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Showing drug card for Lithium (DB01356)

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Version 2.5
Creation Date 2007-07-06 19:50:35
Update Date 2009-04-16 16:48:23
Primary Accession Number DB01356
Secondary Accession Number Not Available
Name Lithium
Drug Type
  • Approved
  • Small Molecule
Description Lithium was used during the 19th century to treat gout. Lithium salts such as lithium carbonate (Li2CO3), lithium citrate, and lithium orotate are mood stabilizers. They are used in the treatment of bipolar disorder, since unlike most other mood altering drugs, they counteract both mania and depression. Lithium can also be used to augment other antidepressant drugs. It is also sometimes prescribed as a preventive treatment for migraine disease and cluster headaches. The active principle in these salts is the lithium ion Li+, which having a smaller diameter, can easily displace K+ and Na+ and even Ca+2, in spite of its greater charge, occupying their sites in several critical neuronal enzymes and neurotransmitter receptors.
Synonyms Not Available
Brand Names
  1. Eskalith
  2. LithoTab
Brand Mixtures Not Available
Chemical IUPAC Name lithium(+1) cation
Chemical Formula Li
Chemical Structure Structure
CAS Registry Number 7439-93-2
InChI Identifier InChI=1/Li/q+1
InChI Key HBBGRARXTFLTSG-UHFFFAOYAV
KEGG Drug Not Available
KEGG Compound C15473 Link Image
PubChem Compound 28486 Link Image
PubChem Substance 11538471 Link Image
ChEBI ID 30142 Link Image
PharmGKB ID PA450243 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 00236683 Link Image
RxList Link http://www.rxlist.com/cgi/generic/lithium.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Lithium Link Image
FDA Label
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 6.9410
Monoisotopic Molecular Weight 7.0160
State Solid
Melting Point 0.512 g·cm −3
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 Show Link Image | Download Link Image
SDF File Show Link Image | Download Link Image
PDB File Show Link Image | Download Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Isomeric SMILES [Li+]
Canonical SMILES [Li+]
Drug Category Not Available
ATC Codes
AHFS Codes
  • 28:28.00
  • 92:02.00*
Indication Not Available
Pharmacology Not Available
Mechanism of Action The precise mechanism of action of Li+ as a mood-stabilizing agent is currently unknown. It is possible that Li+ produces its effects by interacting with the transport of monovalent or divalent cations in neurons. An increasing number of scientists have come to the conclusion that the excitatory neurotransmitter glutamate is the key factor in understanding how lithium works. Lithium has been shown to change the inward and outward currents of glutamate receptors (especially GluR3), without a shift in reversal potential. Lithium has been found to exert a dual effect on glutamate receptors, acting to keep the amount of glutamate active between cells at a stable, healthy level, neither too much nor too little. It is postulated that too much glutamate in the space between neurons causes mania, and too little, depression. Another mechanism by which lithium might help to regulate mood include the non-competitive inhibition of an enzyme called inositol monophosphatase. Alternately lithium's action may be enhanced through the deactivation of the GSK-3B enzyme. The regulation of GSK-3B by lithium may affect the circadian clock. GSK-3 is known for phosphorylating and thus inactivating glycogen synthase. GSK-3B has also been implicated in the control of cellular response to damaged DNA.
Absorption Not Available
Toxicity Not Available
Protein Binding Not Available
Biotransformation Not Available
Half Life Not Available
Dosage Forms
Form Route
Capsule Oral
Liquid Oral
Syrup Oral
Tablet, extended release Oral
Patient Information Not Available
Contraindications Not Available
Interactions Not Available
Drug Interactions
Drug Interaction
Aminophylline Theophylline decreases serum levels of lithium
Benazepril The ACE inhibitor increases serum levels of lithium
Bendroflumethiazide The thiazide diuretic increases serum levels of lithium
Benzthiazide The thiazide diuretic increases serum levels of lithium
Bromfenac The NSAID increases serum levels of lithium
Caffeine Caffeine decreases serum levels of lithium
Candesartan The ARB increases serum levels of lithium
Captopril The ACE inhibitor increases serum levels of lithium
Celecoxib The COX-2 inhibitor increases serum levels of lithium
Chlorothiazide The thiazide diuretic increases serum levels of lithium
Chlorthalidone The thiazide diuretic increases serum levels of lithium
Cilazapril The ACE inhibitor increases serum levels of lithium
Citric Acid The urine alkalizer decreases the effect of lithium
Cyclothiazide The thiazide diuretic increases serum levels of lithium
Diclofenac The NSAID increases serum levels of lithium
Dyphylline Theophylline decreases serum levels of lithium
Enalapril The ACE inhibitor increases serum levels of lithium
Eplerenone Eplerenone increases serum levels of lithium
Eprosartan The ARB increases serum levels of lithium
Etoricoxib Etoricoxib increases serum levels of lithium
Fluoxetine The SSRI increases serum levels of lithium
Fluvoxamine The SSRI increases serum levels of lithium
Forasartan The ARB increases serum levels of lithium
Fosinopril The ACE inhibitor increases serum levels of lithium
Haloperidol Possible extrapyramidal effects and neurotoxicity with this combination
Hydrochlorothiazide The thiazide diuretic increases serum levels of lithium
Hydroflumethiazide The thiazide diuretic increases serum levels of lithium
Ibuprofen The NSAID increases serum levels of lithium
Indapamide The thiazide diuretic increases serum levels of lithium
Indomethacin The NSAID increases serum levels of lithium
Iodine Possible hypothyroidism with this combination
Irbesartan The ARB increases serum levels of lithium
Ketorolac The NSAID increases serum levels of lithium
Lisinopril The ACE inhibitor increases serum levels of lithium
Losartan Losartan increases serum levels of lithium
Lumiracoxib The COX-2 inhibitor increases serum levels of lithium
Mefenamic acid The NSAID increases serum levels of lithium
Meloxicam Meloxicam increases serum levels of lithium
Methyclothiazide The thiazide diuretic increases serum levels of lithium
Methyldopa Signs of increased lithium without increase with this combination
Metolazone The thiazide diuretic increases serum levels of lithium
Metronidazole Metronidazole increases the effect and toxicity of lithium
Moexipril The ACE inhibitor increases serum levels of lithium
Naproxen The NSAID increases serum levels of lithium
Oxtriphylline Theophylline decreases serum levels of lithium
Perindopril The ACE inhibitor increases serum levels of lithium
Phenylbutazone The NSAID increases serum levels of lithium
Piroxicam The NSAID increases serum levels of lithium
Polythiazide The thiazide diuretic increases serum levels of lithium
Potassium The urine alkalizer decreases the effect of lithium
Quinapril The ACE inhibitor increases serum levels of lithium
Quinethazone The thiazide diuretic increases serum levels of lithium
Ramipril The ACE inhibitor increases serum levels of lithium
Rofecoxib The COX-2 inhibitor increases serum levels of lithium
Saprisartan The ARB increases serum levels of lithium
Sibutramine Possible serotoninergic syndrome with this combination
Sodium bicarbonate The urine alkalizer decreases the effect of lithium
Spirapril The ACE inhibitor increases serum levels of lithium
Sumatriptan Possible serotoninergic syndrome with this combination
Tasosartan The ARB increases serum levels of lithium
Telmisartan The ARB increases serum levels of lithium
Theophylline Theophylline decreases serum levels of lithium
Topiramate Topiramate could modify lithium levels
Trandolapril The ACE inhibitor increases serum levels of lithium
Trichlormethiazide The thiazide diuretic increases serum levels of lithium
Valdecoxib The COX-2 inhibitor increases serum levels of lithium
Valsartan The ARB increases serum levels of lithium
Verapamil Signs of lithium toxicity
Food Interactions
  • Avoid alcohol.
