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Showing drug card for Calcium (DB01373)

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Version 2.5
Creation Date 2007-07-06 20:28:41
Update Date 2008-03-20 01:50:34
Primary Accession Number DB01373
Secondary Accession Number Not Available
Name Calcium
Drug Type
  • Experimental
  • Small Molecule
Description Calcium plays a vital role in the anatomy, physiology and biochemistry of organisms and of the cell, particularly in signal transduction pathways. The skeleton acts as a major mineral storage site for the element and releases Ca2+ ions into the bloodstream under controlled conditions. Circulating calcium is either in the free, ionized form or bound to blood proteins such as serum albumin. Although calcium flow to and from the bone is neutral, about 5 mmol is turned over a day. Bone serves as an important storage point for calcium, as it contains 99% of the total body calcium. Low calcium intake may also be a risk factor in the development of osteoporosis. The best-absorbed form of calcium from a pill is a calcium salt like carbonate or phosphate. Calcium gluconate and calcium lactate are absorbed well by pregnant women. Seniors absorb calcium lactate, gluconate and citrate better unless they take their calcium supplement with a full breakfast.
Synonyms Not Available
Brand Names Not Available
Brand Mixtures Not Available
Chemical IUPAC Name Not Available
Chemical Formula Ca
Chemical Structure Structure
CAS Registry Number Not Available
InChI Identifier Not Available
InChI Key Not Available
KEGG Drug Not Available
KEGG Compound Not Available
PubChem Compound Not Available
PubChem Substance Not Available
ChEBI ID Not Available
PharmGKB ID Not Available
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] Not Available
RxList Link Not Available
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Calcium Link Image
FDA Label
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 40.0780
Monoisotopic Molecular Weight 39.9626
State Solid
Melting Point Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility Not Available Calculated using ALOGPS
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP Not Available Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS Not Available Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point Not Available
Mass Spectrum Not Available
MOL File Not Available
SDF File Not Available
PDB File Not Available
Experimental PDB ID Not Available
Isomeric SMILES Not Available
Canonical SMILES Not Available
Drug Category Not Available
ATC Codes
AHFS Codes
  • 34:00.00
  • 40:12.00
  • 40:18.17
  • 40:18.19
  • 40:34.00*
  • 56:04.00
  • 56:12.00
  • 88:08.00
  • 88:12.00
  • 88:29.00*
  • 92:02.00*
Indication Not Available
Pharmacology Not Available
Mechanism of Action Calcium plays a vital role in the anatomy, physiology and biochemistry of organisms and of the cell, particularly in signal transduction pathways. More than 500 human proteins are known to bind or transport calcium. The skeleton acts as a major mineral storage site for the element and releases Ca2+ ions into the bloodstream under controlled conditions. Circulating calcium is either in the free, ionized form or bound to blood proteins such as serum albumin. Parathyroid hormone (secreted from the parathyroid gland) regulates the resorption of Ca2+ from bone. Calcitonin stimulates incorporation of calcium in bone, although this process is largely independent of calcitonin. Although calcium flow to and from the bone is neutral, about 5 mmol is turned over a day. Bone serves as an important storage point for calcium, as it contains 99% of the total body calcium. Low calcium intake may also be a risk factor in the development of osteoporosis. The best-absorbed form of calcium from a pill is a calcium salt like carbonate or phosphate. Calcium gluconate and calcium lactate are absorbed well by pregnant women. Seniors absorb calcium lactate, gluconate and citrate better unless they take their calcium supplement with a full breakfast. The currently recommended calcium intake is 1,500 milligrams per day for women not taking estrogen and 800 milligrams per day for women on estrogen. There is close to 300 milligrams of calcium in one cup of fluid milk. Calcium carbonate is currently the best and least expensive form of calcium supplement available.
