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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-06-23 18:05:51
Primary Accession Number DB01229
Secondary Accession Number
  • APRD00259
Name Paclitaxel
Drug Type
  • Approved
  • Investigational
  • Small Molecule
Description A cyclodecane isolated from the bark of the Pacific yew tree, TAXUS brevifolia. It stabilizes microtubules in their polymerized form leading to cell death. [PubChem]
Synonyms
  1. 7-Epipaclitaxel
  2. 7-Epitaxol
  3. 7-epi-Paclitaxel
  4. 7-epi-Taxol
Brand Names
  1. Epitaxol
  2. LipoPac
  3. Onxol
  4. Paxceed
  5. Paxene
  6. Taxol
  7. Taxol A
  8. Vascular Wrap
  9. Xorane
Brand Mixtures Not Available
Chemical IUPAC Name 5 beta,20-Epoxy-1,2a,4,7 beta,10 beta,13 alpha-hexahydroxytax-11-en-9-one 4,10-diacetate 2-benzoate 13-ester with (2 R,3S)-N-benzoyl-3-phenylisoserine
Chemical Formula C47H51NO14
Chemical Structure Structure
CAS Registry Number 33069-62-4
InChI Identifier InChI=1/C47H51NO14/c1-25-31(60-43(56)36(52)35(28-16-10-7-11-17-28)48-41(54)29-18-12-8-13-19-29)23-47(57)40(61-42(55)30-20-14-9-15-21-30)38-45(6,32(51)22-33-46(38,24-58-33)62-27(3)50)39(53)37(59-26(2)49)34(25)44(47,4)5/h7-21,31-33,35-38,40,51-52,57H,22-24H2,1-6H3,(H,48,54)/t31-,32-,33+,35-,36+,37-,38-,40-,45+,46-,47+/m0/s1/f/h48H
InChI Key RCINICONZNJXQF-CLDWUXIMDD
KEGG Drug D00491 Link Image
KEGG Compound C07394 Link Image
PubChem Compound 36314 Link Image
PubChem Substance 177831 Link Image
ChEBI ID 7887 Link Image
PharmGKB ID PA450761 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 02244372 Link Image
RxList Link http://www.rxlist.com/cgi/generic/paclitaxel.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Paclitaxel Link Image
FDA Label
Material Safety Data Sheet (MSDS)
Synthesis Reference Rao KV et al. J Med Chem. 1995 Aug 18;38(17):3411-4.
Average Molecular Weight 853.9061
Monoisotopic Molecular Weight 853.3310
State Solid
Melting Point 213-216 oC
Experimental Water Solubility Insoluble Source: PhysProp
Predicted Water Solubility 5.56e-03 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 3 Source: PhysProp
Predicted LogP 3.20 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -5.19 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 CC(=O)O[C@@H]1C(=O)[C@]2(C)[C@@H](O)C[C@H]3OC[C@@]3(OC(C)=O)[C@H]2[C@H](OC(=O)C2=CC=CC=C2)[C@]2(O)C[C@H](OC(=O)[C@H](O)[C@@H](NC(=O)C3=CC=CC=C3)C3=CC=CC=C3)C(C)=C1C2(C)C
Canonical SMILES CC(=O)OC1C(=O)C2(C)C(O)CC3OCC3(OC(C)=O)C2C(OC(=O)C2=CC=CC=C2)C2(O)CC(OC(=O)C(O)C(NC(=O)C3=CC=CC=C3)C3=CC=CC=C3)C(C)=C1C2(C)C
Drug Category
  • Antineoplastic Agents
  • Antineoplastic Agents, Phytogenic
  • Tubulin Modulators
ATC Codes
AHFS Codes
  • 10:00.00
Indication Used in the treatment of Kaposi's sarcoma and cancer of the lung, ovarian, and breast.
Pharmacology Paclitaxel is a taxoid antineoplastic agent indicated as first-line and subsequent therapy for the treatment of advanced carcinoma of the ovary, and other various cancers including breast cancer. Paclitaxel is a novel antimicrotubule agent that promotes the assembly of microtubules from tubulin dimers and stabilizes microtubules by preventing depolymerization. This stability results in the inhibition of the normal dynamic reorganization of the microtubule network that is essential for vital interphase and mitotic cellular functions. In addition, paclitaxel induces abnormal arrays or "bundles" of microtubules throughout the cell cycle and multiple asters of microtubules during mitosis.