  • Avoid excessive quantities of coffee or tea (Caffeine).
  • Avoid iodine supplements.
  • Do not change your salt intake from day to day without telling your doctor.
  • Take with food to reduce irritation. Drink plenty of liquids.
Pathways Not Available
General References
  1. Wikipedia Link Image
  2. RxList Link Image
Organisms Affected Not Available
Targets
  1. Inositol monophosphatase 2
  2. Catenin beta-1
  3. Glycogen synthase kinase-3 beta
  4. Inositol monophosphatase
  5. Inositol polyphosphate 1-phosphatase
Drug Target 1 [top]
Target 1 ID 1387
Target 1 Name Inositol monophosphatase 2
Target 1 Synonyms
  1. EC 3.1.3.25
  2. IMP 2
  3. IMPase 2
  4. Inositol- 1(or 4)-monophosphatase 2
  5. Myo-inositol monophosphatase A2
Target 1 Gene Name IMPA2
Target 1 Protein Sequence >Inositol monophosphatase 2 
MKPSGEDQAALAAGPWEECFQAAVQLALRAGQIIRKALTEEKRVSTKTSAADLVTETDHL
VEDLIISELRERFPSHRFIAEEAAASGAKCVLTHSPTWIIDPIDGTCNFVHRFPTVAVSI
GFAVRQELEFGVIYHCTEERLYTGRRGRGAFCNGQRLRVSGETDLSKALVLTEIGPKRDP
ATLKLFLSNMERLLHAKAHGVRVIGSSTLALCHLASGAADAYYQFGLHCWDLAAATVIIR
EAGGIVIDTSGGPLDLMACRVVAASTREMAMLIAQALQTINYGRDDEK
Target 1 Number of Residues 292
Target 1 Molecular Weight 31321
Target 1 Theoretical pI 6.59
Target 1 GO Classification
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on ester bonds
phosphoric ester hydrolase activity
phosphoric monoester hydrolase activity
inositol or phosphatidylinositol phosphatase activity
Process
Not Available
Component
Not Available
Target 1 General Function Carbohydrate transport and metabolism
Target 1 Specific Function Myo-inositol phosphate + H(2)O = myo-inositol + phosphate
Target 1 Pathways
Name SMPDB Link KEGG Link
Streptomycin biosynthesis map00521 Link Image
Target 1 Reactions
  • myo-inositol phosphate + H2O = myo-inositol + phosphate
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 2406666 Link Image
Target 1 UniProtKB/Swiss-Prot ID O14732 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name IMPA2_HUMAN Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location
  • Cytoplasmic
Target 1 Gene Sequence >867 bp 
ATGAAGCCGAGCGGCGAGGACCAGGCGGCGCTGGCGGCCGGCCCCTGGGAGGAGTGCTTC
CAGGCGGCCGTGCAGCTGGCGCTGCGGGCAGGACAGATCATCAGAAAAGCCCTTACTGAG
GAAAAACGTGTCTCAACAAAAACATCAGCTGCAGATCTTGTGACAGAAACAGATCACCTT
GTGGAAGATTTAATTATTTCTGAGTTGCGAGAGAGGTTTCCTTCACACAGGTTCATTGCA
GAAGAGGCCGCGGCTTCTGGGGCCAAGTGTGTGCTCACCCACAGCCCGACGTGGATCATC
GACCCCATCGACGGCACCTGCAATTTTGTGCACAGATTCCCGACTGTGGCGGTTAGCATT
GGATTTGCTGTTCGACAAGAGCTTGAATTCGGAGTGATTTACCACTGCACAGAGGAGCGG
CTGTACACGGGCCGGCGGGGTCGGGGCGCCTTCTGCAATGGCCAGCGGCTCCGGGTCTCC
GGGGAGACAGATCTCTCAAAGGCCTTGGTTCTGACAGAAATTGGCCCCAAACGTGACCCT
GCGACCCTGAAGCTGTTCCTGAGTAACATGGAGCGGCTGCTGCATGCCAAGGCGCATGGG
GTCCGAGTGATTGGAAGCTCCACATTGGCACTCTGCCACCTGGCCTCAGGGGCCGCGGAT
GCCTATTACCAGTTTGGCCTGCACTGCTGGGATCTGGCGGCTGCCACAGTCATCATCAGA
GAAGCAGGCGGCATCGTGATAGACACTTCGGGTGGACCCCTCGACCTCATGGCTTGCAGA
GTGGTTGCGGCCAGCACCCGGGAGATGGCGATGCTCATAGCTCAGGCCTTACAGACCATT
AACTATGGGCGGGATGATGAGAAGTGA
Target 1 GenBank Gene ID
Target 1 GeneCard ID IMPA2 Link Image
Target 1 GenAtlas ID IMPA2 Link Image
Target 1 HGNC ID HGNC:6051 Link Image
Target 1 Chromosome Location 18
Target 1 Locus 18p11.2
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Sjoholt G, Gulbrandsen AK, Lovlie R, Berle JO, Molven A, Steen VM: A human myo-inositol monophosphatase gene (IMPA2) localized in a putative susceptibility region for bipolar disorder on chromosome 18p11.2: genomic structure and polymorphism screening in manic-depressive patients. Mol Psychiatry. 2000 Mar;5(2):172-80. [PubMed Link Image]
  2. Yoshikawa T, Turner G, Esterling LE, Sanders AR, Detera-Wadleigh SD: A novel human myo-inositol monophosphatase gene, IMP.18p, maps to a susceptibility region for bipolar disorder. Mol Psychiatry. 1997 Sep;2(5):393-7. [PubMed Link Image]
Target 1 Drug References
  1. Cryns K, Shamir A, Shapiro J, Daneels G, Goris I, Van Craenendonck H, Straetemans R, Belmaker RH, Agam G, Moechars D, Steckler T: Lack of lithium-like behavioral and molecular effects in IMPA2 knockout mice. Neuropsychopharmacology. 2007 Apr;32(4):881-91. Epub 2006 Jul 12. [PubMed Link Image]
