260PathwayLabetalol Action PathwayLabetalol (also known as Albetol or Ibidomide) is an inhibitor/antagonist of beta-1 adrenergic receptor that can be used for treating high blood pressure and reducing cardiac output. Labetalol can bind to beta-1 adrenergic receptor on both vascular smooth muscle, which lead to inhibition of vasoconstriction in peripheral blood vessels and adrenergic stimulation of endothelial cell function. Drug ActionPW000389TopPathwayVisualizationContext4058001500#000099PathwayVisualization289260Labetalol PathwayLabetalol (also known as Albetol or Ibidomide) is an inhibitor/antagonist of beta-1 adrenergic receptor that can be used for treating high blood pressure and reducing cardiac output. Labetalol can bind to beta-1 adrenergic receptor on both vascular smooth muscle, which lead to inhibition of vasoconstriction in peripheral blood vessels and adrenergic stimulation of endothelial cell function. Drug1444Labetalol inhibition of Beta-1 adrenergic receptorInhibitorySubPathway7019087Compound65702104ProteinComplex65445Labetalol inhibition of Alpha-1A adrenergic receptorInhibitorySubPathway7039087Compound52704749ProteinComplex521252Borchard, U. Pharmacological properties of beta-adrenoceptor blocking drugs. Journal of Clinical and Basic Cardiology. 1998;1(1):5-9.260Pathway1253DiPiro, J.T., Talbert, R.L., Yee, G.C., Matzke, G.R., Wells, B.G, & Posey, M.L. Pharmacotherapy: A pathologic approach. (6th ed) (2005) p.207-208. New York: McGraw-Hill Medical Publishing Division.260Pathway1254Trandate. (2009). e-CPS (online version of Compendium of Pharmaceuticals and Specialties). Retrieved July 25, 2009.260Pathway4Cardiomyocyte CL:00007466MyocyteCL:00001873NeuronCL:00005401Homo sapiens9606EukaryoteHuman62Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)62977Prokaryote10Cell MembraneGO:000588611HeartBTO:000056273105cardiocyteBTO:00015399MuscleBTO:00008871411865111PW_BS00006514101PW_BS0000143451014PW_BS000034451014PW_BS00004511PW_BS00000165110624PW_BS0005085291016PW_BS000052731013PW_BS0000739087LaβlolHMDB0014736Labetalol is only found in individuals that have used or taken this drug. It is a blocker of both alpha- and beta-adrenergic receptors that is used as an antihypertensive (PubChem). Labetalol HCl combines both selective, competitive, alpha-1-adrenergic blocking and nonselective, competitive, beta-adrenergic blocking activity in a single substance. In man, the ratios of alpha- to beta- blockade have been estimated to be approximately 1:3 and 1:7 following oral and intravenous (IV) administration, respectively. The principal physiologic action of labetalol is to competitively block adrenergic stimulation of β-receptors within the myocardium (β1-receptors) and within bronchial and vascular smooth muscle (β2-receptors), and α1-receptors within vascular smooth muscle. This causes a decrease in systemic arterial blood pressure and systemic vascular resistance without a substantial reduction in resting heart rate, cardiac output, or stroke volume, apparently because of its combined α- and β-adrenergic blocking activity.36894-69-6C07063386963433734DB00598CC(CCC1=CC=CC=C1)NCC(O)C1=CC(C(N)=O)=C(O)C=C1C19H24N2O3InChI=1S/C19H24N2O3/c1-13(7-8-14-5-3-2-4-6-14)21-12-18(23)15-9-10-17(22)16(11-15)19(20)24/h2-6,9-11,13,18,21-23H,7-8,12H2,1H3,(H2,20,24)SGUAFYQXFOLMHL-UHFFFAOYSA-N2-hydroxy-5-{1-hydroxy-2-[(4-phenylbutan-2-yl)amino]ethyl}benzamide328.4055328.178692644-4.754labetalol01Labetolol;Labetalolum [inn-latin];3-carboxamido-4-hydroxy-alpha-((1-methyl-3-phenylpropylamino)methyl)benzyl alcohol;5-(1-hydroxy-2-(1-methyl-3-phenylpropylamino)ethyl)salicylamide;Labetalolum;3-carboxamido-4-hydroxy-a-((1-methyl-3-phenylpropylamino)methyl)benzyl alcohol;3-carboxamido-4-hydroxy-α-((1-methyl-3-phenylpropylamino)methyl)benzyl alcoholPW_C009087Laβlol3032651513Beta-1 adrenergic receptorP08588Beta-adrenergic receptors mediate the catecholamine- induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinityHMDBP01632ADRB110q24-q26AY567837174614108234117045301365434011361286512654Alpha-1A adrenergic receptorP35348This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol- calcium second messenger system. Its effect is mediated by G(q) and G(11) proteinsHMDBP07433ADRA1A8p21.2AY3895051303452318373104Beta-1 adrenergic receptor1PW_P0001041191513749Alpha-1A adrenergic receptor1PW_P000749844265416085908765157false3657010regular200190101669087157false9007010regular200190250215136580false3603408subunitregular200130250326545280false8953358subunitregular20013022401042896524952502224174928952249625039251M465 260 C464 296 464 290 465 365 148false18falsetrueM 410.0013331555819 205.19998222459225 L 425 205 L 439.9986668444181 204.800017775407759252M400 410 C370 410 367 130 337 130 5true189255M1000 260 C1000 289 999 332 1000 360 148false18falsetrueM 930 225 L 930 210 L 930 1959256M935 405 C905 405 922 150 892 150 5true1816110M900 165 C862 165 597 166 565 166 83false18trueM 887.0096189432334 172.5 L 900 165 L 887.0096189432334 157.5falsetrueM 577.9903810567666 158.5 L 565 166 L 577.9903810567666 173.5false47544428914true1879516regular46860859251Left14422409252Right47644528914true74211516regular46960859255Left14522419256Right6310166171161103677310501.01.002101762163681411310700.40.40218423333386M275 510 C275 460 325 410 375 410 C434 410 511 410 570 410 C620 410 670 460 670 510 C670 542 670 583 670 615 C670 665 620 715 570 715 C511 715 434 715 375 715 C325 715 275 665 275 615 C275 583 275 542 275 510 1true6395.0305.0387M820 505 C820 455 870 405 920 405 C973 405 1042 405 1095 405 C1145 405 1195 455 1195 505 C1195 537 1195 580 1195 612 C1195 662 1145 712 1095 712 C1042 712 973 712 920 712 C870 712 820 662 820 612 C820 580 820 537 820 505 1true6375.0307.062815Cardiomyocyte385610201.01.01601562915Myocyte925605201.01.016015163112170215337277693945127361641378137761341258768404497734CenterPathwayVisualizationContext76747003450#000099PathwayVisualization355373Striated Muscle ContractionTubular striated muscle cells (i.e. skeletal and cardiac myocytes) are composed of bundles of rod-like myofibrils. Each individual myofibril consists of many repeating units called sarcomeres. These functional units, in turn, are composed of many alternating actin and mysoin protein filaments that produce muscle contraction. The muscle contraction process is initiated when the muscle cell is depolarized enough for an action potential to occur. When acetylcholine is released from the motor neuron axon terminals that are adjacent to the muscle cells, it binds to receptors on the sarcolemma (muscle cell membrane), causing nicotinic acetylcholine receptors to be activated and the sodium/potassium channels to be opened. The fast influx of sodium and slow efflux of potassium through the channel causes depolarization. The resulting action potential that