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Showing drug card for Halothane (DB01159)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-06-23 18:06:33
Primary Accession Number DB01159
Secondary Accession Number
  • APRD00598
Name Halothane
Drug Type
  • Approved
  • Small Molecule
Description A nonflammable, halogenated, hydrocarbon anesthetic that provides relatively rapid induction with little or no excitement. Analgesia may not be adequate. nitrous oxide is often given concomitantly. Because halothane may not produce sufficient muscle relaxation, supplemental neuromuscular blocking agents may be required. (From AMA Drug Evaluations Annual, 1994, p178)
Synonyms
  1. Alotano [Dcit]
  2. Bromchlortrifluoraethanum
  3. Bromochlorotrifluoroethane
  4. Cf3chclbr
  5. Fluorotane
  6. Fluorothane
  7. Freon 123b1
  8. Ftorotan [Russian]
  9. Ftuorotan
  10. Halotano [INN-Spanish]
  11. Halothan
  12. Halothanum [INN-Latin]
  13. Narcotann Ne-Spofa [Russian]
Brand Names
  1. Anestan
  2. Chalothane
  3. Fluktan
  4. Fluothane
  5. Halan
  6. Halotan
  7. Halothane
  8. Halsan
  9. Narcotan
  10. Narcotane
  11. Narkotan
  12. Phthorothanum
  13. Rhodialothan
Brand Mixtures Not Available
Chemical IUPAC Name 2-bromo-2-chloro-1,1,1-trifluoroethane
Chemical Formula C2HBrClF3
Chemical Structure Structure
CAS Registry Number 151-67-7
InChI Identifier InChI=1/C2HBrClF3/c3-1(4)2(5,6)7/h1H
InChI Key BCQZXOMGPXTTIC-UHFFFAOYAO
KEGG Drug D00542 Link Image
KEGG Compound C07515 Link Image
PubChem Compound 3562 Link Image
PubChem Substance 7847608 Link Image
ChEBI ID 5615 Link Image
PharmGKB ID PA449845 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 00589187 Link Image
RxList Link http://www.rxlist.com/cgi/generic2/halothane.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Halothane Link Image
FDA Label Not Available
Material Safety Data Sheet (MSDS)
Synthesis Reference Suckling, Raventos, U.S. pat. 2,921,098 (1960 to I.C.I.); Scherer, Kuhn, U.S. pat. 2,959,624 (1960 to Hoechst)
Average Molecular Weight 197.3820
Monoisotopic Molecular Weight 195.8902
State Liquid
Melting Point -118 oC
Experimental Water Solubility 3.45 mg/ml Source: PhysProp
Predicted Water Solubility 3.81e+00 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 2.7 Source: PhysProp
Predicted LogP 2.50 Calculated using ALOGPS
Experimental LogS -1.71 [ADME Research, USCD]
Predicted LogS -1.71 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 FC(F)(F)[C@H](Cl)Br
Canonical SMILES FC(F)(F)C(Cl)Br
Drug Category
  • Anesthetics
  • Anesthetics, Inhalation
  • General Anesthetics
ATC Codes
AHFS Codes
  • 28:04.00
Indication For the induction and maintenance of general anesthesia
Pharmacology Halothane is a general inhalation anesthetic used for induction and maintenance of general anesthesia. It reduces the blood pressure and frequently decreases the pulse rate and depresses respiration. It induces muscle relaxation and reduces pains sensitivity by altering tissue excitability. It does so by decreasing the extent of gap junction mediated cell-cell coupling and altering the activity of the channels that underlie the action potential.
Mechanism of Action Halothane induces a reduction in junctional conductance by decreasing gap junction channel opening times and increasing gap junction channel closing times. Halothane also activates calcium dependent ATPase in the sarcoplasmic reticulum by increasing the fluidity of the lipid membrane. Also appears to bind the D subunit of ATP synthase and NADH dehydogenase. Halothane also binds to the GABA receptor, the large conductance Ca2+ activated potassium channel, the glutamate receptor and the glycine receptor.
Absorption Not Available
Toxicity Not Available
Protein Binding Not Available
Biotransformation Not Available
Half Life Not Available
Dosage Forms
Form Route
Liquid Respiratory (inhalation)
Solution Respiratory (inhalation)
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions Not Available
Food Interactions Not Available
Pathways Not Available
General References
  1. Drugs.com Link Image
  2. Wikipedia Link Image
  3. RxList Link Image
Organisms Affected
  • Humans and other mammals
Phase 1 Metabolizing Enzymes
  1. Cytochrome P450 2A6 (CYP2A6)
  2. Cytochrome P450 2E1 (CYP2E1)
Targets
  1. Calcium-transporting ATPase type 2C member 1
  2. Intermediate conductance calcium-activated potassium channel protein 4
  3. Glycine receptor subunit alpha-1
  4. Potassium large conductance calcium-activated channel, subfamily M, alpha member 1
  5. ATP synthase delta chain, mitochondrial
  6. NADH-ubiquinone oxidoreductase chain 1
  7. Serum albumin
  8. Glutamate receptor 1
  9. Gamma-aminobutyric-acid receptor subunit alpha-1
  10. Neuropeptide S receptor
  11. G protein-activated inward rectifier potassium channel 1
  12. G protein-activated inward rectifier potassium channel 2
  13. Guanine nucleotide-binding protein G(I)/G(S)/G(O) gamma-2 subunit
  14. Rhodopsin
Phase 1 Metabolizing Enzyme 1 [top]
Enzyme 1 Name Cytochrome P450 2A6 (CYP2A6)
Enzyme 1 Gene Name CYP2A6
Enzyme 1 SwissProt ID P11509 Link Image
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 Protein Sequence >sp|P11509|CP2A6_HUMAN Cytochrome P450 2A6 (EC 1.14.14.1)
MLASGMLLVALLVCLTVMVLMSVWQQRKSKGKLPPGPTPLPFIGNYLQLNTEQMYNSLMK
ISERYGPVFTIHLGPRRVVVLCGHDAVREALVDQAEEFSGRGEQATFDWVFKGYGVVFSN
GERAKQLRRFSIATLRDFGVGKRGIEERIQEEAGFLIDAHRGTGGANIDPTFFLSRTVSN
VISSIVFGDRFDYKDKEFLSLLRMMLGIFQFTSTSTGQLYEMFSSVMKHLPGPQQQAFQL
LQGLEDFIAKKVEHNQRTLDPNSPRDFIDSFLIRMQEEEKNPNTEFYLKNLVMTTLNLFI
GGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGKNRQPKFEDRAKMPYMEAVIHEIQ
RFGDVIPMSLARRVKKDTKFRDFFLPKGTEVYPMLGSVLRDPSFFSNPQDFNPQHFLNEK
GQFKKSDAFVPFSIGKRNCFGEGLARMELFLFFTTVMQNFRLKSSQSPKDIDVSPKHVGF
ATIPRNYTMSFLPR
Phase 1 Metabolizing Enzyme 2 [top]
Enzyme 2 Name Cytochrome P450 2E1 (CYP2E1)
Enzyme 2 Gene Name CYP2E1
Enzyme 2 SwissProt ID P05181 Link Image
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 Protein Sequence >sp|P05181|CP2E1_HUMAN Cytochrome P450 2E1 (EC 1.14.14.1)
MSALGVTVALLVWAAFLLLVSMWRQVHSSWNLPPGPFPLPIIGNLFQLELKNIPKSFTRL
AQRFGPVFTLYVGSQRMVVMHGYKAVKEALLDYKDEFSGRGDLPAFHAHRDRGIIFNNGP
TWKDIRRFSLTTLRNYGMGKQGNESRIQREAHFLLEALRKTQGQPFDPTFLIGCAPCNVI
ADILFRKHFDYNDEKFLRLMYLFNENFHLLSTPWLQLYNNFPSFLHYLPGSHRKVIKNVA
EVKEYVSERVKEHHQSLDPNCPRDLTDCLLVEMEKEKHSAERLYTMDGITVTVADLFFAG
TETTSTTLRYGLLILMKYPEIEEKLHEEIDRVIGPSRIPAIKDRQEMPYMDAVVHEIQRF
ITLVPSNLPHEATRDTIFRGYLIPKGTVVVPTLDSVLYDNQEFPDPEKFKPEHFLNENGK
FKYSDYFKPFSTGKRVCAGEGLARMELFLLLCAILQHFNLKPLVDPKDIDLSPIHIGFGC
IPPRYKLCVIPRS
Drug Target 1 [top]
Target 1 ID 241
Target 1 Name Calcium-transporting ATPase type 2C member 1
Target 1 Synonyms
  1. ATP-dependent Ca(2+
  2. ATPase 2C1
  3. EC 3.6.3.8
Target 1 Gene Name ATP2C1
Target 1 Protein Sequence >Calcium-transporting ATPase type 2C member 1
MKVARFQKIPNGENETMIPVLTSKKASELPVSEVASILQADLQNGLNKCEVSHRRAFHGW
NEFDISEDEPLWKKYISQFKNPLIMLLLASAVISVLMHQFDDAVSITVAILIVVTVAFVQ
EYRSEKSLEELSKLVPPECHCVREGKLEHTLARDLVPGDTVCLSVGDRVPADLRLFEAVD
LSIDESSLTGETTPCSKVTAPQPAATNGDLASRSNIAFMGTLVRCGKAKGVVIGTGENSE
FGEVFKMMQAEEAPKTPLQKSMDLLGKQLSFYSFGIIGIIMLVGWLLGKDILEMFTISVS
LAVAAIPEGLPIVVTVTLALGVMRMVKKRAIVKKLPIVETLGCCNVICSDKTGTLTKNEM
TVTHIFTSDGLHAEVTGVGYNQFGEVIVDGDVVHGFYNPAVSRIVEAGCVCNDAVIRNNT
LMGKPTEGALIALAMKMGLDGLQQDYIRKAEYPFSSEQKWMAVKCVHRTQQDRPEICFMK
GAYEQVIKYCTTYQSKGQTLTLTQQQRDVYQQEKARMGSAGLRVLALASGPELGQLTFLG
LVGIIDPPRTGVKEAVTTLIASGVSIKMITGDSQETAVAIASRLGLYSKTSQSVSGEEID
AMDVQQLSQIVPKVAVFYRASPRHKMKIIKSLQKNGSVVAMTGDGVNDAVALKAADIGVA
MGQTGTDVCKEAADMILVDDDFQTIMSAIEEGKGIYNNIKNFVRFQLSTSIAALTLISLA
TLMNFPNPLNAMQILWINIIMDGPPAQSLGVEPVDKDVIRKPPRNWKDSILTKNLILKIL
VSSIIIVCGTLFVFWRELRDNVITPRDTTMTFTCFVFFDMFNALSSRSQTKSVFEIGLCS
NRMFCYAVLGSIMGQLLVIYFPPLQKVFQTESLSILDLLFLLGLTSSVCIVAEIIKKVER
SREKIQKHVSSTSSSFLEV
Target 1 Number of Residues 934
Target 1 Molecular Weight 100579
Target 1 Theoretical pI 6.72
Target 1 GO Classification
Function
hydrolase activity
hydrolase activity, acting on acid anhydrides
hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
catalytic activity
ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
binding
nucleotide binding
purine nucleotide binding
adenyl nucleotide binding
ATP binding
transporter activity
ion transporter activity
cation transporter activity
di-, tri-valent inorganic cation transporter activity
calcium ion transporter activity
calcium-transporting ATPase activity
Process
metabolism
physiological process
cellular physiological process
transport
ion transport
cation transport
di-, tri-valent inorganic cation transport
calcium ion transport
Component
cell
membrane
intrinsic to membrane
integral to membrane
Target 1 General Function Inorganic ion transport and metabolism
Target 1 Specific Function This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of the calcium
Target 1 Pathways Not Available
Target 1 Reactions
  • ATP + H2O + Ca2+cis = ADP + phosphate + Ca2+trans
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • 71-91
  • 105-123
  • 263-282
  • 295-312
  • 700-719
  • 730-750
  • 771-793
  • 809-828
  • 842-860
  • 876-896
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 6715131 Link Image
Target 1 UniProtKB/Swiss-Prot ID P98194 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name AT2C1_HUMAN Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location
  • Golgi apparatus
  • Golgi apparatus membrane
  • multi-pass membrane protein
Target 1 Gene Sequence >2760 bp
ATGAAGGTTGCACGTTTTCAAAAAATACCTAATGGTGAAAATGAGACAATGATTCCTGTA
TTGACATCAAAAAAAGCAAGTGAATTACCAGTCAGTGAAGTTGCAAGCATTCTCCAAGCT
GATCTTCAGAATGGTCTAAACAAATGTGAAGTTAGTCATAGGCGAGCCTTTCATGGCTGG
AATAAGTTTGATATTAGTGAAGATGAGCCACTGTGGAAGAAGTATATTTCTCAGTTTAAA
AATCCCCTTATTATGCTGCTTCTGGCTTCTGCAGTCATCAGTGTTTTAATGCATCAGTTT
GATGATGCCGTCAGTATCACTGTGGCAATACTTATCGTTGTTACAGTTGCCTTTGTTCAG
GAATATCGTTCAGAAAAATCTCTTGAAGAATTGAGTAAACTTGTGCCACCAGAATGCCAT
TGTGTGCGTGAAGGAAAATTGGAGCATACACTTGCCCGAGACTTGGTTCCAGGTGATACA
GTTTGCCTTTCTGTTGGGGATAGAGTTCCTGCTGACTTACGCTTGTTTGAGGCTGTGGAT
CTTTCCATTGATGAGTCCAGCTTGACAGGTGAGACAACGCCTTGTTCTAAGGTGACAGCT
CCTCAGCCAGCTGCAACTAATGGAGATCTTGCATCGAGAAGTAACATTGCCTTTATGGGA
ACACTGGTCAGATGTGGCAAAGCAAAGGGTGTTGTCATTGGAACAGGAGAAAATTCTGAA
TTTGGGGAGGTTTTTAAAATGATGCAAGCAGAAGAGGCACCAAAAACCCCTCTGCAGAAG
AGCATGGACCTCTTAGGAAAACAACTTTCCTTTTACTCCTTTGGTATAATAGGAATCATC
ATGTTGGTTGGCTGGTTACTGGGAAAAGATATCCTGGAAATGTTTACTATTAGTGTAAGT
TTGGCTGTAGCAGCAATTCCTGAAGGTCTCCCCATTGTGGTCACAGTGACGCTAGCTCTT
GGTGTTATGAGAATGGTGAAGAAAAGGGCCATTGTGAAAAAGCTGCCTATTGTTGAAACT
CTGGGCTGCTGTAATGTGATTTGTTCAGATAAAACTGGAACACTGACGAAGAATGAAATG
ACTGTTACTCACATATTTACTTCAGATGGTCTGCATACTGAGGTTACTGGAGTTGGCTAT
AATCAATTTGGGGAAGTGATTGTTGATGGTGATGTTGTTCATGGATTCTATAACCCAGCT
GTTAGCAGAATTGTTGAGGCGGGCTGTGTGTGCAATGATGCTGTAATTAGAAACAATACT
CTAATGGGGAAGCCAACAGAAGGGGCCTTAATTGCTCTTGCAATGAAGATGGGTCTTGAT
GGACTTCAACAAGACTACATCAGAAAAGCTGAATACCCTTTTAGCTCTGAGCAAAAGTGG
ATGGCTGTTAAGTGTGTACACCGAACACAGCAGGACAGACCAGAGATTTGTTTTATGAAA
GGTGCTTACGAACAAGTAATTAAGTACTGTACTACATACCAGAGCAAAGGGCAGACCTTG
ACACTTACTCAGCAGCAGAGAGATGTGTACCAACAAGAGAAGGCACGCATGGGCTCAGCG
GGACTCAGAGTTCTTGCTTTGGCTTCTGGTCCTGAACTGGGACAGCTGACATTTCTTGGC
TTGGTGGGAATCATTGATCCACCTAGAACTGGTGTGAAAGAAGCTGTTACAACACTCATT
GCCTCAGGAGTATCAATAAAAATGATTACTGGAGATTCACAGGAGACTGCAGTTGCAATC
GCCAGTCGTCTGGGATTGTATTCCAAAACTTCCCAGTCAGTCTCAGGAGAAGAAATAGAT
GCAATGGATGTTCAGCAGCTTTCACAAATAGTACCAAAGGTTGCAGTATTTTACAGAGCT
AGCCCAAGGCACAAGATGAAAATTATTAAGTCGCTACAGAAGAACGGTTCAGTTGTAGCC
ATGACAGGAGATGGAGTAAATGATGCAGTTGCTCTGAAGGCTGCAGACATTGGAGTTGCG
ATGGGCCAGACTGGTACAGATGTTTGCAAAGAGGCAGCAGACATGATCCTAGTGGATGAT
GATTTTCAAACCATAATGTCTGCAATCGAAGAGGGTAAAGGGATTTATAATAACATTAAA
AATTTCGTTAGATTCCAGCTGAGCACGAGTATAGCAGCATTAACTTTAATCTCATTGGCT
ACATTAATGAACTTTCCTAATCCTCTCAATGCCATGCAGATTTTGTGGATCAATATTATT
ATGGATGGACCCCCAGCTCAGAGCCTTGGAGTAGAACCAGTGGATAAAGATGTCATTCGT
AAACCTCCTCGCAACTGGAAAGACAGCATTTTGACTAAAAACTTGATACTTAAAATACTT
GTTTCATCAATAATCATTGTTTGTGGGACTTTGTTTGTCTTCTGGCGTGAGCTACGAGAC
AATGTGATTACACCTCGAGACACAACAATGACCTTCACATGCTTTGTGTTTTTTGACATG
TTCAATGCACTAAGTTCCAGATCCCAGACCAAGTCTGTGTTTGAGATTGGACTCTGCAGT
AATAGAATGTTTTGCTATGCAGTTCTTGGATCCATCATGGGACAATTACTAGTTATTTAC
TTTCCTCCGCTTCAGAAGGTTTTTCAGACTGAGAGCCTAAGCATACTGGATCTGTTGTTT
CTTTTGGGTCTCACCTCATCAGTGTGCATAGTGGCAGAAATTATAAAGAAGGTTGAAAGG
AGCAGGGAAAAGATCCAGAAGCATGTTAGTTCGACATCATCATCTTTTCTTGAAGTATGA
Target 1 GenBank Gene ID
Target 1 GeneCard ID ATP2C1 Link Image
Target 1 GenAtlas ID ATP2C1 Link Image
Target 1 HGNC ID HGNC:13211 Link Image
Target 1 Chromosome Location 3
Target 1 Locus 3q22.1
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Hu Z, Bonifas JM, Beech J, Bench G, Shigihara T, Ogawa H, Ikeda S, Mauro T, Epstein EH Jr: Mutations in ATP2C1, encoding a calcium pump, cause Hailey-Hailey disease. Nat Genet. 2000 Jan;24(1):61-5. [PubMed Link Image]
  2. Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Feb 28;7(1):65-73. [PubMed Link Image]