Absorption Not Available
Toxicity Not Available
Protein Binding Not Available
Biotransformation Not Available
Half Life Not Available
Dosage Forms
Form Route
Capsule Oral
Liquid Dental
Liquid Intravenous
Liquid Oral
Liquid Sublingual
Paste Dental
Powder Oral
Powder, for solution Oral
Solution Intramuscular
Solution Intravenous
Solution Oral
Solution / drops Oral
Syrup Oral
Tablet Oral
Tablet, chewable Oral
Patient Information Not Available
Contraindications Not Available
Interactions Not Available
Drug Interactions
Drug Interaction
Alendronate Formation of non-absorbable complexes
Amprenavir The antiacid decreases the absorption of amprenavir
Atazanavir This gastric pH modifier decreases the levels/effects of atazanavir
Chloroquine The antiacid decreases the absorption of chloroquine
Ciprofloxacin Formation of non-absorbable complexes
Clodronate Formation of non-absorbable complexes
Dapsone Formation of non-absorbable complexes
Delavirdine The antiacid decreases the effect of delavirdine
Demeclocycline Formation of non-absorbable complexes
Doxycycline Formation of non-absorbable complexes
Enoxacin Formation of non-absorbable complexes
Etidronic acid Formation of non-absorbable complexes
Fosamprenavir The antiacid decreases the absorption of amprenavir
Grepafloxacin Formation of non-absorbable complexes
Ibandronate Formation of non-absorbable complexes
Indinavir The antiacid decreases the absorption of indinavir
Itraconazole The antacid decreases the effect of the imidazole
Ketoconazole The antacid decreases the effect of the imidazole
Levofloxacin Formation of non-absorbable complexes
Levothyroxine Calcium decreases absorption of levothyroxine
Lomefloxacin Formation of non-absorbable complexes
Methacycline Formation of non-absorbable complexes
Minocycline Formation of non-absorbable complexes
Moxifloxacin Formation of non-absorbable complexes
Mycophenolate mofetil Formation of non-absorbable complexes
Norfloxacin Formation of non-absorbable complexes
Ofloxacin Formation of non-absorbable complexes
Oxytetracycline Formation of non-absorbable complexes
Pefloxacin Formation of non-absorbable complexes
Polystyrene sulfonate Formation of non-absorbable complexes
Risedronate Formation of non-absorbable complexes
Temafloxacin Formation of non-absorbable complexes
Tetracycline Formation of non-absorbable complexes
Trovafloxacin Formation of non-absorbable complexes
Food Interactions Not Available
Pathways Not Available
General References
  1. Porthouse J, Cockayne S, King C, Saxon L, Steele E, Aspray T, Baverstock M, Birks Y, Dumville J, Francis R, Iglesias C, Puffer S, Sutcliffe A, Watt I, Torgerson DJ: Randomised controlled trial of calcium and supplementation with cholecalciferol (vitamin D3) for prevention of fractures in primary care. BMJ. 2005 Apr 30;330(7498):1003. [PubMed Link Image]
  2. Grant AM, Avenell A, Campbell MK, McDonald AM, MacLennan GS, McPherson GC, Anderson FH, Cooper C, Francis RM, Donaldson C, Gillespie WJ, Robinson CM, Torgerson DJ, Wallace WA: Oral vitamin D3 and calcium for secondary prevention of low-trauma fractures in elderly people (Randomised Evaluation of Calcium Or vitamin D, RECORD): a randomised placebo-controlled trial. Lancet. 2005 May 7-13;365(9471):1621-8. [PubMed Link Image]
  3. Weingarten MA, Zalmanovici A, Yaphe J: Dietary calcium supplementation for preventing colorectal cancer and adenomatous polyps. Cochrane Database Syst Rev. 2005 Jul 20;(3):CD003548. [PubMed Link Image]
  4. Jackson RD, LaCroix AZ, Gass M, Wallace RB, Robbins J, Lewis CE, Bassford T, Beresford SA, Black HR, Blanchette P, Bonds DE, Brunner RL, Brzyski RG, Caan B, Cauley JA, Chlebowski RT, Cummings SR, Granek I, Hays J, Heiss G, Hendrix SL, Howard BV, Hsia J, Hubbell FA, Johnson KC, Judd H, Kotchen JM, Kuller LH, Langer RD, Lasser NL, Limacher MC, Ludlam S, Manson JE, Margolis KL, McGowan J, Ockene JK, O'Sullivan MJ, Phillips L, Prentice RL, Sarto GE, Stefanick ML, Van Horn L, Wactawski-Wende J, Whitlock E, Anderson GL, Assaf AR, Barad D: Calcium plus vitamin D supplementation and the risk of fractures. N Engl J Med. 2006 Feb 16;354(7):669-83. [PubMed Link Image]
