Oxalic acid (T3D0856)

IdentificationTaxonomyBiological PropertiesPhysical PropertiesToxicity ProfileSpectraConcentrationsLinksReferencesGene RegulationTargets (6)XML
Targets (6)
Record Information
Version2.0
Creation Date2009-06-09 20:08:59 UTC
Update Date2014-12-24 20:22:53 UTC
Accession NumberT3D0856
Identification
Common NameOxalic acid
ClassSmall Molecule
DescriptionOxalic acid is a dicarboxylic acid. It is a colorless crystalline solid that dissolves in water to give colorless, acidic solutions. In terms of acid strength, it is much stronger than acetic acid. Oxalic acid, because of its di-acid structure can also act as a chelating agent for metal cations. About 25% of produced oxalic acid is used as a mordant in dyeing processes. It is also used in bleaches, especially for pulpwood. Oxalic acid's main applications include cleaning (it is also found in baking powder) or bleaching, especially for the removal of rust. Oxalic acid is found in a number of common foods with members of the spinach family being particularly high in oxalates. Beat leaves, parsley, chives and cassava are quite rich in oxalate. Rhubarb leaves contain about 0.5% oxalic acid and jack-in-the-pulpit (Arisaema triphyllum) contains calcium oxalate crystals. Bacteria naturally produce oxalates from the oxidation of carbohydrates. At least two pathways exist for the enzyme-mediated formation of oxalate in humans. In one pathway, oxaloacetate (part of the citric acid cycle) can be hydrolyzed to oxalate and acetic acid by the enzyme oxaloacetase. Oxalic acid can also be generated from the dehydrogenation of glycolic acid, which is produced by the metabolism of ethylene glycol. Oxalate is a competitive inhibitor of lactate dehydrogenase (LDH). LDH catalyses the conversion of pyruvate to lactic acid oxidizing the coenzyme NADH to NAD+ and H+ concurrently. As cancer cells preferentially use aerobic glycolysis, inhibition of LDH has been shown to inhibit tumor formation and growth. However, oxalic acid is not particularly safe and is considered a mild toxin. In particular, it is a well-known uremic toxin. In humans, ingested oxalic acid has an oral lowest-published-lethal-dose of 600 mg/kg. It has been reported that the lethal oral dose is 15 to 30 grams. The toxicity of oxalic acid is due to kidney failure caused by precipitation of solid calcium oxalate, the main component of kidney stones. Oxalic acid can also cause joint pain due to the formation of similar precipitates in the joints.
Compound Type
  • Food Toxin
  • Household Toxin
  • Industrial/Workplace Toxin
  • Metabolite
  • Natural Compound
  • Organic Compound
  • Plant Toxin
  • Reducing Agent
Chemical Structure
Thumb
MOLSDFPDBSMILESInChI
Synonyms
Synonym
Ammonium oxalate
Ethane-1,2-dioate
Ethane-1,2-dioic acid
Ethanedioate
Ethanedioic acid
Ethanedioic acid dihydrate
Ethanedionate
Ethanedionic acid
Kyselina stavelova
Oxaalzuur
Oxalate
Oxalic acid 2-Hydrate
Oxalic acid anhydrous
Oxalic acid diammonium salt
Oxalic acid dihydrate
Chemical FormulaC2H2O4
Average Molecular Mass90.035 g/mol
Monoisotopic Mass89.995 g/mol
CAS Registry Number144-62-7
IUPAC Nameoxalic acid
Traditional Nameoxalic acid
SMILESOC(=O)C(O)=O
InChI IdentifierInChI=1S/C2H2O4/c3-1(4)2(5)6/h(H,3,4)(H,5,6)
InChI KeyInChIKey=MUBZPKHOEPUJKR-UHFFFAOYSA-N
Chemical Taxonomy
Description belongs to the class of organic compounds known as dicarboxylic acids and derivatives. These are organic compounds containing exactly two carboxylic acid groups.