  3. Sudbrak R, Brown J, Dobson-Stone C, Carter S, Ramser J, White J, Healy E, Dissanayake M, Larregue M, Perrussel M, Lehrach H, Munro CS, Strachan T, Burge S, Hovnanian A, Monaco AP: Hailey-Hailey disease is caused by mutations in ATP2C1 encoding a novel Ca(2+) pump. Hum Mol Genet. 2000 Apr 12;9(7):1131-40. [PubMed Link Image]
  4. Stanchi F, Bertocco E, Toppo S, Dioguardi R, Simionati B, Cannata N, Zimbello R, Lanfranchi G, Valle G: Characterization of 16 novel human genes showing high similarity to yeast sequences. Yeast. 2001 Jan 15;18(1):69-80. [PubMed Link Image]
  5. Fairclough RJ, Dode L, Vanoevelen J, Andersen JP, Missiaen L, Raeymaekers L, Wuytack F, Hovnanian A: Effect of Hailey-Hailey Disease mutations on the function of a new variant of human secretory pathway Ca2+/Mn2+-ATPase (hSPCA1). J Biol Chem. 2003 Jul 4;278(27):24721-30. Epub 2003 Apr 21. [PubMed Link Image]
Target 1 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 462
Target 2 Name Intermediate conductance calcium-activated potassium channel protein 4
Target 2 Synonyms
  1. IK1
  2. IKCa1
  3. KCa4
  4. Putative Gardos channel
  5. SK4
Target 2 Gene Name KCNN4
Target 2 Protein Sequence >Intermediate conductance calcium-activated potassium channel protein 4
MGGDLVLGLGALRRRKRLLEQEKSLAGWALVLAGTGIGLMVLHAEMLWFGGCSWALYLFL
VKCTISISTFLLLCLIVAFHAKEVQLFMTDNGLRDWRVALTGRQAAQIVLELVVCGLHPA
PVRGPPCVQDLGAPLTSPQPWPGFLGQGEALLSLAMLLRLYLVPRAVLLRSGVLLNASYR
SIGALNQVRFRHWFVAKLYMNTHPGRLLLGLTLGLWLTTAWVLSVAERQAVNATGHLSDT
LWLIPITFLTIGYGDVVPGTMWGKIVCLCTGVMGVCCTALLVAVVARKLEFNKAEKHVHN
FMMDIQYTKEMKESAARVLQEAWMFYKHTRRKESHAARRHQRKLLAAINAFRQVRLKHRK
LREQVNSMVDISKMHMILYDLQQNLSSSHRALEKQIDTLAGKLDALTELLSTALGPRQLP
EPSQQSK
Target 2 Number of Residues 434
Target 2 Molecular Weight 47696
Target 2 Theoretical pI 10.39
Target 2 GO Classification
Function
voltage-gated ion channel activity
voltage-gated potassium channel activity
transporter activity
ion transporter activity
ion channel activity
cation channel activity
potassium channel activity
calcium-activated potassium channel activity
binding
protein binding
calmodulin binding
Process
physiological process
cellular physiological process
transport
ion transport
cation transport
monovalent inorganic cation transport
potassium ion transport
Component
protein complex
voltage-gated potassium channel complex
cell
membrane
intrinsic to membrane
integral to membrane
Target 2 General Function Inorganic ion transport and metabolism
Target 2 Specific Function Forms a voltage-independent potassium channel that is activated by intracellular calcium. Activation is followed by membrane hyperpolarization which promotes calcium influx. The channel is blocked by clotrimazole and charybdotoxin but is insensitive to apamin
Target 2 Pathways Not Available
Target 2 Reactions Not Available
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • 29-49
  • 59-79
  • 108-128
  • 143-163
  • 207-227
  • 241-261
  • 265-285
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 2584866 Link Image
Target 2 UniProtKB/Swiss-Prot ID O15554 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name KCNN4_HUMAN Link Image
Target 2 PDB ID Not Available
Target 2 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 2 Gene Sequence >1284 bp
ATGGGCGGGGATCTGGTGCTTGGCCTGGGGGCCTTGAGACGCCGAAAGCGCTTGCTGGAG
CAGGAGAAGTCTCTGGCCGGCTGGGCACTGGTGCTGGCAGGAACTGGCATTGGACTCATG
GTGCTGCATGCAGAGATGCTGTGGTTCGGGGGGTGCTCGTGGGCGCTCTACCTGTTCCTG
GTTAAATGCACGATCAGCATTTCCACCTTCTTACTCCTCTGCCTCATCGTGGCCTTTCAT
GCCAAAGAGGTCCAGCTGTTCATGACCGACAACGGGCTGCGGGACTGGCGCGTGGCGCTG
ACCGGGCGGCAGGCGGCGCAGATCGTGCTGGAGCTGGTGGTGTGTGGGCTGCACCCGGCG
CCCGTGCGGGGCCCGCCGTGCGTGCAGGATTTAGGGGCGCCGCTGACCTCCCCGCAGCCC
TGGCCGGGATTCCTGGGCCAAGGGGAAGCGCTGCTGTCCCTGGCCATGCTGCTGCGTCTC
TACCTGGTGCCCCGCGCCGTGCTCCTGCGCAGCGGCGTCCTGCTCAACGCTTCCTACCGC
AGCATCGGCGCTCTCAATCAAGTCCGCTTCCGCCACTGGTTCGTGGCCAAGCTTTACATG
AACACGCACCCTGGCCGCCTGCTGCTCGGCCTCACGCTTGGCCTCTGGCTGACCACCGCC
TGGGTGCTGTCCGTGGCCGAGAGGCAGGCTGTTAATGCCACTGGGCACCTTTCAGACACA
CTTTGGCTGATCCCCATCACATTCCTGACCATCGGCTATGGTGACGTGGTGCCGGGCACC
ATGTGGGGCAAGATCGTCTGCCTGTGCACTGGAGTCATGGGTGTCTGCTGCACAGCCCTG
CTGGTGGCCGTGGTGGCCCGGAAGCTGGAGTTTAACAAGGCAGAGAAGCACGTGCACAAC
TTCATGATGGATATCCAGTATACCAAAGAGATGAAGGAGTCCGCTGCCCGAGTGCTACAA
GAAGCCTGGATGTTCTACAAACATACTCGCAGGAAGGAGTCTCATGCTGCCCGCAGGCAT
CAGCGCAAGCTGCTGGCCGCCATCAACGCGTTCCGCCAGGTGCGGCTGAAACACCGGAAG
CTCCGGGAACAAGTGAACTCCATGGTGGACATCTCCAAGATGCACATGATCCTGTATGAC
CTGCAGCAGAATCTGAGCAGCTCACACCGGGCCCTGGAGAAACAGATTGACACGCTGGCG
GGGAAGCTGGATGCCCTGACTGAGCTGCTTAGCACTGCCCTGGGGCCGAGGCAGCTTCCA
GAACCCAGCCAGCAGTCCAAGTAG
Target 2 GenBank Gene ID
Target 2 GeneCard ID KCNN4 Link Image
Target 2 GenAtlas ID KCNN4 Link Image
Target 2 HGNC ID HGNC:6293 Link Image
Target 2 Chromosome Location 19
Target 2 Locus 19q13.2
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Fanger CM, Ghanshani S, Logsdon NJ, Rauer H, Kalman K, Zhou J, Beckingham K, Chandy KG, Cahalan MD, Aiyar J: Calmodulin mediates calcium-dependent activation of the intermediate conductance KCa channel, IKCa1. J Biol Chem. 1999 Feb 26;274(9):5746-54. [PubMed Link Image]
  2. Wulff H, Gutman GA, Cahalan MD, Chandy KG: Delineation of the clotrimazole/TRAM-34 binding site on the intermediate conductance calcium-activated potassium channel, IKCa1. J Biol Chem. 2001 Aug 24;276(34):32040-5. Epub 2001 Jun 25. [PubMed Link Image]
  3. Ishii TM, Silvia C, Hirschberg B, Bond CT, Adelman JP, Maylie J: A human intermediate conductance calcium-activated potassium channel. Proc Natl Acad Sci U S A. 1997 Oct 14;94(21):11651-6. [PubMed Link Image]
  4. Joiner WJ, Wang LY, Tang MD, Kaczmarek LK: hSK4, a member of a novel subfamily of calcium-activated potassium channels. Proc Natl Acad Sci U S A. 1997 Sep 30;94(20):11013-8. [PubMed Link Image]
  5. Logsdon NJ, Kang J, Togo JA, Christian EP, Aiyar J: A novel gene, hKCa4, encodes the calcium-activated potassium channel in human T lymphocytes. J Biol Chem. 1997 Dec 26;272(52):32723-6. [PubMed Link Image]
  6. Ghanshani S, Coleman M, Gustavsson P, Wu AC, Gargus JJ, Gutman GA, Dahl N, Mohrenweiser H, Chandy KG: Human calcium-activated potassium channel gene KCNN4 maps to chromosome 19q13.2 in the region deleted in diamond-blackfan anemia. Genomics. 1998 Jul 1;51(1):160-1. [PubMed Link Image]
Target 2 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 482
Target 3 Name Glycine receptor subunit alpha-1
Target 3 Synonyms
  1. Glycine receptor 48 kDa subunit
  2. Glycine receptor strychnine-binding subunit
  3. Glycine receptor subunit alpha-1 precursor
Target 3 Gene Name GLRA1
Target 3 Protein Sequence >Glycine receptor subunit alpha-1 precursor
MYSFNTLRLYLWETIVFFSLAASKEAEAARSAPKPMSPSDFLDKLMGRTSGYDARIRPNF
KGPPVNVSCNIFINSFGSIAETTMDYRVNIFLRQQWNDPRLAYNEYPDDSLDLDPSMLDS
IWKPDLFFANEKGAHFHEITTDNKLLRISRNGNVLYSIRITLTLACPMDLKNFPMDVQTC
IMQLESFGYTMNDLIFEWQEQGAVQVADGLTLPQFILKEEKDLRYCTKHYNTGKFTCIEA
RFHLERQMGYYLIQMYIPSLLIVILSWISFWINMDAAPARVGLGITTVLTMTTQSSGSRA
SLPKVSYVKAIDIWMAVCLLFVFSALLEYAAVNFVSRQHKELLRFRRKRRHHKSPMLNLF
QEDEAGEGRFNFSAYGMGPACLQAKDGISVKGANNSNTTNPPPAPSKSPEEMRKLFIQRA
KKIDKISRIGFPMAFLIFNMFYWIIYKIVRREDVHNQ
Target 3 Number of Residues 464
Target 3 Molecular Weight 52625
Target 3 Theoretical pI 9.04
Target 3 GO Classification
Function
neurotransmitter receptor activity
anion channel activity
chloride channel activity
glycine-gated chloride channel activity
transporter activity
ion transporter activity
ion channel activity
ligand-gated ion channel activity
extracellular ligand-gated ion channel activity
signal transducer activity
receptor activity
transmembrane receptor activity
GABA receptor activity
GABA-A receptor activity
Process
anion transport
inorganic anion transport
chloride transport
physiological process
cellular physiological process
transport
ion transport
Component
postsynaptic membrane
cell
membrane
intrinsic to membrane
integral to membrane
Target 3 General Function Involved in GABA-A receptor activity
Target 3 Specific Function The glycine receptor is a neurotransmitter-gated ion channel. Binding of glycine to its receptor increases the chloride conductance and thus produces hyperpolarization (inhibition of neuronal firing)
Target 3 Pathways Not Available
Target 3 Reactions Not Available
Target 3 Pfam Domain Function
Target 3 Signals
  • 1-28
Target 3 Transmembrane Regions
  • 248-274
  • 281-298
  • 313-336
  • 429-446
Target 3 Essentiality Non-Essential
Target 3 GenBank ID Protein 31851 Link Image
Target 3 UniProtKB/Swiss-Prot ID P23415 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name GLRA1_HUMAN Link Image
Target 3 PDB ID Not Available
Target 3 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 3 Gene Sequence >1350 bp
ATGTACAGCTTCAATACTCTTCGACTCTACCTTTCGGGAGCCATTGTATTCTTCAGCCTT
GCTGCTTCTAAGGAGGCTGAAGCTGCTCGCTCCGCAACCAAGCCTATGTCACCCTCGGAT
TTCCTGGATAAGCTAATGGGGAGAACCTCCGGATATGATGCCAGGATCAGGCCCAATTTT
AAAGGTCCCCCAGTGAACGTGAGCTGCAACATTTTCATCAACAGCTTTGGTTCCATTGCT
GAGACAACCATGGACTATAGGGTCAACATCTTCCTGCGGCAGCAATGGAACGACCCCCGC
CTGGCCTATAATGAATACCCTGACGACTCTCTGGACCTGGACCCATCCATGCTGGACTCC
ATCTGGAAACCTGACCTGTTCTTTGCCAACGAGAAGGGGGCCCACTTCCATGAGATCACC
ACAGACAACAAATTGCTAAGGATCTCCCGGAATGGGAATGTCCTCTACAGCATCAGAATC
ACCCTGACACTGGCCTGCCCCATGGACTTGAAGAATTTCCCCATGGATGTCCAGACATGT
ATCATGCAACTGGAAAGCTTTGGATATACGATGAATGACCTCATCTTTGAGTGGCAGGAA
CAGGGAGCCGTGCAGGTAGCAGATGGACTAACTCTGCCCCAGTTTATCTTGAAGGAAGAG
AAGGACTTGAGATACTGCACCAAGCACTACAACACAGGTAAATTCACCTGCATTGAGGCC
CGGTTCCACCTGGAGCGGCAGATGGGTTACTACCTGATTCAGATGTATATTCCCAGCCTG
CTCATTGTCATCCTCTCATGGATCTCCTTCTGGATCAACATGGATGCTGCACCTGCTCGT
GTGGGCCTAGGCATCACCACTGTGCTCACCATGACCACCCAGAGCTCCGGCTCTCGAGCA
TCTCTGCCCAAGGTGTCCTATGTGAAAGCCATTGACATTTGGATGGCAGTTTGCCTGCTC
TTTGTGTTCTCAGCCCTATTAGAATATGCTGCCGTTAACTTTGTGTCTCGGCAACATAAG
GAGCTGCTCCGATTCAGGAGGAAGCGGAGACATCACAAGGAGGATGAAGCTGGAGAAGGC
CGCTTTAACTTCTCTGCCTATGGGATGGGCCCAGCCTGTCTACAGGCCAAGGATGGCATC
TCAGTCAAGGGCGCCAACAACAGTAACACCACCAACCCCCCTCCTGCACCATCTAAGTCC
CCAGAGGAGATGCGAAAACTCTTCATCCAGAGGGCCAAGAAGATCGACAAAATATCCCGC
ATTGGCTTCCCCATGGCCTTCCTCATTTTCAACATGTTCTACTGGATCATCTACAAGATT
GTCCGTAGAGAGGACGTCCACAACCAGTGA
Target 3 GenBank Gene ID
Target 3 GeneCard ID GLRA1 Link Image
Target 3 GenAtlas ID GLRA1 Link Image
Target 3 HGNC ID HGNC:4326 Link Image
Target 3 Chromosome Location 5
Target 3 Locus 5q32
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Vergouwe MN, Tijssen MA, Peters AC, Wielaard R, Frants RR: Hyperekplexia phenotype due to compound heterozygosity for GLRA1 gene mutations. Ann Neurol. 1999 Oct;46(4):634-8. [PubMed Link Image]
  2. Grenningloh G, Schmieden V, Schofield PR, Seeburg PH, Siddique T, Mohandas TK, Becker CM, Betz H: Alpha subunit variants of the human glycine receptor: primary structures, functional expression and chromosomal localization of the corresponding genes. EMBO J. 1990 Mar;9(3):771-6. [PubMed Link Image]
  3. Shiang R, Ryan SG, Zhu YZ, Fielder TJ, Allen RJ, Fryer A, Yamashita S, O'Connell P, Wasmuth JJ: Mutational analysis of familial and sporadic hyperekplexia. Ann Neurol. 1995 Jul;38(1):85-91. [PubMed Link Image]
  4. Rees MI, Andrew M, Jawad S, Owen MJ: Evidence for recessive as well as dominant forms of startle disease (hyperekplexia) caused by mutations in the alpha 1 subunit of the inhibitory glycine receptor. Hum Mol Genet. 1994 Dec;3(12):2175-9. [PubMed Link Image]
  5. Langosch D, Laube B, Rundstrom N, Schmieden V, Bormann J, Betz H: Decreased agonist affinity and chloride conductance of mutant glycine receptors associated with human hereditary hyperekplexia. EMBO J. 1994 Sep 15;13(18):4223-8. [PubMed Link Image]
  6. Schorderet DF, Pescia G, Bernasconi A, Regli F: An additional family with Startle disease and a G1192A mutation at the alpha 1 subunit of the inhibitory glycine receptor gene. Hum Mol Genet. 1994 Jul;3(7):1201. [PubMed Link Image]
  7. Shiang R, Ryan SG, Zhu YZ, Hahn AF, O'Connell P, Wasmuth JJ: Mutations in the alpha 1 subunit of the inhibitory glycine receptor cause the dominant neurologic disorder, hyperekplexia. Nat Genet. 1993 Dec;5(4):351-8. [PubMed Link Image]
  8. Milani N, Dalpra L, del Prete A, Zanini R, Larizza L: A novel mutation (Gln266-->His) in the alpha 1 subunit of the inhibitory glycine-receptor gene (GLRA1) in hereditary hyperekplexia. Am J Hum Genet. 1996 Feb;58(2):420-2. [PubMed Link Image]
  9. Elmslie FV, Hutchings SM, Spencer V, Curtis A, Covanis T, Gardiner RM, Rees M: Analysis of GLRA1 in hereditary and sporadic hyperekplexia: a novel mutation in a family cosegregating for hyperekplexia and spastic paraparesis. J Med Genet. 1996 May;33(5):435-6. [PubMed Link Image]
  10. Seri M, Bolino A, Galietta LJ, Lerone M, Silengo M, Romeo G: Startle disease in an Italian family by mutation (K276E): The alpha-subunit of the inhibiting glycine receptor. Hum Mutat. 1997;9(2):185-7. [PubMed Link Image]
  11. 9920650 Saul B, Kuner T, Sobetzko D, Brune W, Hanefeld F, Meinck HM, Becker CM: Novel GLRA1 missense mutation (P250T) in dominant hyperekplexia defines an intracellular determinant of glycine receptor channel gating. J Neurosci. 1999 Feb 1;19(3):869-77.
