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Record Information
Version3.6
Creation Date2005-11-16 15:48:42 UTC
Update Date2013-05-29 19:31:35 UTC
HMDB IDHMDB01429
Secondary Accession Numbers
  • HMDB05947
Metabolite Identification
Common NamePhosphate
DescriptionPhosphate is a salt of phosphoric acid. In organic chemistry, a phosphate, or organophosphate, is an ester of phosphoric acid. Organic phosphates are important in biochemistry, biogeochemistry and ecology. Phosphate (Pi) is an essential component of life. In biological systems, phosphorus is found as a free phosphate ion in solution and is called inorganic phosphate, to distinguish it from phosphates bound in various phosphate esters. Inorganic phosphate is generally denoted Pi and at physiological (neutral) pH primarily consists of a mixture of HPO2-4 and H2PO-4 ions. phosphates are most commonly found in the form of adenosine phosphates, (AMP, ADP and ATP) and in DNA and RNA and can be released by the hydrolysis of ATP or ADP. Similar reactions exist for the other nucleoside diphosphates and triphosphates. Phosphoanhydride bonds in ADP and ATP, or other nucleoside diphosphates and triphosphates, contain high amounts of energy which give them their vital role in all living organisms. Phosphate must be actively transported into cells against its electrochemical gradient. In vertebrates, two unrelated families of Na+-dependent Pi transporters carry out this task. Remarkably, the two families transport different Pi species: whereas type II Na+/Pi cotransporters (SCL34) prefer divalent HPO4(2), type III Na+/Pi cotransporters (SLC20) transport monovalent H2PO4. The SCL34 family comprises both electrogenic and electroneutral members that are expressed in various epithelia and other polarized cells. Through regulated activity in apical membranes of the gut and kidney, they maintain body Pi homeostasis, and in salivary and mammary glands, liver, and testes they play a role in modulating the Pi content of luminal fluids. Phosphate levels in the blood play an important role in hormone signaling and in bone homeostasis. In classical endocrine regulation, low serum phosphate induces the renal production of the seco-steroid hormone 1,25-dihydroxyvitamin D3 (1,25(OH)2D3).This active metabolite of vitamin D acts to restore circulating mineral (i.e. phosphate and calcium) levels by increasing absorption in the intestine, reabsorption in the kidney, and mobilization of calcium and phosphate from bone. Thus, chronic renal failure is associated with hyperparathyroidism, which in turn contributes to osteomalacia (softening of the bones). Another complication of chronic renal failure is hyperphosphatemia (low levels of phosphate in the blood). Hyperphosphatemia (excess levels of phosphate in the blood) is a prevalent condition in kidney dialysis patients and is associated with increased risk of mortality. Hypophosphatemia (hungry bone syndrome) has been associated to postoperative electrolyte aberrations and after parathyroidectomy. (PMID: 17581921 , 11169009 , 11039261 , 9159312 , 17625581 )Fibroblast growth factor 23 (FGF-23) has recently been recognized as a key mediator of phosphate homeostasis, its most notable effect being promotion of phosphate excretion. FGF-23 was discovered to be involved in diseases such as autosomal dominant hypophosphatemic rickets, X-linked hypophosphatemia, and tumor-induced osteomalacia in which phosphate wasting was coupled to inappropriately low levels of 1,25(OH)2D3. FGF-23 is regulated by dietary phosphate in humans. In particular it was found that phosphate restriction decreased FGF-23, and phosphate loading increased FGF-23.