is generated travels along the sarcolemma and down the T-tubule, activating the L-type voltage-dependent calcium channels on the sarcolemma and ryanodine receptors on the sarcoplasmic reticulum. When these are activated, it triggers the release of calcium ions from the sarcoplasmic reticulum into the cytosol. From there, the calcium ions bind to the protein troponin which displaces the tropomysoin filaments from the binding sites on the actin filaments. This allows for myosin filaments to be able to bind to the actin. According to the Sliding Filament Theory, the myosin heads that have an ADP and phosphate attached binds to the actin, forming a cross-bridge. Once attached, the myosin performs a powerstroke which slides the actin filaments together. The ATP and phosphate are dislodged during this process. However, ATP now binds to the myosin head, which causes the myosin to detach from the actin. The cycle repeats once the attached ATP dissociates into ADP and phosphate, and the myosin performs another powerstroke, bringing the actin filaments even closer together. Numerous actin filaments being pulled together simultaneously across many muscles cells triggers muscle contraction.Physiological1318G-protein signalling cascadeActivatingSubPathway478694ProteinComplex45479676ProteinComplex319Cardiac phospholamban inhibits Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 InhibitorySubPathway480696ProteinComplex47481695ProteinComplex320G-protein signalling cascadeActivatingSubPathway482104ProteinComplex45483217ProteinComplex46484218ProteinComplex46321cAMP-dependent protein kinase catalytic subunit alpha activates Voltage-depenent L-type calcium channelActivatingSubPathway485217ProteinComplex46486321ProteinComplex45322cAMP-dependent protein kinase catalytic subunit alpha activates Ryanodine receptor 2ActivatingSubPathway487217ProteinComplex4648879ProteinComplex47325Calcium activates Ryanodine receptor 2 ActivatingSubPathway493353Compound4649479ProteinComplex47109962Muscle ContractionSubPathway109520996ProteinComplex5027987115173218Cooke R: The sliding filament model: 1972-2004. J Gen Physiol. 2004 Jun;123(6):643-56. doi: 10.1085/jgp.200409089.373Pathway2798724610574Szent-Gyorgyi A: The mechanism of muscle contraction. Proc Natl Acad Sci U S A. 1974 Sep;71(9):3343-4.373Pathway27987325646377Kuo IY, Ehrlich BE: Signaling in muscle contraction. Cold Spring Harb Perspect Biol. 2015 Feb 2;7(2):a006023. doi: 10.1101/cshperspect.a006023.373Pathway6MyocyteCL:00001871CellCL:00000007Epithelial CellCL:00000663NeuronCL:00005408Beta cellCL:00006392Platelet CL:00002334Cardiomyocyte CL:00007465HepatocyteCL:00001829Pancreatic Beta CellCL:00001691Homo sapiens9606EukaryoteHuman3Escherichia coli562Prokaryote18Saccharomyces cerevisiae4932EukaryoteYeast23Pseudomonas aeruginosa287Prokaryote12Mus musculus10090EukaryoteMouse5Bos taurus9913EukaryoteCattle17Rattus norvegicus10116EukaryoteRat24Solanum lycopersicum4081EukaryoteTomato4Arabidopsis thaliana3702EukaryoteThale cress51Picea sitchensis3332EukaryoteSitka spruce10Drosophila melanogaster7227EukaryoteFruit fly6Caenorhabditis elegans6239EukaryoteRoundworm2Bacteria2ProkaryoteBacteria19Schizosaccharomyces pombe4896Eukaryote21Xenopus laevis8355EukaryoteAfrican clawed frog25Escherichia coli (strain K12)83333Prokaryote49Bathymodiolus platifrons220390EukaryoteDeep sea mussel60Nitzschia sp.0001EukaryoteNitzschia429Saccharomyces cerevisiae (strain ATCC 204508 / S288c)559292EukaryoteBaker's yeast62Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)62977Prokaryote5CytoplasmGO:000573711Extracellular SpaceGO:00056151CytosolGO:000582931Periplasmic SpaceGO:000562035ChloroplastGO:000950710Cell MembraneGO:000588619sarcoplasmic reticulumGO:00165292MitochondrionGO:00057397Endoplasmic Reticulum MembraneGO:000578924Mitochondrial Intermembrane SpaceGO:000575825Golgi apparatusGO:000579414Mitochondrial Outer MembraneGO:000574112Mitochondrial Inner MembraneGO:000574313Endoplasmic ReticulumGO:00057836LysosomeGO:000576416Lysosomal LumenGO:004320236MembraneGO:00160203Mitochondrial MatrixGO:000575915NucleusGO:00056344PeroxisomeGO:000577727Peroxisome MembraneGO:000577832Inner MembraneGO:007025818Melanosome MembraneGO:003316220Endoplasmic Reticulum LumenGO:000578821SynapseGO:004520253Endoplasmic Reticulum BodyGO:001016834Plant-Type VacuoleGO:000032540PeriplasmGO:004259756Basal Cell MembraneGO:000992522post-synaptic membraneGO:00452119MuscleBTO:00008871411825IntestineBTO:00006488Blood VesselBTO:000110274113Sympathetic Nervous SystemBTO:000183218PancreasBTO:00009882Endothelium BTO:00003935cardiocyteBTO:00015391LiverBTO:00007597297Nervous SystemBTO:00014844Adrenal 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is essential for the normal growth and maintenance of bones and teeth, and calcium requirements must be met throughout life. Requirements are greatest during periods of growth, such as childhood, during pregnancy and when breast-feeding. Long-term calcium deficiency can lead to osteoporosis, in which the bone deteriorates and there is an increased risk of fractures. Adults need between 1,000 and 1,300 mg of calcium in their daily diet. Calcium is essential for living organisms, particularly in cell physiology, and is the most common metal in many animals. Physiologically, it exists as an ion in the body. Calcium combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes. Calcium is an important component of a healthy diet. A deficit can affect bone and tooth formation, while overretention can cause kidney stones. Vitamin D is needed to absorb calcium. Dairy products, such as milk and cheese, are a well-known source of calcium. However, some individuals are allergic to dairy products and even more people, particularly those of non-European descent, are lactose-intolerant, leaving them unable to consume dairy products. Fortunately, many other good sources of calcium exist. These include: seaweeds such as kelp, wakame and hijiki; nuts and seeds (like almonds and sesame); beans; amaranth; collard greens; okra; rutabaga; broccoli; kale; and fortified products such as orange juice and soy milk. Calcium has also been found to assist in the production of lymphatic fluids.14127-61-8C0007627129108CA%2b2266DB01373[Ca++]CaInChI=1S/Ca/q+2BHPQYMZQTOCNFJ-UHFFFAOYSA-Ncalcium(2+) ion40.07839.9625911550calcium(2+) ion22FDB003513Ca;Calcium element;Ca(2+);Ca2+;Calcium ion;Calcium, doubly charged positive ionPW_C000353Ca2+276163038553146012941159932199735104631163461164471478491491421552432116582138172796182937931597131607239422941866647821048222853401115780101717920572322117258160728119011774213118371981184221012198164122152851528815115350308693361773893317760011578154132782663567852634578724130789081148041374805892288182651120220122120465405121049124121300418121377419121850383121923125122370409122895135123099376123613118123870454123936455124403398124476136124924137125571297125711478125981489126009299126050490126533495127203209127434506127460388127502507128105390458SodiumHMDB0000588Sodium