Target 3 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 4 [top]
Target 4 ID 536
Target 4 Name Potassium large conductance calcium-activated channel, subfamily M, alpha member 1
Target 4 Synonyms Not Available
Target 4 Gene Name KCNMA1
Target 4 Protein Sequence >Potassium large conductance calcium-activated channel, subfamily M, alpha member 1
MANGGGGGGGSSGGGGGGGGSSLRMSSNIHANHLSLDASSSSSSSSSSSSSSSSSSSSSS
VHEPKMDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCH
CGGKTKEAQKINNGSSQADGTLKPVDEKEEAVAAEVGWMTSVKDWAGVMISAQTLTGRVL
VVLVFALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDKL
WFWLEVNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKL
VNLLSIFISTWLTAAGFIHLVENSGDPWENFQNNQALTYWECVYLLMVTMSTVGYGDVYA
KTTLGRLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVSGRKHIVVCGHITLES
VSNFLKDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARVK
IESADACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPSW
NWKEGDDAICLAELKLGFIAQSCLAQGLSTMLANLFSMRSFIKIEEDTWQKYYLEGVSNE
MYTEYLSSAFVGLSFPTVCELCFVKLKLLMIAIEYKSANRESRILINPGNHLKIQEGTLG
FFIASDAKEVKRAFFYCKACHDDITDPKRIKKCGCKRLEDEQPSTLSPKKKQRNGGMRNS
PNTSPKLMRHDPLLIPGNDQIDNMDSNVKKYDSTGMFHWCAPKEIEKVILTRSEAAMTVL
SGHVVVCIFGDVSSALIGLRNLVMPLRASNFHYHELKHIVFVGSIEYLKREWETLHNFPK
VSILPGTPLSRADLRAVNINLCDMCVILSANQNNIDDTSLQDKECILASLNIKSMQFDDS
IGVLQANSQGFTPPGMDRSSPDNSPVHGMLRQPSITTGVNIPIITELVNDTNVQFLDQDD
DDDPDTELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIRTLVTGGATPELEALIAE
ENALRGGYSTPQTLANRDRCRVAQLALLDGPFADLGDGGCYGDLFCKALKTYNMLCFGIY
RLRDAHLSTPSQCTKRYVITNPPYEFELVPTDLIFCLMQFDHNAGQSRASLSHSSHSSQS
SSKKSSSVHSIPSTANRQNRPKSRESRDKQKKEMVYR
Target 4 Number of Residues 1196
Target 4 Molecular Weight 130889
Target 4 Theoretical pI 6.88
Target 4 GO Classification
Function
catalytic activity
transferase activity
transferase activity, transferring one-carbon groups
methyltransferase activity
N-methyltransferase activity
binding
nucleic acid binding
DNA binding
voltage-gated ion channel activity
voltage-gated potassium channel activity
transporter activity
ion transporter activity
ion channel activity
cation channel activity
potassium channel activity
calcium-activated potassium channel activity
Process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
DNA metabolism
DNA modification
DNA alkylation
DNA methylation
physiological process
cellular physiological process
transport
ion transport
cation transport
monovalent inorganic cation transport
potassium ion transport
Component
protein complex
voltage-gated potassium channel complex
cell
membrane
Target 4 General Function Inorganic ion transport and metabolism
Target 4 Specific Function Not Available
Target 4 Pathways Not Available
Target 4 Reactions Not Available
Target 4 Pfam Domain Function
Target 4 Signals
  • None
Target 4 Transmembrane Regions
  • 86-108; 179-198; 213-235; 300-322; 337-356; 363-385
Target 4 Essentiality Non-Essential
Target 4 GenBank ID Protein 55962729 Link Image
Target 4 UniProtKB/Swiss-Prot ID Q5SQR9 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name Q5SQR9_HUMAN Link Image
Target 4 PDB ID Not Available
Target 4 Cellular Location
  • Cytoplasmic
Target 4 Gene Sequence >378 bp
ATGGCAAATGGTGGCGGCGGCGGCGGCGGCAGCAGCGGCGGCGGCGGCGGCGGCGGAGGC
AGCAGTCTTAGAATGAGTAGCAATATCCACGCGAACCATCTCAGCCTAGACGCGTCCTCC
TCCTCCTCCTCCTCCTCTTCCTCTTCTTCTTCTTCCTCCTCCTCTTCCTCCTCGTCCTCG
GTCCACGAGCCCAAGATGGATGCGCTCATCATCCCGGTGACCATGGAGGTGCCGTGCGAC
AGCCGGGGCCAACGCATGTGGTGGGCTTTCCTGGCCTCCTCCATGGTGACTTTCTTCGGG
GGCCTCTTCATCATCTTGCTCTGGCGGACGCTCAAGTACCTGTGGACCGTGTGCTGCCAC
TGCGGGGGCAAGACGAAG
Target 4 GenBank Gene ID
Target 4 GeneCard ID KCNMA1 Link Image
Target 4 GenAtlas ID KCNMA1 Link Image
Target 4 HGNC ID HGNC:6284 Link Image
Target 4 Chromosome Location 10
Target 4 Locus 10q22.3
Target 4 SNPs SNPJam Report Link Image
Target 4 General References Not Available
Target 4 Drug References
  1. Namba T, Ishii TM, Ikeda M, Hisano T, Itoh T, Hirota K, Adelman JP, Fukuda K: Inhibition of the human intermediate conductance Ca(2+)-activated K(+) channel, hIK1, by volatile anesthetics. Eur J Pharmacol. 2000 Apr 28;395(2):95-101. [PubMed Link Image]
Drug Target 5 [top]
Target 5 ID 537
Target 5 Name ATP synthase delta chain, mitochondrial
Target 5 Synonyms
  1. ATP synthase delta chain, mitochondrial precursor
  2. EC 3.6.3.14
Target 5 Gene Name ATP5D
Target 5 Protein Sequence >ATP synthase delta chain, mitochondrial precursor
MLPAALLRRPGLGRLVRHARAYAEAAAAPAAASGPNQMSFTFASPTQVFFNGANVRQVDV
PTLTGAFGILAAHVPTLQVLRPGLVVVHAEDGTTSKYFVSSGSIAVNADSSVQLLAEEAV
TLDMLDLGAAKANLEKAQAELVGTADEATRAEIQIRIEANEALVKALE
Target 5 Number of Residues 170
Target 5 Molecular Weight 17490
Target 5 Theoretical pI 5.19
Target 5 GO Classification
Function
hydrogen-transporting ATPase activity, rotational mechanism
transporter activity
ion transporter activity
cation transporter activity
monovalent inorganic cation transporter activity
hydrogen ion transporter activity
hydrogen-transporting ATP synthase activity, rotational mechanism
Process
physiological process
metabolism
cellular metabolism
cofactor metabolism
coenzyme metabolism
group transfer coenzyme metabolism
nucleoside phosphate metabolism
ATP biosynthesis
ATP synthesis coupled proton transport
Component
cell
membrane
intrinsic to membrane
integral to membrane
proton-transporting two-sector ATPase complex
Target 5 General Function Energy production and conversion
Target 5 Specific Function Produces ATP from ADP in the presence of a proton gradient across the membrane
Target 5 Pathways
Name SMPDB Link KEGG Link
ATP synthesis map00193 Link Image
Flagellar assembly map02040 Link Image
Oxidative phosphorylation map00190 Link Image
Photosynthesis map00195 Link Image
Type III secretion system map03070 Link Image
Target 5 Reactions
  • ATP + H2O + H+in = ADP + phosphate + H+out
Target 5 Pfam Domain Function
Target 5 Signals
  • None
Target 5 Transmembrane Regions
  • None
Target 5 Essentiality Non-Essential
Target 5 GenBank ID Protein 12586 Link Image
Target 5 UniProtKB/Swiss-Prot ID P30049 Link Image
Target 5 UniProtKB/Swiss-Prot Entry Name ATPD_HUMAN Link Image
Target 5 PDB ID 1E79 Link Image
Target 5 PDB File Show
Target 5 3D Structure
Target 5 Cellular Location
  • Mitochondrion
Target 5 Gene Sequence >507 bp
ATGCTGCCCGCCGCGCTGCTCCGCCGCCCGGGACTTGGCCGCCTCGTCCGCCACGCCCGT
GCCTATGCCGAGGCCGCCGCCGCCCCGGCTGCCGCCTCTGGCCCCAACCAGATGTCCTTC
ACCTTCGCCTCTCCCACGCAGGTGTTCTTCAACGGTGCCAACGTCCGGCAGGTGGACGTG
CCCACGCTGACCGGAGCCTTCGGCATCCTGGCGGCCCACGTGCCCACGCTGCAGGTCCTG
CGGCCGGGGCTGGTCGTGGTGCATGCAGAGGACGGCACCACCTCCAAATACTTTGTGAGC
AGCGGTTCCATCGCAGTGAACGCCGACTCTTCGGTGCAGTTGTTGGCCGAAGAGGCCGTG
ACGCTGGACATGTTGGACCTGGGGGCAGCCAAGGCAAACTTGGAGAAGGCCCAGGCGGAG
CTGGTGGGGACAGCTGACGAGGCCACGCGGGCAGAGATCCAGATCCGAATCGAGGCCAAC
GAGGCCCTGGTGAAGGCCCTGGAGTAG
Target 5 GenBank Gene ID
Target 5 GeneCard ID ATP5D Link Image
Target 5 GenAtlas ID ATP5D Link Image
Target 5 HGNC ID HGNC:837 Link Image
Target 5 Chromosome Location 19
Target 5 Locus 19p13.3
Target 5 SNPs SNPJam Report Link Image
Target 5 General References
  1. Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [PubMed Link Image]
  2. Jordan EM, Breen GA: Molecular cloning of an import precursor of the delta-subunit of the human mitochondrial ATP synthase complex. Biochim Biophys Acta. 1992 Feb 28;1130(1):123-6. [PubMed Link Image]
Target 5 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 6 [top]
Target 6 ID 559
Target 6 Name NADH-ubiquinone oxidoreductase chain 1
Target 6 Synonyms
  1. EC 1.6.5.3
  2. NADH dehydrogenase subunit 1
Target 6 Gene Name MT-ND1
Target 6 Protein Sequence >NADH-ubiquinone oxidoreductase chain 1
MPMANLLLLIVPILIAMAFLMLTERKILGYMQLRKGPNVVGPYGLLQPFADAMKLFTKEP
LKPATSTITLYITAPTLALTIALLLWTPLPMPNPLVNLNLGLLFILATSSLAVYSILWSG
WASNSNYALIGALRAVAQTISYEVTLAIILLSTLLMSGSFNLSTLITTQEHLWLLLPSWP
LAMMWFISTLAETNRTPFDLAEGESELVSGFNIEYAAGPFALFFMAEYTNIIMMNTLTTT
IFLGTTYDALSPELYTTYFVTKTLLLTSLFLWIRTAYPRFRYDQLMHLLWKNFLPLTLAL
LMWYVSMPITISSIPPQT
Target 6 Number of Residues 323
Target 6 Molecular Weight 35661
Target 6 Theoretical pI 6.53
Target 6 GO Classification
Function
Not Available
Process
metabolism
cellular metabolism
generation of precursor metabolites and energy
electron transport
physiological process
cellular physiological process
transport
Component
cell
membrane
Target 6 General Function Energy production and conversion
Target 6 Specific Function Not Available
Target 6 Pathways
Name SMPDB Link KEGG Link
Oxidative phosphorylation map00190 Link Image
Ubiquinone biosynthesis SMP00065 Link Image map00130 Link Image
Target 6 Reactions
  • NADH + H+ + ubiquinone = NAD+ + ubiquinol
Target 6 Pfam Domain Function
Target 6 Signals
  • None
Target 6 Transmembrane Regions
  • 4-23; 68-90; 100-122; 135-157; 172-191; 222-244; 254-273; 293-315
Target 6 Essentiality Non-Essential
Target 6 GenBank ID Protein 13004 Link Image
Target 6 UniProtKB/Swiss-Prot ID P03886 Link Image
Target 6 UniProtKB/Swiss-Prot Entry Name NU1M_HUMAN Link Image
Target 6 PDB ID Not Available
Target 6 Cellular Location
  • Mitochondrion
  • mitochondrial inner membrane
  • multi-pass membrane protein (Probable)
Target 6 Gene Sequence >957 bp
ATACCCATGGCCAACCTCCTACTCCTCATTGTACCCATTCTAATCGCAATGGCATTCCTA
ATGCTTACCGAACGAAAAATTCTAGGCTATATACAACTACGCAAAGGCCCCAACGTGGTA
GGCCCCTACGGGCTACTACAACCCTTCGCTGACGCCATAAAACTCTTCACCAAAGAGCCC
CTAAAACCCGCCACATCTACCATCACCCTCTACATCACCGCCCCGACCTTAGCTCTCACC
ATCGCTCTTCTACTATGAACCCCCCTCCCCATACCCAACCCCCTGGTCAACCTCAACCTA
GGCCTCCTATTTATTCTAGCCACCTCTAGCCTAGCCGTTTACTCAATCCTCTGATCAGGG
TGAGCATCAAACTCAAACTACGCCCTGATCGGCGCACTGCGAGCAGTAGCCCAAACAATC
TCATATGAAGTCACCCTAGCCATCATTCTACTATCAACATTACTAATAAGTGGCTCCTTT
AACCTCTCCACCCTTATCACAACACAAGAACACCTCTGATTACTCCTGCCATCATGACCC
TTGGCCATAATATGATTTATCTCCACACTAGCAGAGACCAACCGAACCCCCTTCGACCTT
GCCGAAGGGGAGTCCGAACTAGTCTCAGGCTTCAACATCGAATACGCCGCAGGCCCCTTC
GCCCTATTCTTCATAGCCGAATACACAAACATTATTATAATAAACACCCTCACCACTACA
ATCTTCCTAGGAACAACATATGACGCACTCTCCCCTGAACTCTACACAACATATTTTGTC
ACCAAGACCCTACTTCTAACCTCCCTGTTCTTATGAATTCGAACAGCATACCCCCGATTC
CGCTACGACCAACTCATACACCTCCTATGAAAAAACTTCCTACCACTCACCCTAGCATTA
CTTATATGATATGTCTCCATACCCATTACAATCTCCAGCATTCCCCCTCAAACCTAA
Target 6 GenBank Gene ID
Target 6 GeneCard ID MT-ND1 Link Image
Target 6 GenAtlas ID MT-ND1 Link Image
Target 6 HGNC ID HGNC:7455 Link Image
Target 6 Chromosome Location MT
Target 6 Locus -
Target 6 SNPs SNPJam Report Link Image
Target 6 General References
  1. Ingman M, Kaessmann H, Paabo S, Gyllensten U: Mitochondrial genome variation and the origin of modern humans. Nature. 2000 Dec 7;408(6813):708-13. [PubMed Link Image]
  2. Ingman M, Gyllensten U: Mitochondrial genome variation and evolutionary history of Australian and New Guinean aborigines. Genome Res. 2003 Jul;13(7):1600-6. [PubMed Link Image]
  3. Johns DR, Neufeld MJ, Park RD: An ND-6 mitochondrial DNA mutation associated with Leber hereditary optic neuropathy. Biochem Biophys Res Commun. 1992 Sep 30;187(3):1551-7. [PubMed Link Image]
  4. Huoponen K, Vilkki J, Aula P, Nikoskelainen EK, Savontaus ML: A new mtDNA mutation associated with Leber hereditary optic neuroretinopathy. Am J Hum Genet. 1991 Jun;48(6):1147-53. [PubMed Link Image]
  5. Marzuki S, Noer AS, Lertrit P, Thyagarajan D, Kapsa R, Utthanaphol P, Byrne E: Normal variants of human mitochondrial DNA and translation products: the building of a reference data base. Hum Genet. 1991 Dec;88(2):139-45. [PubMed Link Image]
  6. Johns DR, Berman J: Alternative, simultaneous complex I mitochondrial DNA mutations in Leber's hereditary optic neuropathy. Biochem Biophys Res Commun. 1991 Feb 14;174(3):1324-30. [PubMed Link Image]
  7. Howell N, Bindoff LA, McCullough DA, Kubacka I, Poulton J, Mackey D, Taylor L, Turnbull DM: Leber hereditary optic neuropathy: identification of the same mitochondrial ND1 mutation in six pedigrees. Am J Hum Genet. 1991 Nov;49(5):939-50. [PubMed Link Image]
  8. Majander A, Huoponen K, Savontaus ML, Nikoskelainen E, Wikstrom M: Electron transfer properties of NADH:ubiquinone reductase in the ND1/3460 and the ND4/11778 mutations of the Leber hereditary optic neuroretinopathy (LHON). FEBS Lett. 1991 Nov 4;292(1-2):289-92. [PubMed Link Image]
  9. Howell N, Kubacka I, Xu M, McCullough DA: Leber hereditary optic neuropathy: involvement of the mitochondrial ND1 gene and evidence for an intragenic suppressor mutation. Am J Hum Genet. 1991 May;48(5):935-42. [PubMed Link Image]
  10. Chomyn A, Mariottini P, Cleeter MW, Ragan CI, Matsuno-Yagi A, Hatefi Y, Doolittle RF, Attardi G: Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase. Nature. 1985 Apr 18-24;314(6012):592-7. [PubMed Link Image]
  11. 6260957 Sanger F, Coulson AR, Barrell BG, Smith AJ, Roe BA: Cloning in single-stranded bacteriophage as an aid to rapid DNA sequencing. J Mol Biol. 1980 Oct 25;143(2):161-78.