Structure
Thumb
Synonyms
  1. NFB Orthophosphate
  2. O-Phosphoric acid
  3. Ortho-phosphate
  4. Orthophosphate (PO43-)
  5. Orthophosphate(3-)
  6. Phosphate
  7. Phosphate (PO43-)
  8. Phosphate anion(3-)
  9. Phosphate ion (PO43-)
  10. Phosphate ion(3-)
  11. Phosphate trianion
  12. Phosphate(3-)
  13. Phosphoric acid ion(3-)
  14. Pi
Chemical FormulaO4P
Average Molecular Weight94.9714
Monoisotopic Molecular Weight94.95342
IUPAC Namephosphate
Traditional IUPAC Namephosphate
CAS Registry Number14265-44-2
SMILES
[O-]P([O-])([O-])=O
InChI Identifier
InChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
InChI KeyNBIIXXVUZAFLBC-UHFFFAOYSA-K
Chemical Taxonomy
KingdomInorganic Compounds
Super ClassHomogeneous Non-metal Compounds
ClassNon-metal Oxoanionic Compounds
Sub ClassNon-metal Phosphates
Other Descriptors
  • phosphate ion(ChEBI)
Substituents
  • N/A
Direct ParentNon-metal Phosphates
Ontology
StatusDetected and Quantified
Origin
  • Drug metabolite
  • Endogenous
Biofunction
  • Osmolyte, enzyme cofactor, signalling
  • Waste products
ApplicationNot Available
Cellular locations
  • Cytoplasm
  • Extracellular
  • Mitochondria
  • Nucleus
  • Lysosome
  • Endoplasmic reticulum
  • Golgi apparatus
  • Peroxisome
Physical Properties
StateSolid
Experimental Properties
PropertyValueReference
Melting PointNot AvailableNot Available
Boiling PointNot AvailableNot Available
Water Solubility1000 mg/mLMERCK INDEX (1996)
LogPNot AvailableNot Available
Predicted Properties
PropertyValueSource
logP-1ChemAxon
pKa (strongest acidic)1.8ChemAxon
physiological charge-2ChemAxon
hydrogen acceptor count4ChemAxon
hydrogen donor count0ChemAxon
polar surface area86.25ChemAxon
rotatable bond count0ChemAxon
refractivity11.29ChemAxon
polarizability4.93ChemAxon
Spectra
SpectraNot Available
Biological Properties
Cellular Locations
  • Cytoplasm
  • Extracellular
  • Mitochondria
  • Nucleus
  • Lysosome
  • Endoplasmic reticulum
  • Golgi apparatus
  • Peroxisome
Biofluid Locations
  • Blood
  • Urine
Tissue Location
  • Kidney
  • Liver
  • Prostate
PathwaysNot Available
Normal Concentrations
BiofluidStatusValueAgeSexConditionReferenceDetails
BloodDetected and Quantified379.1 +/- 31.6 uMAdult (>18 years old)MaleNormal details
UrineDetected and Quantified1364.27 +/- 915.27 umol/mmol creatinineInfant (0-1 year old)BothNormal details
Abnormal Concentrations
BiofluidStatusValueAgeSexConditionReferenceDetails
BloodDetected and Quantified450 +/- 30 uMAdult (>18 years old)Not Specified
Hypophosphatemia
details
BloodDetected and Quantified290 +/- 50 uMAdult (>18 years old)Not Specified
Hypophosphatemia
details
BloodDetected and Quantified653.0 +/- 126.0 uMAdult (>18 years old)BothHemodialysis details
BloodDetected and Quantified270 (0-540) uMAdult (>18 years old)Not Specified
Hypophosphatemia
details
BloodDetected and Quantified610 +/- 130 uMAdult (>18 years old)Not Specified
Hypophosphatemia
details
Associated Disorders and Diseases
Disease References
Hemodialysis
  1. Oikawa O, Higuchi T, Yamazaki T, Yamamoto C, Fukuda N, Matsumoto K: Evaluation of serum fetuin-A relationships with biochemical parameters in patients on hemodialysis. Clin Exp Nephrol. 2007 Dec;11(4):304-8. Epub 2007 Dec 21. Pubmed: 18085392
Hypophosphatemia
  1. Amanzadeh J, Reilly RF Jr: Hypophosphatemia: an evidence-based approach to its clinical consequences and management. Nat Clin Pract Nephrol. 2006 Mar;2(3):136-48. Pubmed: 16932412
