Record Information
Version2.0
Creation Date2009-03-26 21:10:18 UTC
Update Date2014-12-24 20:22:37 UTC
Accession NumberT3D0709
Identification
Common NameSilver chromate
ClassSmall Molecule
DescriptionSilver chromate is a chemical compound of silver and hexavalent chromium. It is used in photography. Hexavalent chromium refers to chemical compounds that contain the element chromium in the +6 oxidation state. Chromium(VI) is more toxic than other oxidation states of the chromium atom because of its greater ability to enter cells and higher redox potential. Silver is a metallic element with the chemical symbol Ag and atomic number 47. It occurs naturally in its pure, free form, as an alloy with gold and other metals, and in minerals such as argentite and chlorargyrite. (14, 15, 10, 11)
Compound Type
  • Chromium Compound
  • Industrial/Workplace Toxin
  • Inorganic Compound
  • Pollutant
  • Silver Compound
  • Synthetic Compound
Chemical Structure
Thumb
Synonyms
Synonym
Ag2CrO4
Silver chromate(VI)
Silver chromic acid
Silver dichromate
Chemical FormulaAg2CrO4
Average Molecular Mass331.730 g/mol
Monoisotopic Mass329.730 g/mol
CAS Registry Number7784-01-2
IUPAC Namedioxo-2,4-dioxa-1,5-diargenta-3-chromapentane
Traditional Namedioxo-2,4-dioxa-1,5-diargenta-3-chromapentane
SMILES[Ag]O[Cr](=O)(=O)O[Ag]
InChI IdentifierInChI=1S/2Ag.Cr.4O
InChI KeyInChIKey=GWVVXXOAOVGAEF-UHFFFAOYSA-N
Chemical Taxonomy
Description belongs to the class of inorganic compounds known as transition metal chromates. These are inorganic compounds in which the largest oxoanion is chromate, and in which the heaviest atom is a transition metal.
KingdomInorganic compounds
Super ClassMixed metal/non-metal compounds
ClassTransition metal oxoanionic compounds
Sub ClassTransition metal chromates
Direct ParentTransition metal chromates
Alternative Parents
Substituents
  • Transition metal chromate
  • Chromate
  • Inorganic silver salt
  • Inorganic oxide
  • Inorganic salt
Molecular FrameworkNot Available
External DescriptorsNot Available
Biological Properties
StatusDetected and Not Quantified
OriginExogenous
Cellular Locations
  • Cytoplasm
  • Extracellular
Biofluid LocationsNot Available
Tissue LocationsNot Available
PathwaysNot Available
ApplicationsNot Available
Biological RolesNot Available
Chemical RolesNot Available
Physical Properties
StateSolid
AppearanceRed-brown powder.
Experimental Properties
PropertyValue
Melting PointNot Available
Boiling PointNot Available
SolubilityNot Available
LogPNot Available
Predicted Properties
PropertyValueSource
logP-1.2ChemAxon
pKa (Strongest Basic)-6.2ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count2ChemAxon
Hydrogen Donor Count0ChemAxon
Polar Surface Area52.6 ŲChemAxon
Rotatable Bond Count2ChemAxon
Refractivity5.59 m³·mol⁻¹ChemAxon
Polarizability9.74 ųChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Spectra
Spectra
Spectrum TypeDescriptionSplash KeyDeposition DateView
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-001i-0019000000-a2c15be30d4296fed7062019-02-22View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-001i-0049000000-ef7e4376e43a06296a5c2019-02-22View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-0a4i-0292000000-4d550bbea763a6b304652019-02-22View Spectrum
Toxicity Profile
Route of ExposureInhalation (10) ; oral (10) ; dermal (10)