Mechanism of Action Paclitaxel interferes with the normal function of microtubule growth. Whereas drugs like colchicine cause the depolymerization of microtubules in vivo, paclitaxel arrests their function by having the opposite effect; it hyper-stabilizes their structure. This destroys the cell's ability to use its cytoskeleton in a flexible manner. Specifically, paclitaxel binds to the β subunit of tubulin. Tubulin is the "building block" of mictotubules, and the binding of paclitaxel locks these building blocks in place. The resulting microtubule/paclitaxel complex does not have the ability to disassemble. This adversely affects cell function because the shortening and lengthening of microtubules (termed dynamic instability) is necessary for their function as a transportation highway for the cell. Chromosomes, for example, rely upon this property of microtubules during mitosis. Further research has indicated that paclitaxel induces programmed cell death (apoptosis) in cancer cells by binding to an apoptosis stopping protein called Bcl-2 (B-cell leukemia 2) and thus arresting its function.
Absorption I.V injected
Toxicity Rat (ipr) LD50=32530 µg/kg. Symptoms of overdose include bone marrow suppression, peripheral neurotoxicity, and mucositis. Overdoses in pediatric patients may be associated with acute ethanol toxicity.
Protein Binding 89%-98%
Biotransformation Hepatic. In vitro studies with human liver microsomes and tissue slices showed that paclitaxel was metabolized primarily to 6a-hydrox-ypaclitaxel by the cytochrome P450 isozyme CYP2C8; and to two minor metabolites, 3’-p-hydroxypaclitaxel and 6a, 3’-p-dihydroxypaclitaxel, by CYP3A4.
Half Life Average distribution half-life of 0.34 hours and an average elimination half-life of 5.8 hours.
Dosage Forms
Form Route
Powder, for suspension Intravenous
Solution Intravenous
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Aprepitant Aprepitant may change levels of chemotherapy agent
Cisplatin Cisplatin increases the effect and toxicity of paclitaxel
Gemcitabine Paclitaxel increases the effect/toxicity of gemcitabine
Quinupristin This combination presents an increased risk of toxicity
Food Interactions Not Available
Pathways Not Available
General References
  1. Wani MC, Taylor HL, Wall ME, Coggon P, McPhail AT: Plant antitumor agents. VI. The isolation and structure of taxol, a novel antileukemic and antitumor agent from Taxus brevifolia. J Am Chem Soc. 1971 May 5;93(9):2325-7. [PubMed Link Image]
  2. Fuchs DA, Johnson RK: Cytologic evidence that taxol, an antineoplastic agent from Taxus brevifolia, acts as a mitotic spindle poison. Cancer Treat Rep. 1978 Aug;62(8):1219-22. [PubMed Link Image]
  3. Saville MW, Lietzau J, Pluda JM, Feuerstein I, Odom J, Wilson WH, Humphrey RW, Feigal E, Steinberg SM, Broder S, et al.: Treatment of HIV-associated Kaposi's sarcoma with paclitaxel. Lancet. 1995 Jul 1;346(8966):26-8. [PubMed Link Image]
  4. Wall ME, Wani MC: Camptothecin and taxol: discovery to clinic--thirteenth Bruce F. Cain Memorial Award Lecture. Cancer Res. 1995 Feb 15;55(4):753-60. [PubMed Link Image]