Associated OMIM IDsNone
DrugBank IDNot Available
DrugBank Metabolite IDDBMET00532
Phenol Explorer Compound IDNot Available
Phenol Explorer Metabolite IDNot Available
FoodDB IDFDB022617
KNApSAcK IDNot Available
Chemspider ID1032
KEGG Compound IDC00009
BioCyc IDCPD-8587
BiGG ID33499
Wikipedia LinkPhosphate
NuGOwiki LinkHMDB01429
Metagene LinkHMDB01429
METLIN ID3231
PubChem Compound1061
PDB IDPO4
ChEBI ID18367
References
Synthesis ReferenceCremer, Josef; Hartmann, Fridolin; Rodis, Franz; Hinz, Arnulf. Preparation of alkali or alkaline earth phosphates with simultaneous recovery of volatile mineral acids. Ger. (1966), 2 pp. CODEN: GWXXAW DE 1227435 19661027 CAN 66:12584 AN 1967:12584
Material Safety Data Sheet (MSDS)Download (PDF)
General References
  1. 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
  2. Hem SL, Hogenesch H: Relationship between physical and chemical properties of aluminum-containing adjuvants and immunopotentiation. Expert Rev Vaccines. 2007 Oct;6(5):685-98. Pubmed: 17931150
  3. Srivastava T, Alon US: Pathophysiology of hypercalciuria in children. Pediatr Nephrol. 2007 Oct;22(10):1659-73. Epub 2007 Apr 27. Pubmed: 17464515
  4. Pietak AM, Reid JW, Stott MJ, Sayer M: Silicon substitution in the calcium phosphate bioceramics. Biomaterials. 2007 Oct;28(28):4023-32. Epub 2007 May 17. Pubmed: 17544500
  5. Keul P, Sattler K, Levkau B: HDL and its sphingosine-1-phosphate content in cardioprotection. Heart Fail Rev. 2007 Dec;12(3-4):301-6. Pubmed: 17554629
  6. Isales CM, McDonald JM: Future developments in therapy. Ann N Y Acad Sci. 2007 Nov;1117:258-63. Epub 2007 Jun 21. Pubmed: 17584984
  7. Pumo V, Sciacca D, Malaguarnera M: Tumor lysis syndrome in elderly. Crit Rev Oncol Hematol. 2007 Oct;64(1):31-42. Epub 2007 Jul 19. Pubmed: 17658268
  8. Breitkreutz D, Braiman-Wiksman L, Daum N, Denning MF, Tennenbaum T: Protein kinase C family: on the crossroads of cell signaling in skin and tumor epithelium. J Cancer Res Clin Oncol. 2007 Nov;133(11):793-808. Epub 2007 Jul 28. Pubmed: 17661083
  9. Tiwari S, Riazi S, Ecelbarger CA: Insulin's impact on renal sodium transport and blood pressure in health, obesity, and diabetes. Am J Physiol Renal Physiol. 2007 Oct;293(4):F974-84. Epub 2007 Aug 8. Pubmed: 17686957
  10. Argraves KM, Argraves WS: HDL serves as a S1P signaling platform mediating a multitude of cardiovascular effects. J Lipid Res. 2007 Nov;48(11):2325-33. Epub 2007 Aug 13. Pubmed: 17698855
  11. Brown BA, Kantesaria PP, McDevitt LM: Fingolimod: a novel immunosuppressant for multiple sclerosis. Ann Pharmacother. 2007 Oct;41(10):1660-8. Epub 2007 Sep 4. Pubmed: 17785617
  12. Toussaint ND, Kerr PG: Vascular calcification and arterial stiffness in chronic kidney disease: implications and management. Nephrology (Carlton). 2007 Oct;12(5):500-9. Pubmed: 17803475
  13. Munteanu A, Zingg JM: Cellular, molecular and clinical aspects of vitamin E on atherosclerosis prevention. Mol Aspects Med. 2007 Oct-Dec;28(5-6):538-90. Epub 2007 Aug 3. Pubmed: 17825403
  14. Nauseef WM: How human neutrophils kill and degrade microbes: an integrated view. Immunol Rev. 2007 Oct;219:88-102. Pubmed: 17850484
  15. Allen LA, McCaffrey RL: To activate or not to activate: distinct strategies used by Helicobacter pylori and Francisella tularensis to modulate the NADPH oxidase and survive in human neutrophils. Immunol Rev. 2007 Oct;219:103-17. Pubmed: 17850485