  2. Ohnishi T, Ohba H, Seo KC, Im J, Sato Y, Iwayama Y, Furuichi T, Chung SK, Yoshikawa T: Spatial expression patterns and biochemical properties distinguish a second myo-inositol monophosphatase IMPA2 from IMPA1. J Biol Chem. 2007 Jan 5;282(1):637-46. Epub 2006 Oct 26. [PubMed Link Image]
  3. Ohnishi T, Yamada K, Ohba H, Iwayama Y, Toyota T, Hattori E, Inada T, Kunugi H, Tatsumi M, Ozaki N, Iwata N, Sakamoto K, Iijima Y, Iwata Y, Tsuchiya KJ, Sugihara G, Nanko S, Osumi N, Detera-Wadleigh SD, Kato T, Yoshikawa T: A promoter haplotype of the inositol monophosphatase 2 gene (IMPA2) at 18p11.2 confers a possible risk for bipolar disorder by enhancing transcription. Neuropsychopharmacology. 2007 Aug;32(8):1727-37. Epub 2007 Jan 24. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 1392
Target 2 Name Catenin beta-1
Target 2 Synonyms
  1. Beta-catenin
Target 2 Gene Name CTNNB1
Target 2 Protein Sequence >Catenin beta-1 
MATQADLMELDMAMEPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEEEDVDTS
QVLYEWEQGFSQSFTQEQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPT
NVQRLAEPSQMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSK
KEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPAL
VKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDC
LQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEA
GGMQALGLHLTDPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCA
AGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEM
AQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLL
VRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFV
QLLYSPIENIQRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLF
RMSEDKPQDYKKRLSVELTSSLFRTEPMAWNETADLGLDIGAQGEPLGYRQDDPSYRSFH
SGGYGQDALGMDPMMEHEMGGHHPGADYPVDGLPDLGHAQDLMDGLPPGDSNQLAWFDTD
L
Target 2 Number of Residues 794
Target 2 Molecular Weight 85498
Target 2 Theoretical pI 5.71
Target 2 GO Classification
Function
binding
Process
Not Available
Component
Not Available
Target 2 General Function Involved in cell adhesion and signal transduction
Target 2 Specific Function Involved in the regulation of cell adhesion and in signal transduction through the Wnt pathway
Target 2 Pathways Not Available
Target 2 Reactions Not Available
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 860988 Link Image
Target 2 UniProtKB/Swiss-Prot ID P35222 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name CTNB1_HUMAN Link Image
Target 2 PDB ID 1V18 Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location
  • Cytoplasm. Nucleus. Note=Cytoplasmic when it is unstabilized (high level of phosphorylation) or boun
Target 2 Gene Sequence >2346 bp 
ATGGCTACTCAAGCTGATTTGATGGAGTTGGACATGGCCATGGAACCAGACAGAAAAGCG
GCTGTTAGTCACTGGCAGCAACAGTCTTACCTGGACTCTGGAATCCATTCTGGTGCCACT
ACCACAGCTCCTTCTCTGAGTGGTAAAGGCAATCCTGAGGAAGAGGATGTGGATACCTCC
CAAGTCCTGTATGAGTGGGAACAGGGATTTTCTCAGTCCTTCACTCAAGAACAAGTAGCT
GATATTGATGGACAGTATGCAATGACTCGAGCTCAGAGGGTACGAGCTGCTATGTTCCCT
GAGACATTAGATGAGGGCATGCAGATCCCATCTACACAGTTTGATGCTGCTCATCCCACT
AATGTCCAGCGTTTGGCTGAACCATCACAGATGCTGAAACATGCAGTTGTAAACTTGATT
AACTATCAAGATGATGCAGAACTTGCCACACGTGCAATCCCTGAACTGACAAAACTGCTA
AATGACGAGGACCAGGTGGTGGTTAATAAGGCTGCAGTTATGGTCCATCAGCTTTCTAAA
AAGGAAGCTTCCAGACACGCTATCATGCGTTCTCCTCAGATGGTGTCTGCTATTGTACGT
ACCATGCAGAATACAAATGATGTAGAAACAGCTCGTTGTACCGCTGGGACCTTGCATAAC
CTTTCCCATCATCGTGAGGGCTTACTGGCCATCTTTAAGTCTGGAGGCATTCCTGCCCTG
GTGAAAATGCTTGGTTCACCAGTGGATTCTGTGTTGTTTTATGCCATTACAACTCTCCAC
AACCTTTTATTACATCAAGAAGGAGCTAAAATGGCAGTGCGTTTAGCTGGTGGGCTGCAG
AAAATGGTTGCCTTGCTCAACAAAACAAATGTTAAATTCTTGGCTATTACGACAGACTGC
CTTCAAATTTTAGCTTATGGCAACCAAGAAAGCAAGCTCATCATACTGGCTAGTGGTGGA
CCCCAAGCTTTAGTAAATATAATGAGGACCTATACTTACGAAAAACTACTGTGGACCACA
AGCAGAGTGCTGAAGGTGCTATCTGTCTGCTCTAGTAATAAGCCGGCTATTGTAGAAGCT
GGTGGAATGCAAGCTTTAGGACTTCACCTGACAGATCCAAGTCAACGTCTTGTTCAGAAC
TGTCTTTGGACTCTCAGGAATCTTTCAGATGCTGCAACTAAACAGGAAGGGATGGAAGGT