KingdomOrganic compounds
Super ClassOrganic acids and derivatives
ClassCarboxylic acids and derivatives
Sub ClassDicarboxylic acids and derivatives
Direct ParentDicarboxylic acids and derivatives
Alternative Parents
Substituents
  • Dicarboxylic acid or derivatives
  • Carboxylic acid
  • Organic oxygen compound
  • Organic oxide
  • Hydrocarbon derivative
  • Organooxygen compound
  • Carbonyl group
  • Aliphatic acyclic compound
Molecular FrameworkAliphatic acyclic compounds
External Descriptors
Biological Properties
StatusDetected and Not Quantified
OriginEndogenous
Cellular Locations
  • Cytoplasm
  • Extracellular
  • Mitochondria
  • Peroxisome
Biofluid LocationsNot Available
Tissue Locations
  • Bladder
  • Epidermis
  • Eye Lens
  • Fibroblasts
  • Intestine
  • Kidney
  • Liver
  • Pancreas
  • Testes
Pathways
NameSMPDB LinkKEGG Link
Primary Hyperoxaluria Type ISMP00352 Not Available
Primary hyperoxaluria II, PH2SMP00558 Not Available
ApplicationsNot Available
Biological Roles
Chemical RolesNot Available
Physical Properties
StateSolid
AppearanceWhite crystals
Experimental Properties
PropertyValue
Melting Point189.5°C
Boiling PointNot Available
Solubility220 mg/mL at 25°C
LogPNot Available
Predicted Properties
PropertyValueSource
Water Solubility65.7 g/LALOGPS
logP-0.51ALOGPS
logP-0.26ChemAxon
logS-0.14ALOGPS
pKa (Strongest Acidic)1.36ChemAxon
Physiological Charge-2ChemAxon
Hydrogen Acceptor Count4ChemAxon
Hydrogen Donor Count2ChemAxon
Polar Surface Area74.6 ŲChemAxon
Rotatable Bond Count1ChemAxon
Refractivity14.44 m³·mol⁻¹ChemAxon
Polarizability6.23 ųChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Spectra
Spectra
Spectrum TypeDescriptionSplash KeyDeposition DateView
GC-MSGC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (2 TMS)splash10-0002-0900000000-eaa92cf80964dd7d345a2014-06-16View Spectrum
GC-MSGC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (Non-derivatized)splash10-0002-0900000000-b9206a3a54b5be6f07d92014-06-16View Spectrum
GC-MSGC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (2 TMS)splash10-00dj-9500000000-e5db327eab9e8a2f149e2014-06-16View Spectrum
GC-MSGC-MS Spectrum - GC-MS (2 TMS)splash10-00sl-3910000000-75af6e42d4cc12d798f42014-06-16View Spectrum
GC-MSGC-MS Spectrum - EI-B (Non-derivatized)splash10-0006-9000000000-8aef9a64d926571c2de02017-09-12View Spectrum
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-0002-0900000000-eaa92cf80964dd7d345a2017-09-12View Spectrum
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-0002-0900000000-b9206a3a54b5be6f07d92017-09-12View Spectrum
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-00dj-9500000000-e5db327eab9e8a2f149e2017-09-12View Spectrum
GC-MSGC-MS Spectrum - GC-MS (Non-derivatized)splash10-00sl-3910000000-75af6e42d4cc12d798f42017-09-12View Spectrum
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-0002-0900000000-3cee49bf06349fbe625e2017-09-12View Spectrum
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positivesplash10-000f-9000000000-f5e8094c68372ab25a632017-09-01View Spectrum
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (2 TMS) - 70eV, Positivesplash10-00xr-9510000000-28b0e365a156d2091afd2017-10-06View Spectrum
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, PositiveNot Available2021-10-12View Spectrum
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 10V, Positive (Annotated)splash10-00di-9000000000-cb3d53cc3c40c1cbbba72012-07-25View Spectrum
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 25V, Positive (Annotated)splash10-0uk9-9000000000-53a009b344e3920ffca12012-07-25View Spectrum
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 40V, Positive (Annotated)splash10-000i-9000000000-2bafb6c472ab1030cd0f2012-07-25View Spectrum
LC-MS/MSLC-MS/MS Spectrum - EI-B (Unknown) , Positivesplash10-0006-9000000000-8aef9a64d926571c2de02012-08-31View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-0006-9000000000-d1ff7c94a720b1eecaf22015-04-24View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-0006-9000000000-21d33d1d99d80526ee712015-04-24View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-0006-9000000000-ac27102ff43446c313d32015-04-24View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-000i-9000000000-fe58eaea122c39178fbe2015-04-25View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-000i-9000000000-3850c6a7016e2874d55b2015-04-25View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-000i-9000000000-32ac4118fe0eb9a5abb22015-04-25View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-000i-9000000000-43de084d66dd1bebdeac2021-09-23View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-000i-9000000000-159ed524013577f6f8012021-09-23View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-0006-9000000000-d948d5d95ae14e701f572021-09-23View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-00di-9000000000-8e2d2f7a8acc88f001952021-09-25View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-0006-9000000000-d7b47276d03e46ce72a22021-09-25View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-0006-9000000000-a1e091bb1f5fa6e9cbc72021-09-25View Spectrum