  16. Giavazzi R, Bani MR, Taraboletti G: Tumor-host interaction in the optimization of paclitaxel-based combination therapies with vascular targeting compounds. Cancer Metastasis Rev. 2007 Dec;26(3-4):481-8. Pubmed: 17896168
  17. Tonelli M, Wiebe N, Culleton B, Lee H, Klarenbach S, Shrive F, Manns B: Systematic review of the clinical efficacy and safety of sevelamer in dialysis patients. Nephrol Dial Transplant. 2007 Oct;22(10):2856-66. Pubmed: 17906326
  18. Miyamoto K, Tatsumi S, Ito M, Segawa H: [New aspect of renal phosphate reabsorption and phosphate metabolism] Clin Calcium. 2007 Oct;17(10):1485-92. Pubmed: 17906398
  19. Michigami T: [Vitamin D metabolism and action] Clin Calcium. 2007 Oct;17(10):1493-8. Pubmed: 17906399
  20. Hoshi K: [Mechanisms of bone calcification] Clin Calcium. 2007 Oct;17(10):1499-507. Pubmed: 17906400
  21. Takeuchi Y: [Pathophysiology in rickets/osteomalacia] Clin Calcium. 2007 Oct;17(10):1508-13. Pubmed: 17906401
  22. Ito N, Fukumoto S: [FGF23-related hypophosphatemic rickets/osteomalacia] Clin Calcium. 2007 Oct;17(10):1514-20. Pubmed: 17906402
  23. Sekine T: [Rickets/osteomalacia due to tubular dysfunction] Clin Calcium. 2007 Oct;17(10):1529-33. Pubmed: 17906404
  24. Sato K: [Drug-induced osteomalacia] Clin Calcium. 2007 Oct;17(10):1536-42. Pubmed: 17906405
  25. Hasegawa Y, Miyamoto J: [Hypophosphatemic rickets/osteomalacia. - Mainly on patients with PHEX mutations -] Clin Calcium. 2007 Oct;17(10):1592-9. Pubmed: 17906414
  26. Bragadeesh TK, Mathur G, Clark AL, Cleland JG: Novel cardiac myosin activators for acute heart failure. Expert Opin Investig Drugs. 2007 Oct;16(10):1541-8. Pubmed: 17922619
  27. Worthington HV, Clarkson JE, Eden OB: Interventions for preventing oral mucositis for patients with cancer receiving treatment. Cochrane Database Syst Rev. 2007 Oct 17;(4):CD000978. Pubmed: 17943748
  28. Nixon GF, Mathieson FA, Hunter I: The potential roles of sphingolipids in vascular smooth-muscle function. Biochem Soc Trans. 2007 Nov;35(Pt 5):908-9. Pubmed: 17956243
  29. Johnson D, Shepherd RM, Gill D, Gorman T, Smith DM, Dunne MJ: Glucokinase activators: molecular tools for studying the physiology of insulin-secreting cells. Biochem Soc Trans. 2007 Nov;35(Pt 5):1208-10. Pubmed: 17956314
  30. Ku NO, Strnad P, Zhong BH, Tao GZ, Omary MB: Keratins let liver live: Mutations predispose to liver disease and crosslinking generates Mallory-Denk bodies. Hepatology. 2007 Nov;46(5):1639-49. Pubmed: 17969036
  31. Beutler E, Duparc S: Glucose-6-phosphate dehydrogenase deficiency and antimalarial drug development. Am J Trop Med Hyg. 2007 Oct;77(4):779-89. Pubmed: 17978087
  32. Van Brocklyn JR: Sphingolipid signaling pathways as potential therapeutic targets in gliomas. Mini Rev Med Chem. 2007 Oct;7(10):984-90. Pubmed: 17979800
  33. Raben DM, Tu-Sekine B: Nuclear diacylglycerol kinases: regulation and roles. Front Biosci. 2008 Jan 1;13:590-7. Pubmed: 17981572
  34. Dubin A, Estenssoro E: Mechanisms of tissue hypercarbia in sepsis. Front Biosci. 2008 Jan 1;13:1340-51. Pubmed: 17981634
  35. Deng ZL, Sharff KA, Tang N, Song WX, Luo J, Luo X, Chen J, Bennett E, Reid R, Manning D, Xue A, Montag AG, Luu HH, Haydon RC, He TC: Regulation of osteogenic differentiation during skeletal development. Front Biosci. 2008 Jan 1;13:2001-21. Pubmed: 17981687
  36. Liu X, Elojeimy S, Turner LS, Mahdy AE, Zeidan YH, Bielawska A, Bielawski J, Dong JY, El-Zawahry AM, Guo GW, Hannun YA, Holman DH, Rubinchik S, Szulc Z, Keane TE, Tavassoli M, Norris JS: Acid ceramidase inhibition: a novel target for cancer therapy. Front Biosci. 2008 Jan 1;13:2293-8. Pubmed: 17981711