  5. Dawson-Hughes B, Harris SS, Krall EA, Dallal GE: Effect of calcium and vitamin D supplementation on bone density in men and women 65 years of age or older. N Engl J Med. 1997 Sep 4;337(10):670-6. [PubMed Link Image]
  6. Wikipedia Link Image
Organisms Affected Not Available
Targets
  1. Calmodulin
  2. Cartilage oligomeric matrix protein
  3. Calpastatin
  4. Protein S100-B
Drug Target 1 [top]
Target 1 ID 465
Target 1 Name Calmodulin
Target 1 Synonyms
  1. CaM
Target 1 Gene Name CALM1
Target 1 Protein Sequence >Calmodulin 
ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGN
GTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEE
VDEMIREADIDGDGQVNYEEFVQMMTAK
Target 1 Number of Residues 150
Target 1 Molecular Weight 16707
Target 1 Theoretical pI 3.84
Target 1 GO Classification
Function
binding
ion binding
cation binding
calcium ion binding
Process
Not Available
Component
Not Available
Target 1 General Function Involved in calcium ion binding
Target 1 Specific Function Calmodulin mediates the control of a large number of enzymes and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases
Target 1 Pathways Not Available
Target 1 Reactions Not Available
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 179888 Link Image
Target 1 UniProtKB/Swiss-Prot ID P62158 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name CALM_HUMAN Link Image
Target 1 PDB ID 1IQ5 Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location Not Available
Target 1 Gene Sequence >450 bp 
ATGGCTGACCAGCTGACTGAGGAGCAGATTGCAGAGTTCAAGGAGGCCTTCTCCCTCTTT
GACAAGGATGGAGATGGCACTATCACCACCAAGGAGTTGGGGACAGTGATGAGATCCCTG
GGACAGAACCCCACTGAAGCAGAGCTGCAGGATATGATCAATGAGGTGGATGCAGATGGG
AACGGGACCATTGACTTCCCGGAGTTCCTGACCATGATGGCCAGAAAGATGAAGGACACA
GACAGTGAGGAGGAGATCCGAGAGGCGTTCCGTGTCTTTGACAAGGATGGGAATGGCTAC
ATCAGCGCCGCAGAGCTGCGTCACGTAATGACGAACCTGGGGGAGAAGCTGACCGATGAG
GAGGTGGATGAGATGATCAGGGAGGCTGACATCGATGGAGATGGCCAGGTCAATTATGAA
GAGTTTGTACAGATGATGACTGCAAAGTGA
Target 1 GenBank Gene ID
Target 1 GeneCard ID CALM1 Link Image
Target 1 GenAtlas ID CALM1 Link Image
Target 1 HGNC ID HGNC:1442 Link Image
Target 1 Chromosome Location 14
Target 1 Locus 14q24-q31
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Drum CL, Yan SZ, Bard J, Shen YQ, Lu D, Soelaiman S, Grabarek Z, Bohm A, Tang WJ: Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin. Nature. 2002 Jan 24;415(6870):396-402. [PubMed Link Image]
  2. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed Link Image]
  3. Koller M, Schnyder B, Strehler EE: Structural organization of the human CaMIII calmodulin gene. Biochim Biophys Acta. 1990 Oct 23;1087(2):180-9. [PubMed Link Image]
  4. SenGupta B, Friedberg F, Detera-Wadleigh SD: Molecular analysis of human and rat calmodulin complementary DNA clones. Evidence for additional active genes in these species. J Biol Chem. 1987 Dec 5;262(34):16663-70. [PubMed Link Image]
  5. Fischer R, Koller M, Flura M, Mathews S, Strehler-Page MA, Krebs J, Penniston JT, Carafoli E, Strehler EE: Multiple divergent mRNAs code for a single human calmodulin. J Biol Chem. 1988 Nov 15;263(32):17055-62. [PubMed Link Image]
  6. Wawrzynczak EJ, Perham RN: Isolation and nucleotide sequence of a cDNA encoding human calmodulin. Biochem Int. 1984 Aug;9(2):177-85. [PubMed Link Image]
  7. Sasagawa T, Ericsson LH, Walsh KA, Schreiber WE, Fischer EH, Titani K: Complete amino acid sequence of human brain calmodulin. Biochemistry. 1982 May 11;21(10):2565-9. [PubMed Link Image]
  8. Rhyner JA, Ottiger M, Wicki R, Greenwood TM, Strehler EE: Structure of the human CALM1 calmodulin gene and identification of two CALM1-related pseudogenes CALM1P1 and CALM1P2. Eur J Biochem. 1994 Oct 1;225(1):71-82. [PubMed Link Image]
  9. Toutenhoofd SL, Foletti D, Wicki R, Rhyner JA, Garcia F, Tolon R, Strehler EE: Characterization of the human CALM2 calmodulin gene and comparison of the transcriptional activity of CALM1, CALM2 and CALM3. Cell Calcium. 1998 May;23(5):323-38. [PubMed Link Image]
Target 1 Drug References
  1. Sosa V, Carbo R, Guarner V: Participation of glucose transporters on atrial natriuretic peptide-induced glucose uptake by adult and neonatal cardiomyocytes under oxygenation and hypoxia. Eur J Pharmacol. 2007 Jul 30;568(1-3):83-8. Epub 2007 Apr 30. [PubMed Link Image]