  5. Drugs.com Link Image
  6. Wikipedia Link Image
  7. RxList Link Image
Organisms Affected
  • Humans and other mammals
Phase 1 Metabolizing Enzymes
  1. Cytochrome P450 3A4 (CYP3A4)
  2. Cytochrome P450 2C8 (CYP2C8)
Targets
  1. Tubulin beta-1 chain
  2. Apoptosis regulator Bcl-2
Phase 1 Metabolizing Enzyme 1 [top]
Enzyme 1 Name Cytochrome P450 3A4 (CYP3A4)
Enzyme 1 Gene Name CYP3A4
Enzyme 1 SwissProt ID P08684 Link Image
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 Protein Sequence >sp|P08684|CP3A4_HUMAN Cytochrome P450 3A4 (EC 1.14.13.67) 
ALIPDLAMETWLLLAVSLVLLYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFD
MECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISIA
EDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYSM
DVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICVF
PREVTNFLRKSVKRMKESRLEDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSII
FIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVLQMEYLDMVVN
ETLRLFPIAMRLERVCKKDVEINGMFIPKGWVVMIPSYALHRDPKYWTEPEKFLPERFSK
KNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLGG
LLQPEKPVVLKVESRDGTVSGA
Phase 1 Metabolizing Enzyme 2 [top]
Enzyme 2 Name Cytochrome P450 2C8 (CYP2C8)
Enzyme 2 Gene Name CYP2C8
Enzyme 2 SwissProt ID P10632 Link Image
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 Protein Sequence >sp|P10632|CP2C8_HUMAN Cytochrome P450 2C8 (EC 1.14.14.1) 
MEPFVVLVLCLSFMLLFSLWRQSCRRRKLPPGPTPLPIIGNMLQIDVKDICKSFTNFSKV
YGPVFTVYFGMNPIVVFHGYEAVKEALIDNGEEFSGRGNSPISQRITKGLGIISSNGKRW
KEIRRFSLTTLRNFGMGKRSIEDRVQEEAHCLVEELRKTKASPCDPTFILGCAPCNVICS
VVFQKRFDYKDQNFLTLMKRFNENFRILNSPWIQVCNNFPLLIDCFPGTHNKVLKNVALT
RSYIREKVKEHQASLDVNNPRDFIDCFLIKMEQEKDNQKSEFNIENLVGTVADLFVAGTE
TTSTTLRYGLLLLLKHPEVTAKVQEEIDHVIGRHRSPCMQDRSHMPYTDAVVHEIQRYSD
LVPTGVPHAVTTDTKFRNYLIPKGTTIMALLTSVLHDDKEFPNPNIFDPGHFLDKNGNFK
KSDYFMPFSAGKRICAGEGLARMELFLFLTTILQNFNLKSVDDLKNLNTTAVTKGIVSLP
PSYQICFIPV
Drug Target 1 [top]
Target 1 ID 29
Target 1 Name Tubulin beta-1 chain
Target 1 Synonyms Not Available
Target 1 Gene Name TUBB1
Target 1 Protein Sequence >Tubulin beta-1 chain 
MREIVHIQIGQCGNQIGAKFWEMIGEEHGIDLAGSDRGASALQLERISVYYNEAYGRKYV
PRAVLVDLEPGTMDSIRSSKLGALFQPDSFVHGNSGAGNNWAKGHYTEGAELIENVLEVV
RHESESCDCLQGFQIVHSLGGGTGSGMGTLLMNKIREEYPDRIMNSFSVMPSPKVSDTVV
EPYNAVLSIHQLIENADACFCIDNEALYDICFRTLKLTTPTYGDLNHLVSLTMSGITTSL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTAQGSQQYRALSVAELTQQMFDARNTM
AACDLRRGRYLTVACIFRGKMSTKEVDQQLLSVQTRNSSCFVEWIPNNVKVAVCDIPPRG
LSMAATFIGNNTAIQEIFNRVSEHFSAMFKRKAFVHWYTSEGMDINEFGEAENNIHDLVS
EYQQFQDAKAVLEEDEEVTEEAEMEPEDKGH
Target 1 Number of Residues 458
Target 1 Molecular Weight 50328
Target 1 Theoretical pI 4.82
Target 1 GO Classification
Function
binding
nucleotide binding
purine nucleotide binding
guanyl nucleotide binding
GTP binding
catalytic activity
hydrolase activity
hydrolase activity, acting on acid anhydrides
hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
pyrophosphatase activity
nucleoside-triphosphatase activity
GTPase activity
structural molecule activity
Process
metabolism
macromolecule metabolism
protein metabolism