  37. Su N, Du X, Chen L: FGF signaling: its role in bone development and human skeleton diseases. Front Biosci. 2008 Jan 1;13:2842-65. Pubmed: 17981758
  38. Trimble JL, Kockler DR: Statin treatment of cerebral vasospasm after aneurysmal subarachnoid hemorrhage. Ann Pharmacother. 2007 Dec;41(12):2019-23. Epub 2007 Nov 6. Pubmed: 17986515
  39. Zeitels SM, Burns JA: Office-based laryngeal laser surgery with the 532-nm pulsed-potassium-titanyl-phosphate laser. Curr Opin Otolaryngol Head Neck Surg. 2007 Dec;15(6):394-400. Pubmed: 17986877
  40. Pebay A, Bonder CS, Pitson SM: Stem cell regulation by lysophospholipids. Prostaglandins Other Lipid Mediat. 2007 Nov;84(3-4):83-97. Epub 2007 Sep 5. Pubmed: 17991611
  41. Komarova YA, Mehta D, Malik AB: Dual regulation of endothelial junctional permeability. Sci STKE. 2007 Nov 13;2007(412):re8. Pubmed: 18000237
  42. Burger EL, Patel V: Calcium phosphates as bone graft extenders. Orthopedics. 2007 Nov;30(11):939-42. Pubmed: 18019987
  43. Qin C, D'Souza R, Feng JQ: Dentin matrix protein 1 (DMP1): new and important roles for biomineralization and phosphate homeostasis. J Dent Res. 2007 Dec;86(12):1134-41. Pubmed: 18037646
  44. Andress DL: Bone and mineral guidelines for patients with chronic kidney disease: a call for revision. Clin J Am Soc Nephrol. 2008 Jan;3(1):179-83. Epub 2007 Dec 5. Pubmed: 18057310
  45. Fukumoto S: [Parathyroid and bone. Calcimimetics and bone metabolism] Clin Calcium. 2007 Dec;17(12):1865-9. Pubmed: 18057662
  46. Fei X, Qin Z, Liang Z: Contribution of CDP/Cux, a transcription factor, to cell cycle progression. Acta Biochim Biophys Sin (Shanghai). 2007 Dec;39(12):923-30. Pubmed: 18064384
  47. Bonomini F, Tengattini S, Fabiano A, Bianchi R, Rezzani R: Atherosclerosis and oxidative stress. Histol Histopathol. 2008 Mar;23(3):381-90. Pubmed: 18072094
  48. Orcel P, Chapurlat R: [Fibrous dysplasia of bone] Rev Prat. 2007 Oct 31;57(16):1749-55. Pubmed: 18092715
  49. Damron TA: Use of 3D beta-tricalcium phosphate (Vitoss) scaffolds in repairing bone defects. Nanomed. 2007 Dec;2(6):763-75. Pubmed: 18095844
  50. Hertz A, Bruce IJ: Inorganic materials for bone repair or replacement applications. Nanomed. 2007 Dec;2(6):899-918. Pubmed: 18095853
  51. Cappellini MD, Fiorelli G: Glucose-6-phosphate dehydrogenase deficiency. Lancet. 2008 Jan 5;371(9606):64-74. Pubmed: 18177777
  52. Virkki LV, Biber J, Murer H, Forster IC: Phosphate transporters: a tale of two solute carrier families. Am J Physiol Renal Physiol. 2007 Sep;293(3):F643-54. Epub 2007 Jun 20. Pubmed: 17581921
  53. Pohlmeier R, Vienken J: Phosphate removal and hemodialysis conditions. Kidney Int Suppl. 2001 Feb;78:S190-4. Pubmed: 11169009
  54. Gallar P, Ortega O, Gutierrez M, Munoz M, Hilara L, Oliet A, Rodriguez I, Gimenez E, Vigil A: [Influencing factors in the control of phosphorus in peritoneal dialysis. Therapeutic options]. Nefrologia. 2000 Jul-Aug;20(4):355-61. Pubmed: 11039261
  55. Cruz DN, Perazella MA: Biochemical aberrations in a dialysis patient following parathyroidectomy. Am J Kidney Dis. 1997 May;29(5):759-62. Pubmed: 9159312
  56. Nemere I: The ins and outs of phosphate homeostasis. Kidney Int. 2007 Jul;72(2):140-2. Pubmed: 17625581

Only showing the first 50 proteins. There are 330 proteins in total.