Mechanism of ToxicityHexavalent chromium's carcinogenic effects are caused by its metabolites, pentavalent and trivalent chromium. The DNA damage may be caused by hydroxyl radicals produced during reoxidation of pentavalent chromium by hydrogen peroxide molecules present in the cell. Trivalent chromium may also form complexes with peptides, proteins, and DNA, resulting in DNA-protein crosslinks, DNA strand breaks, DNA-DNA interstrand crosslinks, chromium-DNA adducts, chromosomal aberrations and alterations in cellular signaling pathways. It has been shown to induce carcinogenesis by overstimulating cellular regulatory pathways and increasing peroxide levels by activating certain mitogen-activated protein kinases. It can also cause transcriptional repression by cross-linking histone deacetylase 1-DNA methyltransferase 1 complexes to CYP1A1 promoter chromatin, inhibiting histone modification. Chromium may increase its own toxicity by modifying metal regulatory transcription factor 1, causing the inhibition of zinc-induced metallothionein transcription. Metallic silver is oxidized and may deposit in the tissues, causing arygria. The silver ion is known to inhibit glutathione peroxidase and NA+,K+-ATPase activity, disrupting selenium-catalyzed sulfhydryl oxidation-reduction reactions and intracellular ion concentrations, respectively. Silver nanoparticles are believed to disrupt the mitochondrial respiratory chain, causing oxidative stress, reduced ATP synthesis, and DNA damage. (14, 6, 7, 8, 9, 1, 10, 2, 3, 4)
MetabolismChromium is absorbed from oral, inhalation, or dermal exposure and distributes to nearly all tissues, with the highest concentrations found in kidney and liver. Bone is also a major storage site and may contribute to long-term retention. Hexavalent chromium's similarity to sulfate and chromate allow it to be transported into cells via sulfate transport mechanisms. Inside the cell, hexavalent chromium is reduced first to pentavalent chromium, then to trivalent chromium by many substances including ascorbate, glutathione, and nicotinamide adenine dinucleotide. Chromium is almost entirely excreted with the urine. Silver compounds can also be absorbed orally and dermally. It distributes throughout the body in the blood, particularily to the liver. Insoluble silver salts are transformed into soluble silver sulfide albuminates, bind to amino or carboxyl groups in RNA, DNA, and proteins, or are reduced to metallic silver by ascorbic acid or catecholamines. Metallic silver is oxidized and may deposit in the tissues, causing arygria. Silver is eliminated primarily in the faeces. (14, 1, 10)
Toxicity ValuesNot Available
Lethal Dose1 to 3 grams for an adult human (hexavalent chromium). (5)
Carcinogenicity (IARC Classification)1, carcinogenic to humans. (13)
Uses/SourcesSilver chromate is used in photography. (11)
Minimum Risk LevelIntermediate Oral: 0.005 mg/kg/day (12) Chronic Oral: 0.001 mg/kg/day (12)
Health EffectsHexavalent chromium is a known carcinogen. Chronic inhalation especially has been linked to lung cancer. Hexavalent chromium has also been know to cause reproductive and developmental defects. Exposure to high levels of silver for a long period of time may result in a condition called arygria, a blue-gray discoloration of the skin and other body tissues. Argyria is a permanent effect but does not appear to be harmful to health. While silver itself is not toxic, most silver salts are, and may damage the liver, kidney, and central nervous system, as well as be carcinogenic. (14, 15, 16, 1)
SymptomsBreathing hexavalent chromium can cause irritation to the lining of the nose, nose ulcers, runny nose, and breathing problems, such as asthma, cough, shortness of breath, or wheezing. Ingestion of hexavalent chromium causes irritation and ulcers in the stomach and small intestine, as well as anemia. Skin contact can cause skin ulcers. Exposure to high levels of silver for a long period of time may result in a condition called arygria, a blue-gray discoloration of the skin and other body tissues. Argyria is a permanent effect but does not appear to be harmful to health. Exposure to high levels of silver in the air has resulted in breathing problems, lung and throat irritation, and stomach pains. Skin contact with silver can cause mild allergic reactions such as rash, swelling, and inflammation in some people. (14, 10)