ions are necessary for regulation of blood and body fluids, transmission of nerve impulses, heart activity, and certain metabolic functions. Physiologically, it exists as an ion in the body. Sodium is needed by animals, which maintain high concentrations in their blood and extracellular fluids, but the ion is not needed by plants. The human requirement for sodium in the diet is less than 500 mg per day, which is typically less than a tenth as much as many diets "seasoned to taste." Most people consume far more sodium than is physiologically needed. For certain people with salt-sensitive blood pressure, this extra intake may cause a negative effect on health.17341-25-2C0133092329101899[Na+]NaInChI=1S/Na/q+1FKNQFGJONOIPTF-UHFFFAOYSA-Nsodium(1+) ion22.989822.9897696750sodium(1+) ion11FDB003523Sodium;Sodium ion;Na(+);Na+PW_C000458Na+209315209422724602725613157713158723185743615514607858601055861107586210871491877150188423373184233831578239353782433267824935279047132122389436122390437122635416122636124124942472124946452124960471125209118457PotassiumHMDB0000586Potassium is an essential electrolyte. Potassium balance is crucial for regulating the excitability of nerves and muscles and so critical for regulating contractility of cardiac muscle. Although the most important changes seen in the presence of deranged potassium are cardiac, smooth muscle is also affected with increasing muscle weakness, a feature of both hyperkalaemia and hypokalaemia. Physiologically, it exists as an ion in the body. Potassium (K+) is a positively charged electrolyte, cation, which is present throughout the body in both intracellular and extracellular fluids. The majority of body potassium, >90%, are intracellular. It moves freely from intracellular fluid (ICF) to extracellular fluid (ECF) and vice versa when adenosine triphosphate increases the permeability of the cell membrane. It is mainly replaced inside or outside the cells by another cation, sodium (Na+). The movement of potassium into or out of the cells is linked to certain body hormones and also to certain physiological states. Standard laboratory tests measure ECF potassium. Potassium enters the body rapidly during food ingestion. Insulin is produced when a meal is eaten; this causes the temporary movement of potassium from ECF to ICF. Over the ensuing hours, the kidneys excrete the ingested potassium and homeostasis is returned. In the critically ill patient, suffering from hyperkalaemia, this mechanism can be manipulated beneficially by administering high concentration (50%) intravenous glucose. Insulin can be added to the glucose, but glucose alone will stimulate insulin production and cause movement of potassium from ECF to ICF. The stimulation of alpha receptors causes increased movement of potassium from ICF to ECF. A noradrenaline infusion can elevate serum potassium levels. An adrenaline infusion, or elevated adrenaline levels, can lower serum potassium levels. Metabolic acidosis causes a rise in extracellular potassium levels. In this situation, excess of hydrogen ions (H+) are exchanged for intracellular potassium ions, probably as a result of the cellular response to a falling blood pH. Metabolic alkalosis causes the opposite effect, with potassium moving into the cells. (PMID: 17883675).24203-36-9C0023881329103K%2b791DB01345[K+]KInChI=1S/K/q+1NPYPAHLBTDXSSS-UHFFFAOYSA-Npotassium(1+) ion39.098338.9637068610potassium(1+) ion11FDB003521K+;Kalium;Potassium;Potassium (k+);Potassium (ion);Potassium cation;Potassium ion;Potassium ion (k+);Potassium ion (k1+);Potassium ion(+);Potassium ion(1+);Potassium monocation;Potassium(+);Potassium(1+);Potassium(1+) ion;Potassium(i) cation;K(+)PW_C000457K+5738931191926220951530336631617231627136135136146159211475952151690216011810198152223067702322577115132776101117824132678246353120484122121198124123105135123768118124944452124949472125860297125965299127322205127421388414Adenosine triphosphateHMDB0000538Adenosine triphosphate (ATP) is a nucleotide consisting of a purine base (adenine) attached to the first carbon atom of ribose (a pentose sugar). Three phosphate groups are esterified at the fifth carbon atom of the ribose. ATP is incorporated into nucleic acids by polymerases in the processes of DNA replication and transcription. ATP contributes to cellular energy charge and participates in overall energy balance, maintaining cellular homeostasis. ATP can act as an extracellular signaling molecule via interactions with specific purinergic receptors to mediate a wide variety of processes as diverse as neurotransmission, inflammation, apoptosis, and bone remodelling. Extracellular ATP and its metabolite adenosine have also been shown to exert a variety of effects on nearly every cell type in human skin, and ATP seems to play a direct role in triggering skin inflammatory, regenerative, and fibrotic responses to mechanical injury, an indirect role in melanocyte proliferation and apoptosis, and a complex role in Langerhans cell-directed adaptive immunity. During exercise, intracellular homeostasis depends on the matching of adenosine triphosphate (ATP) supply and ATP demand. Metabolites play a useful role in communicating the extent of ATP demand to the metabolic supply pathways. Effects as different as proliferation or differentiation, chemotaxis, release of cytokines or lysosomal constituents, and generation of reactive oxygen or nitrogen species are elicited upon stimulation of blood cells with extracellular ATP. The increased concentration of adenosine triphosphate (ATP) in erythrocytes from patients with chronic renal failure (CRF) has been observed in many studies but the mechanism leading to these abnormalities still is controversial. (PMID: 15490415, 15129319, 14707763, 14696970, 11157473).56-65-5C00002595715422ATP5742DB00171NC1=NC=NC2=C1N=CN2[C@@H]1O[C@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)[C@@H](O)[C@H]1OC10H16N5O13P3InChI=1S/C10H16N5O13P3/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(26-10)1-25-30(21,22)28-31(23,24)27-29(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H,23,24)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1ZKHQWZAMYRWXGA-KQYNXXCUSA-N({[({[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy](hydroxy)phosphoryl}oxy)phosphonic acid507.181506.995745159-2.057adenosine triphosphate0-3FDB0218135'-(tetrahydrogen triphosphate) adenosine;5'-atp;Atp;Adenosine 5'-triphosphate;Adenosine 5'-triphosphorate;Adenosine 5'-triphosphoric acid;Adenosine triphosphate;Adenylpyrophosphorate;Adenylpyrophosphoric acid;Adephos;Adetol;Adynol;Atipi;Atriphos;Cardenosine;Fosfobion;Glucobasin;Myotriphos;Phosphobion;Striadyne;Triadenyl;Triphosphaden;Triphosphoric