  12. 7219534 Anderson S, Bankier AT, Barrell BG, de Bruijn MH, Coulson AR, Drouin J, Eperon IC, Nierlich DP, Roe BA, Sanger F, Schreier PH, Smith AJ, Staden R, Young IG: Sequence and organization of the human mitochondrial genome. Nature. 1981 Apr 9;290(5806):457-65.
  13. 7530363 Horai S, Hayasaka K, Kondo R, Tsugane K, Takahata N: Recent African origin of modern humans revealed by complete sequences of hominoid mitochondrial DNAs. Proc Natl Acad Sci U S A. 1995 Jan 17;92(2):532-6.
  14. 7733935 Nakagawa Y, Ikegami H, Yamato E, Takekawa K, Fujisawa T, Hamada Y, Ueda H, Uchigata Y, Miki T, Kumahara Y, et al.: A new mitochondrial DNA mutation associated with non-insulin-dependent diabetes mellitus. Biochem Biophys Res Commun. 1995 Apr 17;209(2):664-8.
  15. 8104867 Shoffner JM, Brown MD, Torroni A, Lott MT, Cabell MF, Mirra SS, Beal MF, Yang CC, Gearing M, Salvo R, et al.: Mitochondrial DNA variants observed in Alzheimer disease and Parkinson disease patients. Genomics. 1993 Jul;17(1):171-84.
  16. 8723687 Jaksch M, Hofmann S, Kaufhold P, Obermaier-Kusser B, Zierz S, Gerbitz KD: A novel combination of mitochondrial tRNA and ND1 gene mutations in a syndrome with MELAS, cardiomyopathy, and diabetes mellitus. Hum Mutat. 1996;7(4):358-60.
Target 6 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 7 [top]
Target 7 ID 587
Target 7 Name Serum albumin
Target 7 Synonyms
  1. Serum albumin precursor
Target 7 Gene Name ALB
Target 7 Protein Sequence >Serum albumin precursor
MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPF
EDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEP
ERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLF
FAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAV
ARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLK
ECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYAR
RHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFE
QLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVV
LNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTL
SEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLV
AASQAALGL
Target 7 Number of Residues 619
Target 7 Molecular Weight 69367
Target 7 Theoretical pI 6.21
Target 7 GO Classification
Function
transporter activity
carrier activity
Process
physiological process
cellular physiological process
transport
Component
extracellular region
extracellular space
Target 7 General Function Involved in antioxidant activity
Target 7 Specific Function Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood
Target 7 Pathways Not Available
Target 7 Reactions Not Available
Target 7 Pfam Domain Function
Target 7 Signals
  • 1-18
Target 7 Transmembrane Regions
  • None
Target 7 Essentiality Non-Essential
Target 7 GenBank ID Protein 28590 Link Image
Target 7 UniProtKB/Swiss-Prot ID P02768 Link Image
Target 7 UniProtKB/Swiss-Prot Entry Name ALBU_HUMAN Link Image
Target 7 PDB ID 1HA2 Link Image
Target 7 PDB File Show
Target 7 3D Structure
Target 7 Cellular Location
  • Secreted protein
Target 7 Gene Sequence >1830 bp
ATGAAGTGGGTAACCTTTATTTCCCTTCTTTTTCTCTTTAGCTCGGCTTATTCCAGGGGT
GTGTTTCGTCGAGATGCACACAAGAGTGAGGTTGCTCATCGGTTTAAAGATTTGGGAGAA
GAAAATTTCAAAGCCTTGGTGTTGATTGCCTTTGCTCAGTATCTTCAGCAGTGTCCATTT
GAAGATCATGTAAAATTAGTGAATGAAGTAACTGAATTTGCAAAAACATGTGTTGCTGAT
GAGTCAGCTGAAAATTGTGACAAATCACTTCATACCCTTTTTGGAGACAAATTATGCACA
GTTGCAACTCTTCGTGAAACCTATGGTGAAATGGCTGACTGCTGTGCAAAACAAGAACCT
GGGAGAAATGAATGCTTCTTGCAACACAAAGATGACAACCCAAACCTCCCCCGATTGGTG
AGACCAGAGGTTGATGTGATGTGCACTGCTTTTCATGACAATGAAGAGACATTTTTGAAA
AAATACTTATATGAAATTGCCAGAAGACATCCTTACTTTTATGCCCCGGAACTCCTTTTC
TTTGCTAAAAGGTATAAAGCTGCTTTTACAGAATGTTGCCAAGCTGCTGATAAAGCTGCC
TGCCTGTTGCCAAAGCTCGATGAACTTCGGGATGAAGGGAAGGCTTCGTCTGCCAAACAG
AGACTCAAGTGTGCCAGTCTCCAAAAATTTGGAGAAAGAGCTTTCAAAGCATGGGCAGTA
GCTCGCCTGAGCCAGAGATTTCCCAAAGCTGAGTTTGCAGAAGTTTCCAAGTTAGTGACA
GATCTTACCAAAGTCCACACGGAATGCTGCCATGGAGATCTGCTTGAATGTGCTGATGAC
AGGGCGGACCTTGCCAAGTATATCTGTGAAAATCAAGATTCGATCTCCAGTAAACTGAAG
GAATGCTGTGAAAAACCTCTGTTGGAAAAATCCCACTGCATTGCCGAAGTGGAAAATGAT
GAGATGCCTGCTGACTTGCCTTCATTAGCTGCTGATTTTGTTGAAAGTAAGGATGTTTGC
AAAAACTATGCTGAGGCAAAGGATGTCTTCTTGGGCATGTTTTTGTATGAATATGCAAGA
AGGCATCCTGATTACTCTGTCGTGCTGCTGCTGAGACTTGCCAAGACATATGAAACCACT
CTAGAGAAGTGCTGTGCCGCTGCAGATCCTCATGAATGCTATGCCAAAGTGTTCGATGAA
TTTAAACCTCTTGTGGAAGAGCCTCAGAATTTAATCAAACAAAATTGTGAGCTTTTTGAG
CAGCTTGGAGAGTACAAATTCCAGAATGCGCTGTTAGTTCGTTACACCAAGAAAGTACCC
GAAGTGTCAACTCCAACTCTTGTAGAGGTCTCAAGAAACCTAGGAAAAGTGGGCAGCAAA
TGTTGTAAACATCCTGAAGCAAAAAGAATGCCCTGTGCAGAAGACTATCTATCCGTGGTC
CTGAACCAGTTATGTGTGTTGCATGAGAAAACGCCAGTAAGTGACAGAGTCACCAAATGC
TGCACAGAATCCTTGGTGAACAGGCGACCATGCTTTTCAGCTCTGGAAGTCGATGAAACA
TACGTTCCCAAAGAGTTTAATGCTGAAACATTCACCTTCCATGCAGATATATGCACACTT
TCTGAGAAGGAGAGACAAATCAAGAAACAAACTGCACTTGTTGAGCTCGTGAAACACAAG
CCCAAGGCAACAAAAGAGCAACTGAAAGCTGTTATGGATGATTTCGCTGCTTTTGTAGAG
AAGTGCTGCAAGGCTGACGATAAGGAGACCTGCTTTGCCGAGGAGGGTAAAAAACTTGTT
GCTGCAAGTCAAGCTGCCTTAGGCTTATAA
Target 7 GenBank Gene ID
Target 7 GeneCard ID ALB Link Image
Target 7 GenAtlas ID ALB Link Image
Target 7 HGNC ID HGNC:399 Link Image
Target 7 Chromosome Location 4
Target 7 Locus 4q11-q13
Target 7 SNPs SNPJam Report Link Image
Target 7 General References
  1. Sugio S, Kashima A, Mochizuki S, Noda M, Kobayashi K: Crystal structure of human serum albumin at 2.5 A resolution. Protein Eng. 1999 Jun;12(6):439-46. [PubMed Link Image]
  2. Bhattacharya AA, Curry S, Franks NP: Binding of the general anesthetics propofol and halothane to human serum albumin. High resolution crystal structures. J Biol Chem. 2000 Dec 8;275(49):38731-8. [PubMed Link Image]
  3. Minchiotti L, Campagnoli M, Rossi A, Cosulich ME, Monti M, Pucci P, Kragh-Hansen U, Granel B, Disdier P, Weiller PJ, Galliano M: A nucleotide insertion and frameshift cause albumin Kenitra, an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges. Eur J Biochem. 2001 Jan;268(2):344-52. [PubMed Link Image]
  4. Yu Y, Zhang C, Zhou G, Wu S, Qu X, Wei H, Xing G, Dong C, Zhai Y, Wan J, Ouyang S, Li L, Zhang S, Zhou K, Zhang Y, Wu C, He F: Gene expression profiling in human fetal liver and identification of tissue- and developmental-stage-specific genes through compiled expression profiles and efficient cloning of full-length cDNAs. Genome Res. 2001 Aug;11(8):1392-403. [PubMed Link Image]
  5. Spahr CS, Davis MT, McGinley MD, Robinson JH, Bures EJ, Beierle J, Mort J, Courchesne PL, Chen K, Wahl RC, Yu W, Luethy R, Patterson SD: Towards defining the urinary proteome using liquid chromatography-tandem mass spectrometry. I. Profiling an unfractionated tryptic digest. Proteomics. 2001 Jan;1(1):93-107. [PubMed Link Image]
  6. Petitpas I, Grune T, Bhattacharya AA, Curry S: Crystal structures of human serum albumin complexed with monounsaturated and polyunsaturated fatty acids. J Mol Biol. 2001 Dec 14;314(5):955-60. [PubMed Link Image]
  7. Meloun B, Moravek L, Kostka V: Complete amino acid sequence of human serum albumin. FEBS Lett. 1975 Oct 15;58(1):134-7. [PubMed Link Image]
  8. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  9. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  10. Minchiotti L, Galliano M, Stoppini M, Ferri G, Crespeau H, Rochu D, Porta F: Two alloalbumins with identical electrophoretic mobility are produced by differently charged amino acid substitutions. Biochim Biophys Acta. 1992 Mar 12;1119(3):232-8. [PubMed Link Image]
  11. 1518850 Carlson J, Sakamoto Y, Laurell CB, Madison J, Watkins S, Putnam FW: Alloalbuminemia in Sweden: structural study and phenotypic distribution of nine albumin variants. Proc Natl Acad Sci U S A. 1992 Sep 1;89(17):8225-9.
  12. 1630489 He XM, Carter DC: Atomic structure and chemistry of human serum albumin. Nature. 1992 Jul 16;358(6383):209-15.
  13. 1859851 Peach RJ, Brennan SO: Structural characterization of a glycoprotein variant of human serum albumin: albumin Casebrook (494 Asp----Asn). Biochim Biophys Acta. 1991 Jul 26;1097(1):49-54.
  14. 1946412 Madison J, Arai K, Sakamoto Y, Feld RD, Kyle RA, Watkins S, Davis E, Matsuda Y, Amaki I, Putnam FW: Genetic variants of serum albumin in Americans and Japanese. Proc Natl Acad Sci U S A. 1991 Nov 1;88(21):9853-7.
  15. 2068071 Watkins S, Madison J, Davis E, Sakamoto Y, Galliano M, Minchiotti L, Putnam FW: A donor splice mutation and a single-base deletion produce two carboxyl-terminal variants of human serum albumin. Proc Natl Acad Sci U S A. 1991 Jul 15;88(14):5959-63.
  16. 2104980 Brennan SO, Myles T, Peach RJ, Donaldson D, George PM: Albumin Redhill (-1 Arg, 320 Ala----Thr): a glycoprotein variant of human serum albumin whose precursor has an aberrant signal peptidase cleavage site. Proc Natl Acad Sci U S A. 1990 Jan;87(1):26-30.
  17. 2247440 Galliano M, Minchiotti L, Porta F, Rossi A, Ferri G, Madison J, Watkins S, Putnam FW: Mutations in genetic variants of human serum albumin found in Italy. Proc Natl Acad Sci U S A. 1990 Nov;87(22):8721-5.