Enzymes

General function:
Involved in nucleotide binding
Specific function:
Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides. Helps to regulate adenosine levels (By similarity).
Gene Name:
NT5C1B
Uniprot ID:
Q96P26
Molecular weight:
68803.055
General function:
Involved in nucleotide binding
Specific function:
Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides and has a broad substrate specificity. Helps to regulate adenosine levels in heart during ischemia and hypoxia.
Gene Name:
NT5C1A
Uniprot ID:
Q9BXI3
Molecular weight:
41020.145
General function:
Involved in metal ion binding
Specific function:
Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides, with a preference for dUMP and dTMP, intermediate activity towards dGMP, and low activity towards dCMP and dAMP.
Gene Name:
NT5C
Uniprot ID:
Q8TCD5
Molecular weight:
Not Available
General function:
Involved in phosphatase activity
Specific function:
Dephosphorylates specifically the 5' and 2'(3')-phosphates of uracil and thymine deoxyribonucleotides, and so protects mitochondrial DNA replication from excess dTTP. Has only marginal activity towards dIMP and dGMP.
Gene Name:
NT5M
Uniprot ID:
Q9NPB1
Molecular weight:
Not Available
General function:
Involved in ATP citrate synthase activity
Specific function:
ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Has a central role in de novo lipid synthesis. In nervous tissue it may be involved in the biosynthesis of acetylcholine.
Gene Name:
ACLY
Uniprot ID:
P53396
Molecular weight:
120838.27
General function:
Involved in acetyl-CoA carboxylase activity
Specific function:
ACC-beta may be involved in the provision of malonyl-CoA or in the regulation of fatty acid oxidation, rather than fatty acid biosynthesis. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.
Gene Name:
ACACB
Uniprot ID:
O00763
Molecular weight:
276538.575
General function:
Involved in catalytic activity
Specific function:
Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second. Catalyzes in a tissue specific manner, the initial reactions of glucose (liver, kidney) and lipid (adipose tissue, liver, brain) synthesis from pyruvate.
Gene Name:
PC
Uniprot ID:
P11498
Molecular weight:
129632.565
General function:
Involved in acetyl-CoA carboxylase activity
Specific function:
Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.
Gene Name:
ACACA
Uniprot ID:
Q13085
Molecular weight:
269997.01
General function:
Involved in hydrolase activity
Specific function:
In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Could also be implicated in the prevention of platelet aggregation by hydrolyzing platelet-activating ADP to AMP. Hydrolyzes ATP and ADP equally well.
Gene Name:
ENTPD1
Uniprot ID:
P49961
Molecular weight:
58706.0
General function:
Involved in calcium ion binding
Specific function:
Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP. Involved in proteoglycan synthesis.
Gene Name:
CANT1
Uniprot ID:
Q8WVQ1
Molecular weight:
44839.24
General function:
Involved in hydrolase activity
Specific function:
Has a threefold preference for the hydrolysis of ATP over ADP.
Gene Name:
ENTPD3
Uniprot ID:
O75355
Molecular weight:
59104.76
General function:
Involved in catalytic activity
Specific function:
Not Available
Gene Name:
ALPP
Uniprot ID:
P05187
Molecular weight:
57953.31
General function:
Involved in catalytic activity
Specific function:
Not Available
Gene Name:
ALPI
Uniprot ID:
P09923
Molecular weight:
56811.695
General function:
Involved in acid phosphatase activity
Specific function:
Not Available
Gene Name:
ACP2
Uniprot ID:
P11117
Molecular weight:
48343.92
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
General function:
Involved in catalytic activity
Specific function:
This isozyme may play a role in skeletal mineralization.
Gene Name:
ALPL
Uniprot ID:
P05186
Molecular weight:
57304.435
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
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
General function:
Involved in catalytic activity
Specific function:
Not Available
Gene Name:
ALPPL2
Uniprot ID:
P10696
Molecular weight:
57376.515
General function:
Involved in catalytic activity
Specific function:
Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). In addition it hydrolyzes lysophosphatidic acid (LPA), ceramide-1-phosphate (C-1-P) and sphingosine-1-phosphate (S-1-P). The relative catalytic efficiency is PA > C-1-P > LPA > S-1-P.