acid adenosine ester;Adenosine-5'-triphosphate;H4atp;Adenosine triphosphoric acid;Adenosine-5'-triphosphoric acidPW_C000414ATP922146082661641422478137333279959343997632105182112102146492156142160582405592434272726462812293029663163723616613617514399234474314768914864545032895035265155752059752151005250104529110153131115346112539010354061175430118544312055421295556132556913356031355621108584614358541465876107589714759241516048155610916162301666493178683918868701606976199715720571842067209210722521372292117298198730221673902177408218743216374812227499190818622511847277119031701201028112039164121782851257822612691290132642231532730842326315426213224269431877028253772181347723332977468333776323367803733278041350781681287821435178240353784113357849411578850130788653317891933480028368800461848067411985629194826124113234941132823881162801091199141221199924061201544071202453821203624121212464291213921231213974331214714081219744101220651251220793831220834051224024221224444351229193991230094461238164641239514471239564681240293741245274441246161361246303981246343761249434721249723751250114701253042971253714791253922991255154811255954841261234851262203001262344951262404781265474911265964991269135011271233891277315161277813951277963901278012091281195081281675171420WaterHMDB0002111Water is a chemical substance that is essential to all known forms of life. It appears colorless to the naked eye in small quantities, though it is actually slightly blue in color. It covers 71% of Earth's surface. Current estimates suggest that there are 1.4 billion cubic kilometers (330 million m3) of it available on Earth, and it exists in many forms. It appears mostly in the oceans (saltwater) and polar ice caps, but it is also present as clouds, rain water, rivers, freshwater aquifers, lakes, and sea ice. Water in these bodies perpetually moves through a cycle of evaporation, precipitation, and runoff to the sea. Clean water is essential to human life. In many parts of the world, it is in short supply. From a biological standpoint, water has many distinct properties that are critical for the proliferation of life that set it apart from other substances. It carries out this role by allowing organic compounds to react in ways that ultimately allow replication. All known forms of life depend on water. Water is vital both as a solvent in which many of the body's solutes dissolve and as an essential part of many metabolic processes within the body. Metabolism is the sum total of anabolism and catabolism. In anabolism, water is removed from molecules (through energy requiring enzymatic chemical reactions) in order to grow larger molecules (e.g. starches, triglycerides and proteins for storage of fuels and information). In catabolism, water is used to break bonds in order to generate smaller molecules (e.g. glucose, fatty acids and amino acids to be used for fuels for energy use or other purposes). Water is thus essential and central to these metabolic processes. Water is also central to photosynthesis and respiration. Photosynthetic cells use the sun's energy to split off water's hydrogen from oxygen. Hydrogen is combined with CO2 (absorbed from air or water) to form glucose and release oxygen. All living cells use such fuels and oxidize the hydrogen and carbon to capture the sun's energy and reform water and CO2 in the process (cellular respiration). Water is also central to acid-base neutrality and enzyme function. An acid, a hydrogen ion (H+, that is, a proton) donor, can be neutralized by a base, a proton acceptor such as hydroxide ion (OH-) to form water. Water is considered to be neutral, with a pH (the negative log of the hydrogen ion concentration) of 7. Acids have pH values less than 7 while bases have values greater than 7. Stomach acid (HCl) is useful to digestion. However, its corrosive effect on the esophagus during reflux can temporarily be neutralized by ingestion of a base such as aluminum hydroxide to produce the neutral molecules water and the salt aluminum chloride. Human biochemistry that involves enzymes usually performs optimally around a biologically neutral pH of 7.4. (Wikipedia).7732-18-5C0000196215377937OH2OInChI=1S/H2O/h1H2XLYOFNOQVPJJNP-UHFFFAOYSA-Nwater18.015318.0105646861water00FDB013390Dihydrogen oxide;Steam;[oh2];Acqua;Agua;Aqua;Bound water;Dihydridooxygen;Eau;H2o;Hoh;Hydrogen hydroxide;WasserPW_C001420H2O55894910951394151316214481135261562428652106912077033823188382109431137749146554159043201824253222267860272746277817280529314370316472363461459836472737494193503027515675195975214100522794523610352971055319111534311353551125402110547012354831255492126550712755341305537114554112955911355608118562210856916575914057781015841143585314658771075890955910147594015160321556059157608716161231636133159621516218166647717865071806600152671311768401886888160716220571812077193206721121172282137238214724321572951987350216738821074012127467222749222475001907588170820122582372268414162926526118502771192216412011281122132851225028612264287123272491252022712632651269329012705291127152921300729813019300130253011303730213261223133272941534030842327315426953184369132276914293770192537710213277131133772151347737833177397332774713337751611577536334776283367772233777759341778163437798234778071329782353527824235378270356791133608001436880039370805912288065611993830383947943841105573901106393911158443981198792321199151221199634061200084071200464081201131241203654121204304051204384091206064151207944141211584251212404291213511211213814191216074341221183821223844361227531201227973741228044431230124461230643761230721371231314471231421361231624481232314511233844501237304601238104641239404551241654691246703991249384711249454721253052971253534791253864811254244821254802991256824831257074781257454871260544901262384951262734841267644801268965011269635021270173881271772081271992091272275041275065071275765151278363891280823951281765131034Adenosine diphosphateHMDB0001341Adenosine diphosphate, abbreviated ADP, is a nucleotide. It is an ester of pyrophosphoric acid with the nucleotide adenine. ADP consists of the pyrophosphate group, the pentose sugar ribose, and the nucleobase adenine. ADP is the product of ATP dephosphorylation by ATPases. ADP is converted back to ATP by ATP synthases.58-64-0C00008602216761ADP5800NC1=NC=NC2=C1N=CN2[C@@H]1O[C@H](COP(O)(=O)OP(O)(O)=O)[C@@H](O)[C@H]1OC10H15N5O10P2InChI=1S/C10H15N5O10P2/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(24-10)1-23-27(21,22)25-26(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1XTWYTFMLZFPYCI-KQYNXXCUSA-N[({[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy]phosphonic acid427.2011427.029414749-2.126adenosine-diphosphate0-2FDB021817Adp;Adenosindiphosphorsaeure;Adenosine 5'-pyrophosphate;Adenosine