MSMass Spectrum (Electron Ionization)splash10-0002-9000000000-538465f019815d5e1b4a2014-09-20View Spectrum
1D NMR13C NMR Spectrum (1D, 100 MHz, H2O, predicted)Not Available2022-08-20View Spectrum
1D NMR13C NMR Spectrum (1D, 1000 MHz, H2O, predicted)Not Available2022-08-20View Spectrum
1D NMR13C NMR Spectrum (1D, 200 MHz, H2O, predicted)Not Available2022-08-20View Spectrum
1D NMR13C NMR Spectrum (1D, 300 MHz, H2O, predicted)Not Available2022-08-20View Spectrum
1D NMR13C NMR Spectrum (1D, 400 MHz, H2O, predicted)Not Available2022-08-20View Spectrum
1D NMR13C NMR Spectrum (1D, 500 MHz, H2O, predicted)Not Available2022-08-20View Spectrum
1D NMR13C NMR Spectrum (1D, 600 MHz, H2O, predicted)Not Available2022-08-20View Spectrum
1D NMR13C NMR Spectrum (1D, 700 MHz, H2O, predicted)Not Available2022-08-20View Spectrum
1D NMR13C NMR Spectrum (1D, 800 MHz, H2O, predicted)Not Available2022-08-20View Spectrum
1D NMR13C NMR Spectrum (1D, 900 MHz, H2O, predicted)Not Available2022-08-20View Spectrum
Toxicity Profile
Route of ExposureNot Available
Mechanism of ToxicityThe affinity of divalent metal ions is sometimes reflected in their tendency to form insoluble precipitates. Thus in the body, oxalic acid also combines with metals ions such as Ca2+, Fe2+, and Mg2+ to deposit crystals of the corresponding oxalates, which irritate the gut and kidneys. (2) Therefore the toxicity of oxalic acid is due to kidney failure caused by precipitation of solid calcium oxalate, the main component of kidney stones. Oxalic acid can also cause joint pain due to the formation of similar precipitates in the joints. Ingestion of ethylene glycol results in oxalic acid as a metabolite that can also cause acute kidney failure.
MetabolismOxalic acid is not metabolized but excreted in the urine.
Toxicity ValuesNot Available
Lethal DoseOral LDLo (lowest published lethal dose) of 600 mg/kg. It has been reported that the lethal oral dose is 15 to 30 grams.
Carcinogenicity (IARC Classification)No indication of carcinogenicity (not listed by IARC). (23)
Uses/SourcesOxalic acid and oxalates are abundantly present in many plants, most notably fat hen (lamb's quarters), sorrel, and Oxalis species. The root and/or leaves of rhubarb and buckwheat are listed being high in oxalic acid.[8] Other edible plants that contain significant concentrations of oxalic acid include—in decreasing order—star fruit (carambola), black pepper, parsley, poppy seed, amaranth, spinach, chard, beets, cocoa, chocolate, most nuts, most berries, and beans. (22)
Minimum Risk LevelNot Available
Health EffectsBecause it binds vital nutrients such as calcium, long-term consumption of foods high in oxalic acid can be problematic. Healthy individuals can safely consume such foods in moderation, but those with kidney disorders, gout, rheumatoid arthritis, or certain forms of chronic vulvar pain (vulvodynia) are typically advised to avoid foods high in oxalic acid or oxalates. The calcium oxalate precipitate (better known as kidney stones) obstruct the kidney tubules. Conversely, calcium supplements taken along with foods high in oxalic acid can cause calcium oxalate to precipitate out in the gut and drastically reduce the levels of oxalate absorbed by the body (by 97% in some cases.) Chronically high levels of oxalic acid are associated with at least 2 inborn errors of metabolism including: Type I primary hyperoxaluria and Primary hyperoxaluria. Oxalate stones in primary hyperoxaluria tend to be severe, resulting in relatively early kidney damage (before age 20), which impairs the excretion of oxalate leading to a further acceleration in accumulation of oxalate in the body. After the development of renal failure patients may develop oxalate deposits in the bones, joints and bone marrow. Severe cases may develop haematological problems such as anaemia and thrombocytopaenia. The deposition of oxalate in the body is sometimes called "oxalosis" to be distinguished from "oxaluria" which refers to oxalate in the urine.