  18. 2374930 Carter DC, He XM: Structure of human serum albumin. Science. 1990 Jul 20;249(4966):302-3.
  19. 2404284 Arai K, Madison J, Shimizu A, Putnam FW: Point substitutions in albumin genetic variants from Asia. Proc Natl Acad Sci U S A. 1990 Jan;87(1):497-501.
  20. 2419329 Urano Y, Watanabe K, Sakai M, Tamaoki T: The human albumin gene. Characterization of the 5' and 3' flanking regions and the polymorphic gene transcripts. J Biol Chem. 1986 Mar 5;261(7):3244-51.
  21. 2437111 Carraway RE, Mitra SP, Cochrane DE: Structure of a biologically active neurotensin-related peptide obtained from pepsin-treated albumin(s). J Biol Chem. 1987 May 5;262(13):5968-73.
  22. 2727704 Carter DC, He XM, Munson SH, Twigg PD, Gernert KM, Broom MB, Miller TY: Three-dimensional structure of human serum albumin. Science. 1989 Jun 9;244(4909):1195-8.
  23. 2762316 Arai K, Madison J, Huss K, Ishioka N, Satoh C, Fujita M, Neel JV, Sakurabayashi I, Putnam FW: Point substitutions in Japanese alloalbumins. Proc Natl Acad Sci U S A. 1989 Aug;86(16):6092-6.
  24. 2911589 Arai K, Ishioka N, Huss K, Madison J, Putnam FW: Identical structural changes in inherited albumin variants from different populations. Proc Natl Acad Sci U S A. 1989 Jan;86(2):434-8.
  25. 3009475 Minghetti PP, Ruffner DE, Kuang WJ, Dennison OE, Hawkins JW, Beattie WG, Dugaiczyk A: Molecular structure of the human albumin gene is revealed by nucleotide sequence within q11-22 of chromosome 4. J Biol Chem. 1986 May 25;261(15):6747-57.
  26. 3087352 Mogard MH, Kobayashi R, Chen CF, Lee TD, Reeve JR Jr, Shively JE, Walsh JH: The amino acid sequence of kinetensin, a novel peptide isolated from pepsin-treated human plasma: homology with human serum albumin, neurotensin and angiotensin. Biochem Biophys Res Commun. 1986 May 14;136(3):983-8.
  27. 3474609 Takahashi N, Takahashi Y, Blumberg BS, Putnam FW: Amino acid substitutions in genetic variants of human serum albumin and in sequences inferred from molecular cloning. Proc Natl Acad Sci U S A. 1987 Jul;84(13):4413-7.
  28. 3479777 Takahashi N, Takahashi Y, Isobe T, Putnam FW, Fujita M, Satoh C, Neel JV: Amino acid substitutions in inherited albumin variants from Amerindian and Japanese populations. Proc Natl Acad Sci U S A. 1987 Nov;84(22):8001-5.
  29. 3828358 Brennan SO, Herbert P: Albumin Canterbury (313 Lys----Asn). A point mutation in the second domain of serum albumin. Biochim Biophys Acta. 1987 Apr 8;912(2):191-7.
  30. 6171778 Lawn RM, Adelman J, Bock SC, Franke AE, Houck CM, Najarian RC, Seeburg PH, Wion KL: The sequence of human serum albumin cDNA and its expression in E. coli. Nucleic Acids Res. 1981 Nov 25;9(22):6103-114.
  31. 6275391 Dugaiczyk A, Law SW, Dennison OE: Nucleotide sequence and the encoded amino acids of human serum albumin mRNA. Proc Natl Acad Sci U S A. 1982 Jan;79(1):71-5.
  32. 656055 Jacobsen C: Lysine residue 240 of human serum albumin is involved in high-affinity binding of bilirubin. Biochem J. 1978 May 1;171(2):453-9.
  33. 7852505 Rushbrook JI, Becker E, Schussler GC, Divino CM: Identification of a human serum albumin species associated with familial dysalbuminemic hyperthyroxinemia. J Clin Endocrinol Metab. 1995 Feb;80(2):461-7.
  34. 7895732 Corbett JM, Wheeler CH, Baker CS, Yacoub MH, Dunn MJ: The human myocardial two-dimensional gel protein database: update 1994. Electrophoresis. 1994 Nov;15(11):1459-65.
  35. 7902134 Galliano M, Minchiotti L, Iadarola P, Stoppini M, Giagnoni P, Watkins S, Madison J, Putnam FW: Protein and DNA sequence analysis of a 'private' genetic variant: albumin Ortonovo (Glu-505-->Lys). Biochim Biophys Acta. 1993 Nov 25;1225(1):27-32.
  36. 8022807 Madison J, Galliano M, Watkins S, Minchiotti L, Porta F, Rossi A, Putnam FW: Genetic variants of human serum albumin in Italy: point mutants and a carboxyl-terminal variant. Proc Natl Acad Sci U S A. 1994 Jul 5;91(14):6476-80.
  37. 8048949 Sunthornthepvarakul T, Angkeow P, Weiss RE, Hayashi Y, Refetoff S: An identical missense mutation in the albumin gene results in familial dysalbuminemic hyperthyroxinemia in 8 unrelated families. Biochem Biophys Res Commun. 1994 Jul 29;202(2):781-7.
  38. 8347685 Brennan SO, Fellowes AP: Albumin Hawkes Bay; a low level variant caused by loss of a sulphydryl group at position 177. Biochim Biophys Acta. 1993 Aug 4;1182(1):46-50.
  39. 8513793 Minchiotti L, Galliano M, Zapponi MC, Tenni R: The structural characterization and bilirubin-binding properties of albumin Herborn, a [Lys240-->Glu] albumin mutant. Eur J Biochem. 1993 Jun 1;214(2):437-44.
  40. 9329347 Wada N, Chiba H, Shimizu C, Kijima H, Kubo M, Koike T: A novel missense mutation in codon 218 of the albumin gene in a distinct phenotype of familial dysalbuminemic hyperthyroxinemia in a Japanese kindred. J Clin Endocrinol Metab. 1997 Oct;82(10):3246-50.
  41. 955075 Walker JE: Lysine residue 199 of human serum albumin is modified by acetylsalicyclic acid. FEBS Lett. 1976 Jul 15;66(2):173-5.
  42. 9589637 Sunthornthepvarakul T, Likitmaskul S, Ngowngarmratana S, Angsusingha K, Kitvitayasak S, Scherberg NH, Refetoff S: Familial dysalbuminemic hypertriiodothyroninemia: a new, dominantly inherited albumin defect. J Clin Endocrinol Metab. 1998 May;83(5):1448-54.
  43. 9731778 Curry S, Mandelkow H, Brick P, Franks N: Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites. Nat Struct Biol. 1998 Sep;5(9):827-35.
Target 7 Drug References
  1. Chan K, Meng QC, Johansson JS, Eckenhoff RG: Low-affinity analytical chromatography for measuring inhaled anesthetic binding to isolated proteins. Anal Biochem. 2002 Feb 15;301(2):308-13. [PubMed Link Image]
  2. Solt K, Johansson JS: Binding of the active metabolite of chloral hydrate, 2,2,2-trichloroethanol, to serum albumin demonstrated using tryptophan fluorescence quenching. Pharmacology. 2002;64(3):152-9. [PubMed Link Image]
  3. Liu R, Pidikiti R, Ha CE, Petersen CE, Bhagavan NV, Eckenhoff RG: The role of electrostatic interactions in human serum albumin binding and stabilization by halothane. J Biol Chem. 2002 Sep 27;277(39):36373-9. Epub 2002 Jul 12. [PubMed Link Image]
  4. Liu R, Meng Q, Xi J, Yang J, Ha CE, Bhagavan NV, Eckenhoff RG: Comparative binding character of two general anaesthetics for sites on human serum albumin. Biochem J. 2004 May 15;380(Pt 1):147-52. [PubMed Link Image]
  5. Streiff JH, Juranic NO, Macura SI, Warner DO, Jones KA, Perkins WJ: Saturation transfer difference nuclear magnetic resonance spectroscopy as a method for screening proteins for anesthetic binding. Mol Pharmacol. 2004 Oct;66(4):929-35. [PubMed Link Image]
Drug Target 8 [top]
Target 8 ID 705
Target 8 Name Glutamate receptor 1
Target 8 Synonyms
  1. AMPA-selective glutamate receptor 1
  2. GluR-1
  3. GluR-A
  4. GluR-K1
  5. Glutamate receptor 1 precursor
  6. Glutamate receptor ionotropic, AMPA 1
Target 8 Gene Name GRIA1
Target 8 Protein Sequence >Glutamate receptor 1 precursor
MQHIFAFFCTGFLGAVVGANFPNNIQIGGLFPNQQSQEHAAFRFALSQLTEPPKLLPQID
IVNISDSFEMTYRFCSQFSKGVYAIFGFYERRTVNMLTSFCGALHVCFITPSFPVDTSNQ
FVLQLRPELQDALISIIDHYKWQKFVYIYDADRGLSVLQKVLDTAAEKNWQVTAVNILTT
TEEGYRMLFQDLEKKKERLVVVDCESERLNAILGQIIKLEKNGIGYHYILANLGFMDIDL
NKFKESGANVTGFQLVNYTDTIPAKIMQQWKNSDARDHTRVDWKRPKYTSALTYDGVKVM
AEAFQSLRRQRIDISRRGNAGDCLANPAVPWGQGIDIQRALQQVRFEGLTGNVQFNEKGR
RTNYTLHVIEMKHDGIRKIGYWNEDDKFVPAATDAQAGGDNSSVQNRTYIVTTILEDPYV
MLKKNANQFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDGKYGARDPDTKAWNGMVGE
LVYGRADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIW
MCIVFAYIGVSVVLFLVSRFSPYEWHSEEFEEGRDQTTSDQSNEFGIFNSLWFSLGAFMQ
QGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIA
YGTLEAGSTKEFFRRSKIAVFEKMWTYMKSAEPSVFVRTTEEGMIRVRKSKGKYAYLLES
TMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKW
WYDKGECGSGGGDSKDKTSALSLSNVAGVFYILIGGLGLAMLVALIEFCYKSRSESKRMK
GFCLIPQQSINEAIRTSTLPRNSGAGASSGGSGENGRVVSHDFPKSMQSIPCMSHSSGMP
LGATGL
Target 8 Number of Residues 921
Target 8 Molecular Weight 101507
Target 8 Theoretical pI 7.78
Target 8 GO Classification
Function
transporter activity
ion transporter activity
ion channel activity
ligand-gated ion channel activity
extracellular ligand-gated ion channel activity
excitatory extracellular ligand-gated ion channel activity
glutamate-gated ion channel activity
signal transducer activity
receptor activity
transmembrane receptor activity
glutamate receptor activity
ionotropic glutamate receptor activity
Process
physiological process
cellular physiological process
transport
ion transport
Component
cell
membrane
Target 8 General Function Involved in ionotropic glutamate receptor activity
Target 8 Specific Function L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists
Target 8 Pathways Not Available
Target 8 Reactions Not Available
Target 8 Pfam Domain Function
Target 8 Signals
  • 1-18
Target 8 Transmembrane Regions
  • 537-557
  • 585-605
  • 618-638
  • 806-826
Target 8 Essentiality Non-Essential
Target 8 GenBank ID Protein 183281 Link Image
Target 8 UniProtKB/Swiss-Prot ID P42261 Link Image
Target 8 UniProtKB/Swiss-Prot Entry Name GRIA1_HUMAN Link Image
Target 8 PDB ID 1WVJ Link Image
Target 8 PDB File Show
Target 8 3D Structure
Target 8 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 8 Gene Sequence >2724 bp
ATGCAGCACATTTTTGCCTTCTTCTGCACCGGTTTCCTAGGCGCGGTAGTAGGTGCCAAT
TTCCCCAACAATATCCAGATCGGGGGATTATTTCCAAACCAGCAGTCACAGGAACATGCT
GCTTTTAGATTTGCTTTGTCGCAACTCACAGAGCCCCCGAAGCTGCTCCCCCAGATTGAT
ATTGTGAACATCAGCGACAGCTTTGAGATGACCTATAGATTCTGTTCCCAGTTCTCCAAA
GGAGTCTATGCCATCTTTGGGTTTTATGAACGTAGGACTGTCAACATGCTGACCTCCTTT
TGTGGGGCCCTCCACGTCTGCTTCATTACGCCGAGCTTTCCCGTTGATACATCCAATCAG
TTTGTCCTTCAGCTGCGCCCTGAACTGCAGGATGCCCTCATCAGCATCATTGACCATTAC
AAGTGGCAGAAATTTGTCTACATTTATGATGCCGACCGGGGCTTATCCGTCCTGCAGAAA
GTCCTGGATACAGCTGCTGAGAAGAACTGGCAGGTGACAGCAGTCAACATCTTGACAACC
ACAGAGGAGGGATACCGGATGCTCTTTCAGGACCTGGAGAAGAAAAAGGAGCGGCTGGTG
GTGGTGGACTGTGAATCAGAACGCCTCAATGCTATCTTGGGCCAGATTATAAAGCTAGAG
AAGAATGGCATCGGCTACCACTACATTCTTGCAAATCTGGGCTTCATGGACATTGACTTA
AACAAATTCAAGGAGAGTGGCGCCAATGTGACAGGTTTCCAGCTGGTGAACTACACAGAC
ACTATTCCGGCCAAGATCATGCAGCAGTGGAAGAATAGTGATGCTCGAGACCACACACGG
GTGGACTGGAAGAGACCCAAGTACACCTCTGCGCTCACCTACGATGGGGTGAAGGTGATG
GCTGAGGCTTTCCAGAGCCTGCGGAGGCAGAGAATTGATATATCTCGCCGGGGGAATGCT
GGGGATTGTCTGGCTAACCCAGCTGTTCCCTGGGGCCAAGGGATCGACATCCAGAGAGCT
CTGCAGCAGGTGCGATTTGAAGGTTTAACAGGAAACGTGCAGTTTAATGAGAAAGGACGC
CGGACCAACTACACGCTCCACGTGATTGAAATGAAACATGACGGCATCCGAAAGATTGGT
TACTGGAATGAAGATGATAAGTTTGTCCCTGCAGCCACCGATGCCCAAGCTGGGGGCGAT
AATTCAAGTGTTCAGAACAGAACATACATCGTCACAACAATCCTAGAAGATCCTTATGTG
ATGCTCAAGAAGAACGCCAATCAGTTTGAGGGCAATGACCGTTACGAGGGCTACTGTGTA
GAGCTGGCGGCAGAGATTGCCAAGCACGTGGGCTACTCCTACCGTCTGGAGATTGTCAGT
GATGGAAAATACGGAGCCCGAGACCCTGACACGAAGGCCTGGAATGGCATGGTGGGAGAG
CTGGTCTATGGAAGAGCAGATGTGGCTGTGGCTCCCTTAACTATCACTTTGGTCCGGGAA
GAAGTTATAGATTTCTCCAAACCATTTATGAGTTTGGGGATCTCCATCATGATTAAAAAA
CCACAGAAATCCAAGCCGGGTGTCTTCTCCTTCCTTGATCCTTTGGCTTATGAGATTTGG
ATGTGCATTGTTTTTGCCTACATTGGAGTGAGTGTTGTCCTCTTCCTGGTCAGCCGCTTC
AGTCCCTATGAATGGCACAGTGAAGAGTTTGAGGAAGGACGGGACCAGACAACCAGTGAC
CAGTCCAATGAGTTTGGGATATTCAACAGTTTGTGGTTCTCCCTGGGAGCCTTCATGCAG
CAAGGATGTGACATTTCTCCCAGGTCCCTGTCTGGTCGCATCGTTGGTGGCGTCTGGTGG
TTCTTCACCTTAATCATCATCTCCTCATATACAGCCAATCTGGCCGCCTTCCTGACCGTG
GAGAGGATGGTGTCTCCCATTGAGAGTGCAGAGGACCTAGCGAAGCAGACAGAAATTGCC
TACGGGACGCTGGAAGCAGGATCTACTAAGGAGTTCTTCAGGAGGTCTAAAATTGCTGTG
TTTGAGAAGATGTGGACATACATGAAGTCAGCAGAGCCATCAGTTTTTGTGCGGACCACA
GAGGAGGGGATGATTCGAGTGAGGAAATCCAAAGGCAAATATGCCTACCTCCTGGAGTCC
ACCATGAATGAGTACATTGAGCAGCGGAAACCCTGTGACACCATGAAGGTGGGAGGTAAC
TTGGATTCCAAAGGCTATGGCATTGCAACACCCAAGGGGTCTGCCCTGAGAGGTCCCGTA
AACCTAGCGGTTTTGAAACTCAGTGAGCAAGGCGTCTTAGACAAGCTGAAAAGCAAATGG
TGGTACGATAAAGGGGAATGTGGAAGCAAGGACTCCGGAAGTAAGGACAAGACAAGCGCT
CTGAGCCTCAGCAATGTGGCAGGCGTGTTCTACATCCTGATCGGAGGACTTGGACTAGCC