diphosphate;Adenosine pyrophosphate;Adenosine-5'-diphosphate;Adenosine-5-diphosphate;Adenosine-diphosphate;5'-adenylphosphoric acid;Adenosine 5'-diphosphate;H3adp;5'-adenylphosphate;Adenosine 5'-diphosphoric acid;Adenosine-5'-diphosphoric acidPW_C001034ADP2341348415224821380159631597831061141518219014921041821131021615824085924352727284727364628552931657236356144002344763147709150362651577520897521710053151115349112539210354461205544129557213356241085741117576410158491435856146587810758991475926151605015561111616231166649517867009468411886872160715920571872067208210722621372312117300198730321673912177410218743316374832228187225118512771190517012013281121802851326222315329308423283154239831342622322426963187702925377087132772161347730632977472333776633367803933278043350781701287821535178244353784143357849511578705331788491307892033480030368806221188065113580676119948271241132833881162041091199441221199944061201564071203183821203664121212484291213941231213994331214724081218993831219764101220641251220854051224054221224454351229733991230134461238184641239534471239584681240303741244523981245294441246151361246363761249474721249753751250124701253342971253734791254922991255174811256454841261254851262193001262354951262424781265504911265974991269155011277335161277803951277973901278032091281225081281685171283133891104PhosphateHMDB0001429Phosphate 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 HPO<sup>2-</sup><sub>4</sub> and H<sub>2</sub>PO<sup>-</sup><sub>4</sub> 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-23.14265-44-2C00009106118367CPD-85871032[O-]P([O-])([O-])=OO4PInChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3NBIIXXVUZAFLBC-UHFFFAOYSA-Kphosphoric acid94.971494.953423phosphoric acid0-2DBMET00532FDB022617Nfb orthophosphate;O-phosphoric acid;Ortho-phosphate;Orthophosphate (po43-);Orthophosphate(3-);Phosphate;Phosphate (po43-);Phosphate anion(3-);Phosphate ion (po43-);Phosphate ion(3-);Phosphate trianion;Phosphate(3-);Phosphoric acid ion(3-);Pi;[po4](3-);Orthophosphate;Phosphate ion;Po4(3-);Phosphoric acid;Orthophosphoric acid;Phosphoric acid ionPW_C001104Pi2448488145818188312980317631417674925001027294727374631292931667236366138512342492244753150312751587520797521610053171115351112538110354471205543129557313356051355625108569365848143585514659111475941151604015561001616294107648717866911016714117684218868891607161205718920672122117306198738921074022127436163747522281962258258227101182411013425711748132117611151177321311904170119271641201428112728290132632233481917422553044235031542435318436923227701825377194293772171347794033677966130780483327805732978245353786693318002236889279308938313839479638411055839011064039111323594115845398116206109119982406120069122120699407121057124121216125121268429121352121121409123121423382121852405123304119123621118123786136123838464123968447123981399124405376124948472125362479125446297125774481125954299126221478126594300126604298126723484126904501127413388127783209128166395128177513128315389536TroponinProteinComplex993ProteinComplexPW_EC000536ChEBITroponi136072501294Sodium/potassium-transporting ATPase subunit alpha-1P05023This 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.
HMDBP01387ATP1A11p21AL13637613.6.3.92645143167733637613928755069271362996811423Sodium/potassium-transporting ATPase subunit alpha-2P50993This 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.
HMDBP01534ATP1A21q23.2J0509613.6.3.92646143168733638613929755070271363016811316Sodium/potassium-transporting ATPase subunit alpha-3P13637This 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.
HMDBP01416ATP1A319q13.31M3745513.6.3.92647143169733639613930755071271363006812269Sodium/potassium-transporting ATPase subunit alpha-4Q13733This 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.
HMDBP03142ATP1A41q23.2AF31064613.6.3.92648143170733640613931755072271363026811154Sodium/potassium-transporting ATPase subunit beta-1P05026This 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 membraneHMDBP01228ATP1B11q24X1716112649143171733641613932755073271363036811150Sodium/potassium-transporting ATPase subunit beta-2P14415This 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 knownHMDBP01224ATP1B217p13.1CH47110812650143172733642613933755074271363046811126Sodium/potassium-transporting ATPase subunit beta-3P54709This 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 knownHMDBP01199ATP1B33q23AF00589412651143173733643613934755075271363056815708ATPase, (Na+)/K+ transporting, beta 4 polypeptideB7ZKV8BC143404126521431747336446139357550762784562281363066812684Sodium/potassium-transporting ATPase subunit gammaP54710May be involved in forming the receptor site for cardiac glycoside binding or may modulate the transport function of the sodium ATPaseHMDBP07463FXYD211q23U50743126531431757336456139367550772784572281363076811933Inward rectifier potassium channel 2P63252Probably participates in establishing action potential waveform and excitability of neuronal and muscle tissues. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium or cesiumHMDBP02418KCNJ217q24.3AF01190413502143958Inward rectifier potassium channel 4P48050This receptor is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium and cesiumHMDBP08742KCNJ422q13.1U0736413503143957G protein-activated inward rectifier potassium channel 1P48549This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This receptor plays a crucial role in regulating the heartbeatHMDBP08741KCNJ32q24.1GU07451518489228136314743959G protein-activated inward rectifier potassium channel 4P48544This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by external bariumHMDBP08743KCNJ511q24BC07483818490228136315744921Potassium voltage-gated channel subfamily D member 3Q9UK17Pore-forming (alpha) subunit of voltage-gated rapidly inactivating A-type potassium channels. May contribute to I(To) current in heart and I(Sa) current in neurons. Channel properties are modulated by interactions with other alpha subunits and with regulatory subunitsHMDBP10844KCND31p13.3AL45099713506142972Kv channel-interacting protein 2Q9NS61Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels. Probably modulates channels density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner. In vitro, modulates KCND2/Kv4.2 and KCND3/Kv4.3 currents. Involved in KCND2 and KCND3 trafficking to the cell surfaceHMDBP07751KCNIP210q24AK0273471912383507145723Potassium voltage-gated channel subfamily A member 5P22460M8325418491145724Disks large homolog 1Q12959CH47119111976Potassium voltage-gated channel subfamily KQT member 1P51787Probably important in cardiac repolarization. Associates with KCNE1 (MinK) to form the I(Ks) cardiac potassium current. Elicits a rapidly activating, potassium-selective outward current. Muscarinic agonist oxotremorine-M strongly suppresses KCNQ1/KCNE1 current