TreatmentThere is no know antidote for chromium poisoning. Exposure is usually handled with symptomatic treatment. (10)
Normal Concentrations
Not Available
Abnormal Concentrations
Not Available
DrugBank IDNot Available
HMDB IDNot Available
PubChem Compound ID62666
ChEMBL IDNot Available
ChemSpider IDNot Available
KEGG IDNot Available
UniProt IDNot Available
OMIM ID
ChEBI IDNot Available
BioCyc IDNot Available
CTD IDC038224
Stitch IDSilver chromate
PDB IDNot Available
ACToR IDNot Available
Wikipedia LinkNot Available
References
Synthesis ReferenceNot Available
MSDST3D0709.pdf
General References
  1. Salnikow K, Zhitkovich A: Genetic and epigenetic mechanisms in metal carcinogenesis and cocarcinogenesis: nickel, arsenic, and chromium. Chem Res Toxicol. 2008 Jan;21(1):28-44. Epub 2007 Oct 30. [17970581 ]
  2. Kim G, Yurkow EJ: Chromium induces a persistent activation of mitogen-activated protein kinases by a redox-sensitive mechanism in H4 rat hepatoma cells. Cancer Res. 1996 May 1;56(9):2045-51. [8616849 ]
  3. Schnekenburger M, Talaska G, Puga A: Chromium cross-links histone deacetylase 1-DNA methyltransferase 1 complexes to chromatin, inhibiting histone-remodeling marks critical for transcriptional activation. Mol Cell Biol. 2007 Oct;27(20):7089-101. Epub 2007 Aug 6. [17682057 ]
  4. Kimura T: [Molecular mechanism involved in chromium(VI) toxicity]. Yakugaku Zasshi. 2007 Dec;127(12):1957-65. [18057785 ]
  5. Barceloux DG: Chromium. J Toxicol Clin Toxicol. 1999;37(2):173-94. [10382554 ]
  6. Bianchini A, Playle RC, Wood CM, Walsh PJ: Mechanism of acute silver toxicity in marine invertebrates. Aquat Toxicol. 2005 Mar 25;72(1-2):67-82. Epub 2004 Dec 29. [15748748 ]
  7. AshaRani PV, Low Kah Mun G, Hande MP, Valiyaveettil S: Cytotoxicity and genotoxicity of silver nanoparticles in human cells. ACS Nano. 2009 Feb 24;3(2):279-90. doi: 10.1021/nn800596w. [19236062 ]
  8. Kim S, Choi JE, Choi J, Chung KH, Park K, Yi J, Ryu DY: Oxidative stress-dependent toxicity of silver nanoparticles in human hepatoma cells. Toxicol In Vitro. 2009 Sep;23(6):1076-84. doi: 10.1016/j.tiv.2009.06.001. Epub 2009 Jun 7. [19508889 ]
  9. Dillard CJ, Tappel AL: Mercury, silver, and gold inhibition of selenium-accelerated cysteine oxidation. J Inorg Biochem. 1986 Sep;28(1):13-20. [3760861 ]
  10. ATSDR - Agency for Toxic Substances and Disease Registry (2008). Toxicological profile for chromium. U.S. Public Health Service in collaboration with U.S. Environmental Protection Agency (EPA). [Link]
  11. Wikipedia. Silver chromate. Last Updated 19 March 2009. [Link]
  12. ATSDR - Agency for Toxic Substances and Disease Registry (2001). Minimal Risk Levels (MRLs) for Hazardous Substances. U.S. Public Health Service in collaboration with U.S. Environmental Protection Agency (EPA). [Link]
  13. International Agency for Research on Cancer (2014). IARC Monographs on the Evaluation of Carcinogenic Risks to Humans. [Link]
  14. ATSDR - Agency for Toxic Substances and Disease Registry (1990). Toxicological profile for silver. U.S. Public Health Service in collaboration with U.S. Environmental Protection Agency (EPA). [Link]
  15. Wikipedia. Silver. Last updated Dec 2014. [Link]
  16. International Programme on Chemical Safety (IPCS) INCHEM (1977). WHO Food Additive Series No. 12: Silver. [Link]
Gene Regulation
Up-Regulated GenesNot Available
Down-Regulated GenesNot Available

Targets

1. DNA
General Function:
Used for biological information storage.