  2. Zhou Z, Yin J, Dou Z, Tang J, Zhang C, Cao Y: The calponin homology domain of Vav1 associates with calmodulin and is prerequisite to T cell antigen receptor-induced calcium release in Jurkat T lymphocytes. J Biol Chem. 2007 Aug 10;282(32):23737-44. Epub 2007 Jun 5. [PubMed Link Image]
  3. Schallreuter KU, Gibbons NC, Zothner C, Abou Elloof MM, Wood JM: Hydrogen peroxide-mediated oxidative stress disrupts calcium binding on calmodulin: more evidence for oxidative stress in vitiligo. Biochem Biophys Res Commun. 2007 Aug 17;360(1):70-5. Epub 2007 Jun 11. [PubMed Link Image]
  4. Caride AJ, Filoteo AG, Penniston JT, Strehler EE: The plasma membrane Ca2+ pump isoform 4a differs from isoform 4b in the mechanism of calmodulin binding and activation kinetics: implications for Ca2+ signaling. J Biol Chem. 2007 Aug 31;282(35):25640-8. Epub 2007 Jun 26. [PubMed Link Image]
  5. Lo LW, Chen YC, Chen YJ, Wongcharoen W, Lin CI, Chen SA: Calmodulin kinase II inhibition prevents arrhythmic activity induced by alpha and beta adrenergic agonists in rabbit pulmonary veins. Eur J Pharmacol. 2007 Oct 1;571(2-3):197-208. Epub 2007 Jun 13. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 1089
Target 2 Name Cartilage oligomeric matrix protein
Target 2 Synonyms
  1. COMP
  2. Cartilage oligomeric matrix protein precursor
Target 2 Gene Name COMP
Target 2 Protein Sequence >Cartilage oligomeric matrix protein precursor 
MVPDTACVLLLTLAALGASGQGQSPLGSDLGPQMLRELQETNAALQDVRDWLRQQVREIT
FLKNTVMECDACGMQQSVRTGLPSVRPLLHCAPGFCFPGVACIQTESGGRCGPCPAGFTG
NGSHCTDVNECNAHPCFPRVRCINTSPGFRCEACPPGYSGPTHQGVGLAFAKANKQVCTD
INECETGQHNCVPNSVCINTRGSFQCGPCQPGFVGDQASGCQRGAQRFCPDGSPSECHEH
ADCVLERDGSRSCVCRVGWAGNGILCGRDTDLDGFPDEKLRCPEPQCRKDNCVTVPNSGQ
EDVDRDGIGDACDPDADGDGVPNEKDNCPLVRNPDQRNTDEDKWGDACDNCRSQKNDDQK
DTDQDGRGDACDDDIDGDRIRNQADNCPRVPNSDQKDSDGDGIGDACDNCPQKSNPDQAD
VDHDFVGDACDSDQDQDGDGHQDSRDNCPTVPNSAQEDSDHDGQGDACDDDDDNDGVPDS
RDNCRLVPNPGQEDADRDGVGDVCQDDFDADKVVDKIDVCPENAEVTLTDFRAFQTVVLD
PEGDAQIDPNWVVLNQGREIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTVTDDDYAGFI
FGYQDSSSFYVVMWKQMEQTYWQANPFRAVAEPGIQLKAVKSSTGPGEQLRNALWHTGDT
ESQVRLLWKDPRNVGWKDKKSYRWFLQHRPQVGYIRVRFYEGPELVADSNVVLDTTMRGG
RLGVFCFSQENIIWANLRYRCNDTIPEDYETHQLRQA
Target 2 Number of Residues 769
Target 2 Molecular Weight 82833
Target 2 Theoretical pI 4.14
Target 2 GO Classification
Function
binding
ion binding
cation binding
calcium ion binding
Process
cellular process
cell adhesion
Component
extracellular region
Target 2 General Function Amino acid transport and metabolism
Target 2 Specific Function Not Available
Target 2 Pathways Not Available
Target 2 Reactions Not Available
Target 2 Pfam Domain Function
Target 2 Signals
  • 1-20
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 602450 Link Image
Target 2 UniProtKB/Swiss-Prot ID P49747 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name COMP_HUMAN Link Image
Target 2 PDB ID Not Available
Target 2 Cellular Location
  • Secreted protein
Target 2 Gene Sequence >2274 bp 
ATGGTCCCCGACACCGCCTGCGTTCTTCTGCTCACCCTGGCTGCCCTCGGCGCGTCCGGA
CAGGGCCAGAGCCCGTTGGGCTCAGACCTGGGCCCGCAGATGCTTCGGGAACTGCAGGAA
ACCAACGCGGCGCTGCAGGACGTGCGGGACTGGCTGCGGCAGCAGGTCAGGGAGATCACG
TTCCTGAAAAACACGGTGATGGAGTGTGACGCGTGCGGGATGCAGCAGTCAGTACGCACC
GGCCTACCCAGCGTGCGGCCCCTGCTCCACTGCGCGCCCGGCTTCTGCTTCCCCGGCGTG
GCCTGCATCCAGACGGAGAGCGGCGGCCGCTGCGGCCCCTGCCCCGCGGGCTTCACGGGC
AACGGCTCGCACTGCACCGACGTCAACGAGTGCAACGCCCACCCCTGCTTCCCCCGAGTC
CGCTGTATCAACACCAGCCCGGGGTTCCGCTGCGAGGCTTGCCCGCCGGGGTACAGCGGC
CCCACCCACCAGGGCGTGGGGCTGGCTTTCGCCAAGGCCAACAAGCAGGTTTGCACGGAC
ATCAACGAGTGTGAGACCGGGCAACATAACTGCGTCCCCAACTCCGTGTGCATCAACACC
CGGGGCTCCTTCCAGTGCGGCCCGTGCCAGCCCGGCTTCGTGGGCGACCAGGCGTCCGGC
TGCCAGCGCGGCGCACAGCGCTTCTGCCCCGACGGCTCGCCCAGCGAGTGCCACGAGCAT
GCAGACTGCGTCCTAGAGCGCGATGGCTCGCGGTCGTGCGTGTGTCGCGTTGGCTGGGCC
GGCAACGGGATCCTCTGTGGTCGCGACACTGACCTAGACGGCTTCCCGGACGAGAAGCTG
CGCTGCCCGGAGCCGCAGTGCCGTAAGGACAACTGCGTGACTGTGCCCAACTCAGGGCAG
GAGGATGTGGACCGCGATGGCATCGGAGACGCCTGCGATCCGGATGCCGACGGGGACGGG
GTCCCCAATGAAAAGGACAACTGCCCGCTGGTGCGGAACCCAGACCAGCGCAACACGGAC
GAGGACAAGTGGGGCGATGCGTGCGACAACTGCCGGTCCCAGAAGAACGACGACCAAAAG
GACACAGACCAGGACGGCCGGGGCGATGCGTGCGACGACGACATCGACGGCGACCGGATC
CGCAACCAGGCCGACAACTGCCCTAGGGTACCCAACTCAGACCAGAAGGACAGTGATGGC
GATGGTATAGGGGATGCCTGTGACAACTGTCCCCAGAAGAGCAACCCGGATCAGGCGGAT