in CHO cells in which cloned KCNQ1/KCNE1 channels were coexpressed with M1 muscarinic receptors. May associate also with KCNE3 (MiRP2) to form the potassium channel that is important for cyclic AMP-stimulated intestinal secretion of chloride ions, which is reduced in cystic fibrosis and pathologically stimulated in cholera and other forms of secretory diarrheaHMDBP02530KCNQ111p15.5AF00057113596144915Potassium voltage-gated channel subfamily E member 1P15382Ancillary protein that assembles as a beta subunit with a voltage-gated potassium channel complex of pore-forming alpha subunits. Modulates the gating kinetics and enhances stability of the channel complex. Assembled with KCNQ1/KVLQT1 is proposed to form the slowly activating delayed rectifier cardiac potassium (IKs) channel. The outward current reaches its steady state only after 50 seconds. Assembled with KCNH2/HERG may modulate the rapidly activating component of the delayed rectifying potassium current in heart (IKr)HMDBP10838KCNE121q22.1-q22.2|21q22.12AF13518813597144919Potassium voltage-gated channel subfamily E member 2Q9Y6J6Ancillary protein that assembles as a beta subunit with a voltage-gated potassium channel complex of pore-forming alpha subunits. Modulates the gating kinetics and enhances stability of the channel complex. Associated with KCNH2/HERG is proposed to form the rapidly activating component of the delayed rectifying potassium current in heart (IKr). May associate with KCNQ2 and/or KCNQ3 and modulate the native M-type current. May associate with KCNQ1/KVLTQ1 and elicit a voltage-independent current. May associate with HCN1 and HCN2 and increase potassium currentHMDBP10842KCNE221q22.12BC09389213510143527523531455089651362248136227151840Potassium voltage-gated channel subfamily H member 2Q12809Pore-forming (alpha) subunit of voltage-gated inwardly rectifying potassium channel. Channel properties are modulated by cAMP and subunit assembly. Mediates the rapidly activating component of the delayed rectifying potassium current in heart (IKr). Isoform 3 has no channel activity by itself, but modulates channel characteristics when associated with isoform 1HMDBP02212KCNH27q36.1AJ01053913511143528523532455090651362258136228154382Putative Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferaseQ5I7T1Putative alpha-1,2-glucosyltransferase, which adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol. When coupled to KCNH2 may reduce KCNH2 sensitivity to classic proarrhythmic drug blockade, possibly by mediating glycosylation of KCNH2.
HMDBP09186ALG10B12q12AC11737212.4.1.2563512143529523533455091651362268136229154840ATP-binding cassette sub-family C member 8Q09428Putative subunit of the beta-cell ATP-sensitive potassium channel (KATP). Regulator of ATP-sensitive K(+) channels and insulin releaseHMDBP10762ABCC811p15.1L7822313031673076698492143961ATP-sensitive inward rectifier potassium channel 8Q15842This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by external bariumHMDBP08745KCNJ812p11.23D50315184932282157ATP-sensitive inward rectifier potassium channel 11Q14654This receptor is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular bariumHMDBP02918KCNJ1111p15.1D50582184942285725ATP-binding cassette sub-family C member 9O60706AF061302184952284928Potassium channel subfamily K member 1O00180Weakly inward rectifying potassium channelHMDBP10851KCNK11q42-q43AL35635712212Sodium/calcium exchanger 1P32418Rapidly transports Ca(2+) during excitation-contraction coupling. Ca(2+) is extruded from the cell during relaxation so as to prevent overloading of intracellular storesHMDBP03051SLC8A12p23-p22AC00737718496141363656813351Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4Q9Y3Q4Hyperpolarization-activated ion channel with very slow activation and inactivation exhibiting weak selectivity for potassium over sodium ions. May contribute to the native pacemaker currents in heart (If) and in neurons (Ih). Activated by cAMP. May mediate responses to sour stimuliHMDBP08131HCN415q24.1AJ13242918497144295Sodium channel protein type 5 subunit alphaQ14524This protein mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. It is a tetrodotoxin-resistant Na(+) channel isoform. This channel is responsible for the initial upstroke of the action potential in the electrocardiogramHMDBP09086SCN5A3p21BC144621134841434935235224584982283222Beta-2-syntrophinQ13425Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex. May play a role in the regulation of secretory granules via its interaction with PTPRNHMDBP08002SNTB216q22.1AF24338513485143494523523451590Beta-1-syntrophinQ13884Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complexHMDBP01766SNTB18q23-q24AK29265513486143495523524453221Alpha-1-syntrophinQ13424Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the extracellular matrix via the dystrophin glycoprotein complex. Plays an important role in synapse formation and in the organization of UTRN and acetylcholine receptors at the neuromuscular synapse. Binds to phosphatidylinositol 4,5- biphosphateHMDBP08001SNTA120q11.2U4057113487143496523525451845Voltage-dependent L-type calcium channel subunit alpha-1CQ13936Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1C gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. They are blocked by dihydropyridines (DHP), phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to omega-conotoxin- GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA). Calcium channels containing the alpha-1C subunit play an important role in excitation-contraction coupling in the heart. The various isoforms display marked differences in the sensitivity to DHP compounds. Binding of calmodulin or CABP1 at the same regulatory sites results in an opposit effects on the channel functionHMDBP02220CACNA1C12p13.3L29537199134276745351314353852509465805558807512281361316512706Voltage-dependent calcium channel subunit alpha-2/delta-2Q9NY47The alpha-2/delta subunit of voltage-dependent calcium channels regulates calcium current density and activation/inactivation kinetics of the calcium channel. Acts as a regulatory subunit for P/Q-type calcium channel (CACNA1A), N-type (CACNA1B), L-type (CACNA1C OR CACNA1D) and possibly T-type (CACNA1G). Overexpression induces apoptosisHMDBP07485CACNA2D23p21.3AJ25136819403927684535141435395250956584992281361326512720Voltage-dependent L-type calcium channel subunit beta-1Q02641The beta subunit of voltage-dependent calcium channels contributes to the function of the calcium channel by increasing peak calcium current, shifting the voltage dependencies of activation and inactivation, modulating G protein inhibition and controlling the alpha-1 subunit membrane targetingHMDBP07499CACNB117q21-q22CH471152193839276945351514354052509665807532281361336514887Muscarinic acetylcholine receptor M2P08172The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is adenylate cyclase inhibitionHMDBP10810CHRM27q31-q35AF49891612722451361266513195Ryanodine receptor 2Q92736Communication between transverse-tubules and sarcoplasmic reticulum. Contraction of cardiac muscle is triggered by release of calcium ions from SR following depolarization of T- tubulesHMDBP07975RYR21q43AJ002511199635106316277247354245136134652136326441365Sarcoplasmic/endoplasmic reticulum calcium ATPase 2P16615This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Isoform 2 is involved in the regulation of the contraction/relaxation cycle.