SymptomsOxalic acid poisoning symptoms include weakness, burning in the mouth, death from cardiovascular collapse, on the respiratory system, throat – burning in the throat, abdominal pain, nausea, vomiting, diarrhea, convulsions, and coma.
TreatmentAcute Exposure: If oxalic acid is swallowed, immediately give the person water or milk, unless instructed otherwise by a health care provider. DO NOT give water or milk if the person is having symptoms (such as vomiting, convulsions, or a decreased level of alertness) that make it hard to swallow. If acute exposure occurs to the eyes, irrigate opened eyes for several minutes under running water. Chronic exposure: in some patients with primary hyperoxaluria type 1, pyridoxine treatment (vitamin B6) may decrease oxalate excretion and prevent kidney stone formation.
Normal Concentrations
Not Available
Abnormal Concentrations
Not Available
DrugBank IDDB03902
HMDB IDHMDB02329
PubChem Compound ID971
ChEMBL IDCHEMBL146755
ChemSpider ID946
KEGG IDC00209
UniProt IDNot Available
OMIM ID109600 , 138500 , 167030 , 240400 , 259900 , 260000 , 260005
ChEBI ID16995
BioCyc IDCUPRIZONE
CTD IDD019815
Stitch IDOxalic Acid
PDB IDOXD
ACToR ID3709
Wikipedia LinkOxalic acid
References
Synthesis Reference

Giuseppe Messina, Giovanni M. Sechi, Loreno Lorenzoni, Giovanni Chessa, “Method of preparation of oxalic acid esters and amides.” U.S. Patent US4981963, issued July, 1971.

MSDSLink
General References
  1. de O G Mendonca C, Martini LA, Baxmann AC, Nishiura JL, Cuppari L, Sigulem DM, Heilberg IP: Effects of an oxalate load on urinary oxalate excretion in calcium stone formers. J Ren Nutr. 2003 Jan;13(1):39-46. [12563622 ]
  2. Singh S, Tai C, Ganz G, Yeung CK, Magil A, Rosenberg F, Applegarth D, Levin A: Steroid-responsive pleuropericarditis and livedo reticularis in an unusual case of adult-onset primary hyperoxaluria. Am J Kidney Dis. 1999 Apr;33(4):e5. [10196036 ]
  3. Astarcioglu I, Karademir S, Gulay H, Bora S, Astarcioglu H, Kavukcu S, Turkmen M, Soylu A: Primary hyperoxaluria: simultaneous combined liver and kidney transplantation from a living related donor. Liver Transpl. 2003 Apr;9(4):433-6. [12682898 ]
  4. Selvam R, Kalaiselvi P: A novel basic protein from human kidney which inhibits calcium oxalate crystal growth. BJU Int. 2000 Jul;86(1):7-13. [10886075 ]
  5. Kwak C, Jeong BC, Kim HK, Kim EC, Chox MS, Kim HH: Molecular epidemiology of fecal Oxalobacter formigenes in healthy adults living in Seoul, Korea. J Endourol. 2003 May;17(4):239-43. [12816588 ]
  6. Vicanova J, Boelsma E, Mommaas AM, Kempenaar JA, Forslind B, Pallon J, Egelrud T, Koerten HK, Ponec M: Normalization of epidermal calcium distribution profile in reconstructed human epidermis is related to improvement of terminal differentiation and stratum corneum barrier formation. J Invest Dermatol. 1998 Jul;111(1):97-106. [9665394 ]
  7. Mydlik M, Derzsiova K, Pribylincova V, Reznicek J: [Urinary oxalic acid excretion in chronic kidney failure and after kidney transplantation]. Vnitr Lek. 1996 Dec;42(12):813-7. [9072879 ]
  8. Mizusawa Y, Parnham AP, Falk MC, Burke JR, Nicol D, Yamanaka J, Lynch SV, Strong RW: Potential for bilateral nephrectomy to reduce oxalate release after combined liver and kidney transplantation for primary hyperoxaluria type 1. Clin Transplant. 1997 Oct;11(5 Pt 1):361-5. [9361924 ]
  9. Pecorella I, McCartney AC, Lucas S, Michaels L, Ciardi A, Di Tondo U, Garner A: Histological study of oxalosis in the eye and adnexa of AIDS patients. Histopathology. 1995 Nov;27(5):431-8. [8575733 ]
  10. Huang MY, Chaturvedi LS, Koul S, Koul HK: Oxalate stimulates IL-6 production in HK-2 cells, a line of human renal proximal tubular epithelial cells. Kidney Int. 2005 Aug;68(2):497-503. [16014026 ]
  11. Shapiro R, Weismann I, Mandel H, Eisenstein B, Ben-Ari Z, Bar-Nathan N, Zehavi I, Dinari G, Mor E: Primary hyperoxaluria type 1: improved outcome with timely liver transplantation: a single-center report of 36 children. Transplantation. 2001 Aug 15;72(3):428-32. [11502971 ]