GTGGACCACGACTTTGTGGGAGATGCTTGTGACAGCGATCAAGACCAGGATGGAGACGGA
CATCAGGACTCTCGGGACAACTGTCCCACGGTGCCTAACAGTGCCCAGGAGGACTCAGAC
CACGATGGCCAGGGTGATGCCTGCGACGACGACGACGACAATGACGGAGTCCCTGACAGT
CGGGACAACTGCCGCCTGGTGCCTAACCCCGGCCAGGAGGACGCGGACAGGGACGGCGTG
GGCGACGTGTGCCAGGACGACTTTGATGCAGACAAGGTGGTAGACAAGATCGACGTGTGT
CCGGAGAACGCTGAAGTCACGCTCACCGACTTCAGGGCCTTCCAGACAGTCGTGCTGGAC
CCGGAGGGTGACGCGCAGATTGACCCCAACTGGGTGGTGCTCAACCAGGGAAGGGAGATC
GTGCAGACAATGAACAGCGACCCAGGCCTGGCTGTGGGTTACACTGCCTTCAATGGCGTG
GACTTCGAGGGCACGTTCCATGTGAACACGGTCACGGATGACGACTATGCGGGCTTCATC
TTTGGCTACCAGGACAGCTCCAGCTTCTACGTGGTCATGTGGAAGCAGATGGAGCAAACG
TATTGGCAGGCGAACCCCTTCCGTGCTGTGGCCGAGCCTGGCATCCAACTCAAGGCTGTG
AAGTCTTCCACAGGCCCCGGGGAACAGCTGCGGAACGCTCTGTGGCATACAGGAGACACA
GAGTCCCAGGTGCGGCTGCTGTGGAAGGACCCGCGAAACGTGGGTTGGAAGGACAAGAAG
TCCTATCGTTGGTTCCTGCAGCACCGGCCCCAAGTGGGCTACATCAGGGTGCGATTCTAT
GAGGGCCCTGAGCTGGTGGCCGACAGCAACGTGGTCTTGGACACAACCATGCGGGGTGGC
CGCCTGGGGGTCTTCTGCTTCTCCCAGGAGAACATCATCTGGGCCAACCTGCGTTACCGC
TGCAATGACACCATCCCAGAGGACTATGAGACCCATCAGCTGCGGCAAGCCTAG
Target 2 GenBank Gene ID
Target 2 GeneCard ID COMP Link Image
Target 2 GenAtlas ID COMP Link Image
Target 2 HGNC ID HGNC:2227 Link Image
Target 2 Chromosome Location 19
Target 2 Locus 19p13.1
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Mabuchi A, Haga N, Ikeda T, Manabe N, Ohashi H, Takatori Y, Nakamura K, Ikegawa S: Novel mutation in exon 18 of the cartilage oligomeric matrix protein gene causes a severe pseudoachondroplasia. Am J Med Genet. 2001 Nov 22;104(2):135-9. [PubMed Link Image]
  2. Unger S, Korkko J, Krakow D, Lachman RS, Rimoin DL, Cohn DH: Double heterozygosity for pseudoachondroplasia and spondyloepiphyseal dysplasia congenita. Am J Med Genet. 2001 Nov 22;104(2):140-6. [PubMed Link Image]
  3. Hecht JT, Nelson LD, Crowder E, Wang Y, Elder FF, Harrison WR, Francomano CA, Prange CK, Lennon GG, Deere M, et al.: Mutations in exon 17B of cartilage oligomeric matrix protein (COMP) cause pseudoachondroplasia. Nat Genet. 1995 Jul;10(3):325-9. [PubMed Link Image]
  4. Briggs MD, Hoffman SM, King LM, Olsen AS, Mohrenweiser H, Leroy JG, Mortier GR, Rimoin DL, Lachman RS, Gaines ES, et al.: Pseudoachondroplasia and multiple epiphyseal dysplasia due to mutations in the cartilage oligomeric matrix protein gene. Nat Genet. 1995 Jul;10(3):330-6. [PubMed Link Image]
  5. Newton G, Weremowicz S, Morton CC, Copeland NG, Gilbert DJ, Jenkins NA, Lawler J: Characterization of human and mouse cartilage oligomeric matrix protein. Genomics. 1994 Dec;24(3):435-9. [PubMed Link Image]
  6. Ballo R, Briggs MD, Cohn DH, Knowlton RG, Beighton PH, Ramesar RS: Multiple epiphyseal dysplasia, ribbing type: a novel point mutation in the COMP gene in a South African family. Am J Med Genet. 1997 Feb 11;68(4):396-400. [PubMed Link Image]
  7. Susic S, McGrory J, Ahier J, Cole WG: Multiple epiphyseal dysplasia and pseudoachondroplasia due to novel mutations in the calmodulin-like repeats of cartilage oligomeric matrix protein. Clin Genet. 1997 Apr;51(4):219-24. [PubMed Link Image]
  8. Loughlin J, Irven C, Mustafa Z, Briggs MD, Carr A, Lynch SA, Knowlton RG, Cohn DH, Sykes B: Identification of five novel mutations in cartilage oligomeric matrix protein gene in pseudoachondroplasia and multiple epiphyseal dysplasia. Hum Mutat. 1998;Suppl 1:S10-7. [PubMed Link Image]
  9. Susic S, Ahier J, Cole WG: Pseudoachondroplasia due to the substitution of the highly conserved Asp482 by Gly in the seventh calmodulin-like repeat of cartilage oligomeric matrix protein. Hum Mutat. 1998;Suppl 1:S125-7. [PubMed Link Image]
  10. Briggs MD, Mortier GR, Cole WG, King LM, Golik SS, Bonaventure J, Nuytinck L, De Paepe A, Leroy JG, Biesecker L, Lipson M, Wilcox WR, Lachman RS, Rimoin DL, Knowlton RG, Cohn DH: Diverse mutations in the gene for cartilage oligomeric matrix protein in the pseudoachondroplasia-multiple epiphyseal dysplasia disease spectrum. Am J Hum Genet. 1998 Feb;62(2):311-9. [PubMed Link Image]
  11. 9921895 Ikegawa S, Ohashi H, Nishimura G, Kim KC, Sannohe A, Kimizuka M, Fukushima Y, Nagai T, Nakamura Y: Novel and recurrent COMP (cartilage oligomeric matrix protein) mutations in pseudoachondroplasia and multiple epiphyseal dysplasia. Hum Genet. 1998 Dec;103(6):633-8.