HMDBP01470ATP2A212q24.11AY18657813.6.3.82730473534451361256522026Cardiac phospholambanP26678Phospholamban has been postulated to regulate the activity of the calcium pump of cardiac sarcoplasmic reticulumHMDBP02625PLN6q22.1M6041112740471361276521513Beta-1 adrenergic receptorP08588Beta-adrenergic receptors mediate the catecholamine- induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinityHMDBP01632ADRB110q24-q26AY567837174614108234117045301365434011361286511262cAMP-dependent protein kinase catalytic subunit alphaP17612Phosphorylates a large number of substrates in the cytoplasm and the nucleusHMDBP01352PRKACA19p13.1X0776712.7.11.11990212762468052081361296531990cAMP-dependent protein kinase type I-alpha regulatory subunitP10644HMDBP02560PRKAR1A17q23-q24S5470511001212763468052181361306533290Tropomyosin alpha-1 chainP09493Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filamentsHMDBP08070TPM115q22.1BC05354514184461361476533291Tropomyosin beta chainP07951Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filamentsHMDBP08071TPM29p13M1212514185461361486532717Voltage-dependent T-type calcium channel subunit alpha-1HO95180Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1H gives rise to T-type calcium currents. T-type calcium channels belong to the "low-voltage activated (LVA)" group and are strongly blocked by nickel and mibefradil. A particularity of this type of channels is an opening at quite negative potentials, and a voltage-dependent inactivation. T-type channels serve pacemaking functions in both central neurons and cardiac nodal cells and support calcium signaling in secretory cells and vascular smooth muscle. They may also be involved in the modulation of firing patterns of neurons which is important for information processing as well as in cell growth processesHMDBP07496CACNA1H16p13.3AE00646615092658500228136233142716Voltage-dependent T-type calcium channel subunit alpha-1GO43497Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1G gives rise to T-type calcium currents. T-type calcium channels belong to the "low-voltage activated (LVA)" group and are strongly blocked by mibefradil. A particularity of this type of channels is an opening at quite negative potentials and a voltage-dependent inactivation. T-type channels serve pacemaking functions in both central neurons and cardiac nodal cells and support calcium signaling in secretory cells and vascular smooth muscle. They may also be involved in the modulation of firing patterns of neurons which is important for information processing as well as in cell growth processesHMDBP07495CACNA1G17q22DQ494473150936585012281866Amiloride-sensitive sodium channel subunit alphaP37088Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perceptionHMDBP02267SCNN1A12p13AC00605712636141362972304301Amiloride-sensitive sodium channel subunit betaP51168Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perceptionHMDBP09092SCNN1B16p12.2-p12.1AF26022612637141362962304302Amiloride-sensitive sodium channel subunit deltaP51172Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perceptionHMDBP09093SCNN1D1p36.3-p36.2BC03675212638141362952302161Amiloride-sensitive sodium channel subunit gammaP51170Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perceptionHMDBP02930SCNN1G16p12AF35650012639148464230545Sodium/potassium ATPase1PW_P000545577129457814235791316580226958111545821150583112658457085852684207814675Inward rectifier potassium channel (IK1)1PW_P00067574919337503958268214676Acetylcholine-activated potassium channel (IKACh)1PW_P00067675139577523959677Voltage-gated rapidly activating transient outward delayed rectifying potassium channel (IKto)1PW_P00067775349217542972268314678Voltage-gated ultra rapid delayed rectifying potassium channel 1PW_P00067875557237565724268414679Voltage-gated slow delayed rectifying potassium channel (IK5)1PW_P00067975719767584915268514680Voltage-gated rapid delayed rectifying potassium channel (IKr)1PW_P000680759491976018407614382268614681ATP-sensitive inward rectifier potassium channel (IKATP)1PW_P0006817624840763396176421577655725268714682Inward rectifying potassium channel (IKP)1PW_P0006827664928268814685Sodium/calcium exchanger 11PW_P0006857732212269914686Funny channel (If)1PW_P0006867743351270014687Voltage-gated sodium channel (INa)1PW_P0006877754295776322277715907783221321Voltage-depenent L-type calcium channel1PW_P000321340184513412706134227201116245694Muscarinic acetylcholine receptor M21PW_P000694786488779Ryanodine receptor 21PW_P0000799331954116144695Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 1PW_P0006957871365696Cardiac phospholamban1PW_P00069678820265104Beta-1 adrenergic receptor1PW_P0001041191513217cAMP-dependent protein kinase catalytic subunit alpha1PW_P0002172351262218cAMP-dependent protein kinase type I-alpha regulatory subunit1PW_P0002182361990996Tropomyosin1PW_P000996113232901113332911688Voltage-gated T-type calcium channel (ICaT)1PW_P00068877927177802716270414583Epithelial Sodium Channel1PW_P0005836241866625430162643026272161224714179579PW_R179579Right6777033531Compoundfalse6777045361ElementCollectionfalse6777055071Boundfalse4PW_RCT000004Right124414Compound1461341420Compound146144353Compound1461541034Compound1461641104Compound146174353Compound147453PW_T000053594583Compound215Right604572Compound215Left235452013-08-08T13:59:27-06:002013-08-08T13:59:27-06:00116PW_T0001161344571Compound4615Right826752013-08-26T11:06:53-06:002013-08-27T09:27:29-06:0045836762013-08-26T11:06:53-06:002013-08-27T09:27:29-06:0045846772013-08-26T11:06:53-06:002013-08-27T09:27:29-06:0045856782013-08-26T11:06:53-06:002013-08-27T09:27:29-06:0045866792013-08-26T11:06:53-06:002013-08-27T09:27:29-06:0045876802013-08-26T11:06:53-06:002013-08-27T09:27:29-06:0045886812013-08-26T11:06:53-06:002013-08-27T09:27:29-06:0045896822013-08-26T11:06:53-06:002013-08-27T09:27:29-06:0045119PW_T0001191373531Compound4615Right1384583Compound4615Left906852013-08-26T12:33:12-06:002013-08-27T09:29:27-06:0045120PW_T0001201394581Compound1546Right1404571Compound1546Left916862013-08-26T13:04:08-06:002013-08-27T09:30:21-06:004562PW_T000062724581Compound152Right335832013-08-13T10:38:44-06:002013-08-26T13:11:37-06:0014926872013-08-26T13:11:37