Gene Name:
PPAP2C
Uniprot ID:
O43688
Molecular weight:
32573.435
General function:
Involved in catalytic activity
Specific function:
Broad-specificity phosphohydrolase that dephosphorylates exogenous bioactive glycerolipids and sphingolipids. Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). Pivotal regulator of lysophosphatidic acid (LPA) signaling in the cardiovascular system. Major enzyme responsible of dephosphorylating LPA in platelets, which terminates signaling actions of LPA. May control circulating, and possibly also regulate localized, LPA levels resulting from platelet activation. It has little activity towards ceramide-1-phosphate (C-1-P) and sphingosine-1-phosphate (S-1-P). The relative catalytic efficiency is LPA > PA > S-1-P > C-1-P. It's down-regulation may contribute to the development of colon adenocarcinoma.
Gene Name:
PPAP2A
Uniprot ID:
O14494
Molecular weight:
32155.715
General function:
Involved in catalytic activity
Specific function:
Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). In addition it hydrolyzes lysophosphatidic acid (LPA), ceramide-1-phosphate (C-1-P) and sphingosine-1-phosphate (S-1-P). The relative catalytic efficiency is LPA = PA > C-1-P > S-1-P. May be involved in cell adhesion and in cell-cell interactions.
Gene Name:
PPAP2B
Uniprot ID:
O14495
Molecular weight:
35115.61
General function:
Involved in ligase activity
Specific function:
Not Available
Gene Name:
PCCB
Uniprot ID:
P05166
Molecular weight:
58215.13
General function:
Involved in catalytic activity
Specific function:
Not Available
Gene Name:
PCCA
Uniprot ID:
P05165
Molecular weight:
80058.295
General function:
Involved in catalytic activity
Specific function:
Not Available
Gene Name:
GART
Uniprot ID:
P22102
Molecular weight:
107766.295
General function:
Involved in catalytic activity
Specific function:
Produces N-acetylneuraminic acid (Neu5Ac) and 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN). Can also use N-acetylmannosamine 6-phosphate and mannose 6-phosphate as substrates to generate phosphorylated forms of Neu5Ac and KDN, respectively.
Gene Name:
NANS
Uniprot ID:
Q9NR45
Molecular weight:
40307.26
General function:
Involved in inositol or phosphatidylinositol phosphatase activity
Specific function:
Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. Has 1000-fold lower activity towards inositol 1,4-bisphosphate (Ins(1,4)P2) and inositol 1,3,4-trisphosphate (Ins(1,3,4)P3), but does not hydrolyze Ins(1)P, Ins(3,4)P2, Ins(1,3,4,5)P4 or InsP6.
Gene Name:
BPNT1
Uniprot ID:
O95861
Molecular weight:
33392.035
General function:
Involved in catalytic activity
Specific function:
Involved in the urea cycle of ureotelic animals where the enzyme plays an important role in removing excess ammonia from the cell.
Gene Name:
CPS1
Uniprot ID:
P31327
Molecular weight:
165649.075
General function:
Involved in inositol or phosphatidylinositol phosphatase activity
Specific function:
Major isoenzyme hydrolyzing the calcium-mobilizing second messenger Ins(1,4,5)P3, this is a signal-terminating reaction.
Gene Name:
INPP5A
Uniprot ID:
Q14642
Molecular weight:
47819.155
General function:
Involved in inositol or phosphatidylinositol phosphatase activity
Specific function:
Not Available
Gene Name:
INPP1
Uniprot ID:
P49441
Molecular weight:
43997.62
General function:
Involved in inositol or phosphatidylinositol phosphatase activity
Specific function:
Inositol 5-phosphatase, which converts inositol 1,4,5-trisphosphate to inositol 1,4-bisphosphate. Also converts phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 4-phosphate and inositol 1,3,4,5-tetrakisphosphate to inositol 1,3,4-trisphosphate in vitro. May be involved in modulation of the function of inositol and phosphatidylinositol polyphosphate-binding proteins that are present at membranes ruffles (By similarity).