CTCCTTGGGACTCTTGTTCAGCTTCTGGGTTCAGATGATATAAATGTGGTCACCTGTGCA
GCTGGAATTCTTTCTAACCTCACTTGCAATAATTATAAGAACAAGATGATGGTCTGCCAA
GTGGGTGGTATAGAGGCTCTTGTGCGTACTGTCCTTCGGGCTGGTGACAGGGAAGACATC
ACTGAGCCTGCCATCTGTGCTCTTCGTCATCTGACCAGCCGACACCAAGAAGCAGAGATG
GCCCAGAATGCAGTTCGCCTTCACTATGGACTACCAGTTGTGGTTAAGCTCTTACACCCA
CCATCCCACTGGCCTCTGATAAAGGCTACTGTTGGATTGATTCGAAATCTTGCCCTTTGT
CCCGCAAATCATGCACCTTTGCGTGAGCAGGGTGCCATTCCACGACTAGTTCAGTTGCTT
GTTCGTGCACATCAGGATACCCAGCGCCGTACGTCCATGGGTGGGACACAGCAGCAATTT
GTGGAGGGGGTCCGCATGGAAGAAATAGTTGAAGGTTGTACCGGAGCCCTTCACATCCTA
GCTCGGGATGTTCACAACCGAATTGTTATCAGAGGACTAAATACCATTCCATTGTTTGTG
CAGCTGCTTTATTCTCCCATTGAAAACATCCAAAGAGTAGCTGCAGGGGTCCTCTGTGAA
CTTGCTCAGGACAAGGAAGCTGCAGAAGCTATTGAAGCTGAGGGAGCCACAGCTCCTCTG
ACAGAGTTACTTCACTCTAGGAATGAAGGTGTGGCGACATATGCAGCTGCTGTTTTGTTC
CGAATGTCTGAGGACAAGCCACAAGATTACAAGAAACGGCTTTCAGTTGAGCTGACCAGC
TCTCTCTTCAGAACAGAGCCAATGGCTTGGAATGAGACTGCTGATCTTGGACTTGATATT
GGTGCCCAGGGAGAACCCCTTGGATATCGCCAGGATGATCCTAGCTATCGTTCTTTTCAC
TCTGGTGGATATGGCCAGGATGCCTTGGGTATGGACCCCATGATGGAACATGAGATGGGT
GGCCACCACCCTGGTGCTGACTATCCAGTTGATGGGCTGCCAGATCTGGGGCATGCCCAG
GACCTCATGGATGGGCTGCCTCCAGGTGACAGCAATCAGCTGGCCTGGTTTGATACTGAC
CTGTAA
Target 2 GenBank Gene ID
Target 2 GeneCard ID CTNNB1 Link Image
Target 2 GenAtlas ID CTNNB1 Link Image
Target 2 HGNC ID HGNC:2514 Link Image
Target 2 Chromosome Location 3
Target 2 Locus 3p21
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Muller T, Choidas A, Reichmann E, Ullrich A: Phosphorylation and free pool of beta-catenin are regulated by tyrosine kinases and tyrosine phosphatases during epithelial cell migration. J Biol Chem. 1999 Apr 9;274(15):10173-83. [PubMed Link Image]
  2. Kikuchi A: Regulation of beta-catenin signaling in the Wnt pathway. Biochem Biophys Res Commun. 2000 Feb 16;268(2):243-8. [PubMed Link Image]
  3. von Kries JP, Winbeck G, Asbrand C, Schwarz-Romond T, Sochnikova N, Dell'Oro A, Behrens J, Birchmeier W: Hot spots in beta-catenin for interactions with LEF-1, conductin and APC. Nat Struct Biol. 2000 Sep;7(9):800-7. [PubMed Link Image]
  4. Graham TA, Weaver C, Mao F, Kimelman D, Xu W: Crystal structure of a beta-catenin/Tcf complex. Cell. 2000 Dec 8;103(6):885-96. [PubMed Link Image]
  5. Piedra J, Martinez D, Castano J, Miravet S, Dunach M, de Herreros AG: Regulation of beta-catenin structure and activity by tyrosine phosphorylation. J Biol Chem. 2001 Jun 8;276(23):20436-43. Epub 2001 Mar 13. [PubMed Link Image]
  6. Matsuzawa SI, Reed JC: Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses. Mol Cell. 2001 May;7(5):915-26. [PubMed Link Image]
  7. Janssens B, Goossens S, Staes K, Gilbert B, van Hengel J, Colpaert C, Bruyneel E, Mareel M, van Roy F: alphaT-catenin: a novel tissue-specific beta-catenin-binding protein mediating strong cell-cell adhesion. J Cell Sci. 2001 Sep;114(Pt 17):3177-88. [PubMed Link Image]
  8. Graham TA, Ferkey DM, Mao F, Kimelman D, Xu W: Tcf4 can specifically recognize beta-catenin using alternative conformations. Nat Struct Biol. 2001 Dec;8(12):1048-52. [PubMed Link Image]
  9. Poy F, Lepourcelet M, Shivdasani RA, Eck MJ: Structure of a human Tcf4-beta-catenin complex. Nat Struct Biol. 2001 Dec;8(12):1053-7. [PubMed Link Image]
  10. Tutter AV, Fryer CJ, Jones KA: Chromatin-specific regulation of LEF-1-beta-catenin transcription activation and inhibition in vitro. Genes Dev. 2001 Dec 15;15(24):3342-54. [PubMed Link Image]
  11. 11834740 van Noort M, Meeldijk J, van der Zee R, Destree O, Clevers H: Wnt signaling controls the phosphorylation status of beta-catenin. J Biol Chem. 2002 May 17;277(20):17901-5. Epub 2002 Feb 7.
  12. 12019147 Kim JS, Crooks H, Dracheva T, Nishanian TG, Singh B, Jen J, Waldman T: Oncogenic beta-catenin is required for bone morphogenetic protein 4 expression in human cancer cells. Cancer Res. 2002 May 15;62(10):2744-8.
  13. 12027456 van Noort M, van de Wetering M, Clevers H: Identification of two novel regulated serines in the N terminus of beta-catenin. Exp Cell Res. 2002 Jun 10;276(2):264-72.