-06:002013-08-27T09:30:58-06:004536PW_T000036383531Compound4746Unknown10792013-07-10T11:58:58-06:002013-07-10T11:58:58-06:004735PW_T000035373531Compound1546Right93212013-07-10T11:56:28-06:002013-07-10T11:56:28-06:0045936882013-08-26T14:50:04-06:002013-08-26T14:50:04-06:00452851ActivationPW_I0028515701507Bound15702996ProteinComplex118035075035510612680166366224778915046366224826801663535051false2521337910regular78785209458258false916378810regular787852104581558false1439378810regular78785211457257false916408110regular787852124571557false1439408110regular78785247457257false3106239610regular787852484571557false3106202310regular78785249457257false215295210regular787852504571557false741295310regular78785253457257false1706239610regular787852544571557false1706202310regular78785261457257false21626866regular787852624571557false74126886regular78785267457257false2401239610regular787852684571557false2401202310regular78785269457257false2051239610regular787852704571557false2051202310regular78785278457257false2751239610regular787852794571557false2751202310regular78785280457257false216408110regular787852814571557false741407810regular78785291353251false916342810regular787852923531551false1439342810regular787852934581558false916353610regular78785294458258false1439353610regular787852954581558false741342810regular78785296458258false216342610regular78785297457257false739353810regular787852984571557false214353610regular787852994581558false216379110regular78785300458258false741379310regular787853093531551false916295110regular787853113531551false91626866regular787853123534651false1706280810regular787853563534751false2219280810regular787853573534651false2221319810regular787853614144642false1938260810regular5030536214204649false1813258510regular787853633534651false2049251110regular7878536410344643false2190260310regular5030536511044646false2288260110regular444353663534751false2051288810regular787826800913534651false2953322310regular787826800923531551false2955280810regular787826800934584658false3103322110regular787826800944581558false3105280610regular78781504653614450false2379338412regular150701504553614450false2554320412regular150702128129476false104438628subunitregular150702129142376false101939278subunitregular15070213013161476false103939878subunitregular15070213122691476false107940428subunitregular15070213211541476false120440579subunitregular15070213311501476false126939978subunitregular150702134112676false129939377subunitregular150702135570822876false126438726subunitregular150702136268422876false116438225subunitregular150702153193376false307022419subunitregular150702154395876false307021818subunitregular150702155395722876false441299119subunitregular150702156395922876false441292119subunitregular150702157492176false167021868subunitregular150702158297276false167022468subunitregular15070216357231476false44026568subunitregular150702164572476false44027218subunitregular150702166197676false236521768subunitregular150702167491576false236522368subunitregular15070216849191476false201521618subunitregular15070216918401476false2090222119subunitregular15070217043821476false1940222119subunitregular15070217548401476false264522118subunitregular150702176396122876false267521518subunitregular150702177215722876false275522518subunitregular150702178572522876false278521918subunitregular150702179492876false44040818subunitregular15070218422121476false114434878subunitregular15070218533511476false44034868subunitregular150702186429522876false44537418subunitregular150702187322276false37537968subunitregular150702188159076false51537968subunitregular150702189322176false44538468subunitregular150702191184576false114028918subunitregular150702192270622876false114029568subunitregular150702193272076false114030218subunitregular1507022114887452false44132388subunitregular15070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3827 C1024 3827 1409 3827 1439 3827 83false18trueM 180.99038105676658 456.5 L 168 464 L 180.99038105676658 471.5false7918M1439 3827 C1409 3827 1344 3857 1314 3857 83true187919M994 4120 C1024 4120 1134 3857 1164 3857 83true187920M1439 4120 C1409 4120 1024 4120 994 4120 83false18trueM 605.0096189432334 749.5 L 618 742 L 605.0096189432334 734.5false7977M3145 2396 C3145 2366 3145 2328 3145 2311 83false187978M3145 2101 C3145 2131 3145 2151 3145 2181 83false18trueM 781.5 305.9903810567666 L 774 293 L 766.5 305.9903810567666false7979M293 2992 C339 2992 424 2992 449 2992 83false187980M741 2992 C705 2992 610 2992 581 2992 83false18trueM 1151.5 330.9903810567666 L 1144 318 L 1136.5 330.9903810567666false7983M1745 2396 C1745 2366 1745 2346 1745 2316 83false187984M1745 2101 C1745 2131 1745 2156 1745 2186 83false18trueM 1416.5 315.9903810567666 L 1409 303 L 1401.5 315.9903810567666false7991M294 2727 C326 2727 405 2727 442 2727 83false77992M741 2727 C717 2727 599 2727 562 2727 83false7trueM 1686.5 310.9903810567666 L 1679 298 L 1671.5 310.9903810567666false7999M2440 2396 C2440 2366 2440 2336 2440 2306 83false188000M2440 2101 C2440 2131 2440 2146 2440 2176 83false18trueM 1956.5 310.9903810567666 L 1949 298 L 1941.5 310.9903810567666false8001M2090 2396 C2090 2366 2090 2310 2090 2280 83false188002M2090 2101 C2090 2131 2090 2131 2090 2161 83false18trueM 2251.5 305.9903810567666 L 2244 293 L 2236.5 305.9903810567666false8011M2790 2396 C2790 2366 2790 2350 2790 2321 83false188012M2790 2101 C2790 2131 2790 2121 2790 2151 83false18trueM 2661.5 305.9903810567666 L 2654 293 L 2646.5 305.9903810567666false8013M294 4117 C324 4117 407 4117 440 4117 83false188014M741 4117 C722 4117 618 4117 590 4117 83false18trueM 2961.5 310.9903810567666 L 2954 298 L 2946.5 310.9903810567666false8027M994 3467 C992 3512 1061 3522 1144 3522 83false18trueM 250.99038105676658 1106.5 L 238 1114 L 250.99038105676658 1121.5false8028M1439 3467 C1440 3505 1352 3520 1294 3522 83false18trueM 535.0096189432334 1126.5 L 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2249 C154 2249 469 2249 517 2249 C517 2349 516 4078 517 4174 C520 4631 1218 4630 1217 4172 C1217 4022 1216 2348 1216 2248 C1276 2248 3300 2248 3350 2248 1false13249.01926.0369667M2842 3058 C2885 3058 3251 3058 3289 3058 84false6447.00.045046015Cardiac Muscle1227542202.52.51601545046115Skeletal Muscle1747532202.52.51601545046215Striated Muscle Cell2026867202.22.21601545046315Nucleus1528897201.61.61601545046415Mitochondrion11991417201.61.61601545046515Myofibril21041342201.91.91601545046615Sarcoplasmic Reticulum20131048201.91.91601545046715Myofibril1331904202.82.81601545047315Sarcolema12272163202.22.21601545047415Sarcoplasmic Reticulum23572838202.52.51601545048915Calcium binding to troponin displaces tropomyosin from the myosin binding sites on the actin filaments20793395201.61.61601545049015Myosin, with an ADP and phosphate attached, binds to actin to form a cross bridge. 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