Specific Function:
DNA contains the instructions needed for an organism to develop, survive and reproduce.
Molecular Weight:
2.15 x 1012 Da
References
  1. ATSDR - Agency for Toxic Substances and Disease Registry (2008). Toxicological profile for chromium. U.S. Public Health Service in collaboration with U.S. Environmental Protection Agency (EPA). [Link]
General Function:
Glutathione peroxidase activity
Specific Function:
Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione. May constitute a glutathione peroxidase-like protective system against peroxide damage in sperm membrane lipids.
Gene Name:
GPX5
Uniprot ID:
O75715
Molecular Weight:
25202.14 Da
References
  1. Dillard CJ, Tappel AL: Mercury, silver, and gold inhibition of selenium-accelerated cysteine oxidation. J Inorg Biochem. 1986 Sep;28(1):13-20. [3760861 ]
General Function:
Sh3 domain binding
Specific Function:
Protects the hemoglobin in erythrocytes from oxidative breakdown.
Gene Name:
GPX1
Uniprot ID:
P07203
Molecular Weight:
22087.94 Da
References
  1. Dillard CJ, Tappel AL: Mercury, silver, and gold inhibition of selenium-accelerated cysteine oxidation. J Inorg Biochem. 1986 Sep;28(1):13-20. [3760861 ]
General Function:
Glutathione peroxidase activity
Specific Function:
Could play a major role in protecting mammals from the toxicity of ingested organic hydroperoxides. Tert-butyl hydroperoxide, cumene hydroperoxide and linoleic acid hydroperoxide but not phosphatidycholine hydroperoxide, can act as acceptors.
Gene Name:
GPX2
Uniprot ID:
P18283
Molecular Weight:
21953.835 Da
References
  1. Dillard CJ, Tappel AL: Mercury, silver, and gold inhibition of selenium-accelerated cysteine oxidation. J Inorg Biochem. 1986 Sep;28(1):13-20. [3760861 ]
General Function:
Transcription factor binding
Specific Function:
Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione.
Gene Name:
GPX3
Uniprot ID:
P22352
Molecular Weight:
25552.185 Da
References
  1. Dillard CJ, Tappel AL: Mercury, silver, and gold inhibition of selenium-accelerated cysteine oxidation. J Inorg Biochem. 1986 Sep;28(1):13-20. [3760861 ]
General Function:
Glutathione peroxidase activity
Specific Function:
Not Available
Gene Name:
GPX6
Uniprot ID:
P59796
Molecular Weight:
24970.46 Da
References
  1. Dillard CJ, Tappel AL: Mercury, silver, and gold inhibition of selenium-accelerated cysteine oxidation. J Inorg Biochem. 1986 Sep;28(1):13-20. [3760861 ]
General Function:
Peroxidase activity
Specific Function:
It protects esophageal epithelia from hydrogen peroxide-induced oxidative stress. It suppresses acidic bile acid-induced reactive oxigen species (ROS) and protects against oxidative DNA damage and double-strand breaks.
Gene Name:
GPX7
Uniprot ID:
Q96SL4
Molecular Weight:
20995.88 Da
References
  1. Dillard CJ, Tappel AL: Mercury, silver, and gold inhibition of selenium-accelerated cysteine oxidation. J Inorg Biochem. 1986 Sep;28(1):13-20. [3760861 ]
General Function:
Transcription regulatory region sequence-specific dna binding
Specific Function:
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Deacetylates SP proteins, SP1 and SP3, and regulates their function. Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons. Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B. Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation.