ATGCTGGTTGCCTTAATCGAGTTCTGCTACAAATCCCGTAGTGAATCCAAGCGGATGAAG
GGTTTTTGTTTGATCCCACAGCAATCCATCAACGAAGCCATACGGACATCGACCCTCCCC
CGCAACAGCGCGGGCACGGCACCGAGCAGCGGCGGCAGTGGAGAGAATGGTCGGGTGGTC
AGCCATGACTTCCCCAAGTCCATGCAATCGATTCCTTGCATGAGCCACAGTTCAGGGATG
CCCTTGGGAGCCACGGGATTGTAA
Target 8 GenBank Gene ID
Target 8 GeneCard ID GRIA1 Link Image
Target 8 GenAtlas ID GRIA1 Link Image
Target 8 HGNC ID HGNC:4571 Link Image
Target 8 Chromosome Location 5
Target 8 Locus 5q33|5q31.1
Target 8 SNPs SNPJam Report Link Image
Target 8 General References
  1. Sun W, Ferrer-Montiel AV, Schinder AF, McPherson JP, Evans GA, Montal M: Molecular cloning, chromosomal mapping, and functional expression of human brain glutamate receptors. Proc Natl Acad Sci U S A. 1992 Feb 15;89(4):1443-7. [PubMed Link Image]
  2. Potier MC, Spillantini MG, Carter NP: The human glutamate receptor cDNA GluR1: cloning, sequencing, expression and localization to chromosome 5. DNA Seq. 1992;2(4):211-8. [PubMed Link Image]
  3. Puckett C, Gomez CM, Korenberg JR, Tung H, Meier TJ, Chen XN, Hood L: Molecular cloning and chromosomal localization of one of the human glutamate receptor genes. Proc Natl Acad Sci U S A. 1991 Sep 1;88(17):7557-61. [PubMed Link Image]
Target 8 Drug References
  1. Plested AJ, Wildman SS, Lieb WR, Franks NP: Determinants of the sensitivity of AMPA receptors to xenon. Anesthesiology. 2004 Feb;100(2):347-58. [PubMed Link Image]
Drug Target 9 [top]
Target 9 ID 872
Target 9 Name Gamma-aminobutyric-acid receptor subunit alpha-1
Target 9 Synonyms
  1. Gamma-aminobutyric-acid receptor subunit alpha-1 precursor
Target 9 Gene Name GABRA1
Target 9 Protein Sequence >Gamma-aminobutyric-acid receptor subunit alpha-1 precursor
MRKSPGLSDCLWAWILLLSTLTGRSYGQPSLQDELKDNTTVFTRILDRLLDGYDNRLRPG
LGERVTEVKTDIFVTSFGPVSDHDMEYTIDVFFRQSWKDERLKFKGPMTVLRLNNLMASK
IWTPDTFFHNGKKSVAHNMTMPNKLLRITEDGTLLYTMRLTVRAECPMHLEDFPMDAHAC
PLKFGSYAYTRAEVVYEWTREPARSVVVAEDGSRLNQYDLLGQTVDSGIVQSSTGEYVVM
TTHFHLKRKIGYFVIQTYLPCIMTVILSQVSFWLNRESVPARTVFGVTTVLTMTTLSISA
RNSLPKVAYATAMDWFIAVCYAFVFSALIEFATVNYFTKRGYAWDGKSVVPEKPKKVKDP
LIKKNNTYAPTATSYTPNLARGDPGLATIAKSATIEPKEVKPETKPPEPKKTFNSVSKID
RLSRIAFPLLFGIFNLVYWATYLNREPQLKAPTPHQ
Target 9 Number of Residues 463
Target 9 Molecular Weight 51802
Target 9 Theoretical pI 9.61
Target 9 GO Classification
Function
neurotransmitter receptor activity
transporter activity
ion transporter activity
ion channel activity
ligand-gated ion channel activity
extracellular ligand-gated ion channel activity
signal transducer activity
receptor activity
transmembrane receptor activity
GABA receptor activity
GABA-A receptor activity
Process
cellular process
cell communication
signal transduction
cell surface receptor linked signal transduction
G-protein coupled receptor protein signaling pathway
gamma-aminobutyric acid signaling pathway
anion transport
inorganic anion transport
chloride transport
physiological process
cellular physiological process
transport
ion transport
Component
postsynaptic membrane
cell
membrane
intrinsic to membrane
integral to membrane
Target 9 General Function Involved in GABA-A receptor activity
Target 9 Specific Function GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel
Target 9 Pathways Not Available
Target 9 Reactions Not Available
Target 9 Pfam Domain Function
Target 9 Signals
  • 1-27
Target 9 Transmembrane Regions
  • 252-273
  • 279-300
  • 313-334
  • 422-443
Target 9 Essentiality Non-Essential
Target 9 GenBank ID Protein 31631 Link Image
Target 9 UniProtKB/Swiss-Prot ID P14867 Link Image
Target 9 UniProtKB/Swiss-Prot Entry Name GBRA1_HUMAN Link Image
Target 9 PDB ID Not Available
Target 9 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 9 Gene Sequence >1371 bp
ATGAGGAAAAGTCCAGGTCTGTCTGACTGTCTTTGGGCCTGGATCCTCCTTCTGAGCACA
CTGACTGGAAGAAGCTATGGACAGCCGTCATTACAAGATGAACTTAAAGACAATACCACT
GTCTTCACCAGGATTTTGGACAGACTCCTAGATGGTTATGACAATCGCCTGAGACCAGGA
TTGGGAGAGCGTGTAACCGAAGTGAAGACTGATATCTTCGTCACCAGTTTCGGACCCGTT
TCAGACCATGATATGGAATATACAATAGATGTATTTTTCCGTCAAAGCTGGAAGGATGAA
AGGTTAAAATTTAAAGGACCTATGACAGTCCTCCGGTTAAATAACCTAATGGCAAGTAAA
ATCTGGACTCCGGACACATTTTTCCACAATGGAAAGAAGTCAGTGGCCCACAACATGACC
ATGCCCAACAAACTCCTGCGGATCACAGAGGATGGCACCTTGCTGTACACCATGAGGCTG
ACAGTGAGAGCTGAATGTCCGATGCATTTGGAGGACTTCCCTATGGATGCCCATGCTTGC
CCACTAAAATTTGGAAGTTATGCTTATACAAGAGCAGAAGTTGTTTATGAATGGACCAGA
GAGCCAGCACGCTCAGTGGTTGTAGCAGAAGATGGATCACGTCTAAACCAGTATGACCTT
CTTGGACAAACAGTAGACTCTGGAATTGTCCAGTCAAGTACAGGAGAATATGTTGTTATG
ACCACTCATTTCCACTTGAAGAGAAAGATTGGCTACTTTGTTATTCAAACATACCTGCCA
TGCATAATGACAGTGATTCTCTCACAAGTCTCCTTCTGGCTCAACAGAGAGTCTGTACCA
GCAAGAACTGTCTTTGGAGTAACAACTGTGCTCACCATGACAACATTGAGCATCAGTGCC
AGAAACTCCCTCCCTAAGGTGGCTTATGCAACAGCTATGGATTGGTTTATTGCCGTGTGC
TATGCCTTTGTGTTCTCAGCTCTGATTGAGTTTGCCACAGTAAACTATTTCACTAAGAGA
GGTTATGCATGGGATGGCAAAAGTGTGGTTCCAGAAAAGCCAAAGAAAGTAAAGGATCCT
CTTATTAAGAAAAACAACACTTACGCTCCAACAGCAACCAGCTACACCCCTAATTTGGCC
AGGGGCGACCCGGGCTTAGCCACCATTGCTAAAAGTGCAACCATAGAACCTAAAGAGGTC
AAGCCCGAAACAAAACCACCAGAACCCAAGAAAACCTTTAACAGTGTCAGCAAAATTGAC
CGACTGTCAAGAATAGCCTTCCCGCTGCTATTTGGAATCTTTAACTTAGTCTACTGGGCT
ACGTATTTAAACAGAGAGCCTCAGCTAAAAGCCCCCACACCACATCAATAG
Target 9 GenBank Gene ID
Target 9 GeneCard ID GABRA1 Link Image
Target 9 GenAtlas ID GABRA1 Link Image
Target 9 HGNC ID HGNC:4075 Link Image
Target 9 Chromosome Location 5
Target 9 Locus 5q34-q35
Target 9 SNPs SNPJam Report Link Image
Target 9 General References
  1. Cossette P, Liu L, Brisebois K, Dong H, Lortie A, Vanasse M, Saint-Hilaire JM, Carmant L, Verner A, Lu WY, Wang YT, Rouleau GA: Mutation of GABRA1 in an autosomal dominant form of juvenile myoclonic epilepsy. Nat Genet. 2002 Jun;31(2):184-9. Epub 2002 May 6. [PubMed Link Image]
  2. Schofield PR, Pritchett DB, Sontheimer H, Kettenmann H, Seeburg PH: Sequence and expression of human GABAA receptor alpha 1 and beta 1 subunits. FEBS Lett. 1989 Feb 27;244(2):361-4. [PubMed Link Image]
  3. Garrett KM, Duman RS, Saito N, Blume AJ, Vitek MP, Tallman JF: Isolation of a cDNA clone for the alpha subunit of the human GABA-A receptor. Biochem Biophys Res Commun. 1988 Oct 31;156(2):1039-45. [PubMed Link Image]
Target 9 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 10 [top]
Target 10 ID 1268
Target 10 Name Neuropeptide S receptor
Target 10 Synonyms
  1. G-protein coupled receptor 154
  2. G-protein coupled receptor PGR14
  3. G-protein coupled receptor for asthma susceptibility
Target 10 Gene Name NPSR1
Target 10 Protein Sequence >Neuropeptide S receptor
MPANFTEGSFDSSGTGQTLDSSPVACTETVTFTEVVEGKEWGSFYYSFKTEQLITLWVLF
VFTIVGNSVVLFSTWRRKKKSRMTFFVTQLAITDSFTGLVNILTDINWRFTGDFTAPDLV
CRVVRYLQVVLLYASTYVLVSLSIDRYHAIVYPMKFLQGEKQARVLIVIAWSLSFLFSIP
TLIIFGKRTLSNGEVQCWALWPDDSYWTPYMTIVAFLVYFIPLTIISIMYGIVIRTIWIK
SKTYETVISNCSDGKLCSSYNRGLISKAKIKAIKYSIIIILAFICCWSPYFLFDILDNFN
LLPDTQERFYASVIIQNLPALNSAINPLIYCVFSSSISFPCREQRSQDSRMTFRERTERH
EMQILSKPEFI
Target 10 Number of Residues 377
Target 10 Molecular Weight 42687
Target 10 Theoretical pI 8.44
Target 10 GO Classification
Function
peptide receptor activity, G-protein coupled
vasopressin-like receptor activity
vasopressin receptor activity
signal transducer activity
receptor activity
transmembrane receptor activity
G-protein coupled receptor activity
rhodopsin-like receptor activity
Process
cellular process
cell communication
signal transduction
cell surface receptor linked signal transduction
G-protein coupled receptor protein signaling pathway
Component
cell
membrane
intrinsic to membrane
integral to membrane
Target 10 General Function Involved in rhodopsin-like receptor activity
Target 10 Specific Function May be active in signaling pathway in an autocrine or paracrine fashion in several tissues. Receptor for neuropeptide S, it may mediate its action, such as inhibitory effects, on cell growth. Involved in pathogenesis of asthma and other IgE-mediated diseases
Target 10 Pathways Not Available
Target 10 Reactions Not Available
Target 10 Pfam Domain Function
Target 10 Signals
  • None
Target 10 Transmembrane Regions
  • 53-73
  • 83-103
  • 124-144
  • 165-185
  • 213-233
  • 276-296
  • 313-333
Target 10 Essentiality Non-Essential
Target 10 GenBank ID Protein 34596864 Link Image
Target 10 UniProtKB/Swiss-Prot ID Q6W5P4 Link Image
Target 10 UniProtKB/Swiss-Prot Entry Name NPSR1_HUMAN Link Image
Target 10 PDB ID Not Available
Target 10 Cellular Location
  • Isoform 1:Cell membrane
  • multi-pass membrane p
  • multi-pass membrane protein. Isoform 3:Cell membrane
Target 10 Gene Sequence >1116 bp
ATGCCAGCCAACTTCACAGAGGGCAGCTTCGATTCCAGTGGGACCGGGCAGACGCTGGAT
TCTTCCCCAGTGGCTTGCACTGAAACAGTGACTTTTACTGAAGTGGTGGAAGGAAAGGAA
TGGGGTTCCTTCTACTACTCCTTTAAGACTGAGCAATTGATAACTCTGTGGGTCCTCTTT
GTTTTTACCATTGTTGGAAACTCCGTTGTGCTTTTTTCCACATGGAGGAGAAAGAAGAAG
TCAAGAATGACCTTCTTTGTGACTCAGCTGGCCATCACAGATTCTTTCACAGGACTGGTC
AACATCTTGACAGATATTAATTGGCGATTCACTGGAGACTTCACGGCACCTGACCTGGTT
TGCCGAGTGGTCCGCTATTTGCAGGTTGTGCTGCTCTACGCCTCTACCTACGTCCTGGTG
TCCCTCAGCATAGACAGATACCATGCCATCGTCTACCCCATGAAGTTCCTTCAAGGAGAA
AAGCAAGCCAGGGTCCTCATTGTGATCGCCTGGAGCCTGTCTTTTCTGTTCTCCATTCCC
ACCCTGATCATATTTGGGAAGAGGACACTGTCCAACGGTGAAGTGCAGTGCTGGGCCCTG
TGGCCTGACGACTCCTACTGGACCCCATACATGACCATCGTGGCCTTCCTGGTGTACTTC
ATCCCTCTGACAATCATCAGCATCATGTATGGCATTGTGATCCGAACTATTTGGATTAAA
AGCAAAACCTACGAAACAGTGATTTCCAACTGCTCAGATGGGAAACTGTGCAGCAGCTAT
AACCGAGGACTCATCTCAAAGGCAAAAATCAAGGCTATCAAGTATAGCATCATCATCATT
CTTGCCTTCATCTGCTGTTGGAGTCCATACTTCCTGTTTGACATTTTGGACAATTTCAAC
CTCCTTCCAGACACCCAGGAGCGTTTCTATGCCTCTGTGATCATTCAGAACCTGCCAGCA
TTGAATAGTGCCATCAACCCCCTCATCTACTGTGTCTTCAGCAGCTCCATCTCTTTCCCC
TGCAGGGAGCAAAGATCACAGGATTCCAGAATGACGTTCCGGGAGAGAACTGAGAGGCAT
GAGATGCAGATTCTGTCCAAGCCAGAATTCATCTAG
Target 10 GenBank Gene ID
Target 10 GeneCard ID NPSR1 Link Image
Target 10 GenAtlas ID NPSR1 Link Image
Target 10 HGNC ID HGNC:23631 Link Image
Target 10 Chromosome Location 7
Target 10 Locus 7p14.3
Target 10 SNPs SNPJam Report Link Image
Target 10 General References Not Available
Target 10 Drug References
  1. Ishizawa Y, Sharp R, Liebman PA, Eckenhoff RG: Halothane binding to a G protein coupled receptor in retinal membranes by photoaffinity labeling. Biochemistry. 2000 Jul 25;39(29):8497-502. [PubMed Link Image]
  2. Ishizawa Y, Pidikiti R, Liebman PA, Eckenhoff RG: G protein-coupled receptors as direct targets of inhaled anesthetics. Mol Pharmacol. 2002 May;61(5):945-52. [PubMed Link Image]
  3. Streiff J, Jones K, Perkins WJ, Warner DO, Jones KA: Effect of halothane on the guanosine 5' triphosphate binding activity of G-protein alphai subunits. Anesthesiology. 2003 Jul;99(1):105-11. [PubMed Link Image]
Drug Target 11 [top]
Target 11 ID 1571
Target 11 Name G protein-activated inward rectifier potassium channel 1
Target 11 Synonyms
  1. GIRK1
  2. Inward rectifier K(+) channel Kir3.1
  3. Potassium channel, inwardly rectifying subfamily J member 3
Target 11 Gene Name KCNJ3
Target 11 Protein Sequence >G protein-activated inward rectifier potassium channel 1
MSALRRKFGDDYQVVTTSSSGSGLQPQGPGQDPQQQLVPKKKRQRFVDKNGRCNVQHGNL
GSETSRYLSDLFTTLVDLKWRWNLFIFILTYTVAWLFMASMWWVIAYTRGDLNKAHVGNY
TPCVANVYNFPSAFLFFIETEATIGYGYRYITDKCPEGIILFLFQSILGSIVDAFLIGCM
FIKMSQPKKRAETLMFSEHAVISMRDGKLTLMFRVGNLRNSHMVSAQIRCKLLKSRQTPE
GEFLPLDQLELDVGFSTGADQLFLVSPLTICHVIDAKSPFYDLSQRSMQTEQFEIVVILE
GIVETTGMTCQARTSYTEDEVLWGHRFFPVISLEEGFFKVDYSQFHATFEVPTPPYSVKE
QEEMLLMSSPLIAPAITNSKERHNSVECLDGLDDITTKLPSKLQKITGREDFPKKLLRMS
STTSEKAYSLGDLPMKLQRISSVPGNSEEKLVSKTTKMLSDPMSQSVADLPPKLQKMAGG
AARMEGNLPAKLRKMNSDRFT
Target 11 Number of Residues 509
Target 11 Molecular Weight 56604
Target 11 Theoretical pI 8.36
Target 11 GO Classification
Function
G-protein activated inward rectifier potassium channel activity
transporter activity
ion transporter activity
ion channel activity
voltage-gated ion channel activity