Gene Name:
INPP5J
Uniprot ID:
Q15735
Molecular weight:
70238.575
General function:
Involved in inositol or phosphatidylinositol phosphatase activity
Specific function:
Inositol 5-phosphatase which acts on inositol 1,4,5-trisphosphate, inositol 1,3,4,5-tetrakisphosphate, phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. Has 6-fold higher affinity for phosphatidylinositol 4,5-bisphosphate than for inositol 1,4,5-trisphosphate. May negatively regulate assembly of the actin cytoskeleton.
Gene Name:
INPP5K
Uniprot ID:
Q9BT40
Molecular weight:
42783.425
General function:
Involved in hydrolase activity, hydrolyzing O-glycosyl compounds
Specific function:
LPH splits lactose in the small intestine.
Gene Name:
LCT
Uniprot ID:
P09848
Molecular weight:
218584.77
General function:
Involved in phosphorylase activity
Specific function:
Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
Gene Name:
PYGL
Uniprot ID:
P06737
Molecular weight:
93133.25
General function:
Involved in phosphorylase activity
Specific function:
Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
Gene Name:
PYGM
Uniprot ID:
P11217
Molecular weight:
87316.355
General function:
Involved in phosphorylase activity
Specific function:
Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
Gene Name:
PYGB
Uniprot ID:
P11216
Molecular weight:
96695.18
General function:
Involved in catalytic activity
Specific function:
Hydrolyzes glucose-6-phosphate to glucose in the endoplasmic reticulum. Forms with the glucose-6-phosphate transporter (SLC37A4/G6PT) the complex responsible for glucose production through glycogenolysis and gluconeogenesis. Hence, it is the key enzyme in homeostatic regulation of blood glucose levels.
Gene Name:
G6PC
Uniprot ID:
P35575
Molecular weight:
40483.21
General function:
Involved in transferase activity, transferring pentosyl groups
Specific function:
Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.
Gene Name:
MTAP
Uniprot ID:
Q13126
Molecular weight:
31235.76
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
General function:
Involved in ligase activity
Specific function:
Not Available
Gene Name:
MCCC2
Uniprot ID:
Q9HCC0
Molecular weight:
61332.65
General function:
Involved in catalytic activity
Specific function:
Not Available
Gene Name:
MCCC1
Uniprot ID:
Q96RQ3
Molecular weight:
80472.45
General function:
Involved in glutamate-cysteine ligase activity
Specific function:
Not Available
Gene Name:
GCLC
Uniprot ID:
P48506
Molecular weight:
68629.42
General function:
Involved in acylphosphatase activity
Specific function:
Its physiological role is not yet clear.
Gene Name:
ACYP2
Uniprot ID:
P14621
Molecular weight:
11139.52
General function:
Involved in acylphosphatase activity
Specific function:
Its physiological role is not yet clear.
Gene Name:
ACYP1
Uniprot ID:
P07311
Molecular weight:
11260.84
General function:
Involved in catalytic activity
Specific function:
Synthesizes selenophosphate from selenide and ATP.
Gene Name:
SEPHS1
Uniprot ID:
P49903
Molecular weight:
42910.325
General function:
Involved in catalytic activity
Specific function:
Synthesizes selenophosphate from selenide and ATP.
Gene Name:
SEPHS2
Uniprot ID:
Q99611
Molecular weight:
47304.695
General function:
Involved in CTP synthase activity
Specific function:
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen.
Gene Name:
CTPS1
Uniprot ID:
P17812
Molecular weight:
66689.9
General function:
Involved in glyceraldehyde-3-phosphate dehydrogenase activity
Specific function:
May play an important role in regulating the switch between different pathways for energy production during spermiogenesis and in the spermatozoon. Required for sperm motility and male fertility (By similarity).
Gene Name:
GAPDHS
Uniprot ID:
O14556
Molecular weight:
44500.835
General function:
Involved in glyceraldehyde-3-phosphate dehydrogenase activity
Specific function:
Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC. Modulates the organization and assembly of the cytoskeleton. Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules (By similarity). Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. 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 treatment 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:
GAPDH
Uniprot ID:
P04406
Molecular weight:
31547.76
General function:
Involved in catalytic activity
Specific function:
Not Available
Gene Name:
GSS
Uniprot ID:
P48637
Molecular weight:
52384.325

Transporters

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

Only showing the first 50 proteins. There are 330 proteins in total.