  14. 12051714 Hagen T, Vidal-Puig A: Characterisation of the phosphorylation of beta-catenin at the GSK-3 priming site Ser45. Biochem Biophys Res Commun. 2002 Jun 7;294(2):324-8.
  15. 12077367 Sadot E, Conacci-Sorrell M, Zhurinsky J, Shnizer D, Lando Z, Zharhary D, Kam Z, Ben-Ze'ev A, Geiger B: Regulation of S33/S37 phosphorylated beta-catenin in normal and transformed cells. J Cell Sci. 2002 Jul 1;115(Pt 13):2771-80.
  16. 12297051 Walters RW, Freimuth P, Moninger TO, Ganske I, Zabner J, Welsh MJ: Adenovirus fiber disrupts CAR-mediated intercellular adhesion allowing virus escape. Cell. 2002 Sep 20;110(6):789-99.
  17. 12408824 Graham TA, Clements WK, Kimelman D, Xu W: The crystal structure of the beta-catenin/ICAT complex reveals the inhibitory mechanism of ICAT. Mol Cell. 2002 Sep;10(3):563-71.
  18. 12830000 Shibata T, Chuma M, Kokubu A, Sakamoto M, Hirohashi S: EBP50, a beta-catenin-associating protein, enhances Wnt signaling and is over-expressed in hepatocellular carcinoma. Hepatology. 2003 Jul;38(1):178-86.
  19. 7806582 Hulsken J, Birchmeier W, Behrens J: E-cadherin and APC compete for the interaction with beta-catenin and the cytoskeleton. J Cell Biol. 1994 Dec;127(6 Pt 2):2061-9.
Target 2 Drug References
  1. Fathke C, Wilson L, Shah K, Kim B, Hocking A, Moon R, Isik F: Wnt signaling induces epithelial differentiation during cutaneous wound healing. BMC Cell Biol. 2006 Jan 20;7:4. [PubMed Link Image]
  2. Caldwell GM, Jones CE, Taniere P, Warrack R, Soon Y, Matthews GM, Morton DG: The Wnt antagonist sFRP1 is downregulated in premalignant large bowel adenomas. Br J Cancer. 2006 Mar 27;94(6):922-7. [PubMed Link Image]
  3. Du Q, Park KS, Guo Z, He P, Nagashima M, Shao L, Sahai R, Geller DA, Hussain SP: Regulation of human nitric oxide synthase 2 expression by Wnt beta-catenin signaling. Cancer Res. 2006 Jul 15;66(14):7024-31. [PubMed Link Image]
  4. Gould TD, Einat H, O'donnell KC, Picchini AM, Schloesser RJ, Manji HK: beta-Catenin Overexpression in the Mouse Brain Phenocopies Lithium-Sensitive Behaviors. Neuropsychopharmacology. 2007 Oct;32(10):2173-83. Epub 2007 Feb 14. [PubMed Link Image]
  5. Shim SB, Lim HJ, Chae KR, Kim CK, Hwang DY, Jee SW, Lee SH, Sin JS, Leem YH, Lee SH, Cho JS, Lee HH, Choi SY, Kim YK: Tau overexpression in transgenic mice induces glycogen synthase kinase 3beta and beta-catenin phosphorylation. Neuroscience. 2007 May 11;146(2):730-40. Epub 2007 Mar 2. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 1721
Target 3 Name Glycogen synthase kinase-3 beta
Target 3 Synonyms
  1. EC 2.7.11.26
  2. GSK-3 beta
Target 3 Gene Name GSK3B
Target 3 Protein Sequence >Glycogen synthase kinase-3 beta 
MSGRPRTTSFAESCKPVQQPSAFGSMKVSRDKDGSKVTTVVATPGQGPDRPQEVSYTDTK
VIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSG
EKKDEVYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHR
DIKPQNLLLDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDV
WSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHP
WTKVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPNVKLPNGRDTPALF
NFTTQELSSNPPLATILIPPHARIQAAASTPTNATAASDANTGDRGQTNNAASASASNST
Target 3 Number of Residues 427
Target 3 Molecular Weight 46745
Target 3 Theoretical pI 8.97
Target 3 GO Classification
Function
protein serine/threonine kinase activity
binding
nucleotide binding
purine nucleotide binding
adenyl nucleotide binding
ATP binding
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
kinase activity
protein kinase activity
Process
physiological process
metabolism
macromolecule metabolism
biopolymer metabolism
biopolymer modification
protein modification
protein amino acid phosphorylation
Component
Not Available
Target 3 General Function Involved in protein kinase activity
Target 3 Specific Function Participates in the Wnt signaling pathway. Implicated in the hormonal control of several regulatory proteins including glycogen synthase, MYB and the transcription factor JUN. Phosphorylates JUN at sites proximal to its DNA-binding domain, thereby reducing its affinity for DNA
Target 3 Pathways Not Available
Target 3 Reactions
  • ATP + [tau-protein] = ADP + O-phospho-[tau-protein] ALL_REAC (other) R03744
Target 3 Pfam Domain Function
Target 3 Signals
  • None
Target 3 Transmembrane Regions
  • None
Target 3 Essentiality Non-Essential
Target 3 GenBank ID Protein 529237 Link Image
Target 3 UniProtKB/Swiss-Prot ID P49841 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name GSK3B_HUMAN Link Image