voltage-gated potassium channel activity
inward rectifier potassium channel activity
Process
physiological process
cellular physiological process
transport
ion transport
cation transport
monovalent inorganic cation transport
potassium ion transport
Component
cell
membrane
Target 11 General Function Involved in inward rectifier potassium channel activity
Target 11 Specific Function This 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 heartbeat
Target 11 Pathways Not Available
Target 11 Reactions Not Available
Target 11 Pfam Domain Function
Target 11 Signals
  • None
Target 11 Transmembrane Regions
  • 81-105
  • 158-179
Target 11 Essentiality Non-Essential
Target 11 GenBank ID Protein 1055028 Link Image
Target 11 UniProtKB/Swiss-Prot ID P48549 Link Image
Target 11 UniProtKB/Swiss-Prot Entry Name IRK3_HUMAN Link Image
Target 11 PDB ID 1U4E Link Image
Target 11 PDB File Show
Target 11 3D Structure
Target 11 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 11 Gene Sequence >1506 bp
ATGTCTGCACTCCGAAGGAAATTTGGGGACGATTATCAGGTAGTGACCACATCGTCCAGC
GGCTCGGGCTTGCAGCCCCAGGGGCCAGGCCAGGACCCTCAGCAGCAGCTTGTGCCCAAG
AAGAAGCGGCAGCGGTTCGTGGACAAGAACGGCCGGTGCAATGTACAGCACGGCAACCTG
GGCAGCGAGACAAGCCGCTACCTCTCGGACCTCTTCACCACGCTGGTGGACCTCAAGTGG
CGCTGGAACCTCTTCATCTTCATTCTCACCTACACCGTGGCCTGGCTTTTCATGGCGTCC
ATGTGGTGGGTGATCGCCTACACTCGGGGCGACCTGAACAAAGCCCACGTCGGTAACTAC
ACGCCTTGCGTGGCCAATGTCTATAACTTCCCTTCTGCCTTCCTCTTCTTCATCGAGACG
GAGGCCACCATCGGCTATGGCTACCGATACATCACAGACAAGTGCCCCGAGGGCATCATC
CTCTTCCTCTTCCAGTCCATCCTGGGCTCCATCGTGGACGCCTTCCTCATCGGCTGCATG
TTCATCAAGATGTCCCAGCCCAAGAAGCGCGCCGAGACCCTCATGTTCAGCGAGCACGCG
GTGATCTCCATGAGGGACGGAAAACTCACGCTTATGTTCCGGGTGGGCAACCTGCGCAAC
AGCCACATGGTCTCCGCGCAGATTCGCTGCAAGCTGCTCAAATCTCGGCAGACACCTGAG
GGTGAGTTCCTTCCCCTTGACCAACTTGAACTGGATGTAGGTTTTAGTACAGGGGCAGAT
CAACTTTTTCTTGTGTCCCCCCTCACAATTTGCCACGTGATCGATGCCAAAAGCCCCTTT
TATGACCTATCCCAGCGAAGCATGCAAACTGAACAGTTCGAGATTGTCGTCATCCTAGAA
GGCATTGTGGAAACAACTGGGATGACTTGTCAAGCTCGAACATCATATACTGAAGATGAA
GTTCTTTGGGGTCATCGTTTTTTTCCTGTAATTTCCTTAGAAGAGGGATTCTTTAAAGTT
GATTATTCCCAGTTCCATGCAACATTTGAAGTCCCCACCCCACCTTACAGTGTGAAAGAG
CAGGAGGAAATGCTTCTCATGTCGTCCCCCTTAATAGCACCAGCCATAACTAACAGCAAA
GAAAGACATAATTCTGTGGAATGCTTAGATGGACTAGATGATATTACTACAAAACTACCA
TCTAAGCTGCAGAAAATTACTGGAAGAGAAGACTTTCCCAAAAAACTCTTGAGGATGAGT
TCTACAACTTCAGAAAAAGCCTACAGCTTGGGAGACTTGCCCATGAAACTTCAACGAATA
AGTTCAGTTCCGGGCAACTCAGAAGAAAAACTGGTATCTAAAACCACCAAGATGTTATCT
GATCCCATGAGCCAGTCTGTGGCTGATTTGCCACCAAAGCTTCAAAAGATGGCTGGAGGA
GCAGCTAGGATGGAAGGGAACCTTCCAGCCAAATTAAGAAAAATGAACTCTGATCGCTTC
ACATAA
Target 11 GenBank Gene ID
Target 11 GeneCard ID KCNJ3 Link Image
Target 11 GenAtlas ID KCNJ3 Link Image
Target 11 HGNC ID HGNC:6264 Link Image
Target 11 Chromosome Location 2
Target 11 Locus 2q24.1
Target 11 SNPs SNPJam Report Link Image
Target 11 General References
  1. Schoots O, Yue KT, MacDonald JF, Hampson DR, Nobrega JN, Dixon LM, Van Tol HH: Cloning of a G protein-activated inwardly rectifying potassium channel from human cerebellum. Brain Res Mol Brain Res. 1996 Jul;39(1-2):23-30. [PubMed Link Image]
  2. Chan KW, Langan MN, Sui JL, Kozak JA, Pabon A, Ladias JA, Logothetis DE: A recombinant inwardly rectifying potassium channel coupled to GTP-binding proteins. J Gen Physiol. 1996 Mar;107(3):381-97. [PubMed Link Image]
Target 11 Drug References
  1. Weigl LG, Schreibmayer W: G protein-gated inwardly rectifying potassium channels are targets for volatile anesthetics. Mol Pharmacol. 2001 Aug;60(2):282-9. [PubMed Link Image]
  2. Yamakura T, Lewohl JM, Harris RA: Differential effects of general anesthetics on G protein-coupled inwardly rectifying and other potassium channels. Anesthesiology. 2001 Jul;95(1):144-53. [PubMed Link Image]
  3. Milovic S, Steinecker-Frohnwieser B, Schreibmayer W, Weigl LG: The sensitivity of G protein-activated K+ channels toward halothane is essentially determined by the C terminus. J Biol Chem. 2004 Aug 13;279(33):34240-9. Epub 2004 Jun 2. [PubMed Link Image]
Drug Target 12 [top]
Target 12 ID 1581
Target 12 Name G protein-activated inward rectifier potassium channel 2
Target 12 Synonyms
  1. BIR1
  2. GIRK2
  3. Inward rectifier K(+) channel Kir3.2
  4. KATP-2
  5. Potassium channel, inwardly rectifying subfamily J member 6
Target 12 Gene Name KCNJ6
Target 12 Protein Sequence >G protein-activated inward rectifier potassium channel 2
MAKLTESMTNVLEGDSMDQDVESPVAIHQPKLPKQARDDLPRHISRDRTKRKIQRYVRKD
GKCNVHHGNVRETYRYLTDIFTTLVDLKWRFNLLIFVMVYTVTWLFFGMIWWLIAYIRGD
MDHIEDPSWTPCVTNLNGFVSAFLFSIETETTIGYGYRVITDKCPEGIILLLIQSVLGSI
VNAFMVGCMFVKISQPKKRAETLVFSTHAVISMRDGKLCLMFRVGDLRNSHIVEASIRAK
LIKSKQTSEGEFIPLNQTDINVGYYTGDDRLFLVSPLIISHEINQQSPFWEISKAQLPKE
ELEIVVILEGMVEATGMTCQARSSYITSEILWGYRFTPVLTLEDGFYEVDYNSFHETYET
STPSLSAKELAELASRAELPLSWSVSSKLNQHAELETEEEEKNLEEQTERNGDVANLENE
SKV
Target 12 Number of Residues 430
Target 12 Molecular Weight 48452
Target 12 Theoretical pI 5.04
Target 12 GO Classification
Function
G-protein activated inward rectifier potassium channel activity
transporter activity
ion transporter activity
ion channel activity
voltage-gated ion channel activity
voltage-gated potassium channel activity
inward rectifier potassium channel activity
Process
physiological process
cellular physiological process
transport
ion transport
cation transport
monovalent inorganic cation transport
potassium ion transport
Component
cell
membrane
Target 12 General Function Involved in inward rectifier potassium channel activity
Target 12 Specific Function This potassium channel may be involved in the regulation of insulin secretion by glucose and/or neurotransmitters acting through G-protein-coupled receptors. 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
Target 12 Pathways Not Available
Target 12 Reactions Not Available
Target 12 Pfam Domain Function
Target 12 Signals
  • None
Target 12 Transmembrane Regions
  • 90-114
  • 167-188
Target 12 Essentiality Non-Essential
Target 12 GenBank ID Protein 1052875 Link Image
Target 12 UniProtKB/Swiss-Prot ID P48051 Link Image
Target 12 UniProtKB/Swiss-Prot Entry Name IRK6_HUMAN Link Image
Target 12 PDB ID Not Available
Target 12 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 12 Gene Sequence >1272 bp
ATGGCCAAGCTGACAGAATCCATGACTAACGTCCTGGAGGGCGACTCCATGGATCAGGAC
GTCGAAAGCCCAGTGGCCATTCACCAGCCAAAGTTGCCTAAGCAGGCCAGGGATGACCTG
CCAAGACACATCAGCCGAGATCGGACCAAAAGGAAAATCCAGAGGTACGTGAGGAAAGAC
GGAAAGTGCAATGTTCATCACGGCAACGTGAGGGAGACCTATCGCTACCTGACCGATATC
TTCACCACATTAGTGGACCTGAAGTGGAGATTCAACCTATTGATTTTTGTCATGGTTTAC
ACAGTGACCTGGCTCTTTTTTGGAATGATCTGGTGGTTGATCGCATACATACGGGGAGAC
ATGGACCACATAGAGGACCCCTCCTGGACTCCTTGTGTTACCAACCTCAACGGGTTCGTC
TCTGCTTTTTTATTCTCAATAGAGACAGAAACCACCATTGGTTATGGCTACCGGGTCATC
ACAGATAAATGCCCGGAGGGAATTATTCTTCTCTTAATCCAATCTGTGTTGGGGTCCATT
GTCAATGCATTCATGGTGGGATGCATGTTTGTAAAAATCTCTCAACCCAAGAAGAGGGCA
GAGACCCTGGTCTTTTCCACCCATGCAGTGATCTCCATGCGGGATGGGAAACTGTGCCTG
ATGTTCCGGGTAGGGGACCTTAGGAATTCCCACATTGTGGAGGCTTCCATCAGAGCCAAG
TTGATCAAATCCAAACAGACCTCGGAGGGGGAGTTCATCCCGTTGAACCAGACGGATATC
AACGTAGGGTATTACACGGGGGATGACCGTCTGTTTCTGGTGTCACCGCTGATCATTAGC
CATGAAATTAACCAACAGAGTCCTTTCTGGGAGATCTCCAAAGCCCAGCTGCCCAAAGAG
GAACTGGAAATTGTGGTCATCCTAGAAGGAATGGTGGAAGCCACAGGGATGACATGCCAA
GCTCGAAGCTCCTACATCACCAGTGAGATCCTGTGGGGTTACCGGTTCACACCTGTCCTG
ACCCTGGAGGATGGGTTCTACGAAGTTGACTACAACAGCTTCCATGAGACCTATGAGACC
AGCACCCCATCCCTTAGTGCCAAAGAGCTGGCCGAGTTAGCCAGCAGGGCAGAGCTGCCC
CTGAGTTGGTCTGTATCCAGCAAACTCAACCAACATGCAGAACTGGAGACTGAAGAGGAA
GAAAAGAACCTCGAAGAGCAAACAGAAAGAAATGGTGATGTGGCAAACCTGGAGAATGAA
TCCAAAGTTTAG
Target 12 GenBank Gene ID
Target 12 GeneCard ID KCNJ6 Link Image
Target 12 GenAtlas ID KCNJ6 Link Image
Target 12 HGNC ID HGNC:6267 Link Image
Target 12 Chromosome Location Not Available
Target 12 Locus Not Available
Target 12 SNPs SNPJam Report Link Image
Target 12 General References
  1. Schoots O, Wilson JM, Ethier N, Bigras E, Hebert TE, Van Tol HH: Co-expression of human Kir3 subunits can yield channels with different functional properties. Cell Signal. 1999 Dec;11(12):871-83. [PubMed Link Image]
  2. Ferrer J, Nichols CG, Makhina EN, Salkoff L, Bernstein J, Gerhard D, Wasson J, Ramanadham S, Permutt A: Pancreatic islet cells express a family of inwardly rectifying K+ channel subunits which interact to form G-protein-activated channels. J Biol Chem. 1995 Nov 3;270(44):26086-91. [PubMed Link Image]
  3. Tsaur ML, Menzel S, Lai FP, Espinosa R 3rd, Concannon P, Spielman RS, Hanis CL, Cox NJ, Le Beau MM, German MS, et al.: Isolation of a cDNA clone encoding a KATP channel-like protein expressed in insulin-secreting cells, localization of the human gene to chromosome band 21q22.1, and linkage studies with NIDDM. Diabetes. 1995 May;44(5):592-6. [PubMed Link Image]
  4. Sakura H, Bond C, Warren-Perry M, Horsley S, Kearney L, Tucker S, Adelman J, Turner R, Ashcroft FM: Characterization and variation of a human inwardly-rectifying-K-channel gene (KCNJ6): a putative ATP-sensitive K-channel subunit. FEBS Lett. 1995 Jun 26;367(2):193-7. [PubMed Link Image]
Target 12 Drug References
  1. Milovic S, Steinecker-Frohnwieser B, Schreibmayer W, Weigl LG: The sensitivity of G protein-activated K+ channels toward halothane is essentially determined by the C terminus. J Biol Chem. 2004 Aug 13;279(33):34240-9. Epub 2004 Jun 2. [PubMed Link Image]
  2. Hara K, Yamakura T, Sata T, Harris RA: The effects of anesthetics and ethanol on alpha2 adrenoceptor subtypes expressed with G protein-coupled inwardly rectifying potassium channels in Xenopus oocytes. Anesth Analg. 2005 Nov;101(5):1381-8. [PubMed Link Image]
Drug Target 13 [top]
Target 13 ID 1768
Target 13 Name Guanine nucleotide-binding protein G(I)/G(S)/G(O) gamma-2 subunit
Target 13 Synonyms
  1. G gamma-I
  2. Guanine nucleotide-binding protein G(I)/G(S)/G(O) gamma-2 subunit precursor
Target 13 Gene Name GNG2
Target 13 Protein Sequence >Guanine nucleotide-binding protein G(I)/G(S)/G(O) gamma-2 subunit precursor
MASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENP
FREKKFFCAIL
Target 13 Number of Residues 72
Target 13 Molecular Weight 7850
Target 13 Theoretical pI 8.22
Target 13 GO Classification
Function
signal transducer activity
Process
cellular process
cell communication
signal transduction
cell surface receptor linked signal transduction
G-protein coupled receptor protein signaling pathway
Component
cell
membrane
extrinsic to membrane
extrinsic to plasma membrane
heterotrimeric G-protein complex
Target 13 General Function Involved in signal transducer activity
Target 13 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction
Target 13 Pathways Not Available
Target 13 Reactions Not Available
Target 13 Pfam Domain Function
Target 13 Signals
  • None
Target 13 Transmembrane Regions
  • None
Target 13 Essentiality Non-Essential
Target 13 GenBank ID Protein 20147633 Link Image
Target 13 UniProtKB/Swiss-Prot ID P59768 Link Image
Target 13 UniProtKB/Swiss-Prot Entry Name GBG2_HUMAN Link Image
Target 13 PDB ID 1GP2 Link Image
Target 13 PDB File Show
Target 13 3D Structure
Target 13 Cellular Location
  • Cell membrane
  • cytoplasmic side (Potential)
  • lipid-anchor
Target 13 Gene Sequence >216 bp
ATGGCCAGCAACAACACCGCCAGCATAGCACAAGCCAGGAAGCTGGTAGAGCAGCTTAAG
ATGGAAGCCAATATCGACAGGATAAAGGTGTCCAAGGCAGCTGCAGATTTGATGGCCTAC
TGTGAAGCACATGCCAAGGAAGACCCCCTCCTGACCCCTGTTCCGGCTTCAGAAAACCCG
TTTAGGGAGAAGAAGTTTTTCTGTGCCATCCTTTAA
Target 13 GenBank Gene ID
Target 13 GeneCard ID GNG2 Link Image
Target 13 GenAtlas ID GNG2 Link Image
Target 13 HGNC ID HGNC:4404 Link Image
Target 13 Chromosome Location 14
Target 13 Locus 14q21
Target 13 SNPs SNPJam Report Link Image
Target 13 General References
  1. Modarressi MH, Taylor KE, Wolfe J: Cloning, characterization, and mapping of the gene encoding the human G protein gamma 2 subunit. Biochem Biophys Res Commun. 2000 Jun 7;272(2):610-5. [PubMed Link Image]