Target 2 Drug References
  1. Chen FH, Herndon ME, Patel N, Hecht JT, Tuan RS, Lawler J: Interaction of cartilage oligomeric matrix protein/thrombospondin 5 with aggrecan. J Biol Chem. 2007 Aug 24;282(34):24591-8. Epub 2007 Jun 22. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 1108
Target 3 Name Calpastatin
Target 3 Synonyms
  1. Calpain inhibitor
  2. Sperm BS-17 component
Target 3 Gene Name CAST
Target 3 Protein Sequence >Calpastatin 
MNPTETKAIPVSQQMEGPHLPNKKKHKKQAVKTEPEKKSQSTKLSVVHEKKSQEGKPKEH
TEPKSLPKQASDTGSNDAHNKKAVSRSAEQQPSEKSTEPKTKPQDMISAGGESVAGITAI
SGKPGDKKKEKKSLTPAVPVESKPDKPSGKSGMDAALDDLIDTLGGPEETEEENTTYTGP
EVSDPMSSTYIEELGKREVTIPPKYRELLAKKEGITGPPADSSKPIGPDDAIDALSSDFT
CGSPTAAGKKTEKEESTEVLKAQSAGTVRSAAPPQEKKRKVEKDTMSDQALEALSASLGT
RQAEPELDLRSIKEVDEAKAKEEKLEKCGEDDETIPSEYRLKPATDKDGKPLLPEPEEKP
KPRSESELIDELSEDFDRSECKEKPSKPTEKTEESKAAAPAPVSEAVCRTSMCSIQSAPP
EPATLKGTVPDDAVEALADSLGKKEADPEDGKPVMDKVKEKAKEEDREKLGEKEETIPPD
YRLEEVKDKDGKPLLPKESKEQLPPMSEDFLLDALSEDFSGPQNASSLKFEDAKLAAAIS
EVVSQTPASTTQAGAPPRDTSQSDKDLDDALDKLSDSLGQRQPDPDENKPMEDKVKEKAK
AEHRDKLGERDDTIPPEYRHLLDDNGQDKPVKPPTKKSEDSKKPADDQDPIDALSGDLDS
CPSTTETSQNTAKDKCKKAASSSKAPKNGGKAKDSAKTTEETSKPKDD
Target 3 Number of Residues 719
Target 3 Molecular Weight 76573
Target 3 Theoretical pI 4.70
Target 3 GO Classification
Function
enzyme regulator activity
enzyme inhibitor activity
protease inhibitor activity
endopeptidase inhibitor activity
cysteine protease inhibitor activity
calpain inhibitor activity
Process
Not Available
Component
Not Available
Target 3 General Function Cell motility
Target 3 Specific Function Specific inhibition of calpain (calcium-dependent cysteine protease). Plays a key role in postmortem tenderization of meat and have been proposed to be involved in muscle protein degradation in living tissue
Target 3 Pathways Not Available
Target 3 Reactions Not Available
Target 3 Pfam Domain Function
Target 3 Signals
  • None
Target 3 Transmembrane Regions
  • None
Target 3 Essentiality Non-Essential
Target 3 GenBank ID Protein 303599 Link Image
Target 3 UniProtKB/Swiss-Prot ID P20810 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name ICAL_HUMAN Link Image
Target 3 PDB ID Not Available
Target 3 Cellular Location Not Available
Target 3 Gene Sequence >2127 bp 
ATGAATCCCACAGAAACCAAGGCCATTCCAGTCAGCCAACAGATGGAAGGACCACATCTT
CCTAACAAGAAAAAACACAAAAAACAGGCTGTAAAAACAGAACCTGAGAAGAAGTCACAG
TCAACCAAGCTGTCTGTGGTTCATGAGAAAAAATCCCAAGAAGGAAAGCCAAAAGAACAC
ACAGAGCCAAAAAGCCTACCCAAGCAGGCATCAGATACAGGAAGTAACGATGCTCACAAT
AAAAAAGCAGTTTCCAGATCAGCTGAACAGCAGCCATCAGAGAAATCAACAGAACCAAAG
ACTAAACCACAAGACATGATTTCTGCTGGTGGAGAGAGTGTTGCTGGTATCACTGCAATA
TCTGGCAAGCCGGGTGACAAGAAAAAAGAAAAGAAATCATTAACCCCAGCTGTGCCAGTT
GAATCTAAACCGGATAAACCATCGGGAAAGTCAGGCATGGATGCTGCTTTGGATGACTTA
ATAGATACTTTAGGAGGACCTGAAGAAACTGAAGAAGAAAATACAACGTATACTGGACCA
GAAGTTTCAGATCCAATGAGTTCCACCTACATAGAGGAATTGGGTAAAAGAGAAGTCACA
ATTCCTCCAAAATATAGGGAACTATTGGCTAAAAAGGAAGGGATCACAGGGCCTCCTGCA
GACTCTTCAAAACCCATAGGGCCAGATGATGCTATAGACGCCTTGTCATCTGACTTCACC
TGTGGGTCGCCTACAGCTGCTGGAAAGAAAACTGAAAAAGAGGAATCTACAGAAGTTTTA
AAAGCTCAGTCAGCAGGGACAGTCAGAAGTGCTGCTCCACCCCAAGAGAAGAAAAGAAAG
GTGGAGAAGGATACAATGAGTGATCAAGCACTCGAGGCTCTGTCGGCTTCACTGGGCACC
CGGCAAGCAGAACCTGAGCTCGACCTCCGCTCAATTAAGGAAGTCGATGAGGCAAAAGCT
AAAGAAGAAAAACTAGAGAAGTGTGGTGAGGATGATGAAACAATCCCATCTGAGTACAGA
TTAAAACCAGCCACGGATAAAGATGGAAAACCACTATTGCCAGAGCCTGAAGAAAAACCC
AAGCCTCGGAGTGAATCAGAACTCATTGATGAACTTTCAGAAGATTTTGACCGGTCTGAA
TGTAAAGAGAAACCATCTAAGCCAACTGAAAAGACAGAAGAATCTAAGGCCGCTGCTCCA
GCTCCTGTGTCGGAGGCTGTGTCTCGGACCTCCATGTGTAGTATACAGTCAGCACCCCCT
GAGCCGGCTACCTTGAAGGGCACAGTGCCAGATGATGCTGTAGAAGCCTTGGCTGATAGC
CTGGGGAAAAAGGAAGCAGATCCAGAAGATGGAAAACCTGTGATGGATAAAGTCAAGGAG
AAGGCCAAAGAAGAAGACCGTGAAAAGCTTGGTGAAAAAGAAGAAACAATTCCTCCTGAT