Gene Name:
HDAC1
Uniprot ID:
Q13547
Molecular Weight:
55102.615 Da
References
  1. Schnekenburger M, Talaska G, Puga A: Chromium cross-links histone deacetylase 1-DNA methyltransferase 1 complexes to chromatin, inhibiting histone-remodeling marks critical for transcriptional activation. Mol Cell Biol. 2007 Oct;27(20):7089-101. Epub 2007 Aug 6. [17682057 ]
General Function:
Transcriptional activator activity, rna polymerase ii core promoter proximal region sequence-specific binding
Specific Function:
Activates the metallothionein I promoter. Binds to the metal responsive element (MRE).
Gene Name:
MTF1
Uniprot ID:
Q14872
Molecular Weight:
80956.22 Da
References
  1. Kimura T: [Molecular mechanism involved in chromium(VI) toxicity]. Yakugaku Zasshi. 2007 Dec;127(12):1957-65. [18057785 ]
General Function:
Rna polymerase ii carboxy-terminal domain kinase activity
Specific Function:
Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade plays also a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis. The substrates include transcription factors (such as ATF2, BCL6, ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG), regulators of translation (such as EIF4EBP1) and a variety of other signaling-related molecules (like ARHGEF2, DCC, FRS2 or GRB10). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK/ERK signal to additional cytosolic and nuclear targets, thereby extending the specificity of the cascade. Mediates phosphorylation of TPR in respons to EGF stimulation. May play a role in the spindle assembly checkpoint. Phosphorylates PML and promotes its interaction with PIN1, leading to PML degradation.Acts as a transcriptional repressor. Binds to a [GC]AAA[GC] consensus sequence. Repress the expression of interferon gamma-induced genes. Seems to bind to the promoter of CCL5, DMP1, IFIH1, IFITM1, IRF7, IRF9, LAMP3, OAS1, OAS2, OAS3 and STAT1. Transcriptional activity is independent of kinase activity.
Gene Name:
MAPK1
Uniprot ID:
P28482
Molecular Weight:
41389.265 Da
References
  1. Kim G, Yurkow EJ: Chromium induces a persistent activation of mitogen-activated protein kinases by a redox-sensitive mechanism in H4 rat hepatoma cells. Cancer Res. 1996 May 1;56(9):2045-51. [8616849 ]
General Function:
Phosphatase binding
Specific Function:
Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade plays also a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis. The substrates include transcription factors (such as ATF2, BCL6, ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG), regulators of translation (such as EIF4EBP1) and a variety of other signaling-related molecules (like ARHGEF2, FRS2 or GRB10). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK/ERK signal to additional cytosolic and nuclear targets, thereby extending the specificity of the cascade.
Gene Name:
MAPK3
Uniprot ID:
P27361
Molecular Weight:
43135.16 Da
References
  1. Kim G, Yurkow EJ: Chromium induces a persistent activation of mitogen-activated protein kinases by a redox-sensitive mechanism in H4 rat hepatoma cells. Cancer Res. 1996 May 1;56(9):2045-51. [8616849 ]
General Function:
Phospholipid-hydroperoxide glutathione peroxidase activity
Specific Function:
Protects cells against membrane lipid peroxidation and cell death. Required for normal sperm development and male fertility. Could play a major role in protecting mammals from the toxicity of ingested lipid hydroperoxides. Essential for embryonic development. Protects from radiation and oxidative damage.
Gene Name:
GPX4
Uniprot ID:
P36969
Molecular Weight:
22174.52 Da
References
  1. Dillard CJ, Tappel AL: Mercury, silver, and gold inhibition of selenium-accelerated cysteine oxidation. J Inorg Biochem. 1986 Sep;28(1):13-20. [3760861 ]
General Function:
Peroxidase activity
Specific Function:
Not Available
Gene Name:
GPX8
Uniprot ID:
Q8TED1
Molecular Weight:
23880.83 Da
References
  1. Dillard CJ, Tappel AL: Mercury, silver, and gold inhibition of selenium-accelerated cysteine oxidation. J Inorg Biochem. 1986 Sep;28(1):13-20. [3760861 ]
General Function:
Steroid hormone binding
Specific Function:
This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients.