Target 13 Drug References
  1. Ishizawa Y, Sharp R, Liebman PA, Eckenhoff RG: Halothane binding to a G protein coupled receptor in retinal membranes by photoaffinity labeling. Biochemistry. 2000 Jul 25;39(29):8497-502. [PubMed Link Image]
  2. Zang WJ, Yu XJ, Zang YM: [Effect of halothane on the muscarinic potassium current of the heart] Sheng Li Xue Bao. 2000 Apr;52(2):175-8. [PubMed Link Image]
  3. Yoshimura H, Jones KA, Perkins WJ, Warner DO: Dual effects of hexanol and halothane on the regulation of calcium sensitivity in airway smooth muscle. Anesthesiology. 2003 Apr;98(4):871-80. [PubMed Link Image]
  4. Streiff J, Jones K, Perkins WJ, Warner DO, Jones KA: Effect of halothane on the guanosine 5' triphosphate binding activity of G-protein alphai subunits. Anesthesiology. 2003 Jul;99(1):105-11. [PubMed Link Image]
  5. Milovic S, Steinecker-Frohnwieser B, Schreibmayer W, Weigl LG: The sensitivity of G protein-activated K+ channels toward halothane is essentially determined by the C terminus. J Biol Chem. 2004 Aug 13;279(33):34240-9. Epub 2004 Jun 2. [PubMed Link Image]
Drug Target 14 [top]
Target 14 ID 2207
Target 14 Name Rhodopsin
Target 14 Synonyms
  1. Opsin-2
Target 14 Gene Name RHO
Target 14 Protein Sequence >Rhodopsin
MNGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQFSMLAAYMFLLIVLGFPINFLTLY
VTVQHKKLRTPLNYILLNLAVADLFMVLGGFTSTLYTSLHGYFVFGPTGCNLEGFFATLG
GEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMALACAAPPLAGWSRYIP
EGLQCSCGIDYYTLKPEVNNESFVIYMFVVHFTIPMIIIFFCYGQLVFTVKEAAAQQQES
ATTQKAEKEVTRMVIIMVIAFLICWVPYASVAFYIFTHQGSNFGPIFMTIPAFFAKSAAI
YNPVIYIMMNKQFRNCMLTTICCGKNPLGDDEASATVSKTETSQVAPA
Target 14 Number of Residues 353
Target 14 Molecular Weight 38893
Target 14 Theoretical pI 6.64
Target 14 GO Classification
Function
signal transducer activity
receptor activity
transmembrane receptor activity
G-protein coupled receptor activity
rhodopsin-like receptor activity
Process
response to stimulus
response to abiotic stimulus
response to radiation
response to light stimulus
detection of light stimulus
phototransduction
physiological process
organismal physiological process
neurophysiological process
sensory perception
sensory perception of light stimulus
visual perception
cellular process
cell communication
signal transduction
cell surface receptor linked signal transduction
G-protein coupled receptor protein signaling pathway
Component
cell
membrane
intrinsic to membrane
integral to membrane
Target 14 General Function Involved in rhodopsin-like receptor activity
Target 14 Specific Function Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal
Target 14 Pathways Not Available
Target 14 Reactions Not Available
Target 14 Pfam Domain Function
Target 14 Signals
  • None
Target 14 Transmembrane Regions
  • 37-61
  • 74-98
  • 114-133
  • 153-176
  • 203-230
  • 253-276
  • 285-309
Target 14 Essentiality Non-Essential
Target 14 GenBank ID Protein 1236137 Link Image
Target 14 UniProtKB/Swiss-Prot ID P08100 Link Image
Target 14 UniProtKB/Swiss-Prot Entry Name OPSD_HUMAN Link Image
Target 14 PDB ID 1LN6 Link Image
Target 14 PDB File Show
Target 14 3D Structure
Target 14 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 14 Gene Sequence >1047 bp
ATGAATGGCACAGAAGGCCCTAACTTCTACGTGCCCTTCTCCAATGCGACGGGTGTGGTA
CGCAGCCCCTTCGAGTACCCACAGTACTACCTGGCTGAGCCATGGCAGTTCTCCATGCTG
GCCGCCTACATGTTTCTGCTGATCGTGCTGGGCTTCCCCATCAACTTCCTCACGCTCTAC
GTCACCGTCCAGCACAAGAAGCTGCGCACGCCTCTCAACTACATCCTGCTCAACCTAGCC
GTGGCTGACCTCTTCATGGTCCTAGGTGGCTTCACCAGCACCCTCTACACCTCTCTGCAT
GGATACTTCGTCTTCGGGCCCACAGGATGCAATTTGGAGGGCTTCTTTGCCACCCTGGGC
GGTGAAATTGCCCTGTGGTCCTTGGTGGTCCTGGCCATCGAGCGGTACGTGGTGGTGTGT
AAGCCCATGAGCAACTTCCGCTTCGGGGAGAACCATGCCATCATGGGCGTTGCCTTCACC
TGGGTCATGGCGCTGGCCTGCGCCGCACCCCCACTCGCCGGCTGGTCCAGGTACATCCCC
GAGGGCCTGCAGTGCTCGTGTGGAATCGACTACTACACGCTCAAGCCGGAGGTCAACAAC
GAGTCTTTTGTCATCTACATGTTCGTGGTCCACTTCACCATCCCCATGATTATCATCTTT
TTCTGCTATGGGCAGCTCGTCTTCACCGTCAAGGAGGCCGCTGCCCAGCAGCAGGAGTCA
GCCACCACACAGAAGGCAGAGAAGGAGGTCACCCGCATGGTCATCATCATGGTCATCGCT
TTCCTGATCTGCTGGGTGCCCTACGCCAGCGTGGCATTCTACATCTTCACCCACCAGGGC
TCCAACTTCGGTCCCATCTTCATGACCATCCCAGCGTTCTTTGCCAAGAGCGCCGCCATC
TACAACCCTGTCATCTATATCATGATGAACAAGCAGTTCCGGAACTGCATGCTCACCACC
ATCTGCTGCGGCAAGAACCCACTGGGTGACGATGAGGCCTCTGCTACCGTGTCCAAGACG
GAGACGAGCCAGGTGGCCCCGGCCTAA
Target 14 GenBank Gene ID
Target 14 GeneCard ID RHO Link Image
Target 14 GenAtlas ID RHO Link Image
Target 14 HGNC ID HGNC:10012 Link Image
Target 14 Chromosome Location 3
Target 14 Locus 3q21-q24
Target 14 SNPs SNPJam Report Link Image
Target 14 General References
  1. Farrar GJ, Findlay JB, Kumar-Singh R, Kenna P, Humphries MM, Sharpe E, Humphries P: Autosomal dominant retinitis pigmentosa: a novel mutation in the rhodopsin gene in the original 3q linked family. Hum Mol Genet. 1992 Dec;1(9):769-71. [PubMed Link Image]
  2. Fujiki K, Hotta Y, Hayakawa M, Sakuma H, Shiono T, Noro M, Sakuma T, Tamai M, Hikiji K, Kawaguchi R, et al.: Point mutations of rhodopsin gene found in Japanese families with autosomal dominant retinitis pigmentosa (ADRP). Jpn J Hum Genet. 1992 Jun;37(2):125-32. [PubMed Link Image]
  3. Dryja TP, Hahn LB, Cowley GS, McGee TL, Berson EL: Mutation spectrum of the rhodopsin gene among patients with autosomal dominant retinitis pigmentosa. Proc Natl Acad Sci U S A. 1991 Oct 15;88(20):9370-4. [PubMed Link Image]
  4. Gal A, Artlich A, Ludwig M, Niemeyer G, Olek K, Schwinger E, Schinzel A: Pro-347-Arg mutation of the rhodopsin gene in autosomal dominant retinitis pigmentosa. Genomics. 1991 Oct;11(2):468-70. [PubMed Link Image]
  5. Sung CH, Davenport CM, Hennessey JC, Maumenee IH, Jacobson SG, Heckenlively JR, Nowakowski R, Fishman G, Gouras P, Nathans J: Rhodopsin mutations in autosomal dominant retinitis pigmentosa. Proc Natl Acad Sci U S A. 1991 Aug 1;88(15):6481-5. [PubMed Link Image]
  6. Sheffield VC, Fishman GA, Beck JS, Kimura AE, Stone EM: Identification of novel rhodopsin mutations associated with retinitis pigmentosa by GC-clamped denaturing gradient gel electrophoresis. Am J Hum Genet. 1991 Oct;49(4):699-706. [PubMed Link Image]
  7. Inglehearn CF, Bashir R, Lester DH, Jay M, Bird AC, Bhattacharya SS: A 3-bp deletion in the rhodopsin gene in a family with autosomal dominant retinitis pigmentosa. Am J Hum Genet. 1991 Jan;48(1):26-30. [PubMed Link Image]
  8. Dryja TP, McGee TL, Reichel E, Hahn LB, Cowley GS, Yandell DW, Sandberg MA, Berson EL: A point mutation of the rhodopsin gene in one form of retinitis pigmentosa. Nature. 1990 Jan 25;343(6256):364-6. [PubMed Link Image]
  9. Dryja TP, McGee TL, Hahn LB, Cowley GS, Olsson JE, Reichel E, Sandberg MA, Berson EL: Mutations within the rhodopsin gene in patients with autosomal dominant retinitis pigmentosa. N Engl J Med. 1990 Nov 8;323(19):1302-7. [PubMed Link Image]
  10. Farrar GJ, Kenna P, Redmond R, McWilliam P, Bradley DG, Humphries MM, Sharp EM, Inglehearn CF, Bashir R, Jay M, et al.: Autosomal dominant retinitis pigmentosa: absence of the rhodopsin proline----histidine substitution (codon 23) in pedigrees from Europe. Am J Hum Genet. 1990 Dec;47(6):941-5. [PubMed Link Image]
  11. 6589631 Nathans J, Hogness DS: Isolation and nucleotide sequence of the gene encoding human rhodopsin. Proc Natl Acad Sci U S A. 1984 Aug;81(15):4851-5.
  12. 7633434 Macke JP, Hennessey JC, Nathans J: Rhodopsin mutation proline347-to-alanine in a family with autosomal dominant retinitis pigmentosa indicates an important role for proline at position 347. Hum Mol Genet. 1995 Apr;4(4):775-6.
  13. 7846071 Sieving PA, Richards JE, Naarendorp F, Bingham EL, Scott K, Alpern M: Dark-light: model for nightblindness from the human rhodopsin Gly-90-->Asp mutation. Proc Natl Acad Sci U S A. 1995 Jan 31;92(3):880-4.
  14. 7981701 Fuchs S, Kranich H, Denton MJ, Zrenner E, Bhattacharya SS, Humphries P, Gal A: Three novel rhodopsin mutations (C110F, L131P, A164V) in patients with autosomal dominant retinitis pigmentosa. Hum Mol Genet. 1994 Jul;3(7):1203.
  15. 7987326 Antinolo G, Sanchez B, Borrego S, Rueda T, Chaparro P, Cabeza JC: Identification of a new mutation at codon 171 of rhodopsin gene causing autosomal dominant retinitis pigmentosa. Hum Mol Genet. 1994 Aug;3(8):1421.
  16. 7987331 Souied E, Gerber S, Rozet JM, Bonneau D, Dufier JL, Ghazi I, Philip N, Soubrane G, Coscas G, Munnich A, et al.: Five novel missense mutations of the rhodopsin gene in autosomal dominant retinitis pigmentosa. Hum Mol Genet. 1994 Aug;3(8):1433-4.
  17. 7987385 Kumaramanickavel G, Maw M, Denton MJ, John S, Srikumari CR, Orth U, Oehlmann R, Gal A: Missense rhodopsin mutation in a family with recessive RP. Nat Genet. 1994 Sep;8(1):10-1.
  18. 8045708 Rosas DJ, Roman AJ, Weissbrod P, Macke JP, Nathans J: Autosomal dominant retinitis pigmentosa in a large family: a clinical and molecular genetic study. Invest Ophthalmol Vis Sci. 1994 Jul;35(8):3134-44.
  19. 8076945 Reig C, Antich J, Gean E, Garcia-Sandoval B, Ramos C, Ayuso C, Carballo M: Identification of a novel rhodopsin mutation (Met-44-Thr) in a simplex case of retinitis pigmentosa. Hum Genet. 1994 Sep;94(3):283-6.
  20. 8081400 al-Maghtheh M, Inglehearn C, Lunt P, Jay M, Bird A, Bhattacharya S: Two new rhodopsin transversion mutations (L40R; M216K) in families with autosomal dominant retinitis pigmentosa. Hum Mutat. 1994;3(4):409-10.
  21. 8088850 Vaithinathan R, Berson EL, Dryja TP: Further screening of the rhodopsin gene in patients with autosomal dominant retinitis pigmentosa. Genomics. 1994 May 15;21(2):461-3.
  22. 8317502 Macke JP, Davenport CM, Jacobson SG, Hennessey JC, Gonzalez-Fernandez F, Conway BP, Heckenlively J, Palmer R, Maumenee IH, Sieving P, et al.: Identification of novel rhodopsin mutations responsible for retinitis pigmentosa: implications for the structure and function of rhodopsin. Am J Hum Genet. 1993 Jul;53(1):80-9.
  23. 8353500 Kranich H, Bartkowski S, Denton MJ, Krey S, Dickinson P, Duvigneau C, Gal A: Autosomal dominant 'sector' retinitis pigmentosa due to a point mutation predicting an Asn-15-Ser substitution of rhodopsin. Hum Mol Genet. 1993 Jun;2(6):813-4.
  24. 8358437 Dryja TP, Berson EL, Rao VR, Oprian DD: Heterozygous missense mutation in the rhodopsin gene as a cause of congenital stationary night blindness. Nat Genet. 1993 Jul;4(3):280-3.
  25. 8401533 al-Maghtheh M, Gregory C, Inglehearn C, Hardcastle A, Bhattacharya S: Rhodopsin mutations in autosomal dominant retinitis pigmentosa. Hum Mutat. 1993;2(4):249-55.
  26. 8554077 Souied E, Soubrane G, Benlian P, Coscas GJ, Gerber S, Munnich A, Kaplan J: Retinitis punctata albescens associated with the Arg135Trp mutation in the rhodopsin gene. Am J Ophthalmol. 1996 Jan;121(1):19-25.
  27. 9452035 Goliath R, Bardien S, September A, Martin R, Ramesar R, Greenberg J: Rhodopsin mutation G109R in a family with autosomal dominant retinitis pigmentosa. Hum Mutat. 1998;Suppl 1:S40-1.
  28. 9888392 al-Jandal N, Farrar GJ, Kiang AS, Humphries MM, Bannon N, Findlay JB, Humphries P, Kenna PF: A novel mutation within the rhodopsin gene (Thr-94-Ile) causing autosomal dominant congenital stationary night blindness. Hum Mutat. 1999;13(1):75-81.
Target 14 Drug References
  1. Ishizawa Y, Sharp R, Liebman PA, Eckenhoff RG: Halothane binding to a G protein coupled receptor in retinal membranes by photoaffinity labeling. Biochemistry. 2000 Jul 25;39(29):8497-502. [PubMed Link Image]
  2. Keller C, Grimm C, Wenzel A, Hafezi F, Reme C: Protective effect of halothane anesthesia on retinal light damage: inhibition of metabolic rhodopsin regeneration. Invest Ophthalmol Vis Sci. 2001 Feb;42(2):476-80. [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.