Target 3 PDB ID 1J1C Link Image
Target 3 PDB File Show
Target 3 3D Structure
Target 3 Cellular Location Not Available
Target 3 Gene Sequence >1263 bp 
ATGTCAGGGCGGCCCAGAACCACCTCCTTTGCGGAGAGCTGCAAGCCGGTGCAGCAGCCT
TCAGCTTTTGGCAGCATGAAAGTTAGCAGAGACAAGGACGGCAGCAAGGTGACAACAGTG
GTGGCAACTCCTGGGCAGGGTCCAGACAGGCCACAAGAAGTCAGCTATACAGACACTAAA
GTGATTGGAAATGGATCATTTGGTGTGGTATATCAAGCCAAACTTTGTGATTCAGGAGAA
CTGGTCGCCATCAAGAAAGTATTGCAGGACAAGAGATTTAAGAATCGAGAGCTCCAGATC
ATGAGAAAGCTAGATCACTGTAACATAGTCCGATTGCGTTATTTCTTCTACTCCAGTGGT
GAGAAGAAAGATGAGGTCTATCTTAATCTGGTGCTGGACTATGTTCCGGAAACAGTATAC
AGAGTTGCCAGACACTATAGTCGAGCCAAACAGACGCTCCCTGTGATTTATGTCAAGTTG
TATATGTATCAGCTGTTCCGAAGTTTAGCCTATATCCATTCCTTTGGAATCTGCCATCGG
GATATTAAACCGCAGAACCTCTTGTTGGATCCTGATACTGCTGTATTAAAACTCTGTGAC
TTTGGAAGTGCAAAGCAGCTGGTCCGAGGAGAACCCAATGTTTCGTATATCTGTTCTCGG
TACTATAGGGCACCAGAGTTGATCTTTGGAGCCACTGATTATACCTCTAGTATAGATGTA
TGGTCTGCTGGCTGTGTGTTGGCTGAGCTGTTACTAGGACAACCAATATTTCCAGGGGAT
AGTGGTGTGGATCAGTTGGTAGAAATAATCAAGGTCCTGGGAACTCCAACAAGGGAGCAA
ATCAGAGAAATGAACCCAAACTACACAGAATTTAAATTCCCTCAAATTAAGGCACATCCT
TGGACTAAGGTCTTCCGACCCCGAACTCCACCGGAGGCAATTGCACTGTGTAGCCGTCTG
CTGGAGTATACACCAACTGCCCGACTAACACCACTGGAAGCTTGTGCACATTCATTTTTT
GATGAATTACGGGACCCAAATGTCAAACATCCAAATGGGCGAGACACACCTGCACTCTTC
AACTTCACCACTCAAGAACTGTCAAGTAATCCACCTCTGGCTACCATCCTTATTCCTCCT
CATGCTCGGATTCAAGCAGCTGCTTCAACCCCCACAAATGCCACAGCAGCGTCAGATGCT
AATACTGGAGACCGTGGACAGACCAATAATGCTGCTTCTGCATCAGCTTCCAACTCCACC
TGA
Target 3 GenBank Gene ID
Target 3 GeneCard ID GSK3B Link Image
Target 3 GenAtlas ID GSK3B Link Image
Target 3 HGNC ID HGNC:4617 Link Image
Target 3 Chromosome Location 3
Target 3 Locus 3q13.3
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Lau KF, Miller CC, Anderton BH, Shaw PC: Molecular cloning and characterization of the human glycogen synthase kinase-3beta promoter. Genomics. 1999 Sep 1;60(2):121-8. [PubMed Link Image]
  2. Rhoads AR, Karkera JD, Detera-Wadleigh SD: Radiation hybrid mapping of genes in the lithium-sensitive wnt signaling pathway. Mol Psychiatry. 1999 Sep;4(5):437-42. [PubMed Link Image]
  3. Hong YR, Chen CH, Chang JH, Wang S, Sy WD, Chou CK, Howng SL: Cloning and characterization of a novel human ninein protein that interacts with the glycogen synthase kinase 3beta. Biochim Biophys Acta. 2000 Jul 24;1492(2-3):513-6. [PubMed Link Image]
  4. Dajani R, Fraser E, Roe SM, Young N, Good V, Dale TC, Pearl LH: Crystal structure of glycogen synthase kinase 3 beta: structural basis for phosphate-primed substrate specificity and autoinhibition. Cell. 2001 Jun 15;105(6):721-32. [PubMed Link Image]
  5. Bax B, Carter PS, Lewis C, Guy AR, Bridges A, Tanner R, Pettman G, Mannix C, Culbert AA, Brown MJ, Smith DG, Reith AD: The structure of phosphorylated GSK-3beta complexed with a peptide, FRATtide, that inhibits beta-catenin phosphorylation. Structure. 2001 Dec;9(12):1143-52. [PubMed Link Image]
  6. Stambolic V, Woodgett JR: Mitogen inactivation of glycogen synthase kinase-3 beta in intact cells via serine 9 phosphorylation. Biochem J. 1994 Nov 1;303 ( Pt 3):701-4. [PubMed Link Image]
  7. Delcommenne M, Tan C, Gray V, Rue L, Woodgett J, Dedhar S: Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase. Proc Natl Acad Sci U S A. 1998 Sep 15;95(19):11211-6. [PubMed Link Image]
Target 3 Drug References
  1. Borsotto M, Cavarec L, Bouillot M, Romey G, Macciardi F, Delaye A, Nasroune M, Bastucci M, Sambucy JL, Luan JJ, Charpagne A, Jouet V, Leger R, Lazdunski M, Cohen D, Chumakov I: PP2A-Bgamma subunit and KCNQ2 K+ channels in bipolar disorder. Pharmacogenomics J. 2007 Apr;7(2):123-32. Epub 2006 May 30. [PubMed Link Image]
  2. Adli M, Hollinde DL, Stamm T, Wiethoff K, Tsahuridu M, Kirchheiner J, Heinz A, Bauer M: Response to Lithium Augmentation in Depression is Associated with the Glycogen Synthase Kinase 3-Beta -50T/C Single Nucleotide Polymorphism. Biol Psychiatry. 2007 Jul 10;. [PubMed Link Image]
Drug Target 4 [top]
Target 4 ID 2026
Target 4 Name Inositol monophosphatase
Target 4 Synonyms
  1. EC 3.1.3.25
  2. IMP
  3. IMPase
  4. Inositol-1(or 4)-monophosphatase
  5. Lithium-sensitive myo-inositol monophosphatase A1
Target 4 Gene Name IMPA1
Target 4 Protein Sequence >Inositol monophosphatase 
MADPWQECMDYAVTLARQAGEVVCEAIKNEMNVMLKSSPVDLVTATDQKVEKMLISSIKE
KYPSHSFIGEESVAAGEKSILTDNPTWIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFG
VVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTELGSSRTPETVRMVLSNME
KLFCIPVHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDVAGAGIIVTEAGGVLMDVTG
GPFDLMSRRVIAANNRILAERIAKEIQVIPLQRDDED
Target 4 Number of Residues 281
Target 4 Molecular Weight 30189
Target 4 Theoretical pI 4.91
Target 4 GO Classification
Function
phosphoric monoester hydrolase activity
inositol or phosphatidylinositol phosphatase activity
catalytic activity
hydrolase activity
hydrolase activity, acting on ester bonds
phosphoric ester hydrolase activity
Process
physiological process
metabolism
macromolecule metabolism
carbohydrate metabolism
Component
Not Available
Target 4 General Function Carbohydrate transport and metabolism
Target 4 Specific Function Responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides and has been implicated as the pharmacological target for lithium action in brain
Target 4 Pathways
Name SMPDB Link KEGG Link
Streptomycin biosynthesis map00521 Link Image
Target 4 Reactions
  • myo-inositol phosphate + H2O = myo-inositol + phosphate
Target 4 Pfam Domain Function
Target 4 Signals
  • None
Target 4 Transmembrane Regions
  • None
Target 4 Essentiality Non-Essential
Target 4 GenBank ID Protein 395340 Link Image
Target 4 UniProtKB/Swiss-Prot ID P29218 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name IMPA1_HUMAN Link Image
Target 4 PDB ID 1IMB Link Image
Target 4 PDB File Show
Target 4 3D Structure
Target 4 Cellular Location
  • Cytoplasm
Target 4 Gene Sequence >834 bp 
ATGGCTGATCCTTGGCAGGAATGCATGGATTATGCAGTAACTCTAGCAAGACAAGCTGGA
GAGGTAGTTTGTGAAGCTATAAAAAATGAAATGAATGTTATGCTGAAAAGTTCTCCAGTT
GATTTGGTAACTGCTACGGACCAAAAAGTTGAAAAAATGCTTATCTCTTCCATAAAGGAA
AAGTATCCATCTCACAGTTTCATTGGTGAAGAATCTGTGGCAGCTGGGGAAAAAAGTATC
TTAACCGACAACCCCACATGGATCATTGACCCTATTGATGGAACAACTAACTTTGTACAT
AGATTTCCTTTTGTAGCTGTTTCAATTGGCTTTGCTGTAAATAAAAAGATAGAATTTGGA
GTTGTGTACAGTTGTGTGGAAGGCAAGATGTACACTGCCAGAAAAGGAAAAGGGGCCTTT
TGTAATGGTCAAAAACTACAAGTTTCACAACAAGAAGATATTACCAAATCTCTCTTGGTG
ACTGAGTTGGGCTCTTCTAGAACACCAGAGACTGTGAGAATGGTTCTTTCTAATATGGAA
AAGCTTTTTTGCATTCCTGTTCATGGGATCCGGAGTGTTGGAACAGCAGCTGTTAATATG
TGCCTTGTGGCAACTGGCGGAGCAGATGCATATTATGAAATGGGAATTCACTGCTGGGAT
GTTGCAGGAGCTGGCATTATTGTTACTGAAGCTGGTGGCGTGCTAATGGATGTTACAGGT
GGACCATTTGATTTGATGTCACGAAGAGTAATTGCTGCAAATAATAGAATATTAGCAGAA
AGGATAGCTAAAGAAATTCAGGTTATACCTTTGCAACGAGACGACGAAGATTAA
Target 4 GenBank Gene ID
Target 4 GeneCard ID IMPA1 Link Image
Target 4 GenAtlas ID IMPA1 Link Image
Target 4 HGNC ID HGNC:6050 Link Image
Target 4 Chromosome Location 8
Target 4 Locus 8q21.13-q21.3
Target 4 SNPs SNPJam Report Link Image
Target 4 General References
  1. Bone R, Springer JP, Atack JR: Structure of inositol monophosphatase, the putative target of lithium therapy. Proc Natl Acad Sci U S A. 1992 Nov 1;89(21):10031-5. [PubMed Link Image]
  2. McAllister G, Whiting P, Hammond EA, Knowles MR, Atack JR, Bailey FJ, Maigetter R, Ragan CI: cDNA cloning of human and rat brain myo-inositol monophosphatase. Expression and characterization of the human recombinant enzyme. Biochem J. 1992 Jun 15;284 ( Pt 3):749-54. [PubMed Link Image]
  3. Sjoholt G, Molven A, Lovlie R, Wilcox A, Sikela JM, Steen VM: Genomic structure and chromosomal localization of a human myo-inositol monophosphatase gene (IMPA). Genomics. 1997 Oct 1;45(1):113-22. [PubMed Link Image]
Target 4 Drug References
  1. Sarkar S, Rubinsztein DC: Inositol and IP3 levels regulate autophagy: biology and therapeutic speculations. Autophagy. 2006 Apr-Jun;2(2):132-4. Epub 2006 Apr 6. [PubMed Link Image]
  2. Trinquet E, Fink M, Bazin H, Grillet F, Maurin F, Bourrier E, Ansanay H, Leroy C, Michaud A, Durroux T, Maurel D, Malhaire F, Goudet C, Pin JP, Naval M, Hernout O, Chretien F, Chapleur Y, Mathis G: D-myo-inositol 1-phosphate as a surrogate of D-myo-inositol 1,4,5-tris phosphate to monitor G protein-coupled receptor activation. Anal Biochem. 2006 Nov 1;358(1):126-35. Epub 2006 Aug 30. [PubMed Link Image]
  3. Ohnishi T, Ohba H, Seo KC, Im J, Sato Y, Iwayama Y, Furuichi T, Chung SK, Yoshikawa T: Spatial expression patterns and biochemical properties distinguish a second myo-inositol monophosphatase IMPA2 from IMPA1. J Biol Chem. 2007 Jan 5;282(1):637-46. Epub 2006 Oct 26. [PubMed Link Image]
  4. Tanizawa Y, Kuhara A, Inada H, Kodama E, Mizuno T, Mori I: Inositol monophosphatase regulates localization of synaptic components and behavior in the mature nervous system of C. elegans. Genes Dev. 2006 Dec 1;20(23):3296-310. [PubMed Link Image]