Gene Name:
ATP1A1
Uniprot ID:
P05023
Molecular Weight:
112895.01 Da
References
  1. Bianchini A, Playle RC, Wood CM, Walsh PJ: Mechanism of acute silver toxicity in marine invertebrates. Aquat Toxicol. 2005 Mar 25;72(1-2):67-82. Epub 2004 Dec 29. [15748748 ]
General Function:
Steroid hormone binding
Specific Function:
This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium, providing the energy for active transport of various nutrients.
Gene Name:
ATP1A2
Uniprot ID:
P50993
Molecular Weight:
112264.385 Da
References
  1. Bianchini A, Playle RC, Wood CM, Walsh PJ: Mechanism of acute silver toxicity in marine invertebrates. Aquat Toxicol. 2005 Mar 25;72(1-2):67-82. Epub 2004 Dec 29. [15748748 ]
General Function:
Steroid hormone binding
Specific Function:
This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients.
Gene Name:
ATP1A3
Uniprot ID:
P13637
Molecular Weight:
111747.51 Da
References
  1. Bianchini A, Playle RC, Wood CM, Walsh PJ: Mechanism of acute silver toxicity in marine invertebrates. Aquat Toxicol. 2005 Mar 25;72(1-2):67-82. Epub 2004 Dec 29. [15748748 ]
General Function:
Sodium:potassium-exchanging atpase activity
Specific Function:
This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients. Plays a role in sperm motility.
Gene Name:
ATP1A4
Uniprot ID:
Q13733
Molecular Weight:
114165.44 Da
References
  1. Bianchini A, Playle RC, Wood CM, Walsh PJ: Mechanism of acute silver toxicity in marine invertebrates. Aquat Toxicol. 2005 Mar 25;72(1-2):67-82. Epub 2004 Dec 29. [15748748 ]
General Function:
Sodium:potassium-exchanging atpase activity
Specific Function:
This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane.Involved in cell adhesion and establishing epithelial cell polarity.
Gene Name:
ATP1B1
Uniprot ID:
P05026
Molecular Weight:
35061.07 Da
References
  1. Bianchini A, Playle RC, Wood CM, Walsh PJ: Mechanism of acute silver toxicity in marine invertebrates. Aquat Toxicol. 2005 Mar 25;72(1-2):67-82. Epub 2004 Dec 29. [15748748 ]
General Function:
Sodium:potassium-exchanging atpase activity
Specific Function:
This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The exact function of the beta-2 subunit is not known.Mediates cell adhesion of neurons and astrocytes, and promotes neurite outgrowth.
Gene Name:
ATP1B2
Uniprot ID:
P14415
Molecular Weight:
33366.925 Da
References
  1. Bianchini A, Playle RC, Wood CM, Walsh PJ: Mechanism of acute silver toxicity in marine invertebrates. Aquat Toxicol. 2005 Mar 25;72(1-2):67-82. Epub 2004 Dec 29. [15748748 ]
General Function:
Sodium:potassium-exchanging atpase activity
Specific Function:
This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The exact function of the beta-3 subunit is not known.
Gene Name:
ATP1B3
Uniprot ID:
P54709
Molecular Weight:
31512.34 Da
References
  1. Bianchini A, Playle RC, Wood CM, Walsh PJ: Mechanism of acute silver toxicity in marine invertebrates. Aquat Toxicol. 2005 Mar 25;72(1-2):67-82. Epub 2004 Dec 29. [15748748 ]
General Function:
Transporter activity
Specific Function:
May be involved in forming the receptor site for cardiac glycoside binding or may modulate the transport function of the sodium ATPase.
Gene Name:
FXYD2
Uniprot ID:
P54710
Molecular Weight:
7283.265 Da
References
  1. Bianchini A, Playle RC, Wood CM, Walsh PJ: Mechanism of acute silver toxicity in marine invertebrates. Aquat Toxicol. 2005 Mar 25;72(1-2):67-82. Epub 2004 Dec 29. [15748748 ]