cellular protein metabolism
protein polymerization
physiological process
cellular physiological process
cell organization and biogenesis
organelle organization and biogenesis
cytoskeleton organization and biogenesis
microtubule-based process
microtubule-based movement
Component
protein complex
organelle
non-membrane-bound organelle
intracellular non-membrane-bound organelle
cytoskeleton
microtubule cytoskeleton
microtubule
Target 1 General Function Cell cycle control, cell division, chromosome partitioning
Target 1 Specific Function Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha-chain
Target 1 Pathways Not Available
Target 1 Reactions Not Available
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 11230445 Link Image
Target 1 UniProtKB/Swiss-Prot ID Q9H4B7 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name TBB1_HUMAN Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location
  • Cytoplasmic
Target 1 Gene Sequence >1356 bp 
ATGCGTGAAATTGTCCATATTCAGATTGGCCAGTGTGGCAACCAGATCGGAGCCAAGTTC
TGGGAGATGATTGGTGAGGAACACGGGATCGACTTGGCTGGGAGCGACCGCGGGGCCTCG
GCCTTGCAGCTGGAGAGAATCAGCGTGTACTACAACGAAGCCTACGGTAGGAAATATGTG
CCCCGAGCAGTCTTGGTGGACCTAGAACCTGGGACGATGGACAGCATTCGATCTAGCAAA
TTAGGAGCTCTCTTTCAACCCGACAGTTTTGTCCATGGTAACTCTGGGGCTGGCAACAAC
TGGGCCAAAGGCCACTACACGGAGGGAGCCGAGCTGATCGAGAATGTCCTAGAGGTGGTG
AGGCACGAGAGTGAGAGCTGTGACTGCCTGCAGGGCTTCCAGATCGTCCACTCCCTGGGC
GGGGGCACAGGCTCCGGGATGGGCACTCTGCTCATGAACAAGATTAGAGAGGAGTACCCG
GACCGGATCATGAATTCCTTCAGCGTCATGCCTTCTCCCAAGGTGTCGGACACGGTGGTG
GAGCCCTACAACGCGGTTCTGTCTATCCACCAGCTGATTGAGAATGCAGATGCCTGTTTC
TGCATTGACAATGAGGCCCTCTATGACATCTGCTTCCGTACCCTGAAGCTGACGACACCC
ACCTATGGGGATCTCAACCACCTAGTGTCCTTGACCATGAGCGGCATAACCACCTCCCTC
CGGTTCCCGGGTCAGCTCAACGCAGACCTGCGCAAGCTGGCGGTGAACATGGTCCCCTTC
CCCCGCCTGCACTTCTTTATGCCCGGCTTTGCCCCACTCACGGCCCAGGGCAGCCAGCAG
TACCGAGCCCTCTCCGTGGCCGAGCTCACCCAGCAGATGTTCGATGCCCGCAATACCATG
GCTGCCTGTGACCTCCGCCGTGGCCGCTACCTCACAGTGGCCTGCATTTTCCGGGGCAAG
ATGTCCACCAAGGAAGTGGACCAGCAACTGCTCTCCGTGCAGACCAGGAACAGCAGCTGC
TTTGTGGAGTGGATTCCCAACAACGTCAAGGTGGCTGTCTGCGACATCCCGCCCCGGGGG
CTGAGCATGGCCGCCACCTTCATTGGCAACAACACGGCCATCCAAGAGATCTTTAATAGG
GTCTCTGAGCATTTCTCAGCCATGTTCAAAAGGAAAGCTTTTGTGCACTGGTACACCAGC
GAAGGGATGGACATAAACGAATTTGGGGAAGCTGAAAATAACATCCATGATTTGGTATCC
GAGTACCAACAATTTCAAGATGCCAAAGCAGTTCTAGAGGAAGATGAAGAGGTCACGGAG
GAGGCAGAAATGGAGCCAGAAGATAAGGGACATTAA
Target 1 GenBank Gene ID
Target 1 GeneCard ID TUBB1 Link Image
Target 1 GenAtlas ID TUBB1 Link Image
Target 1 HGNC ID HGNC:16257 Link Image
Target 1 Chromosome Location 20
Target 1 Locus 20q13.32
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  2. 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]
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 273
Target 2 Name Apoptosis regulator Bcl-2
Target 2 Synonyms Not Available
Target 2 Gene Name BCL2
Target 2 Protein Sequence >Apoptosis regulator Bcl-2 
MAHAGRTGYDNREIVMKYIHYKLSQRGYEWDAGDVGAAPPGAAPAPGIFSSQPGHTPHPA
ASRDPVARTSPLQTPAAPGAAAGPALSPVPPVVHLTLRQAGDDFSRRYRRDFAEMSSQLH
LTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVNREMSPLVDNIALWMTEY
LNRHLHTWIQDNGGWDAFVELYGPSMRPLFDFSWLSLKTLLSLALVGACITLGAYLGHK