TATAGATTAGAAGAGGTCAAGGATAAAGATGGAAAGCCACTCCTGCCAAAAGAGTCTAAG
GAACAGCTTCCACCCATGAGTGAAGACTTCCTTCTGGATGCTTTGTCTGAGGACTTCTCT
GGTCCACAAAATGCTTCATCTCTTAAATTTGAAGATGCTAAACTTGCTGCTGCCATCTCT
GAAGTGGTTTCCCAAACCCCAGCTTCAACGACCCAAGCTGGAGCCCCACCCCGTGATACC
TCGCAGAGTGACAAAGACCTCGATGATGCCTTGGATAAACTCTCTGACAGTCTAGGACAA
AGGCAGCCTGACCCAGATGAGAACAAACCAATGGGAGATAAAGTAAAGGAAAAAGCTAAA
GCTGAACATAGAGACAAGCTTGGAGAAAGAGATGACACTATCCCACCTGAATACAGACAT
CTCCTGGATGATAATGGACAGGACAAACCAGTGAAGCCACCTACAAAGAAATCAGAGGAT
TCAAAGAAACCTGCAGATGACCAAGACCCCATTGATGCTCTCTCAGGAGATCTGGACAGC
TGTCCCTCCACTACAGAAACCTCACAGAACACAGCAAAGGATAAGTGCAAGAAGGCTGCT
TCCAGCTCCAAAGCACCTAAGAATGGAGGTAAAGCGAAGGATTCAGCAAAGACAACAGAG
GAAACTTCCAAGCCAAAAGATGACTAA
Target 3 GenBank Gene ID
Target 3 GeneCard ID CAST Link Image
Target 3 GenAtlas ID CAST Link Image
Target 3 HGNC ID HGNC:1515 Link Image
Target 3 Chromosome Location 5
Target 3 Locus 5q15
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Lee WJ, Ma H, Takano E, Yang HQ, Hatanaka M, Maki M: Molecular diversity in amino-terminal domains of human calpastatin by exon skipping. J Biol Chem. 1992 Apr 25;267(12):8437-42. [PubMed Link Image]
  2. Adachi Y, Ishida-Takahashi A, Takahashi C, Takano E, Murachi T, Hatanaka M: Phosphorylation and subcellular distribution of calpastatin in human hematopoietic system cells. J Biol Chem. 1991 Feb 25;266(6):3968-72. [PubMed Link Image]
  3. Uemori T, Shimojo T, Asada K, Asano T, Kimizuka F, Kato I, Maki M, Hatanaka M, Murachi T, Hanzawa H, et al.: Characterization of a functional domain of human calpastatin. Biochem Biophys Res Commun. 1990 Feb 14;166(3):1485-93. [PubMed Link Image]
  4. Maki M, Bagci H, Hamaguchi K, Ueda M, Murachi T, Hatanaka M: Inhibition of calpain by a synthetic oligopeptide corresponding to an exon of the human calpastatin gene. J Biol Chem. 1989 Nov 15;264(32):18866-9. [PubMed Link Image]
  5. Asada K, Ishino Y, Shimada M, Shimojo T, Endo M, Kimizuka F, Kato I, Maki M, Hatanaka M, Murachi T: cDNA cloning of human calpastatin: sequence homology among human, pig, and rabbit calpastatins. J Enzyme Inhib. 1989;3(1):49-56. [PubMed Link Image]
  6. Despres N, Talbot G, Plouffe B, Boire G, Menard HA: Detection and expression of a cDNA clone that encodes a polypeptide containing two inhibitory domains of human calpastatin and its recognition by rheumatoid arthritis sera. J Clin Invest. 1995 Apr;95(4):1891-6. [PubMed Link Image]
  7. Wang LF, Wei SG, Miao SY, Liu QY, Koide SS: Calpastatin gene in human testis. Biochem Mol Biol Int. 1994 May;33(2):245-51. [PubMed Link Image]
Target 3 Drug References
  1. Hanna RA, Garcia-Diaz BE, Davies PL: Calpastatin simultaneously binds four calpains with different kinetic constants. FEBS Lett. 2007 Jun 26;581(16):2894-8. Epub 2007 May 25. [PubMed Link Image]
  2. De Tullio R, Averna M, Stifanese R, Parr T, Bardsley RG, Pontremoli S, Melloni E: Multiple rat brain calpastatin forms are produced by distinct starting points and alternative splicing of the N-terminal exons. Arch Biochem Biophys. 2007 Sep 1;465(1):148-56. Epub 2007 May 30. [PubMed Link Image]
Drug Target 4 [top]
Target 4 ID 2132
Target 4 Name Protein S100-B
Target 4 Synonyms
  1. S-100 protein beta chain
  2. S-100 protein beta subunit
  3. S100 calcium-binding protein B
Target 4 Gene Name S100B
Target 4 Protein Sequence >Protein S100-B 
MSELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKEQEVVDKVMET
LDNDGDGECDFQEFMAFVAMVTTACHEFFEHE
Target 4 Number of Residues 93
Target 4 Molecular Weight 10713
Target 4 Theoretical pI 4.25
Target 4 GO Classification
Function
binding
ion binding
cation binding
calcium ion binding
Process
Not Available
Component
Not Available
