight:
22394.965
References
  1. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. Pubmed: 10592235
General function:
Involved in acid phosphatase activity
Specific function:
Hydrolyzes lysophosphatidic acid to monoacylglycerol.
Gene Name:
ACP6
Uniprot ID:
Q9NPH0
Molecular weight:
48853.955
Reactions
Flavin Mononucleotide + Water → Riboflavin + Phosphoric aciddetails
General function:
Involved in FMN adenylyltransferase activity
Specific function:
Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme.
Gene Name:
FLAD1
Uniprot ID:
Q8NFF5
Molecular weight:
49197.795
Reactions
Adenosine triphosphate + Flavin Mononucleotide → Pyrophosphate + FADdetails
General function:
Involved in oxidoreductase activity
Specific function:
Oxidoreductase that catalyzes the NADP-dependent reduction of cytochrome c and one-electron acceptors, such as doxorubicin, potassium ferricyanide and menadione (in vitro)
Gene Name:
NDOR1
Uniprot ID:
Q9UHB4
Molecular weight:
66761.9
General function:
Involved in oxidoreductase activity
Specific function:
Catalyzes the oxidative NADPH-dependent deiodination of monoiodotyrosine (L-MIT) or diiodotyrosine (L-DIT). Acts during the hydrolysis of thyroglobulin to liberate iodide, which can then reenter the hormone-producing pathways. Acts more efficiently on monoiodotyrosine than on diiodotyrosine.
Gene Name:
IYD
Uniprot ID:
Q6PHW0
Molecular weight:
33781.22
General function:
Involved in iron ion binding
Specific function:
Probable component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA
Gene Name:
TYW1
Uniprot ID:
Q9NV66
Molecular weight:
83701.7
General function:
Involved in iron ion binding
Specific function:
Probable component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA
Gene Name:
TYW1B
Uniprot ID:
Q6NUM6
Molecular weight:
76945.9
General function:
Involved in acid phosphatase activity
Specific function:
Dephosphorylates receptor tyrosine-protein kinase erbB-4 and inhibits the ligand-induced proteolytic cleavage.
Gene Name:
ACPT
Uniprot ID:
Q9BZG2
Molecular weight:
46089.015
Reactions
Flavin Mononucleotide + Water → Riboflavin + Phosphoric aciddetails
General function:
Involved in protein tyrosine phosphatase activity
Specific function:
Not Available
Gene Name:
ACP1
Uniprot ID:
B5MCC7
Molecular weight:
12230.0