Target 2 Number of Residues 242
Target 2 Molecular Weight 26266
Target 2 Theoretical pI 7.32
Target 2 GO Classification
Function
Not Available
Process
regulation of biological process
regulation of physiological process
regulation of cellular physiological process
regulation of programmed cell death
regulation of apoptosis
Component
cell
membrane
Target 2 General Function Involved in BH3 domain binding
Target 2 Specific Function Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1)
Target 2 Pathways Not Available
Target 2 Reactions Not Available
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • 212-233
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 179367 Link Image
Target 2 UniProtKB/Swiss-Prot ID P10415 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name BCL2_HUMAN Link Image
Target 2 PDB ID Not Available
Target 2 Cellular Location
  • Mitochondrion
  • mitochondrial outer membrane
  • nuclear membrane
  • single-pass membrane protein. Nucleus
Target 2 Gene Sequence >720 bp 
ATGGCGCACGCTGGGAGAACGGGGTACGACAACCGGGAGATAGTGATGAAGTACATCCAT
TATAAGCTGTCGCAGAGGGGCTACGAGTGGGATGCGGGAGATGTGGGCGCCGCGCCCCCG
GGGGCCGCCCCCGCACCGGGCATCTTCTCCTCCCAGCCCGGGCACACGCCCCATCCAGCC
GCATCCCGCGACCCGGTCGCCAGGACCTCGCCGCTGCAGACCCCGGCTGCCCCCGGCGCC
GCCGCGGGGCCTGCGCTCAGCCCGGTGCCACCTGTGGTCCACCTGGCCCTCCGCCAAGCC
GGCGACGACTTCTCCCGCCGCTACCGCGGCGACTTCGCCGAGATGTCCAGCCAGCTGCAC
CTGACGCCCTTCACCGCGCGGGGACGCTTTGCCACGGTGGTGGAGGAGCTCTTCAGGGAC
GGGGTGAACTGGGGGAGGATTGTGGCCTTCTTTGAGTTCGGTGGGGTCATGTGTGTGGAG
AGCGTCAACCGGGAGATGTCGCCCCTGGTGGACAACATCGCCCTGTGGATGACTGAGTAC
CTGAACCGGCACCTGCACACCTGGATCCAGGATAACGGAGGCTGGGATGCCTTTGTGGAA
CTGTACGGCCCCAGCATGCGGCCTCTGTTTGATTTCTCCTGGCTGTCTCTGAAGACTCTG
CTCAGTTTGGCCCTGGTGGGAGCTTGCATCACCCTGGGTGCCTATCTGAGCCACAAGTGA
Target 2 GenBank Gene ID
Target 2 GeneCard ID BCL2 Link Image
Target 2 GenAtlas ID BCL2 Link Image
Target 2 HGNC ID HGNC:990 Link Image
Target 2 Chromosome Location 18
Target 2 Locus 18q21.33|18q21.3
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Yamamoto K, Ichijo H, Korsmeyer SJ: BCL-2 is phosphorylated and inactivated by an ASK1/Jun N-terminal protein kinase pathway normally activated at G(2)/M. Mol Cell Biol. 1999 Dec;19(12):8469-78. [PubMed Link Image]
  2. Ruvolo PP, Deng X, May WS: Phosphorylation of Bcl2 and regulation of apoptosis. Leukemia. 2001 Apr;15(4):515-22. [PubMed Link Image]
  3. Yu J, Zhang L, Hwang PM, Kinzler KW, Vogelstein B: PUMA induces the rapid apoptosis of colorectal cancer cells. Mol Cell. 2001 Mar;7(3):673-82. [PubMed Link Image]
  4. Qin W, Hu J, Guo M, Xu J, Li J, Yao G, Zhou X, Jiang H, Zhang P, Shen L, Wan D, Gu J: BNIPL-2, a novel homologue of BNIP-2, interacts with Bcl-2 and Cdc42GAP in apoptosis. Biochem Biophys Res Commun. 2003 Aug 22;308(2):379-85. [PubMed Link Image]
  5. Tanaka S, Louie DC, Kant JA, Reed JC: Frequent incidence of somatic mutations in translocated BCL2 oncogenes of non-Hodgkin's lymphomas. Blood. 1992 Jan 1;79(1):229-37. [PubMed Link Image]