Target 4 General Function Involved in calcium ion binding
Target 4 Specific Function Weakly binds calcium but binds zinc very tightly- distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase
Target 4 Pathways Not Available
Target 4 Reactions Not Available
Target 4 Pfam Domain Function
Target 4 Signals
  • None
Target 4 Transmembrane Regions
  • None
Target 4 Essentiality Non-Essential
Target 4 GenBank ID Protein 337730 Link Image
Target 4 UniProtKB/Swiss-Prot ID P04271 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name S100B_HUMAN Link Image
Target 4 PDB ID 1UWO Link Image
Target 4 PDB File Show
Target 4 3D Structure
Target 4 Cellular Location
  • Cytoplasm. Nucleus
Target 4 Gene Sequence >279 bp 
ATGTCTGAGCTGGAGAAGGCCATGGTGGCCCTCATCGACGTTTTCCACCAATATTCTGGA
AGGGAGGGAGACAAGCACAAGCTGAAGAAATCCGAACTCAAGGAGCTCATCAACAATGAG
CTTTCCCATTTCTTAGAGGAAATCAAAGAGCAGGAGGTTGTGGACAAAGTCATGGAAACA
CTGGACAATGATGGAGACGGCGAATGTGACTTCCAGGAATTCATGGCCTTTGTTGCCATG
GTTACTACTGCCTGCCACGAGTTCTTTGAACATGAGTGA
Target 4 GenBank Gene ID
Target 4 GeneCard ID S100B Link Image
Target 4 GenAtlas ID S100B Link Image
Target 4 HGNC ID HGNC:10500 Link Image
Target 4 Chromosome Location Not Available
Target 4 Locus Not Available
Target 4 SNPs SNPJam Report Link Image
Target 4 General References
  1. Allore RJ, Friend WC, O'Hanlon D, Neilson KM, Baumal R, Dunn RJ, Marks A: Cloning and expression of the human S100 beta gene. J Biol Chem. 1990 Sep 15;265(26):15537-43. [PubMed Link Image]
  2. Jensen R, Marshak DR, Anderson C, Lukas TJ, Watterson DM: Characterization of human brain S100 protein fraction: amino acid sequence of S100 beta. J Neurochem. 1985 Sep;45(3):700-5. [PubMed Link Image]
  3. Baudier J, Glasser N, Haglid K, Gerard D: Purification, characterization and ion binding properties of human brain S100b protein. Biochim Biophys Acta. 1984 Oct 23;790(2):164-73. [PubMed Link Image]
  4. Smith SP, Shaw GS: A novel calcium-sensitive switch revealed by the structure of human S100B in the calcium-bound form. Structure. 1998 Feb 15;6(2):211-22. [PubMed Link Image]
  5. Yang Q, O'Hanlon D, Heizmann CW, Marks A: Demonstration of heterodimer formation between S100B and S100A6 in the yeast two-hybrid system and human melanoma. Exp Cell Res. 1999 Feb 1;246(2):501-9. [PubMed Link Image]
Target 4 Drug References
  1. Lee TS, Mane S, Eid T, Zhao H, Lin A, Guan Z, Kim JH, Schweitzer J, King-Stevens D, Weber P, Spencer SS, Spencer DD, de Lanerolle NC: Gene expression in temporal lobe epilepsy is consistent with increased release of glutamate by astrocytes. Mol Med. 2007 Jan-Feb;13(1-2):1-13. [PubMed Link Image]
  2. Marlatt NM, Shaw GS: Amide exchange shows calcium-induced conformational changes are transmitted to the dimer interface of S100B. Biochemistry. 2007 Jun 26;46(25):7478-87. Epub 2007 May 31. [PubMed Link Image]
  3. Liang J, Luo G, Ning X, Shi Y, Zhai H, Sun S, Jin H, Liu Z, Zhang F, Lu Y, Zhao Y, Chen X, Zhang H, Guo X, Wu K, Fan D: Differential expression of calcium-related genes in gastric cancer cells transfected with cellular prion protein. Biochem Cell Biol. 2007 Jun;85(3):375-83. [PubMed Link Image]
  4. Friel LA, Romero R, Edwin S, Nien JK, Gomez R, Chaiworapongsa T, Kusanovic JP, Tolosa JE, Hassan SS, Espinoza J: The calcium binding protein, S100B, is increased in the amniotic fluid of women with intra-amniotic infection/inflammation and preterm labor with intact or ruptured membranes. J Perinat Med. 2007;35(5):385-93. [PubMed Link Image]

This project is supported by Genome Alberta & Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government. This project is also supported in part by GenomeQuest, Inc., an enterprise genomic information company serving the life science community.