  12. Motoyoshil Y, Hattori M, Chikamoto H, Nakakura H, Furue T, Miyakawa S, Kohno M, Ito K, Kai K, Nakajima I, Fuchinoue S, Teraoka S, Akiba T, Kitayama H, Wada N, Ogawa Y: [Sequential combined liver-kidney transplantation for a one-year-old boy with infantile primary hyperoxaluria type 1]. Nihon Jinzo Gakkai Shi. 2006;48(1):22-8. [16480063 ]
  13. de Water R, Noordermeer C, van der Kwast TH, Nizze H, Boeve ER, Kok DJ, Schroder FH: Calcium oxalate nephrolithiasis: effect of renal crystal deposition on the cellular composition of the renal interstitium. Am J Kidney Dis. 1999 Apr;33(4):761-71. [10196021 ]
  14. van Woerden CS, Groothof JW, Wanders RJ, Waterham HR, Wijburg FR: [From gene to disease; primary hyperoxaluria type I caused by mutations in the AGXT gene]. Ned Tijdschr Geneeskd. 2006 Jul 29;150(30):1669-72. [16922352 ]
  15. Pirulli D, Marangella M, Amoroso A: Primary hyperoxaluria: genotype-phenotype correlation. J Nephrol. 2003 Mar-Apr;16(2):297-309. [12768081 ]
  16. Amoroso A, Pirulli D, Florian F, Puzzer D, Boniotto M, Crovella S, Zezlina S, Spano A, Mazzola G, Savoldi S, Ferrettini C, Berutti S, Petrarulo M, Marangella M: AGXT gene mutations and their influence on clinical heterogeneity of type 1 primary hyperoxaluria. J Am Soc Nephrol. 2001 Oct;12(10):2072-9. [11562405 ]
  17. Robertson WG: Renal stones in the tropics. Semin Nephrol. 2003 Jan;23(1):77-87. [12563603 ]
  18. Nakagawa Y, Abram V, Parks JH, Lau HS, Kawooya JK, Coe FL: Urine glycoprotein crystal growth inhibitors. Evidence for a molecular abnormality in calcium oxalate nephrolithiasis. J Clin Invest. 1985 Oct;76(4):1455-62. [4056037 ]
  19. Massey LK, Palmer RG, Horner HT: Oxalate content of soybean seeds (Glycine max: Leguminosae), soyfoods, and other edible legumes. J Agric Food Chem. 2001 Sep;49(9):4262-6. [11559120 ]
  20. Petrarulo M, Vitale C, Facchini P, Marangella M: Biochemical approach to diagnosis and differentiation of primary hyperoxalurias: an update. J Nephrol. 1998 Mar-Apr;11 Suppl 1:23-8. [9604805 ]
  21. New Zealand Food Safety Authority (2009). Natural Toxins In Food. [Link]
  22. Wikipedia. Oxalic Acid. Last Updated 20 April 2009. [Link]
  23. International Agency for Research on Cancer (2014). IARC Monographs on the Evaluation of Carcinogenic Risks to Humans. [Link]
Gene Regulation
Up-Regulated Genes
GeneGene SymbolGene IDInteractionChromosomeDetails
Down-Regulated GenesNot Available

Targets

Target Details
1. Proto-oncogene tyrosine-protein kinase Src
General Function:
Sh3/sh2 adaptor activity
Specific Function:
Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates such as AFAP1. Phosphorylation of AFAP1 allows the SRC SH2 domain to bind AFAP1 and to localize to actin filaments. Cytoskeletal reorganization is also controlled through the phosphorylation of cortactin (CTTN). When cells adhere via focal adhesions to the extracellular matrix, signals are transmitted by integrins into the cell resulting in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN). In addition to phosphorylating focal adhesion proteins, SRC is also active at the sites of cell-cell contact adherens junctions and phosphorylates substrates such as beta-catenin (CTNNB1), delta-catenin (CTNND1), and plakoglobin (JUP). Another type of cell-cell junction, the gap junction, is also a target for SRC, which phosphorylates connexin-43 (GJA1). SRC is implicated in regulation of pre-mRNA-processing and phosphorylates RNA-binding proteins such as KHDRBS1. Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors. Involved in the RAS pathway through phosphorylation of RASA1 and RASGRF1. Plays a role in EGF-mediated calcium-activated chloride channel activation. Required for epidermal growth factor receptor (EGFR) internalization through phosphorylation of clathrin heavy chain (CLTC and CLTCL1) at 'Tyr-1477'. Involved in beta-arrestin (ARRB1 and ARRB2) desensitization through phosphorylation and activation of ADRBK1, leading to beta-arrestin phosphorylation and internalization. Has a critical role in the stimulation of the CDK20/MAPK3 mitogen-activated protein kinase cascade by epidermal growth factor. Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus. Plays an important role in osteoclastic bone resorption in conjunction with PTK2B/PYK2. Both the formation of a SRC-PTK2B/PYK2 complex and SRC kinase activity are necessary for this function. Recruited to activated integrins by PTK2B/PYK2, thereby phosphorylating CBL, which in turn induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function. Promotes energy production in osteoclasts by activating mitochondrial cytochrome C oxidase. Phosphorylates DDR2 on tyrosine residues, thereby promoting its subsequent autophosphorylation. Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-731'. Enhances DDX58/RIG-I-elicited antiviral signaling. Phosphorylates PDPK1 at 'Tyr-9', 'Tyr-373' and 'Tyr-376'. Phosphorylates BCAR1 at 'Tyr-128'. Phosphorylates CBLC at multiple tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3 activity. Required for podosome formation (By similarity).
Gene Name:
SRC
Uniprot ID:
P12931
Molecular Weight:
59834.295 Da
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. [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. [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. [10592235 ]
Target Details
2. Prothrombin
General Function:
Thrombospondin receptor activity
Specific Function:
Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing.
Gene Name:
F2
Uniprot ID:
P00734
Molecular Weight:
70036.295 Da
References
  1. Moryama MT, Domiki C, Miyazawa K, Tanaka T, Suzuki K: Effects of oxalate exposure on Madin-Darby canine kidney cells in culture: renal prothrombin fragment-1 mRNA expression. Urol Res. 2005 Dec;33(6):470-5. Epub 2005 Dec 1. [16320015 ]
  2. Sekiya K, Okuda H: Inhibitory action of soluble elastin on thromboxane B2 formation in blood platelets. Biochim Biophys Acta. 1984 Mar 1;797(3):348-53. [6320905 ]
Target Details
3. Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial
General Function:
Ubiquinone binding
Specific Function:
Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Gene Name:
SDHD
Uniprot ID:
O14521
Molecular Weight:
17042.82 Da
References
  1. Wozniak AJ, Glisson BS, Hande KR, Ross WE: Inhibition of etoposide-induced DNA damage and cytotoxicity in L1210 cells by dehydrogenase inhibitors and other agents. Cancer Res. 1984 Feb;44(2):626-32. [6318974 ]
Target Details
4. Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial
General Function:
Succinate dehydrogenase activity
Specific Function:
Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). Can act as a tumor suppressor.
Gene Name:
SDHA
Uniprot ID:
P31040
Molecular Weight:
72690.975 Da
References
  1. Wozniak AJ, Glisson BS, Hande KR, Ross WE: Inhibition of etoposide-induced DNA damage and cytotoxicity in L1210 cells by dehydrogenase inhibitors and other agents. Cancer Res. 1984 Feb;44(2):626-32. [6318974 ]
Target Details
5. Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial
General Function:
Ubiquinone binding
Specific Function:
Iron-sulfur protein (IP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Gene Name:
SDHB
Uniprot ID:
P21912
Molecular Weight:
31629.365 Da
References
  1. Wozniak AJ, Glisson BS, Hande KR, Ross WE: Inhibition of etoposide-induced DNA damage and cytotoxicity in L1210 cells by dehydrogenase inhibitors and other agents. Cancer Res. 1984 Feb;44(2):626-32. [6318974 ]
Target Details
6. Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
General Function:
Succinate dehydrogenase activity
Specific Function:
Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Gene Name:
SDHC
Uniprot ID:
Q99643
Molecular Weight:
18610.03 Da
References
  1. Wozniak AJ, Glisson BS, Hande KR, Ross WE: Inhibition of etoposide-induced DNA damage and cytotoxicity in L1210 cells by dehydrogenase inhibitors and other agents. Cancer Res. 1984 Feb;44(2):626-32. [6318974 ]