  6. Eguchi Y, Ewert DL, Tsujimoto Y: Isolation and characterization of the chicken bcl-2 gene: expression in a variety of tissues including lymphoid and neuronal organs in adult and embryo. Nucleic Acids Res. 1992 Aug 25;20(16):4187-92. [PubMed Link Image]
  7. Hockenbery D, Nunez G, Milliman C, Schreiber RD, Korsmeyer SJ: Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death. Nature. 1990 Nov 22;348(6299):334-6. [PubMed Link Image]
  8. Seto M, Jaeger U, Hockett RD, Graninger W, Bennett S, Goldman P, Korsmeyer SJ: Alternative promoters and exons, somatic mutation and deregulation of the Bcl-2-Ig fusion gene in lymphoma. EMBO J. 1988 Jan;7(1):123-31. [PubMed Link Image]
  9. Cleary ML, Smith SD, Sklar J: Cloning and structural analysis of cDNAs for bcl-2 and a hybrid bcl-2/immunoglobulin transcript resulting from the t(14;18) translocation. Cell. 1986 Oct 10;47(1):19-28. [PubMed Link Image]
  10. Hua C, Zorn S, Jensen JP, Coupland RW, Ko HS, Wright JJ, Bakhshi A: Consequences of the t(14;18) chromosomal translocation in follicular lymphoma: deregulated expression of a chimeric and mutated BCL-2 gene. Oncogene Res. 1988 Feb;2(3):263-75. [PubMed Link Image]
  11. 3523487 Tsujimoto Y, Croce CM: Analysis of the structure, transcripts, and protein products of bcl-2, the gene involved in human follicular lymphoma. Proc Natl Acad Sci U S A. 1986 Jul;83(14):5214-8.
  12. 8183370 Yin XM, Oltvai ZN, Korsmeyer SJ: BH1 and BH2 domains of Bcl-2 are required for inhibition of apoptosis and heterodimerization with Bax. Nature. 1994 May 26;369(6478):321-3.
  13. 8668206 Naumovski L, Cleary ML: The p53-binding protein 53BP2 also interacts with Bc12 and impedes cell cycle progression at G2/M. Mol Cell Biol. 1996 Jul;16(7):3884-92.
  14. 9395403 Cheng EH, Kirsch DG, Clem RJ, Ravi R, Kastan MB, Bedi A, Ueno K, Hardwick JM: Conversion of Bcl-2 to a Bax-like death effector by caspases. Science. 1997 Dec 12;278(5345):1966-8.
Target 2 Drug References
  1. Gan Y, Wientjes MG, Au JL: Expression of basic fibroblast growth factor correlates with resistance to paclitaxel in human patient tumors. Pharm Res. 2006 Jun;23(6):1324-31. Epub 2006 Jun 8. [PubMed Link Image]
  2. Thomadaki H, Talieri M, Scorilas A: Treatment of MCF-7 cells with taxol and etoposide induces distinct alterations in the expression of apoptosis-related genes BCL2, BCL2L12, BAX, CASPASE-9 and FAS. Biol Chem. 2006 Aug;387(8):1081-6. [PubMed Link Image]
  3. Yoshino T, Shiina H, Urakami S, Kikuno N, Yoneda T, Shigeno K, Igawa M: Bcl-2 expression as a predictive marker of hormone-refractory prostate cancer treated with taxane-based chemotherapy. Clin Cancer Res. 2006 Oct 15;12(20 Pt 1):6116-24. [PubMed Link Image]
  4. Matsuyoshi S, Shimada K, Nakamura M, Ishida E, Konishi N: Bcl-2 phosphorylation has pathological significance in human breast cancer. Pathobiology. 2006;73(4):205-12. [PubMed Link Image]
  5. Zhang X, Wang Q, Ling MT, Wong YC, Leung SC, Wang X: Anti-apoptotic role of TWIST and its association with Akt pathway in mediating taxol resistance in nasopharyngeal carcinoma cells. Int J Cancer. 2007 May 1;120(9):1891-8. [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.