  5. Ohnishi T, Yamada K, Ohba H, Iwayama Y, Toyota T, Hattori E, Inada T, Kunugi H, Tatsumi M, Ozaki N, Iwata N, Sakamoto K, Iijima Y, Iwata Y, Tsuchiya KJ, Sugihara G, Nanko S, Osumi N, Detera-Wadleigh SD, Kato T, Yoshikawa T: A promoter haplotype of the inositol monophosphatase 2 gene (IMPA2) at 18p11.2 confers a possible risk for bipolar disorder by enhancing transcription. Neuropsychopharmacology. 2007 Aug;32(8):1727-37. Epub 2007 Jan 24. [PubMed Link Image]
Drug Target 5 [top]
Target 5 ID 3934
Target 5 Name Inositol polyphosphate 1-phosphatase
Target 5 Synonyms
  1. EC 3.1.3.57
  2. IPP
  3. IPPase
Target 5 Gene Name INPP1
Target 5 Protein Sequence >Inositol polyphosphate 1-phosphatase 
MSDILRELLCVSEKAANIARACRQQEALFQLLIEEKKEGEKNKKFAVDFKTLADVLVQEV
IKQNMENKFPGLEKNIFGEESNEFTNDWGEKITLRLCSTEEETAELLSKVLNGNKVASEA
LARVVHQDVAFTDPTLDSTEINVPQDILGIWVDPIDSTYQYIKGSADIKSNQGIFPCGLQ
CVTILIGVYDIQTGVPLMGVINQPFVSRDPNTLRWKGQCYWGLSYMGTNMHSLQLTISRR
NGSETHTGNTGSEAAFSPSFSAVISTSEKETIKAALSRVCGDRIFGAAGAGYKSLCVVQG
LVDIYIFSEDTTFKWDSCAAHAILRAMGGGIVDLKECLERNPETGLDLPQLVYHVENEGA
AGVDRWANKGGLIAYRSRKRLETFLSLLVQNLAPAETHT
Target 5 Number of Residues 405
Target 5 Molecular Weight 43998
Target 5 Theoretical pI 4.91
Target 5 GO Classification
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on ester bonds
phosphoric ester hydrolase activity
phosphoric monoester hydrolase activity
inositol or phosphatidylinositol phosphatase activity
Process
Not Available
Component
Not Available
Target 5 General Function Inorganic ion transport and metabolism
Target 5 Specific Function 1D-myo-inositol 1,4-bisphosphate + H(2)O = 1D- myo-inositol 4-phosphate + phosphate
Target 5 Pathways
Name SMPDB Link KEGG Link
Phosphatidylinositol signaling system map00562 Link Image
Target 5 Reactions
  • 1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-phosphate + phosphate
Target 5 Pfam Domain Function
Target 5 Signals
  • None
Target 5 Transmembrane Regions
  • None
Target 5 Essentiality Non-Essential
Target 5 GenBank ID Protein 186426 Link Image
Target 5 UniProtKB/Swiss-Prot ID P49441 Link Image
Target 5 UniProtKB/Swiss-Prot Entry Name INPP_HUMAN Link Image
Target 5 PDB ID Not Available
Target 5 Cellular Location
  • Cytoplasmic
Target 5 Gene Sequence >1200 bp 
ATGTCAGATATCCTCCGGGAGCTGCTCTGTGTCTCTGAGAAGGCTGCTAACATTGCCCGG
GCGTGCAGACAGCAGGAAGCCCTCTTCCAGCTGCTGATCGAAGAAAAGAAAGAGGGAGAA
AAGAACAAGAAGTTTGCAGTTGACTTCAAGACTCTGGCTGATGTACTGGTACAGGAAGTT
ATAAAACAGAATATGGAGAACAAGTTTCCAGGCTTGGAAAAAAATATTTTTGGAGAAGAA
TCCAATGAGTTTACTAATGACTGGGGGGAAAAGATTACCTTGAGGTTGTGTTCAACAGAG
GAAGAAACAGCAGAGCTTCTTAGCAAAGTCCTCAATGGTAACAAGGTAGCATCTGAAGCA
TTAGCCAGGGTTGTTCATCAGGATGTTGCCTTTACTGACCCAACTCTGGATTCCACAGAG
ATCAATGTTCCACAGGACATTTTGGGAATTTGGGTGGACCCCATAGATTCAACTTATCAG
TATATAAAAGGTTCTGCTGACATTAAATCCAACCAGGGAATCTTCCCCTGTGGACTTCAG
TGTGTCACCATTTTAATTGGTGTCTATGACATACAGACAGGGGTTCCCCTGATGGGAGTC
ATCAATCAACCTTTTGTGTCACGAGATCCAAACACCCTCAGGTGGAAAGGACAGTGCTAT
TGGGGCCTTTCTTACATGGGGACCAACATGCATTCACTACAGCTCACCATCTCTAGAAGA
AACGGCAGTGAAACACACACTGGAAACACCGGCTCTGAGGCAGCATTCTCCCCCAGTTTT
TCAGCCGTAATTAGTACAAGTGAAAAGGAGACTATCAAAGCTGCATTGTCACGTGTGTGT
GGAGATCGCATATTTGGGGCAGCTGGGGCTGGTTATAAGAGCCTATGTGTTGTCCAAGGC
CTCGTTGACATTTACATCTTTTCAGAAGATACCACATTCAAATGGGACTCTTGTGCTGCT
CATGCCATACTGCGGGCCATGGGTGGGGGAATAGTAGACTTGAAAGAATGCTTAGAAAGA
AATCCAGAAACAGGGCTTGATTTGCCACAGTTGGTGTACCACGTGGAAAATGAGGGTGCT
GCTGGGGTGGATCGGTGGGCCAACAAGGGAGGACTCATTGCATACAGATCCAGGAAGCGG
CTGGAGACATTCCTGAGCCTCCTGGTCCAAAACCTGGCACCTGCAGAGACGCATACCTAG
Target 5 GenBank Gene ID
Target 5 GeneCard ID INPP1 Link Image
Target 5 GenAtlas ID INPP1 Link Image
Target 5 HGNC ID HGNC:6071 Link Image
Target 5 Chromosome Location 2
Target 5 Locus 2q32
Target 5 SNPs SNPJam Report Link Image
Target 5 General References
  1. Lovlie R, Gulbrandsen AK, Molven A, Steen VM: Genomic structure and sequence analysis of a human inositol polyphosphate 1-phosphatase gene (INPP1). Pharmacogenetics. 1999 Aug;9(4):517-28. [PubMed Link Image]
  2. York JD, Veile RA, Donis-Keller H, Majerus PW: Cloning, heterologous expression, and chromosomal localization of human inositol polyphosphate 1-phosphatase. Proc Natl Acad Sci U S A. 1993 Jun 15;90(12):5833-7. [PubMed Link Image]
Target 5 Drug References
  1. Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [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.